|
Name |
Accession |
Description |
Interval |
E-value |
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
18-157 |
2.75e-73 |
|
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: 241.04 E-value: 2.75e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 18 QAYEEVREKYKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpreKGR 97
Cdd:cd21236 1 QAYENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPRE------------KGR 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 98 MRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 157
Cdd:cd21236 69 MRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
32-148 |
2.89e-73 |
|
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 240.00 E-value: 2.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 32 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprekGRMRFHKLQNVQIALD 111
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRER------------GRMRFHRLQNVQTALD 68
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237970 112 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 148
Cdd:cd21188 69 FLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
29-159 |
1.97e-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: 232.61 E-value: 1.97e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 29 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpreKGRMRFHKLQNVQI 108
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE------------KGRMRFHKLQNVQI 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1920237970 109 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 159
Cdd:cd21235 69 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
161-266 |
1.15e-69 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 229.91 E-value: 1.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 161 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 240
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1920237970 241 PEDVDVPQPDEKSIITYVSSLYDAMP 266
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
162-266 |
3.99e-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: 213.79 E-value: 3.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 162 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 241
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1920237970 242 EDVDVPQPDEKSIITYVSSLYDAMP 266
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
29-158 |
1.92e-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: 204.11 E-value: 1.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 29 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGdslprerdvirsSRLPREKGRMRFHKLQNVQI 108
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSG------------VKLPREKGRMRFHRLQNVQI 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1920237970 109 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 158
Cdd:cd21237 69 ALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
162-266 |
1.43e-56 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 192.51 E-value: 1.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 162 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 241
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1920237970 242 EDVDVPQPDEKSIITYVSSLYDAMP 266
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
160-266 |
6.63e-50 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 173.30 E-value: 6.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 160 DMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 239
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1920237970 240 DPEDVDVPQPDEKSIITYVSSLYDAMP 266
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
34-149 |
9.82e-48 |
|
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409035 Cd Length: 107 Bit Score: 167.17 E-value: 9.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 34 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGdslprerdvirsSRLPREKGRMRFHKLQNVQIALDY 112
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTG------------KKLKPEKGRMRVHHLNNVNRALQV 69
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237970 113 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 149
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 ... |
20-145 |
2.91e-46 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 163.31 E-value: 2.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 20 YEEVREK-YKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRM 98
Cdd:cd21246 1 FERSRIKaLADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKP-----------TKGKM 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237970 99 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 145
Cdd:cd21246 70 RIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
162-262 |
6.66e-45 |
|
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: 159.11 E-value: 6.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 162 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 241
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1920237970 242 EDVDVPQPDEKSIITYVSSLY 262
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
33-373 |
3.37e-43 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 170.12 E-value: 3.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 33 RVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLprerdvIRSSRLPRekgrMRFHKLQNVQIALD 111
Cdd:COG5069 8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNA------GEYNETPE----TRIHVMENVSGRLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 112 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGCQ-GLRCDNFTTSW 190
Cdd:COG5069 78 FIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 191 RDGRLFNAIIHRHKPTLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS------SL 261
Cdd:COG5069 155 RDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyiirfGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 262 YD----AMPRVPDVQDGVKANElQLRwQEYRELVLLLLQWIRAHTAGFEERRFPSSFEEIEILWCQFLKFKETE--LPAK 335
Cdd:COG5069 235 LEkidiALHRVYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCsrAPLE 312
|
330 340 350
....*....|....*....|....*....|....*....
gi 1920237970 336 EAD-KNRSKGIYQSLEgAVQAGQLKVPPGYHPLDVEKEW 373
Cdd:COG5069 313 TTDlHSLAGQILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
162-262 |
4.63e-43 |
|
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: 153.71 E-value: 4.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 162 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 241
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1920237970 242 EDVDVPQPDEKSIITYVSSLY 262
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
20-145 |
1.55e-42 |
|
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: 152.84 E-value: 1.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 20 YEEVR-EKYKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRM 98
Cdd:cd21193 1 FEKGRiRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKP-----------NRGRL 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237970 99 RFHKLQNVQIALDYLrHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 145
Cdd:cd21193 70 RVQKIENVNKALAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
30-149 |
9.73e-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: 150.22 E-value: 9.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 30 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDslprerdvirssRLPREKGRM--RFHKLQN 105
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGE------------KLPCEKGRRlkRVHFLSN 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1920237970 106 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 149
Cdd:cd21241 69 INTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
161-266 |
5.90e-41 |
|
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: 147.85 E-value: 5.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 161 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 240
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1920237970 241 PEDVDVPQPDEKSIITYVSSLYDAMP 266
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
30-149 |
7.39e-41 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 147.72 E-value: 7.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 30 ERDRVQKKTFTKWVNKHLikaQRH-----ISDLYEDLRDGHNLISLLEVLSGDslprerdvirssRLPREKGRM--RFHK 102
Cdd:cd21190 1 EQERVQKKTFTNWINSHL---AKLsqpivINDLFVDIKDGTALLRLLEVLSGQ------------KLPIESGRVlqRAHK 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237970 103 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 149
Cdd:cd21190 66 LSNIRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
149-264 |
8.64e-40 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 144.81 E-value: 8.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 149 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 228
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237970 229 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 264
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
29-145 |
3.33e-38 |
|
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: 141.32 E-value: 3.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 29 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMRFHKLQNVQI 108
Cdd:cd21318 33 DEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKP-----------TRGRMRIHSLENVDK 101
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237970 109 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 145
Cdd:cd21318 102 ALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1305-1880 |
1.45e-37 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 156.25 E-value: 1.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1305 DLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEErERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRM 1384
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE-AELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1385 QEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLrIEEEIRVVRLQLEATERQRGGAEGELQA 1464
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1465 LRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEA 1544
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1545 ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAtrraqqqaEAERARAEAERELERWQLK 1624
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL--------AGLRGLAGAVAVLIGVEAA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1625 ANEALRLRLQAeevAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIR 1704
Cdd:COG1196 536 YEAALEAALAA---ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1705 LRAETEQGEqqrqLLEEELARLQREAAAATqkRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfr 1784
Cdd:COG1196 613 ARYYVLGDT----LLGRTLVAARLEAALRR--AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE---- 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1785 ELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQR 1864
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570
....*....|....*.
gi 1920237970 1865 RLLEEQAAQHKADIEA 1880
Cdd:COG1196 763 EELERELERLEREIEA 778
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
32-145 |
1.48e-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: 137.91 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 32 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerdvirssrlPREKGRMRFHKLQNVQIALD 111
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLP-----------KPERGKMRFHKIANVNKALD 71
|
90 100 110
....*....|....*....|....*....|....
gi 1920237970 112 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 145
Cdd:cd21214 72 FIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
158-262 |
2.06e-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: 138.27 E-value: 2.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 158 SEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 237
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1920237970 238 LLDPEDVDVPQPDEKSIITYVSSLY 262
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
20-145 |
2.36e-37 |
|
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: 138.65 E-value: 2.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 20 YEEVREK-YKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRM 98
Cdd:cd21317 16 FERSRIKaLADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKP-----------TKGRM 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237970 99 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 145
Cdd:cd21317 85 RIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
158-262 |
4.48e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 137.06 E-value: 4.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 158 SEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 237
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1920237970 238 LLDPEDVDVPQPDEKSIITYVSSLY 262
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1333-2038 |
1.05e-36 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 154.53 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1333 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSiqEELQHL 1412
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKA--EDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1413 RQSSEAEIQAKARQVEAAERSRlRIEEEIRVVRLQlEATERQRGGAEGELQALRaRAEEAeaqkRQAQEEAERLRRQVQD 1492
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDAR-KAEAARKAEEER-KAEEARKAEDAKKAEAVK-KAEEA----KKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1493 ETQRKRQAEAELALRVQAEAEAAREKQRAlqalEELRlQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASF 1572
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKA----DELK-KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1573 AEKTAQ-LERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEAlrlRLQAEEVAQQKSLTQaeaek 1651
Cdd:PTZ00121 1327 AKKKADaAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA---KKKAEEKKKADEAKK----- 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1652 qkeeaerearrrgKAEEQAVRQRELAEQELEKQR-QLAEGTAQQRLAAEqELIRLRAETEQGEQQRQLLE-----EELAR 1725
Cdd:PTZ00121 1399 -------------KAEEDKKKADELKKAAAAKKKaDEAKKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEeakkaEEAKK 1464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1726 LQREAAAATQKRRELE----AELAKVRAEmevllASKARAEEESRSTSEKSKqrleAEAGRFRELAEEAARLRAlAEEAK 1801
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEeakkADEAKKKAE-----EAKKKADEAKKAAEAKKK----ADEAKKAEEAKKADEAKK-AEEAK 1534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1802 RQRQLAEEDAVRQRAEAERvlAEKLAAISEatrlKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEAR 1881
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKK--AEELKKAEE----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1882 LAQLRKASESELERQKGLVEDTLRQRrqveEEILALKGSFEKAAAGKAELELELGRIRGT-----AEDTLRSKEQA--EQ 1954
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKK----VEQLKKKEAEEKKKAEELKKAEEENKIKAAeeakkAEEDKKKAEEAkkAE 1684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1955 EAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE----VERLKAKVEEARRLRERAEQESARQLQLAQEAA 2030
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
....*...
gi 1920237970 2031 QKRLQAEE 2038
Cdd:PTZ00121 1765 EEEKKAEE 1772
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
34-147 |
1.24e-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: 135.61 E-value: 1.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 34 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprEKGRMRFHKLQNVQIALDYL 113
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYN----------KNPKMRVQKLENVNKALEFI 73
|
90 100 110
....*....|....*....|....*....|....
gi 1920237970 114 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 147
Cdd:cd21215 74 KSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1338-1939 |
2.14e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 152.40 E-value: 2.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1338 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKaQAEReAQGLQrrmqeevarreevaveAQEQKRSIQEELQHLRQSs 1416
Cdd:COG1196 177 AERKLEATEENLERLEDILgELERQLEPLERQAE-KAER-YRELK----------------EELKELEAELLLLKLREL- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1417 EAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQR 1496
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1497 KRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALEtaQRSAEAELQSEHASFAEKT 1576
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1577 AQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEA 1656
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1657 EREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIR------LRAETEQGEQQRQLLEEELARLQREA 1730
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgavavlIGVEAAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1731 AAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED 1810
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1811 AVRQRAEAERVLAEKLAA--ISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKA 1888
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGegGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1920237970 1889 SESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIR 1939
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
30-149 |
5.92e-36 |
|
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: 133.80 E-value: 5.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 30 ERDRVQKKTFTKWVNKHLIKAQ--RHISDLYEDLRDGHNLISLLEVLSGDslprerdvirssRLPREKGRMRFHKLQNVQ 107
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQ------------QLPREKGHNVFQCRSNIE 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1920237970 108 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 149
Cdd:cd21242 69 TALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
161-262 |
1.17e-35 |
|
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: 132.68 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 161 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 240
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1920237970 241 PEDVDVPQPDEKSIITYVSSLY 262
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1465-2065 |
4.43e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 148.16 E-value: 4.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1465 LRARAEEAEAQKRQAQEEAERL---RRQVqdETQR---KRQAE-AELALRVQAEAEAaREKQRALQALEELRLQAEEAER 1537
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLediLGEL--ERQLeplERQAEkAERYRELKEELKE-LEAELLLLKLRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1538 RLRQAEAERARqvqvaLETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAvvQLREEATRRAQQQAEAERARAEAERE 1617
Cdd:COG1196 247 ELEELEAELEE-----LEAELAELEAELEELRLELEELELELEEAQAEEYEL--LAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1618 LERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA 1697
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---------AELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1698 AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1777
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1778 AEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLA----AISEATRLKTEAEIALKEKEAENERL 1853
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagAVAVLIGVEAAYEAALEAALAAALQN 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1854 RRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELEL 1933
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1934 ELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRE 2013
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 2014 RAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLER 2065
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
165-266 |
1.22e-34 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 129.47 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 165 EKLLL-WSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 243
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1920237970 244 VDVPQPDEKSIITYVSSLYDAMP 266
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
146-262 |
1.57e-34 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 130.56 E-value: 1.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 146 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQA 225
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237970 226 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 262
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1668-2236 |
3.11e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 145.46 E-value: 3.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1668 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1747
Cdd:COG1196 210 EKAERYRELKEELKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1748 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAVRQRAEAERVLAEKLA 1827
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1828 AISEATRLKTEAEIALKEKEAENERLRRlaedEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQR 1907
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALR----AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1908 RQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEA 1987
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1988 ARQRKAALEEVERLKAKVEEAR---RLRERAEQESARQLQLAQEAAQKRL-----QAEEKAHAFAVQQKEQELQQTLQQE 2059
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAAlaaALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAV 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2060 QSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2139
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2140 EQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2219
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
570
....*....|....*..
gi 1920237970 2220 LRVQMEELGKLKARIEA 2236
Cdd:COG1196 762 LEELERELERLEREIEA 778
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
29-149 |
6.58e-34 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 127.73 E-value: 6.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 29 DERDRVQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGdslprerdvirsSRLPREKGRMRFHKLQNVQ 107
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTG------------QKLVKEKGSTRVHALNNVN 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1920237970 108 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 149
Cdd:cd21231 69 KALQVLQKNNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
162-262 |
5.65e-32 |
|
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: 122.13 E-value: 5.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 162 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 241
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1920237970 242 EDVDVPQPDEKSIITYVSSLY 262
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
33-150 |
6.10e-32 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 122.56 E-value: 6.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 33 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpREKGRMRFHKLQNVQIALDY 112
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKF----------NKRPTFRSQKLENVSVALKF 83
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237970 113 LRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 150
Cdd:cd21311 84 LEEDEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
34-149 |
1.11e-31 |
|
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 121.24 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 34 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRerdVIRssrlpreKGRMRFHKLQNVQIALDYL 113
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGR---VIK-------KPLNQHQKLENVTLALKAM 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237970 114 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 149
Cdd:cd21227 74 AEDGIKLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
161-259 |
4.52e-31 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 119.45 E-value: 4.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 161 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 240
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1920237970 241 PEDVDVPQPDEKSIITYVS 259
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1326-1930 |
1.16e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 134.50 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1326 ETLRRMEEEERLAEQQRAE------------ERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREE 1393
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEavkkaeeakkdaEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1394 V--AVEAQ--EQKRSIQEELQHLRQSSEAEiQAKARQVEA---AERSRLRIEEEirvvRLQLEATERQRGGAEGELQALR 1466
Cdd:PTZ00121 1289 KkkADEAKkaEEKKKADEAKKKAEEAKKAD-EAKKKAEEAkkkADAAKKKAEEA----KKAAEAAKAEAEAAADEAEAAE 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1467 ARAEEAEAQKRQAQEEAERLRRQVQ-----DETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRlQAEEAERRLRQ 1541
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEekkkaDEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEE 1442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1542 A--------EAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLR--EEATRRAQQQAEAERAR 1611
Cdd:PTZ00121 1443 AkkadeakkKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKkaAEAKKKADEAKKAEEAK 1522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1612 AEAERELERWQLKANEALRlrlqAEEVAQQKSLTQAEAEKQKEEAEREARRRgKAEEqavrQRELAEQELEKQRQLAEGT 1691
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKK----AEEKKKADELKKAEELKKAEEKKKAEEAK-KAEE----DKNMALRKAEEAKKAEEAR 1593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1692 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEK 1771
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1772 SKQRLEAEagrfRELAEEAARLRALAEEAKRQRQLAEedaVRQRAEAERVLAEKLAAISEATRLKteAEIALKEKEAENE 1851
Cdd:PTZ00121 1674 KKKAEEAK----KAEEDEKKAAEALKKEAEEAKKAEE---LKKKEAEEKKKAEELKKAEEENKIK--AEEAKKEAEEDKK 1744
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 1852 RLRRLAEDEAFQRRLleeqaAQHKADIEARLAQLRKASESELErqKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAE 1930
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKI-----AHLKKEEEKKAEEIRKEKEAVIE--EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
149-264 |
1.60e-30 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 118.40 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 149 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 228
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237970 229 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 264
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
161-259 |
1.66e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 118.01 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 161 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 240
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1920237970 241 PEDVDVPQPDEKSIITYVS 259
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
165-266 |
1.80e-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: 117.75 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 165 EKLLL-WSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 243
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1920237970 244 VDVPQPDEKSIITYVSSLYDAMP 266
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1326-1958 |
1.84e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 134.11 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1326 ETLRRMEEEERLAEQQRAEERERLAEVEAALE--KQRQLAEAHAQAKAQAEREAQGLQR----------RMQEEVARREE 1393
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVRKAEElrKAEDARKAEAARKAEEERKAEEARKaedakkaeavKKAEEAKKDAE 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1394 VAVEAQEQKRSIQ-EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRlQLEATERQRGGAEGELQALRAR-AEE 1471
Cdd:PTZ00121 1241 EAKKAEEERNNEEiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKkADE 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1472 AEAQKRQAQEEAERLRRQVQdETQRKRQAEAELALRVQAEAEAAREKQRALQ-ALEELRLQAEEAERRlrqaeAERARQV 1550
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkKKEEAKKKADAAKKK-----AEEKKKA 1393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1551 QVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARaeaerelerwqlKANEALR 1630
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE------------EAKKAEE 1461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1631 LRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELiRLRAETE 1710
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA-KKADEAK 1540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1711 QGEQQR---QLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEaEAGRFRELA 1787
Cdd:PTZ00121 1541 KAEEKKkadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAK 1619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1788 EEAARLRALAEEAKRQRQLAEEDA--------VRQRAEAERVLAEKLAAISEATrlKTEAEIALKEKEAENERLRRLAED 1859
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAeekkkaeeLKKAEEENKIKAAEEAKKAEED--KKKAEEAKKAEEDEKKAAEALKKE 1697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1860 EAFQRRLleEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVeEEILALKGSFEKAAAGKAELELELGRIR 1939
Cdd:PTZ00121 1698 AEEAKKA--EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA-EEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
650
....*....|....*....
gi 1920237970 1940 GTAEDTLRSKEQAEQEAAR 1958
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRR 1793
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
12-145 |
2.02e-30 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 119.38 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 12 DEQDFIQAYEEVREK-YKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssr 90
Cdd:cd21316 30 NENSSARLFERSRIKaLADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKP-------- 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 91 lprEKGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 145
Cdd:cd21316 102 ---TKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
881-958 |
4.48e-30 |
|
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: 115.78 E-value: 4.48e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237970 881 LAWQSLGRDMQLIRSWSLATFRTLKPEEQRQALRSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSRHYQQLLQS 958
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
34-149 |
6.04e-30 |
|
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 116.26 E-value: 6.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 34 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprekGRMRFHKLQNVQIALDY 112
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKER------------GSTRVHALNNVNRVLQV 69
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237970 113 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 149
Cdd:cd21232 70 LHQNNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1735-2446 |
1.75e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 130.06 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1735 QKRRELEAELAKVRAEMEvllaskaRAEEEsrsTSEKSKQ--RLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEedav 1812
Cdd:COG1196 172 ERKEEAERKLEATEENLE-------RLEDI---LGELERQlePLERQA----EKAERYRELKEELKELEAELLLLK---- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1813 RQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAqhkadiEARLAQLRKASESE 1892
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL------LAELARLEQDIARL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1893 LERQkglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRRE 1972
Cdd:COG1196 308 EERR----RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1973 AEERVQKSLAAEEEAARQRKAALEEVERLKAkvEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQEL 2052
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLE--RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2053 QQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQE 2132
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2133 AARRAQAEQAALRQKQAAdaemekhkqfAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRgq 2212
Cdd:COG1196 542 AALAAALQNIVVEDDEVA----------AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR-- 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2213 vEEELFSLRVQMEELGklkarieaenRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2292
Cdd:COG1196 610 -EADARYYVLGDTLLG----------RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2293 ALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERL 2372
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2373 RLRVAEMSRAQARAEEDARRFRK-------QAEDIGERLyrTELATQekvmlVQTLETQRqqsdrdaERLREAIAELEHE 2445
Cdd:COG1196 759 PPDLEELERELERLEREIEALGPvnllaieEYEELEERY--DFLSEQ-----REDLEEAR-------ETLEEAIEEIDRE 824
|
.
gi 1920237970 2446 K 2446
Cdd:COG1196 825 T 825
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
165-267 |
3.04e-29 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 114.64 E-value: 3.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 165 EKLLL-WSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 242
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1920237970 243 DVDVPQPDEKSIITYVSSLYDAMPR 267
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
167-262 |
3.44e-29 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 113.98 E-value: 3.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 167 LLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 245
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1920237970 246 VPQPDEKSIITYVSSLY 262
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
30-151 |
3.90e-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: 114.21 E-value: 3.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 30 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRErdvIRSSRlprekgrMRFHKLQNVQ 107
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQE---YKPSS-------HRIFRLNNIA 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1920237970 108 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 151
Cdd:cd21191 71 KALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
33-147 |
6.98e-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: 6.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 33 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlprEKGRMRFHKLQNVQIALDY 112
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYN---------RRPAFQQHYLENVSTALKF 73
|
90 100 110
....*....|....*....|....*....|....*
gi 1920237970 113 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 147
Cdd:cd21183 74 IEADHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
147-264 |
3.52e-28 |
|
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: 112.10 E-value: 3.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 147 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAF 226
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237970 227 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 264
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1181-1799 |
4.67e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.43 E-value: 4.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1181 QTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVpLANSQAVREQLRQEKALLED-IERHGEKveecqrfa 1259
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELeLEEAQAE-------- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1260 kqyinaikdyELQLVTYKAQLEPVASPAKkpkvqsgsESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAE 1339
Cdd:COG1196 290 ----------EYELLAELARLEQDIARLE--------ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1340 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAqglqrrmqeEVARREEVAVEAQEQKRSIQEELQHLRQSSEAE 1419
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL---------EALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1420 IQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRqvQDETQRKRQ 1499
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA--RLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1500 AEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAE----K 1575
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflplD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1576 TAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEE 1655
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1656 AEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQ 1735
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 1736 KRRELEAELAKVRAEMEvllaskaraEEESRSTSEKSKQRLEAEAGRF--------RELAEEAARLRALAEE 1799
Cdd:COG1196 741 LLEEEELLEEEALEELP---------EPPDLEELERELERLEREIEALgpvnllaiEEYEELEERYDFLSEQ 803
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1495-2210 |
5.64e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.05 E-value: 5.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1495 QRKRQAEAELAlrvQAEAEAAR--------EKQralqaLEELRLQAEEAERRLRQAEAERARQVQVALetaqrsaeAELQ 1566
Cdd:COG1196 172 ERKEEAERKLE---ATEENLERledilgelERQ-----LEPLERQAEKAERYRELKEELKELEAELLL--------LKLR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1567 SEHASFAEKTAQLERTLKEEHVAVVQLREEATRRaqqqaeaeraraeaerelerwqlkanEALRLRLQAEEvaqqksltq 1646
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAEL--------------------------EELRLELEELE--------- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1647 aeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARL 1726
Cdd:COG1196 281 ------------------LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1727 QREAAAATQKRRELEAELAKVRAEmevLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQL 1806
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEA---LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1807 AEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLR 1886
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1887 KASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEE 1966
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1967 ERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQ 2046
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2047 QKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLR 2126
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2127 KEAEQEAARRAQAEQAALRQKQAADAEMEKHKqfAEQALRQKAQV----EQELTALRLQLEETDHQKSILDEELQRLK-- 2200
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELER--LEREIEALGPVnllaIEEYEELEERYDFLSEQREDLEEARETLEea 817
|
730
....*....|.
gi 1920237970 2201 -AEVTEAARQR 2210
Cdd:COG1196 818 iEEIDRETRER 828
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1709-2599 |
9.48e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 121.79 E-value: 9.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1709 TEQGEQQRQLLEEELARLQREAAAATqkRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFREL-- 1786
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgk 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1787 AEEAARlralAEEAKRQrqlAEEdaVRQRAEAERvlAEKLAAISEATRLKTE--AEIALKEKEAENERLRRLAEDeafQR 1864
Cdd:PTZ00121 1111 AEEARK----AEEAKKK---AED--ARKAEEARK--AEDARKAEEARKAEDAkrVEIARKAEDARKAEEARKAED---AK 1176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1865 RLLEEQAAqhkadIEARLA-QLRKASESelerqkglvedtlrqrRQVEEeilalkgsfekaaAGKAELELELGRIRgTAE 1943
Cdd:PTZ00121 1177 KAEAARKA-----EEVRKAeELRKAEDA----------------RKAEA-------------ARKAEEERKAEEAR-KAE 1221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1944 DTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQL 2023
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR---KADELKKAEEKKKADEAKKA 1298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2024 QLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERlrseaeaarraaeeaeaareraereaaqsRRQVEEAER 2103
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE-----------------------------AKKAAEAAK 1349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2104 LKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQaLRQKAQVEQELTALRLQLE 2183
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAE 1428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2184 ETDHQksildEELQRLKAEVTEAARQRGQVEEelfslRVQMEELGKlkaRIEAENRALVLRDKDSAQRLLQE---EAEKM 2260
Cdd:PTZ00121 1429 EKKKA-----DEAKKKAEEAKKADEAKKKAEE-----AKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEakkKAEEA 1495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2261 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQED 2336
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2337 KeQMAQQLAQETQgfqktlETERQRQLEMSAEAERLRLRVAEmsraQARAEEDARrfrKQAEDIGErlyrtelaTQEKVM 2416
Cdd:PTZ00121 1576 K-NMALRKAEEAK------KAEEARIEEVMKLYEEEKKMKAE----EAKKAEEAK---IKAEELKK--------AEEEKK 1633
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2417 LVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQalqqsflsekdslLQRErci 2496
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA-------------LKKE--- 1697
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2497 EQEKAKLEQL---FQDEVAKAQALREEQQRQQQqmqqekqqlaaSMEEARRRQHE----AEEgVRRQQEELQRLAQQQQQ 2569
Cdd:PTZ00121 1698 AEEAKKAEELkkkEAEEKKKAEELKKAEEENKI-----------KAEEAKKEAEEdkkkAEE-AKKDEEEKKKIAHLKKE 1765
|
890 900 910
....*....|....*....|....*....|....
gi 1920237970 2570 QEKLLAEENQR----LRERLQHLEEERRAALARS 2599
Cdd:PTZ00121 1766 EEKKAEEIRKEkeavIEEELDEEDEKRRMEVDKK 1799
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
165-264 |
1.15e-26 |
|
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: 106.99 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 165 EKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 243
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1920237970 244 VDVPQPDEKSIITYVSSLYDA 264
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
149-264 |
1.72e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 107.09 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 149 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 228
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237970 229 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 264
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
33-147 |
4.14e-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: 4.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 33 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlprEKGRMRFHKLQNVQIALDY 112
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYN---------KRPTFRQMKLENVSVALEF 73
|
90 100 110
....*....|....*....|....*....|....*
gi 1920237970 113 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 147
Cdd:cd21228 74 LERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
149-264 |
8.47e-26 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 105.19 E-value: 8.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 149 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 228
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237970 229 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 264
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1875-2603 |
9.79e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 118.32 E-value: 9.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1875 KADIEARLAQLRKASESELERQKGLVEDTlRQRRQVEEEilalKGSFE---KAAAGKAELELELGRIRGTAEDTLRSKE- 1950
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDN-RADEATEEA----FGKAEeakKTETGKAEEARKAEEAKKKAEDARKAEEa 1133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1951 -QAE-----QEAARQRQLAAEEERRRREAEERVQKSLAAEE----EAARQ----RKAA----LEEVERLKA--KVEEARR 2010
Cdd:PTZ00121 1134 rKAEdarkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDakkaEAARKaeevRKAEelrkAEDARKAEAarKAEEERK 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2011 LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAERE 2090
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2091 AAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADA--EMEKHKQFAEQALRQK 2168
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAadEAEAAEEKAEAAEKKK 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2169 AQVEQELTALRLQLEETDHQksildEELQRLKAEVTEAARQRGQVEEElfslrvqmeelgKLKARiEAENRALVLRDKDS 2248
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKA-----DEAKKKAEEDKKKADELKKAAAA------------KKKAD-EAKKKAEEKKKADE 1435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2249 AQRLLQE--EAEKMKQVAEEAARLSVAAQEAARLRQlAEEdlAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELA 2326
Cdd:PTZ00121 1436 AKKKAEEakKADEAKKKAEEAKKAEEAKKKAEEAKK-ADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2327 QEqARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRlRVAEMSRAQA--RAEEDARRFRKQAEDigerL 2404
Cdd:PTZ00121 1513 DE-AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK-KAEEKKKAEEakKAEEDKNMALRKAEE----A 1586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2405 YRTELATQEKVM-LVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFL 2483
Cdd:PTZ00121 1587 KKAEEARIEEVMkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2484 SEKDsllqrerciEQEKAKLEQLFQDEVAKAQAlrEEQQRQQQQMQQEKQQLAASMEEARRRQHE---AEEGVRRQQEEL 2560
Cdd:PTZ00121 1667 AKKA---------EEDKKKAEEAKKAEEDEKKA--AEALKKEAEEAKKAEELKKKEAEEKKKAEElkkAEEENKIKAEEA 1735
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1920237970 2561 QRLAQQ-QQQQEKLLAEENQrlRERLQHL--EEERRAALARSEEIA 2603
Cdd:PTZ00121 1736 KKEAEEdKKKAEEAKKDEEE--KKKIAHLkkEEEKKAEEIRKEKEA 1779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1401-2203 |
1.42e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 117.93 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1401 QKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEaEAQKRQAQ 1480
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE-ARKAEEAK 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1481 EEAERLR-----RQVQD--ETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAE----AERARQ 1549
Cdd:PTZ00121 1122 KKAEDARkaeeaRKAEDarKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEelrkAEDARK 1201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1550 VQVAletaqRSAEAELQSEHASFAEKTAQLERTLKEEHVAvvQLREEATRRAQQQAEAERARAEAERELERWQLKANEAL 1629
Cdd:PTZ00121 1202 AEAA-----RKAEEERKAEEARKAEDAKKAEAVKKAEEAK--KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1630 RLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQavRQRELAEQELEKQRQLAEGTAQQrlaAEQEliRLRAET 1709
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKKADAAKKK---AEEA--KKAAEA 1347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1710 EQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEmEVLLA--SKARAEEESRSTSEKSKQrlEAEAGRFRELA 1787
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-EKKKAdeAKKKAEEDKKKADELKKA--AAAKKKADEAK 1424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1788 EEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVlAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLL 1867
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1868 EEQAAQHKADiEARLAQLRKASEsELERQKglvedtlrQRRQVEEeilaLKGSFEKAAAGKAELELELGRirgtAEDTlR 1947
Cdd:PTZ00121 1504 KAAEAKKKAD-EAKKAEEAKKAD-EAKKAE--------EAKKADE----AKKAEEKKKADELKKAEELKK----AEEK-K 1564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1948 SKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRlrerAEQESARQLQLaq 2027
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK----AEEEKKKVEQL-- 1638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2028 eaaqKRLQAEEKAHAFAVQQKEQELQQTLqqeqsvlERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQs 2107
Cdd:PTZ00121 1639 ----KKKEAEEKKKAEELKKAEEENKIKA-------AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE- 1706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2108 aeeQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADaemEKHKQFAEQALRQKAQVEQELTALRLQLEETDH 2187
Cdd:PTZ00121 1707 ---LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE---EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
810
....*....|....*.
gi 1920237970 2188 QKSILDEELQRLKAEV 2203
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEV 1796
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
33-150 |
2.58e-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: 2.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 33 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlPREKgrMRFHKLQNVQIALDY 112
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYH-------PRPN--FRQMKLENVSVALEF 85
|
90 100 110
....*....|....*....|....*....|....*...
gi 1920237970 113 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 150
Cdd:cd21310 86 LDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
18-149 |
1.34e-24 |
|
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: 101.76 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 18 QAYEEVR-EKYKDERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprE 94
Cdd:cd21247 3 TEYEKGHiRKLQEQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRP-----------S 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 95 KGRMRFHKLQNVQIALDYLRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 149
Cdd:cd21247 72 RGKMRVHFLENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
149-264 |
2.45e-24 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 100.92 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 149 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 228
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237970 229 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 264
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1338-2549 |
4.17e-24 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 112.61 E-value: 4.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1338 AEQQRAEERERLAEVEAalEKQRQLAE-AHAQAKAQAEREAQGLQRRMQ--EEVARREEvAVEAQEQKRSIQEELQHLRQ 1414
Cdd:NF041483 85 ADQLRADAERELRDARA--QTQRILQEhAEHQARLQAELHTEAVQRRQQldQELAERRQ-TVESHVNENVAWAEQLRART 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1415 SSEA-----EIQAKARQVEAAERSRlrieeeirVVRLQLEAteRQRGGAEGElqalRARAEeAEAQKRQAQEEAERLRRQ 1489
Cdd:NF041483 162 ESQArrlldESRAEAEQALAAARAE--------AERLAEEA--RQRLGSEAE----SARAE-AEAILRRARKDAERLLNA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1490 VQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQaeEAERRLRQAEAERARQVQVALETA-QRSAEAELQSE 1568
Cdd:NF041483 227 ASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAAaKQLASAESANE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1569 hasfaektaQLERTLKEEhvaVVQLREEATRRAQQQAEAERARAEAERELERWQL-KANEALRLRLQAEEVAQQKSLTQA 1647
Cdd:NF041483 305 ---------QRTRTAKEE---IARLVGEATKEAEALKAEAEQALADARAEAEKLVaEAAEKARTVAAEDTAAQLAKAART 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1648 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ-RLAAEQELIRLRAETEQgeqqrqlLEEELARL 1726
Cdd:NF041483 373 AEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVE-------LQEEARRL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1727 QREAAaatQKRRELEAELAKVRAEmevllaskARAEeesrstsekSKQRLEAEAGRFRELAEEAarlRALAEEAKRQrql 1806
Cdd:NF041483 446 RGEAE---QLRAEAVAEGERIRGE--------ARRE---------AVQQIEEAARTAEELLTKA---KADADELRST--- 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1807 aeedavrQRAEAERVLAEklaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAA-QHKADIEARLAQL 1885
Cdd:NF041483 500 -------ATAESERVRTE---AIERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAArELREETERAIAAR 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1886 RKASESELERQKGLVEdtlrQRRQVEEEilALKGSFEKAAAGKAELELELGRIRGTAEDTLRS-KEQAEQEAARQRqlaa 1964
Cdd:NF041483 570 QAEAAEELTRLHTEAE----ERLTAAEE--ALADARAEAERIRREAAEETERLRTEAAERIRTlQAQAEQEAERLR---- 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1965 eeerrRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE-ARRLR-------ERAEQESARQLQLAQ-EAAQKRLQ 2035
Cdd:NF041483 640 -----TEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQEsADRVRaeaaaaaERVGTEAAEALAAAQeEAARRRRE 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2036 AEE---KAHAFAVQQKEQELQQTLQQEQSVLERLrseaeaarraaeeaeaareraEREAAQSRRQVEEAERlkqsaeeqa 2112
Cdd:NF041483 715 AEEtlgSARAEADQERERAREQSEELLASARKRV---------------------EEAQAEAQRLVEEADR--------- 764
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2113 qaqaqaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEET-DHQKSI 2191
Cdd:NF041483 765 --------------------------------RATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAaERTRTE 812
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2192 LDEELQRLKAEvteAARQRGQVEEELFSLRVQ-MEELGKLKARIEAEnralVLRDKDSAQRLLQEEAEKMKQVAEEAA-R 2269
Cdd:NF041483 813 AQEEADRVRSD---AYAERERASEDANRLRREaQEETEAAKALAERT----VSEAIAEAERLRSDASEYAQRVRTEASdT 885
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2270 LSVAAQEAARLRQLAEEDLAQQRALA---EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAq 2346
Cdd:NF041483 886 LASAEQDAARTRADAREDANRIRSDAaaqADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIA- 964
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2347 etqgfqktleterqrqlEMSAEAERLRLRVAE-MSRAQARAE---EDARRFRKQAEDIGERLyRTELATQEKVMLVQTLE 2422
Cdd:NF041483 965 -----------------EATGEAERLRAEAAEtVGSAQQHAErirTEAERVKAEAAAEAERL-RTEAREEADRTLDEARK 1026
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2423 TQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLL----QETQALQQSFLSEKDSLLQRERcieq 2498
Cdd:NF041483 1027 DANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVgaarKEAERIVAEATVEGNSLVEKAR---- 1102
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|.
gi 1920237970 2499 ekAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLaasMEEARRRQHEA 2549
Cdd:NF041483 1103 --TDADELLVGARRDATAIRERAEELRDRITGEIEEL---HERARRESAEQ 1148
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
37-146 |
6.43e-24 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 98.93 E-value: 6.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 37 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVirssrlprEKGRMRFHKLQNVQIALDYLRH 115
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVD-KKKV--------AASLSRFKKIENINLALSFAEK 71
|
90 100 110
....*....|....*....|....*....|.
gi 1920237970 116 RQVKLVNIRNDDIADGnPKLTLGLIWTIILH 146
Cdd:smart00033 72 LGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
167-262 |
6.47e-24 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 99.15 E-value: 6.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 167 LLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 245
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1920237970 246 VPQPDEKSIITYVSSLY 262
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
161-267 |
7.08e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 99.28 E-value: 7.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 161 MTAKEKLLLWSQRMVEGC-QGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 237
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1920237970 238 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 267
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1375-2235 |
1.17e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 111.30 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1375 REAQGLQRRMQEEVARREEVAVEAQEQKRSIQ------EELQHLR-QSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQ 1447
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLErqaekaERYKELKaELRELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1448 LEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEE 1527
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1528 LRLQAEEAERRLrqaeaerarqvqvaletaqrsaeAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATrraqqqaea 1607
Cdd:TIGR02168 335 LAEELAELEEKL-----------------------EELKEELESLEAELEELEAELEELESRLEELEEQLE--------- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1608 eraraeaerelerwQLKANEALRLRLQAEEVAQQKSLTQAEaekqkeeaerearrrgkaeEQAVRQRELAEQELEKQRQL 1687
Cdd:TIGR02168 383 --------------TLRSKVAQLELQIASLNNEIERLEARL-------------------ERLEDRRERLQQEIEELLKK 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1688 AEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRS 1767
Cdd:TIGR02168 430 LE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1768 TSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaeEDAVRQRAEAERVLAEKLAAiSEATRLKTEAEIALKE 1845
Cdd:TIGR02168 508 VKAllKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRL---QAVVVENLNAAKKAIAFLKQ-NELGRVTFLPLDSIKG 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1846 KEAENERLRRLAEDEAFQRRL--LEEQAAQHKADIEARLAQLRKASEselerqkglVEDTLRQRRQVEEEIL-------- 1915
Cdd:TIGR02168 584 TEIQGNDREILKNIEGFLGVAkdLVKFDPKLRKALSYLLGGVLVVDD---------LDNALELAKKLRPGYRivtldgdl 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1916 -----ALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQlaaeeerRRREAEERVQKSLAAEEEAARQ 1990
Cdd:TIGR02168 655 vrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRK-------ELEELEEELEQLRKELEELSRQ 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1991 RKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAfaVQQKEQELQQTLQQEQSVLERLRSEA 2070
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEELKALREAL 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2071 EAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAA 2150
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2151 DAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLK---AEVTEAARQRGQVEEELFSLRVQMEEL 2227
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvriDNLQERLSEEYSLTLEEAEALENKIED 965
|
....*...
gi 1920237970 2228 GKLKARIE 2235
Cdd:TIGR02168 966 DEEEARRR 973
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
34-149 |
3.73e-23 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 96.97 E-value: 3.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 34 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLPrerdvirssrlPREKGRMRFHKLQNVQIALD 111
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVD-----------KKKLNKSEFDKLENINLALD 70
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237970 112 YLRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 149
Cdd:pfam00307 71 VAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1301-2037 |
9.19e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.22 E-value: 9.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1301 QEYVDLRTRYSELS-TLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAAL--------EKQRQLAEA------ 1365
Cdd:TIGR02168 213 ERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLeelrlevsELEEEIEELqkelya 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1366 HAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQE------ELQHLRQSSEAEIQAKARQVEAAERSRLRIEE 1439
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDElaeelaELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1440 EIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELALRVQAEAEAAREKQ 1519
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI--EELLKKLEEAELKELQAELEELEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1520 RALQALEELRLQAEEAERRLRQAEAERarqvqvaletaqRSAEAELQsEHASFAEKTAQLERTLKEEHVAVVQLREEAtr 1599
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQAL------------DAAERELA-QLQARLDSLERLQENLEGFSEGVKALLKNQ-- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1600 raQQQAEAERARAEAERELERWQLKANEALRLRLQA---EEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQREL 1676
Cdd:TIGR02168 516 --SGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1677 AEQELEKQRQLA---EGTAQQRLAAEQELIRLR-AETEQG--EQQRQLLEEELA------------RLQREAAAATQKRR 1738
Cdd:TIGR02168 594 LKNIEGFLGVAKdlvKFDPKLRKALSYLLGGVLvVDDLDNalELAKKLRPGYRIvtldgdlvrpggVITGGSAKTNSSIL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1739 ELEAELAKVRAEMEvLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEA 1818
Cdd:TIGR02168 674 ERRREIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1819 ERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAED-----EAFQRRLLEEQAAQHKADIEARLAQLRKAS-ESE 1892
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeelKALREALDELRAELTLLNEEAANLRERLESlERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1893 LERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELgrirgtaEDTLRSKEQAEQEAARQRQLAAEEERRRRE 1972
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-------EALLNERASLEEALALLRSELEELSEELRE 905
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237970 1973 AEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE-ARRLRERA--EQESARQLQLAQEAAQKRLQAE 2037
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYslTLEEAEALENKIEDDEEEARRR 973
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1693-2485 |
9.66e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.22 E-value: 9.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1693 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAtQKRRELEAELAKVRAEmevLLASKARAEEESRSTSEKS 1772
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKA-ERYKELKAELRELELA---LLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1773 KQRLEAEagrFRELAEEAARLRALAEEAKRQRQLAEEDAvrqrAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENER 1852
Cdd:TIGR02168 248 LKEAEEE---LEELTAELQELEEKLEELRLEVSELEEEI----EELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1853 LRRLAEDEAFQRRLLEEQAAQHKADIEaRLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFekaaagkAELE 1932
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV-------AQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1933 LELGRIRGTAEDTLRSKEQAEQEAARQRQ-LAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRL 2011
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2012 RERAEQESARQLQLAQE--AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAER 2089
Cdd:TIGR02168 473 AEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2090 EAAQSRRQVEEAerLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAaDAEMEKHKQFAeqaLRQKA 2169
Cdd:TIGR02168 553 ENLNAAKKAIAF--LKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKF-DPKLRKALSYL---LGGVL 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2170 QVEQELTALRLQlEETDHQKSI--LDEELQRLKAEVTEAARQRGQVeeeLFSLRVQMEELGKLKARIEAENRAL--VLRD 2245
Cdd:TIGR02168 627 VVDDLDNALELA-KKLRPGYRIvtLDGDLVRPGGVITGGSAKTNSS---ILERRREIEELEEKIEELEEKIAELekALAE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2246 KDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE-----------KMQAVQEATRLKA 2314
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaeieeleerLEEAEEELAEAEA 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2315 EAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRlrvaEMSRAQARAEEDARRFR 2394
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE----DLEEQIEELSEDIESLA 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2395 KQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTvRQEQLLQE 2474
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL-RLEGLEVR 937
|
810
....*....|.
gi 1920237970 2475 TQALQQSFLSE 2485
Cdd:TIGR02168 938 IDNLQERLSEE 948
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
163-262 |
9.87e-23 |
|
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: 95.71 E-value: 9.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 163 AKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 242
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1920237970 243 D-VDVPQPDEKSIITYVSSLY 262
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1864-2505 |
1.40e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.33 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1864 RRLLEEQA--AQHKADIEARLAQLRKASE---------SELERQKglveDTLRQRRQVEEEILALKGSFEKAaagkaELE 1932
Cdd:COG1196 158 RAIIEEAAgiSKYKERKEEAERKLEATEEnlerledilGELERQL----EPLERQAEKAERYRELKEELKEL-----EAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1933 LELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR 2012
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2013 ERAEQESARQLQLAQEAAQKRLQAEEKAhafavqqkeqelqqtlqqeqsvlERLRSEAEAARRAAEEAEAARERAEREAA 2092
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELE-----------------------EELEELEEELEEAEEELEEAEAELAEAEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2093 QSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVE 2172
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2173 QELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAenrALVLRDKDSAQRL 2252
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG---VKAALLLAGLRGL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2253 LQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARR 2332
Cdd:COG1196 523 AGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2333 LQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQ 2412
Cdd:COG1196 603 LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2413 EKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQR 2492
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
650
....*....|...
gi 1920237970 2493 ERcIEQEKAKLEQ 2505
Cdd:COG1196 763 EE-LERELERLER 774
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1329-2040 |
1.59e-22 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 107.60 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1329 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLA-EAHAQAKAQAEREAQGLQRRMQEEVARreeVAVEAQEQKRSIQE 1407
Cdd:NF041483 254 RQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAkEAAAKQLASAESANEQRTRTAKEEIAR---LVGEATKEAEALKA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1408 ELQHLRQSSEAEiqAKARQVEAAERSRLRIEEEirvvrlqlEATERQRGGAEGElQALRARAEEAEAQKRQAQEEAERLR 1487
Cdd:NF041483 331 EAEQALADARAE--AEKLVAEAAEKARTVAAED--------TAAQLAKAARTAE-EVLTKASEDAKATTRAAAEEAERIR 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1488 RQVQDETQRKRQAEAELALRVQAEAEAAREKQRAlqalEELRLQaEEAeRRLRqAEAERARqvqvaletaqrsaeaelqs 1567
Cdd:NF041483 400 REAEAEADRLRGEAADQAEQLKGAAKDDTKEYRA----KTVELQ-EEA-RRLR-GEAEQLR------------------- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1568 ehasfAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELErwqlkANEALRLRLQAEEVAqqKSLTQA 1647
Cdd:NF041483 454 -----AEAVAEGERIRGEARREAVQQIEEAARTAEELLTKAKADADELRSTA-----TAESERVRTEAIERA--TTLRRQ 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1648 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA-AEQELIRLRAETEQ----GEQQRQLLEEE 1722
Cdd:NF041483 522 AEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEErltaAEEALADARAE 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1723 LARLQREAAAATQKRRELEAE-----LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrelAEEAARLRALA 1797
Cdd:NF041483 602 AERIRREAAEETERLRTEAAErirtlQAQAEQEAERLRTEAAADASAARAEGENVAVRLRSEA------AAEAERLKSEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1798 EE-AKRQRQLAEEDAVRQRAEAERVLAeklAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrllEEQAAQHKA 1876
Cdd:NF041483 676 QEsADRVRAEAAAAAERVGTEAAEALA---AAQEEAARRRREAEETLGSARAEADQERERAREQS------EELLASARK 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1877 DIEARLAQLRKASESELERQKGLV---EDTLRQRR--------QVEEEILALKGSFEKAAA-GKAELELELGRIRGtaeD 1944
Cdd:NF041483 747 RVEEAQAEAQRLVEEADRRATELVsaaEQTAQQVRdsvaglqeQAEEEIAGLRSAAEHAAErTRTEAQEEADRVRS---D 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1945 TLRSKEQAEQEAARQRQlaaeeerrrreaeERVQKSLAAEEEAARQRKAALEEVERLKAKVEE-ARRLRERAeqeSARQL 2023
Cdd:NF041483 824 AYAERERASEDANRLRR-------------EAQEETEAAKALAERTVSEAIAEAERLRSDASEyAQRVRTEA---SDTLA 887
|
730
....*....|....*..
gi 1920237970 2024 QLAQEAAQKRLQAEEKA 2040
Cdd:NF041483 888 SAEQDAARTRADAREDA 904
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
165-265 |
1.72e-22 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 94.84 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 165 EKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 244
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1920237970 245 DVPQPDEKSIITYVSSLYDAM 265
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
162-260 |
2.08e-22 |
|
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: 94.61 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 162 TAKEKLLLWSQRMVEGCqglRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 240
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1920237970 241 PEDVDVPQPDEKSIITYVSS 260
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1672-2442 |
2.75e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 106.68 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1672 RQRELAEQELEKQRQLAEgtaqqrlaAEQELIRLRAETeqgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVRAEM 1751
Cdd:TIGR02168 207 RQAEKAERYKELKAELRE--------LELALLVLRLEE---------LREELEELQEELKEAEEELEELTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1752 EVLLASKARAEEEsrstsekskqrLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISE 1831
Cdd:TIGR02168 270 EELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1832 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQH---KADIEARLAQLRKASeSELERQKGLVEDTLRQRR 1908
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetlRSKVAQLELQIASLN-NEIERLEARLERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1909 QVEEEILALKGSFEKAAagKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRrreaeervQKSLAAEEEAA 1988
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA--------LDAAERELAQL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1989 RQRKAALEEV-ERLKAKVEEARRLRERAEQ------------ESARQLQLAQEAA-QKRLQA------EEKAHAFAVQQK 2048
Cdd:TIGR02168 488 QARLDSLERLqENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEAAlGGRLQAvvvenlNAAKKAIAFLKQ 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2049 EQELQQTLQQEQSVLER-LRSEAEAARRAAEEAEAARERAEREAAQSRRQVEE-------AERLKQSAEEQAQAQAQAQA 2120
Cdd:TIGR02168 568 NELGRVTFLPLDSIKGTeIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGYRI 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2121 AAEKLRKEAEQEAARRAQAEQAALRQKQaaDAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLK 2200
Cdd:TIGR02168 648 VTLDGDLVRPGGVITGGSAKTNSSILER--RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2201 AEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAEnRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQ----- 2275
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE-IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrea 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2276 ------------EAARLRQLAEEDLAQQRALAEKML----KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQ 2339
Cdd:TIGR02168 805 ldelraeltllnEEAANLRERLESLERRIAATERRLedleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2340 MAQQLAQ---ETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDigerLYRTELATQEKvm 2416
Cdd:TIGR02168 885 LEEALALlrsELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE----EYSLTLEEAEA-- 958
|
810 820
....*....|....*....|....*.
gi 1920237970 2417 LVQTLETQRQQSDRDAERLREAIAEL 2442
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
162-262 |
2.97e-22 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 94.41 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 162 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 241
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 1920237970 242 EDVDVPQ-PDEKSIITYVSSLY 262
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1325-2041 |
3.32e-22 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 106.45 E-value: 3.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1325 SETLRRMEEEERL---AEQQRAE---ERERLaEVEAALEKQRQLAEAHAQAK---AQAEREAQGLQRRMQEEVAR-REEV 1394
Cdd:NF041483 433 AKTVELQEEARRLrgeAEQLRAEavaEGERI-RGEARREAVQQIEEAARTAEellTKAKADADELRSTATAESERvRTEA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1395 AVEAQEQKRSIQEELQHLRqsSEAEiQAKARQVEAAERSRLRIEEEIRVVRLQLE-ATERQRGGAEGELQALRARAEE-- 1471
Cdd:NF041483 512 IERATTLRRQAEETLERTR--AEAE-RLRAEAEEQAEEVRAAAERAARELREETErAIAARQAEAAEELTRLHTEAEErl 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1472 --AEAQKRQAQEEAERLRRQVQDETQRKRQAEAE--LALRVQAEAEAAREKQRALQALEELRLQAEEAERRLR-QAEAER 1546
Cdd:NF041483 589 taAEEALADARAEAERIRREAAEETERLRTEAAEriRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLRsEAAAEA 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1547 ARQVQVALETAQRsaeaeLQSEHASFAEKTAQlertlkeehvavvqlreeatrraqqqaeaeraraeaerelerwqlKAN 1626
Cdd:NF041483 669 ERLKSEAQESADR-----VRAEAAAAAERVGT---------------------------------------------EAA 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1627 EALrlrlqaeevaqqksltqaeaekqkeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELI--- 1703
Cdd:NF041483 699 EAL----------------------------------AAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasa 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1704 RLRAETEQGEQQRqLLEEELARLQREAAAATQKRRELEAELAKV--RAEMEV--LLASKARAEEESRSTSEKSKQRLEAE 1779
Cdd:NF041483 745 RKRVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVRDSVAGLqeQAEEEIagLRSAAEHAAERTRTEAQEEADRVRSD 823
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1780 AGRFRELA-EEAARLRALA-EEAKRQRQLAEEDAVRQRAEAERVLAEklaAISEATRLKTEAEIALKEKEAENERLRRLA 1857
Cdd:NF041483 824 AYAERERAsEDANRLRREAqEETEAAKALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADA 900
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1858 EDEAFQRRllEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAElelelgR 1937
Cdd:NF041483 901 REDANRIR--SDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAE------R 972
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1938 IRGTAEDTLRSkeqAEQEAARQRQLAAEEERRrreaeervqkslaAEEEAARQRKAALEEVERL--KAKVEEARRLRERA 2015
Cdd:NF041483 973 LRAEAAETVGS---AQQHAERIRTEAERVKAE-------------AAAEAERLRTEAREEADRTldEARKDANKRRSEAA 1036
|
730 740
....*....|....*....|....*.
gi 1920237970 2016 EQESARQLQLAQEAAQKRLQAEEKAH 2041
Cdd:NF041483 1037 EQADTLITEAAAEADQLTAKAQEEAL 1062
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1979-2594 |
5.05e-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: 5.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1979 KSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQ 2058
Cdd:COG1196 203 EPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2059 EQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQ 2138
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2139 AEQAALRQKQAADAEMEKHKQFAEQALRQkaqvEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELF 2218
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEA----LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2219 SLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM 2298
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2299 LKEKMQAVQEATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRV 2376
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2377 AEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLL 2456
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2457 QLKSEEMQTVRQEQLLQETQALQQsflsekdsLLQRERCIEQEKAKLEQlfqdevakaqalreeqqrqqqqmqqekqqlA 2536
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAE--------EEEERELAEAEEERLEE------------------------------E 720
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237970 2537 ASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRA 2594
Cdd:COG1196 721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1776-2591 |
7.09e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.14 E-value: 7.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1776 LEAEAGRFRELAEEAA---RLRALAEEAKRQRQLAEEDAVR------------QRAEAERVLAEKLAAISEATRlKTEAE 1840
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAgisKYKERRKETERKLERTRENLDRledilnelerqlKSLERQAEKAERYKELKAELR-ELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1841 IALKEKEAENERLRRLAEDEAFQRRLLEEQAAQhKADIEARLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEILAL 1917
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAE-LQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1918 KGSFEKAAAGKAELELELgrirgtaEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 1997
Cdd:TIGR02168 308 RERLANLERQLEELEAQL-------EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1998 VERLKAKVEEARR--LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQ-QKEQELQQTLQQEQSVLERLRSEAEAAR 2074
Cdd:TIGR02168 381 LETLRSKVAQLELqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2075 RAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQaeqaaLRQKQAADAEM 2154
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV-----LSELISVDEGY 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2155 EKHKQFAEQALRQKAQVEQELTALRLQleetDHQKsilDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARI 2234
Cdd:TIGR02168 536 EAAIEAALGGRLQAVVVENLNAAKKAI----AFLK---QNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2235 EAENRA-----------LVLRDKDSAQRLLQEEAEKMKQVAEEAARLS---VAAQEAARLRQLAeedLAQQRALAEkmLK 2300
Cdd:TIGR02168 609 KFDPKLrkalsyllggvLVVDDLDNALELAKKLRPGYRIVTLDGDLVRpggVITGGSAKTNSSI---LERRREIEE--LE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2301 EKMQAVQEAtrlkaEAELLQQQKELAQEQarrlqedkeqmaQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMS 2380
Cdd:TIGR02168 684 EKIEELEEK-----IAELEKALAELRKEL------------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2381 RAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKS 2460
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2461 EEMQTvRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQMQQEKQQLAASME 2540
Cdd:TIGR02168 827 ESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELR 904
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1920237970 2541 EARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEE 2591
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
162-266 |
7.20e-22 |
|
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: 93.32 E-value: 7.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 162 TAKEKLLLWSQRMVEGcQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 241
Cdd:cd21245 3 KAIKALLNWVQRRTRK-YGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1920237970 242 EDVDVPQPDEKSIITYVSSLYDAMP 266
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1003-1548 |
7.65e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.02 E-value: 7.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1003 ARECAQRITEQQKAQAEVDGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1082
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1083 RSTQEAEEVLRAHEEQLKEAQAvpATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVE 1162
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1163 RWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALL 1242
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1243 EDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaSPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQYIR 1322
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL---LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1323 FISETLRRMEEEERLAEQQRAE----ERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEA 1398
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAGRATflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1399 QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegELQALRARAEEAEAQKRQ 1478
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE-----EELELEEALLAEEEEERE 708
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1479 AQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERAR 1548
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
33-150 |
4.22e-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: 4.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 33 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlprEKGRMRFHKLQNVQIALDY 112
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHN---------QRPTFRQMQLENVSVALEF 89
|
90 100 110
....*....|....*....|....*....|....*...
gi 1920237970 113 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 150
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 ... |
33-150 |
6.07e-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: 91.68 E-value: 6.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 33 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlpREKGRMRFHKLQNVQIALDY 112
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKY---------HQRPTFRQMQLENVSVALEF 86
|
90 100 110
....*....|....*....|....*....|....*...
gi 1920237970 113 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 150
Cdd:cd21309 87 LDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1472-2606 |
1.14e-20 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 101.44 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1472 AEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAE--AEAAREKQRALQALEELRLQAE-EAERRLRQAEAERAR 1548
Cdd:NF041483 81 AQIQADQLRADAERELRDARAQTQRILQEHAEHQARLQAElhTEAVQRRQQLDQELAERRQTVEsHVNENVAWAEQLRAR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1549 QVQVA---LETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVvqlREEATRRAQQQAEAERARAEAERELERWQLKA 1625
Cdd:NF041483 161 TESQArrlLDESRAEAEQALAAARAEAERLAEEARQRLGSEAESA---RAEAEAILRRARKDAERLLNAASTQAQEATDH 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1626 NEALRLRLQAE-EVAQQKSltqaeaekqkeeaereaRRRGKAEEQAVRQrelAEQELEKQRQLAEGTAQQrlAAEQELIR 1704
Cdd:NF041483 238 AEQLRSSTAAEsDQARRQA-----------------AELSRAAEQRMQE---AEEALREARAEAEKVVAE--AKEAAAKQ 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1705 LRAETEQGEQQRQLLEEELARLQREAAA-ATQKRRELEAELAKVRAEMEVLLAS---KARAEEESRSTSEKSKQRLEAEA 1780
Cdd:NF041483 296 LASAESANEQRTRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVAEaaeKARTVAAEDTAAQLAKAARTAEE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1781 GRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAI---------------SEATRLKTEAEIALKE 1845
Cdd:NF041483 376 VLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvelqEEARRLRGEAEQLRAE 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1846 KEAENERLRRLAEDEAFQR-----RLLEEQAAQHKADIEarlaQLRKASESELERQKG-LVEDTLRQRRQVEEeilALKG 1919
Cdd:NF041483 456 AVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADAD----ELRSTATAESERVRTeAIERATTLRRQAEE---TLER 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1920 SFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQ------LAAEEERRRREAEERVQKSLAAEEEAARQRKA 1993
Cdd:NF041483 529 TRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQaeaaeeLTRLHTEAEERLTAAEEALADARAEAERIRRE 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1994 ALEEVERLKAKV-EEARRLRERAEQESARqlqLAQEAAQKRLQAEEKAHAFAVqqkeqelqqtlqqeqsvleRLRSEAEa 2072
Cdd:NF041483 609 AAEETERLRTEAaERIRTLQAQAEQEAER---LRTEAAADASAARAEGENVAV-------------------RLRSEAA- 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2073 arraaeeaeaareraereaaqsrrqvEEAERLKqsaeeqaqaqAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQaada 2152
Cdd:NF041483 666 --------------------------AEAERLK----------SEAQESADRVRAEAAAAAERVGTEAAEALAAAQ---- 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2153 emekhkqfaEQALRQKAQVEQELTALRLQLEEtdhqksildeelqrlkaevtEAARQRGQVEEELFSLRVQMEELGKLKA 2232
Cdd:NF041483 706 ---------EEAARRRREAEETLGSARAEADQ--------------------ERERAREQSEELLASARKRVEEAQAEAQ 756
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2233 RI--EAENRA--LVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAA-RLRQLAEEDLAQQRALAekmLKEKMQAVQ 2307
Cdd:NF041483 757 RLveEADRRAteLVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAAeRTRTEAQEEADRVRSDA---YAERERASE 833
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2308 EATRLKAEAellQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLemsAEAERlrlrvaEMSRAQARAE 2387
Cdd:NF041483 834 DANRLRREA---QEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDTL---ASAEQ------DAARTRADAR 901
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2388 EDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREaiaelehEKDKLKQEAQLLQLKSEEMQTVR 2467
Cdd:NF041483 902 EDANRIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERV-------RADAAAQAEQLIAEATGEAERLR 974
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2468 QEQLLQETQALQQSflsekdsllqrerciEQEKAKLEQLFQDEVAKAQALReeqqrqqqqmqqekqqlAASMEEARRRQH 2547
Cdd:NF041483 975 AEAAETVGSAQQHA---------------ERIRTEAERVKAEAAAEAERLR-----------------TEAREEADRTLD 1022
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 2548 EAeegvrrQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIAPSR 2606
Cdd:NF041483 1023 EA------RKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTM 1075
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1084-1888 |
1.62e-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: 100.90 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1084 STQEAEEVLRAHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVER 1163
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1164 WRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLE 1243
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1244 DIERhgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQyirf 1323
Cdd:TIGR02168 401 EIER-----------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE---- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1324 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQE-EVARREEVAVEAQ--- 1399
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELiSVDEGYEAAIEAAlgg 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1400 -------EQKRSIQEELQHLRQSSE------AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALR 1466
Cdd:TIGR02168 546 rlqavvvENLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1467 ARAEEAEAQKRQAQEEAERLR-------------------RQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEE 1527
Cdd:TIGR02168 626 LVVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRK 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1528 LRLQAEEAERRLRQAEAERARQVqvaleTAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQqqaea 1607
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQI-----SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE----- 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1608 eraraeaerelerwQLKANEALRLRLQAeEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELaEQELEKQRQL 1687
Cdd:TIGR02168 776 --------------ELAEAEAEIEELEA-QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL-ERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1688 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAE---EE 1764
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRrelEE 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1765 SRSTSEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEDAVRQRAEAERvLAEKLAAISEATRLkteaeiAL 1843
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLA------AI 992
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1920237970 1844 KEKEAENERLRRLaedeafqrrlleeqaAQHKADIEARLAQLRKA 1888
Cdd:TIGR02168 993 EEYEELKERYDFL---------------TAQKEDLTEAKETLEEA 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1985-2604 |
3.49e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.63 E-value: 3.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1985 EEAARQRKAALEEVERLKAKVEEARR----LRERAEQ-ESARQLQlaqeAAQKRLQAEEKAHAFAVQQKEqelqqtlqqe 2059
Cdd:COG1196 175 EEAERKLEATEENLERLEDILGELERqlepLERQAEKaERYRELK----EELKELEAELLLLKLRELEAE---------- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2060 qsvLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQsaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQA 2139
Cdd:COG1196 241 ---LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE-------------EAQAEEYELLAELARLEQDI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2140 EQAALRQKQAADAEMEKHKQfAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2219
Cdd:COG1196 305 ARLEERRRELEERLEELEEE-LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2220 LRVQMEELgklkARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2299
Cdd:COG1196 384 LAEELLEA----LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2300 KEKmQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAER---LRLRV 2376
Cdd:COG1196 460 ALL-ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveAAYEA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2377 AEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLL 2456
Cdd:COG1196 539 ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2457 Q--LKSEEMQTVRQEQLLQETQALQQSFLS---EKDSLLQRERCIEQEKAKLEQlfqdEVAKAQALREEQQRQQQQMQQE 2531
Cdd:COG1196 619 GdtLLGRTLVAARLEAALRRAVTLAGRLREvtlEGEGGSAGGSLTGGSRRELLA----ALLEAEAELEELAERLAEEELE 694
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237970 2532 KQQLAASMEEARRRQHEAEEGVRRQQEELQRLAqqqqqqEKLLAEENQRLRERLQHLEEERRAALARSEEIAP 2604
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALE------EQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1086-1855 |
8.93e-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: 98.21 E-value: 8.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1086 QEAEEVLRAHEEQLKEAQAVpatlpeLEATKAALKKLRAQAEAQQPvFDALRDELRgaqevgerlqqrHGERDVEVERWR 1165
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDI------LNELERQLKSLERQAEKAER-YKELKAELR------------ELELALLVLRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1166 ErvtlLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVRE---QLRQEKALL 1242
Cdd:TIGR02168 236 E----LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1243 EDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPV-----ASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLT 1317
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEElesleAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1318 SQYIRFISETLRRMEEE-ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAV 1396
Cdd:TIGR02168 392 ELQIASLNNEIERLEARlERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1397 EAQEQKRSIQEELQHLR------QSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAE----GELQALR 1466
Cdd:TIGR02168 472 EAEQALDAAERELAQLQarldslERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalgGRLQAVV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1467 ARAEEAEAQKRQAQEEAERLRR----------QVQDETQRKRQAEAELALRVQAEAEAAREK-QRALQALEELRLQAEEA 1535
Cdd:TIGR02168 552 VENLNAAKKAIAFLKQNELGRVtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKlRKALSYLLGGVLVVDDL 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1536 ERRLRQAEAERARQVQVALE---------TAQRSAEAEL-----QSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRA 1601
Cdd:TIGR02168 632 DNALELAKKLRPGYRIVTLDgdlvrpggvITGGSAKTNSsilerRREIEELEEKIEELEEKIAELEKALAELRKELEELE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1602 QQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQEL 1681
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1682 EKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARA 1761
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1762 EEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE------DAVRQRAEAERVLAEKLAAISEATRL 1835
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEElreklaQLELRLEGLEVRIDNLQERLSEEYSL 951
|
810 820
....*....|....*....|.
gi 1920237970 1836 KTEAEIALKEK-EAENERLRR 1855
Cdd:TIGR02168 952 TLEEAEALENKiEDDEEEARR 972
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
166-263 |
1.91e-19 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 86.63 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 166 KLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 244
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1920237970 245 DVPQPDEKSIITYVSSLYD 263
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1332-2068 |
2.36e-19 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 97.20 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1332 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaQAKAQAEREAQGLQRRMQEEVARreeVAVEAQEQKRSIQEELQh 1411
Cdd:NF041483 560 EETERAIAARQAEAAEELTRLHTEAEERLTAAE---EALADARAEAERIRREAAEETER---LRTEAAERIRTLQAQAE- 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1412 lrqsSEAEiqaKARQVEAAERSRLRIEEEIRVVRLQLEA-TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQV 1490
Cdd:NF041483 633 ----QEAE---RLRTEAAADASAARAEGENVAVRLRSEAaAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQ 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1491 QDETQRKRQAEAELAlrvQAEAEAAREKQRALQALEELrlqAEEAERRLRQAEAERARQVqvalETAQRSAeaelqSEHA 1570
Cdd:NF041483 706 EEAARRRREAEETLG---SARAEADQERERAREQSEEL---LASARKRVEEAQAEAQRLV----EEADRRA-----TELV 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1571 SFAEKTAQLERTlkeehvAVVQLREEATRraqqqaeaeraraeaerelerwqlkanEALRLRLQAEEVAQQksLTQAEAE 1650
Cdd:NF041483 771 SAAEQTAQQVRD------SVAGLQEQAEE---------------------------EIAGLRSAAEHAAER--TRTEAQE 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1651 KQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQ--------------- 1715
Cdd:NF041483 816 EADRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSE---AIAEAERLRSDASEYAQRvrteasdtlasaeqd 892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1716 ----RQLLEEELARLQREAAA-----ATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrel 1786
Cdd:NF041483 893 aartRADAREDANRIRSDAAAqadrlIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEA------ 966
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1787 AEEAARLRALAEEAKRQrqlAEEDAVRQRAEAERVLAEklaAISEATRLKTEAEialkekeAENERLRRLAEDEAFQRR- 1865
Cdd:NF041483 967 TGEAERLRAEAAETVGS---AQQHAERIRTEAERVKAE---AAAEAERLRTEAR-------EEADRTLDEARKDANKRRs 1033
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1866 ---------LLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELG 1936
Cdd:NF041483 1034 eaaeqadtlITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVEKARTDADELLVGAR 1113
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1937 R----IRGTAEDtLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLK--------AK 2004
Cdd:NF041483 1114 RdataIRERAEE-LRDRITGEIEELHERARRESAEQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANseaskvriAA 1192
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2005 VEEARRLRERAEQESARQLQLAQ------EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRS 2068
Cdd:NF041483 1193 VKKAEGLLKEAEQKKAELVREAEkikaeaEAEAKRTVEEGKRELDVLVRRREDINAEISRVQDVLEALES 1262
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
162-261 |
1.39e-18 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 84.07 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 162 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 241
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1920237970 242 ED-VDVPQPDEKSIITYVSSL 261
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
780-846 |
3.39e-18 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 81.15 E-value: 3.39e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237970 780 QLKPRSpaHPMRGRVPLLAVCDYKQVEVTVHKGDECQMVGPAQPFYWKVLGSSCSEAAMPSVCFLVP 846
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
162-262 |
4.07e-18 |
|
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: 82.78 E-value: 4.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 162 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 241
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1920237970 242 EDVDV--PQPDEKSIITYVSSLY 262
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
158-263 |
4.23e-18 |
|
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: 82.69 E-value: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 158 SEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 237
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1920237970 238 LLDPEDV-DVPQPDEKSIITYVSSLYD 263
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
165-261 |
4.61e-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: 82.36 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 165 EKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 240
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1920237970 241 PEDVDVPQPDEKSIITYVSSL 261
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1326-1914 |
6.61e-18 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 92.29 E-value: 6.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1326 ETLRRMEEEERLAEQQR------AEERERLAEVEAALEKQRQLAEAHAQAKAQAERE-AQGLQRRMQEEVARREEVAVEA 1398
Cdd:COG4913 235 DDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRLWFAQRRLElLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1399 QEQKRSIQEELQHLRQ-----------SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATE-----------RQRG 1456
Cdd:COG4913 315 EARLDALREELDELEAqirgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAeefaalraeaaALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1457 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELrLQAEEAE 1536
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGEL-IEVRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1537 RRLRQAeAERarqvqvALETAQRSaeaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAER 1616
Cdd:COG4913 474 ERWRGA-IER------VLGGFALT----LLVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDF 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1617 ELERWQLKANEALRLR---LQAEEVAQ----QKSLTQAEAEKQKEEAEREARRRGKAEE-----QAVRQRELAEQELEK- 1683
Cdd:COG4913 543 KPHPFRAWLEAELGRRfdyVCVDSPEElrrhPRAITRAGQVKGNGTRHEKDDRRRIRSRyvlgfDNRAKLAALEAELAEl 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1684 QRQLAEGTAQ-QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA---ELAKVRAEMEVLLASKA 1759
Cdd:COG4913 623 EEELAEAEERlEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1760 RAEEESRSTSEKsKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRlKTEA 1839
Cdd:COG4913 703 ELEEELDELKGE-IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERID-ALRA 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1840 EIALKEKEAENERLRRLAEDEAFQ-------------RRLLEEQAAQHKADIEARLAQLRKasESELERQKGLVEDTLRQ 1906
Cdd:COG4913 781 RLNRAEEELERAMRAFNREWPAETadldadleslpeyLALLDRLEEDGLPEYEERFKELLN--ENSIEFVADLLSKLRRA 858
|
....*...
gi 1920237970 1907 RRQVEEEI 1914
Cdd:COG4913 859 IREIKERI 866
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1324-1895 |
2.91e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 89.71 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1324 ISETLRRMEEEERLAEQQR----------AEERERLAEVEAALEKQRQlaeahaqAKAQAEREAQGLQRRMQEEVARREE 1393
Cdd:PRK02224 218 LDEEIERYEEQREQARETRdeadevleehEERREELETLEAEIEDLRE-------TIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1394 vaveaqeqkrsIQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAE 1470
Cdd:PRK02224 291 -----------LEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1471 EAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELALRVQAEAEAAREKQRalQALEELRLQAEEAERRLRQAEAErarqv 1550
Cdd:PRK02224 360 ELREEAAELESELEEAREAV--EDRREEIEELEEEIEELRERFGDAPVDL--GNAEDFLEELREERDELREREAE----- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1551 qvaLETAQRSAEAELQSEHASFAE-KTAQLERTLKE-EHVAVVQLREEatrraqqqaeaeraraeaerelerwQLKANEA 1628
Cdd:PRK02224 431 ---LEATLRTARERVEEAEALLEAgKCPECGQPVEGsPHVETIEEDRE-------------------------RVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1629 LRLRLQAEEVAQQKSLTQAEAEKqkeeaerearrrgKAEEQAVR---QRELAEQELEKQRQLAEGTAQQRLAAEQELIRL 1705
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAEDLV-------------EAEDRIERleeRREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1706 RAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAeMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRE 1785
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERRER 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1786 LAEEAARLRALAEEAKRQRqLAEEDAVRQRAEA--ERVlAEKLAAISEAtRLKTEAEIALKEKEAEN-ERLR-RLAEDEA 1861
Cdd:PRK02224 629 LAEKRERKRELEAEFDEAR-IEEAREDKERAEEylEQV-EEKLDELREE-RDDLQAEIGAVENELEElEELReRREALEN 705
|
570 580 590
....*....|....*....|....*....|....*.
gi 1920237970 1862 FQRRL--LEEQAAQHKADIEARLAQLRKASESELER 1895
Cdd:PRK02224 706 RVEALeaLYDEAEELESMYGDLRAELRQRNVETLER 741
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
36-145 |
5.21e-17 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 79.30 E-value: 5.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 36 KKTFTKWVNKHL-IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpREKGRMRFHKLQNVQIALDYLR 114
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKI----------NKKPKSPFKKRENINLFLNACK 70
|
90 100 110
....*....|....*....|....*....|...
gi 1920237970 115 HRQV-KLVNIRNDDI-ADGNPKLTLGLIWTIIL 145
Cdd:cd00014 71 KLGLpELDLFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
35-147 |
5.48e-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: 79.16 E-value: 5.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 35 QKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPRerdvirssrlPREKGRMRFHKLQNVQIALDY 112
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPG----------IHSRPKTRAQKLENIQACLQF 70
|
90 100 110
....*....|....*....|....*....|....*
gi 1920237970 113 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 147
Cdd:cd21212 71 LAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1384-2289 |
6.40e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 88.88 E-value: 6.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1384 MQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERsrlriEEEIRVVRLQLEATERQRGGAEGELQ 1463
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA-----KKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1464 ALRARAEEAEAQKRQAQEEAERLRRQVQDetqrKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAE 1543
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIE----KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1544 AERARQVQVALETAQRSAEAELQSEHASFAEKtaqleRTLKEEHVAVVQLREEatrraqqqaeaeraraeaerelerwql 1623
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEEL-----EKELKELEIKREAEEE--------------------------- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1624 kANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELI 1703
Cdd:pfam02463 357 -EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1704 RLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEA----- 1778
Cdd:pfam02463 436 EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKvllal 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1779 -EAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLA 1857
Cdd:pfam02463 516 iKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIA 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1858 EDEAFQR--RLLEEQAAQHKADIEARLA----QLRKASESELERQKGLVEDTLRQRRQVEEEILALKG---SFEKAAAGK 1928
Cdd:pfam02463 596 VLEIDPIlnLAQLDKATLEADEDDKRAKvvegILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEvkaSLSELTKEL 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1929 AELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEA 2008
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2009 RRLRERAEQESARQLQLAQEAAQKRLQAEEKAhafAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAE 2088
Cdd:pfam02463 756 RLKKEEKEEEKSELSLKEKELAEEREKTEKLK---VEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKE 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2089 REAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQaadAEMEKHKQFAEQALRQK 2168
Cdd:pfam02463 833 EELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKE---EKEKEEKKELEEESQKL 909
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2169 AQVEQELTALRLQLEETDHQKSILDEELQRLKAEvteaarQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDS 2248
Cdd:pfam02463 910 NLLEEKENEIEERIKEEAEILLKYEEEPEELLLE------EADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEF 983
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 1920237970 2249 AQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLA 2289
Cdd:pfam02463 984 EEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1331-2202 |
6.56e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 88.88 E-value: 6.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1331 MEEEERLAEQQRAEERERLAEVEaaLEKQRQLAEAHAQAKAQAEREAQGLqrRMQEEVARREEVAVEAQEQKRSIQEELQ 1410
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELK--LKEQAKKALEYYQLKEKLELEEEYL--LYLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1411 HLRQSSEAEIQakarqvEAAERSRLRIEEE--IRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR 1488
Cdd:pfam02463 255 SSKQEIEKEEE------KLAQVLKENKEEEkeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1489 QVQDETQRKRQAEAELAL--RVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERA--RQVQVALETAQRSAEAE 1564
Cdd:pfam02463 329 ELKKEKEEIEELEKELKEleIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAakLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1565 LQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSL 1644
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1645 TQAEAEKQKEEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEE 1721
Cdd:pfam02463 489 LLSRQKLEERSQKESKARSGLKVLLALIKDGvggRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1722 ELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEaeagrfRELAEEAARLRALAEEAK 1801
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKV------VEGILKDTELTKLKESAK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1802 RQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEAR 1881
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1882 LAQLRKaseSELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQ 1961
Cdd:pfam02463 723 LADRVQ---EAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1962 laaeeerrrreaeervQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAH 2041
Cdd:pfam02463 800 ----------------EEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEI 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2042 AFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAA 2121
Cdd:pfam02463 864 TKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2122 AEKLRKEAEQEAARRAQAEQAALRQKQAadAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKA 2201
Cdd:pfam02463 944 EADEKEKEENNKEEEEERNKRLLLAKEE--LGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
.
gi 1920237970 2202 E 2202
Cdd:pfam02463 1022 F 1022
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
953-1862 |
7.32e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 88.97 E-value: 7.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 953 QQLLQSLEQGEQEESRCQRCISELKDiRLQLEACETRTVHRLRLPLDKEPARECAQRITEQQKAQAEVDGLGKGVARLSA 1032
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1033 EAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL---------KTISLVIRSTQEAEEVLRAHEEQLKEAQ 1103
Cdd:TIGR02169 252 ELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvkEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1104 AVPATL-PELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERvtlllerwqavlaqT 1182
Cdd:TIGR02169 322 ERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE--------------L 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1183 DVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAvplansqavreqlrqekalleDIERHGEKVEECQRFAKQY 1262
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1263 INAIKDYELQLVTYKAQLepvaspakkpkvqsgsESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQR 1342
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1343 AEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGlqrRMQEEVARREEVAVEAQEQKRS-------------IQEEL 1409
Cdd:TIGR02169 511 AVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGN---RLNNVVVEDDAVAKEAIELLKRrkagratflplnkMRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1410 QHLRQSSEA--------------EIQAKARQV-------EAAERSRlRIEEEIRVVRLQLEATERQ---RGGA-EGELQA 1464
Cdd:TIGR02169 588 RDLSILSEDgvigfavdlvefdpKYEPAFKYVfgdtlvvEDIEAAR-RLMGKYRMVTLEGELFEKSgamTGGSrAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1465 LRARAEEAEAQkrQAQEEAERLRRQVQDETQRKRQAEAELalrvqaeAEAAREKQRALQALEELRLQAEEAERRlRQAEA 1544
Cdd:TIGR02169 667 LFSRSEPAELQ--RLRERLEGLKRELSSLQSELRRIENRL-------DELSQELSDASRKIGEIEKEIEQLEQE-EEKLK 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1545 ERARQVQVALETAQRSAEAElQSEHASFAEKTAQLERTLKEEHVAVVQLREEatrraqqqaeaeraraeaeRELERWQLK 1624
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENV-KSELKELEARIEELEEDLHKLEEALNDLEAR-------------------LSHSRIPEI 796
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1625 ANEalrLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAEQELIR 1704
Cdd:TIGR02169 797 QAE---LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE-ELEEELEE 872
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1705 LRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRStsekskqrLEAEAGRFR 1784
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE--------IEDPKGEDE 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1785 ELAEEAARLRALAEEAKR-QRQLAEEDAVRQRA--EAERVLAEKLAAISEATRLKTEAEiALKEKEAENERLRRLAEDEA 1861
Cdd:TIGR02169 945 EIPEEELSLEDVQAELQRvEEEIRALEPVNMLAiqEYEEVLKRLDELKEKRAKLEEERK-AILERIEEYEKKKREVFMEA 1023
|
.
gi 1920237970 1862 F 1862
Cdd:TIGR02169 1024 F 1024
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
162-261 |
1.21e-16 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 78.36 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 162 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 241
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1920237970 242 ED-VDVPQPDEKSIITYVSSL 261
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1302-1955 |
1.23e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 88.20 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1302 EYVDLRTR-----YSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAERE 1376
Cdd:TIGR02169 212 RYQALLKEkreyeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL---LEELNKKIKDLGEEE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1377 AQGLQRRMQEEVARREEvAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAaersrlrIEEEIRVVRLQLEATERQRG 1456
Cdd:TIGR02169 289 QLRVKEKIGELEAEIAS-LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE-------LEREIEEERKRRDKLTEEYA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1457 GAEGELQALRARAEEAEAQKR--------------QAQEEAERLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRAL 1522
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAetrdelkdyrekleKLKREINELKRELDRLQEELQRLSEELA-DLNAAIAGIEAKINEL 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1523 QA-LEELRLQAEEAERRLRQAEAER--ARQVQVALETAQRSAEAELQS--EHASFAEKTAQLERTLKEEHVAVVQLREEa 1597
Cdd:TIGR02169 440 EEeKEDKALEIKKQEWKLEQLAADLskYEQELYDLKEEYDRVEKELSKlqRELAEAEAQARASEERVRGGRAVEEVLKA- 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1598 trraqQQAEAERARAEAERELERWQLKANEALRLRLQA-----EEVAQQK---------------SLTQAEAEKQKEEAE 1657
Cdd:TIGR02169 519 -----SIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvvedDAVAKEAiellkrrkagratflPLNKMRDERRDLSIL 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1658 REARRRGKA---------EEQAVR---QRELAEQELEKQRQL--------------------------AEGTAQQRLAAE 1699
Cdd:TIGR02169 594 SEDGVIGFAvdlvefdpkYEPAFKyvfGDTLVVEDIEAARRLmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEP 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1700 QELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLL----ASKARAEEESRSTSEKSKQR 1775
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEqeeeKLKERLEELEEDLSSLEQEI 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1776 LEAEAgrfrELAEEAARLRALaEEAKRQRQLAEED--------AVRQRAEAERVLAEKLAAISEATRlktEAEIALKEKE 1847
Cdd:TIGR02169 754 ENVKS----ELKELEARIEEL-EEDLHKLEEALNDlearlshsRIPEIQAELSKLEEEVSRIEARLR---EIEQKLNRLT 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1848 AENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKAsESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAG 1927
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
730 740
....*....|....*....|....*...
gi 1920237970 1928 KAELELELGRIRGTAEDTLRSKEQAEQE 1955
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1111-2037 |
6.03e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 85.79 E-value: 6.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1111 ELEATKAALKKLRAQAEAQQPVFDALRDELRGaqevgerlqqrhgerdveverwrervtlllerwqavlaqtdvRQRELE 1190
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQ------------------------------------------ELKLKE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1191 QLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALL-EDIERHGEKVEECQRFAKQYINAIKDY 1269
Cdd:pfam02463 205 QAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSkQEIEKEEEKLAQVLKENKEEEKEKKLQ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1270 ELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRtryselstltsqyIRFISETLRRMEEEERLAEQQRAEERERL 1349
Cdd:pfam02463 285 EEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE-------------KKKAEKELKKEKEEIEELEKELKELEIKR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1350 AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQsseaeiQAKARQVEA 1429
Cdd:pfam02463 352 EAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQ------LEDLLKEEK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1430 AERSRLRIEEEIRVVRLQLEATERQrggaegelqaLRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQ 1509
Cdd:pfam02463 426 KEELEILEEEEESIELKQGKLTEEK----------EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1510 AEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ-LERTLKEEHV 1588
Cdd:pfam02463 496 EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQkLVRALTELPL 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1589 AVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGK--A 1666
Cdd:pfam02463 576 GARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVslE 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1667 EEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAK 1746
Cdd:pfam02463 656 EGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKIN 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1747 VRAEMEVLLASKARAEEESRSTSEKSKQRLEAEagrfRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKL 1826
Cdd:pfam02463 736 EELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE----LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1827 AAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDT-LR 1905
Cdd:pfam02463 812 EEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELeSK 891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1906 QRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAArQRQLAAEEERRRREAEERVQKSLAAEE 1985
Cdd:pfam02463 892 EEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE-EADEKEKEENNKEEEEERNKRLLLAKE 970
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 1986 EAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAE 2037
Cdd:pfam02463 971 ELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1417-2343 |
6.78e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.50 E-value: 6.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1417 EAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEA-----QKRQAQEEAERLRRQVQ 1491
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellkEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1492 DETQRKRQAEAELALRVQAEAEAAR------EKQRALQALEELRLQAEEAE-----RRLRQAEAERARQVQVALETaqrs 1560
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGEleaeiASLERSIAEKERELEDAEER---- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1561 aEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQaeaeraraeaerelerwqlkanEALRLRLQAEEVAQ 1640
Cdd:TIGR02169 324 -LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL----------------------EDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1641 QKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1719
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1720 EEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAEAGRFRELAEeaarlral 1796
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGVHGTVAQLGS-------- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1797 aeeAKRQRQLAEEDAVRQRAEAERVLAEKLAAiseatrlktEAEIALKEKEAENER---LRRLAEDEAFQRRLLEEQAAQ 1873
Cdd:TIGR02169 533 ---VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKMRDERRDLSILSEDGVIG 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1874 HKADIEARLAQLRKASESELeRQKGLVEDTLRQRRQVEE-EILALKGS-FEKAAA--GKAElelelgRIRGTAEDTLRSK 1949
Cdd:TIGR02169 601 FAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLMGKyRMVTLEGElFEKSGAmtGGSR------APRGGILFSRSEP 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1950 EQAEQEAARqrqlaaeeerrrreaeervqkslaaEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ-----ESARQLQ 2024
Cdd:TIGR02169 674 AELQRLRER-------------------------LEGLKRELSSLQSELRRIENRLDELSQELSDASRkigeiEKEIEQL 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2025 LAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRseaeaarraAEEAEAARERAEREAAQSRRQVEEAERL 2104
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE---------EDLHKLEEALNDLEARLSHSRIPEIQAE 799
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2105 KQSAEeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEE 2184
Cdd:TIGR02169 800 LSKLE--------------EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2185 tdhqksiLDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRlLQEEAEKMKQVA 2264
Cdd:TIGR02169 866 -------LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK-LEALEEELSEIE 937
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 2265 EEAARLSVAAQEAARLRQLAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQ 2343
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
166-263 |
1.04e-15 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 75.69 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 166 KLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 244
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1920237970 245 DVPQPDEKSIITYVSSLYD 263
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1129-2039 |
1.16e-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: 84.84 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1129 QQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQA----------VLAQTDVRQRELEQLGRQLRY 1198
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeeMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1199 YRESADPLGAWLRDAKQR-QEQIQAVP--LANSQAVREQLRQEKALLE-DIERHGEKVEECQRFAKQYINAIKDYELQLV 1274
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKmQQHIQDLEeqLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1275 TYKAQLEPVASPAKK-PKVQSGSESIIQEyVDLRTRYSElstltsqyirfisETLRRMEEEERLAEQQRAEERERLAEVE 1353
Cdd:pfam01576 163 EFTSNLAEEEEKAKSlSKLKNKHEAMISD-LEERLKKEE-------------KGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1354 AalekqrQLAEAHAQAkAQAEREAQGLQRRMQEEVARREevavEAQEQKRSIQEELQHLRQSSEAEIQAKARqveaAERS 1433
Cdd:pfam01576 229 A------QIAELRAQL-AKKEEELQAALARLEEETAQKN----NALKKIRELEAQISELQEDLESERAARNK----AEKQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1434 RLRIEEEIRVVRLQLEATErqrgGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELalrvqaeA 1512
Cdd:pfam01576 294 RRDLGEELEALKTELEDTL----DTTAAQQELRSKREqEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL-------T 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1513 EAAREKQRALQALEELRlQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEktAQLERTLKEEHVAVVQ 1592
Cdd:pfam01576 363 EQLEQAKRNKANLEKAK-QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAEKLSKLQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1593 LREEATRRAQQQAEAERARAEAERELERWQLKANEALRlrlqAEEVAQQKSLTQAEAEKqkeeaerearrrgkaEEQAVR 1672
Cdd:pfam01576 440 SELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL----QEETRQKLNLSTRLRQL---------------EDERNS 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1673 QRELAEQELEKQRQLaegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAK------ 1746
Cdd:pfam01576 501 LQEQLEEEEEAKRNV----ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektkn 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1747 -VRAEMEVLLAS-------------------KARAEEESRSTS-EKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQ 1805
Cdd:pfam01576 577 rLQQELDDLLVDldhqrqlvsnlekkqkkfdQMLAEEKAISARyAEERDRAEAEA---REKETRALSLARALEEALEAKE 653
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1806 LAEEDAVRQRAEAERVLAEKLAA---ISEATRLKTEAEIALKEKEAENERLR-RLAEDEAFQRRL---LEEQAAQHKADI 1878
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVgknVHELERSKRALEQQVEEMKTQLEELEdELQATEDAKLRLevnMQALKAQFERDL 733
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1879 EARlaqlrkaSESELERQKGLVedtlRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAAR 1958
Cdd:pfam01576 734 QAR-------DEQGEEKRRQLV----KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1959 QRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQEAAQKRLQAE 2037
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQD 882
|
..
gi 1920237970 2038 EK 2039
Cdd:pfam01576 883 EK 884
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1344-1906 |
1.38e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 84.58 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1344 EERERLAEVEAALEKQRQLAEAHAQAKAQAEreaqglQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRqsseaeIQAK 1423
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDARE------QIELLEPIRELAERYAAARERLAELEYLRAALR------LWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1424 ARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE-AQKRQAQEEAERLRRQvQDETQRKRQAEA 1502
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERE-LEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1503 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQS-------EHASFAEK 1575
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASlerrksnIPARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1576 TAQLERTLKEEHVAV------VQLREEAtrraqqqaeaeraraeaerelERWQLKANEAL---RLRL--------QAEEV 1638
Cdd:COG4913 446 RDALAEALGLDEAELpfvgelIEVRPEE---------------------ERWRGAIERVLggfALTLlvppehyaAALRW 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1639 AQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEK--QRQLAEGTAQQRLAAEQELIRL-RAETEQG--- 1712
Cdd:COG4913 505 VNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRFDYVCVDSPEELRRHpRAITRAGqvk 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1713 ------------------------EQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRST 1768
Cdd:COG4913 585 gngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1769 S-EKSKQRLEAEagrFRELAEEAARLRALAEEAKRQRQlAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKE 1847
Cdd:COG4913 665 SaEREIAELEAE---LERLDASSDDLAALEEQLEELEA-ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 1848 AENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRkaseSELERQKGLVEDTLRQ 1906
Cdd:COG4913 741 DLARLELRALLEERFAAALGDAVERELRENLEERIDALR----ARLNRAEEELERAMRA 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
908-1596 |
1.42e-15 |
|
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: 84.72 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 908 EQRQALRSLELHYQA----FLRDSQDAGgfgPEDRLQAEREYGSCSRHYQQLLQSLEQGEQE----ESRCQRCISELKDI 979
Cdd:TIGR02168 217 ELKAELRELELALLVlrleELREELEEL---QEELKEAEEELEELTAELQELEEKLEELRLEvselEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 980 RLQLEACETRTVH---RLRlPLDKEPARECAQRITEQQKAQAEVDGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELEL 1056
Cdd:TIGR02168 294 ANEISRLEQQKQIlreRLA-NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1057 TLGKL-EQVRSLSAIYLEKLKTISLvIRSTQEaeeVLRAHEEQLKEAQAVPATlpelEATKAALKKLRAQAEAQQPVFDA 1135
Cdd:TIGR02168 373 RLEELeEQLETLRSKVAQLELQIAS-LNNEIE---RLEARLERLEDRRERLQQ----EIEELLKKLEEAELKELQAELEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1136 LRDELRGAQEVGERLQQRHGERDVEVERWRERVTLL---LERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRD 1212
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1213 AKQR---------------QEQIQAVPLANSQAVR---EQLRQEK----ALLEDIERHGEKVEECQRFAKQYINAIKDYE 1270
Cdd:TIGR02168 525 LSELisvdegyeaaieaalGGRLQAVVVENLNAAKkaiAFLKQNElgrvTFLPLDSIKGTEIQGNDREILKNIEGFLGVA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1271 LQLVTYKAQLEPVASP---------------AKKPKVQSGSESIIQEYVDLRTRYS--------ELSTL-TSQYIRFISE 1326
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYllggvlvvddldnalELAKKLRPGYRIVTLDGDLVRPGGVitggsaktNSSILeRRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1327 TLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQ 1406
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1407 EELQHLRQSSEAEiqakarqvEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1486
Cdd:TIGR02168 765 ELEERLEEAEEEL--------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1487 RRQVQDETQRKRQAEAELAlrvqaeaeaarekqRALQALEELRLQAEEAERRLRQAEAERArQVQVALETAqRSAEAELQ 1566
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIE--------------SLAAEIEELEELIEELESELEALLNERA-SLEEALALL-RSELEELS 900
|
730 740 750
....*....|....*....|....*....|..
gi 1920237970 1567 SEHASFAEKTAQLERTLKE--EHVAVVQLREE 1596
Cdd:TIGR02168 901 EELRELESKRSELRRELEElrEKLAQLELRLE 932
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2792-2830 |
2.57e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 72.36 E-value: 2.57e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1920237970 2792 LLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEMNRVL 2830
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1301-1957 |
2.78e-15 |
|
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: 83.73 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1301 QEYVDLRTRYSELSTLTSQYIRFISETLRRMEE-EERLAE--QQRAEERERLAEVEAALEKQRQLAEAhAQAKAQAEREA 1377
Cdd:pfam12128 248 QEFNTLESAELRLSHLHFGYKSDETLIASRQEErQETSAElnQLLRTLDDQWKEKRDELNGELSAADA-AVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1378 QGLQRRMQEEVarREEVAVEAQEQKRSIQEELQHLRQSSEAeIQAKARQVEAA-ERSRLRIEEEIR--VVRL------QL 1448
Cdd:pfam12128 327 LEDQHGAFLDA--DIETAAADQEQLPSWQSELENLEERLKA-LTGKHQDVTAKyNRRRSKIKEQNNrdIAGIkdklakIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1449 EATERQRGGAEGELQALRAR-AEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEA-----EAAREKQ--- 1519
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENfderiERAREEQeaa 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1520 -----RALQALEELRLQAEEAERRLRQAEAeRARQVQVALETAQR-------------SAEAELQSEHASFAEKTAQLER 1581
Cdd:pfam12128 484 naeveRLQSELRQARKRRDQASEALRQASR-RLEERQSALDELELqlfpqagtllhflRKEAPDWEQSIGKVISPELLHR 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1582 TLKEEHVAVVQLREEATRRaqqqaeaeraraeaerelerwqlkaneALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREAR 1661
Cdd:pfam12128 563 TDLDPEVWDGSVGGELNLY---------------------------GVKLDLKRIDVPEWAASEEELRERLDKAEEALQS 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1662 RRGKAEEQAvRQRELAEQELEKQrQLAEGTAQQRLA-AEQELIRLraeTEQGEQQRQLLEEELARLQREaaaATQKRREL 1740
Cdd:pfam12128 616 AREKQAAAE-EQLVQANGELEKA-SREETFARTALKnARLDLRRL---FDEKQSEKDKKNKALAERKDS---ANERLNSL 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1741 EAELAKVraEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQraeaer 1820
Cdd:pfam12128 688 EAQLKQL--DKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRD------ 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1821 vLAEKlaAISEATRLKTEAEIalKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASeSELERQKG-L 1899
Cdd:pfam12128 760 -LASL--GVDPDVIAKLKREI--RTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAI-SELQQQLArL 833
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237970 1900 VEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTlrSKEQAEQEAA 1957
Cdd:pfam12128 834 IADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDA--NSEQAQGSIG 889
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4029-4067 |
5.84e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.20 E-value: 5.84e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1920237970 4029 LLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEMNEIL 4067
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3451-3489 |
5.84e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.20 E-value: 5.84e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1920237970 3451 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFDEEMNRVL 3489
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
29-146 |
7.76e-15 |
|
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: 73.47 E-value: 7.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 29 DERDrvqKKTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLsgDSLprERDVIRSSRLPREKGRMRFHKLQNVQI 108
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVL--DKI--QPGCVNWKKVNKPKPLNKFKKVENCNY 69
|
90 100 110
....*....|....*....|....*....|....*...
gi 1920237970 109 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 146
Cdd:cd21219 70 AVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
164-275 |
8.76e-15 |
|
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: 73.49 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 164 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 243
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 1920237970 244 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 275
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
32-143 |
9.74e-15 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 72.95 E-value: 9.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 32 DRVQKKTFTKWVNKHLIKAQ-RHISDLYEDLRDGHNLISLLEVLSGDSLPRERDVIRSSRLPRekgrmrfhkLQNVQIAL 110
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEPKNRIQM---------IQNLHLAM 72
|
90 100 110
....*....|....*....|....*....|....
gi 1920237970 111 DYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTI 143
Cdd:cd21225 73 LFIEEDlKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1735-2602 |
1.05e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 81.65 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1735 QKRRELEAELAKVrAEMEvllASKARAEEESrstsEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEdavRQ 1814
Cdd:TIGR02169 153 VERRKIIDEIAGV-AEFD---RKKEKALEEL----EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE---KR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1815 RAEAERVLAEKLAAisEATRLKTEAEIAlkEKEAENERLRRLAEDeafqrrlLEEQAAQHKADIEARLAQLRKASESELE 1894
Cdd:TIGR02169 222 EYEGYELLKEKEAL--ERQKEAIERQLA--SLEEELEKLTEEISE-------LEKRLEEIEQLLEELNKKIKDLGEEEQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1895 RQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDtlrSKEQAEQEAARQRQLAAEEERRRREAE 1974
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1975 ERVQKSLAAEEEAARQR---KAALEEVERLKAKVEE----ARRLRERAEQESARQLQLAQ-----EAAQKRLQAEEKAHA 2042
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRdelKDYREKLEKLKREINElkreLDRLQEELQRLSEELADLNAaiagiEAKINELEEEKEDKA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2043 FAVQQKEQELQQTLQQEQSVLERLRseaeaarraaeeaeaareraerEAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAA 2122
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELY----------------------DLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2123 EKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTAlrlqleetdhQKSIldEELQRLKA- 2201
Cdd:TIGR02169 506 VRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVA----------KEAI--ELLKRRKAg 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2202 EVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENR-----------ALVLRDKDSAQRLLQ---------EEAEKMK 2261
Cdd:TIGR02169 574 RATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafkyvfgdTLVVEDIEAARRLMGkyrmvtlegELFEKSG 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2262 QVA----EEAARLSVAAQEAARLRQLAEE---------DLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2328
Cdd:TIGR02169 654 AMTggsrAPRGGILFSRSEPAELQRLRERleglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2329 QARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARaeEDARRFRKQAEDIGERLYRTE 2408
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2409 LATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQalqqsfLSEKDS 2488
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD------LESRLG 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2489 LLQRERC-IEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEG---------VRRQQE 2558
Cdd:TIGR02169 886 DLKKERDeLEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsledvqaeLQRVEE 965
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 1920237970 2559 ELQRLAQQQQQQEKLLAEENQR---LRERLQHLEEERRAALARSEEI 2602
Cdd:TIGR02169 966 EIRALEPVNMLAIQEYEEVLKRldeLKEKRAKLEEERKAILERIEEY 1012
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
850-1580 |
1.41e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 81.26 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 850 QEAQEAIARLEAQHQALVALWHQLHTEMKSLLAWQSLGRDMQLIRSWSLATFRTLKpEEQRQALRSLELHYQAFLRDSQD 929
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL-EELKEELESLEAELEELEAELEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 930 AggfgpEDRLQA-EREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQ 1008
Cdd:TIGR02168 370 L-----ESRLEElEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1009 RITEQQKAQAEVDGLGKGVARLSAE-AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLS---AIYLEKLKTISLVIRS 1084
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREElEEAEQALDAAERELAQLQARLDSLERLQENLEGFSegvKALLKNQSGLSGILGV 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1085 TQEAEEVlrahEEQLKeaQAVPATLPE---------LEATKAALKKLrAQAEAQQPVFDALrDELRGAQEVGERLQQRHG 1155
Cdd:TIGR02168 525 LSELISV----DEGYE--AAIEAALGGrlqavvvenLNAAKKAIAFL-KQNELGRVTFLPL-DSIKGTEIQGNDREILKN 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1156 ERDV-----EVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYR------ESADPLGAWLRDAKQRqeqiQAVP 1224
Cdd:TIGR02168 597 IEGFlgvakDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRivtldgDLVRPGGVITGGSAKT----NSSI 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1225 LANSQAVREqLRQEKALLEDIERHGEKveecqrfakqyinAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYV 1304
Cdd:TIGR02168 673 LERRREIEE-LEEKIEELEEKIAELEK-------------ALAELRKELEELEEELE---------QLRKELEELSRQIS 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1305 DLRTRYSELST---LTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQ 1381
Cdd:TIGR02168 730 ALRKDLARLEAeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1382 ---RRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQR 1455
Cdd:TIGR02168 810 aelTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelsEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1456 GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA-LRVQAEAEAAREKQRALQALEELRLQAEE 1534
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnLQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1920237970 1535 AERRLRQAEAERARQVQVALEtaqrsAEAELQSEHASFAEKTAQLE 1580
Cdd:TIGR02168 970 ARRRLKRLENKIKELGPVNLA-----AIEEYEELKERYDFLTAQKE 1010
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1086-1586 |
1.55e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.85 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1086 QEAEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRaqaeaqqpvfDALRDELRGAQEVGERLQQRHGERDVEVERWR 1165
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAETERER----------EELAEEVRDLRERLEELEEERDDLLAEAGLDD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1166 ERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQ---AVPLANSQAVREQLRQEKALL 1242
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRREEI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1243 EDIERHGEKVEEcqRFAKqyinaikdyelqlvtykaqlepvaSPAKKPKVQSGSESIIQEYVDLRTRYSELSTLtsqyir 1322
Cdd:PRK02224 387 EELEEEIEELRE--RFGD------------------------APVDLGNAEDFLEELREERDELREREAELEAT------ 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1323 fISETLRRMEEEERLAEQQR-----------------AEERERLAEVEAALE----KQRQLAEAHAQAK--AQAEREAQG 1379
Cdd:PRK02224 435 -LRTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRERVEELEAELEdleeEVEEVEERLERAEdlVEAEDRIER 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1380 LQRR---MQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvRLQLEATERQRG 1456
Cdd:PRK02224 514 LEERredLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKERIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1457 GAEGELQALRARAE---EAEAQKRQAQEEAERLRR-QVQDETQRKRQAEAELAlrvQAEAEAARE-KQRALQALeelrlq 1531
Cdd:PRK02224 592 ERIRTLLAAIADAEdeiERLREKREALAELNDERReRLAEKRERKRELEAEFD---EARIEEAREdKERAEEYL------ 662
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 1532 aEEAERRLRQAEAERAR-QVQVALETAQRSAEAELQSEHASFAEKTAQLErTLKEE 1586
Cdd:PRK02224 663 -EQVEEKLDELREERDDlQAEIGAVENELEELEELRERREALENRVEALE-ALYDE 716
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1231-1895 |
1.56e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 81.11 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1231 VREQLRQEKALLEDIERhgekveecqrfAKQYINAIKDYELQLVTYKAQ---LEPVaspakkpkvqsgsESIIQEYVDLR 1307
Cdd:COG4913 213 VREYMLEEPDTFEAADA-----------LVEHFDDLERAHEALEDAREQielLEPI-------------RELAERYAAAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1308 TRYSELSTLTSQY-IRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ----LAEAHAQAKAQAEREAQGLQR 1382
Cdd:COG4913 269 ERLAELEYLRAALrLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREeldeLEAQIRGNGGDRLEQLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1383 RMQEEVARREEVAVEAQEQKRSI--------------QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQL 1448
Cdd:COG4913 349 RLERELEERERRRARLEALLAALglplpasaeefaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1449 EATERQRGGAEGELQALRARAEEAeaqkrqAQEEAERLR-----RQVQDETQRKRQAeAELALRVQA-----EAEAAREK 1518
Cdd:COG4913 429 ASLERRKSNIPARLLALRDALAEA------LGLDEAELPfvgelIEVRPEEERWRGA-IERVLGGFAltllvPPEHYAAA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1519 QRALQALE-ELRLQAEEAERRLRQAEAER------ARQVQVALETAQRSAEAELQSehaSFAEKTAQLERTLKEEHVAV- 1590
Cdd:COG4913 502 LRWVNRLHlRGRLVYERVRTGLPDPERPRldpdslAGKLDFKPHPFRAWLEAELGR---RFDYVCVDSPEELRRHPRAIt 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1591 --VQLREEATrraqqqaeaERARAEAERELERWQL-KANEALRLRLQAEEVAQQKSLTQAEAEKQKEeaerearrrgKAE 1667
Cdd:COG4913 579 raGQVKGNGT---------RHEKDDRRRIRSRYVLgFDNRAKLAALEAELAELEEELAEAEERLEAL----------EAE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1668 EQAVRQRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQqrqlLEEELARLQREAAAATQKRRELEAEL 1744
Cdd:COG4913 640 LDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEI 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1745 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAE 1824
Cdd:COG4913 716 GRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 1825 -KLAAISEATRLKTEAEiALKEKEAENERLR--RLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELER 1895
Cdd:COG4913 796 fNREWPAETADLDADLE-SLPEYLALLDRLEedGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
164-263 |
1.95e-14 |
|
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: 72.31 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 164 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 243
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1920237970 244 VDV--PQPDEKSIITYVSSLYD 263
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1046-1799 |
2.14e-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: 80.78 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1046 AAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLkeaqavPATLPELEATKAALKKLRAQ 1125
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCM------PDTYHERKQVLEKELKHLRE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1126 AEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEverwrervtllLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdp 1205
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAR-----------IEELRAQEAVLEETQERINRARKAAPLAAHIK-- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1206 lgAWLRDAKQRQEQIQAvpLANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVAS 1285
Cdd:TIGR00618 301 --AVTQIEQQAQRIHTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1286 PAKKPKVQSGSESIIQEyvDLRTRYSELSTLTSQYIRFISETLRRMEEEERL--AEQQRAEERERLAEVEAALEKQRQ-- 1361
Cdd:TIGR00618 377 LTQHIHTLQQQKTTLTQ--KLQSLCKELDILQREQATIDTRTSAFRDLQGQLahAKKQQELQQRYAELCAAAITCTAQce 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1362 -LAEAHAQAKAQAERE-------AQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEA--EIQAKARQVEAAE 1431
Cdd:TIGR00618 455 kLEKIHLQESAQSLKEreqqlqtKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDidNPGPLTRRMQRGE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1432 RSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRaRAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAE 1511
Cdd:TIGR00618 535 QTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ-QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1512 AEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVV 1591
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLT 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1592 QLREEATRRAQQQAEAERARAEAERELERWQLkANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREArrrgkaEEQAV 1671
Cdd:TIGR00618 694 YWKEMLAQCQTLLRELETHIEEYDREFNEIEN-ASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE------AHFNN 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1672 RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR-----QLLEEELARLQREAAAATQKRRELEAELAK 1746
Cdd:TIGR00618 767 NEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipsdeDILNLQCETLVQEEEQFLSRLEEKSATLGE 846
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1920237970 1747 VRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEE 1799
Cdd:TIGR00618 847 ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHE 899
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1326-1817 |
2.31e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 79.81 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1326 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHA--QAKAQAEREAQGLQRRMQEEVARREEVAvEAQEQKR 1403
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELR-ELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1404 SIQEELQHLRQSSEaeiqakarqvEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEA 1483
Cdd:COG4717 167 ELEAELAELQEELE----------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1484 ER--LRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSA 1561
Cdd:COG4717 237 EAaaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1562 EAElqsehasfaektaQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAqq 1641
Cdd:COG4717 317 EEE-------------ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV-- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1642 ksltqaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQqrqlLEE 1721
Cdd:COG4717 382 -----------------------EDEEELRAALEQAEEYQELKEELEE--LEEQLEELLGELEELLEALDEEE----LEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1722 ELARLQREAAAATQKRRELEAELAKVRAEMEVLlaskaraeeESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAK 1801
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQL---------EEDGELAELLQELEELKAELRELAEEWAALKLALELLE 503
|
490
....*....|....*....
gi 1920237970 1802 RQRQLAEED---AVRQRAE 1817
Cdd:COG4717 504 EAREEYREErlpPVLERAS 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
936-1475 |
4.16e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 936 EDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLrlpldkeparecAQRITEQQK 1015
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL------------EELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1016 AQAEVDGLGKGVARLSAEAEKVLAlpepspaapTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAH 1095
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEE---------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1096 EEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERw 1175
Cdd:COG1196 413 LERLERLEE------ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE- 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1176 qavlaqtdvRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEkALLEDIERHGEKVEEC 1255
Cdd:COG1196 486 ---------LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA-LEAALAAALQNIVVED 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1256 QRFAKQYINAIKDYELQLVT-YKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEE 1334
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1335 ERLAEQQRAEERERLAEVEAALEKQRqLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQ 1414
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGS-LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237970 1415 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQ 1475
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
35-147 |
4.31e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 71.17 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 35 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerDVIRSsrlPREKGRMRfhklQNVQIALDY 112
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLP---GIDWN---PTTDAERK----ENVEKVLQF 70
|
90 100 110
....*....|....*....|....*....|....*
gi 1920237970 113 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 147
Cdd:cd21213 71 MASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1320-2039 |
4.35e-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: 79.63 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1320 YIRFISETLRRMEEEERLAEQQRAEERERLAEVEAaLEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQ 1399
Cdd:TIGR00618 140 YKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFP-LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1400 EQKRSIQEELQHLR--QSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQAL---RARAEEAEA 1474
Cdd:TIGR00618 219 ERKQVLEKELKHLReaLQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERInraRKAAPLAAH 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1475 QKRQAQEEAERLRRQVQ-DETQRKRQAEAELALRVQAEAEAAREKQRALQAL--EELRLQAEEAERRLRQAEAERARQVQ 1551
Cdd:TIGR00618 299 IKAVTQIEQQAQRIHTElQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLhsQEIHIRDAHEVATSIREISCQQHTLT 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1552 VALETAQRSAEAELQSEHASFAEKTaqlertlkeehvavvQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRL 1631
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELD---------------ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELC 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1632 RLQAEEVAQQKSLTQAEAEKQKEEAerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtaqQRLAAEQELIRLRAETEQ 1711
Cdd:TIGR00618 444 AAAITCTAQCEKLEKIHLQESAQSL--------KEREQQLQTKEQIHLQETRKKAVVL----ARLLELQEEPCPLCGSCI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1712 GEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLAS----KARAEEESRSTSEKSKQR---------LEA 1778
Cdd:TIGR00618 512 HPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQraslKEQMQEIQQSFSILTQCDnrskedipnLQN 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1779 EAGRFRELAEEAARLR-ALAEEAKRQ-RQLAEEDAVRQRAEAERVLAEKLAaiSEATRLKTEAEIALKEKEAENERLRRL 1856
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEdMLACEQHALlRKLQPEQDLQDVRLHLQQCSQELA--LKLTALHALQLTLTQERVREHALSIRV 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1857 AEDEAFQRRLLEEQAAQHKADieaRLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELG 1936
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKE---QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1937 RIRGTAEDTLRSKEQAEQEAARQrqlaaeeerrRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAE 2016
Cdd:TIGR00618 747 ELMHQARTVLKARTEAHFNNNEE----------VTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE 816
|
730 740
....*....|....*....|....
gi 1920237970 2017 QE-SARQLQLAQEAAQKRLQAEEK 2039
Cdd:TIGR00618 817 DIlNLQCETLVQEEEQFLSRLEEK 840
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
162-259 |
5.10e-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: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 162 TAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI----DMNKVYRqtnLENLDQAFSVAERDLGVTR 237
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
|
90 100
....*....|....*....|..
gi 1920237970 238 LLDPEDVDVPQPDEKSIITYVS 259
Cdd:cd21230 75 LITPEEIINPNVDEMSVMTYLS 96
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
164-267 |
5.18e-14 |
|
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: 71.23 E-value: 5.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 164 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 243
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1920237970 244 VDV--PQPDEKSIITYVSSLYDAMPR 267
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
167-262 |
6.05e-14 |
|
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: 70.85 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 167 LLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 245
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1920237970 246 VPQPDEKSIITYVSSLY 262
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1138-1917 |
7.06e-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: 78.96 E-value: 7.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1138 DELRGAQEVGERLQQRHGERDvEVERWRERVTLLLERwqaVLAQTDVRQRELEQLGRqlryYREsadplgawLRDAKQRQ 1217
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELE-EVEENIERLDLIIDE---KRQQLERLRREREKAER----YQA--------LLKEKREY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1218 EQiqAVPLANSQAVREQLRQEKALLEDIERHGEKVEEcqrfakqyinAIKDYELQLVTYKAQLEPVASPAKKpkvqSGSE 1297
Cdd:TIGR02169 224 EG--YELLKEKEALERQKEAIERQLASLEEELEKLTE----------EISELEKRLEEIEQLLEELNKKIKD----LGEE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1298 SIIQEYVDLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREA 1377
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERS-IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1378 QGLQRRMQEEVARREEVAVEAQEQKRSIqEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGG 1457
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKL-EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1458 AEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRALQALEEL---RLQA-- 1532
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVlkaSIQGvh 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1533 ----------EEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFA-----EKTAQLERTLKEEHVA-------- 1589
Cdd:TIGR02169 525 gtvaqlgsvgERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRAtflplNKMRDERRDLSILSEDgvigfavd 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1590 --------------------VVQLREEATRRAQQQAEAERA--------------RAEAERELERWQLKAnEALRLRLQA 1635
Cdd:TIGR02169 605 lvefdpkyepafkyvfgdtlVVEDIEAARRLMGKYRMVTLEgelfeksgamtggsRAPRGGILFSRSEPA-ELQRLRERL 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1636 EEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAV---RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG 1712
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGeieKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1713 EQQRQLLEEELARLQreAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTsEKSKQRLEAEAGRFRELAEEAAR 1792
Cdd:TIGR02169 764 EARIEELEEDLHKLE--EALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREI-EQKLNRLTLEKEYLEKEIQELQE 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1793 LRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAA 1872
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1873 QHKADIEA---RLAQLRKASESELERQKGL--VEDTLRQRRQVEEEILAL 1917
Cdd:TIGR02169 921 ELKAKLEAleeELSEIEDPKGEDEEIPEEElsLEDVQAELQRVEEEIRAL 970
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1313-2224 |
1.08e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 78.29 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1313 LSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEV----EAALEKQRQLAEAHAQAkAQAEREAQGLQRRMQEEV 1388
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEStdlqEQIAELQAQIAELRAQL-AKKEEELQAALARLEEET 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1389 ARREEvaveAQEQKRSIQEELQHLRQSSEAEIQAKARqveaAERSRLRIEEEIRVVRLQLEATErqrgGAEGELQALRAR 1468
Cdd:pfam01576 257 AQKNN----ALKKIRELEAQISELQEDLESERAARNK----AEKQRRDLGEELEALKTELEDTL----DTTAAQQELRSK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1469 AE-EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlrvqaeaEAAREKQRALQALEELRlQAEEAERRLRQAEAERA 1547
Cdd:pfam01576 325 REqEVTELKKALEEETRSHEAQLQEMRQKHTQALEELT-------EQLEQAKRNKANLEKAK-QALESENAELQAELRTL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1548 RQVQVALETAQRSAEAELQSEHASFAEktAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANE 1627
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1628 ALRlrlqAEEVAQQKSLTQAEAEKqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAegtaQQRLAAEQELIRLRA 1707
Cdd:pfam01576 475 ELL----QEETRQKLNLSTRLRQL---------------EDERNSLQEQLEEEEEAKRNVE----RQLSTLQAQLSDMKK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1708 ETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAK-------VRAEMEVLLAS-------------------KARA 1761
Cdd:pfam01576 532 KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektknrLQQELDDLLVDldhqrqlvsnlekkqkkfdQMLA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1762 EEESRSTS-EKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAA---ISEATRLKT 1837
Cdd:pfam01576 612 EEKAISARyAEERDRAEAEA---REKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVgknVHELERSKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1838 EAEIALKEKEAENERLR-RLAEDEAFQRRL---LEEQAAQHKADIEARlaqlrkaSESELERQKGLVedtlRQRRQVEEE 1913
Cdd:pfam01576 689 ALEQQVEEMKTQLEELEdELQATEDAKLRLevnMQALKAQFERDLQAR-------DEQGEEKRRQLV----KQVRELEAE 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1914 ILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 1993
Cdd:pfam01576 758 LEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKN 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1994 ALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQEAAQKRLQAEEKAHAFA-VQQKEQELQQTLQQEQSVLERLRSEAE 2071
Cdd:pfam01576 838 LEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQDEKRRLEArIAQLEEELEEEQSNTELLNDRLRKSTL 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2072 AARR---AAEEAEAARERAEREAAQSRRQVEEAeRLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQ 2148
Cdd:pfam01576 918 QVEQlttELAAERSTSQKSESARQQLERQNKEL-KAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKL 996
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2149 AADAE---------MEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2219
Cdd:pfam01576 997 VRRTEkklkevllqVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVST 1076
|
....*
gi 1920237970 2220 LRVQM 2224
Cdd:pfam01576 1077 LKSKL 1081
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3710-3748 |
1.19e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 67.35 E-value: 1.19e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1920237970 3710 LLEAQAATGFLLDPVKGERLAVDEAVRKGLVGPELHDRL 3748
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
20-150 |
1.63e-13 |
|
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: 69.96 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 20 YEEVREKykderdrvqkKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLsgdslprERDVIRSSRLPREKGRMR 99
Cdd:cd21298 2 IEETREE----------KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKI-------KPGVVDWSRVNKPFKKLG 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1920237970 100 --FHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 150
Cdd:cd21298 63 anMKKIENCNYAVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1062-1565 |
1.71e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.65 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1062 EQVRSLSAI--YLEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPatlpELEATKAALKKLRAQAEAQQPVFDALRDE 1139
Cdd:COG4913 249 EQIELLEPIreLAERYAAARERLAELEYLRAALRLWFAQRRLELLEA----ELEELRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1140 LRGAQEV-----GERLQQRhgERDVE-VERWRERVTLLLERWQAVLAQTDVR---------------QRELEQLGRQLRY 1198
Cdd:COG4913 325 LDELEAQirgngGDRLEQL--EREIErLERELEERERRRARLEALLAALGLPlpasaeefaalraeaAALLEALEEELEA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1199 YRESADPLGAWLRDAKQRQEQIQA-----------VPlANSQAVREQLRQEKALLED---------------------IE 1246
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAeiaslerrksnIP-ARLLALRDALAEALGLDEAelpfvgelievrpeeerwrgaIE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1247 R--HGEK----VEEcQRFAK--QYINAIKDyELQLVTYKAQLEPVASPAKKPKVQS------GSESIIQEYVD--LRTRY 1310
Cdd:COG4913 482 RvlGGFAltllVPP-EHYAAalRWVNRLHL-RGRLVYERVRTGLPDPERPRLDPDSlagkldFKPHPFRAWLEaeLGRRF 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1311 S--------ELST----LTSQYIRFISETLRRMEEEERL---------AEQQRAEERERLAEVEAALEKQRQLAEAHAQA 1369
Cdd:COG4913 560 DyvcvdspeELRRhpraITRAGQVKGNGTRHEKDDRRRIrsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1370 KAQAEREAQGLQRRmqEEVARREEVAVEAQEQKRSIQEELQHLRQSSeAEIQAKARQVEAAERSRLRIEEEIRVVRLQLE 1449
Cdd:COG4913 640 LDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIG 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1450 ATERQRGGAEGELQALRARAEEAE------------------AQKRQAQEEAERLRRQVQDETQRKRQAEAEL------- 1504
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEdlarlelralleerfaaaLGDAVERELRENLEERIDALRARLNRAEEELeramraf 796
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237970 1505 -------ALRVQAEAEAAREKQRALQALEELRL---QAEEAERRLRQAEAERArQVQVALETAQRSAEAEL 1565
Cdd:COG4913 797 nrewpaeTADLDADLESLPEYLALLDRLEEDGLpeyEERFKELLNENSIEFVA-DLLSKLRRAIREIKERI 866
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1622-2482 |
2.42e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 77.03 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1622 QLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA---- 1697
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLersi 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1698 --AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1775
Cdd:TIGR02169 311 aeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1776 LEAEAGRFRELAEEAARLRALAEEAKRQRQlaeedavrQRAEAERVLAEKLAAISEatrLKTEAEIALKEKEAENERLRR 1855
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSE--------ELADLNAAIAGIEAKINE---LEEEKEDKALEIKKQEWKLEQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1856 LAED-EAFQRRLLEEQAAQhkADIEARLAQLRKaSESELERQKGLVEDTLRQRRQVEEeilalkgsfekaaagkaELELE 1934
Cdd:TIGR02169 460 LAADlSKYEQELYDLKEEY--DRVEKELSKLQR-ELAEAEAQARASEERVRGGRAVEE-----------------VLKAS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1935 LGRIRGTAEDTLRSKEQ---AEQEAARQRqlaaeeerrrrEAEERVQKSLAAEE--EAARQRK---AALEEVERLKAKVE 2006
Cdd:TIGR02169 520 IQGVHGTVAQLGSVGERyatAIEVAAGNR-----------LNNVVVEDDAVAKEaiELLKRRKagrATFLPLNKMRDERR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2007 EARRLRERAEQESARQLqlaQEAAQKRlqaeEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARER 2086
Cdd:TIGR02169 589 DLSILSEDGVIGFAVDL---VEFDPKY----EPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRA 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2087 AEREAAQSRRQVEEAERL---KQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQ 2163
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLrerLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2164 ALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQveEELFSLRVQMEELGKLKARIEAENRALvl 2243
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREI-- 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2244 rDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAELLQQQK 2323
Cdd:TIGR02169 818 -EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGDLKKER 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2324 ELAQEQARRLQEDKEQMAQQlaqetqgfqktLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRfRKQAEDIGER 2403
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQ-----------IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAE 959
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 2404 LYRTELAtqekvmlVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSF 2482
Cdd:TIGR02169 960 LQRVEEE-------IRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENF 1031
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1053-1575 |
2.55e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.26 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1053 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEvLRAHEEQLKEAQAvpaTLPELEATKAALKKLRAQAEAQQpv 1132
Cdd:COG4913 266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAE-LARLEAELERLEA---RLDALREELDELEAQIRGNGGDR-- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1133 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTdvrQRELEQLGRQLRYYRESADPLGAWLRD 1212
Cdd:COG4913 340 LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA---AALLEALEEELEALEEALAEAEAALRD 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1213 AKQRQEQIQA-----------VPlANSQAVREQLRQEKALLED---------------------IER--HGEK----VEE 1254
Cdd:COG4913 417 LRRELRELEAeiaslerrksnIP-ARLLALRDALAEALGLDEAelpfvgelievrpeeerwrgaIERvlGGFAltllVPP 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1255 cQRFAK--QYINAIKDyELQLVTYKAQLEPVASPAKKPKVQSGSEsiiqeyvdlrtrysELSTLTSQYIRFISETLRRM- 1331
Cdd:COG4913 496 -EHYAAalRWVNRLHL-RGRLVYERVRTGLPDPERPRLDPDSLAG--------------KLDFKPHPFRAWLEAELGRRf 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1332 -----EEEERLAEQQRAEERERLA-EVEAALEK--QRQLAEAH------AQAKAQAEREAQGLQRRMQEEVARREEVAvE 1397
Cdd:COG4913 560 dyvcvDSPEELRRHPRAITRAGQVkGNGTRHEKddRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALE-A 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1398 AQEQKRSIQEELQHLRQSSEAEIQakarqVEAAERSRLRIEEEIRvvrlQLEAterqrggAEGELQALRARAEEAEAQKR 1477
Cdd:COG4913 639 ELDALQERREALQRLAEYSWDEID-----VASAEREIAELEAELE----RLDA-------SSDDLAALEEQLEELEAELE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1478 QAQEEAERLRRQVQDETQRKRQAEAEL-ALRVQAEAEAAREKQRALQALEELRlqAEEAERRLRQAEAERARQVQVALET 1556
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELdELQDRLEAAEDLARLELRALLEERF--AAALGDAVERELRENLEERIDALRA 780
|
570
....*....|....*....
gi 1920237970 1557 AQRSAEAELQSEHASFAEK 1575
Cdd:COG4913 781 RLNRAEEELERAMRAFNRE 799
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1703-2516 |
3.33e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.55 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1703 IRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAE--MEVLLASKARAEEESRSTSEKSKQRLEAea 1780
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtfTRVVLLPQGEFAQFLKAKSKEKKELLMN-- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1781 grfrelAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAErvlAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDE 1860
Cdd:TIGR00618 172 ------LFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQ---LLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1861 AFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEeilalkgsfeKAAAGKAELELELGRIRG 1940
Cdd:TIGR00618 243 AYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAP----------LAAHIKAVTQIEQQAQRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1941 TAEdtLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2020
Cdd:TIGR00618 313 HTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2021 rQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEE 2100
Cdd:TIGR00618 391 -LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2101 AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRL 2180
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2181 QLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLkarIEAENRAlvlrdKDSAQRLLQEEAEKm 2260
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL---TEKLSEA-----EDMLACEQHALLRK- 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2261 KQVAEEAARLSVAAQEAARLRQLAEEDLAQqraLAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQA--RRLQEDKE 2338
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHA---LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSekEQLTYWKE 697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2339 QMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEdigERLYRTELATQEKVMLV 2418
Cdd:TIGR00618 698 MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK---ARTEAHFNNNEEVTAAL 774
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2419 QTLeTQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQ 2498
Cdd:TIGR00618 775 QTG-AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
810
....*....|....*...
gi 1920237970 2499 EKAKLEQlfQDEVAKAQA 2516
Cdd:TIGR00618 854 YEECSKQ--LAQLTQEQA 869
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2144-2603 |
4.34e-13 |
|
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: 76.25 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2144 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQ 2223
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2224 MEELGKLKARIEAEnRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2303
Cdd:TIGR02168 311 LANLERQLEELEAQ-LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2304 QAVQEATRLKAEAELLQQQKE-LAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA 2382
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLErLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2383 QARAEEDARRFRKQAEDIGERLYRTE-----------------------------LATQEKV------------------ 2415
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLErlqenlegfsegvkallknqsglsgilgvLSELISVdegyeaaieaalggrlqa 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2416 MLVQTLETQRQ--QSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEE-----------------------MQTVRQEQ 2470
Cdd:TIGR02168 550 VVVENLNAAKKaiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEgflgvakdlvkfdpklrkalsylLGGVLVVD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2471 LLQETQALQ------------------------QSFLSEKDSLLQRERCIEQEKAKLEQLfQDEVAKAQALREEQQRQQQ 2526
Cdd:TIGR02168 630 DLDNALELAkklrpgyrivtldgdlvrpggvitGGSAKTNSSILERRREIEELEEKIEEL-EEKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237970 2527 QMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIA 2603
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1343-2449 |
5.61e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 76.15 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1343 AEERERLaeVEAALEKQRQLAEAHAQAKAQAEReaqglqrrmQEEVARREEvavEAQEQKRSIQEELQ----HLRQSSEA 1418
Cdd:PRK04863 278 ANERRVH--LEEALELRRELYTSRRQLAAEQYR---------LVEMARELA---ELNEAESDLEQDYQaasdHLNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1419 EIQAKA--RQVEAAERSRLRIEEEIRVVRlqlEATERQrggaegelqalraraEEAEAQKRQAQEEAERLRRQVQDETQr 1496
Cdd:PRK04863 344 LRQQEKieRYQADLEELEERLEEQNEVVE---EADEQQ---------------EENEARAEAAEEEVDELKSQLADYQQ- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1497 krqaeaelALRVQAEAeaAREKQRALQALEELR-------LQAEEAERRLRQAEAERARQVQVALETAQRSAEAElqsEH 1569
Cdd:PRK04863 405 --------ALDVQQTR--AIQYQQAVQALERAKqlcglpdLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ---AA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1570 ASFAEKTAQLERTLKEEHVavvqlREEAtrraqqqaeaeraraeaerelerWQlKANEALRlrlqaeevaqqksltqaea 1649
Cdd:PRK04863 472 HSQFEQAYQLVRKIAGEVS-----RSEA-----------------------WD-VARELLR------------------- 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1650 ekqkeeaerearrrgkaeeQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQRE 1729
Cdd:PRK04863 504 -------------------RLREQRHLAEQLQQLRMRLSE--LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1730 AAAAtqkRRELEAELAKVRAEMEVLlaskaRAEEESrstSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1809
Cdd:PRK04863 563 LEAR---LESLSESVSEARERRMAL-----RQQLEQ---LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTE 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1810 dAVRQRAEAERVLAEKLAAISEA-TRLKTEAEIALKEKEAENERLRRLAEDeaFQRRLLEEQ----AAQHKADIEARLAQ 1884
Cdd:PRK04863 632 -YMQQLLERERELTVERDELAARkQALDEEIERLSQPGGSEDPRLNALAER--FGGVLLSEIyddvSLEDAPYFSALYGP 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1885 LRKASeseLERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAG--KAElELELGRIRGTAEDTLR-SKEQAEQ---EAAR 1958
Cdd:PRK04863 709 ARHAI---VVPDLSDAAEQLAGLEDCPEDLYLIEGDPDSFDDSvfSVE-ELEKAVVVKIADRQWRySRFPEVPlfgRAAR 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1959 QRQLaaeeerrrreaeervqkslaaeEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLA---------QEA 2029
Cdd:PRK04863 785 EKRI----------------------EQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpeaelRQL 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2030 AQKRLQAEEKahafavqqkeqelqqtlqqeqsvLERLRSeaeaarraaeeaeaareraerEAAQSRRQVEEAERLKQSae 2109
Cdd:PRK04863 843 NRRRVELERA-----------------------LADHES---------------------QEQQQRSQLEQAKEGLSA-- 876
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2110 eqaqaqaqaqaaaekLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRlqleeTDhqk 2189
Cdd:PRK04863 877 ---------------LNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQ-----SD--- 933
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2190 silDEELQRLKAEVTEAARQRGQVEEELFSLrvqmEELGKLKARIEAENRALVLRDKDSAQRLLQ---EEAEKMKQVAEE 2266
Cdd:PRK04863 934 ---PEQFEQLKQDYQQAQQTQRDAKQQAFAL----TEVVQRRAHFSYEDAAEMLAKNSDLNEKLRqrlEQAEQERTRARE 1006
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2267 AARlsvaaQEAARLRQLAE--EDLAQQRALAEKMLKEKMQAVQEAT-RLKAEAE-LLQQQKELAQEQARRLQEDKEQMAQ 2342
Cdd:PRK04863 1007 QLR-----QAQAQLAQYNQvlASLKSSYDAKRQMLQELKQELQDLGvPADSGAEeRARARRDELHARLSANRSRRNQLEK 1081
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2343 QLaqetqgfqkTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEkvmlvqtLE 2422
Cdd:PRK04863 1082 QL---------TFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRELAYLS-------AD 1145
|
1130 1140
....*....|....*....|....*..
gi 1920237970 2423 TQRQQSDRDAERLREAIAELEHEKDKL 2449
Cdd:PRK04863 1146 ELRSMSDKALGALRLAVADNEHLRDVL 1172
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
164-259 |
6.82e-13 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 67.80 E-value: 6.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 164 KEKLLLWSQRMVEGCqglRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 242
Cdd:cd21229 5 KKLMLAWLQAVLPEL---KITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1920237970 243 DVDVPQPDEKSIITYVS 259
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3044-3082 |
8.38e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.04 E-value: 8.38e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1920237970 3044 LLEAQAGTGHIIDPTTSARLTVDEAVRAGLVGPELHEKL 3082
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1109-1568 |
8.39e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.80 E-value: 8.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1109 LPELEATKAALKKLRAQAEAqqpvFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTL--LLERWQAVLAQTDVRQ 1186
Cdd:COG4717 70 LKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1187 RELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQA----VPLANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQY 1262
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEElleqLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1263 INAIKDYELQLVTYKAQlEPVASPAKKPKVQSGSESIIQEYVDLRTRYSE-----LSTLTSQYIRFISETLRRMEEEERL 1337
Cdd:COG4717 226 EEELEQLENELEAAALE-ERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1338 AEQQRAEERERL--AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKrsIQEELQHLRQS 1415
Cdd:COG4717 305 EELQALPALEELeeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--IAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1416 SEAEIQAKARQVEAAErsrlRIEEEIRVVRLQLEA--TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1493
Cdd:COG4717 383 DEEELRAALEQAEEYQ----ELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEELREELAEL 458
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237970 1494 TQRKRQAEAElalrvqaeaeaarekqralQALEELRLQAEEAERRLRQAEAERARQ--VQVALETAQRSAEAELQSE 1568
Cdd:COG4717 459 EAELEQLEED-------------------GELAELLQELEELKAELRELAEEWAALklALELLEEAREEYREERLPP 516
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
164-265 |
9.25e-13 |
|
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: 67.80 E-value: 9.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 164 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 243
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1920237970 244 -VDVPQPDEKSIITYVSSLYDAM 265
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2145-2676 |
1.19e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2145 RQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRV-Q 2223
Cdd:PTZ00121 1110 KAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVrK 1189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2224 MEELGKLKA--RIEAENRALVLRDKDSAQRllQEEAEKMKQV--AEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2299
Cdd:PTZ00121 1190 AEELRKAEDarKAEAARKAEEERKAEEARK--AEDAKKAEAVkkAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFAR 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2300 KEKMQAVQEATrlKAEaELLQQQKELAQEQARRLQEDKEqmAQQLAQETQGFQKTLETERQRQlEMSAEAERLRLRVAEM 2379
Cdd:PTZ00121 1268 RQAAIKAEEAR--KAD-ELKKAEEKKKADEAKKAEEKKK--ADEAKKKAEEAKKADEAKKKAE-EAKKKADAAKKKAEEA 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2380 SRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLEtQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQlK 2459
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK-KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK-K 1419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2460 SEEMQTvRQEQLLQETQALQQSFLSEKDSLLQRErciEQEKAKLEQLFQ--DEVAKAQALREEQQRqqqqmqqekqqlAA 2537
Cdd:PTZ00121 1420 ADEAKK-KAEEKKKADEAKKKAEEAKKADEAKKK---AEEAKKAEEAKKkaEEAKKADEAKKKAEE------------AK 1483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2538 SMEEARRRQHEAeegvRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALAR-SEEIAPSRA-AAARALPN 2615
Cdd:PTZ00121 1484 KADEAKKKAEEA----KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkAEEKKKADElKKAEELKK 1559
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237970 2616 GQDAADGPAAAAEPEHAFDGLRR-----KVPAQRLQEVGVL-------SAEELQQLAQGRTTVAELAQREDVR 2676
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKaeeakKAEEARIEEVMKLyeeekkmKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
162-262 |
1.20e-12 |
|
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: 67.41 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 162 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 241
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1920237970 242 ED-VDVPQPDEKSIITYVSSLY 262
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1312-1529 |
1.50e-12 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 73.37 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1312 ELSTLTSQYIR-----FISETLRRMEEEERLAEQQRAEeRERLAEVEAAlEKQRQLAEAHAQAKAQAER----EAQGLQR 1382
Cdd:COG2268 170 ELESVAITDLEdennyLDALGRRKIAEIIRDARIAEAE-AERETEIAIA-QANREAEEAELEQEREIETariaEAEAELA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1383 RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrlqLEATERQRGGAEGEL 1462
Cdd:COG2268 248 KKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAE-------LEADVRKPAEAEKQA 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237970 1463 QALRARAeEAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELALRVQAEAEAAREKQRALQALEELR 1529
Cdd:COG2268 321 AEAEAEA-EAEAIRAKGLAEAEGKRALA--EAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1087-1583 |
1.56e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.57 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1087 EAEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELrgAQEVGERLQQRHGERDVEVERWRE 1166
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1167 RVTLLLERWQAVLAQ-TDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDI 1245
Cdd:COG4913 317 RLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1246 ERHGEKVEECQRFAKQyinAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRFIS 1325
Cdd:COG4913 397 EEELEALEEALAEAEA---ALRDLRRELRELEAEIA---------SLERRKSNIPARLLALRDALAEALGLDEAELPFVG 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1326 ETLRRMEEEERLaeqQRAEER-------------ERLAEVEAALEKQR-------QLAEAHAQAKAQAEREAQGLQRRM- 1384
Cdd:COG4913 465 ELIEVRPEEERW---RGAIERvlggfaltllvppEHYAAALRWVNRLHlrgrlvyERVRTGLPDPERPRLDPDSLAGKLd 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1385 ----------QEEVARREEVA-VEAQEQ----KRSIQEELQ--------------HLRQ------SSEAEIQAKARQVEA 1429
Cdd:COG4913 542 fkphpfrawlEAELGRRFDYVcVDSPEElrrhPRAITRAGQvkgngtrhekddrrRIRSryvlgfDNRAKLAALEAELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1430 AERSRLRIEEEIRVVRLQLEATERQRGGAEG---------ELQALRARAEEAEAQKRQAQE---EAERLRRQVQDETQRK 1497
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1498 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV--QVALETAQRSAEAELQSEHASFAEK 1575
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVERELRENLEERIDALRAR 781
|
....*...
gi 1920237970 1576 TAQLERTL 1583
Cdd:COG4913 782 LNRAEEEL 789
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1329-1831 |
1.88e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 74.22 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1329 RRMEEEERLAEQQRAEERERLAE----VEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRS 1404
Cdd:COG3096 242 RMTLEAIRVTQSDRDLFKHLITEatnyVAADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSAR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1405 iQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEeirvVRLQLEATERQRGGAEGELqalraraEEAEAQKRQAQE 1481
Cdd:COG3096 322 -ESDLEQDYQAASdhlNLVQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1482 EAERLRRQVQDETQrkrqaeaelALRVQAEAeaAREKQRALQALEELR-------LQAEEAERRLRQAEAERARQVQVAL 1554
Cdd:COG3096 390 EVDSLKSQLADYQQ---------ALDVQQTR--AIQYQQAVQALEKARalcglpdLTPENAEDYLAAFRAKEQQATEEVL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1555 ETAQRSAEAElqsEHASFAEKTAQLERTLKEEHVavvqlREEAtrraqqqaeaeraraeaerelerWQlKANEALR---- 1630
Cdd:COG3096 459 ELEQKLSVAD---AARRQFEKAYELVCKIAGEVE-----RSQA-----------------------WQ-TARELLRryrs 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1631 LRLQAEEVAQQKSltqaeaekqkeeaerearRRGKAEEQAVRQRELAEQelekQRQLAEGTAQQRLAAEQelirLRAETE 1710
Cdd:COG3096 507 QQALAQRLQQLRA------------------QLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEE----LEELLA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1711 QGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEA 1780
Cdd:COG3096 561 ELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLERER 640
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1920237970 1781 GRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISE 1831
Cdd:COG3096 641 EATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERLGGVLLSEIYD 691
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1460-2038 |
2.86e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.54 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1460 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRqaEAELALRVQAEAEAAREKQRALQALEELRLQAEEA--ER 1537
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKE--EKDLHERLNGLESELAELDEEIERYEEQREQARETrdEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1538 RLRQAEAERARQVQVALETA---QRSAEAELQSEHASFAEKTAQLERTLKEehvavvqLREEATRRAQQQAEAERARAEA 1614
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEiedLRETIAETEREREELAEEVRDLRERLEE-------LEEERDDLLAEAGLDDADAEAV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1615 ERELERWQlKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEaerearrrgKAEEQAVRQRELA---EQELEKQRQLAEGT 1691
Cdd:PRK02224 313 EARREELE-DRDEELRDRLEECRVAAQAHNEEAESLREDAD---------DLEERAEELREEAaelESELEEAREAVEDR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1692 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVR---AEMEVLLA------------ 1756
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEagkcpecgqpve 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1757 --SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--EDAVRQRAEAERVLAEKLAAISEA 1832
Cdd:PRK02224 463 gsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEEKRERAEEL 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1833 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIE---------ARLAQLRKASESELERQKGLVE-- 1901
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllAAIADAEDEIERLREKREALAEln 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1902 ----DTLRQRRqveEEILALKGSFEKAAAGKAELELElgrirgTAEDTLRSKEQAEQEAARQRqlaaeeerrrreaeERV 1977
Cdd:PRK02224 623 derrERLAEKR---ERKRELEAEFDEARIEEAREDKE------RAEEYLEQVEEKLDELREER--------------DDL 679
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237970 1978 QKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2038
Cdd:PRK02224 680 QAEIGAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLE 740
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3786-3824 |
3.22e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.50 E-value: 3.22e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1920237970 3786 LLDAQLATGGIVDPRLGFHLPLDVAYQRGYLDKDTHDQL 3824
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1330-2454 |
3.32e-12 |
|
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: 73.29 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1330 RMEEEERLAEQQRAEERERLAEVEAAL----EKQRQLAEAHAQAKAQAEREAqglqrrmqEEVARREEVAVEAQEQKRSI 1405
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELkeleKKHQQLCEEKNALQEQLQAET--------ELCAEAEEMRARLAARKQEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1406 QEELQHLrqssEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQALRARAEEAEAQKRQAQEEAER 1485
Cdd:pfam01576 74 EEILHEL----ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAAR-------QKLQLEKVTTEAKIKKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1486 LRRQVQDETQRKRQAE---AELALRVQAEAEAA------REKQRALQALEELRLQAEEAERRlrqaEAERARQVQVALET 1556
Cdd:pfam01576 143 LEDQNSKLSKERKLLEeriSEFTSNLAEEEEKAkslsklKNKHEAMISDLEERLKKEEKGRQ----ELEKAKRKLEGEST 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1557 AQRSAEAELQsehASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAeaeraraeaerelerwQLKANEALRLRLQaE 1636
Cdd:pfam01576 219 DLQEQIAELQ---AQIAELRAQLAKKEEELQAALARLEEETAQKNNALK----------------KIRELEAQISELQ-E 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1637 EVAQQKSltqaeaekqkeeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEGT-----AQQRLAA--EQELIRLR--- 1706
Cdd:pfam01576 279 DLESERA----------------------ARNKAEKQRRDLGEELEALKTELEDTldttaAQQELRSkrEQEVTELKkal 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1707 -AETEQGEQQRQ-----------LLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEEsRSTSEKSKQ 1774
Cdd:pfam01576 337 eEETRSHEAQLQemrqkhtqaleELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHK-RKKLEGQLQ 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1775 RLEA---EAGRFR-ELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERV---LAEKLAAISEATRLKTEAEIALKEKE 1847
Cdd:pfam01576 416 ELQArlsESERQRaELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLesqLQDTQELLQEETRQKLNLSTRLRQLE 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1848 AENERLRRLAEDEAFQRRLLEEQAAQHkadiEARLAQLRKASESELERQKGLVEDtlrqRRQVEEEILALKGSFEKAAAG 1927
Cdd:pfam01576 496 DERNSLQEQLEEEEEAKRNVERQLSTL----QAQLSDMKKKLEEDAGTLEALEEG----KKRLQRELEALTQQLEEKAAA 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1928 KAELELELGRIRGTAEDTLRSKEQaeqeaarQRQLAAEEERRRREAEErvqksLAAEEEAARQRKAALEEVERLKAKVEE 2007
Cdd:pfam01576 568 YDKLEKTKNRLQQELDDLLVDLDH-------QRQLVSNLEKKQKKFDQ-----MLAEEKAISARYAEERDRAEAEAREKE 635
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2008 ARRLRERAEQESARQLQLAQEAAQKRLQAEekahafavqqkeqelqqtlqqeqsvLERLRSEAEAARRAAEEAEAARERA 2087
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQLRAE-------------------------MEDLVSSKDDVGKNVHELERSKRAL 690
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2088 EREAAQSRRQVEEAERLKQSaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQAeqaalRQKQAADAEMEKHKQfaeQALRQ 2167
Cdd:pfam01576 691 EQQVEEMKTQLEELEDELQA------------TEDAKLRLEVNMQALKAQFE-----RDLQARDEQGEEKRR---QLVKQ 750
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2168 KAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKD 2247
Cdd:pfam01576 751 VRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKE 830
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2248 SAQRLLQEEAEKMkQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2327
Cdd:pfam01576 831 SEKKLKNLEAELL-QLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLN 909
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2328 EQARRLQEDKEQMAQQLAQETQGFQKtLETERQrqlEMSAEAERLRLRVAEMSRAQ---------------ARAEEDARR 2392
Cdd:pfam01576 910 DRLRKSTLQVEQLTTELAAERSTSQK-SESARQ---QLERQNKELKAKLQEMEGTVkskfkssiaaleakiAQLEEQLEQ 985
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 2393 FRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQ 2454
Cdd:pfam01576 986 ESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEAS 1047
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3375-3413 |
4.95e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 4.95e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1920237970 3375 LLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPELHEKL 3413
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4298-4336 |
5.15e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.73 E-value: 5.15e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1920237970 4298 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 4336
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
164-263 |
6.01e-12 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 65.05 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 164 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 239
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1920237970 240 DPEDVdVPQPDEKSIITYVSSLYD 263
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1665-1886 |
7.48e-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: 70.56 E-value: 7.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1665 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1744
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1745 AKVRAE----------------MEVLLASKARAEEESRSTSEKS-KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA 1807
Cdd:COG4942 100 EAQKEElaellralyrlgrqppLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 1808 EEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdeafqrRLLEEQAAQHKADIEARLAQLR 1886
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA------RLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1863-2603 |
9.87e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 71.93 E-value: 9.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1863 QRRLLEEQAA---QHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIR 1939
Cdd:pfam02463 153 ERRLEIEEEAagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1940 GTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQES 2019
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2020 ARQLQLAQE---AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRR 2096
Cdd:pfam02463 313 EEKLKESEKekkKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2097 QVEEAErlKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELT 2176
Cdd:pfam02463 393 KEEELE--LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2177 ALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEE 2256
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVI 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2257 AEKMKQVAEEAARLSVAAQEAARLRQLAEedlaqqralaekmlkekmqavqeaTRLKAEAELLQQQKELAQEQARRLQED 2336
Cdd:pfam02463 551 VEVSATADEVEERQKLVRALTELPLGARK------------------------LRLLIPKLKLPLKSIAVLEIDPILNLA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2337 KEQMAQQLAQETQGFQKTLETERQRQLEMSaeaERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVM 2416
Cdd:pfam02463 607 QLDKATLEADEDDKRAKVVEGILKDTELTK---LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2417 LVQTLETQRQQSdrdaERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCI 2496
Cdd:pfam02463 684 KAESELAKEEIL----RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKK 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2497 EQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGvrrQQEELQRLAQQQQQQEKLLAE 2576
Cdd:pfam02463 760 EEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAE---LLEEEQLLIEQEEKIKEEELE 836
|
730 740
....*....|....*....|....*..
gi 1920237970 2577 ENQRLRERLQHLEEERRAALARSEEIA 2603
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEELERLEEEI 863
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1004-1589 |
1.08e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 71.91 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1004 RECAQRITEQQKAQAEVDGLGKGVARLSAEAEkvlalpepspaaptlrsELELTLGKLEqvrslsaiylEKLKTISLVIR 1083
Cdd:COG3096 522 AELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-----------------ELEELLAELE----------AQLEELEEQAA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1084 STQEAEEVLRAHEEQLKE-AQAVPATLPELEATKAALKKLRAQAEAQqpvFDALRDELRGAQEVGERLQQRHGERDvEVE 1162
Cdd:COG3096 575 EAVEQRSELRQQLEQLRArIKELAARAPAWLAAQDALERLREQSGEA---LADSQEVTAAMQQLLEREREATVERD-ELA 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1163 RWRERVTLLLERWQAVLAQTDVRQREL-EQLGRQL--RYYR----ESADPLGAWLRDAKQrqeqiqAVPLANSQAVREQL 1235
Cdd:COG3096 651 ARKQALESQIERLSQPGGAEDPRLLALaERLGGVLlsEIYDdvtlEDAPYFSALYGPARH------AIVVPDLSAVKEQL 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1236 RQEKALLED---IERHGEKVEECQRFAKQYINAI--KDYELQLVTYKAQLEPV----ASPAKKPKVQSGSESIIQEYVDL 1306
Cdd:COG3096 725 AGLEDCPEDlylIEGDPDSFDDSVFDAEELEDAVvvKLSDRQWRYSRFPEVPLfgraAREKRLEELRAERDELAEQYAKA 804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1307 RTRYSELSTLTSQYIRFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREAQGLQRRMQE 1386
Cdd:COG3096 805 SFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQLDQLKEQLQLLNKLLP 881
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1387 EV---------ARREEVAVE---AQEQKRSIQEELQHLRQSSE--AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATE 1452
Cdd:COG3096 882 QAnlladetlaDRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALS 961
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1453 --RQR------GGAEGEL-------QALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAARE 1517
Cdd:COG3096 962 evVQRrphfsyEDAVGLLgensdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQE 1041
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 1518 -KQRALQALEELRLQAEEaERRLRQAEAERARQVQVALETAQRSAEAELQSEHASF--AEKTAQLERTLKEEHVA 1589
Cdd:COG3096 1042 lEELGVQADAEAEERARI-RRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLrkAERDYKQEREQVVQAKA 1115
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2162-2486 |
1.14e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 71.31 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2162 EQALRQKAQVEQELTALRLQLEETDHQKSIlDEELQRLKAEVTEAARQRGQVEEELFSL--RVQMEELGKLK-------A 2232
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAV-SERQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARqaemdrqA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2233 RIEAENRALVLRDKDSAQRLLQEEaekmKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALAEKMLKEKMQAVQEATRL 2312
Cdd:pfam17380 334 AIYAEQERMAMERERELERIRQEE----RKRELERIRQEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2313 KAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQgfQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARR 2392
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER--AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2393 fRKQAEDIGERLYRTELATQEKVM--------LVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQ 2464
Cdd:pfam17380 486 -RKRAEEQRRKILEKELEERKQAMieeerkrkLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE 564
|
330 340
....*....|....*....|..
gi 1920237970 2465 TVRQEQLLQETQALQQSFLSEK 2486
Cdd:pfam17380 565 RSRLEAMEREREMMRQIVESEK 586
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3953-3991 |
1.17e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 1.17e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1920237970 3953 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 3991
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3120-3158 |
1.30e-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: 1.30e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1920237970 3120 LLDAQLSTGGIVDPSKSHRVPLDVACARGYLDKETSAAL 3158
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
30-141 |
1.68e-11 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 63.98 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 30 ERDRvQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSgdslPRERDVIRSSRLPREKGRMRFHKLQNVQIA 109
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVI----PGSVNWKKVNKAPASAEISRFKAVENTNYA 76
|
90 100 110
....*....|....*....|....*....|..
gi 1920237970 110 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIW 141
Cdd:cd21300 77 VELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
162-262 |
1.68e-11 |
|
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: 63.90 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 162 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 241
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1920237970 242 ED-VDVPQPDEKSIITYVSSLY 262
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1394-1597 |
2.03e-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: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1394 VAVEAQEQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE 1473
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1474 AQKRQAQEEAERLRRQVQDET----QRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRL-----RQAEA 1544
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLaelaaLRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1920237970 1545 ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEA 1597
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1300-1798 |
2.16e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 70.75 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1300 IQEYVDLRTRYSELSTLTSQYirFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAqg 1379
Cdd:COG3096 248 IRVTQSDRDLFKHLITEATNY--VAADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARES-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1380 lqrrmqeevarreevAVEAQEQKRSiqeelQHLrqsseAEIQAKARQVEAAERSRLRIEEeirvVRLQLEATERQRGGAE 1459
Cdd:COG3096 324 ---------------DLEQDYQAAS-----DHL-----NLVQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1460 GELqalraraEEAEAQKRQAQEEAERLRRQVQDETQrkrqaeaelALRVQaeAEAAREKQRALQALEELR-------LQA 1532
Cdd:COG3096 375 EQL-------AEAEARLEAAEEEVDSLKSQLADYQQ---------ALDVQ--QTRAIQYQQAVQALEKARalcglpdLTP 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1533 EEAERRLRQAEAERARQVQVALETAQRSAEAElqsEHASFAEKTAQLERTLKEEHVavvqlREEATRRAQQQAEAERARA 1612
Cdd:COG3096 437 ENAEDYLAAFRAKEQQATEEVLELEQKLSVAD---AARRQFEKAYELVCKIAGEVE-----RSQAWQTARELLRRYRSQQ 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1613 EAERELERWQLKANEA-LRLRLQAEEVAQQKSLtqaeaekqkeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGT 1691
Cdd:COG3096 509 ALAQRLQQLRAQLAELeQRLRQQQNAERLLEEF-------------------CQRIGQQLDAAEELEELLAELEAQLEEL 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1692 AQQRLAAEQELIRLRAETEQGEQQRQLLeEELARLQREAAAATQKRRELEAE----LAKVRAEMEVLLaSKARAEEESRS 1767
Cdd:COG3096 570 EEQAAEAVEQRSELRQQLEQLRARIKEL-AARAPAWLAAQDALERLREQSGEaladSQEVTAAMQQLL-EREREATVERD 647
|
490 500 510
....*....|....*....|....*....|....*
gi 1920237970 1768 TSEKSKQRLEAEAgrfRELA----EEAARLRALAE 1798
Cdd:COG3096 648 ELAARKQALESQI---ERLSqpggAEDPRLLALAE 679
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1361-1731 |
2.17e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 70.54 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1361 QLAEAHAQAKAQAEREAQGLQRRMQEEVARREevaveaqeqKRSIQEELQHLRQSSEAEiqaKARQVEA-------AERS 1433
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLRQE---------KEEKAREVERRRKLEEAE---KARQAEMdrqaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1434 RLRIEEEIRVVRLQLEatERQRggaegELQALRaraEEAEAQKRQAQEEAERLRRQVQDETQRKRQaEAELALRVQ-AEA 1512
Cdd:pfam17380 341 RMAMERERELERIRQE--ERKR-----ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1513 EAAREKQRALQALEELRLQAEEA-ERRLRQAEAERARQVQ-VALETAQRSAEAE-LQSEHASFAEKTAQLERTLKEEHVA 1589
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAREMErVRLEEQERQQQVErLRQQEEERKRKKLELEKEKRDRKRA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1590 VVQLREeatrraqqqaeaeraraeaereLERWQLKANEalrlRLQAEEVAQQKSLTQAEAEKQKEEAEREARRrgKAEEQ 1669
Cdd:pfam17380 490 EEQRRK----------------------ILEKELEERK----QAMIEEERKRKLLEKEMEERQKAIYEEERRR--EAEEE 541
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 1670 AVRQrelaeQELEKQRQLAEgtaqQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA 1731
Cdd:pfam17380 542 RRKQ-----QEMEERRRIQE----QMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2188-2595 |
2.32e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2188 QKSILDEELQRLKAEVTEAARQRG---QVEEELFSLRVQMEELGKLKARIEAENRAL--------VLRDKDSAQRLLQEE 2256
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEeyaELQEELEELEEELEELEAELEELREELEKLekllqllpLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2257 AEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQED 2336
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2337 KEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEED---------------ARRFRKQAEDIG 2401
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2402 ERLYRTELATQEkvmlvQTLETQRQQSDRDAERLREAI--AELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQAL- 2478
Cdd:COG4717 302 KEAEELQALPAL-----EELEEEELEELLAALGLPPDLspEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALl 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2479 QQSFLSEKDSLLQRERCIEQEKAKLEQLfqdEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQE 2558
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEEL---EELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELRE 453
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1920237970 2559 ELQRLAQQQQQQEK-----LLAEENQRLRERLQHLEEERRAA 2595
Cdd:COG4717 454 ELAELEAELEQLEEdgelaELLQELEELKAELRELAEEWAAL 495
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
605-783 |
2.33e-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: 66.32 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 605 LHGFVAAATKELMWLSDREEEEVGFDWSDRNTNMAAKKEGYSALMHELELKEKKIKEIQSTGDRLLREDHPARPTAESFQ 684
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 685 AALQTQWSWMLQLCCCIEAHLKENTAYFQFFSDVREAEEQLRKLQETLRRKYTCDrsiTATRLEDLLQDAQDEKEQLSEY 764
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
|
170
....*....|....*....
gi 1920237970 765 RGHLSGLAKRAKAIVQLKP 783
Cdd:cd00176 159 EPRLKSLNELAEELLEEGH 177
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1073-1958 |
2.62e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 70.39 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1073 EKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRaqaeaqqpvfdalrdelrgaqevgerlqq 1152
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD----------------------------- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1153 rhgERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdplgawlrDAKQRQEQIQAVPLANSQAVR 1232
Cdd:pfam02463 231 ---YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEE--------KEKKLQEEELKLLAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1233 EQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSgsesiIQEYVDLRTRYSE 1312
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL-----EKLQEKLEQLEEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1313 LSTLTSQYIRFISETLRRMEEEERLA-----EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEE 1387
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEEELELKseeekEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1388 VARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLR-IEEEIRVVRLQLEATERQRGGAEGELQALR 1466
Cdd:pfam02463 455 KQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESkARSGLKVLLALIKDGVGGRIISAHGRLGDL 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1467 ARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQ-AEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAE 1545
Cdd:pfam02463 535 GVAVENYKVAISTAVIVEVSATADEVEERQKLVrALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLE 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1546 RARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHvavvQLREEATRRAQQQAEAERARAEAERELERWQLKA 1625
Cdd:pfam02463 615 ADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEE----GLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1626 NEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRL 1705
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELS 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1706 RAETEQGEQQRQLLEEELARLQREAAAATQKrrELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRE 1785
Cdd:pfam02463 771 LKEKELAEEREKTEKLKVEEEKEEKLKAQEE--ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1786 LAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRR 1865
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1866 LLEEQAAQHKADIEARLAQLRKASESELERQKglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDT 1945
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEE---RNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
890
....*....|...
gi 1920237970 1946 LRSKEQAEQEAAR 1958
Cdd:pfam02463 1006 KLIRAIIEETCQR 1018
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1502-2038 |
2.77e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 70.66 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1502 AELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAE-RARQVQVALETAQRSAEAELQSEHAS--------F 1572
Cdd:COG3899 712 ARRALARGAYAEALRYLERALELLPPDPEEEYRLALLLELAEALyLAGRFEEAEALLERALAARALAALAAlrhgnppaS 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1573 AEKTAQLERTLKEEHVAVVQLREEATRRAQQ--QAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQkslTQAEAE 1650
Cdd:COG3899 792 ARAYANLGLLLLGDYEEAYEFGELALALAERlgDRRLEARALFNLGFILHWLGPLREALELLREALEAGLE---TGDAAL 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1651 KQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREA 1730
Cdd:COG3899 869 ALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAA 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1731 AAATQKRRELEAELAKVRAEMEVLLASKARAeeesrstsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED 1810
Cdd:COG3899 949 AAAAALAAALALAAAAAAAAAAALAAAAAAA-------------AAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAAL 1015
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1811 AVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASE 1890
Cdd:COG3899 1016 AAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAA 1095
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1891 SELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRR 1970
Cdd:COG3899 1096 ALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAAL 1175
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237970 1971 REAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2038
Cdd:COG3899 1176 AALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1673-2595 |
2.95e-11 |
|
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: 70.20 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1673 QRELAEQELEKQR-QLAEGTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAe 1750
Cdd:pfam01576 109 EEQLDEEEAARQKlQLEKVTTEAKIKKlEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1751 MEVLLASKARAEEESRSTSEKSKQRLEAEAGrfrELAEEAARLRALAEEAKRQRQLAEEDavrqraeaervLAEKLAAIS 1830
Cdd:pfam01576 188 MISDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEE-----------LQAALARLE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1831 EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRrlleEQAAQHKADIEARLAQLRKASESELERQKGLVEdtLRQRRqv 1910
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQISELQEDLESERAAR----NKAEKQRRDLGEELEALKTELEDTLDTTAAQQE--LRSKR-- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1911 EEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLrsKEQAEQeAARQRQLAAEEERRRREAEERVQKSL----AAEEE 1986
Cdd:pfam01576 326 EQEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL--TEQLEQ-AKRNKANLEKAKQALESENAELQAELrtlqQAKQD 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1987 AARQRKAALEEVERLKAKVEEARRLRERAEQESARqLQLAQEAAQKRLQAEEKahafavqqKEQELQQTLQQEQSVLERL 2066
Cdd:pfam01576 403 SEHKRKKLEGQLQELQARLSESERQRAELAEKLSK-LQSELESVSSLLNEAEG--------KNIKLSKDVSSLESQLQDT 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2067 RSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQ 2146
Cdd:pfam01576 474 QELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2147 KQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLeetDHQKSILDEELQRLKAEVTEAArqrgqvEEELFSLRVQMEe 2226
Cdd:pfam01576 554 LEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDL---DHQRQLVSNLEKKQKKFDQMLA------EEKAISARYAEE- 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2227 lgklKARIEAENRalvlrDKDSAQRLLQEEAEKMKQVAEEAARlsvaaqeAARLRQLAEEDLAQQRALAEKMLKE----K 2302
Cdd:pfam01576 624 ----RDRAEAEAR-----EKETRALSLARALEEALEAKEELER-------TNKQLRAEMEDLVSSKDDVGKNVHElersK 687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2303 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLEtERQRQL-----EMSAEAERLRLRVA 2377
Cdd:pfam01576 688 RALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGE-EKRRQLvkqvrELEAELEDERKQRA 766
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2378 EMSRAQARAEEDARRFRKQAEDIGERlyRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQ 2457
Cdd:pfam01576 767 QAVAAKKKLELDLKELEAQIDAANKG--REEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQ 844
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2458 LKSEEMQTVRQE-QLLQETQALQQ---SFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQ 2533
Cdd:pfam01576 845 LQEDLAASERARrQAQQERDELADeiaSGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTT 924
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2534 QLAAS---------------------------MEEARRRQHEA-----EEGVRRQQEELQRLAQQQQQQEKLLAEENQRL 2581
Cdd:pfam01576 925 ELAAErstsqksesarqqlerqnkelkaklqeMEGTVKSKFKSsiaalEAKIAQLEEQLEQESRERQAANKLVRRTEKKL 1004
|
970
....*....|....
gi 1920237970 2582 RERLQHLEEERRAA 2595
Cdd:pfam01576 1005 KEVLLQVEDERRHA 1018
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1706-2022 |
3.32e-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: 69.77 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1706 RAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAElAKVRAEMEVLLASKARAEEESRSTSEKSkqrlEAEAGRFRE 1785
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQ-AAIYAEQERMAMERERELERIRQEERKR----ELERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1786 LAEEAARLRALaEEAKRQRQLAEEdAVRQRAEAERV--LAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEA-- 1861
Cdd:pfam17380 370 IAMEISRMREL-ERLQMERQQKNE-RVRQELEAARKvkILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAre 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1862 FQRRLLEEQAAQHKADIEARLAQLRKASESELERQKglvedtlRQRRQVEEEilaLKGSFEKAAAGKAELELELGRIRGT 1941
Cdd:pfam17380 448 MERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK-------RDRKRAEEQ---RRKILEKELEERKQAMIEEERKRKL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1942 AEDTLRSKEQAEQEAARQRQlaaeeerrrREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2021
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRRE---------AEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
|
.
gi 1920237970 2022 Q 2022
Cdd:pfam17380 589 A 589
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1413-2038 |
3.41e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 70.25 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1413 RQSSEAEIQAKARQVEA--AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE----RL 1486
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1487 RRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAeLQ 1566
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1567 SEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAerelerwqlkANEALRLRLQAEEVAQQKSLTQ 1646
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAED----------DLQALESELREQLEAGKLEFNE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1647 AEAEKQKEEAEREARRRG-KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR 1725
Cdd:pfam12128 438 EEYRLKSRLGELKLRLNQaTATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1726 LQREAAAATQ----KRRELEAELAKVRAEMEVLLASKARAEEESRS------TSEKSKQRLEAEAGRFRELAEEAARLRA 1795
Cdd:pfam12128 518 RQSALDELELqlfpQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTdldpevWDGSVGGELNLYGVKLDLKRIDVPEWAA 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1796 LAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHK 1875
Cdd:pfam12128 598 SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERK 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1876 A-------DIEARLAQLRKASESELERQKG---------------LVEDTLRQRRQVEEEILALKGSFE----------- 1922
Cdd:pfam12128 678 DsanerlnSLEAQLKQLDKKHQAWLEEQKEqkreartekqaywqvVEGALDAQLALLKAAIAARRSGAKaelkaletwyk 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1923 --------------KAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAA 1988
Cdd:pfam12128 758 rdlaslgvdpdviaKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADT 837
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 1989 RQRKAALEevERLKAKVEEARRLRE-----RAEQESARQLQLAQEAAQKRLQAEE 2038
Cdd:pfam12128 838 KLRRAKLE--MERKASEKQQVRLSEnlrglRCEMSKLATLKEDANSEQAQGSIGE 890
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2716-2754 |
3.46e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 60.42 E-value: 3.46e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1920237970 2716 LLEAQAASGFLLDPVRNRRLAVNEAVKEGIVGPELHHKL 2754
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2150-2506 |
4.29e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.68 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2150 ADAEMEKHKQFAEQA--LRQKA-QVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEE 2226
Cdd:PRK02224 344 AESLREDADDLEERAeeLREEAaELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2227 LGKLKARIEAENRALVLRDKDsAQRLLQE-EAEKMKQVAEEAARLSVAAQEAARLRQLAEE--DLAQQRALAEKMLKEKM 2303
Cdd:PRK02224 424 LREREAELEATLRTARERVEE-AEALLEAgKCPECGQPVEGSPHVETIEEDRERVEELEAEleDLEEEVEEVEERLERAE 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2304 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSraQ 2383
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRER-AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN--S 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2384 ARAEEDARrfRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERL---REAIAELEHEKDklkqEAQLLQLKS 2460
Cdd:PRK02224 580 KLAELKER--IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLaekRERKRELEAEFD----EARIEEARE 653
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1920237970 2461 EEMQTVR-QEQLLQETQALQQsflsEKDSLLQRERCIEQEKAKLEQL 2506
Cdd:PRK02224 654 DKERAEEyLEQVEEKLDELRE----ERDDLQAEIGAVENELEELEEL 696
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
53-144 |
4.56e-11 |
|
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: 62.61 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 53 HISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirsSRLPrEKGRMRfhKLQNVQIALDYLRHRQV----KLVNIRNDDI 128
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSK-----LRVP-AISRLQ--KLHNVEVALKALKEAGVlrggDGGGITAKDI 96
|
90
....*....|....*.
gi 1920237970 129 ADGNPKLTLGLIWTII 144
Cdd:cd21223 97 VDGHREKTLALLWRII 112
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1383-2481 |
5.64e-11 |
|
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: 69.43 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1383 RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEA--AERSRLRIEEEIRvVRLQLEATErqrggAEG 1460
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQlqAETELCAEAEEMR-ARLAARKQE-----LEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1461 ELQALRARAEEAEAQKRQAQEEAERLRRQVQDetqrkrqAEAELalrvqAEAEAAREKqralqaleeLRLQAEEAERRLR 1540
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEKKKMQQHIQD-------LEEQL-----DEEEAARQK---------LQLEKVTTEAKIK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1541 QAEAErarqvqVALETAQRSaeaELQSEHASFAEKTAQLERTLKEEHVAVVQL-----REEATRRAQQQAEAERARAEAE 1615
Cdd:pfam01576 135 KLEED------ILLLEDQNS---KLSKERKLLEERISEFTSNLAEEEEKAKSLsklknKHEAMISDLEERLKKEEKGRQE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1616 RELERWQLKAnEALRLRlqaEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQR 1695
Cdd:pfam01576 206 LEKAKRKLEG-ESTDLQ---EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE--LQED 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1696 LAAEqelirlRAETEQGEQQRQLLEEELARLQRE---AAAATQKRRELEAelakvRAEMEVLLASKArAEEESRSTSEKS 1772
Cdd:pfam01576 280 LESE------RAARNKAEKQRRDLGEELEALKTEledTLDTTAAQQELRS-----KREQEVTELKKA-LEEETRSHEAQL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1773 KQRLEAEAGRFRELAEE---AARLRALAEEAK--------------RQRQLAEEDAVRQRAEAERVLAEKLAAISEATRL 1835
Cdd:pfam01576 348 QEMRQKHTQALEELTEQleqAKRNKANLEKAKqalesenaelqaelRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQ 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1836 KTEAEIALKEKEAENERLRRLAEDeafqrrlLEEQAAQHKADIEARLAQLRKASE--SELERQKGLVEDTLrqrRQVEEE 1913
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNE-------AEGKNIKLSKDVSSLESQLQDTQEllQEETRQKLNLSTRL---RQLEDE 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1914 ILALKGSFEKAAAGKAELELELGRIRGTAEDTlrsKEQAEQEAARQRQLaaeeerrrreaeERVQKSLAAEEEAARQRka 1993
Cdd:pfam01576 498 RNSLQEQLEEEEEAKRNVERQLSTLQAQLSDM---KKKLEEDAGTLEAL------------EEGKKRLQRELEALTQQ-- 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1994 aLEEVERLKAKVEEAR-RLRERAE-----QESARQLQLAQEAAQKR---LQAEEKA-HAFAVQQKEQELQQTLQQEQSVL 2063
Cdd:pfam01576 561 -LEEKAAAYDKLEKTKnRLQQELDdllvdLDHQRQLVSNLEKKQKKfdqMLAEEKAiSARYAEERDRAEAEAREKETRAL 639
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2064 ERLRSeaeaarraaeeaeaareraereAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAA 2143
Cdd:pfam01576 640 SLARA----------------------LEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEM 697
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2144 LRQKQaadaEMEKHKQFAEQA-LR-------QKAQVEQELTALRLQLEEtdhQKSILDEELQRLKAEVTEAARQRGQvee 2215
Cdd:pfam01576 698 KTQLE----ELEDELQATEDAkLRlevnmqaLKAQFERDLQARDEQGEE---KRRQLVKQVRELEAELEDERKQRAQ--- 767
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2216 eLFSLRVQME-ELGKLKARIEAENRAlvlrdKDSAQRLLQEEAEKMKQVAeeaarlsvaaqeaarlRQLAEEDLAQQRAL 2294
Cdd:pfam01576 768 -AVAAKKKLElDLKELEAQIDAANKG-----REEAVKQLKKLQAQMKDLQ----------------RELEEARASRDEIL 825
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2295 AEKMLKEKmqavqeatRLKA-EAELLQQQKELA-QEQARR-LQEDKEQMAQQLAQETQGfqKTLETERQRQLEmsaeaER 2371
Cdd:pfam01576 826 AQSKESEK--------KLKNlEAELLQLQEDLAaSERARRqAQQERDELADEIASGASG--KSALQDEKRRLE-----AR 890
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2372 LRLRVAEMSRAQARAEEDARRFRKQAEDIgERLyRTELATQEKvmLVQTLETQRQQSDRDAERLREAIAELEHE-KDKLK 2450
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQV-EQL-TTELAAERS--TSQKSESARQQLERQNKELKAKLQEMEGTvKSKFK 966
|
1130 1140 1150
....*....|....*....|....*....|.
gi 1920237970 2451 QEAQLLQLKSEEMqtvrQEQLLQETQALQQS 2481
Cdd:pfam01576 967 SSIAALEAKIAQL----EEQLEQESRERQAA 993
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1346-1871 |
5.80e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 69.50 E-value: 5.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1346 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKAR 1425
Cdd:COG3899 722 AEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1426 QVEAAERSRLRIEEEIRVV-RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL--RRQVQDETQRKRQAEA 1502
Cdd:COG3899 802 LLGDYEEAYEFGELALALAeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAA 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1503 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERT 1582
Cdd:COG3899 882 AAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1583 LKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARR 1662
Cdd:COG3899 962 AAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAA 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1663 RGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA 1742
Cdd:COG3899 1042 ALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALA 1121
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1743 ELAKVRAEMEVLLASKARAEEESRSTsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVL 1822
Cdd:COG3899 1122 ALALAAAARAAAALLLLAAALALALA------ALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAAL 1195
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1920237970 1823 AEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQA 1871
Cdd:COG3899 1196 LAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2145-2347 |
6.11e-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: 67.87 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2145 RQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQM 2224
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2225 EELGK---LKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2301
Cdd:COG4942 114 YRLGRqppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1920237970 2302 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQE 2347
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
984-1539 |
9.08e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 9.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 984 EACETRTVHRLRLPLDKEPARECAQRITEQQKAqaevDGLGKGV--ARLSAEAEKVLAlPEPSPAAPTLRSELELTLGKL 1061
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA----DEAKKKAeeAKKKADAAKKKA-EEAKKAAEAAKAEAEAAADEA 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1062 EQVRSLS-AIYLEKLKTISLVIRSTQEAEEVLRAhEEQLKEAQAVPATLPELEATKAALKK---LRAQAEAQQPVfdalr 1137
Cdd:PTZ00121 1360 EAAEEKAeAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKadeAKKKAEEKKKA----- 1433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1138 DELRGAQEvgERLQQRHGERDVEVERWRERVTLLLERwqavlaqtdvrQRELEQLGRQLRYYREsADPLGAWLRDAKQRQ 1217
Cdd:PTZ00121 1434 DEAKKKAE--EAKKADEAKKKAEEAKKAEEAKKKAEE-----------AKKADEAKKKAEEAKK-ADEAKKKAEEAKKKA 1499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1218 EQIQAVPLANSQAVREQLRQEKALLEDIERHGE--KVEEcqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSG 1295
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakKADE----AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1296 SESIIQEYVDLR----TRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERlaeveaalEKQRQLAEAHAQAKA 1371
Cdd:PTZ00121 1576 KNMALRKAEEAKkaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK--------KKVEQLKKKEAEEKK 1647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1372 QAEReaqgLQRRMQEEVARREEVAVEAQEQKRSIQEelqhLRQSSEAEiqakarqvEAAERSRLRIEEEIRVVRLQLEAT 1451
Cdd:PTZ00121 1648 KAEE----LKKAEEENKIKAAEEAKKAEEDKKKAEE----AKKAEEDE--------KKAAEALKKEAEEAKKAEELKKKE 1711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1452 ERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAElalrvQAEAEAAREKQRALQALEELRLQ 1531
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK-----KEEEKKAEEIRKEKEAVIEEELD 1786
|
....*...
gi 1920237970 1532 AEEAERRL 1539
Cdd:PTZ00121 1787 EEDEKRRM 1794
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
164-264 |
9.71e-11 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 61.60 E-value: 9.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 164 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 243
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 1920237970 244 VdVPQPDEKSIITYVSSLYDA 264
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1332-1832 |
1.37e-10 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 68.35 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1332 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER-----EAQGLQRRMQEEVARREEVAVEAQEQKRSIQ 1406
Cdd:COG3899 741 EEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRhgnppASARAYANLGLLLLGDYEEAYEFGELALALA 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1407 EELQHLRQSSEAEIqAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1486
Cdd:COG3899 821 ERLGDRRLEARALF-NLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAA 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1487 RRQVQDETQRKRQAEAELALRVQAEAEAAREkqRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQ 1566
Cdd:COG3899 900 AAAALAAAAAAAALAAAELARLAAAAAAAAA--LALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAA 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1567 SEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQ 1646
Cdd:COG3899 978 AAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAA 1057
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1647 AEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARL 1726
Cdd:COG3899 1058 AAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLL 1137
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1727 QREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQL 1806
Cdd:COG3899 1138 LAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLAL 1217
|
490 500
....*....|....*....|....*.
gi 1920237970 1807 AEEDAVRQRAEAERVLAEKLAAISEA 1832
Cdd:COG3899 1218 EAAALLLLLLLAALALAAALLALRLL 1243
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2242-2598 |
1.84e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2242 VLRDKDSAQRLLQEEA---EKMKQVAEEAARLSVAAQEA-ARLRQLAEEDLAQQRAL---AEKMlkEKMQAVQEATRlKA 2314
Cdd:TIGR02168 149 IIEAKPEERRAIFEEAagiSKYKERRKETERKLERTRENlDRLEDILNELERQLKSLerqAEKA--ERYKELKAELR-EL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2315 EAELLQQQKELAQEQARRLQEDKEQMAQQLAQET---QGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDAR 2391
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTaelQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2392 RFRKQAEDIGERLYRtelatqekvmlvqtLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQL 2471
Cdd:TIGR02168 306 ILRERLANLERQLEE--------------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2472 LQEtQALQQSFLSEKDSLLQRERCIEQEKAKLEQLfqdeVAKAQALreeqQRQQQQMQQEKQQLAASMEEARRRQHEAE- 2550
Cdd:TIGR02168 372 SRL-EELEEQLETLRSKVAQLELQIASLNNEIERL----EARLERL----EDRRERLQQEIEELLKKLEEAELKELQAEl 442
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1920237970 2551 EGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALAR 2598
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1319-2036 |
2.12e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.45 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1319 QYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEA 1398
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1399 QEQKRSIQEELQHLRQ---SSEAEIQA-KARQVEAAERSRLRIEEEIRVVRLQLE----ATERQRGGAEGELQALRAR-- 1468
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHFRslgsAISKILRELDTEISYLKGRif 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1469 --AEEAEAQKRQAQEEAERLRRQVQDET-QRKRQAEAELAlRVQAEAEAAREKQRALQAleelrlQAEEAERRLRQAEAE 1545
Cdd:pfam15921 242 pvEDQLEALKSESQNKIELLLQQHQDRIeQLISEHEVEIT-GLTEKASSARSQANSIQS------QLEIIQEQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1546 RARQVQvALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAeaerelerwQLKA 1625
Cdd:pfam15921 315 YMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQ---------KLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1626 NEALRLRLQAEEVAQQKSLtqaeaekqkeeaerEARRRGKAEEQAVRQRELAEQELEKQRQLA---------EGTAQQRL 1696
Cdd:pfam15921 385 DLHKREKELSLEKEQNKRL--------------WDRDTGNSITIDHLRRELDDRNMEVQRLEAllkamksecQGQMERQM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1697 AAEQ----ELIRLRAETEQGEQQRQLLEEELARLqreaaaaTQKRRELEAELAKVrAEMEVLLASKARAEEESRSTSEKS 1772
Cdd:pfam15921 451 AAIQgkneSLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTV-SDLTASLQEKERAIEATNAEITKL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1773 KQRLEAEAGRFRELAEEAARLRALAEEAKRQR-QLAEEDAV----RQ----------------------RAEAERVLAEK 1825
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVieilRQqienmtqlvgqhgrtagamqveKAQLEKEINDR 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1826 LAAISEATRLKTEAEIALKEKEAE---------------NERLRRLAEDEAFQRRLLEEQAAQHK------ADIEARLAQ 1884
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARvsdlelekvklvnagSERLRAVKDIKQERDQLLNEVKTSRNelnslsEDYEVLKRN 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1885 LRKASE------SELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAG-KAELELELGRIrgtaeDTLRSK----EQAE 1953
Cdd:pfam15921 683 FRNKSEemetttNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGmQKQITAKRGQI-----DALQSKiqflEEAM 757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1954 QEAARQRQLAAEEERRRREAEERV---QKSLAAEEEAARQRKAALEE--------VERLKAKVEEARRLRERAEQESARq 2022
Cdd:pfam15921 758 TNANKEKHFLKEEKNKLSQELSTVateKNKMAGELEVLRSQERRLKEkvanmevaLDKASLQFAECQDIIQRQEQESVR- 836
|
810
....*....|....
gi 1920237970 2023 LQLAQEAAQKRLQA 2036
Cdd:pfam15921 837 LKLQHTLDVKELQG 850
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1668-2042 |
2.21e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1668 EQAVRQRELAEQELEKQRQL--AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELA 1745
Cdd:COG4717 105 EELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1746 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAV------------- 1812
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallgl 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1813 --RQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASE 1890
Cdd:COG4717 265 ggSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1891 SELERQKGLVE-DTLRQRRQVEEEILALKGSFEKAAAGKAElelelgRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERR 1969
Cdd:COG4717 345 RIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 1970 RREAEERVQKSLAAE-EEAARQRKAALEEVERLKAKVEEAR-RLRERAEQESARQLQLAQEAAQKRLQAEEKAHA 2042
Cdd:COG4717 419 EELLEALDEEELEEElEELEEELEELEEELEELREELAELEaELEQLEEDGELAELLQELEELKAELRELAEEWA 493
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1399-1588 |
2.22e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 65.98 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1399 QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQL--EATERQRGGAEGELQALRARAEEAEAQK 1476
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQkkQAEEAAKQAALKQKQAEEAAAKAAAAAK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1477 RQAQEEAERLRRQV-QDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALE 1555
Cdd:PRK09510 147 AKAEAEAKRAAAAAkKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAA 226
|
170 180 190
....*....|....*....|....*....|...
gi 1920237970 1556 TAQRSAEAELQSEHASFAEKTAQLERTLKEEHV 1588
Cdd:PRK09510 227 AAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2242-2597 |
3.16e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2242 VLRDKDSAQRLLQEEAEKMKQ-----VAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM--LKEKMQAVQEA-TRLK 2313
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERykelkAELRELELALLVLRLEELREELEELQEELKEAEEELeeLTAELQELEEKlEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2314 AEAELLQQQKELAQE---QARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDA 2390
Cdd:TIGR02168 274 LEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2391 RRFRKQAEdigerlyrtelatqEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKqeAQLLQLKSE-EMQTVRQE 2469
Cdd:TIGR02168 354 ESLEAELE--------------ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIERLEARlERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2470 QLLQETQALQQSFLSEKDSLLQRErcIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHeA 2549
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAE--LEELEEELEEL-QEELERLEEALEELREELEEAEQALDAAERELAQLQARLD-S 493
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1920237970 2550 EEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLqHLEEERRAALA 2597
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI-SVDEGYEAAIE 540
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1004-1592 |
5.26e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.52 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1004 RECAQRITEQQKAQaevdglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELEltlgkleqvrslsaiylEKLKTISLVI 1082
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELE-----------------ARLESLSESV 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1083 RSTQEAEEVLRAHEEQLK-EAQAVPATLPELEATKAALKKLRAQAEaqqpvfdalrDELRGAQEVGERLQQrHGERDVEV 1161
Cdd:PRK04863 575 SEARERRMALRQQLEQLQaRIQRLAARAPAWLAAQDALARLREQSG----------EEFEDSQDVTEYMQQ-LLEREREL 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1162 ERWRERVTlllERWQAVLAQTD-VRQRELEQLGRQLRYyresADPLGAWL----------RDAKQRQ----EQIQAVPLA 1226
Cdd:PRK04863 644 TVERDELA---ARKQALDEEIErLSQPGGSEDPRLNAL----AERFGGVLlseiyddvslEDAPYFSalygPARHAIVVP 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1227 NSQAVREQLRQEKALLEDI-------ERHGEKVEECQRFAKQYINAIKDYELQLVTYKAqlEPVASPAKKPK----VQSG 1295
Cdd:PRK04863 717 DLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKrieqLRAE 794
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1296 SESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER 1375
Cdd:PRK04863 795 REELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEAD--PEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKE 872
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1376 EAQGLQR-----------RMQEEVARREEVAVEAQEQKRSIQ---------EELQHLRQSSEAEIQAKARQVEAAE---- 1431
Cdd:PRK04863 873 GLSALNRllprlnlladeTLADRVEEIREQLDEAEEAKRFVQqhgnalaqlEPIVSVLQSDPEQFEQLKQDYQQAQqtqr 952
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1432 --RSRLRIEEEIRVVRLQLEATERQR-GGAEGELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDETQRKRQAEAELALR 1507
Cdd:PRK04863 953 daKQQAFALTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQYNQVLASLKSS 1028
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1508 VQAEAEAAREKQRALQAL---------EELRLQAEEAERRLRQAEAERArqvqvALETAQRSAEAELQsehaSFAEKTAQ 1578
Cdd:PRK04863 1029 YDAKRQMLQELKQELQDLgvpadsgaeERARARRDELHARLSANRSRRN-----QLEKQLTFCEAEMD----NLTKKLRK 1099
|
650
....*....|....
gi 1920237970 1579 LERTLKEEHVAVVQ 1592
Cdd:PRK04863 1100 LERDYHEMREQVVN 1113
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1668-2414 |
5.30e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1668 EQAVRQRELAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1747
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARER---LAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1748 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLA 1827
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLEREL---EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1828 AISEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRRlleeqaaqhKADIEARLAQLRKAseseLERQKGLVEDTLR-- 1905
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELE--AEIASLERR---------KSNIPARLLALRDA----LAEALGLDEAELPfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1906 -QRRQVEEEILALKGSFEKAaagkaelelelgrIRGTAEDTLRSKEQAEQ--EAARQRQLAAEeerrrreaeerVQKSLA 1982
Cdd:COG4913 464 gELIEVRPEEERWRGAIERV-------------LGGFALTLLVPPEHYAAalRWVNRLHLRGR-----------LVYERV 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1983 AEEEAARQRKAALEE--VERLKAKVEEARrlrERAEQESARQLQLAQEAAQKRLQAEEKA--------HAFAVQQKEQEL 2052
Cdd:COG4913 520 RTGLPDPERPRLDPDslAGKLDFKPHPFR---AWLEAELGRRFDYVCVDSPEELRRHPRAitragqvkGNGTRHEKDDRR 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2053 QQTLQqeqSVLerlrseaeaarraaeeaeaareraereAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEaeqe 2132
Cdd:COG4913 597 RIRSR---YVL---------------------------GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDA---- 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2133 aarraqaeqaaLRQKQAADAEMEKHkQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQ 2212
Cdd:COG4913 643 -----------LQERREALQRLAEY-SWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2213 VEEELFSLRvqmEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2292
Cdd:COG4913 711 LKGEIGRLE---KELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2293 ALAEKMLKEKMQAVQEATRLKAEAELLQQ-QKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLeterqrQLEMSAEAER 2371
Cdd:COG4913 788 ELERAMRAFNREWPAETADLDADLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIEFVADL------LSKLRRAIRE 861
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 2372 LRLRVAEMSRA----------------QARAEEDARRFRKQAEDIGERLYRTELATQEK 2414
Cdd:COG4913 862 IKERIDPLNDSlkripfgpgrylrleaRPRPDPEVREFRQELRAVTSGASLFDEELSEA 920
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1757-2028 |
5.56e-10 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 65.74 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1757 SKARAEEESRSTSEKSKQRLEAEAGRF-RELAEEAARlralAEEAKRQRQLAEEDAVrqrAEAERVLAEKLAAISEATRL 1835
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLeREKAAREAR----HKKAAEARAAKDKDAV---AAALARVKAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1836 KTEAEIALKEKEAEnERLRRLAEDEAFQRRLLEEQAAQHKADIEARL--AQLRKASESELERQKGLVEDTlrQRRQVEEE 1913
Cdd:PRK05035 509 KAGARPDNSAVIAA-REARKAQARARQAEKQAAAAADPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDP--KKAAVAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1914 ILALKGSFEKAAAGKAELELELgrirgTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 1993
Cdd:PRK05035 586 IARAKAKKAAQQAASAEPEEQV-----AEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKA 660
|
250 260 270
....*....|....*....|....*....|....*
gi 1920237970 1994 ALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2028
Cdd:PRK05035 661 AQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1522-2017 |
6.26e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1522 LQALEELRLQAEEAE---RRLRQAEAERARQVQVALE-TAQRSAEAELQSEHASFAEKTAQLERtLKEEHVAVVQLREEA 1597
Cdd:PRK02224 161 LGKLEEYRERASDARlgvERVLSDQRGSLDQLKAQIEeKEEKDLHERLNGLESELAELDEEIER-YEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1598 TRRAQQQAEAERARAEAERELERWQLKANEALRLRLQ-AEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQREL 1676
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREElAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1677 AEQELEKQRQLAEGTAQQRlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLA 1756
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQ-AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1757 SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE----------------DAVRQRAEAER 1820
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvETIEEDRERVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1821 VLAEKLAAIsEATRLKTEAEI----ALKEKEAENERLRRlaedeafQRRLLEEQAAQHKADIEA---RLAQLRKAS---E 1890
Cdd:PRK02224 479 ELEAELEDL-EEEVEEVEERLeraeDLVEAEDRIERLEE-------RREDLEELIAERRETIEEkreRAEELRERAaelE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1891 SELERQKglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELElELGRIRgtaeDTLRSKEQAEQEAARQRQLAAEEERRR 1970
Cdd:PRK02224 551 AEAEEKR---EAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLERIR----TLLAAIADAEDEIERLREKREALAELN 622
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1920237970 1971 REAEERVQkslaaeeeAARQRKAALEEvERLKAKVEEARRLRERAEQ 2017
Cdd:PRK02224 623 DERRERLA--------EKRERKRELEA-EFDEARIEEAREDKERAEE 660
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1086-1537 |
7.52e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 7.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1086 QEAEEVLRAHEEQLK--EAQAVPATLPELEATKAALKKLRAQAEAQQPVFDAlrDELRGAQEVGERLQQRHGErdvEVER 1163
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA--DELKKAEELKKAEEKKKAE---EAKK 1571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1164 WRERVTLLLERWQavlaqtDVRQRELEQLGRQLRYYRESADPLGAWLRdaKQRQEQIQAvplansqavrEQLRQEKALLE 1243
Cdd:PTZ00121 1572 AEEDKNMALRKAE------EAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEAKIKA----------EELKKAEEEKK 1633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1244 DIERHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAKKPkvqsgSESIIQEYVDLRtRYSELSTLTSQYIRF 1323
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKK-----AEEAKKAEEDEK-KAAEALKKEAEEAKK 1703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1324 ISETLRRMEEEERLAEQQRAEERERLAEVEaalekqrqlaeahaQAKAQAEREaqglqRRMQEEVARREEVAVEAQEQKR 1403
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAE--------------EAKKEAEED-----KKKAEEAKKDEEEKKKIAHLKK 1764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1404 SIQEELQHLRQSSEAEIQAKARqvEAAERSRLRIEEEIRVVRLQLEATerQRGGAEGELQALRARAEEAEAQKRQAqEEA 1483
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVIEEELD--EEDEKRRMEVDKKIKDIFDNFANI--IEGGKEGNLVINDSKEMEDSAIKEVA-DSK 1839
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 1484 ERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRaLQALEELRLQAEEAER 1537
Cdd:PTZ00121 1840 NMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDL-KEDDEEEIEEADEIEK 1892
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2255-2676 |
8.68e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 8.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2255 EEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLK-AEAELLQQQKELAQ--EQAR 2331
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARkaEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2332 RLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRlRVAEMSRAQ-ARAEEDARRF---RKQAEDIGERLYRT 2407
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEER-KAEEARKAEdAKKAEAVKKAeeaKKDAEEAKKAEEER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2408 ELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQllqlKSEEMQTVrqEQLLQETQALQQSFLSEKD 2487
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK----KAEEKKKA--DEAKKKAEEAKKADEAKKK 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2488 SLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASME-----------EARRRQHEAE---EGV 2553
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkadaakkkaEEKKKADEAKkkaEED 1403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2554 RRQQEELQRLAQQQQQQEKLL--AEENQRLRERLQHLEEERRAalarseEIAPSRAAAARALPNGQDAADGPAAAAEPEH 2631
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKkkAEEKKKADEAKKKAEEAKKA------DEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1920237970 2632 AFDGLRRKVPAQRLQEVGVLSAEELQQLAQGRTTVAELAQREDVR 2676
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1679-2040 |
8.77e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1679 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQR--EAAAATQKRRELEAELAKVRAEMEvlla 1756
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1757 sKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLK 1836
Cdd:COG4717 150 -ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1837 TEAEIALKEKEAENERLRRL---------------AEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVE 1901
Cdd:COG4717 229 LEQLENELEAAALEERLKEArlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1902 DTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERrrreaeerVQKSL 1981
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL--------LAEAG 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1982 AAEEEAARQRKAALEEVERLKAKVEEA-RRLRERAEQESARQLQLAQEAAQKRLQAEEKA 2040
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELeEQLEELLGELEELLEALDEEELEEELEELEEE 440
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1090-1909 |
9.55e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.36 E-value: 9.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1090 EVLRAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAqqpvfdaLRDELRGAQEvGERLQQRHGERDVEVERWRERvt 1169
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQA-------ASDHLNLVQT-ALRQQEKIERYQADLEELEER-- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1170 llLERWQAVLAQTDVRQRELEqlgRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVReQLRQEKALLE----DI 1245
Cdd:PRK04863 364 --LEEQNEVVEEADEQQEENE---ARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ-ALERAKQLCGlpdlTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1246 ERHGEKVEECQRFAKQYINAIKDYELQLVTYKA---QLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQY-- 1320
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQLqq 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1321 IRFISETLRRMEEEERLAEQQRAEERERL-------AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREE 1393
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRAERLLAEFCKRLgknlddeDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1394 VAVEAQEQkRSIQEELQHLRQSSEAE----------IQAKARQVEAAERSRLRIEEEIRVVRLQLEATErQRGGAEGE-L 1462
Cdd:PRK04863 598 LAARAPAW-LAAQDALARLREQSGEEfedsqdvteyMQQLLERERELTVERDELAARKQALDEEIERLS-QPGGSEDPrL 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1463 QALRAR-----------------AEEAEA---QKRQA--QEEAERLRRQVQDET-------------QRKRQA-----EA 1502
Cdd:PRK04863 676 NALAERfggvllseiyddvsledAPYFSAlygPARHAivVPDLSDAAEQLAGLEdcpedlyliegdpDSFDDSvfsveEL 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1503 ELALRVQ-AEAE--------------AAREKQralqaLEELRLQAEEAERRLRQAEAERaRQVQVALETAQR-------- 1559
Cdd:PRK04863 756 EKAVVVKiADRQwrysrfpevplfgrAAREKR-----IEQLRAEREELAERYATLSFDV-QKLQRLHQAFSRfigshlav 829
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1560 SAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVA 1639
Cdd:PRK04863 830 AFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEA 909
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1640 QQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ--------------LAEGTAQQRLAAEQEL-IR 1704
Cdd:PRK04863 910 KRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQqafaltevvqrrahFSYEDAAEMLAKNSDLnEK 989
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1705 LRAETEQGEQQRQLLEEEL--------------ARLQREAAAATQKRRELEAELAK--VRAEMEVLLASKARAEE----- 1763
Cdd:PRK04863 990 LRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQMLQELKQELQDlgVPADSGAEERARARRDElharl 1069
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1764 ----ESRSTSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAKRQRQLAeEDAVRQRAEAERVLAEKLAAIS--EAT 1833
Cdd:PRK04863 1070 sanrSRRNQLEKQLTFCEAEmdnlTKKLRKLERDYHEMREQVVNAKAGWCAV-LRLVKDNGVERRLHRRELAYLSadELR 1148
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1834 RLKTEAEIALKEKEAENERLR---RLAEDEAFQ----------RRLLEEQAAQhkaDIeARLAQLRKASEsELERQKGLV 1900
Cdd:PRK04863 1149 SMSDKALGALRLAVADNEHLRdvlRLSEDPKRPerkvqfyiavYQHLRERIRQ---DI-IRTDDPVEAIE-QMEIELSRL 1223
|
....*....
gi 1920237970 1901 EDTLRQRRQ 1909
Cdd:PRK04863 1224 TEELTSREQ 1232
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1194-1864 |
1.37e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1194 RQLRYYRESADPLGAWLRDAKQRQEQIQAvpLANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDY---- 1269
Cdd:PRK03918 111 SSVREWVERLIPYHVFLNAIYIRQGEIDA--ILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFikrt 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1270 ---ELQLVTYKAQLEPVASPAKK-----PKVQSGSESIIQEYVDLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQ 1341
Cdd:PRK03918 189 eniEELIKEKEKELEEVLREINEisselPELREELEKLEKEVKELEELKEEIEELEKE-LESLEGSKRKLEEKIRELEER 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1342 RAEERERLAEVE---AALEKQRQLAEAHAQAK-----------------AQAEREAQGLQRRMQEEVARREEVAvEAQEQ 1401
Cdd:PRK03918 268 IEELKKEIEELEekvKELKELKEKAEEYIKLSefyeeyldelreiekrlSRLEEEINGIEERIKELEEKEERLE-ELKKK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1402 KRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQE 1481
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1482 EAERLRRQVQDETQRKRQAEAELALRVQAEAEAarEKQRALQALEELRLQAEEAERRLRQAEAERARQ--VQVALETAQ- 1558
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRELTEEHRKELLEEYTA--ELKRIEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKELAEq 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1559 -RSAEAELQSEHASFAEKTAQLERTLKEEhvaVVQLREEATRRAQqqaeaeraraeaerelerwQLKANEALRLRLQAEE 1637
Cdd:PRK03918 505 lKELEEKLKKYNLEELEKKAEEYEKLKEK---LIKLKGEIKSLKK-------------------ELEKLEELKKKLAELE 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1638 VAQQKsltqaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLaEGTAQQRLAAEQELIRLRaeteQGEQQRQ 1717
Cdd:PRK03918 563 KKLDE----------------------LEEELAELLKELEELGFESVEEL-EERLKELEPFYNEYLELK----DAEKELE 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1718 LLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLasKARAEEESRSTSEKskqrleaeagrFRELAEEAARLRALA 1797
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELE--KKYSEEEYEELREE-----------YLELSRELAGLRAEL 682
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1798 EEAKRQRQLAEEDAvrqraeaeRVLAEKLAAISEATRLKTEAEIALKEKEAENERLRR---LAEDEAFQR 1864
Cdd:PRK03918 683 EELEKRREEIKKTL--------EKLKEELEEREKAKKELEKLEKALERVEELREKVKKykaLLKERALSK 744
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
36-144 |
1.42e-09 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 58.35 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 36 KKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERdvirssRLPREKGRMRFHKLQNV 106
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTID-ER------KLNKKKPKNIFEATENL 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 1920237970 107 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 144
Cdd:cd21217 76 NLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
937-1586 |
1.80e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.32 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 937 DRLQAEREYgscSRHYQQLLQSLEQGEQEESrcqrcISELKDIRLQLEACEtrtvhrlrlpldkepaRECAQRITEQQKA 1016
Cdd:TIGR02169 201 ERLRREREK---AERYQALLKEKREYEGYEL-----LKEKEALERQKEAIE----------------RQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1017 QAEVDGLGKGVA----RLSAEAEKVLALPEPSPAAptLRSELELTLGKLEQVRSLSAIYLEKL--------KTISLVIRS 1084
Cdd:TIGR02169 257 TEEISELEKRLEeieqLLEELNKKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKERELedaeerlaKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1085 TQEAEEVLRAHEEQLKEAQAVPAtlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGE-------- 1156
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTE---EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINElkreldrl 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1157 ------RDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQ--------- 1221
Cdd:TIGR02169 412 qeelqrLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEkelsklqre 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1222 -----AVPLANSQAVREQLRQEKALLEDI--------------ERHGEKVE-------------------ECQRFAKQY- 1262
Cdd:TIGR02169 492 laeaeAQARASEERVRGGRAVEEVLKASIqgvhgtvaqlgsvgERYATAIEvaagnrlnnvvveddavakEAIELLKRRk 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1263 --------INAIK---------------DYELQLVTYKAQLEPVASPAKKPKV-----QSGSESIIQ-----------EY 1303
Cdd:TIGR02169 572 agratflpLNKMRderrdlsilsedgviGFAVDLVEFDPKYEPAFKYVFGDTLvvediEAARRLMGKyrmvtlegelfEK 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1304 VDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRR 1383
Cdd:TIGR02169 652 SGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1384 MQEEVARREEVAVEAQEQKRSIQEELQHLrQSSEAEIQAKARQVEAAERSRLRIE-----EEIRVVRLQLEATERQRGGA 1458
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSEL-KELEARIEELEEDLHKLEEALNDLEarlshSRIPEIQAELSKLEEEVSRI 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1459 EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK---RQAEAELALRVQAEAEAAREKQRALQALEE----LRLQ 1531
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIksiEKEIENLNGKKEELEEELEELEAALRDLESrlgdLKKE 890
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 1532 AEEAERRLRQAEaERARQVQVALETAqRSAEAELQSEHASFAEKTAQLERTLKEE 1586
Cdd:TIGR02169 891 RDELEAQLRELE-RKIEELEAQIEKK-RKRLSELKAKLEALEEELSEIEDPKGED 943
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1499-1866 |
2.04e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 63.99 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1499 QAEAELALRVQAEAEAAREKQRALQALEELrlqAEEAERRLRQAEAERARQvqvaletaqrsaeAELQSEHASFAEktaq 1578
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEK---AREVERRRKLEEAEKARQ-------------AEMDRQAAIYAE---- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1579 lertlkEEHVAVVQLREeatrraqqqaeaeraraeaereLERWQLKANEALRLRLQAEEVAQQksLTQAEAEKQKEEAER 1658
Cdd:pfam17380 339 ------QERMAMERERE----------------------LERIRQEERKRELERIRQEEIAME--ISRMRELERLQMERQ 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1659 EARRRGKAEEQAVRQRELAEQE-----LEKQRQLAEGTAQQRLAAEQELIRLraETEQGEQQRQLLEEELARLQReaaaa 1733
Cdd:pfam17380 389 QKNERVRQELEAARKVKILEEErqrkiQQQKVEMEQIRAEQEEARQREVRRL--EEERAREMERVRLEEQERQQQ----- 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1734 TQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKskqrlEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAvR 1813
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK-----ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER-R 535
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 1814 QRAEAER---VLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRL 1866
Cdd:pfam17380 536 REAEEERrkqQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1684-1898 |
2.38e-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: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1684 QRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEE 1763
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1764 ESRSTSEKSKQRLEA--EAGRFRELA--------EEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEAT 1833
Cdd:COG4942 98 ELEAQKEELAELLRAlyRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 1834 RLKTEAEIALKE----KEAENERLRRLAEDEAFQRRLLEEQAAQhKADIEARLAQLRKASESELERQKG 1898
Cdd:COG4942 178 ALLAELEEERAAlealKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAERTPA 245
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1338-1536 |
2.66e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 62.52 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1338 AEQQRAEE-RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARReevavEAQEQKrsiQEELQHLRQSS 1416
Cdd:PRK09510 72 KSAKRAEEqRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQ-----AALKQK---QAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1417 EAEIQAKARQVEAAERSRlRIEEEIRvVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlrrqVQDETQR 1496
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAK-KAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK----AAAEAKK 217
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1920237970 1497 KRQAEAELAL-RVQAEAEAAREKQRALQALEELRLQAEEAE 1536
Cdd:PRK09510 218 KAAAEAKAAAaKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
162-264 |
2.85e-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: 57.77 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 162 TAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 240
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 1920237970 241 PEDVDVPQPDEKSIITYVSSLYDA 264
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1231-1821 |
2.92e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1231 VREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDlrtRY 1310
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE---EY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1311 SELSTLTSQYIrfisETLRRMEEEERLAEQQRAEERERLAEVEaalEKQRQLaeahaqakaqaeREAQGLQRRMQEEVAR 1390
Cdd:PRK03918 296 IKLSEFYEEYL----DELREIEKRLSRLEEEINGIEERIKELE---EKEERL------------EELKKKLKELEKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1391 REEvAVEAQEQKRSIQEELQHLRQS-SEAEIQAKARQVEAAERSRLRIEEEIRVV---RLQLEATERQRGGAEGELQALR 1466
Cdd:PRK03918 357 LEE-RHELYEEAKAKKEELERLKKRlTGLTPEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1467 ARA---------EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlrvqaEAEAAREKQRALQALEELRLQAEEAER 1537
Cdd:PRK03918 436 GKCpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR-----ELEKVLKKESELIKLKELAEQLKELEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1538 RLRQAEAERarqvqvaLETAQRSAEaELQSEHASFAEKTAQLERTLKEEHvavvQLREEATRRAQQQAEAERARAEAERE 1617
Cdd:PRK03918 511 KLKKYNLEE-------LEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLE----ELKKKLAELEKKLDELEEELAELLKE 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1618 LERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLA 1697
Cdd:PRK03918 579 LEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE--ELEKKY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1698 AEQELIRLRAETEQgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLlaSKARAEEESrstSEKSKQRLE 1777
Cdd:PRK03918 657 SEEEYEELREEYLE-------LSRELAGLRAELEELEKRREEIKKTLEKLKEELEER--EKAKKELEK---LEKALERVE 724
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1778 AEAGRFRELAEEAARlRALAEEAKRQRQLAEE------DAVRQRAEAERV 1821
Cdd:PRK03918 725 ELREKVKKYKALLKE-RALSKVGEIASEIFEEltegkySGVRVKAEENKV 773
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1083-1279 |
3.25e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.15 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1083 RSTQEAEEVLRAHEEQLKEAQaVPATLPELEATKAALKKLRAQAEAQQPVFDALrdelrgaQEVGERLQQRHGERDVEVe 1162
Cdd:cd00176 7 RDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1163 rwRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLGAWLRDAKQRQEQIQavPLANSQAVREQLRQEKALL 1242
Cdd:cd00176 78 --QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELE 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1920237970 1243 EDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1279
Cdd:cd00176 153 EELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2144-2602 |
3.72e-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: 63.45 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2144 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILdeelqRLKAEVTEAARQRGQVEEELFSLRVQ 2223
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA-----PLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2224 MEELGKLKARIEA--ENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAA---RLRQLAEE---DLAQQRALA 2295
Cdd:TIGR00618 320 MRSRAKLLMKRAAhvKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqHIHTLQQQkttLTQKLQSLC 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2296 EKMLKEKMQAVQEATRLKAEAELLQQ------QKELAQEQARRLQEDKEQMAQQLAQETQGFQK-------------TLE 2356
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGQlahakkQQELQQRYAELCAAAITCTAQCEKLEKIHLQEsaqslkereqqlqTKE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2357 TERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLR 2436
Cdd:TIGR00618 480 QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRA 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2437 EAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEqlLQETQALQQSFLSEKDSLLQRERCIE---------QEKAKLEQLF 2507
Cdd:TIGR00618 560 SLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNI--TVRLQDLTEKLSEAEDMLACEQHALLrklqpeqdlQDVRLHLQQC 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2508 QDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEAR---------------------------------RRQHEAEEGVR 2554
Cdd:TIGR00618 638 SQELALKLTALHALQLTLTQERVREHALSIRVLPKEllasrqlalqkmqsekeqltywkemlaqcqtllRELETHIEEYD 717
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1920237970 2555 RQQEELQRLAQQQQQQeklLAEENQRLRERLQHLEEERRAALARSEEI 2602
Cdd:TIGR00618 718 REFNEIENASSSLGSD---LAAREDALNQSLKELMHQARTVLKARTEA 762
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1186-1564 |
4.03e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 63.43 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1186 QRELEQLGRQLRYYRESADplgawlrDAKQRQEQIQA-VPLANSQAvREQLRQekaLLEDIERHGEKVEECQRFAKQYIN 1264
Cdd:COG3096 849 ERELAQHRAQEQQLRQQLD-------QLKEQLQLLNKlLPQANLLA-DETLAD---RLEELREELDAAQEAQAFIQQHGK 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1265 AIkdyelqlvtykAQLEPVASPAKKPKVQSgsESIIQEYVDLRTRYSELStltsQYIRFISETLRRM------EEEERLA 1338
Cdd:COG3096 918 AL-----------AQLEPLVAVLQSDPEQF--EQLQADYLQAKEQQRRLK----QQIFALSEVVQRRphfsyeDAVGLLG 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1339 EQQRAEE--RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEevarreevaveAQEQKRSIQEELQHLrqss 1416
Cdd:COG3096 981 ENSDLNEklRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDA-----------KQQTLQELEQELEEL---- 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1417 eaEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQ 1489
Cdd:COG3096 1046 --GVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcAVLRL 1123
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 1490 VQDETQRKRQAEAELalrvqaeaeaarekqrALQALEELRLQAEEAERRLRQAEAERArQVQVALETAQRSAEAE 1564
Cdd:COG3096 1124 ARDNDVERRLHRREL----------------AYLSADELRSMSDKALGALRLAVADNE-HLRDALRLSEDPRRPE 1181
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1707-2296 |
4.19e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1707 AETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTS--EKSKQRLEAEAG--- 1781
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELEslEGSKRKLEEKIRele 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1782 --------RFRELAEEAARLRALAEEAKRQRQLAEEdaVRQRAEAERVLAEKLAAISEATRlktEAEIALKEKEAENERL 1853
Cdd:PRK03918 266 erieelkkEIEELEEKVKELKELKEKAEEYIKLSEF--YEEYLDELREIEKRLSRLEEEIN---GIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1854 RRLAEDEAFQRRLLEEQAAQHKA--DIEARLAQLRKASES----ELERQKGLVEDTLRQRRQVEEEILAL---KGSFEKA 1924
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEISKItarIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1925 AAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLaaeeerrrrEAEERVQKSLAAEEEAARQRKAALEEVERLKAK 2004
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYT---------AELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2005 VEEARRLRERAEQESARQLQLAQEAAQKrlqAEEKAHAF-AVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAeeaeaa 2083
Cdd:PRK03918 492 ESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEYeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELE------ 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2084 reraereaaqsrRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQ 2163
Cdd:PRK03918 563 ------------KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2164 ALRQKAQVEQELTALRLQLEETdhQKSILDEELQRLKAEVTEaarqrgqVEEELFSLRVQMEELGKLKARIEAEnralvL 2243
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEEL--EKKYSEEEYEELREEYLE-------LSRELAGLRAELEELEKRREEIKKT-----L 696
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 2244 RDkdsaqrlLQEEAEKMKQVAEEAARLSVAAQEAARLRQ--LAEEDLAQQRALAE 2296
Cdd:PRK03918 697 EK-------LKEELEEREKAKKELEKLEKALERVEELREkvKKYKALLKERALSK 744
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
157-259 |
4.35e-09 |
|
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: 57.10 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 157 QSEDMTAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGV 235
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 1920237970 236 TRLLDPEDVDVPQPDEKSIITYVS 259
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4374-4412 |
4.78e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 54.64 E-value: 4.78e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1920237970 4374 FLEVQYLTGGLIEPDTPGRVALDEALQRGTVDARTAQKL 4412
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2290-2592 |
4.85e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.83 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2290 QQRALAEKMLKEKMQAVqEATRLKAEAEL----LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEM 2365
Cdd:pfam17380 280 HQKAVSERQQQEKFEKM-EQERLRQEKEEkareVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2366 SAEAERLRLRVAEMSRAQARAEEDARRFRKQAEdigERLyRTELATQEKVMLvqtLETQRQQSDRDAERLREAIaELEHE 2445
Cdd:pfam17380 359 KRELERIRQEEIAMEISRMRELERLQMERQQKN---ERV-RQELEAARKVKI---LEEERQRKIQQQKVEMEQI-RAEQE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2446 KDKLKQEAQLLQLKSEEMQTVRQEQL--LQETQALQQSFLSEKDSLLQRERcIEQEKAKLEQLFQDEVAKAQALREEQQR 2523
Cdd:pfam17380 431 EARQREVRRLEEERAREMERVRLEEQerQQQVERLRQQEEERKRKKLELEK-EKRDRKRAEEQRRKILEKELEERKQAMI 509
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 2524 QQQQMQQEkqqLAASMEEarRRQHEAEEGVRRQQEELQRlaqqqqqqEKLLAEENQRLRERLQHLEEER 2592
Cdd:pfam17380 510 EEERKRKL---LEKEMEE--RQKAIYEEERRREAEEERR--------KQQEMEERRRIQEQMRKATEER 565
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1363-1586 |
5.09e-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: 61.70 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1363 AEAHAQAKAQAEREAQGLQRRMQEEVARREEvaveAQEQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEE 1439
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAA----LKKEEKALLKQLAALERriaALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1440 EIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ 1519
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 1520 RALQALEELRLQAEEAERRLRQAEAERARQVQV--ALETAQRSAEAELQSEHASFAEKTAQLERTLKEE 1586
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARleKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1480-1961 |
5.66e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1480 QEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQR 1559
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1560 SAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREeatrraqqqaeaeraraeaerelerwqlKANEALRLRLQAEEVA 1639
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEE----------------------------LEAELAELQEELEELL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1640 QQKSLTQAeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1719
Cdd:COG4717 184 EQLSLATE-----------------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1720 EEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRStseKSKQRLEAEAGRFRELAEEAARLRALAEE 1799
Cdd:COG4717 247 EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEEELEE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1800 AKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLE--EQAAQHKAD 1877
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1878 IEARLAQLRKASESELERQKGLVEDTLRQR-RQVEEEILALKGSFEKAAAGKAELELELGRIRGtaEDTLRSKEQAEQEA 1956
Cdd:COG4717 404 LEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEEL 481
|
....*
gi 1920237970 1957 ARQRQ 1961
Cdd:COG4717 482 KAELR 486
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1676-1907 |
5.78e-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: 61.40 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1676 LAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAelakvraemevll 1755
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAK---KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQA------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1756 askARAEEESRSTSEKSKQRLEAEAGRfrelAEEAARLRALAEEAKRQrqlAEEDAVRQRAEAervlAEKLAaisEATRL 1835
Cdd:TIGR02794 111 ---AKQAEEKQKQAEEAKAKQAAEAKA----KAEAEAERKAKEEAAKQ---AEEEAKAKAAAE----AKKKA---EEAKK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 1836 KTEAEiALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIE----ARLAQLRKASESELERQKGLVEDTLRQR 1907
Cdd:TIGR02794 174 KAEAE-AKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEaaaaAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1100-1521 |
6.09e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.45 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1100 KEAQAVPATLPELEA-----------------TKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERdVEVE 1162
Cdd:pfam17380 221 KEVQGMPHTLAPYEKmerrkesfnlaedvttmTPEYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEK-MEQE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1163 RWR---ERVTLLLERWQAVLAQTDVRQRELEqlgRQLRYYRESAdplgawlRDAKQRQEQIQAVPLANSQAVREQLRQEK 1239
Cdd:pfam17380 300 RLRqekEEKAREVERRRKLEEAEKARQAEMD---RQAAIYAEQE-------RMAMERERELERIRQEERKRELERIRQEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1240 ALLEDierhgEKVEECQRFakqyinaikdyelqlvtykaQLEPvaspakkpkvQSGSESIIQEYVDLRtrysELSTLTSQ 1319
Cdd:pfam17380 370 IAMEI-----SRMRELERL--------------------QMER----------QQKNERVRQELEAAR----KVKILEEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1320 YIRFISETLRRMEEEERLAEQQRAEERERLAEveaalEKQRQLAEAHAQakaQAEREAQGLQRRMQEEVARREEVAVEAQ 1399
Cdd:pfam17380 411 RQRKIQQQKVEMEQIRAEQEEARQREVRRLEE-----ERAREMERVRLE---EQERQQQVERLRQQEEERKRKKLELEKE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1400 EQKRSIQEELQhlRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqleatERQRGGAEGElqalRARAEEAEAQKRQA 1479
Cdd:pfam17380 483 KRDRKRAEEQR--RKILEKELEERKQAMIEEERKRKLLEKEME---------ERQKAIYEEE----RRREAEEERRKQQE 547
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1920237970 1480 QEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRA 1521
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4296-4333 |
6.99e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.03 E-value: 6.99e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1920237970 4296 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 4333
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2241-2580 |
7.16e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.06 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2241 LVLRDKDSAQRLLQEEAEKM-----KQVAEEAARlsvaaqEAARLRQLAEEDLAQQRALAEkmlkekmqavqeatrlkaE 2315
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqerlRQEKEEKAR------EVERRRKLEEAEKARQAEMDR------------------Q 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2316 AELLQQQKELAQEQARRL----QEDKEQMAQQLAQETQGFQKTLETERQR-QLEMSAEAERLRLRVAEMSRAQARAEEDA 2390
Cdd:pfam17380 333 AAIYAEQERMAMERERELerirQEERKRELERIRQEEIAMEISRMRELERlQMERQQKNERVRQELEAARKVKILEEERQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2391 RRFRKQAEDIGERLYRTELATQEKVmlvQTLETQRQqsdRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQ 2470
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEQEEARQREV---RRLEEERA---REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDR 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2471 LLQETQ---ALQQSFLSEKDSLLQRERCIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQMQqekqqlaasMEEaRRRQH 2547
Cdd:pfam17380 487 KRAEEQrrkILEKELEERKQAMIEEERKRKLLEKEMEER-QKAIYEEERRREAEEERRKQQE---------MEE-RRRIQ 555
|
330 340 350
....*....|....*....|....*....|...
gi 1920237970 2548 EAEEGVRRQQEELQRLAQQQQQQEKLLAEENQR 2580
Cdd:pfam17380 556 EQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
30-149 |
7.29e-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: 56.93 E-value: 7.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 30 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSSRLPREKGRMRfhKLQNVQIA 109
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIK---VPVDWNKVNKPPYPKLGANMK--KLENCNYA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1920237970 110 LDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 149
Cdd:cd21331 91 VELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1328-1548 |
8.79e-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: 60.93 E-value: 8.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1328 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQE 1407
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1408 ---ELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1484
Cdd:COG4942 109 llrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 1485 RLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERAR 1548
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1354-1578 |
8.87e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.98 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1354 AALEKQRQLAEAHAQAKAQAEREAQGLQRrmQEEVarREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAK---ARQVEAA 1430
Cdd:PRK09510 60 VVEQYNRQQQQQKSAKRAEEQRKKKEQQQ--AEEL--QQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKqaaLKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1431 ERsrlrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDETQRKRQAEAELALRVQ 1509
Cdd:PRK09510 136 EA--------------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAA 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 1510 AEAEAAREKQRALQAleelrlqAEEAErrlRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ 1578
Cdd:PRK09510 197 AEAKKKAEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1807-2340 |
1.03e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1807 AEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdEAFQRRLLEEQAAQHKADIEARLAQLR 1886
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE-EIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1887 KASESELERQKGLVEDT--LRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAA 1964
Cdd:PRK03918 266 ERIEELKKEIEELEEKVkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1965 EEERrrreaeerVQKSLAAEEEAArqrkaalEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAfA 2044
Cdd:PRK03918 346 KLKE--------LEKRLEELEERH-------ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS-K 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2045 VQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEReaaqsRRQVEEAERLKQSAEEQAQAQAQAQAAAEK 2124
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELL-----EEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2125 LRKEAEQEAARraqaeqaaLRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKA--- 2201
Cdd:PRK03918 485 LEKVLKKESEL--------IKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkk 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2202 EVTEAARQRGQVEEELFSLRVQMEELG---------KLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEA-ARLS 2271
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGfesveeleeRLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAfEELA 636
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2272 VAAQEAARLR-QLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2340
Cdd:PRK03918 637 ETEKRLEELRkELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2151-2601 |
1.03e-08 |
|
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: 61.91 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2151 DAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKaevtEAARQRGQVEEELFSLRVQMEELGKL 2230
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR----EAQEEQLKKQQLLKQLRARIEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2231 KARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEA-ARLSVAAQEAARLRQLA------EEDLAQQRALAEKMLKEKM 2303
Cdd:TIGR00618 276 EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIhTELQSKMRSRAKLLMKRaahvkqQSSIEEQRRLLQTLHSQEI 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2304 QAVQEATRLKAEAELLQQQKELAQeQARRLQEDKEQMAQQLaqetQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQ 2383
Cdd:TIGR00618 356 HIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKL----QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2384 ARAEEDARRFRKQAEDIGER----------LYRTELATQEKVMLVQTLETQRQQSDR-----DAERLREAIAELEHEKDK 2448
Cdd:TIGR00618 431 KQQELQQRYAELCAAAITCTaqceklekihLQESAQSLKEREQQLQTKEQIHLQETRkkavvLARLLELQEEPCPLCGSC 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2449 LKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQM 2528
Cdd:TIGR00618 511 IHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ 590
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 2529 QQEKQQLAASMEEARRR------QHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEE 2601
Cdd:TIGR00618 591 NITVRLQDLTEKLSEAEdmlaceQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRV 669
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
25-147 |
1.16e-08 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409071 Cd Length: 121 Bit Score: 56.06 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 25 EKYKDERDRVQ--KKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDVIRSSRLPrekgrmrfHK 102
Cdd:cd21222 5 DLFDEAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPLHEYHLTPSTDD--------EK 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1920237970 103 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 147
Cdd:cd21222 77 LHNVKLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
157-264 |
1.31e-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: 55.48 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 157 QSEDMTAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGV 235
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 1920237970 236 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 264
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1334-1548 |
1.33e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 60.24 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1334 EERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSiQEELQHLR 1413
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQK-QAEEAKAK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1414 QSSEAEIQAKA-RQVEAAERSRLRIEEEirvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE----AERLRR 1488
Cdd:TIGR02794 128 QAAEAKAKAEAeAERKAKEEAAKQAEEE----AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakakAEAAKA 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1489 QVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERAR 1548
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1365-1824 |
1.38e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 61.57 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1365 AHAQAKAQAEREAQGLQRRMQEEVARreeVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVV 1444
Cdd:COG3903 475 EYAAERLAEAGERAAARRRHADYYLA---LAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1445 RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQA 1524
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1525 LEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQ 1604
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1605 AEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1684
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1685 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE 1764
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1765 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAE 1824
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1082-2019 |
1.46e-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: 61.51 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1082 IRSTQEAEEVLRAHEEQLKEAQAvpatlpeleatkaALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQ--RHGERdv 1159
Cdd:COG3096 284 SERALELRRELFGARRQLAEEQY-------------RLVEMARELEELSARESDLEQDYQAASDHLNLVQTalRQQEK-- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1160 eVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVReqlrqek 1239
Cdd:COG3096 349 -IERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ------- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1240 ALledierhgEKVEECQRFAKQYINAIKDYelqLVTYKAQLEpvaspakkpkvqsgseSIIQEYVDLRTRYSELSTLTSQ 1319
Cdd:COG3096 421 AL--------EKARALCGLPDLTPENAEDY---LAAFRAKEQ----------------QATEEVLELEQKLSVADAARRQ 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1320 YIRFIsETLRRMEEE-ERLAEQQRAEERER-------LAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARR 1391
Cdd:COG3096 474 FEKAY-ELVCKIAGEvERSQAWQTARELLRryrsqqaLAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1392 EEVAVEAQEQKRSIQEELQHLRQSSEAEIQakarqveaaersrlrieeeirvvrlqleaTERQRGGAEGELQALRARAEE 1471
Cdd:COG3096 553 EELEELLAELEAQLEELEEQAAEAVEQRSE-----------------------------LRQQLEQLRARIKELAARAPA 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1472 AeaqkRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAeeaeRRLRQAE-AERARQV 1550
Cdd:COG3096 604 W----LAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQI----ERLSQPGgAEDPRLL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1551 Q----------------VALETAQR-------SAEAELQSEHASFAEKTAQLERTLkeEHVAVVQLREEATRRAQQQAEA 1607
Cdd:COG3096 676 AlaerlggvllseiyddVTLEDAPYfsalygpARHAIVVPDLSAVKEQLAGLEDCP--EDLYLIEGDPDSFDDSVFDAEE 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1608 ERARAEAERELERWQL-------------KANEALRLRLQAEEVAQQKSltqaeaekqkeeaerearrrgkaeEQAVRQR 1674
Cdd:COG3096 754 LEDAVVVKLSDRQWRYsrfpevplfgraaREKRLEELRAERDELAEQYA------------------------KASFDVQ 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1675 ELaeQELEKQ-RQLAEGTAQQRLAAEQElirlrAETEQGEQQRQLLEEELARL----QREAAAATQKRRELEAeLAKVRA 1749
Cdd:COG3096 810 KL--QRLHQAfSQFVGGHLAVAFAPDPE-----AELAALRQRRSELERELAQHraqeQQLRQQLDQLKEQLQL-LNKLLP 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1750 EMEVL----LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA--LAEEAKRQRQL---AEEDAVRQRAEAER 1820
Cdd:COG3096 882 QANLLadetLADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSdpEQFEQLQADYLqakEQQRRLKQQIFALS 961
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1821 VLAEKLAAISEAtrlktEAEIALKEKEAENERLR---RLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQK 1897
Cdd:COG3096 962 EVVQRRPHFSYE-----DAVGLLGENSDLNEKLRarlEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQ 1036
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1898 GLvedtlrQRRQVEEEILALKGSFEKAAAGKAELELELGRIRG--TAEDTLRSKEQAEQEAARQRqlaaeeerrrreaEE 1975
Cdd:COG3096 1037 EL------EQELEELGVQADAEAEERARIRRDELHEELSQNRSrrSQLEKQLTRCEAEMDSLQKR-------------LR 1097
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*.
gi 1920237970 1976 RVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRL--RERAEQES 2019
Cdd:COG3096 1098 KAERDYKQEREQVVQAKAGWCAVLRLARDNDVERRLhrRELAYLSA 1143
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2144-2600 |
1.60e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2144 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEET-----DHQKSILDEELQRLKAEVTEAARQRGQVEEELF 2218
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2219 SLRVQMEELG-----KLKARIEAENRALVLRDKDSAQrlLQEEAEKMK-QVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2292
Cdd:COG4913 327 ELEAQIRGNGgdrleQLEREIERLERELEERERRRAR--LEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2293 ALAEKMLKEKMQAVQEATRLKAEAELLQQQK---ELAQEQARR-----LQEDKEQM------------------------ 2340
Cdd:COG4913 405 EALAEAEAALRDLRRELRELEAEIASLERRKsniPARLLALRDalaeaLGLDEAELpfvgelievrpeeerwrgaiervl 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2341 ---AQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLyRTELATQEKVML 2417
Cdd:COG4913 485 ggfALTLLVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWL-EAELGRRFDYVC 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2418 VQTLE-------------------TQRQQSDRDAERL--------REAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQ-- 2468
Cdd:COG4913 564 VDSPEelrrhpraitragqvkgngTRHEKDDRRRIRSryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDal 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2469 EQLLQETQALQQSFLSEKDsLLQRERCIEQEKAKLEQL--FQDEVAKAQALREEqqrqqqqmqqekqqLAASMEEARRRQ 2546
Cdd:COG4913 644 QERREALQRLAEYSWDEID-VASAEREIAELEAELERLdaSSDDLAALEEQLEE--------------LEAELEELEEEL 708
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 2547 HEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSE 2600
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1349-1761 |
1.91e-08 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 61.03 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1349 LAEVEAALEKQRQLAEAHAQAkaqaeREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE----------- 1417
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVA-----REDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1418 --------AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1489
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1490 VQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEH 1569
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1570 ASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEA 1649
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1650 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQRE 1729
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 1920237970 1730 AAAATQKRRELEAELAKVRAEMEVLLASKARA 1761
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1477-1997 |
2.11e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1477 RQAQEEAERLRRQVQD----ETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARqvqv 1552
Cdd:COG4913 238 ERAHEALEDAREQIELlepiRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER---- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1553 aLETAQRSAEAELQSEHASFAEKTAQLERTLKEEhvavvqlreeatrraqqqaeaeraraeaereLERWQLKANEALRLR 1632
Cdd:COG4913 314 -LEARLDALREELDELEAQIRGNGGDRLEQLERE-------------------------------IERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1633 LQAEEVAQQKSLTQAEAEKQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG 1712
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFA----------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1713 EQQRQLLEEELARLQREAAAATQ-KRRELE--AELAKVRAE-------MEVLLASKAR---------------------- 1760
Cdd:COG4913 432 ERRKSNIPARLLALRDALAEALGlDEAELPfvGELIEVRPEeerwrgaIERVLGGFALtllvppehyaaalrwvnrlhlr 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1761 ------------AEEESRSTSEKS-KQRLEAEAGRFR-----ELAEEAARLRALAEEA-----------------KRQRQ 1805
Cdd:COG4913 512 grlvyervrtglPDPERPRLDPDSlAGKLDFKPHPFRawleaELGRRFDYVCVDSPEElrrhpraitragqvkgnGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1806 LAEEDAVRQR----AEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEE-----QAAQHKA 1876
Cdd:COG4913 592 KDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeidvaSAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1877 DIEARLAQLRKASeSELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRirgtAEDTLRSKEQAEQEA 1956
Cdd:COG4913 672 ELEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE----LQDRLEAAEDLARLE 746
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1920237970 1957 ARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 1997
Cdd:COG4913 747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
35-146 |
3.49e-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: 54.43 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 35 QKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirSSRLPRekgRMRFHKLQNVQIALDYLR 114
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKH----ANKPPI---KMPFKKVENCNQVVKIGK 75
|
90 100 110
....*....|....*....|....*....|..
gi 1920237970 115 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 146
Cdd:cd21299 76 QLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
509-698 |
4.05e-08 |
|
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: 57.07 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 509 LRYLQDLLAWVEENQRRLDSAEWGVDLPSVEAQLGSHRGLHQSVEEFRTKIERARTDEGQLSPATRGAY---RDCLGRLD 585
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 586 LQYAKLLSSSKARLRSLE---SLHGFVAAATKELMWLSDREEEEVGFDWSDRNTNMAAKKEGYSALMHELELKEKKIKEI 662
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1920237970 663 QSTGDRLLREDHP-ARPTAESFQAALQTQWSWMLQLC 698
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1087-1442 |
5.11e-08 |
|
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: 59.69 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1087 EAEEVLRAHEEQLKEAQAVPATL-PELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWR 1165
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELrKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1166 ERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLrDAKQRQEQIQAVPLANSQAVREQLRQEKALLED- 1244
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL-DELRAELTLLNEEAANLRERLESLERRIAATERr 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1245 IERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYVDLRTRYSELstltsqyirfi 1324
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELE---------ALLNERASLEEALALLRSELEEL----------- 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1325 SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ------------------LAEAHAQAKAQAEREAQGLQRRMQE 1386
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVridnlqerlseeysltleEAEALENKIEDDEEEARRRLKRLEN 979
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 1387 EVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAErsrlRIEEEIR 1442
Cdd:TIGR02168 980 KIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE----EIDREAR 1031
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1677-1864 |
5.35e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.66 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1677 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA--AATQKRRELEAELAKVRAEMEVL 1754
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQkqAEEAAAKAAAAAKAKAEAEAKRA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1755 LASKARAEEESrstseksKQRLEAEAgrfRELAEEAARLRALAEEAKrqrQLAEEDAVRQRAEAERVlAEKLAAISEATR 1834
Cdd:PRK09510 157 AAAAKKAAAEA-------KKKAEAEA---AKKAAAEAKKKAEAEAAA---KAAAEAKKKAEAEAKKK-AAAEAKKKAAAE 222
|
170 180 190
....*....|....*....|....*....|
gi 1920237970 1835 LKTEAEIALKEKEAENERLRRLAEDEAFQR 1864
Cdd:PRK09510 223 AKAAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1483-1942 |
5.80e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 59.26 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1483 AERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQAleelRLQAEEAERRLRQAEAERARQVQVALETAqrSAE 1562
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLA----RLDAEHDNLRAALRWALAHGDAELALRLA--AAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1563 AELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQK 1642
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1643 SLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1722
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1723 LARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKR 1802
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1803 QRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARL 1882
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1883 AQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTA 1942
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2162-2602 |
5.88e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 59.47 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2162 EQALRQKAQVEQELTALRLQL-EETDHQKSILDEELQRLKAEVTEAARQRGQV---EEELFSLRVQMEELGKLKARIEAE 2237
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERAREEQEAA 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2238 NRAlvlrdkdsaQRLLQEEAEKMKQVAEEAARlsvaaqeaaRLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAE 2317
Cdd:pfam12128 484 NAE---------VERLQSELRQARKRRDQASE---------ALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAP 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2318 LLQQQ--KELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA-------QARAEE 2388
Cdd:pfam12128 546 DWEQSigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEAlqsarekQAAAEE 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2389 DARRFRKQAE--DIGERLYRTELaTQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTV 2466
Cdd:pfam12128 626 QLVQANGELEkaSREETFARTAL-KNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEE 704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2467 RQEQLLQETQALQQSFL---SEKDSLLQR-----ERCIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQMQQEKQQLAAS 2538
Cdd:pfam12128 705 QKEQKREARTEKQAYWQvveGALDAQLALlkaaiAARRSGAKAELKAL-ETWYKRDLASLGVDPDVIAKLKREIRTLERK 783
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 2539 MEEARRRQHEAEEGVRRQQE----ELQRLAQQQQQQEKLLAEENQRL-------RERLQHLEEERRAALARSEEI 2602
Cdd:pfam12128 784 IERIAVRRQEVLRYFDWYQEtwlqRRPRLATQLSNIERAISELQQQLarliadtKLRRAKLEMERKASEKQQVRL 858
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2153-2601 |
6.94e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2153 EMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEE------ELFSLRVQMEE 2226
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiklseFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2227 LGKLKARIEAENRAL--VLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralAEKMLKEKmq 2304
Cdd:PRK03918 312 IEKRLSRLEEEINGIeeRIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--------LERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2305 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQ-----RQLEMSAEAERLRLRVAEM 2379
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2380 SRAQ---ARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKL-KQEAQL 2455
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2456 LQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRER-----CIEQEKAKLEQL--FQDEVAKAQALREEQQRQQQQM 2528
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELepFYNEYLELKDAEKELEREEKEL 621
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237970 2529 QQEKQQLAASMEEARRRQHEAEEgVRRQQEELQRlaqqqqqqeKLLAEENQRLRERLQHLEEERRAALARSEE 2601
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEE-LRKELEELEK---------KYSEEEYEELREEYLELSRELAGLRAELEE 684
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
166-261 |
7.10e-08 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 54.23 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 166 KLLL-WSQrMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNL-----------------------EN 221
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 222 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 261
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1399-1939 |
7.19e-08 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 58.89 E-value: 7.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1399 QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEeirvVRLQLE--ATERQRGGAEGELQALRARaeeaEAQK 1476
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEE----LKLNLEraQTEEAQAKQDSELAKLRVE----EMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1477 RQAQEEAERLRRQVQDETQRKRQAEAELALrVQAE--------AEAAREKQRALQALEELRLQAEEAERRLRQAEAERAr 1548
Cdd:pfam05701 113 GIADEASVAAKAQLEVAKARHAAAVAELKS-VKEEleslrkeyASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1549 QVQVALETAQRS-AEAELQSEHASFA--EKTAQLERTLKEEHVAVVQLREEATRRAQQQAeaeraraeaerelerwQLKA 1625
Cdd:pfam05701 191 ATKESLESAHAAhLEAEEHRIGAALAreQDKLNWEKELKQAEEELQRLNQQLLSAKDLKS----------------KLET 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1626 NEALRLRLQAEEVAQQKSltqaeaekqkeEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEgtaqqRLAAEQEL 1702
Cdd:pfam05701 255 ASALLLDLKAELAAYMES-----------KLKEEADGEGNEKKTSTSIQAalaSAKKELEEVKANIE-----KAKDEVNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1703 IRLRAETEQGEQQRQllEEELARLQREAAAATQKRRELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAeagr 1782
Cdd:pfam05701 319 LRVAAASLRSELEKE--KAELASLRQREGMASIAVSSLEAELNRTKSEIALV---QAKEKEAREKMVELPKQLQQA---- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1783 frelAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEA--ENERLRRLAEDE 1860
Cdd:pfam05701 390 ----AQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlqESESSAESTNQE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1861 AFQR----------------RLLEEQAaqhKADIEARLAQLRKASESELERQKGLvEDTLRQRRQVEEEILALKGSFEKA 1924
Cdd:pfam05701 466 DSPRgvtlsleeyyelskraHEAEELA---NKRVAEAVSQIEEAKESELRSLEKL-EEVNREMEERKEALKIALEKAEKA 541
|
570
....*....|....*
gi 1920237970 1925 AAGKAELELELGRIR 1939
Cdd:pfam05701 542 KEGKLAAEQELRKWR 556
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1640-1835 |
8.21e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.89 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1640 QQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1719
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1720 EEELARLQREAAAATQKRRELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1799
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 1920237970 1800 AKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRL 1835
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2194-2462 |
8.99e-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: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2194 EELQRLKAEVTEAARQRGQVE------EELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEkmkQVAEEA 2267
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA---RLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2268 ARLSVAAQEAARLRQLAEEDLAQQralaekmlkekmqAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQE 2347
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGN-------------GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2348 TQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQaedigerlyrtelatqekvmlVQTLETQRQQ 2427
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE---------------------IASLERRKSN 437
|
250 260 270
....*....|....*....|....*....|....*.
gi 1920237970 2428 SDRDAERLREAIAE-LEHEKDKLKQEAQLLQLKSEE 2462
Cdd:COG4913 438 IPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1387-1552 |
1.04e-07 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 58.61 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1387 EVARR----EEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegel 1462
Cdd:COG1193 490 EIARRlglpEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEK------- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1463 QALRARA-EEAEAQKRQAQEEAERLRRQVQDEtqrkrqaeaelalrvQAEAEAAREKQRALQALEElRLQAEEAERRLRQ 1541
Cdd:COG1193 563 EEILEKArEEAEEILREARKEAEELIRELREA---------------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKA 626
|
170
....*....|.
gi 1920237970 1542 AEAERARQVQV 1552
Cdd:COG1193 627 KPAKPPEELKV 637
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1418-1570 |
1.13e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 57.58 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1418 AEIQAKARQVEA-AERsrlriEEEIRVvrlqleaTERQRGGAEGELQALRARAE----EAEAQKRQAQEEAERlrrqvqd 1492
Cdd:COG2268 195 AEIIRDARIAEAeAER-----ETEIAI-------AQANREAEEAELEQEREIETariaEAEAELAKKKAEERR------- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1493 ETQRKRqAEAELALRVQaEAEAAREKQRALQALE---ELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEH 1569
Cdd:COG2268 256 EAETAR-AEAEAAYEIA-EANAEREVQRQLEIAErerEIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIR 333
|
.
gi 1920237970 1570 A 1570
Cdd:COG2268 334 A 334
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4027-4063 |
1.16e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.56 E-value: 1.16e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1920237970 4027 IRLLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEM 4063
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
37-143 |
1.29e-07 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 52.72 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 37 KTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLpreRDVirsSRLPREKGRMrfhkLQNVQIALDYLR 114
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKV---EDI---NGCPRSQSQM----IENVDVCLSFLA 72
|
90 100
....*....|....*....|....*....
gi 1920237970 115 HRQVKLVNIRNDDIADGNPKLTLGLIWTI 143
Cdd:cd21286 73 ARGVNVQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1467-1918 |
1.42e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1467 ARAEEAEAQKRQAQEEAERLRRQVQD-ETQRKRQAEAELAL----RVQAEAEAAREKQRALQALEELRLQAEEAERRLRQ 1541
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELeelrEELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1542 AEAERARQVQV-----ALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEaer 1616
Cdd:COG4717 151 LEERLEELRELeeeleELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE--- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1617 elerwQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAvrqrELAEQELEKQRQLAEGTAQQRL 1696
Cdd:COG4717 228 -----ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA----GVLFLVLGLLALLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1697 AAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRstsEKSKQRL 1776
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL---EQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1777 EAEAGrfrelAEEAARLRALAEEAKRQRQLAEEdavrqRAEAERVLAEKLAAISEATRLKTEAEiaLKEKEAENERLRRL 1856
Cdd:COG4717 376 LAEAG-----VEDEEELRAALEQAEEYQELKEE-----LEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEE 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 1857 AEDEafqrrllEEQAAQHKADIEARLAQLrkASESELERQKGLVEDTLRQRRQVEEEILALK 1918
Cdd:COG4717 444 LEEE-------LEELREELAELEAELEQL--EEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1053-1501 |
1.79e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1053 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKA-------ALKKLRAQ 1125
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAelaelpeRLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1126 AEAQQPVFDALRDELRGAQEVGERLQQrhgERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADP 1205
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1206 LGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKVeecqrfakQYINAIKDYELQLVTYKAQLEPVAS 1285
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV--------LFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1286 PAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRfiseTLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA 1365
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELL----ELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1366 HAQAKAQAEREAQGLQRRmQEEVARREEVAVEAQEQKRSIQEELQHLRQSS-EAEIQAKARQVEAAERSRLRIEEEIRVV 1444
Cdd:COG4717 380 GVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAEL 458
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237970 1445 RLQLEATERqrggaEGELQALRARAEEAEAQKRQAQEEAERLR------RQVQDETQRKRQAE 1501
Cdd:COG4717 459 EAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPP 516
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1326-1586 |
1.89e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 56.47 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1326 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSI 1405
Cdd:pfam13868 46 DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1406 QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1485
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1486 LR-RQVQDETQRK-RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEA 1563
Cdd:pfam13868 206 LRaKLYQEEQERKeRQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRR 285
|
250 260
....*....|....*....|...
gi 1920237970 1564 ELQSEHASFAEKTAQLERTLKEE 1586
Cdd:pfam13868 286 MKRLEHRRELEKQIEEREEQRAA 308
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1034-1596 |
2.13e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1034 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLKEaqaVPATLPELE 1113
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1114 ATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLqqrhgerdvevERWRERvtllLERWQAVLAQTDVRQRELEQLG 1193
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL-----------SRLEEE----INGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1194 RQLRYYRESADPLGAWLR---DAKQRQEQIqavplansqavrEQLRQEKALL--EDIERHGEKVEECQRFAKQYINAIKD 1268
Cdd:PRK03918 345 KKLKELEKRLEELEERHElyeEAKAKKEEL------------ERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1269 YELQLVTYKAQLEPVASPAKKPKVQS---GSESIIQEYVDLRTRYSElstltsqYIRFISETLRRMEEEERlaeqqraEE 1345
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGKCpvcGRELTEEHRKELLEEYTA-------ELKRIEKELKEIEEKER-------KL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1346 RERLAEVEAALEKQRQLAEAHAQAKaqaereaqglQRRMQEEvaRREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKAR 1425
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELAE----------QLKELEE--KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1426 QVEAAERsrlrIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1505
Cdd:PRK03918 547 ELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1506 lRVQAEAEAAREK-QRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERtLK 1584
Cdd:PRK03918 623 -KLEEELDKAFEElAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK-LK 700
|
570
....*....|..
gi 1920237970 1585 EEHVAVVQLREE 1596
Cdd:PRK03918 701 EELEEREKAKKE 712
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1334-1961 |
2.48e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 57.50 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1334 EERLAEQQRAeeRERLAEVEAALEK-QRQLA------------------EAHAQAKAQAEREAQGLQRRMQEEVARREEV 1394
Cdd:PRK10246 253 DELQQEASRR--QQALQQALAAEEKaQPQLAalslaqparqlrphweriQEQSAALAHTRQQIEEVNTRLQSTMALRARI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1395 AVEAQEQKRSIQEELQHLRQ-SSEAEIQAKARQVEAAERSRL----RIEEEIRVVRLQLEATERQRGGAEGELQALRARa 1469
Cdd:PRK10246 331 RHHAAKQSAELQAQQQSLNTwLAEHDRFRQWNNELAGWRAQFsqqtSDREQLRQWQQQLTHAEQKLNALPAITLTLTAD- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1470 EEAEAQKRQAQEEAER-----LRRQVQDETQRKRQAEAelalrvqAEAEAAREKQRALQALEELRLQAEEAERRLRQAEA 1544
Cdd:PRK10246 410 EVAAALAQHAEQRPLRqrlvaLHGQIVPQQKRLAQLQV-------AIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKT 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1545 ERARQVQVALETAQRsaeAELQS----------EHASFAEKTAqLERTlkeehvaVVQLREEATRRAQQQAeaeraraea 1614
Cdd:PRK10246 483 ICEQEARIKDLEAQR---AQLQAgqpcplcgstSHPAVEAYQA-LEPG-------VNQSRLDALEKEVKKL--------- 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1615 erelerwqlkANEALRLRLQAEEVAQQKSltqaeaekqkeeaerearrrgKAEEQAVRQRElAEQELEKQRQLAEGTAQQ 1694
Cdd:PRK10246 543 ----------GEEGAALRGQLDALTKQLQ---------------------RDESEAQSLRQ-EEQALTQQWQAVCASLNI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1695 RLAAEQELIRLRAETEQGEQQRQLLEEELArLQREAAAATQKRRELEAELAKVRAEMEVLLASKA------RAEEESRST 1768
Cdd:PRK10246 591 TLQPQDDIQPWLDAQEEHERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWLAT 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1769 SEKSKQRLEAEAGRFRELAEEAARLRALAEeakrqrQLAEEDAVrqRAEAERVLAEKLAAISEATrLKTEAEIALKEKEA 1848
Cdd:PRK10246 670 RQQEAQSWQQRQNELTALQNRIQQLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQQD 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1849 ENERLR---------------RLAEDEAFQRRLLEEQAAQhkadieaRLAQLRKASESELERQKGLVEdtlrQRRQVEEE 1913
Cdd:PRK10246 741 VLEAQRlqkaqaqfdtalqasVFDDQQAFLAALLDEETLT-------QLEQLKQNLENQRQQAQTLVT----QTAQALAQ 809
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1920237970 1914 ILALKGSFEKAAAGKAELELELGRIRGT-AEDTLRSKE---QAEQEA-ARQRQ 1961
Cdd:PRK10246 810 HQQHRPDGLDLTVTVEQIQQELAQLAQQlRENTTRQGEirqQLKQDAdNRQQQ 862
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1698-1898 |
2.58e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1698 AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1777
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1778 A---------------EAGRFRELAEEAARLRALAEEAKR---QRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEA 1839
Cdd:COG3883 94 AlyrsggsvsyldvllGSESFSDFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 1840 EIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKG 1898
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1319-1580 |
2.83e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.88 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1319 QYIRFISETLRRMEEEERLAEQ--QRAEER-ERLAEVEAA-LEKQRQLAEAHAQAKAQA---------EREAQGLQRRMQ 1385
Cdd:PRK05035 429 QYYRQAKAEIRAIEQEKKKAEEakARFEARqARLEREKAArEARHKKAAEARAAKDKDAvaaalarvkAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1386 EEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAA-ERSRLRIEEeirvvrlQLEATERQRGGAEGELQA 1464
Cdd:PRK05035 509 KAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAiARAKAKKAA-------QQAANAEAEEEVDPKKAA 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1465 LRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAelalrvqaeAEAAREKQRALQALEELRLQAEEAERRLRQAEA 1544
Cdd:PRK05035 582 VAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAA---------AIARAKAKKAEQQANAEPEEPVDPRKAAVAAAI 652
|
250 260 270
....*....|....*....|....*....|....*.
gi 1920237970 1545 ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLE 1580
Cdd:PRK05035 653 ARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAK 688
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1430-1550 |
2.90e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 55.82 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1430 AERSRLRIEEEIRVVRLQLEATERQRGgAEGELQALRARAEEAEAQKRQAQEEAERLR---------RQVQDETQRKR-Q 1499
Cdd:COG1566 81 LQAALAQAEAQLAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQalykkgavsQQELDEARAALdA 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1920237970 1500 AEAELAlRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV 1550
Cdd:COG1566 160 AQAQLE-AAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1677-1929 |
3.02e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1677 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLA 1756
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1757 SKARAEE---------ESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEK 1825
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1826 LAAISEATRLKteAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLR 1905
Cdd:COG3883 174 EAQQAEQEALL--AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
250 260
....*....|....*....|....
gi 1920237970 1906 QRRQVEEEILALKGSFEKAAAGKA 1929
Cdd:COG3883 252 AGAAGAAAGSAGAAGAAAGAAGAG 275
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1684-1884 |
3.84e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 56.03 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1684 QRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRqllEEELARLQREAAAATQKRRELEAELAKVraemevllaskaraEE 1763
Cdd:COG2268 191 RRKIAEIIRDARIAEAE--AERETEIAIAQANR---EAEEAELEQEREIETARIAEAEAELAKK--------------KA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1764 ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEA-----ERVLAEKLAAISEAtrlKTE 1838
Cdd:COG2268 252 EERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELeadvrKPAEAEKQAAEAEA---EAE 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1920237970 1839 AEIALKEKEAENERLRRLAE-DEAFQRRLLEEQAAQHKADIEARLAQ 1884
Cdd:COG2268 329 AEAIRAKGLAEAEGKRALAEaWNKLGDAAILLMLIEKLPEIAEAAAK 375
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2262-2715 |
4.62e-07 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 56.13 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2262 QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMA 2341
Cdd:COG4995 9 LLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2342 QQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTL 2421
Cdd:COG4995 89 LLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2422 ETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKA 2501
Cdd:COG4995 169 ALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2502 KLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRL 2581
Cdd:COG4995 249 ALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2582 RERLQHLEEERRAALARSEEIAPSRAAAARALPNGQDAADGPAAAAEPEHAFDGLRRKVPAQRLQEVGVLSAEELQQLAQ 2661
Cdd:COG4995 329 ALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQL 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 2662 GRTTVAELAQREDVRHYLQGRSSIAGLL-LKPADEKLTIYAALRRQLLSPGTALI 2715
Cdd:COG4995 409 LRLLLAALALLLALAAYAAARLALLALIeYIILPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1713-1897 |
5.14e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.58 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1713 EQQRQLLEEELAR-LQREAAAATQKRRELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEAGrfrelAEEAA 1791
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAK-----AAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1792 RLRALAEeakrqrQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRrllEEQA 1871
Cdd:PRK09510 146 KAKAEAE------AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK--AEAEAKKK---AAAE 214
|
170 180
....*....|....*....|....*.
gi 1920237970 1872 AQHKADIEARLAQLRKASESELERQK 1897
Cdd:PRK09510 215 AKKKAAAEAKAAAAKAAAEAKAAAEK 240
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2150-2350 |
5.61e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2150 ADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEE--- 2226
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2227 --------LGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM 2298
Cdd:COG3883 94 alyrsggsVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 2299 LKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQG 2350
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1665-1882 |
5.92e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.85 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1665 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRreleAEL 1744
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKA----KEE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1745 AKVRAEMEvllaSKARAEEESRSTSEKSKQRLEAEAgrfreLAEEAARLRALAEEAKRQRQLAEEDA---VRQRAEAERV 1821
Cdd:TIGR02794 148 AAKQAEEE----AKAKAAAEAKKKAEEAKKKAEAEA-----KAKAEAEAKAKAEEAKAKAEAAKAKAaaeAAAKAEAEAA 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 1822 LAEKLAAISEATRLKTEAEIAL-KEKEAENERLRRLAEDEAFQRRLleeqAAQHKADIEARL 1882
Cdd:TIGR02794 219 AAAAAEAERKADEAELGDIFGLaSGSNAEKQGGARGAAAGSEVDKY----AAIIQQAIQQNL 276
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2157-2460 |
6.39e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2157 HKQFAEQALRQKAQVEQ---ELTALRLQLEETDHQKSILDEELQRLKAEVTEAarqrgqvEEELFSLRVQME-------- 2225
Cdd:PRK04863 336 HLNLVQTALRQQEKIERyqaDLEELEERLEEQNEVVEEADEQQEENEARAEAA-------EEEVDELKSQLAdyqqaldv 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2226 ---------------------------ELGKLKARIEAenraLVLRDKDSAQRLLQEE-----AEKMKQVAEEAARL--- 2270
Cdd:PRK04863 409 qqtraiqyqqavqalerakqlcglpdlTADNAEDWLEE----FQAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrk 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2271 ---SVAAQEAARLRQLAEEDLAQQRALAEKM---------LKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKE 2338
Cdd:PRK04863 485 iagEVSRSEAWDVARELLRRLREQRHLAEQLqqlrmrlseLEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELE 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2339 QMAQQLAQEtqgfqktLETERQRQLEMSAEAERLRLRVAE-MSRAQA--RAEEDARRFRKQAEDigerlyrtELATQEKV 2415
Cdd:PRK04863 565 ARLESLSES-------VSEARERRMALRQQLEQLQARIQRlAARAPAwlAAQDALARLREQSGE--------EFEDSQDV 629
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 2416 M--LVQTLETQRQQSdRDAERLREAIAELEHEKDKLKQ-----EAQLLQLKS 2460
Cdd:PRK04863 630 TeyMQQLLERERELT-VERDELAARKQALDEEIERLSQpggseDPRLNALAE 680
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1737-2443 |
6.51e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1737 RRELEAELAKVRAEMEVLLASKARAEEESRStsEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRA 1816
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQ--IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1817 EAERvlaeklaaiSEATRLKTEAEIALKEKEAENERLRRLaedeafqrrllEEQAAQHKADIEARLAQLRKASESELERQ 1896
Cdd:COG4913 298 EELR---------AELARLEAELERLEARLDALREELDEL-----------EAQIRGNGGDRLEQLEREIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1897 KGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQlaaeeerrrreaeer 1976
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR--------------- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1977 vqkSLAAEEEAARQRKAAL-EEVERLKAKVEEARRLRE------------RAEQES-------------------ARQLQ 2024
Cdd:COG4913 423 ---ELEAEIASLERRKSNIpARLLALRDALAEALGLDEaelpfvgelievRPEEERwrgaiervlggfaltllvpPEHYA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2025 LAQEAAQkRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAAREraereaaqSRRQVEEAERL 2104
Cdd:COG4913 500 AALRWVN-RLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAELGRRF--------DYVCVDSPEEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2105 KQSAEEQAQAQaqaqaaaekLRKeaeqeaarraqaEQAALRQKQAADAEMEKHkQFAEQALRQKAQVEQELTALRLQLEE 2184
Cdd:COG4913 571 RRHPRAITRAG---------QVK------------GNGTRHEKDDRRRIRSRY-VLGFDNRAKLAALEAELAELEEELAE 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2185 TDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQmEELGKLKARIEAenralvLRDKDSAQRLLQEEAEKMKQVA 2264
Cdd:COG4913 629 AEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-REIAELEAELER------LDASSDDLAALEEQLEELEAEL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2265 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ-QKELAQEQARRLQEDKEQMAQQ 2343
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAlGDAVERELRENLEERIDALRAR 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2344 LAQETQGFQKTleterqrqleMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERL------YRTELATQEKVML 2417
Cdd:COG4913 782 LNRAEEELERA----------MRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYeerfkeLLNENSIEFVADL 851
|
730 740
....*....|....*....|....*.
gi 1920237970 2418 VQTLETQRQQSDRDAERLREAIAELE 2443
Cdd:COG4913 852 LSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1464-1862 |
6.96e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.11 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1464 ALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAeaelalrvqaeAEAAREKQRALQAL---------EELRLQAEE 1534
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQ-----------LDQLKEQLQLLNKLlpqanlladETLADRLEE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1535 AERRLRQAEAERA--RQVQVALETAQRSAEAeLQSEHASFAEktaqlertLKEEHVAVVQLREEATRRAQQQAEAERARA 1612
Cdd:COG3096 898 LREELDAAQEAQAfiQQHGKALAQLEPLVAV-LQSDPEQFEQ--------LQADYLQAKEQQRRLKQQIFALSEVVQRRP 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1613 EAERELERWQLKANEALRLRLQAeevaqqksltqaeaekqkeeaerearrrgkaeeqavrQRELAEQELEKQRQLAEGTA 1692
Cdd:COG3096 969 HFSYEDAVGLLGENSDLNEKLRA-------------------------------------RLEQAEEARREAREQLRQAQ 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1693 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREA-----AAATQKRRELEAELAKVRAEmevllaskaraeeesRS 1767
Cdd:COG3096 1012 AQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQAdaeaeERARIRRDELHEELSQNRSR---------------RS 1076
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1768 TSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAK----RQRQLAEEDAVRQRAEAERVL---AEKLAAISEatrlk 1836
Cdd:COG3096 1077 QLEKQLTRCEAEmdslQKRLRKAERDYKQEREQVVQAKagwcAVLRLARDNDVERRLHRRELAylsADELRSMSD----- 1151
|
410 420
....*....|....*....|....*....
gi 1920237970 1837 tEAEIALKEKEAENERLR---RLAEDEAF 1862
Cdd:COG3096 1152 -KALGALRLAVADNEHLRdalRLSEDPRR 1179
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1469-1586 |
7.40e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 55.26 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1469 AEEAEAQKRQAQEEAErLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRAlQALEELRLQAEEAERRLRQAEAERAR 1548
Cdd:COG2268 212 TEIAIAQANREAEEAE-LEQEREIETARIAEAEAELA-KKKAEERREAETARA-EAEAAYEIAEANAEREVQRQLEIAER 288
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237970 1549 QVQVALETAQR-SAEAELQSEHASFAEktAQLERTLKEE 1586
Cdd:COG2268 289 EREIELQEKEAeREEAELEADVRKPAE--AEKQAAEAEA 325
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
21-155 |
7.59e-07 |
|
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: 51.60 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 21 EEVREKYKDErdrvQKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRL 91
Cdd:cd21325 15 EGTQHSYSEE----EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTID-ERAINKKKLT 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 92 PrekgrmrFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 155
Cdd:cd21325 90 P-------FIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2145-2586 |
8.07e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.57 E-value: 8.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2145 RQKQAADAEMEKHKQFAEQALRqkaqvEQELTALRLQLEE--TDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRV 2222
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLD-----EEEAARQKLQLEKvtTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2223 QMEE-------LGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMK----------QVAEEAARLS-VAAQEAARLRQLA 2284
Cdd:pfam01576 167 NLAEeeekaksLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKlegestdlqeQIAELQAQIAeLRAQLAKKEEELQ 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2285 E-----EDLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL--AQETQGFQKTLET 2357
Cdd:pfam01576 247 AalarlEEETAQKNNALKKIRELEAQISE---LQEDLESERAARNKAEKQRRDLGEELEALKTELedTLDTTAAQQELRS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2358 ERQRQLEMSAEAERLRLRVAEMSRAQARaeedaRRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLRE 2437
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMR-----QKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2438 AIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQL-------------------------------------LQETQALQQ 2480
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAeklsklqselesvssllneaegkniklskdvsslesqLQDTQELLQ 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2481 SFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQekqqLAASMEEARRRQHEAEEGVRRQQEEL 2560
Cdd:pfam01576 479 EETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSD----MKKKLEEDAGTLEALEEGKKRLQREL 554
|
490 500 510
....*....|....*....|....*....|
gi 1920237970 2561 ----QRLAQQQQQQEKLlaeenQRLRERLQ 2586
Cdd:pfam01576 555 ealtQQLEEKAAAYDKL-----EKTKNRLQ 579
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
21-154 |
8.23e-07 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 51.58 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 21 EEVREKYKDErdrvQKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRL 91
Cdd:cd21323 15 EGTQHSYSEE----EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTID-ERAINKKKLT 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237970 92 PrekgrmrFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 154
Cdd:cd21323 90 P-------FTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2790-2826 |
8.72e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 8.72e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1920237970 2790 IRLLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEM 2826
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2248-2464 |
9.99e-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: 9.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2248 SAQRLLQEEAEKMKQVAEEAARLSVAAQEAARlrqlAEEDLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQ 2327
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKK----EEKALLKQLAALERRIAALARRIRA---LEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2328 EQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRT 2407
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237970 2408 ELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQ 2464
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1089-1751 |
1.09e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.18 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1089 EEVLRAHEEQLKE-----AQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVER 1163
Cdd:pfam01576 337 EEETRSHEAQLQEmrqkhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1164 WRERVT-------LLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAK-QRQEQIQAvPLANSQAVReQL 1235
Cdd:pfam01576 417 LQARLSeserqraELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQeLLQEETRQ-KLNLSTRLR-QL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1236 RQEKALLEdiERHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAK-----KPKVQSGSESIIQEYVDLRTRY 1310
Cdd:pfam01576 495 EDERNSLQ--EQLEEEEEAKRNVERQ----LSTLQAQLSDMKKKLEEDAGTLEaleegKKRLQRELEALTQQLEEKAAAY 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1311 SELS-------------TLTSQYIRFISETLRR-------MEEEERLAEQQRAEERERlAEVEAALEKQRQLAEAHA--- 1367
Cdd:pfam01576 569 DKLEktknrlqqelddlLVDLDHQRQLVSNLEKkqkkfdqMLAEEKAISARYAEERDR-AEAEAREKETRALSLARAlee 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1368 --QAKAQAEREAQGLQRRMQEEVARREEV------------AVEAQEQKRSIQEE-------------------LQHLRQ 1414
Cdd:pfam01576 648 alEAKEELERTNKQLRAEMEDLVSSKDDVgknvhelerskrALEQQVEEMKTQLEeledelqatedaklrlevnMQALKA 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1415 SSEAEIQAKArqvEAAERSRLRIEEEIRVVRLQLEATERQRGGA-------EGELQALRARAEEAEAQKRQAQEEAERLR 1487
Cdd:pfam01576 728 QFERDLQARD---EQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQLKKLQ 804
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1488 RQVQDetqrkRQAEAELALRVQAEAEA-AREKQRALQALEELRLQAEE----AERRLRQAEAERAR-QVQVALETAQRSA 1561
Cdd:pfam01576 805 AQMKD-----LQRELEEARASRDEILAqSKESEKKLKNLEAELLQLQEdlaaSERARRQAQQERDElADEIASGASGKSA 879
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1562 eaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAE-----AERARAEAERELERWQL-KANEALRLRLQA 1635
Cdd:pfam01576 880 ---LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQlttelAAERSTSQKSESARQQLeRQNKELKAKLQE 956
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1636 EEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQA-----VRQRELAEQEL----EKQRQLAEGTAQQRLAAEQELIRLR 1706
Cdd:pfam01576 957 MEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQaanklVRRTEKKLKEVllqvEDERRHADQYKDQAEKGNSRMKQLK 1036
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1920237970 1707 AETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEM 1751
Cdd:pfam01576 1037 RQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2243-2680 |
1.12e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.36 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2243 LRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ 2322
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2323 KELAQEQARRLQEDKEQMA--QQLAQETQGFQKTLETERQRqLEMSAEAERLRLRVAEMSRAQARAEEdarrFRKQAEDI 2400
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAV-LEETQERINRARKAAPLAAHIKAVTQ----IEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2401 GERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKS---EEMQTVRQEQLLQETQA 2477
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCqqhTLTQHIHTLQQQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2478 LQQSFLSEKDSLLQRErciEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQ 2557
Cdd:TIGR00618 393 QKLQSLCKELDILQRE---QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2558 EELQRLAQQQQQQEKlLAEENQRLRERLQHLEEERRAALARSEEIAPSRAAAARALPNGQDAADGPAAAAEPEHAFDGLR 2637
Cdd:TIGR00618 470 EREQQLQTKEQIHLQ-ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1920237970 2638 RKVPA-----QRLQEVGVLSAEELQQLAQGRTTVAELAQR-----EDVRHYLQ 2680
Cdd:TIGR00618 549 HQLTSerkqrASLKEQMQEIQQSFSILTQCDNRSKEDIPNlqnitVRLQDLTE 601
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4130-4158 |
1.14e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 47.71 E-value: 1.14e-06
10 20
....*....|....*....|....*....
gi 1920237970 4130 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4158
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1861-2350 |
1.20e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1861 AFQRRLLEEQAAQHKADIEARLAQLRKASESELERQkglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRg 1940
Cdd:COG4717 41 AFIRAMLLERLEKEADELFKPQGRKPELNLKELKEL----EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1941 tAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2020
Cdd:COG4717 116 -EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2021 RQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVL-ERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVE 2099
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEaAALEERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2100 EAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQA------LRQKAQVEQ 2173
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELlelldrIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2174 ELTALRLQLEETDHQKSIlDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEEL-GKLKARIEAENRALVLRDKDSAQRL 2252
Cdd:COG4717 355 EAEELEEELQLEELEQEI-AALLAEAGVEDEEELRAALEQAEEYQELKEELEELeEQLEELLGELEELLEALDEEELEEE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2253 LQEEAEKMKQVAEEAARLSVAAQEA-ARLRQLAEEDLAQQRALAEKMLKEKMQ-AVQEATRLKAEAELLQQQKELAQEqa 2330
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELeAELEQLEEDGELAELLQELEELKAELReLAEEWAALKLALELLEEAREEYRE-- 511
|
490 500
....*....|....*....|
gi 1920237970 2331 RRLQEDKEQMAQQLAQETQG 2350
Cdd:COG4717 512 ERLPPVLERASEYFSRLTDG 531
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1466-1596 |
1.22e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 54.57 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1466 RARAEEAEAQ------KRQAQEEAerlRRQVQDETQRKRQAEAELALRVQAEAEAAREKQralQALEELRLQAEEAER-- 1537
Cdd:pfam15709 337 RLRAERAEMRrleverKRREQEEQ---RRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQEEEERkq 410
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 1538 -RLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ----LERTLKEEHVAVVQLREE 1596
Cdd:pfam15709 411 rLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQrqkeLEMQLAEEQKRLMEMAEE 474
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1665-2038 |
1.72e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.10 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1665 KAEEQAVRQRElaEQELEKQRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1744
Cdd:pfam02029 14 RAREERRRQKE--EEEPSGQVTESVEPNEHNSYEED--SELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1745 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRElAEEAARLRALAEEAKRQ--RQLAEEDAVRQRAEAERVL 1822
Cdd:pfam02029 90 DPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKE-EETEIREKEYQENKWSTevRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1823 AEKLAAISEatrlKTEAEIALKEKEAENERLRRLAedeafQRRLLEEQAAQhkadiearlaqlrkASESELERQKGLVED 1902
Cdd:pfam02029 169 VPTENFAKE----EVKDEKIKKEKKVKYESKVFLD-----QKRGHPEVKSQ--------------NGEEEVTKLKVTTKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1903 TLRQRRQVEEEilalkgsfEKAAAGKAELELELGRIRGTAEDtlrsKEQAEQEAARQRQLAAEEERRRREAEERVQKSLA 1982
Cdd:pfam02029 226 RQGGLSQSQER--------EEEAEVFLEAEQKLEELRRRRQE----KESEEFEKLRQKQQEAELELEELKKKREERRKLL 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 1983 AEEEaaRQRKAalEEVERLKAKVEEARRLRERAEQESArqlqlaqEAAQKRLQAEE 2038
Cdd:pfam02029 294 EEEE--QRRKQ--EEAERKLREEEEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1329-1592 |
1.75e-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: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1329 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVeaQEQKRSIQEE 1408
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM--DEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1409 LQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR 1488
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEK--EEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1489 QVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEA-ERARQVQVALETAQRSAEAELQS 1567
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELkERRLAEEAEREEEEFERMLRKQA 271
|
250 260
....*....|....*....|....*
gi 1920237970 1568 EHASFAEKTAQLERTLKEEHVAVVQ 1592
Cdd:pfam13868 272 EDEEIEQEEAEKRRMKRLEHRRELE 296
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1333-1517 |
2.07e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 53.66 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1333 EEERLAEQQRAEERERLAEveAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEvaveaqEQKRSIQEELQhl 1412
Cdd:PRK09510 107 EKERLAAQEQKKQAEEAAK--QAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAA------EAKKKAEAEAA-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1413 rQSSEAEIQAKARQVEAAersrlrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqvqd 1492
Cdd:PRK09510 177 -KKAAAEAKKKAEAEAAA----------------KAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA--------- 230
|
170 180
....*....|....*....|....*
gi 1920237970 1493 ETQRKRQAEAELALRVQAEAEAARE 1517
Cdd:PRK09510 231 AAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3449-3485 |
2.09e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 2.09e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1920237970 3449 IRLLEAQIATGGIIDPVHSHRVPVDVAYQRGYFDEEM 3485
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1387-2014 |
2.24e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1387 EVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQ----------LEATERQRG 1456
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEvkeleelkeeIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1457 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEaEAAREKQRALQALEELRLQAEEAE 1536
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE-EYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1537 RRLRQAEAERARQVQValetaqRSAEAELQSEHASFaEKTAQLERTLKEEHVAVVQLREEatrraqqqaeaeraraeaer 1616
Cdd:PRK03918 328 ERIKELEEKEERLEEL------KKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKR-------------------- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1617 elerwqLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREarrrgkaeEQAVRQRELAEQELEKqrqlAEGTAQ--Q 1694
Cdd:PRK03918 381 ------LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL--------KKEIKELKKAIEELKK----AKGKCPvcG 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1695 RLAAEQELIRLRAEteqgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVraEMEVLLASKARAE----EESRSTSE 1770
Cdd:PRK03918 443 RELTEEHRKELLEE----------YTAELKRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLkelaEQLKELEE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1771 KSK----QRLEAEAGRFRELAEEAARLRalaeeaKRQRQLAEEdaVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEK 1846
Cdd:PRK03918 511 KLKkynlEELEKKAEEYEKLKEKLIKLK------GEIKSLKKE--LEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1847 --EAENERLRRLAEDEAFQRRLLEEQAAQHkaDIEARLAQLRKAsESELERQKGLVEDTLRQRRQVEEEILALKGSF--- 1921
Cdd:PRK03918 583 gfESVEELEERLKELEPFYNEYLELKDAEK--ELEREEKELKKL-EEELDKAFEELAETEKRLEELRKELEELEKKYsee 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1922 --EKAAAGKAELELELGRIRGTAEDTLRSKEQAEqeaarqrqlaaeeerrrreaeervqKSLAAEEEAARQRKAALEEVE 1999
Cdd:PRK03918 660 eyEELREEYLELSRELAGLRAELEELEKRREEIK-------------------------KTLEKLKEELEEREKAKKELE 714
|
650
....*....|....*
gi 1920237970 2000 RLKAKVEEARRLRER 2014
Cdd:PRK03918 715 KLEKALERVEELREK 729
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2154-2378 |
2.25e-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: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2154 MEKHKQFAEQALR----QKAQVEQELTALRLQLEE--TDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEEL 2227
Cdd:COG3206 166 LELRREEARKALEfleeQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2228 GKLKARIEAENRALVlrDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEkmqAVQ 2307
Cdd:COG3206 246 RAQLGSGPDALPELL--QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS---LEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237970 2308 EATRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLAQETQGFQKTLET--ERQRQLEMSAEAERLRLRVAE 2378
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPE-LEAELRRLEREVEVARELYESllQRLEEARLAEALTVGNVRVID 392
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2315-2601 |
2.36e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.97 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2315 EAELLQQQKELAQEQA----RRLQEDKEQMAQQ-LAQETQgfQKTLETERQRQLEMS-----AEAERLRLRVAEMSRAQA 2384
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKavseRQQQEKFEKMEQErLRQEKE--EKAREVERRRKLEEAekarqAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2385 RAEEDARRFRKQAEDI-GERLYRTELATQ-EKVMLVQTLETQRQQSDrdaERLREAIAELEHEKDKLKQEAQLLQLKSEE 2462
Cdd:pfam17380 345 ERERELERIRQEERKReLERIRQEEIAMEiSRMRELERLQMERQQKN---ERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2463 MQTVRQEQLLQETQALQQsflsekdslLQRERCIEQEKAKLEQLfqdevakaqalreeqqRqqqqMQQEKQQLAASMEEA 2542
Cdd:pfam17380 422 MEQIRAEQEEARQREVRR---------LEEERAREMERVRLEEQ----------------E----RQQQVERLRQQEEER 472
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 2543 RRRQHEAEEGVRRQQ--EELQRLAQQQQQQEKLLAE-ENQRLRERLQHLEEERRAALARSEE 2601
Cdd:pfam17380 473 KRKKLELEKEKRDRKraEEQRRKILEKELEERKQAMiEEERKRKLLEKEMEERQKAIYEEER 534
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2242-2595 |
2.58e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2242 VLRDKDSAQRLLQEEAEKmKQVAEEAARLSVAAQEAARLRQLAE------EDLAQQRALAEKMLKEKMQAVQEATRLKAE 2315
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEE-KEEKDLHERLNGLESELAELDEEIEryeeqrEQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2316 AELLQQQKELAQ---EQARRLQEDKEQMAQQLAQETQGFQKTLETER-------QRQLEMSAEAERLRLRVAEMSRAQAR 2385
Cdd:PRK02224 260 IEDLRETIAETErerEELAEEVRDLRERLEELEEERDDLLAEAGLDDadaeaveARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2386 AEEDARRFRKQAEDIGERlyrtelaTQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQT 2465
Cdd:PRK02224 340 HNEEAESLREDADDLEER-------AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2466 VRQEqllqetqalqqsFLSEKDSLLQRERCIEqekAKLEQLfQDEVAKAQALREE--------------QQRQQQQMQQE 2531
Cdd:PRK02224 413 FLEE------------LREERDELREREAELE---ATLRTA-RERVEEAEALLEAgkcpecgqpvegspHVETIEEDRER 476
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2532 KQQLAASMEEARRRQHEAEEGVRRQQE------ELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAA 2595
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1329-1590 |
2.62e-06 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 53.12 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1329 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVAR--REEVAVEAQEQKRSIQ 1406
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRAdrREKQVIEKESRWREQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1407 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqleaterqRGGAEGELQALRARAEEAEaQKRQAQEEAERL 1486
Cdd:pfam15558 101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL------------QALREQNSLQLQERLEEAC-HKRQLKEREEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1487 RRQVQDETQRKRQAEAELALRVQAEAEAAREK----QRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1562
Cdd:pfam15558 168 KVQENNLSELLNHQARKVLVDCQAKAEELLRRlsleQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEE 247
|
250 260
....*....|....*....|....*...
gi 1920237970 1563 AELQSEHASFAEKTAQLERTLKEEHVAV 1590
Cdd:pfam15558 248 ERQEHKEALAELADRKIQQARQVAHKTV 275
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1664-1884 |
2.71e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 53.42 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1664 GKAEEQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQ-ELIRLRAETEQGEQ--QRQLLEEELARlqreaaaATQKRREL 1740
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERaEMRRLEVERKRREQeeQRRLQQEQLER-------AEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1741 EAELAKVRAEMEvlLASKARAEEESRSTSEKSKQRLEaeagrfrelaEEAARLRALAEEAKRQRQLAEEDAVRQRAEAER 1820
Cdd:pfam15709 379 ELEQQRRFEEIR--LRKQRLEEERQRQEEEERKQRLQ----------LQAAQERARQQQEEFRRKLQELQRKKQQEEAER 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 1821 VLAEKLAAISEATRLKTEAEIALkeKEAENERLRRLAE-DEAFQRRLLEEQAAQHKADIEARLAQ 1884
Cdd:pfam15709 447 AEAEKQRQKELEMQLAEEQKRLM--EMAEEERLEYQRQkQEAEEKARLEAEERRQKEEEAARLAL 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1462-1736 |
2.92e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1462 LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRALQA--------LEELRLQAE 1533
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQelaaleaeLAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1534 EAERRLRQAEAERARQVQVALETAQRSAEAELQSehasfAEKTAQLERTLKEEHVAVVQLREEATRRAQqqaeaerarae 1613
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRA----------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1614 aerelerwQLKANEALRLRLQAEEVAQQKSLtqaeaekqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAEgtaq 1693
Cdd:COG4942 158 --------DLAELAALRAELEAERAELEALL----------------------AELEEERAALEALKAERQKLLAR---- 203
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1920237970 1694 qrlaAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQK 1736
Cdd:COG4942 204 ----LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2166-2597 |
3.28e-06 |
|
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: 53.60 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2166 RQKAQVEQELTALRLQLEETDHQ---KSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALV 2242
Cdd:pfam07111 190 KQLAEAQKEAELLRKQLSKTQEEleaQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2243 LRDKDSAQRLLQEEAEKMKQVAEEAarlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAE-AELLQQ 2321
Cdd:pfam07111 270 VRVQSLTHMLALQEEELTRKIQPSD---SLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQvAELQEQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2322 QKELAQEQA--RRLQEDKEQMAQQLAQETQGFQKTL----ETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRK 2395
Cdd:pfam07111 347 VTSQSQEQAilQRALQDKAAEVEVERMSAKGLQMELsraqEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2396 QAEDIGERLYRTELATQE----------KVMLVQTLETQRQQSDRDAERLREAIAELEH---EKDKLKQEAQL-LQLKSE 2461
Cdd:pfam07111 427 AVARIPSLSNRLSYAVRKvhtikglmarKVALAQLRQESCPPPPPAPPVDADLSLELEQlreERNRLDAELQLsAHLIQQ 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2462 EMQTVRQE-------------QLLQETQALQQSFLS---EKDSLLQRERCIEQEKAKLEQ-LFQDEVAKAQALREEQQRQ 2524
Cdd:pfam07111 507 EVGRAREQgeaerqqlsevaqQLEQELQRAQESLASvgqQLEVARQGQQESTEEAASLRQeLTQQQEIYGQALQEKVAEV 586
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237970 2525 QQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQ----EELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALA 2597
Cdd:pfam07111 587 ETRLREQLSDTKRRLNEARREQAKAVVSLRQIQhratQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNLMLA 663
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2251-2499 |
3.34e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 53.52 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2251 RLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ-EATRLKA---EAELLQQQKELA 2326
Cdd:PRK10929 123 RQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQaESAALKAlvdELELAQLSANNR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2327 QEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAE-AERLRLRVAEMSRAQARA----EEDARRFRKQAEDIG 2401
Cdd:PRK10929 203 QELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTELLAEQSGDLPKSIVAQfkinRELSQALNQQAQRMD 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2402 ERLYRTELATQEKVMLVQTLETQRQQ------SDRDAERLREAIAELEhEKDKLKQ----EAQLL--QLKSEEMQTvRQE 2469
Cdd:PRK10929 283 LIASQQRQAASQTLQVRQALNTLREQsqwlgvSNALGEALRAQVARLP-EMPKPQQldteMAQLRvqRLRYEDLLN-KQP 360
|
250 260 270
....*....|....*....|....*....|
gi 1920237970 2470 QLLQETQALQQSFLSEKDSLLQRERCIEQE 2499
Cdd:PRK10929 361 QLRQIRQADGQPLTAEQNRILDAQLRTQRE 390
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1359-1487 |
3.36e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 52.36 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1359 QRQLAEAHAQ-AKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKArQVEAAERSRLRI 1437
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQ-ELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1438 EEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLR 1487
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2193-2398 |
3.50e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2193 DEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVlRDKDSAQRLLQEEAEKMKQVAEEAARLSV 2272
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2273 AAQEAARLRQLAE--------EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2344
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 2345 AQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAE 2398
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1396-2231 |
3.67e-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: 53.51 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1396 VEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAersrLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQ 1475
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKA----CEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHN 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1476 KRQAQEEAERLRRQVQDETQRKRQaEAELALRVQAEAEAAREKqraLQALEELR-LQAEEAERRLRQAEAERARQVQVAL 1554
Cdd:TIGR00606 261 LSKIMKLDNEIKALKSRKKQMEKD-NSELELKMEKVFQGTDEQ---LNDLYHNHqRTVREKERELVDCQRELEKLNKERR 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1555 ETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRL--R 1632
Cdd:TIGR00606 337 LLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLcaD 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1633 LQAEEVAQQKSLTQAEAEKQKEEAEREArrrgKAEEQAVRQRELaeQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG 1712
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKGLGRTIEL----KKEILEKKQEEL--KFVIKELQQLEGSSDRILELDQELRKAERELSKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1713 EQQR--QLLEEELARLQREAAAATQKRRELEAELAKV------RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFR 1784
Cdd:TIGR00606 491 EKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFP 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1785 ELAEEAARLRALAEEAKRQRQ-LAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEI----ALKEKEAENERLRRLAED 1859
Cdd:TIGR00606 571 NKKQLEDWLHSKSKEINQTRDrLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcGSQDEESDLERLKEEIEK 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1860 EAFQRRLLEEQAAQHKADIEAR---------LAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKaaagkaE 1930
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQLtdenqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEK------R 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1931 LELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRR--EAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEA 2008
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNdiEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDV 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2009 RRLRERAEQESaRQLQLAQEAAQKRLQAEEKAHAF-AVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERA 2087
Cdd:TIGR00606 805 ERKIAQQAAKL-QGSDLDRTVQQVNQEKQEKQHELdTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2088 EREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKL----------RKEAEQEAARRAQAEQAALRQKQAADAEMEKH 2157
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDqqekeelissKETSNKKAQDKVNDIKEKVKNIHGYMKDIENK 963
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 2158 KQfaEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVtEAARQRGQVEEELFSLRVQMEELGKLK 2231
Cdd:TIGR00606 964 IQ--DGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDI-DTQKIQERWLQDNLTLRKRENELKEVE 1034
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1230-1962 |
3.72e-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: 53.57 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1230 AVREQLRQEKALLEDierhGEKVEECQRFAKQyinaikdyELQLVTYKAQLepvaspakkpKVQSGsesiIQEYVDLRTR 1309
Cdd:pfam05483 96 SIEAELKQKENKLQE----NRKIIEAQRKAIQ--------ELQFENEKVSL----------KLEEE----IQENKDLIKE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1310 yselSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAEREAQGLQRRMQEEva 1389
Cdd:pfam05483 150 ----NNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEK---MILAFEELRVQAENARLEMHFKLKED-- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1390 rreevaveaqeqkrsiQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1469
Cdd:pfam05483 221 ----------------HEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1470 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELR----LQAEEAERRLRQAEaE 1545
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKaahsFVVTEFEATTCSLE-E 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1546 RARQVQVALEtaqrSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATrraqqqaeaerarAEAERELERWQLKA 1625
Cdd:pfam05483 364 LLRTEQQRLE----KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKK-------------ILAEDEKLLDEKKQ 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1626 NEALRLRLQAEEvaQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQR-QLAEGTAQ--------QRL 1696
Cdd:pfam05483 427 FEKIAEELKGKE--QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTAHcdklllenKEL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1697 AAEQE--LIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA---ELAKVRAEMEVLL---ASKARAEEESRST 1768
Cdd:pfam05483 505 TQEASdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESvreEFIQKGDEVKCKLdksEENARSIEYEVLK 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1769 SEKSKQRLEAEAGRFRELAEEAAR-LRALAEEAKRQRQlaEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKE 1847
Cdd:pfam05483 585 KEKQMKILENKCNNLKKQIENKNKnIEELHQENKALKK--KGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1848 AENERL--RRLAEdEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRrqvEEEILALKGSFEKAA 1925
Cdd:pfam05483 663 IEDKKIseEKLLE-EVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER---DSELGLYKNKEQEQS 738
|
730 740 750
....*....|....*....|....*....|....*..
gi 1920237970 1926 AGKAELELELGRIRGtaeDTLRSKEQAEQEAARQRQL 1962
Cdd:pfam05483 739 SAKAALEIELSNIKA---ELLSLKKQLEIEKEEKEKL 772
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1875-2593 |
3.83e-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: 53.69 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1875 KADIEARLAQlRKASESELERQKGLVEDTLRQRrQVEEEILALKGSFEKAAAG-----KAELELELGRIRGTAEDTLRSK 1949
Cdd:pfam12128 199 KSMIVAILED-DGVVPPKSRLNRQQVEHWIRDI-QAIAGIMKIRPEFTKLQQEfntleSAELRLSHLHFGYKSDETLIAS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1950 EQAEQEA--ARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQ 2027
Cdd:pfam12128 277 RQEERQEtsAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSEL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2028 EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQS 2107
Cdd:pfam12128 357 ENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2108 AEEQAQaqaqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDh 2187
Cdd:pfam12128 437 EEEYRL----------KSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQAS- 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2188 qksildEELQRLKAEVTEAARQRGQVEEELFS--------LRVQM----EELGKLKARieaenrALVLR-------DKDS 2248
Cdd:pfam12128 506 ------EALRQASRRLEERQSALDELELQLFPqagtllhfLRKEApdweQSIGKVISP------ELLHRtdldpevWDGS 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2249 AQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2328
Cdd:pfam12128 574 VGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARL 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2329 QARRLQEDKEQMAQQLAQETQGFQKTLETERQrqlEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQA--EDIGERLYR 2406
Cdd:pfam12128 654 DLRRLFDEKQSEKDKKNKALAERKDSANERLN---SLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYwqVVEGALDAQ 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2407 TELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEqLLQETQALQQSFLSEK 2486
Cdd:pfam12128 731 LALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQE-VLRYFDWYQETWLQRR 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2487 DSLLQRERCIEQEKAKLEQlfqdevakaqalreEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQ 2566
Cdd:pfam12128 810 PRLATQLSNIERAISELQQ--------------QLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATL 875
|
730 740
....*....|....*....|....*..
gi 1920237970 2567 QQQQEKllAEENQRLRERLQHLEEERR 2593
Cdd:pfam12128 876 KEDANS--EQAQGSIGERLAQLEDLKL 900
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2249-2576 |
3.89e-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: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2249 AQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2328
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2329 QARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERlrlRVAEMSRAQARAEEDARRFRKQAEDIGERLYrte 2408
Cdd:pfam13868 113 EDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE---RILEYLKEKAEREEEREAEREEIEEEKEREI--- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2409 latqeKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEaqllqlksEEMQTVRQEQLLQETQALQQSFLSEKDS 2488
Cdd:pfam13868 187 -----ARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKERE--------EAEKKARQRQELQQAREEQIELKERRLA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2489 LLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQ 2568
Cdd:pfam13868 254 EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEE 333
|
....*...
gi 1920237970 2569 QQEKLLAE 2576
Cdd:pfam13868 334 ERQKKLKE 341
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1332-1497 |
4.00e-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: 52.54 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1332 EEEERLAEQQRAEERERLAEVEAAleKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQH 1411
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1412 LRQSSEAEIQAKARQVEA-AERSRLRIEEEI----RVVRLQLEATERQRGGAEGELQALRARAEEAEAQK------RQAQ 1480
Cdd:TIGR02794 179 AKAKAEAEAKAKAEEAKAkAEAAKAKAAAEAaakaEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAG 258
|
170
....*....|....*..
gi 1920237970 1481 EEAERLRRQVQDETQRK 1497
Cdd:TIGR02794 259 SEVDKYAAIIQQAIQQN 275
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2154-2457 |
4.08e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2154 MEKHKQFAEQALRQKAQVEQELTAlrlQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKAR 2233
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2234 IEAENRALvlrdKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAarlRQLAEE--DLAQQRALaekmLKEKMQavqeatr 2311
Cdd:TIGR04523 466 LETQLKVL----SRSINKIKQNLEQKQKELKSKEKELKKLNEEK---KELEEKvkDLTKKISS----LKEKIE------- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2312 lKAEAELLQQQKELAQeqarrLQEDKEQMAQQLAQETqgfqktLETERQRQLEmsaEAERLRLRVAEMSRAQARAEEDAR 2391
Cdd:TIGR04523 528 -KLESEKKEKESKISD-----LEDELNKDDFELKKEN------LEKEIDEKNK---EIEELKQTQKSLKKKQEEKQELID 592
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 2392 RFRKQAEDIGERLyrtelatQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQ 2457
Cdd:TIGR04523 593 QKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1349-1443 |
4.44e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 53.42 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1349 LAEVEAALEKQRQLAEAHAQAKAQAEREAqglqRRMQEEVARREEVAVEAQEQKRSIQEELQHLR-QSSEAEIQAKARQV 1427
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALA----EAQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 1920237970 1428 EAAERSRLRI---EEEIRV 1443
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1313-1568 |
4.47e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1313 LSTLTSQYIRFISEtLRRMEEEERLA--EQQRAEERERLAEVEAALEKQRQlaeahAQAKAQAEREAQGLQRRMQEEVAR 1390
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1391 ReevaVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRieEEIRVVRLQLEATERQRGGAEGELQALRARAE 1470
Cdd:COG3206 228 L----AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLR--AQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1471 EAEAQKRQaqeEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAeaeRARQV 1550
Cdd:COG3206 302 ALRAQLQQ---EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL---LQRLE 375
|
250
....*....|....*...
gi 1920237970 1551 QVALETAQRSAEAELQSE 1568
Cdd:COG3206 376 EARLAEALTVGNVRVIDP 393
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3708-3743 |
4.48e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.94 E-value: 4.48e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1920237970 3708 RQLLEAQAATGFLLDPVKGERLAVDEAVRKGLVGPE 3743
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2146-2331 |
4.65e-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: 52.72 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2146 QKQAADAEMEKHKQFAEQALRQKAQvEQELTALRLQLEETDHQKSILDEELQRLKAEVTeaarqrgQVEEELFSLRVQME 2225
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSIK-------QVEEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2226 ELGK---LKARI-----EAENRALVLrdkdsaQRLLQEEAEKMKQVAE--EAARLSVAAQEAARLRQLAEEDLAQQRALA 2295
Cdd:pfam05667 381 ELEKqykVKKKTldllpDAEENIAKL------QALVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLE 454
|
170 180 190
....*....|....*....|....*....|....*....
gi 1920237970 2296 E-KMLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2331
Cdd:pfam05667 455 EiKELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSR 493
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1418-1597 |
4.76e-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: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1418 AEIQAKARQVEAAERSRLRIEEEirvvrlQLEATERQRGGAEGELQALRARAEEAEAqKRQAQEEAERLRRQVQDETQRK 1497
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQ------QAEEAEKQRAAEQARQKELEQRAAAEKA-AKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1498 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTA 1577
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKA 205
|
170 180
....*....|....*....|
gi 1920237970 1578 QLERTLKEEHVAVVQLREEA 1597
Cdd:TIGR02794 206 AAEAAAKAEAEAAAAAAAEA 225
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2194-2602 |
5.38e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2194 EELQRLKAEVteAARQRGQVEEELFSLRVQMEELGKLKARIEaENRALVLRDKDSAQRLLQEEAEKMKQ---VAEEAARL 2270
Cdd:PRK02224 187 GSLDQLKAQI--EEKEEKDLHERLNGLESELAELDEEIERYE-EQREQARETRDEADEVLEEHEERREEletLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2271 SVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaqetQG 2350
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA----QA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2351 FQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLyrtelatqekvmlvQTLETQRQQSDR 2430
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI--------------EELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2431 DAERLREAIAELEHEKDKLKQEAQLLQ--LKSEEMQTVRQEQLLQE------TQALQQSflSEKDSLLQRERCIEQEKAK 2502
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEatLRTARERVEEAEALLEAgkcpecGQPVEGS--PHVETIEEDRERVEELEAE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2503 LEQL------FQDEVAKAQALREEQQR--QQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLL 2574
Cdd:PRK02224 484 LEDLeeeveeVEERLERAEDLVEAEDRieRLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
410 420 430
....*....|....*....|....*....|....
gi 1920237970 2575 AEENQRLRERLQHLEE------ERRAALARSEEI 2602
Cdd:PRK02224 564 EEEAEEAREEVAELNSklaelkERIESLERIRTL 597
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2146-2330 |
5.39e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2146 QKQAADAEMEKHKQFAEQA--LRQKAQVEQEltalRLQLEETDHQKSildeelQRLKAEVTEAARQRGQVEEELFSLRVQ 2223
Cdd:PRK09510 71 QKSAKRAEEQRKKKEQQQAeeLQQKQAAEQE----RLKQLEKERLAA------QEQKKQAEEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2224 MEELGKLKARIEAEN-RALVLRDKDSAQRLLQEEAEK-----MKQVAEEAARLSVAAQEAARLRQLAEE---DLAQQRAL 2294
Cdd:PRK09510 141 AAAAAKAKAEAEAKRaAAAAKKAAAEAKKKAEAEAAKkaaaeAKKKAEAEAAAKAAAEAKKKAEAEAKKkaaAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|....*.
gi 1920237970 2295 AEKmlKEKMQAVQEATRLKAEAELLQQQKELAQEQA 2330
Cdd:PRK09510 221 AEA--KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAK 254
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1326-1559 |
5.46e-06 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 51.96 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1326 ETLRRMEEEERLAEQQRAEERERLA--EVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEvavEAQEQKR 1403
Cdd:pfam15558 51 ERRLLLQQSQEQWQAEKEQRKARLGreERRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQ---RKQCQEQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1404 SIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEA------EAQKR 1477
Cdd:pfam15558 128 RLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELlrrlslEQSLQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1478 QAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ----RALQALEELRL-QAEEAERRLRQAEAERARQVQV 1552
Cdd:pfam15558 208 RSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEERqehkEALAELADRKIqQARQVAHKTVQDKAQRARELNL 287
|
....*..
gi 1920237970 1553 ALETAQR 1559
Cdd:pfam15558 288 EREKNHH 294
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1670-2412 |
5.69e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.03 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1670 AVRQRELAEQELEKQRQLAeGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE-------LARLQrEAAAATQKrrelea 1742
Cdd:COG3096 277 ANERRELSERALELRRELF-GARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhLNLVQ-TALRQQEK------ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1743 eLAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAEAgRFRELAEEAARLRAlaEEAKRQRQLaeeDAVRQRAEAERvl 1822
Cdd:COG3096 349 -IERYQEDLEEL---TERLEEQEEVVEEAAEQLAEAEA-RLEAAEEEVDSLKS--QLADYQQAL---DVQQTRAIQYQ-- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1823 aEKLAAISEATRLKTEAEIALKEKEAENERLRRlAEDEAFQRRLleeQAAQHKADIEARLAQLRKAseseLERQKGLVED 1902
Cdd:COG3096 417 -QAVQALEKARALCGLPDLTPENAEDYLAAFRA-KEQQATEEVL---ELEQKLSVADAARRQFEKA----YELVCKIAGE 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1903 TLRQRR-QVEEEILALKGSFEKAAAGKAELELELGrirgtaedtlrskeQAEQEAARQRQLAAEEERRRREAEERVQKSL 1981
Cdd:COG3096 488 VERSQAwQTARELLRRYRSQQALAQRLQQLRAQLA--------------ELEQRLRQQQNAERLLEEFCQRIGQQLDAAE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1982 AAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEA-----AQKRLQ--AEEKAHAFAVQQkeqelqQ 2054
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawlaAQDALErlREQSGEALADSQ------E 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2055 TLQQEQSVLERLRseaeaarraaeeaeaareraerEAAQSRRQVEEAERlkqsaeeqaqaqaqaqaaaeklrkeaeqeaa 2134
Cdd:COG3096 628 VTAAMQQLLERER----------------------EATVERDELAARKQ------------------------------- 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2135 rraQAEQAALRQKQAADAEMEKHKQFAEQ----------------------AL--------------------------- 2165
Cdd:COG3096 655 ---ALESQIERLSQPGGAEDPRLLALAERlggvllseiyddvtledapyfsALygparhaivvpdlsavkeqlagledcp 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2166 ---------------------------------RQ-------------KAQVEQELTALRLQLEETD---HQKSILDEEL 2196
Cdd:COG3096 732 edlyliegdpdsfddsvfdaeeledavvvklsdRQwrysrfpevplfgRAAREKRLEELRAERDELAeqyAKASFDVQKL 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2197 QRL--------------------KAEVTEAARQRGQVEEELFSLRVQM----EELGKLKARIEAENRAL----VLRDKDS 2248
Cdd:COG3096 812 QRLhqafsqfvgghlavafapdpEAELAALRQRRSELERELAQHRAQEqqlrQQLDQLKEQLQLLNKLLpqanLLADETL 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2249 AQRL--LQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAekmlKEKMQAVQEATRLKAEA---------- 2316
Cdd:COG3096 892 ADRLeeLREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQ----ADYLQAKEQQRRLKQQIfalsevvqrr 967
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2317 -------------------ELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQkTLETERQRQLEMSAEAERlrlRVA 2377
Cdd:COG3096 968 phfsyedavgllgensdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLA-SLKSSRDAKQQTLQELEQ---ELE 1043
|
890 900 910
....*....|....*....|....*....|....*...
gi 1920237970 2378 EMS-RAQARAEEDA--RRFRKQAEDIGERLYRTELATQ 2412
Cdd:COG3096 1044 ELGvQADAEAEERAriRRDELHEELSQNRSRRSQLEKQ 1081
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3913-3950 |
5.73e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.94 E-value: 5.73e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1920237970 3913 QRFLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTA 3950
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
157-264 |
5.85e-06 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 48.26 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 157 QSEDMTAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGV 235
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 1920237970 236 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 264
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1764-2605 |
5.98e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1764 ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIAL 1843
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1844 KEKEAENERlrrlAEDEAFQRRLLEEQAAQHkaDIEARLAQLRKASESELERQKGLVEDTLRQR--------RQVEEEIL 1915
Cdd:pfam15921 161 KEDMLEDSN----TQIEQLRKMMLSHEGVLQ--EIRSILVDFEEASGKKIYEHDSMSTMHFRSLgsaiskilRELDTEIS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1916 ALKGSF----EKAAAGKAELELELGRIRGTAEDTLrskEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQR 1991
Cdd:pfam15921 235 YLKGRIfpveDQLEALKSESQNKIELLLQQHQDRI---EQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1992 KAA----LEEVE----RLKAKVEEARRLRERAEQESARQLQLAQ----EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQE 2059
Cdd:pfam15921 312 NSMymrqLSDLEstvsQLRSELREAKRMYEDKIEELEKQLVLANseltEARTERDQFSQESGNLDDQLQKLLADLHKREK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2060 QSVLERlrseaeaarraaeeaeaareraereaAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2139
Cdd:pfam15921 392 ELSLEK--------------------------EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2140 EQAALRQKQAADAEMEKHKQFAEQALRQKA---QVEQELTALRLQLEETDHQKSILDEELQR----LKAEVTEAARQRGQ 2212
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEmlrKVVEELTAKKMTLESSERTVSDLTASLQEkeraIEATNAEITKLRSR 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2213 VE---EELFSLRVQMEELGKLKAriEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQ-EAArlrQLAEEDL 2288
Cdd:pfam15921 526 VDlklQELQHLKNEGDHLRNVQT--ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvEKA---QLEKEIN 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2289 AQQRALAE-KMLKEKMQAvqEATRLKAEAELLQQQK-ELAQEQARRLQEDKEqmaqqLAQETQGFQKTLETERQRQLEMS 2366
Cdd:pfam15921 601 DRRLELQEfKILKDKKDA--KIRELEARVSDLELEKvKLVNAGSERLRAVKD-----IKQERDQLLNEVKTSRNELNSLS 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2367 AEAERLRlrvaemsraqaraeedaRRFRKQAEDIGERLYRTELATQE-KVMLVQTLETQRQQSDRDAERLREA------I 2439
Cdd:pfam15921 674 EDYEVLK-----------------RNFRNKSEEMETTTNKLKMQLKSaQSELEQTRNTLKSMEGSDGHAMKVAmgmqkqI 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2440 AELEHEKDKLKQEAQLLQlksEEMQTVRQEQ-LLQEtqalqqsflsEKDSLLQRERCIEQEKAKLEQlfQDEVAKAQALR 2518
Cdd:pfam15921 737 TAKRGQIDALQSKIQFLE---EAMTNANKEKhFLKE----------EKNKLSQELSTVATEKNKMAG--ELEVLRSQERR 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2519 eeqqrqqqqMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLA----EENQRLRERLQhleeeRRA 2594
Cdd:pfam15921 802 ---------LKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQgpgyTSNSSMKPRLL-----QPA 867
|
890
....*....|.
gi 1920237970 2595 ALARSEEIAPS 2605
Cdd:pfam15921 868 SFTRTHSNVPS 878
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
30-150 |
6.05e-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: 48.44 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 30 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSSRLPREKGRMRfhKLQNVQIA 109
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMTR---VPVDWGHVNKPPYPALGGNMK--KIENCNYA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1920237970 110 LDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 150
Cdd:cd21329 75 VELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1367-1589 |
6.88e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.77 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1367 AQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKArqveaAERSRLRIEEEIRVvrl 1446
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQKQ--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1447 QLEATERQRggaegelqALRARAEEAEAqKRQAQEEAerlRRQVQDETQRKRQAEAelalrvQAEAEAAREKQRAL---Q 1523
Cdd:TIGR02794 121 AEEAKAKQA--------AEAKAKAEAEA-ERKAKEEA---AKQAEEEAKAKAAAEA------KKKAEEAKKKAEAEakaK 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 1524 ALEELRLQAEEAERRLRQAE----------AERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVA 1589
Cdd:TIGR02794 183 AEAEAKAKAEEAKAKAEAAKakaaaeaaakAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2144-2590 |
8.24e-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: 52.42 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2144 LRQKQAADAEMEKHKQFAEQALRQ-----KAQVEQELTA---LRLQLEETDHQKSI-LDEELQRLKAEVTEAARQRGQVE 2214
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQvymdlNNNIEKMILAfeeLRVQAENARLEMHFkLKEDHEKIQHLEEEYKKEINDKE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2215 EELFSLRVQM-EELGKLKARI----EAENRALVLRDKDSAQ-RLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDL 2288
Cdd:pfam05483 240 KQVSLLLIQItEKENKMKDLTflleESRDKANQLEEKTKLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2289 AQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ--------KELAQEQARRLQEDKEQMaQQLAQETQgfQKTLETERQ 2360
Cdd:pfam05483 320 QIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeattcslEELLRTEQQRLEKNEDQL-KIITMELQ--KKSSELEEM 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2361 RQLEMSAEAERLRLRVAeMSRAQARAEEdarrfRKQAEDIGERLYRTElatQEKVMLVQTLETQRQQSDRDAERLREAIA 2440
Cdd:pfam05483 397 TKFKNNKEVELEELKKI-LAEDEKLLDE-----KKQFEKIAEELKGKE---QELIFLLQAREKEIHDLEIQLTAIKTSEE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2441 ELEHEKDKLKQEAQLLQLKSEEMqTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQdevaKAQALREE 2520
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIEL-TAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK----QIENLEEK 542
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2521 QQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEE 2590
Cdd:pfam05483 543 EMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE 612
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2303-2448 |
9.12e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 52.33 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2303 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQ-QLAQetQGFQKTLETERQRQLEMSAEAERLR 2373
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARgRLER--QKMHDKAKAEEQRTKLLELQAESAA 710
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 2374 LRVAEMSRAQARAEEDARRFRKQAEdigerLYRTEL-ATQEKVMLVQTLETQRQQSDRDAERlREAIAELEHEKDK 2448
Cdd:PTZ00491 711 VESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1214-1533 |
9.18e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 52.36 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1214 KQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQ 1293
Cdd:PRK10929 29 TQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLER-------AKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1294 SGSESIIQEYVDLRTRYSELSTLTSQ---YIRFISETLRRMEeeerlaeQQRAEERERLAEVEAALEKQRQLAEAHAQAK 1370
Cdd:PRK10929 102 MSTDALEQEILQVSSQLLEKSRQAQQeqdRAREISDSLSQLP-------QQQTEARRQLNEIERRLQTLGTPNTPLAQAQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1371 AQAereaqglqrrMQEEVARReevaveaqeqkRSIQEELQhLRQSSEAEIQAKAR-QVEAAERSRLRIEEEIRVVRLQLE 1449
Cdd:PRK10929 175 LTA----------LQAESAAL-----------KALVDELE-LAQLSANNRQELARlRSELAKKRSQQLDAYLQALRNQLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1450 aTERQRggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQ-------AEAEAAREKQRAL 1522
Cdd:PRK10929 233 -SQRQR------------EAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQrmdliasQQRQAASQTLQVR 299
|
330
....*....|.
gi 1920237970 1523 QALEELRLQAE 1533
Cdd:PRK10929 300 QALNTLREQSQ 310
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1291-1505 |
9.46e-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: 51.30 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1291 KVQSGSESIIQEYVDLRTRYSELSTL---TSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA-- 1365
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLal 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1366 --HAQAKAQAEREAQGLQRRMQeevARREEVaveaqEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIrv 1443
Cdd:COG4942 125 llSPEDFLDAVRRLQYLKYLAP---ARREQA-----EELRADLAELAALRAELEAERAELEALLAELEEERAALEALK-- 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 1444 vrlqleaTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1505
Cdd:COG4942 195 -------AERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1664-1946 |
9.77e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 9.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1664 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAE 1743
Cdd:COG4372 23 GILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1744 LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQ----LAEEDAVRQRAEAE 1819
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEelaaLEQELQALSEAEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1820 RVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGL 1899
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1920237970 1900 VEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTL 1946
Cdd:COG4372 263 LELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3915-3953 |
1.00e-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: 1.00e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1920237970 3915 FLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTAFEL 3953
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1512-2043 |
1.01e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1512 AEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQV--ALETAQRSAEAELQS------EHASFAEKTAQLERTL 1583
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREinEISSELPELREELEKlekevkELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1584 KEEHVAVVQLRE---EATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREA 1660
Cdd:PRK03918 248 ESLEGSKRKLEEkirELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1661 RRRGKAEEQAVRQRELAEQELEKQRQLAE--------GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR--LQREA 1730
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEEleerhelyEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKeeIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1731 AAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGR-FRELAEEAARLRALAEEAKRQ-RQLAE 1808
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAeLKRIEKELKEIEEKERKLRKElRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1809 EDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERlRRLAEDEAFQRRLLEEqaAQHKADIEARLAQLRKA 1888
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLK-EKLIKLKGEIKSLKKE--LEKLEELKKKLAELEKK 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1889 SEsELERQKGLVEDTLRQR-----RQVEEEILALKGSFEK---AAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQR 1960
Cdd:PRK03918 565 LD-ELEEELAELLKELEELgfesvEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1961 QLAAEEERRrreaeervqKSLAAEEEAARQRKAALE---EVERLKAKVEEARRLRERAEQ--ESARQLQLAQEAAQKRLQ 2035
Cdd:PRK03918 644 ELRKELEEL---------EKKYSEEEYEELREEYLElsrELAGLRAELEELEKRREEIKKtlEKLKEELEEREKAKKELE 714
|
....*...
gi 1920237970 2036 AEEKAHAF 2043
Cdd:PRK03918 715 KLEKALER 722
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2172-2601 |
1.07e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.10 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2172 EQELTALRLQLEETDHQKSILDEElQRLKAEvtEAARQRGQVEeelfslRVQMEelGKLKariEAENRALVLRDKDSaqR 2251
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQDLE-EQLDEE--EAARQKLQLE------KVTTE--AKIK---KLEEDILLLEDQNS--K 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2252 LLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE-KMQAVQEATRLKAEAELLQqqkelAQEQA 2330
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEeKGRQELEKAKRKLEGESTD-----LQEQI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2331 RRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQA--RAEEDAR-RFRKQAEDIGERL--Y 2405
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEdlESERAARnKAEKQRRDLGEELeaL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2406 RTELA-TQEKVMLVQTLETQRQQsdrDAERLREAIaelehEKDKLKQEAQLLQLKSEEMQTVR--QEQLLQ--------- 2473
Cdd:pfam01576 305 KTELEdTLDTTAAQQELRSKREQ---EVTELKKAL-----EEETRSHEAQLQEMRQKHTQALEelTEQLEQakrnkanle 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2474 -ETQALQQSFL---SEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQalreEQQRQQQQMQQEKQQLAASMEEARRRQHEA 2549
Cdd:pfam01576 377 kAKQALESENAelqAELRTLQQAKQDSEHKRKKLEGQLQELQARLS----ESERQRAELAEKLSKLQSELESVSSLLNEA 452
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 2550 EEGVRRQQEELQRLAQQQQQQEKLLAEENQR---LRERLQHLEEERRAALARSEE 2601
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQELLQEETRQklnLSTRLRQLEDERNSLQEQLEE 507
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2261-2477 |
1.14e-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: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2261 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2340
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2341 AQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKvmlvQT 2420
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AA 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237970 2421 LETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQA 2477
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1341-2045 |
1.21e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.72 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1341 QRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER-EAQGlqrrmqeevarrEEVAVEAQEQKRSIQEELQHLRQsseae 1419
Cdd:PRK10246 168 ERAELLEELTGTEIYGQISAMVFEQHKSARTELEKlQAQA------------SGVALLTPEQVQSLTASLQVLTD----- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1420 iqakarqveaaersrlriEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqvQDETQRKRQ 1499
Cdd:PRK10246 231 ------------------EEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKA-------QPQLAALSL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1500 AEAELALRVQAEaeaarEKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQrsaeaELQSEHASFAEKTAql 1579
Cdd:PRK10246 286 AQPARQLRPHWE-----RIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSA-----ELQAQQQSLNTWLA-- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1580 ertlkeEHVAVVQLREE-----ATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLtqaeaekqke 1654
Cdd:PRK10246 354 ------EHDRFRQWNNElagwrAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQ---------- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1655 eaerearrrgKAEEQAVRQR--ELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLqREAAA 1732
Cdd:PRK10246 418 ----------HAEQRPLRQRlvALHGQIVPQQKRLAQ-LQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADV-KTICE 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1733 ATQKRRELEAELAKVRAEMEVLL--ASKARAEEESRS-TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1809
Cdd:PRK10246 486 QEARIKDLEAQRAQLQAGQPCPLcgSTSHPAVEAYQAlEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDES 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1810 DAvRQRAEAERVLAEKLAAISEA--TRLKTEAEIA--LKEKEAENERLRRLAEDEAFQRRLLE--EQAAQHKADIEARLA 1883
Cdd:PRK10246 566 EA-QSLRQEEQALTQQWQAVCASlnITLQPQDDIQpwLDAQEEHERQLRLLSQRHELQGQIAAhnQQIIQYQQQIEQRQQ 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1884 QLR----------------------KASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGT 1941
Cdd:PRK10246 645 QLLtalagyaltlpqedeeaswlatRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHE 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1942 AEDTLRSK-----EQAEQEAARQRQLAAEEERRRREAEERVQKSLAAE--EEAARQRKAALEevERLKAKVEEARRLRER 2014
Cdd:PRK10246 725 QCLSLHSQlqtlqQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAAllDEETLTQLEQLK--QNLENQRQQAQTLVTQ 802
|
730 740 750
....*....|....*....|....*....|.
gi 1920237970 2015 AEQESARQLQLAQEAAQKRLQAEEKAHAFAV 2045
Cdd:PRK10246 803 TAQALAQHQQHRPDGLDLTVTVEQIQQELAQ 833
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
35-154 |
1.27e-05 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 48.08 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 35 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRLPrekgrmrFHKLQN 105
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTID-ERTINKKKLTP-------FTIQEN 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1920237970 106 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 154
Cdd:cd21324 97 LNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2424-2613 |
1.42e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2424 QRQQSDRDAERLREAIAELEHEKDKLKQEAQLL--QLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKA 2501
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALlkQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2502 KLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASME------EARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLA 2575
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 1920237970 2576 EENQRLRERLQHLEEERRAALARSEEIAPSRAAAARAL 2613
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2312-2598 |
1.61e-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: 51.49 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2312 LKAEAELLQQQKELAQEQARRlqedkEQMAQQLAQETQGfQKTLETERQrqlemsAEAERLRLRVAEMsraqaRAEEDAR 2391
Cdd:COG3096 288 LELRRELFGARRQLAEEQYRL-----VEMARELEELSAR-ESDLEQDYQ------AASDHLNLVQTAL-----RQQEKIE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2392 RFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEA----QLLQLKsEEMQTVR 2467
Cdd:COG3096 351 RYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiqyqQAVQAL-EKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2468 Q---------EQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQ------DEVAKAQA-------LREEQQRQQ 2525
Cdd:COG3096 430 GlpdltpenaEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvckiaGEVERSQAwqtarelLRRYRSQQA 509
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237970 2526 QQMQQEKqqLAASMEEARRRQHEAEEgVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALAR 2598
Cdd:COG3096 510 LAQRLQQ--LRAQLAELEQRLRQQQN-AERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1806-2506 |
1.68e-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: 51.59 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1806 LAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKAdiEARLAQL 1885
Cdd:TIGR00606 165 LSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLES--SREIVKS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1886 RKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQlaae 1965
Cdd:TIGR00606 243 YENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKE---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1966 eerrrrEAEERVQKSLAAEEEAAR---QRKAALE-EVERLKAKVE---EARRLRERAEQESARQLQLAQEAAQKRLQAEE 2038
Cdd:TIGR00606 319 ------RELVDCQRELEKLNKERRllnQEKTELLvEQGRLQLQADrhqEHIRARDSLIQSLATRLELDGFERGPFSERQI 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2039 K-AHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQ 2117
Cdd:TIGR00606 393 KnFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDR 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2118 AQAAAEKLRKEAE---------------QEAARRAQAEQAALRQKQAADAEME----------------KHKQFAEQALR 2166
Cdd:TIGR00606 473 ILELDQELRKAERelskaeknsltetlkKEVKSLQNEKADLDRKLRKLDQEMEqlnhhtttrtqmemltKDKMDKDEQIR 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2167 Q-KAQVEQELTAL------RLQLEETDHQKS----ILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGklkariE 2235
Cdd:TIGR00606 553 KiKSRHSDELTSLlgyfpnKKQLEDWLHSKSkeinQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYE------D 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2236 AENRALVLRDKDSAQRLLQEEAEKM-KQVAEEAARLSVAAQeaaRLRQLAEED-----LAQQRALAEKMLKEKMQAVQEA 2309
Cdd:TIGR00606 627 KLFDVCGSQDEESDLERLKEEIEKSsKQRAMLAGATAVYSQ---FITQLTDENqsccpVCQRVFQTEAELQEFISDLQSK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2310 TRLkAEAELLQQQKELAQEQARRlqEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSR--AQARAE 2387
Cdd:TIGR00606 704 LRL-APDKLKSTESELKKKEKRR--DEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETllGTIMPE 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2388 EDARRFRKQAEDIGERLYRtELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVR 2467
Cdd:TIGR00606 781 EESAKVCLTDVTIMERFQM-ELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI 859
|
730 740 750
....*....|....*....|....*....|....*....
gi 1920237970 2468 QeQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQL 2506
Cdd:TIGR00606 860 Q-HLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV 897
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2162-2601 |
1.70e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2162 EQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAenral 2241
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2242 vLRDKDSAQRLLQEEAEKMKQVAEEaarlsvaaqeaaRLRQLAEedlaqQRALAEKMLKEKMQAVQEATRLKAEAELLQQ 2321
Cdd:PRK03918 236 -LKEEIEELEKELESLEGSKRKLEE------------KIRELEE-----RIEELKKEIEELEEKVKELKELKEKAEEYIK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2322 QKELAQEQARRLQEDKEQMA--QQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMsRAQARAEEDARRFRKQAED 2399
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSrlEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2400 IGERLyrTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKqeAQLLQLKS---------EEMQTVRQEQ 2470
Cdd:PRK03918 377 LKKRL--TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK--KAIEELKKakgkcpvcgRELTEEHRKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2471 LLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEvAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAE 2550
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLK 531
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1920237970 2551 EGVRRQQEELQRLAqQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEE 2601
Cdd:PRK03918 532 EKLIKLKGEIKSLK-KELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1307-1448 |
1.71e-05 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 49.60 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1307 RTRYSELSTLTSQYIRFI----SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRqlaeahaqakAQAEREAQglqR 1382
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKR----------YQDQLEAQ---R 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 1383 RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQL 1448
Cdd:pfam12037 123 RRNEELLRKQEESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAEARAKEERENEDLNLEQ 188
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1727-2048 |
1.75e-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: 51.28 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1727 QREAAAATQKRRELEAELAKVRAEMEvllaSKARAEEESRSTSEKSKQRlEAEAGRFRELAEEAARLralaeEAKRQRQL 1806
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKE----EKAREVERRRKLEEAEKAR-QAEMDRQAAIYAEQERM-----AMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1807 AEEDAVRQRAEAERVLAEKLAAisEATRLKtEAEIALKEKEAENERLRRLAEdEAFQRRLLEEQAAQHKADIEARLAQLR 1886
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAM--EISRMR-ELERLQMERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1887 KASESELERQ-KGLVEDTLRQRRQVEEEilalkgsfekaaagKAELELELGRIRGTAEDTLRSKEQAEQEaaRQRQLAAE 1965
Cdd:pfam17380 427 AEQEEARQREvRRLEEERAREMERVRLE--------------EQERQQQVERLRQQEEERKRKKLELEKE--KRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1966 EERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARrlRERAEQESARQLQLAQE---AAQKRLQAEEKAHA 2042
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER--RREAEEERRKQQEMEERrriQEQMRKATEERSRL 568
|
....*.
gi 1920237970 2043 FAVQQK 2048
Cdd:pfam17380 569 EAMERE 574
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1327-1543 |
1.80e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 51.02 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1327 TLRRMEEEERLAEQQRAEERERLAEVEAALEkqrqlaEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQ 1406
Cdd:pfam02029 134 EIREKEYQENKWSTEVRQAEEEGEEEEDKSE------EAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1407 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRV-VRLQLEATERQRGGAEG-ELQALRARAEEAEAQKRQAQEEAE 1484
Cdd:pfam02029 208 KSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLeAEQKLEELRRRRQEKESeEFEKLRQKQQEAELELEELKKKRE 287
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 1485 RLRRQVQDETQRKRQAEAELALRVQaeaeaaREKQRALQALEelRLQAEEAERRLRQAE 1543
Cdd:pfam02029 288 ERRKLLEEEEQRRKQEEAERKLREE------EEKRRMKEEIE--RRRAEAAEKRQKLPE 338
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1697-1792 |
1.81e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 51.11 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1697 AAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1776
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 1920237970 1777 EAEAGRFrELAEEAAR 1792
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
29-144 |
1.82e-05 |
|
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: 47.06 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 29 DERDRVQkktFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEvlsgDSLPRERDVIRSSRLPRE-KGRM 98
Cdd:cd21294 4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLIN----DSVPDTIDERVLNKPPRKnKPLN 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1920237970 99 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 144
Cdd:cd21294 77 NFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1463-1727 |
1.84e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1463 QALRARAEEAEAQKRQAQEEAERLRRQVqDETQRKRQA--EAELALRVQAEAEAAREKQRALQA-LEELRLQAEEAERRL 1539
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKEL-EEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESqLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1540 RQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAtrraqqqaeaeraraeaerele 1619
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI---------------------- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1620 rwqlkanEALRLRLQAEEVAQQKSLtqaeaekqkeeaerearrrgKAEEQAVRQRelaEQELEKQRQLAEGTAQQRLAAE 1699
Cdd:COG3206 301 -------AALRAQLQQEAQRILASL--------------------EAELEALQAR---EASLQAQLAQLEARLAELPELE 350
|
250 260
....*....|....*....|....*...
gi 1920237970 1700 QELIRLRAETeqgEQQRQLLEEELARLQ 1727
Cdd:COG3206 351 AELRRLEREV---EVARELYESLLQRLE 375
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1377-2013 |
2.04e-05 |
|
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: 50.88 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1377 AQGLQR---RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATER 1453
Cdd:pfam05483 73 SEGLSRlysKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1454 QRGGAEgELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAElaLRVQAEaeaarekqralQALEELRLQAE 1533
Cdd:pfam05483 153 TRHLCN-LLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEE--LRVQAE-----------NARLEMHFKLK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1534 EAERRLRQAEAERARQV-----QVALETAQrSAEAElqsehasfaEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAE 1608
Cdd:pfam05483 219 EDHEKIQHLEEEYKKEIndkekQVSLLLIQ-ITEKE---------NKMKDLTFLLEESRDKANQLEEKTKLQDENLKELI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1609 RARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQla 1688
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR-- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1689 egTAQQRLaaeqelirlraetEQGEQQRQLLEEELARLQREAAAATQ----KRRELEaELAKVRAEMEVLLASKARAEEE 1764
Cdd:pfam05483 367 --TEQQRL-------------EKNEDQLKIITMELQKKSSELEEMTKfknnKEVELE-ELKKILAEDEKLLDEKKQFEKI 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1765 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALaeEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLkteaeialk 1844
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKEIHDLEIQLTAI--KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL--------- 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1845 ekeaENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGL--VEDTLRQRR--------QVEEEI 1914
Cdd:pfam05483 500 ----ENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELesVREEFIQKGdevkckldKSEENA 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1915 LALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKsLAAEEEAARQR--- 1991
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNK-LELELASAKQKfee 654
|
650 660 670
....*....|....*....|....*....|....*...
gi 1920237970 1992 ----------------KAALEEVERLKAKVEEARRLRE 2013
Cdd:pfam05483 655 iidnyqkeiedkkiseEKLLEEVEKAKAIADEAVKLQK 692
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1339-1493 |
2.13e-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: 49.15 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1339 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREaqglQRRMQEEVARREEVAVEAQEQKRSIqeelqhlrqSSEA 1418
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE----IKRLELEIEEVEARIKKYEEQLGNV---------RNNK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 1419 EIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1493
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1338-1766 |
2.20e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.68 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1338 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE 1417
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1418 AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1497
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1498 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTA 1577
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1578 QLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAE 1657
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1658 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKR 1737
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420
....*....|....*....|....*....
gi 1920237970 1738 RELEAELAKVRAEMEVLLASKARAEEESR 1766
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAA 512
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2144-2349 |
2.29e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.99 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2144 LRQKQAADA-----EMEKHKQFAEQALRQKaqveqeltalrlQLEETDH---------QKSILDEELQRLKAEVTEAARQ 2209
Cdd:NF012221 1561 LADKERAEAdrqrlEQEKQQQLAAISGSQS------------QLESTDQnaletngqaQRDAILEESRAVTKELTTLAQG 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2210 RGQVEEElfslRVQMEELGKlKARIEAENRAL--VLRDKDSAQRLLQEEAEKMKQ--------VAEEAARLSVAAQEAAR 2279
Cdd:NF012221 1629 LDALDSQ----ATYAGESGD-QWRNPFAGGLLdrVQEQLDDAKKISGKQLADAKQrhvdnqqkVKDAVAKSEAGVAQGEQ 1703
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2280 LRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQ 2349
Cdd:NF012221 1704 NQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAK 1773
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1524-1962 |
2.34e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 50.79 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1524 ALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQ---------LR 1594
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALrlaaalapfWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1595 EEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQR 1674
Cdd:COG3903 557 LRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAA 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1675 ELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVL 1754
Cdd:COG3903 637 AAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAA 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1755 LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATR 1834
Cdd:COG3903 717 AAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAA 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1835 LKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEI 1914
Cdd:COG3903 797 AAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAA 876
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1920237970 1915 LALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQL 1962
Cdd:COG3903 877 AAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAA 924
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2144-2591 |
2.50e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.59 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2144 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTalrlQLEETDHQKSILDEELQRLKAEVTEAARQRGQVE-----EELF 2218
Cdd:pfam10174 58 LKEQYRVTQEENQHLQLTIQALQDELRAQRDLN----QLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEherqaKELF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2219 SLRVQMEELgklKARIEAENRALVLRDkDSAQRLL---QEEAEKMKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALA 2295
Cdd:pfam10174 134 LLRKTLEEM---ELRIETQKQTLGARD-ESIKKLLemlQSKGLPKKSGEEDWERTRRIAEAEMQLGHL--EVLLDQKEKE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2296 EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLqedkEQMAQQLAQETQgfqkTLETErqrqLEMSAEAERLRLR 2375
Cdd:pfam10174 208 NIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSL----ERNIRDLEDEVQ----MLKTN----GLLHTEDREEEIK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2376 VAEMSRAQARaeedarrFRK-QAEDIGERLYRTE---LATQEKVmlvQTLETQRQQSDRDAERLREAIAELEHEKDKLKQ 2451
Cdd:pfam10174 276 QMEVYKSHSK-------FMKnKIDQLKQELSKKEselLALQTKL---ETLTNQNSDCKQHIEVLKESLTAKEQRAAILQT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2452 EAQLLQLKSEEMQTV-----RQEQLLQETQALQQSFLSE-KDSLLQRERCIEQEKAKLEQL---FQDEVAKAQALREEQQ 2522
Cdd:pfam10174 346 EVDALRLRLEEKESFlnkktKQLQDLTEEKSTLAGEIRDlKDMLDVKERKINVLQKKIENLqeqLRDKDKQLAGLKERVK 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 2523 RQQQQMQQEKQQLAaSMEEARRrqhEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEE 2591
Cdd:pfam10174 426 SLQTDSSNTDTALT-TLEEALS---EKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPE 490
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1363-1578 |
2.54e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1363 AEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLrqssEAEIQAKARQVEAAERsrlRIEEEIR 1442
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEA---EIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1443 VVRLQLEATERQrGGAEGELQAL--------------------RARAEEAEAQKrQAQEEAERLRRQVQDETQRKRQAEA 1502
Cdd:COG3883 87 ELGERARALYRS-GGSVSYLDVLlgsesfsdfldrlsalskiaDADADLLEELK-ADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 1503 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ 1578
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3784-3820 |
2.55e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.55e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1920237970 3784 LRLLDAQLATGGIVDPRLGFHLPLDVAYQRGYLDKDT 3820
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1622-2040 |
2.59e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.29 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1622 QLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1701
Cdd:COG5278 105 QQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1702 LIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG 1781
Cdd:COG5278 185 LLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1782 RFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEA 1861
Cdd:COG5278 265 AALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAAL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1862 FQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGT 1941
Cdd:COG5278 345 ALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1942 AEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2021
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
410
....*....|....*....
gi 1920237970 2022 QLQLAQEAAQKRLQAEEKA 2040
Cdd:COG5278 505 LAALLLAAAEAALAAALAA 523
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1256-1587 |
2.97e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 50.40 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1256 QRFAKQYINAIKDYelqlvtYKAQLEPVASPAKKPKvQSGSESIIQEYVDLRTRY-SELSTLTSQyirfiSETLRRMEEE 1334
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEYlYELNVLKEK-----SEAELTSKTK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1335 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQ----RRMQEEVArreEVAVEAQEQKRSIQEELQ 1410
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPtntyKTLELEIA---ESDVEVKKAELELVKEEA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1411 HLRQSSEAEIQAKAR-QVEAAERSRLrieEEIRVVRLQLEATERQRGGAE-GELQALRARAEEAEAQKRQA--------- 1479
Cdd:NF033838 198 KEPRDEEKIKQAKAKvESKKAEATRL---EKIKTDREKAEEEAKRRADAKlKEAVEKNVATSEQDKPKRRAkrgvlgepa 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1480 -----QEEAERLRRQVQDET-------QRKRQAEAE-LALRVQAEAEAAREKQR---ALQALEELRLQAEEAERRLRQAE 1543
Cdd:NF033838 275 tpdkkENDAKSSDSSVGEETlpspslkPEKKVAEAEkKVEEAKKKAKDQKEEDRrnyPTNTYKTLELEIAESDVKVKEAE 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1920237970 1544 A----ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEH 1587
Cdd:NF033838 355 LelvkEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEA 402
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2160-2391 |
3.34e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 49.69 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2160 FAEQALRQKAQ---VEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQrgqveeelfsLRVQMEELGKLKARIEA 2236
Cdd:PRK11637 38 FSAHASDNRDQlksIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRK----------LRETQNTLNQLNKQIDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2237 ENRalvlrdkdSAQRLLQEEAEKMKqvaeeaarlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQA----VQEAtRL 2312
Cdd:PRK11637 108 LNA--------SIAKLEQQQAAQER---------LLAAQLDAAFRQGEHTGLQLILSGEESQRGERILAyfgyLNQA-RQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2313 KAEAELLQQQKELAQEqaRRLQEDKEQMAQQLAQETQGFQKTLETER-----------------QRQL-EMSAEAERLRL 2374
Cdd:PRK11637 170 ETIAELKQTREELAAQ--KAELEEKQSQQKTLLYEQQAQQQKLEQARnerkktltglesslqkdQQQLsELRANESRLRD 247
|
250
....*....|....*...
gi 1920237970 2375 RVAEMSR-AQARAEEDAR 2391
Cdd:PRK11637 248 SIARAEReAKARAEREAR 265
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2144-2446 |
3.48e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 49.68 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2144 LRQKQAADAEMEKHkqfAEQALRQKAQVEQELTALRLQLEETDHQksildeeLQRLKAEVTEAARQRGQVEEELFSLRVQ 2223
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2224 MEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEkmkqvaeeaarlsVAAQEAARLRQLAEEDLAQQRALAEKM-LKEK 2302
Cdd:pfam19220 183 SEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2303 MQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLAQETQGFQKTLEterqrqlEMSAEAERLRLRVAEMSRA 2382
Cdd:pfam19220 250 LEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRLA-------GLEADLERRTQQFQEMQRA 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237970 2383 QARAEEDARRFRKQAEDIGERLYRTE---LATQEKV-MLVQTLETQRQQSDRDAERLREaiaELEHEK 2446
Cdd:pfam19220 320 RAELEERAEMLTKALAAKDAALERAEeriASLSDRIaELTKRFEVERAALEQANRRLKE---ELQRER 384
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
2223-2603 |
3.50e-05 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 49.99 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2223 QMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK 2302
Cdd:COG5281 1 AAALAAAAALAAAAAAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2303 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA 2382
Cdd:COG5281 81 AAALAEDAAAAAAAAEAALAALAAAALALAAAALAEAALAAAAAAAAAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2383 QARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEE 2462
Cdd:COG5281 161 AAAAAAAAAAAAAAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2463 MQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEA 2542
Cdd:COG5281 241 SAAAQALAALAAAAAAAALALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAAAA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 2543 R-RRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIA 2603
Cdd:COG5281 321 AqALRAAAQALAALAQRALAAAALAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWA 382
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1830-2583 |
3.50e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 50.21 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1830 SEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQ 1909
Cdd:NF041483 22 AEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRSLASRPAYDGADIGYQAEQLLRNAQIQADQLRADAERELRDARA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1910 VEEEIlaLKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQ----------AEQEAARQRQLAAEEERRRREAEERVQK 1979
Cdd:NF041483 102 QTQRI--LQEHAEHQARLQAELHTEAVQRRQQLDQELAERRQtveshvnenvAWAEQLRARTESQARRLLDESRAEAEQA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1980 SLAAEEEAARqrkAALEEVERLKAKVEEARRLRE----RAEQESARQLQLAQEAAQKRLQAEEKAHAF-------AVQQK 2048
Cdd:NF041483 180 LAAARAEAER---LAEEARQRLGSEAESARAEAEailrRARKDAERLLNAASTQAQEATDHAEQLRSStaaesdqARRQA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2049 EQELQQTLQQEQSVLERLR-----SEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAE 2123
Cdd:NF041483 257 AELSRAAEQRMQEAEEALRearaeAEKVVAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQAL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2124 KLRKEAEQEAARRAQAEQAALRQKQAAdAEMEKHKQFAEQALRQKAQVEQELTalRLQLEETDHQKSILDEELQRLKAEV 2203
Cdd:NF041483 337 ADARAEAEKLVAEAAEKARTVAAEDTA-AQLAKAARTAEEVLTKASEDAKATT--RAAAEEAERIRREAEAEADRLRGEA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2204 TEAARQ-RGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAAR-----LSVAAQEA 2277
Cdd:NF041483 414 ADQAEQlKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARtaeelLTKAKADA 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2278 ARLRQLAEEDLAQQRALA-EKMLKEKMQAVQEATRLKAEAELLQQQkelAQEQARRLQEDKEQMAQQLAQETQGFQKTLE 2356
Cdd:NF041483 494 DELRSTATAESERVRTEAiERATTLRRQAEETLERTRAEAERLRAE---AEEQAEEVRAAAERAARELREETERAIAARQ 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2357 TERQRQLE-MSAEAERlRLRVAEMSRAQARAEedARRFRKQAEDIGERLyRTELAtqekvmlvQTLETQRQQSDRDAERL 2435
Cdd:NF041483 571 AEAAEELTrLHTEAEE-RLTAAEEALADARAE--AERIRREAAEETERL-RTEAA--------ERIRTLQAQAEQEAERL 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2436 R-EAIAELEHEkdKLKQEAQLLQLKSEEMQtvRQEQLLQETQALQQSFLSEKDSLLQRercIEQEKAKleqlfqdevaka 2514
Cdd:NF041483 639 RtEAAADASAA--RAEGENVAVRLRSEAAA--EAERLKSEAQESADRVRAEAAAAAER---VGTEAAE------------ 699
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2515 qalreeqqrqqqqmqqekqQLAASMEEARRRQHEAEEGVRRQQEEL-QRLAQQQQQQEKLLAEENQRLRE 2583
Cdd:NF041483 700 -------------------ALAAAQEEAARRRREAEETLGSARAEAdQERERAREQSEELLASARKRVEE 750
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1397-1534 |
3.58e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1397 EAQEQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGA---------EGELQA 1464
Cdd:COG1579 21 RLEHRLKELPAELAELEDelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1465 LRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEE 1534
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1665-1887 |
3.93e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.90 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1665 KAEEQAVRQRELAEQELEK-QRQLAEgtaqqrlaAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRE-LEA 1742
Cdd:COG1842 16 ALLDKAEDPEKMLDQAIRDmEEDLVE--------ARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREdLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1743 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVL 1822
Cdd:COG1842 88 EALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 1823 AEklaaiseatrlkteAEIALKEKEAENERLRRLAEDEAFQRRLLEeqaAQHKADIEARLAQLRK 1887
Cdd:COG1842 168 ER--------------MEEKIEEMEARAEAAAELAAGDSLDDELAE---LEADSEVEDELAALKA 215
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1374-1568 |
4.04e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 50.02 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1374 EREAQGLQRRMQEEVarreEVAVEAQEQKRSIQEELQhlrqsseaEIQAKARqveaAERSRL--RIE-EEIRVVRLQLEA 1450
Cdd:PTZ00491 643 ERTRDSLQKSVQLAI----EITTKSQEAAARHQAELL--------EQEARGR----LERQKMhdKAKaEEQRTKLLELQA 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1451 TerqrgGAEGELQAlRARAE-EAEAQKRQAQEEAErlrrqVQDETQRKRqaeaelALRVQAEAEAAREKQRALQALEELR 1529
Cdd:PTZ00491 707 E-----SAAVESSG-QSRAEaLAEAEARLIEAEAE-----VEQAELRAK------ALRIEAEAELEKLRKRQELELEYEQ 769
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1920237970 1530 LQAE---EAERRLRQAEAERARQVQVAL--ETAQRSAEA--ELQSE 1568
Cdd:PTZ00491 770 AQNEleiAKAKELADIEATKFERIVEALgrETLIAIARAgpELQAK 815
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
937-1507 |
4.05e-05 |
|
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: 50.12 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 937 DRLQAEREYGSCSRHYQQLLQSLEQGEQEESrcqrcISELKDIRL-QLEACETRTVHRLRlpldkepaRECAQRITEQQK 1015
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADLHKREKELS-----LEKEQNKRLwDRDTGNSITIDHLR--------RELDDRNMEVQR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1016 AQAEVDGL-----GKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEE 1090
Cdd:pfam15921 431 LEALLKAMksecqGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKER 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1091 VlraheeqlkeaqavpatlpeLEATKAALKKLRAQAEAQQPVFDALRDE---LRGAQEVGERLQQRHGERDVEVERWRER 1167
Cdd:pfam15921 511 A--------------------IEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQ 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1168 VTLLLE-------RWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLR--DAKQRQEQIQAVPLANSQAvrEQLRQE 1238
Cdd:pfam15921 571 IENMTQlvgqhgrTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRelEARVSDLELEKVKLVNAGS--ERLRAV 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1239 KALLEDIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQsgsesiiqeyvdLRTRYSELSTLTS 1318
Cdd:pfam15921 649 KDIKQERDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ------------LKSAQSELEQTRN 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1319 qyirfiseTLRRMEEEERLAeqqraeererlaeVEAALEKQRQLAEAHAQAKAqaereaqglqrrMQEEVARREEVAVEA 1398
Cdd:pfam15921 714 --------TLKSMEGSDGHA-------------MKVAMGMQKQITAKRGQIDA------------LQSKIQFLEEAMTNA 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1399 QEQKRSIQEELQHLRQsseaeiqakarqveaaersrlrieeeirvvRLQLEATERQRggAEGELQALRA---RAEEAEAQ 1475
Cdd:pfam15921 761 NKEKHFLKEEKNKLSQ------------------------------ELSTVATEKNK--MAGELEVLRSqerRLKEKVAN 808
|
570 580 590
....*....|....*....|....*....|..
gi 1920237970 1476 KRQAQEEAERLRRQVQDETQRKRQAEAELALR 1507
Cdd:pfam15921 809 MEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
30-150 |
4.27e-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: 46.14 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 30 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSSRLPREKGRMRfhKLQNVQIA 109
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIK---VPVDWNRVNKPPYPKLGENMK--KLENCNYA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1920237970 110 LDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 150
Cdd:cd21330 82 VELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1086-1585 |
4.31e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1086 QEAEEVLRAHEEQlkeaQAVPATLPELEATKAALKK-LRAQAEAQQpvfdaLRDELRGAQEVG-------ERLQQRHGER 1157
Cdd:PRK04863 496 DVARELLRRLREQ----RHLAEQLQQLRMRLSELEQrLRQQQRAER-----LLAEFCKRLGKNlddedelEQLQEELEAR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1158 ----DVEVERWRERVTLLlerwQAVLAQTDVRQRELEQLGRQLRYYRESADPL----GAWLRDAKQRQEQIQ--AVPLAN 1227
Cdd:PRK04863 567 leslSESVSEARERRMAL----RQQLEQLQARIQRLAARAPAWLAAQDALARLreqsGEEFEDSQDVTEYMQqlLERERE 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1228 SQAVREQLRQEK-ALLEDIER----HGEKVEECQRFAKQ-------------------YINA-------------IKDYE 1270
Cdd:PRK04863 643 LTVERDELAARKqALDEEIERlsqpGGSEDPRLNALAERfggvllseiyddvsledapYFSAlygparhaivvpdLSDAA 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1271 LQLVT--------YKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSelstltsqyiRFISETL-RRMEEEERLAEQQ 1341
Cdd:PRK04863 723 EQLAGledcpedlYLIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYS----------RFPEVPLfGRAAREKRIEQLR 792
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1342 RaeERERLAEveaalekqrqlaeahaqAKAQAEREAQGLQRRMQE---------EVARREEVAVEAQEQKRSIQEELQHL 1412
Cdd:PRK04863 793 A--EREELAE-----------------RYATLSFDVQKLQRLHQAfsrfigshlAVAFEADPEAELRQLNRRRVELERAL 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1413 RQSSEAEIQAKARQVEAAERSRL--------------RIEEEIRVVRLQLEATE------RQRGGA----EGELQALRAR 1468
Cdd:PRK04863 854 ADHESQEQQQRSQLEQAKEGLSAlnrllprlnlladeTLADRVEEIREQLDEAEeakrfvQQHGNAlaqlEPIVSVLQSD 933
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1469 AEEAEAQKR---QAQEEAERLRRQVQDET---QRKRQAEAELALRVQAEAEAAREKQRalQALEELRLQAEEAERRLRQA 1542
Cdd:PRK04863 934 PEQFEQLKQdyqQAQQTQRDAKQQAFALTevvQRRAHFSYEDAAEMLAKNSDLNEKLR--QRLEQAEQERTRAREQLRQA 1011
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1920237970 1543 EAERARQVQValetaqrsaEAELQSEHASFAEKTAQLERTLKE 1585
Cdd:PRK04863 1012 QAQLAQYNQV---------LASLKSSYDAKRQMLQELKQELQD 1045
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3337-3375 |
4.51e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 43.09 E-value: 4.51e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1920237970 3337 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTATLL 3375
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3337-3372 |
4.77e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.77e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1920237970 3337 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTA 3372
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1390-1743 |
4.84e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1390 RREEVAVEAQEQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1469
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1470 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQ 1549
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1550 VQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEAL 1629
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1630 RLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1709
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 1920237970 1710 EQGEQQRQLLEEELARLQREAAAATQKRRELEAE 1743
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
849-1499 |
4.94e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.97 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 849 NQEAQEAIARlEAQHQALVALWhQLHTEMKSLLAWQSLGRDMQlirsWSLATFRTLKPEE------------QRQALRsL 916
Cdd:TIGR00618 223 VLEKELKHLR-EALQQTQQSHA-YLTQKREAQEEQLKKQQLLK----QLRARIEELRAQEavleetqerinrARKAAP-L 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 917 ELHYQAFLRDSQDAGGFGPEDRLQaEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRL 996
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 997 PLDKEPARECAQRIT----EQQKAQAEVDGLGKGVARLSAEAEKVLALPEPSPAAptlRSELELTLGKLEQVRSLSAIYL 1072
Cdd:TIGR00618 375 HTLTQHIHTLQQQKTtltqKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHA---KKQQELQQRYAELCAAAITCTA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1073 EKLKtisLVIRSTQEAEEVLRAHEEQLKEAQAVpaTLPELEATKAALKKLRAQAEAQQPVFDALR---------DELRGA 1143
Cdd:TIGR00618 452 QCEK---LEKIHLQESAQSLKEREQQLQTKEQI--HLQETRKKAVVLARLLELQEEPCPLCGSCIhpnparqdiDNPGPL 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1144 QEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLgawlrdakqRQEQIQAV 1223
Cdd:TIGR00618 527 TRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL---------QNITVRLQ 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1224 PLansqaVREQLRQEKALLEDIERHGEKVEECQRFAK--QYINAIKDYELQLVTYKAQLEpvASPAKKPKVQSGSESIIQ 1301
Cdd:TIGR00618 598 DL-----TEKLSEAEDMLACEQHALLRKLQPEQDLQDvrLHLQQCSQELALKLTALHALQ--LTLTQERVREHALSIRVL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1302 EYVDLRTRYSELSTLTSQY--IRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQG 1379
Cdd:TIGR00618 671 PKELLASRQLALQKMQSEKeqLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1380 LQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAE 1459
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEE 830
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1920237970 1460 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQ 1499
Cdd:TIGR00618 831 EQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
940-1378 |
4.97e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 940 QAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACE-----TRTVHRLRLPLDKEPAR--ECAQRITE 1012
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAELPERleELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1013 QQKAQAEVDGLGKGVARLSAEAEKVLALPEPSpaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVL 1092
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLA-----TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1093 R------AHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRE 1166
Cdd:COG4717 233 EneleaaALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1167 RVTLLLERWQAVLAQTDVRQREleqlgrQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEkALLEDIE 1246
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDL------SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE-AGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1247 RHGEKVEECQRFaKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELstltSQYIRFISE 1326
Cdd:COG4717 386 ELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL----REELAELEA 460
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 1327 TLRRMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQ 1378
Cdd:COG4717 461 ELEQLEEDGELAEllQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1338-1735 |
4.99e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 49.27 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1338 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEElqhlrqsse 1417
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAE--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1418 aeiqaKARQVEAAERSRLRIEEEIRvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1497
Cdd:COG3064 75 -----AAKKLAEAEKAAAEAEKKAA------AEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1498 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTA 1577
Cdd:COG3064 144 AEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1578 QLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAE 1657
Cdd:COG3064 224 RAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAAL 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237970 1658 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQ 1735
Cdd:COG3064 304 AAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLA 381
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1324-1548 |
5.03e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.48 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1324 ISETLRRMEEEERLAEQQRAEERERLAEVEAAlEKQRQLAEAHAQAKAQAEREAQglqRRMQEEVARREEVavEAQEQKR 1403
Cdd:pfam02029 100 VAERKENNEEEENSSWEKEEKRDSRLGRYKEE-ETEIREKEYQENKWSTEVRQAE---EEGEEEEDKSEEA--EEVPTEN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1404 SIQEELQHLRQSSEAEIQAKARQVEaaERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKrQAQEEA 1483
Cdd:pfam02029 174 FAKEEVKDEKIKKEKKVKYESKVFL--DQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFL-EAEQKL 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 1484 ERLRRQVQD------ETQRKRQAEAELALrvqAEAEAAREKQRAL--------QALEELRLQAEEAERRLRQAEAERAR 1548
Cdd:pfam02029 251 EELRRRRQEkeseefEKLRQKQQEAELEL---EELKKKREERRKLleeeeqrrKQEEAERKLREEEEKRRMKEEIERRR 326
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1504-1773 |
5.29e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1504 LALRVQAEAEAAREKQRALQALEElRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTL 1583
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1584 KEEHVAVVQLREeatrraqqqaeaeRARAEAERELERWQLKANEALRLRLQAEEVAQqksltqaeaekqKEEAEREARRR 1663
Cdd:COG4942 90 KEIAELRAELEA-------------QKEELAELLRALYRLGRQPPLALLLSPEDFLD------------AVRRLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1664 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAE 1743
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
250 260 270
....*....|....*....|....*....|
gi 1920237970 1744 LAKVRAEMEVLLASKARAEEESRSTSEKSK 1773
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4123-4151 |
5.47e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 5.47e-05
10 20
....*....|....*....|....*....
gi 1920237970 4123 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4151
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1634-1810 |
5.85e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1634 QAEEVAQQKsltQAEAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1709
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1710 EQGEQQRQLLEEELArlQREAAAATQKRRELEA-----ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfr 1784
Cdd:PRK09510 161 KKAAAEAKKKAEAEA--AKKAAAEAKKKAEAEAaakaaAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEA---- 234
|
170 180
....*....|....*....|....*.
gi 1920237970 1785 ELAEEAARLRALAEEAKRQRQLAEED 1810
Cdd:PRK09510 235 KAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1072-1540 |
5.87e-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: 49.35 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1072 LEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKAALkklraQAEAQQpVFDALRDELRGAQEVGERLQ 1151
Cdd:pfam05557 51 QELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQ-----LADARE-VISCLKNELSELRRQIQRAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1152 QRHGERDVEVERWRERVTLLLERWQAV---LAQTDVRQREL---EQLGRQLRYYRESADPLGAWLRDAKQRQEQIqavpl 1225
Cdd:pfam05557 125 LELQSTNSELEELQERLDLLKAKASEAeqlRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELARI----- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1226 ANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKK------------PKVQ 1293
Cdd:pfam05557 200 PELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSwvklaqdtglnlRSPE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1294 SGSESIIQEYVDLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQL---------- 1362
Cdd:pfam05557 280 DLSRRIEQLQQREIVLKEENSSLTSS-ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlQRRVllltkerdgy 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1363 ------------AEAHAQAKAQAEREAQGLQRRMQ---EEVARREEVAVEA----QEQKRSIQEELQHLRQ--------S 1415
Cdd:pfam05557 359 railesydkeltMSNYSPQLLERIEEAEDMTQKMQahnEEMEAQLSVAEEElggyKQQAQTLERELQALRQqesladpsY 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1416 SEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ--DE 1493
Cdd:pfam05557 439 SKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIErlKR 518
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1920237970 1494 TQRKRQAEAELALRVQAEAEAAREKQralqaLEELRLQAEEAERRLR 1540
Cdd:pfam05557 519 LLKKLEDDLEQVLRLPETTSTMNFKE-----VLDLRKELESAELKNQ 560
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
184-261 |
6.06e-05 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 44.60 E-value: 6.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237970 184 DNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 261
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1688-2184 |
6.18e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 49.47 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1688 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV----------RAEMEVLLAS 1757
Cdd:COG3899 737 PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYAnlgllllgdyEEAYEFGELA 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1758 KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKT 1837
Cdd:COG3899 817 LALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1838 EAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILAL 1917
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1918 KGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 1997
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1998 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAA 2077
Cdd:COG3899 1057 AAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALL 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2078 EEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKH 2157
Cdd:COG3899 1137 LLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
490 500
....*....|....*....|....*..
gi 1920237970 2158 KQFAEQALRQKAQVEQELTALRLQLEE 2184
Cdd:COG3899 1217 LEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2144-2594 |
6.42e-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: 49.45 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2144 LRQKQAADAEMEKHKQFA--EQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQ-RGQVEEELFSL 2220
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTklQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTlDDQWKEKRDEL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2221 R----VQMEELGKLKARIEA-ENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAA---------RLRQLAEE 2286
Cdd:pfam12128 307 NgelsAADAAVAKDRSELEAlEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKhqdvtakynRRRSKIKE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2287 DLA------QQRALAEKMLKEKMQAVQEATRLKAEAEL---LQQQKELAQEQARRLQEDKEQMAQQLAQETQGfQKTLET 2357
Cdd:pfam12128 387 QNNrdiagiKDKLAKIREARDRQLAVAEDDLQALESELreqLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2358 ERQRQLEMSAEAERLRLRVAEMSRAQaraeEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQ-RQQSDRDAERLR 2436
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQ----SELRQARKRRDQASEALRQASRRLEERQSALDELELQlFPQAGTLLHFLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2437 EAIAELEHEKDKLKQEAQL----LQLKSEEMQTVRQEQLLQETQALQQSflsEKDSLLQRERCIEQEKAKLEQLFQDEVA 2512
Cdd:pfam12128 542 KEAPDWEQSIGKVISPELLhrtdLDPEVWDGSVGGELNLYGVKLDLKRI---DVPEWAASEEELRERLDKAEEALQSARE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2513 KAQALreeqqrqqqqmQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLA----QQQQQQEKLLAEENQRLRERLQHL 2588
Cdd:pfam12128 619 KQAAA-----------EEQLVQANGELEKASREETFARTALKNARLDLRRLFdekqSEKDKKNKALAERKDSANERLNSL 687
|
....*.
gi 1920237970 2589 EEERRA 2594
Cdd:pfam12128 688 EAQLKQ 693
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1324-1529 |
6.58e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.51 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1324 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVAR-REEVAVEAQEQK 1402
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgREDLAREALERK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1403 RSIQEELQHLRQsseaeiqakarQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQALRARAEEAEAQKR----- 1477
Cdd:COG1842 94 AELEAQAEALEA-----------QLAQLEEQVEKLKEALRQLESKLEELKAKK-------DTLKARAKAAKAQEKvneal 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1478 ------QAQEEAERLRRQVqDETQRKRQAEAELALR--VQAEAEAAREKQRALQALEELR 1529
Cdd:COG1842 156 sgidsdDATSALERMEEKI-EEMEARAEAAAELAAGdsLDDELAELEADSEVEDELAALK 214
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1811-2022 |
7.04e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1811 AVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIeARLAQLRKASE 1890
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-AELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1891 SELERQKGLVEDTL----RQRRQVEEEILALKGSFEKAAAGKA-------ELELELGRIRGTAEDTLRSKEQAEQEAARQ 1959
Cdd:COG4942 97 AELEAQKEELAELLralyRLGRQPPLALLLSPEDFLDAVRRLQylkylapARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237970 1960 RQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQ 2022
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3118-3154 |
7.07e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 7.07e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1920237970 3118 LRLLDAQLSTGGIVDPSKSHRVPLDVACARGYLDKET 3154
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1415-1628 |
7.14e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1415 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD-- 1492
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1493 -ETQRKRQAEAELAL------------RVQAEAEAAREKQRALQALEELRLQAEEAerrlrQAEAERARQVQVALETAQR 1559
Cdd:COG3883 93 rALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAK-----KAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 1560 SAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEA 1628
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1814-2204 |
7.25e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1814 QRAEAERVLAEKLAAIsEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRLLEEQAAqhkadIEARLAQLRKASESEL 1893
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAA-----IYAEQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1894 ERQKglVEDTLRQRRQVEEEilalkgsfekaaagkaELELELGRIRGTaeDTLRSKEQAEQEAARQRqlaaeeerrrrea 1973
Cdd:pfam17380 351 ERIR--QEERKRELERIRQE----------------EIAMEISRMREL--ERLQMERQQKNERVRQE------------- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1974 EERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR-ERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKeqel 2052
Cdd:pfam17380 398 LEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLRQQEEERK---- 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2053 qqtlqqeqsvleRLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQE 2132
Cdd:pfam17380 474 ------------RKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEE 541
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 2133 aarraqaeqaalRQKQaadAEMEKHKQFAEQALRqkaqVEQELTALRLQLEETDHQKSILDEELQRLKAEVT 2204
Cdd:pfam17380 542 ------------RRKQ---QEMEERRRIQEQMRK----ATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2256-2391 |
7.56e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 48.72 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2256 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARRLQE 2335
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 2336 DKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDAR 2391
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAE 328
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1295-1597 |
7.92e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.53 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1295 GSESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAaLEKQ--------RQLAEAH 1366
Cdd:pfam19220 63 AYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEA-LERQlaaeteqnRALEEEN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1367 AQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRsiqeeLQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRL 1446
Cdd:pfam19220 142 KALREEAQAAEKALQRAEGELATARERLALLEQENRR-----LQALSEEQAAELAELTRRLAELETQLDATRARLRALEG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1447 QL--EATERQRGGAEGELQALRARAEEAEAQKRQaqeEAERLRRQVQDetqrkrQAEAELALRVQAEAEAAREKQRalqA 1524
Cdd:pfam19220 217 QLaaEQAERERAEAQLEEAVEAHRAERASLRMKL---EALTARAAATE------QLLAEARNQLRDRDEAIRAAER---R 284
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 1525 LEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSE--HASFAEKTAQLERTlkEEHVAVVQLREEA 1597
Cdd:pfam19220 285 LKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEmlTKALAAKDAALERA--EERIASLSDRIAE 357
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1391-1551 |
7.92e-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: 48.98 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1391 REEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAE 1470
Cdd:pfam07111 490 RNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELT 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1471 EAEAQKRQAQEEA-----ERLRRQVQDETQ-----RKRQAEAELALRvQAEAEAAREKQRAlqalEELRLQAEEAerrlR 1540
Cdd:pfam07111 570 QQQEIYGQALQEKvaeveTRLREQLSDTKRrlneaRREQAKAVVSLR-QIQHRATQEKERN----QELRRLQDEA----R 640
|
170
....*....|..
gi 1920237970 1541 QAEAER-ARQVQ 1551
Cdd:pfam07111 641 KEEGQRlARRVQ 652
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1459-1593 |
8.43e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 47.83 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1459 EGELQALRARAEEAEAQkrqAQEEAERLRRQVQDetqRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERR 1538
Cdd:pfam09787 67 RGQIQQLRTELQELEAQ---QQEEAESSREQLQE---LEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1539 LRQAEAERARQ-VQVALETAQRSAEAELQSE-HA---SFAEKTAQLERTLKEEHVAVVQL 1593
Cdd:pfam09787 141 IKDREAEIEKLrNQLTSKSQSSSSQSELENRlHQlteTLIQKQTMLEALSTEKNSLVLQL 200
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2163-2390 |
8.64e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2163 QALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKL--KARIEAENRA 2240
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEieERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2241 LVLRDKDSAQRLLQE--EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2318
Cdd:COG3883 93 RALYRSGGSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 2319 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDA 2390
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1674-2386 |
9.08e-05 |
|
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: 48.96 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1674 RELAEQELEKQRQLAEGTAQQRLAAE---QELIRLRAETEQGEQQRQLLEEELARLQ-REAAAATQK-RRELEAELA--- 1745
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMHfRSLGSAISKiLRELDTEISylk 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1746 ----KVRAEMEVLLA-SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAER 1820
Cdd:pfam15921 238 grifPVEDQLEALKSeSQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1821 VLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQL-----RKASESELER 1895
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhKREKELSLEK 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1896 QK-----------GLVEDTLRQR---RQVEEEIL-ALKGSFEKAAAGkaELELELGRIRGtaedtlrSKEQAEQEAARQR 1960
Cdd:pfam15921 398 EQnkrlwdrdtgnSITIDHLRRElddRNMEVQRLeALLKAMKSECQG--QMERQMAAIQG-------KNESLEKVSSLTA 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1961 QLAAEEERRRREAEERVQKSLAAE--EEAARQRKAALEEVER-LKAKVEEARRLRERAEQesarQLQLAQEaaqkrLQAE 2037
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLEssERTVSDLTASLQEKERaIEATNAEITKLRSRVDL----KLQELQH-----LKNE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2038 EKaHAFAVQQKEQELQQTLQQEQSVLERLRseaeaarraaeeaeaareraereaaqsrRQVEEAERLkqsaeeqaqaqaq 2117
Cdd:pfam15921 540 GD-HLRNVQTECEALKLQMAEKDKVIEILR----------------------------QQIENMTQL------------- 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2118 aqaaaeklrkeaeqeaarraqaeqaalrqkqaadaeMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQ 2197
Cdd:pfam15921 578 ------------------------------------VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIR 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2198 RLKAEVTEAARQRGQV----EEELFSLRVQMEELGKLKARIEAENRAL--VLRDKDSAQRLLQEEAEKMKQVAEE-AARL 2270
Cdd:pfam15921 622 ELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKRNFRNKSEEMETTTNKlKMQL 701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2271 SVAAQEAARLR---QLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAqe 2347
Cdd:pfam15921 702 KSAQSELEQTRntlKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELS-- 779
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1920237970 2348 tqgfqkTLETERQR---QLE-MSAEAERLRLRVAEMSRAQARA 2386
Cdd:pfam15921 780 ------TVATEKNKmagELEvLRSQERRLKEKVANMEVALDKA 816
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1861-2386 |
9.89e-05 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 49.10 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1861 AFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEkAAAGKAELELELGRIRG 1940
Cdd:COG3321 867 PFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAA-LLALVALAAAAAALLAL 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1941 TAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2020
Cdd:COG3321 946 AAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALA 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2021 RQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEE 2100
Cdd:COG3321 1026 ALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAA 1105
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2101 AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRL 2180
Cdd:COG3321 1106 LLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAAL 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2181 QLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEElgklkARIEAENRALVLRDKDSAQRLLQEEAEKM 2260
Cdd:COG3321 1186 AAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAA-----ALALLALAAAAAAVAALAAAAAALLAALA 1260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2261 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2340
Cdd:COG3321 1261 ALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAA 1340
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1920237970 2341 AQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARA 2386
Cdd:COG3321 1341 LALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1498-1782 |
1.07e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.41 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1498 RQAEAELALRVQAEAEAAREKQR--ALQAleelRLQAEEAER--RLRQAEAERARQVQVALETAQRSAEAELQSEHASFA 1573
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARfeARQA----RLEREKAAReaRHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1574 EKTAQlertlKEEHVAVVQLREEATRRAQQQAEAERARAEAERelerwQLKANEALRLRLQAEEVAQQKSLTqaeAEKQK 1653
Cdd:PRK05035 508 IKAGA-----RPDNSAVIAAREARKAQARARQAEKQAAAAADP-----KKAAVAAAIARAKAKKAAQQAANA---EAEEE 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1654 EEAEREARRRGKAEEQAvrqRELAEQELEKQRQLAEGTAQQRLAAEQELIrLRAETEQGEQQRQLLEEElarlqreaaAA 1733
Cdd:PRK05035 575 VDPKKAAVAAAIARAKA---KKAAQQAASAEPEEQVAEVDPKKAAVAAAI-ARAKAKKAEQQANAEPEE---------PV 641
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1920237970 1734 TQKRRELEAELAKVRAEmevlLASKARAEEESRSTSEKSKQRLEAEAGR 1782
Cdd:PRK05035 642 DPRKAAVAAAIARAKAR----KAAQQQANAEPEEAEDPKKAAVAAAIAR 686
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1809-2287 |
1.08e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1809 EDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLleEQAAQHKADIEARLAQLRKA 1888
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL--EALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1889 seselerqkglvedtLRQRRQVEEEILALKgsfEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEER 1968
Cdd:COG4717 155 ---------------LEELRELEEELEELE---AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1969 RRREAEervqKSLAAEEEAARQRKAALEEVERLKakveearRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQK 2048
Cdd:COG4717 217 EAQEEL----EELEEELEQLENELEAAALEERLK-------EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2049 EQELQQTLQQEQSVLERLRseaeaarraaeeaEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKE 2128
Cdd:COG4717 286 LALLFLLLAREKASLGKEA-------------EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2129 AEQEAARRAQAEQAALRQKQAADaeMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQ-KSILDEELQRLKAEVTEAA 2207
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAAL--LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEEL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2208 RQR-GQVEEELFSLRVQMEELGKLKARIEAENRAlvLRDKDSAQRLLQEEAE---KMKQVAEEAARLSVAAQEAARLRQL 2283
Cdd:COG4717 431 EEElEELEEELEELEEELEELREELAELEAELEQ--LEEDGELAELLQELEElkaELRELAEEWAALKLALELLEEAREE 508
|
....
gi 1920237970 2284 AEED 2287
Cdd:COG4717 509 YREE 512
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1986-2291 |
1.11e-04 |
|
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: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1986 EAARQRKAALEEVERLKAKVEEARRLRER----AEQESARQLQLAQEAA----QKRLQAEEKAHAFAVQQKEQELQqtlq 2057
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERrrklEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEERKRE---- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2058 qeqsvLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERlKQSAEEQAQAQAQAQAAAEKLRKEAEQEAArra 2137
Cdd:pfam17380 362 -----LERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR-KVKILEEERQRKIQQQKVEMEQIRAEQEEA--- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2138 qaeqaalRQKQAADAEMEKHKQFaEQALRQKAQVEQELTALRLQLEETDHQKSILD---------EELQRLKAEVTEAAR 2208
Cdd:pfam17380 433 -------RQREVRRLEEERAREM-ERVRLEEQERQQQVERLRQQEEERKRKKLELEkekrdrkraEEQRRKILEKELEER 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2209 QRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEE--AEKMKQVAEEAARLSVAAQEAARLRQLAEE 2286
Cdd:pfam17380 505 KQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRriQEQMRKATEERSRLEAMEREREMMRQIVES 584
|
....*
gi 1920237970 2287 DLAQQ 2291
Cdd:pfam17380 585 EKARA 589
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1668-2378 |
1.20e-04 |
|
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: 48.56 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1668 EQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR-----LQREAAAATQKRRELEA 1742
Cdd:pfam05483 98 EAELKQKENKLQENRKIIE-AQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnlLKETCARSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1743 ELAKVR---AEMEVLLASKARAEEESRSTSEKSkqRLEAEAgrfrELAEEAARLRALAEEAKRQRQlaeedavrqraEAE 1819
Cdd:pfam05483 177 EREETRqvyMDLNNNIEKMILAFEELRVQAENA--RLEMHF----KLKEDHEKIQHLEEEYKKEIN-----------DKE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1820 RVLAEKLAAISEATRLKTEAEIALKEKEaenERLRRLAEDEAFQRRLLEeQAAQHKADIEARLAQLRKASESELERQKGL 1899
Cdd:pfam05483 240 KQVSLLLIQITEKENKMKDLTFLLEESR---DKANQLEEKTKLQDENLK-ELIEKKDHLTKELEDIKMSLQRSMSTQKAL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1900 VED---TLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEerrrreaeer 1976
Cdd:pfam05483 316 EEDlqiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME---------- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1977 VQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ--ESARQLQLAQEAAQKRLQAEEK-AHAFAVQqkeqeLQ 2053
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQELIFLLQAREKeIHDLEIQ-----LT 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2054 QTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLkqsaeeqaqaqaqaqaaaeklrkeaeqea 2133
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDM----------------------------- 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2134 arraqaeQAALRQKQAadaEMEKHKQFAEQALRQKAQVEQELTALRLQLE--------ETDHQKSILD---EELQRLKAE 2202
Cdd:pfam05483 512 -------TLELKKHQE---DIINCKKQEERMLKQIENLEEKEMNLRDELEsvreefiqKGDEVKCKLDkseENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2203 VTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEeaarLSVAAQEAARLRQ 2282
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE----LASAKQKFEEIID 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2283 LAEEDLAQQRALAEKMLKEKMQA---VQEATRLKAEAELLQQQK--------ELAQEQARRLQEDKEQ---MAQQLAQET 2348
Cdd:pfam05483 658 NYQKEIEDKKISEEKLLEEVEKAkaiADEAVKLQKEIDKRCQHKiaemvalmEKHKHQYDKIIEERDSelgLYKNKEQEQ 737
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1920237970 2349 QGFQKTLETER----------QRQLEMS-AEAERLRLRVAE 2378
Cdd:pfam05483 738 SSAKAALEIELsnikaellslKKQLEIEkEEKEKLKMEAKE 778
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
27-144 |
1.22e-04 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 45.35 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 27 YKDErdrvQKKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRLPrekgr 97
Cdd:cd21292 21 YSEE----EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTID-ERAINKKKLTV----- 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237970 98 mrFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 144
Cdd:cd21292 91 --FTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
26-143 |
1.23e-04 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 44.57 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 26 KYKDERDRVQKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLpreRDVirsSRLPREKGRMrfhkL 103
Cdd:cd21285 2 KSWEAENGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKI---EDI---NGCPKNRSQM----I 71
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1920237970 104 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTI 143
Cdd:cd21285 72 ENIDACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1470-1549 |
1.24e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 48.41 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1470 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAE------AEAAREKQRALQA-LEELRLQAEEAERRLRQA 1542
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELvaleglAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 1920237970 1543 EAERARQ 1549
Cdd:PRK11448 218 RKEITDQ 224
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1472-1597 |
1.38e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1472 AEAQKRQAQEEAERLRRQVQDETQRKRQAEaELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLR----QAEAERA 1547
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAE-ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAAlkqkQAEEAAA 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1548 RQVQVA----------LETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEA 1597
Cdd:PRK09510 140 KAAAAAkakaeaeakrAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA 199
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1144-1549 |
1.39e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1144 QEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAV 1223
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETL 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1224 planSQAVREQLRQEKALLED---IERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSE--- 1297
Cdd:TIGR00606 774 ----LGTIMPEEESAKVCLTDvtiMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIElnr 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1298 SIIQEYVD-LRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQR---------AEERERLAEVEAALEKQRQLAEAHA 1367
Cdd:TIGR00606 850 KLIQDQQEqIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTevqslireiKDAKEQDSPLETFLEKDQQEKEELI 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1368 QAKAQAEREAQGLQRRMQEEVarrEEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQ 1447
Cdd:TIGR00606 930 SSKETSNKKAQDKVNDIKEKV---KNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQD 1006
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1448 LEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALrvqaeaeAAREKQRALQALEE 1527
Cdd:TIGR00606 1007 IDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDL-------IKRNHVLALGRQKG 1079
|
410 420
....*....|....*....|..
gi 1920237970 1528 LRLQAEEAERRLRQAEAERARQ 1549
Cdd:TIGR00606 1080 YEKEIKHFKKELREPQFRDAEE 1101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1985-2598 |
1.44e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1985 EEAARQRKAALEEVERLKAKVEEARRlreraeqeSARQLQLAQEAAQKRLQAEEKAhafavqqkeqelqqtlqqeqSVLE 2064
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDARE--------QIELLEPIRELAERYAAARERL--------------------AELE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2065 RLRSEAEAARRAAEEAEAARERAEREAAQSRRQvEEAERLKQsaeeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAAL 2144
Cdd:COG4913 276 YLRAALRLWFAQRRLELLEAELEELRAELARLE-AELERLEA-----------------RLDALREELDELEAQIRGNGG 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2145 RQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETdhqKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQM 2224
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2225 EELGKLKARIEAENRALVLRDKDSAQRLLQeeaekMKQVAEEAARLS-VAAQEAARLRQLAEEDLAQQRAlAEKML---- 2299
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKSNIPARLLA-----LRDALAEALGLDeAELPFVGELIEVRPEEERWRGA-IERVLggfa 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2300 ------KEKMQAVQEAT-RLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETE--RQRQLEMSAEAE 2370
Cdd:COG4913 489 ltllvpPEHYAAALRWVnRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAElgRRFDYVCVDSPE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2371 RLRLRVAEMSRA-QARAeeDARRFRKQAEDIGERLYRTELATQEKvmlVQTLETQRQQSDRDAERLREAIAELEHEKDKL 2449
Cdd:COG4913 569 ELRRHPRAITRAgQVKG--NGTRHEKDDRRRIRSRYVLGFDNRAK---LAALEAELAELEEELAEAEERLEALEAELDAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2450 KQEAQLLQ-LKSEEMQTVRQEQLLQETQALQQsflsekdsllQRERcIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQM 2528
Cdd:COG4913 644 QERREALQrLAEYSWDEIDVASAEREIAELEA----------ELER-LDASSDDLAAL-EEQLEELEAELEELEEELDEL 711
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237970 2529 QQEKQQLAASMEEARRRQHEAEEGVRRqQEELQRLAQQQQQQEKLLAEENQRLRERL-QHLEEERRAALAR 2598
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLEA-AEDLARLELRALLEERFAAALGDAVERELrENLEERIDALRAR 781
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1334-1563 |
1.46e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 47.67 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1334 EERLAEQQRAEERERLAEVEAAlEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELqhlr 1413
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHGA-EISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1414 qsSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1493
Cdd:PRK07735 86 --TEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1494 TQRKRQAEAELALrvqaeaEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEA 1563
Cdd:PRK07735 164 KAKAKAAAAAKAK------AAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGN 227
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3081-3117 |
1.48e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.48e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1920237970 3081 KLLSAEKAVTGYKDPYSGQSVSLFQALKKGLIPREQG 3117
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2167-2410 |
1.52e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.53 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2167 QKAQVEQELTALRLQleetdhQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDK 2246
Cdd:TIGR02794 44 DPGAVAQQANRIQQQ------KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2247 DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARlrQLAEEDLAQQRALAEKMLKE-KMQAVQEA-----TRLKAEAELLQ 2320
Cdd:TIGR02794 118 QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--QAEEEAKAKAAAEAKKKAEEaKKKAEAEAkakaeAEAKAKAEEAK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2321 QQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQaedI 2400
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA---I 272
|
250
....*....|
gi 1920237970 2401 GERLYRTELA 2410
Cdd:TIGR02794 273 QQNLYDDPSF 282
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2254-2352 |
1.55e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 47.19 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2254 QEEAEKMKQVAEEAARLSVAAQEAARL----RQLAEEDLAQQRALAE--KMLKEKMQavQEATRLKAEAELLQQQKElaQ 2327
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLLeeqqRELEQKLEDQERSYEEhlRQLKEKME--EERENLLKEQERALESKL--K 266
|
90 100
....*....|....*....|....*
gi 1920237970 2328 EQARRLQEDKEQMAQQLAQETQGFQ 2352
Cdd:cd16269 267 EQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1668-1863 |
1.59e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1668 EQAVRQRELAEQELEKQRQLAEgTAQQRLAA---EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1744
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1745 AKVRAEMEVLLASKA--------------RAEEESRSTSEKSK-QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1809
Cdd:COG3206 250 GSGPDALPELLQSPViqqlraqlaeleaeLAELSARYTPNHPDvIALRAQIAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 1810 DAVRQRAEAERVLAEKLAAIS-EATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 1863
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEaELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2160-2326 |
1.60e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 47.54 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2160 FAEQALrqkAQVEQELTALRLQLEETDHQKSILDEElqrlkAEVTEAARQRGQVEEELFSLRVQMEELgklkarieaenR 2239
Cdd:COG3524 181 FAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAAL-----------R 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2240 AlVLRDKDSAQRLLQEEAEKM-KQVAEEAARLSVAAQEAARLRQLAE-EDLAQQRALAEKMLKEKMQAVQEAtrlKAEAE 2317
Cdd:COG3524 242 S-YLSPNSPQVRQLRRRIAALeKQIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAALEQA---RIEAA 317
|
....*....
gi 1920237970 2318 llQQQKELA 2326
Cdd:COG3524 318 --RQQRYLA 324
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3953-3987 |
1.63e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.63e-04
10 20 30
....*....|....*....|....*....|....*
gi 1920237970 3953 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 3987
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1407-1781 |
1.63e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1407 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEAT----ERQRGGAEGELQALRARAEEAEAQKRQAQEE 1482
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQrrelESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1483 AERL---RRQVQDETQRKRQAEAELALRVQAEAEAAREKQralQALEELRLQAEEAERRLRQAEAERaRQVQVALETAQ- 1558
Cdd:pfam07888 110 SEELseeKDALLAQRAAHEARIRELEEDIKTLTQRVLERE---TELERMKERAKKAGAQRKEEEAER-KQLQAKLQQTEe 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1559 --RSAEAELQSEHASFAEKTAQLERtLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKAnEALRLRLqaE 1636
Cdd:pfam07888 186 elRSLSKEFQELRNSLAQRDTQVLQ-LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV-EGLGEEL--S 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1637 EVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR 1716
Cdd:pfam07888 262 SMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237970 1717 QLLEEELArlqREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSE---KSKQRLEAEAG 1781
Cdd:pfam07888 342 EKLEVELG---REKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEyirQLEQRLETVAD 406
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1297-1508 |
1.67e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1297 ESIIQEYVDLRTRYSelSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERL------AEVEAALEKQRQLAEAHAQAK 1370
Cdd:COG3206 155 NALAEAYLEQNLELR--REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlsEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1371 AQAeREAQGLQRRMQEEVARREEVAVEA-------------QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRI 1437
Cdd:COG3206 233 AEL-AEAEARLAALRAQLGSGPDALPELlqspviqqlraqlAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 1438 EEEIRVVRLQLEATERQRGGAEGELQALRARAE---EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRV 1508
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQRLEEARLAEALTV 385
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2161-2550 |
1.82e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2161 AEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVT--EAARQRGQVEEELFSLRVQMEELGKLKARIEAEN 2238
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2239 RALVlRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKekmQAVQEATRLKAEAEL 2318
Cdd:COG4717 156 EELR-ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE---EAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2319 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLET----------------------ERQRQLEMSAEAERLRLRV 2376
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSliltiagvlflvlgllallfllLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2377 AEMSRAQARAEEDARRFRKQAEDIGER---LYRTELATQEKVMLVQTLETQRQQSDRDAER---LREAIAELEHEKDKLK 2450
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEElleLLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2451 QEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQ 2530
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL 471
|
410 420
....*....|....*....|
gi 1920237970 2531 EKQQLAASMEEARRRQHEAE 2550
Cdd:COG4717 472 AELLQELEELKAELRELAEE 491
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2161-2595 |
1.85e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2161 AEQALRQKAQVEQELTALRLQL-------EETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLK-A 2232
Cdd:COG3096 524 LEQRLRQQQNAERLLEEFCQRIgqqldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApA 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2233 RIEAENRALVLRD------KDSA------QRLLQEE----------AEKMKQVAEEAARLSVAA-QEAARLRQLAE---- 2285
Cdd:COG3096 604 WLAAQDALERLREqsgealADSQevtaamQQLLEREreatverdelAARKQALESQIERLSQPGgAEDPRLLALAErlgg 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2286 -------EDLAQQRA-LAEKMLKEKMQA--VQEATRLKAEAE----------LLQQQKELAQEQARRLQEDKEQMAQQLA 2345
Cdd:COG3096 684 vllseiyDDVTLEDApYFSALYGPARHAivVPDLSAVKEQLAgledcpedlyLIEGDPDSFDDSVFDAEELEDAVVVKLS 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2346 QETQGFQKTLE------TERQRQLE-MSAEAERLRLRVAEMS---RAQARAEEDARRFrkqaedIGERLYRTELATQEKV 2415
Cdd:COG3096 764 DRQWRYSRFPEvplfgrAAREKRLEeLRAERDELAEQYAKASfdvQKLQRLHQAFSQF------VGGHLAVAFAPDPEAE 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2416 MlvQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQsflsEKDSLLQRERC 2495
Cdd:COG3096 838 L--AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELRE----ELDAAQEAQAF 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2496 IEQEKAKLEQLfqdeVAKAQALReeqqrqqqQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLA 2575
Cdd:COG3096 912 IQQHGKALAQL----EPLVAVLQ--------SDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLL 979
|
490 500
....*....|....*....|....
gi 1920237970 2576 EENQ----RLRERLQHLEEERRAA 2595
Cdd:COG3096 980 GENSdlneKLRARLEQAEEARREA 1003
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1699-1849 |
1.87e-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: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1699 EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRS-TSEKSKQRLE 1777
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvRNNKEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 1778 AE----AGRFRELAEEAARLRALAEEAKRQRQLAEEdavrQRAEAERVLAEKLAAISEATRlKTEAEIALKEKEAE 1849
Cdd:COG1579 96 KEieslKRRISDLEDEILELMERIEELEEELAELEA----ELAELEAELEEKKAELDEELA-ELEAELEELEAERE 166
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1781-2027 |
2.06e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1781 GRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDE 1860
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1861 AFQRRLLEEQAAQHKADIE------ARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELE 1934
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIReleediKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1935 LGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAeervqKSLAAEEEAARQRKAALEE-VERLKAKVEEARRLRE 2013
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN-----EALLEELRSLQERLNASERkVEGLGEELSSMAAQRD 268
|
250
....*....|....*
gi 1920237970 2014 RAEQESAR-QLQLAQ 2027
Cdd:pfam07888 269 RTQAELHQaRLQAAQ 283
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2165-2605 |
2.20e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2165 LRQKAQVEQ-ELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIeaenralvl 2243
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI--------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2244 RDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2323
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2324 ELAQEQARRLQEDKEQMAQQLAQET--QGFQKTLETERQRQLEMSAEAERLRlrvAEMSRAQARAEEDARRFRKQAEDIG 2401
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMdyNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2402 ERL--YRTELAT--QEKVMLVQTLETQRQQSD----------------------------RDAERLREAIAELEHEKDKL 2449
Cdd:PRK01156 416 VKLqdISSKVSSlnQRIRALRENLDELSRNMEmlngqsvcpvcgttlgeeksnhiinhynEKKSRLEEKIREIEIEVKDI 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2450 KQEAQLLQ-----LKSEEM-QTVRQEQLLQETQALQQSFLSE----KDSLLQRERCIEQEKA-KLEQLFQDEVAKAQALR 2518
Cdd:PRK01156 496 DEKIVDLKkrkeyLESEEInKSINEYNKIESARADLEDIKIKinelKDKHDKYEEIKNRYKSlKLEDLDSKRTSWLNALA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2519 EEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEG-----------VRRQQEELQRLaqqqqQQEKLLAEENQRLRERLQH 2587
Cdd:PRK01156 576 VISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGfpddksyidksIREIENEANNL-----NNKYNEIQENKILIEKLRG 650
|
490
....*....|....*...
gi 1920237970 2588 LEEERRAALARSEEIAPS 2605
Cdd:PRK01156 651 KIDNYKKQIAEIDSIIPD 668
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4262-4295 |
2.30e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.30e-04
10 20 30
....*....|....*....|....*....|....
gi 1920237970 4262 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4295
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2159-2605 |
2.30e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.21 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2159 QFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAEN 2238
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2239 RALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2318
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2319 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAE 2398
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2399 DIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQAL 2478
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2479 QQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQE 2558
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1920237970 2559 ELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIAPS 2605
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALA 522
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2364-2598 |
2.54e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2364 EMSAEAERLRLRVAEMSRAQARAEeDARRFRKQAEDIgERLYRTELATQEKVMLVQTLETQRQ--QSDRDAERLREAIAE 2441
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALE-DAREQIELLEPI-RELAERYAAARERLAELEYLRAALRlwFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2442 LEHEKDKLKQEAQLLQLKSEEMQtvrqEQLLQETQALQQSFLSEKDSLlqrERCIEQEKAKLEQLFQdevaKAQALREEQ 2521
Cdd:COG4913 300 LRAELARLEAELERLEARLDALR----EELDELEAQIRGNGGDRLEQL---EREIERLERELEERER----RRARLEALL 368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237970 2522 QRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQqqqekllaeenQRLRERLQHLEEERRAALAR 2598
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL-----------RDLRRELRELEAEIASLERR 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2366-2614 |
2.92e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2366 SAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHE 2445
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2446 KDKLKQEAQLLQLKSEEMQTVRQEQLLqetqaLQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQ 2525
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALL-----LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2526 QqmqqEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIAPS 2605
Cdd:COG4942 174 A----ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
....*....
gi 1920237970 2606 RAAAARALP 2614
Cdd:COG4942 250 ALKGKLPWP 258
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1297-1641 |
2.95e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1297 ESIIQEYVDLRTRYSELST---LTSQYIRFISETLRRMEEEERLAE-QQRAEE-RERLAEVEAALEKQRQLAEAHAQAKA 1371
Cdd:COG4717 98 EELEEELEELEAELEELREeleKLEKLLQLLPLYQELEALEAELAElPERLEElEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1372 QAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQ---- 1447
Cdd:COG4717 178 ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE----ELEELEEELEQLENELEAAALEERLKEARllll 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1448 --------------LEATERQRGGA----EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQ 1509
Cdd:COG4717 254 iaaallallglggsLLSLILTIAGVlflvLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1510 AEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV----------------------QVALETAQRSAEAELQS 1567
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagvedeeelraaleqaeeYQELKEELEELEEQLEE 413
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 1568 -----EHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKAnEALRLRLQAEEVAQQ 1641
Cdd:COG4717 414 llgelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQ-ELEELKAELRELAEE 491
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1460-1682 |
3.00e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1460 GELQALRARAEEAEAQ-KRQAQEEAERLRRQVQDETQRKRQAEAElalRVQAEAEAAREKQRALQALEELRlQAEEAERR 1538
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQrKKKEQQQAEELQQKQAAEQERLKQLEKE---RLAAQEQKKQAEEAAKQAALKQK-QAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1539 LRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAtrraqqqaeaeraraeaerel 1618
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA--------------------- 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 1619 erwQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELE 1682
Cdd:PRK09510 200 ---KKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1665-1877 |
3.02e-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: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1665 KAEEQAVRQRELAEQ-----ELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQRQLLEEElarlqreaaaatqkRRE 1739
Cdd:NF012221 1555 DAAQNALADKERAEAdrqrlEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQRDAILEE--------------SRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1740 LEAELAKVRAEMEVLLAS-------------------KARAEEESRSTSEKSKQRLEAEAGRF----RELAEEAARLRAL 1796
Cdd:NF012221 1618 VTKELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLDDAKKISGKQLADAKQRHvdnqQKVKDAVAKSEAG 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1797 AEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRlLEEQAAQHKA 1876
Cdd:NF012221 1698 VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQ-ADAKGAKQDE 1776
|
.
gi 1920237970 1877 D 1877
Cdd:NF012221 1777 S 1777
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1359-1538 |
3.35e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1359 QRQLAEAHAQAK---AQAEREAQglqrrmqeevARREEVAVEAqeqkrsiQEELQHLRQSSEAEIQAKARQVEAAERsRL 1435
Cdd:PRK12704 30 EAKIKEAEEEAKrilEEAKKEAE----------AIKKEALLEA-------KEEIHKLRNEFEKELRERRNELQKLEK-RL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1436 RIEEEIrvVRLQLEATERQRGGAEGELQALRARAEEAEAQkrqaQEEAERLRRQVQDETQR---KRQAEAELALRVQAEA 1512
Cdd:PRK12704 92 LQKEEN--LDRKLELLEKREEELEKKEKELEQKQQELEKK----EEELEELIEEQLQELERisgLTAEEAKEILLEKVEE 165
|
170 180
....*....|....*....|....*..
gi 1920237970 1513 EAAREKQRALQALEElrlQA-EEAERR 1538
Cdd:PRK12704 166 EARHEAAVLIKEIEE---EAkEEADKK 189
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
936-1597 |
3.38e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 936 EDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRITEQQK 1015
Cdd:pfam02463 293 KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1016 AQAEVDGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAH 1095
Cdd:pfam02463 373 EELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1096 EEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQE-------VGERLQQRHGERDVEVERWRERV 1168
Cdd:pfam02463 453 LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKEskarsglKVLLALIKDGVGGRIISAHGRLG 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1169 TLLLERWQAVLAQTDVRQRELEQLG-----RQLRYYRESADPLGAWLRDAKQRQEQIQAVPLA---NSQAVREQLRQEKA 1240
Cdd:pfam02463 533 DLGVAVENYKVAISTAVIVEVSATAdeveeRQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleIDPILNLAQLDKAT 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1241 LLEDIERHGEKV----EECQRFAKQYINAiKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTL 1316
Cdd:pfam02463 613 LEADEDDKRAKVvegiLKDTELTKLKESA-KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1317 TSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGL-QRRMQEEVARREEVA 1395
Cdd:pfam02463 692 EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSrLKKEEKEEEKSELSL 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1396 VEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrLQLEATERQRGGAEGELQALRARAEEAEAQ 1475
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLE---EEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1476 KRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALE 1555
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1920237970 1556 TAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEA 1597
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKE 970
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2144-2318 |
3.57e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2144 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEE---LFSL 2220
Cdd:PRK09510 80 QRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEakrAAAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2221 RVQMEELGKLKARIEAENRALVLRDK----DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAE 2296
Cdd:PRK09510 160 AKKAAAEAKKKAEAEAAKKAAAEAKKkaeaEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAE 239
|
170 180
....*....|....*....|..
gi 1920237970 2297 KmlKEKMQAVQEATRLKAEAEL 2318
Cdd:PRK09510 240 K--AAAAKAAEKAAAAKAAAEV 259
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1665-1858 |
3.70e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.07 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1665 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1744
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1745 AKVRAEMEVLLASKARAEEESRsTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAE 1824
Cdd:pfam13868 229 KKARQRQELQQAREEQIELKER-RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRA 307
|
170 180 190
....*....|....*....|....*....|....
gi 1920237970 1825 KLAAISEATRLKTEAEIALKEKEAENERLRRLAE 1858
Cdd:pfam13868 308 AEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1756-1953 |
3.73e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1756 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQrqlaEEDAVRQRAEAERVLAEKLAAISEATRL 1835
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1836 KTEAEIALKEKEAENerlrrlAEDEAfQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEIL 1915
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|....*...
gi 1920237970 1916 ALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAE 1953
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3004-3041 |
3.83e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 3.83e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1920237970 3004 RRALRGSGVIAGVWLEEAGQKLSIYEALRKDLLQPEAA 3041
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2151-2347 |
3.92e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2151 DAEMEKHKQFAEQALR---QKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQR------GQVEEELFSLR 2221
Cdd:PRK11281 55 EAEDKLVQQDLEQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslRQLESRLAQTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2222 VQMEELGklKARIEAENRALVLRDK--------DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAeedLAQQRA 2293
Cdd:PRK11281 135 DQLQNAQ--NDLAEYNSQLVSLQTQperaqaalYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQAL---LNAQND 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2294 LAEKMLK--EKMQAVQEATR--LKAEAELLQQQKELAQE--QARRLQEDKEQMAQQLAQE 2347
Cdd:PRK11281 210 LQRKSLEgnTQLQDLLQKQRdyLTARIQRLEHQLQLLQEaiNSKRLTLSEKTVQEAQSQD 269
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1668-1915 |
4.01e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.21 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1668 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLEEELARLQR-------EAAAATQKRREL 1740
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLEQENRRLQAlseeqaaELAELTRRLAEL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1741 EAELAKVRAEMEVLLASKAraeeESRSTSEKSKQRLEAEAGRFR-ELAEEAARLRALAEEAKRQRQLAEE--DAVRQRAE 1817
Cdd:pfam19220 201 ETQLDATRARLRALEGQLA----AEQAERERAEAQLEEAVEAHRaERASLRMKLEALTARAAATEQLLAEarNQLRDRDE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1818 AERVLAEKLaaiSEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQK 1897
Cdd:pfam19220 277 AIRAAERRL---KEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSD 353
|
250
....*....|....*...
gi 1920237970 1898 GLveDTLRQRRQVEEEIL 1915
Cdd:pfam19220 354 RI--AELTKRFEVERAAL 369
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1665-1836 |
4.05e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.93 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1665 KAEEQAVRQR-ELAEQElekqrqlaegtAQQRLaaEQELIRLRAETEqgEQQRQLLeeelarlqreaaaatqkrrELEAE 1743
Cdd:PTZ00491 662 KSQEAAARHQaELLEQE-----------ARGRL--ERQKMHDKAKAE--EQRTKLL-------------------ELQAE 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1744 LAKVRAemevllASKARAEEESRSTSEKSKQRLEAEAGRFRelaEEAARLRALAE-EAKRQRQLAEEDAVRQRAEAERVL 1822
Cdd:PTZ00491 708 SAAVES------SGQSRAEALAEAEARLIEAEAEVEQAELR---AKALRIEAEAElEKLRKRQELELEYEQAQNELEIAK 778
|
170
....*....|....
gi 1920237970 1823 AEKLAAIsEATRLK 1836
Cdd:PTZ00491 779 AKELADI-EATKFE 791
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1664-1845 |
4.23e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1664 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQR-LAAEQELIRLRAEteqgeqQRQLLEEELARLQREAAAATQKRRELEA 1742
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEEReLTEEEEEIRRLEE------QVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1743 ELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEAGRF-RELAEEAARLRALAEEAKRQRQLAEEDavrqrAEAERV 1821
Cdd:COG2433 449 ELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLE-----HSGELV 511
|
170 180
....*....|....*....|....
gi 1920237970 1822 LAEKLAAISEATRLKTEAEIALKE 1845
Cdd:COG2433 512 PVKVVEKFTKEAIRRLEEEYGLKE 535
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1397-1532 |
4.25e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.81 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1397 EAQEQKRSIQEELQHLRQSS--EAEIQAKARQVEAAERSRLRIEEEI-RVVRLQleateRQRGGAEGELQALRARAEEAE 1473
Cdd:COG1566 87 QAEAQLAAAEAQLARLEAELgaEAEIAAAEAQLAAAQAQLDLAQRELeRYQALY-----KKGAVSQQELDEARAALDAAQ 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 1474 AQKRQAQEEAERLRRQVQDETQrKRQAEAELAlrvQAEAEAAREKQRalqaLEELRLQA 1532
Cdd:COG1566 162 AQLEAAQAQLAQAQAGLREEEE-LAAAQAQVA---QAEAALAQAELN----LARTTIRA 212
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3412-3448 |
4.35e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.35e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1920237970 3412 KLLSAEKAVTGYRDPYSGSTISLFQAMKKGLVLREHG 3448
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1665-1894 |
4.60e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.48 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1665 KAEE--------QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEEL--------ARLQR 1728
Cdd:PRK05035 447 KAEEakarfearQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARpdnsaviaAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1729 EAAAATQKRRELEAE-----LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrelaeeAARLRALAeeAKRQ 1803
Cdd:PRK05035 527 KAQARARQAEKQAAAaadpkKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVA---------AAIARAKA--KKAA 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1804 RQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAedeafqrrlleeqAAQHKAdiEARLA 1883
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVA-------------AAIARA--KARKA 660
|
250
....*....|.
gi 1920237970 1884 QLRKASESELE 1894
Cdd:PRK05035 661 AQQQANAEPEE 671
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1305-1585 |
4.63e-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: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1305 DLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQrAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRM 1384
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEEL-SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1385 QEEVARREEVAVEAQEQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGE 1461
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEelrSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1462 LQALRARAEEAEAQKRQAQ------EEAERLRRQVQDETQRKRQAEAELALRVQAEAEAARE-KQRALQALEELRLQAE- 1533
Cdd:pfam07888 236 LEELRSLQERLNASERKVEglgeelSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREgRARWAQERETLQQSAEa 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1920237970 1534 EAERRLRQAEAERARQVQVALETAQR-SAEAELQSEHASFAEKTAQLERTLKE 1585
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERMEReKLEVELGREKDCNRVQLSESRRELQE 368
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1672-2388 |
4.76e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.72 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1672 RQRELAEQEleKQRQLAEGTAQQRLAAEQ-ELIRLRAeTEQGEQQRQLLEeelaRLQREAAAATQKRR---ELEAELAKV 1747
Cdd:PRK10246 251 RLDELQQEA--SRRQQALQQALAAEEKAQpQLAALSL-AQPARQLRPHWE----RIQEQSAALAHTRQqieEVNTRLQST 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1748 RAEMEVLLASKARAEEESRSTSEKSKQRLeAEAGRFRELAEEAARLRALAEEAKRQRQlaEEDAVRQRAEAERvlaEKLA 1827
Cdd:PRK10246 324 MALRARIRHHAAKQSAELQAQQQSLNTWL-AEHDRFRQWNNELAGWRAQFSQQTSDRE--QLRQWQQQLTHAE---QKLN 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1828 AISEATRLKTEAEIAlkekeaenERLRRLAEDEAFQRRLLEEQaAQHkADIEARLAQLrKASESELERQKGLVEDTLRQR 1907
Cdd:PRK10246 398 ALPAITLTLTADEVA--------AALAQHAEQRPLRQRLVALH-GQI-VPQQKRLAQL-QVAIQNVTQEQTQRNAALNEM 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1908 RQVEEEilalkgsfekaaagKAElelELGRIRGTAEDTLRSKEQAEQEAarQRQLAAEEERRRREAEERVQKSLAAEEEA 1987
Cdd:PRK10246 467 RQRYKE--------------KTQ---QLADVKTICEQEARIKDLEAQRA--QLQAGQPCPLCGSTSHPAVEAYQALEPGV 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1988 ARQRKAALE-EVERLKakvEEARRLRERAEQeSARQLQLAQEAAQkRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERL 2066
Cdd:PRK10246 528 NQSRLDALEkEVKKLG---EEGAALRGQLDA-LTKQLQRDESEAQ-SLRQEEQALTQQWQAVCASLNITLQPQDDIQPWL 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2067 rseaeaarraaeeaeaareraereaaqsrrqvEEAERLKQsaeeqaqaqaqaqaaaeklrkeaeqeaarraqaEQAALRQ 2146
Cdd:PRK10246 603 --------------------------------DAQEEHER---------------------------------QLRLLSQ 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2147 KQAADAEMEKH----KQFAEQALRQKAQVEQELTALRLQLEETDHQKSIL---DEELQRLKAEVTEAARQRGQVE--EEL 2217
Cdd:PRK10246 618 RHELQGQIAAHnqqiIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLatrQQEAQSWQQRQNELTALQNRIQqlTPL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2218 FSLRVQMEELGKLKARIEAEN------RALVLRDKDSA--QRLLQEEAEKMKQVAEEAARL--SVAAQEAARLRQLAEED 2287
Cdd:PRK10246 698 LETLPQSDDLPHSEETVALDNwrqvheQCLSLHSQLQTlqQQDVLEAQRLQKAQAQFDTALqaSVFDDQQAFLAALLDEE 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2288 LAQQralAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQK--TLETERQRQLEM 2365
Cdd:PRK10246 778 TLTQ---LEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLREntTRQGEIRQQLKQ 854
|
730 740
....*....|....*....|....
gi 1920237970 2366 SAEA-ERLRLRVAEMSRAQARAEE 2388
Cdd:PRK10246 855 DADNrQQQQALMQQIAQATQQVED 878
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1357-1488 |
4.85e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 43.49 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1357 EKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHL--RQSSEAEIQAKARQVEAAERSR 1434
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeeERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 1435 LRIEEEIRVVRLQLEATERQRGGAEGELQalraraeeaEAQKRQAQEEAERLRR 1488
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER 135
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2244-2414 |
4.90e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.61 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2244 RDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATR-LKAEAELLQQQ 2322
Cdd:TIGR02794 65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAkAKAEAEAERKA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2323 KELAQEQARrlqEDKEQMAQQLAQetqgfQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGE 2402
Cdd:TIGR02794 145 KEEAAKQAE---EEAKAKAAAEAK-----KKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAE 216
|
170
....*....|..
gi 1920237970 2403 RLYRTELATQEK 2414
Cdd:TIGR02794 217 AAAAAAAEAERK 228
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1589-2044 |
4.93e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 46.55 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1589 AVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEE 1668
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1669 QAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVR 1748
Cdd:COG3903 557 LRGLLRE-GRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAA 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1749 AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAA 1828
Cdd:COG3903 636 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAA 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1829 ISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRR 1908
Cdd:COG3903 716 AAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAA 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1909 QVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAA 1988
Cdd:COG3903 796 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAA 875
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 1989 RQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFA 2044
Cdd:COG3903 876 AAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2431-2561 |
4.95e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2431 DAERLREAIAELEHEKDKLKQEAQLLqlkseemqtvrqEQLLQETQALQQSFLSEKDSLLQRErciEQEKAKLEQLFQDE 2510
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEA------------EALLKEAEKLKEELEEKKEKLQEEE---DKLLEEAEKEAQQA 578
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2511 V--AKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGV-------RRQQEELQ 2561
Cdd:PRK00409 579 IkeAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKekkkkkqKEKQEELK 638
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1415-1549 |
5.15e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.44 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1415 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQVQDET 1494
Cdd:PRK12678 69 TPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARR-GAARKAGE 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 1495 QRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQ 1549
Cdd:PRK12678 148 GGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDD 202
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1332-1597 |
5.16e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 46.57 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1332 EEEERLAEQQRAEERER----------LAEVEAALEKQR---QLAEAHAQAKAQAEREAQGLQRR----MQEEVARREEV 1394
Cdd:PRK10811 507 EEAMALPSEEEFAERKRpeqpalatfaMPDVPPAPTPAEpaaPVVAAAPKAAAATPPAQPGLLSRffgaLKALFSGGEET 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1395 AVEAQEQKRSIQEElqhlRQSSEaeiQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEA 1474
Cdd:PRK10811 587 KPQEQPAPKAEAKP----ERQQD---RRKPRQNNRRDRNERRDTRDNRTRREGRENREENRRNRRQAQQQTAETRESQQA 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1475 QKRQAQEEAERLRRQVQDETQRKRQAEAELAlrvQAEAEAarekqralQALEELRLQAEEAERRLRQAEAERAR------ 1548
Cdd:PRK10811 660 EVTEKARTQDEQQQAPRRERQRRRNDEKRQA---QQEAKA--------LNVEEQSVQETEQEERVQQVQPRRKQrqlnqk 728
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 1549 ---QVQVALETAQRSAEAELQSEHASfAEKTAQLERTLKEEHVAVVQLREEA 1597
Cdd:PRK10811 729 vriEQSVAEEAVAPVVEETVAAEPVV-QEVPAPRTELVKVPLPVVAQTAPEQ 779
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1419-1586 |
5.17e-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: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1419 EIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQvQDETQRKR 1498
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1499 QAEAelalrVQAEAEAAREKQRAL-QALEELRLQAEEAERRLRQAEAERARQVQ--VALETAQRSAEAELQSEHASFAEK 1575
Cdd:COG1579 90 EYEA-----LQKEIESLKRRISDLeDEILELMERIEELEEELAELEAELAELEAelEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|.
gi 1920237970 1576 TAQLERTLKEE 1586
Cdd:COG1579 165 REELAAKIPPE 175
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1406-1764 |
5.64e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1406 QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1485
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1486 LRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAEL 1565
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1566 QSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLT 1645
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1646 QAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR 1725
Cdd:COG4372 252 LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331
|
330 340 350
....*....|....*....|....*....|....*....
gi 1920237970 1726 LQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE 1764
Cdd:COG4372 332 LAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3373-3408 |
5.67e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.67e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1920237970 3373 TLLLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPE 3408
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2271-2549 |
5.76e-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: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2271 SVAAQEAARLRQLAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmAQQLAqETQG 2350
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK---QQQLA-AISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2351 FQKTLETERQRQLEMSAEAERlrlrvaemsraqARAEEDARRFRKQAEDIGERLyrtelatqekvmlvQTLETQRQQSDR 2430
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR------------DAILEESRAVTKELTTLAQGL--------------DALDSQATYAGE 1641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2431 DAERLREAIAE--LEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSllqrerciEQEKAKLEQLFQ 2508
Cdd:NF012221 1642 SGDQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG--------EQNQANAEQDID 1713
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1920237970 2509 DEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRR-QHEA 2549
Cdd:NF012221 1714 DAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3044-3077 |
6.14e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 6.14e-04
10 20 30
....*....|....*....|....*....|....
gi 1920237970 3044 LLEAQAGTGHIIDPTTSARLTVDEAVRAGLVGPE 3077
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1655-1818 |
6.42e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.63 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1655 EAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREaaaat 1734
Cdd:COG2268 229 EQEREIETARIAEAEAELAKKKAEERREAETARAE---AEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAE----- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1735 QKRRELEAELaKVRAEmevllASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEedAVRQ 1814
Cdd:COG2268 301 REEAELEADV-RKPAE-----AEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE--IAEA 372
|
....
gi 1920237970 1815 RAEA 1818
Cdd:COG2268 373 AAKP 376
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
34-147 |
6.63e-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: 42.41 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 34 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerdvIRSSRLPREKGRmrfHKLQNVQIALDYL 113
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVP-----LHSFHLTPTSFE---QKVHNVQFAFELM 87
|
90 100 110
....*....|....*....|....*....|....
gi 1920237970 114 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 147
Cdd:cd21306 88 QDAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1693-1961 |
6.67e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1693 QQRLAAEQELIRlraeteQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKS 1772
Cdd:PRK11637 53 QQDIAAKEKSVR------QQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1773 KQRLEAEagrFRELAEEAARLRALAEEAKRqrqlaeedavrqraeAERVLAeKLAAISEAtRLKTEAEialkekeaener 1852
Cdd:PRK11637 127 AAQLDAA---FRQGEHTGLQLILSGEESQR---------------GERILA-YFGYLNQA-RQETIAE------------ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1853 LRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVedtlrqrrqveeeilALKGSFEKAAAGKAELE 1932
Cdd:PRK11637 175 LKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLT---------------GLESSLQKDQQQLSELR 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 1920237970 1933 LELGRIRGT-AEDTLRSKEQAEQEA-------ARQRQ 1961
Cdd:PRK11637 240 ANESRLRDSiARAEREAKARAEREAreaarvrDKQKQ 276
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1664-1786 |
7.64e-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: 44.81 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1664 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELIRLRAETEQGEQQRQLLEEELARLQR-----EAAAATQKR 1737
Cdd:pfam17045 127 GKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRKQCLEASQSEIQRlrsklERAQDSLCA 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 1738 RELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEAGRFREL 1786
Cdd:pfam17045 207 QELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1989-2478 |
8.46e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1989 RQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRS 2068
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2069 EAeaarraaeeaeaareraereaaqsrRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAArraqaeqaalRQKQ 2148
Cdd:COG4717 144 LP-------------------------ERLEELEERLEELRELEEELEELEAELAELQEELEELLE----------QLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2149 AADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKA-EVTEAARQRGQVEEELFSLRVQMEEL 2227
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeERLKEARLLLLIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2228 GKLKARI------EAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2301
Cdd:COG4717 269 LSLILTIagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2302 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKtleTERQRQLEMSAEAERLRLRVAEMSR 2381
Cdd:COG4717 349 LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQEL---KEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2382 AQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAER--LREAIAELEHEKDKLKQEAQLLQLK 2459
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELeeLKAELRELAEEWAALKLALELLEEA 505
|
490
....*....|....*....
gi 1920237970 2460 SEEMQTVRQEQLLQETQAL 2478
Cdd:COG4717 506 REEYREERLPPVLERASEY 524
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1079-1734 |
8.48e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1079 SLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPE-LEATKAALKKLRAQAEAQqpvfdalRDELR-GAQEVGERLQQRHGE 1156
Cdd:pfam05483 158 NLLKETCARSAEKTKKYEYEREETRQVYMDLNNnIEKMILAFEELRVQAENA-------RLEMHfKLKEDHEKIQHLEEE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1157 RDVEVERWRERVTLLLerwqavlAQTDVRQRELEQLGRQLRYYRESADPLgawlrdakQRQEQIQAVPLANSQAVREQLR 1236
Cdd:pfam05483 231 YKKEINDKEKQVSLLL-------IQITEKENKMKDLTFLLEESRDKANQL--------EEKTKLQDENLKELIEKKDHLT 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1237 QEkalLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYK-AQLEPVASPAK---------KPKVQSGSESIIQEYVDL 1306
Cdd:pfam05483 296 KE---LEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKeAQMEELNKAKAahsfvvtefEATTCSLEELLRTEQQRL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1307 RTRYSELSTLTSQYIRFISEtLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLaEAHAQAKAQAEREAQGLQRRMQE 1386
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSE-LEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF-EKIAEELKGKEQELIFLLQAREK 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1387 EVARREEVAVEAQEQKRSIQEELQHLRQSSEAEiqaKARQVEAAERSRLRIEEEIRVVR------LQLEATERQRGGAEG 1460
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKE---KLKNIELTAHCDKLLLENKELTQeasdmtLELKKHQEDIINCKK 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1461 ELQALRARAEEAEAQKRQAQEEAERLRR---QVQDETQRKRQAEAELALRVQAEAEAAREKQRALQ-ALEELRLQAEEAE 1536
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREefiQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEnKCNNLKKQIENKN 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1537 RRLRQAEAE-RARQVQVALETAQRSA--------EAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRaqqqaea 1607
Cdd:pfam05483 608 KNIEELHQEnKALKKKGSAENKQLNAyeikvnklELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKA------- 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1608 eraraeaerelerwQLKANEALRLRLQAEEVAQQKsltqaeaekqkEEAEREARRRGKAEEQAVRQRELAEQELEKQRQL 1687
Cdd:pfam05483 681 --------------KAIADEAVKLQKEIDKRCQHK-----------IAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQ 735
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1920237970 1688 AEGTAqqRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAT 1734
Cdd:pfam05483 736 EQSSA--KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1665-2046 |
8.61e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.42 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1665 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1744
Cdd:COG3064 20 QAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1745 AKVRAEMEVLLASKARAEEESRSTSEKSK--QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVL 1822
Cdd:COG3064 100 AAKEAEAAAAAEKAAAAAEKEKAEEAKRKaeEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1823 AEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVED 1902
Cdd:COG3064 180 AALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1903 TLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLA 1982
Cdd:COG3064 260 LGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEA 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 1983 AEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQ 2046
Cdd:COG3064 340 ALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGL 403
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1321-1585 |
8.68e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.91 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1321 IRFISETLRRMEEEERLAEQQRAEERERLAEV-EAALEKQRQLAEAHAQAKAQAEREAQGLQrrmqeevarreevavEAQ 1399
Cdd:pfam00038 20 VRFLEQQNKLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNLR---------------LAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1400 EQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIrvvrlqleaterqrggaegelQALRaraEEAEAQKRQA 1479
Cdd:pfam00038 85 EDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKI---------------------ESLK---EELAFLKKNH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1480 QEEAERLRRQVQDETQ-------RKRQAEAELA-LRVQAEAEAAREKQRA----LQALEELRLQAEEAERRLRQAEAERA 1547
Cdd:pfam00038 141 EEEVRELQAQVSDTQVnvemdaaRKLDLTSALAeIRAQYEEIAAKNREEAeewyQSKLEELQQAAARNGDALRSAKEEIT 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 1548 ---RQVQ-------------VALETAQRSAEAELQSEHASFAEKTAQLERTLKE 1585
Cdd:pfam00038 221 elrRTIQsleielqslkkqkASLERQLAETEERYELQLADYQELISELEAELQE 274
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1329-1517 |
8.86e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.67 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1329 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEE 1408
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARA-AAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1409 LQHLRQSSEAEIQAKARQVEAAERSRLRieeeiRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR 1488
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGDREDRQAE-----AERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRR 231
|
170 180
....*....|....*....|....*....
gi 1920237970 1489 QVQDETQRKRQAEAELALRVQAEAEAARE 1517
Cdd:PRK12678 232 RRDRRDARGDDNREDRGDRDGDDGEGRGG 260
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2167-2506 |
8.98e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2167 QKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVT-------EAARQRGQVEEELFSLRVQMEELGKLKARIEAENR 2239
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEklnnkynDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2240 AL-----VLRDKDSAQRLLQEEAEKMK----QVAEEAARLSVAAQEAARLRQLAEE---DLAQQRALAEKMLKEKMQAVQ 2307
Cdd:TIGR04523 198 KLelllsNLKKKIQKNKSLESQISELKkqnnQLKDNIEKKQQEINEKTTEISNTQTqlnQLKDEQNKIKKQLSEKQKELE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2308 EATR-----------LKAEAELLQQQKE---------LAQEQARRLQEDKEQMAQ------QLAQETQGFQKTLETERQR 2361
Cdd:TIGR04523 278 QNNKkikelekqlnqLKSEISDLNNQKEqdwnkelksELKNQEKKLEEIQNQISQnnkiisQLNEQISQLKKELTNSESE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2362 QLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAE 2441
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 2442 LEHEKDKLKQEAQLLQLKSEEMQTVRqEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQL 2506
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTR-ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2196-2347 |
9.00e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2196 LQRLKAEVTEAARQR----GQVEEELfsLRVQMEELGKLKaRIEAEnRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLS 2271
Cdd:PRK09510 67 QQQQQKSAKRAEEQRkkkeQQQAEEL--QQKQAAEQERLK-QLEKE-RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAA 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 2272 VAAQEAARLRQLAEEDLAQQrALAEKMLKEKMQAVQEA---TRLKAEAELLQQQKELAQEQArrlQEDKEQMAQQLAQE 2347
Cdd:PRK09510 143 AAAKAKAEAEAKRAAAAAKK-AAAEAKKKAEAEAAKKAaaeAKKKAEAEAAAKAAAEAKKKA---EAEAKKKAAAEAKK 217
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2007-2458 |
9.32e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 45.34 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2007 EARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARER 2086
Cdd:COG4995 3 ALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2087 AEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALR 2166
Cdd:COG4995 83 AALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2167 QKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDK 2246
Cdd:COG4995 163 AALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2247 DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELA 2326
Cdd:COG4995 243 LAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2327 QEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYR 2406
Cdd:COG4995 323 LLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLA 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 2407 TELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQL 2458
Cdd:COG4995 403 LAAAQLLRLLLAALALLLALAAYAAARLALLALIEYIILPDRLYAFVQLYQL 454
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1330-1446 |
9.49e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1330 RMEEEERLAEQQRAEERERLAEVEA---ALEKQ-RQLAEAHAQAKAQAEREAQGLQRRMQEEVAR-----REEVAVEAQE 1400
Cdd:PRK00409 524 SLEELERELEQKAEEAEALLKEAEKlkeELEEKkEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEiikelRQLQKGGYAS 603
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237970 1401 QKRS-IQEELQHLRQSSEAEIQAKARQVEAAErsRLRIEEEIRVVRL 1446
Cdd:PRK00409 604 VKAHeLIEARKRLNKANEKKEKKKKKQKEKQE--ELKVGDEVKYLSL 648
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
21-261 |
9.91e-04 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 45.32 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 21 EEVRE-KYKDERDRVQKKTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLSGDSLPRERDVIRSSRLPREKGRM- 98
Cdd:COG5069 365 EEKPEiEEFDAEGEFEARVFTFWLNSLDVSPE--ITNLFGDLRDQ---LILLQALSKKLMPMTVTHKLVKKQPASGIEEn 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 99 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNpKLTLGLIW-------TIILHFQISDiqvsgqsEDMTAKEKLLLWS 171
Cdd:COG5069 440 RFKAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKD-------GCGLSDSDLCAWL 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 172 QRMV------EGCQGLRCDNFTTSWRDGRLFNAIIHrhkPTLIDMNKVyRQTNLENLDQA-------FSVAERDLGVTRL 238
Cdd:COG5069 512 GSLGlkgdkeEGIRSFGDPAGSVSGVFYLDVLKGIH---SELVDYDLV-TRGFTEFDDIAdarslaiSSKILRSLGAIIK 587
|
250 260
....*....|....*....|...
gi 1920237970 239 LDPEDVDVPQPdEKSIITYVSSL 261
Cdd:COG5069 588 FLPEDINGVRP-RLDVLTFIESL 609
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2147-2435 |
1.01e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2147 KQAADAEMEKHKQFaEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAaRQRGQVEEELfslRVQMEE 2226
Cdd:COG3096 402 QQALDVQQTRAIQY-QQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLEL-EQKLSVADAA---RRQFEK 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2227 LGKLKARIEAEnralVLRDK--DSAQRLLQEEAEKMKQvaeeAARLSVAAQEAARLRQLAEEdlaQQRA--LAEKMLKEK 2302
Cdd:COG3096 477 AYELVCKIAGE----VERSQawQTARELLRRYRSQQAL----AQRLQQLRAQLAELEQRLRQ---QQNAerLLEEFCQRI 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2303 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaQETQGFQKTLETERQRQLEMSAEAERLRlrvaEMSRA 2382
Cdd:COG3096 546 GQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL-EQLRARIKELAARAPAWLAAQDALERLR----EQSGE 620
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1920237970 2383 QARAEEDARRFRKQAedigerLYRTELATQEKvmlvQTLETQRQQSDRDAERL 2435
Cdd:COG3096 621 ALADSQEVTAAMQQL------LEREREATVER----DELAARKQALESQIERL 663
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2148-2471 |
1.01e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2148 QAADAEMEKHKQFAEQALRQKAQVEQELtalRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEEL 2227
Cdd:pfam13868 16 LAAKCNKERDAQIAEKKRIKAEEKEEER---RLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2228 GKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ 2307
Cdd:pfam13868 93 YEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDE-FNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2308 EATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLAQETQGF---QKTLETERQRQLEMSAEAERLRLRVAEMSRA 2382
Cdd:pfam13868 172 EAEREEIEEEKEREIARLRaqQEKAQDEKAERDELRAKLYQEEQERkerQKEREEAEKKARQRQELQQAREEQIELKERR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2383 QARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQtLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEE 2462
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKR-LEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRER 330
|
....*....
gi 1920237970 2463 MQTVRQEQL 2471
Cdd:pfam13868 331 IEEERQKKL 339
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1338-1499 |
1.01e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.28 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1338 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE 1417
Cdd:PRK12678 65 AAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1418 AEIQAKARQVEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEaERLRRQVQDETQRK 1497
Cdd:PRK12678 145 AGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRR 215
|
..
gi 1920237970 1498 RQ 1499
Cdd:PRK12678 216 EE 217
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1668-1949 |
1.10e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1668 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1747
Cdd:COG4372 69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1748 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLA 1827
Cdd:COG4372 149 EEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1828 AISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQR 1907
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1920237970 1908 RQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSK 1949
Cdd:COG4372 309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4372-4409 |
1.11e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.11e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1920237970 4372 QRFLEVQYLTGGLIEPDTPGRVALDEALQRGTVDARTA 4409
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1321-1564 |
1.15e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1321 IRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQE 1400
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1401 QKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALR-------AraeEAE 1473
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKaeleaakA---ELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1474 AQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVA 1553
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
250
....*....|.
gi 1920237970 1554 LETAQRSAEAE 1564
Cdd:COG3883 255 AGAAAGSAGAA 265
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2358-2603 |
1.21e-03 |
|
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: 45.43 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2358 ERQRQLEMSAEA-ERLRLRVAEMSRAQARAEEDARRFRKQAEdigerlYRTELATQEKVMLVQTLETQRQQsdrdAERLR 2436
Cdd:TIGR02168 176 ETERKLERTRENlDRLEDILNELERQLKSLERQAEKAERYKE------LKAELRELELALLVLRLEELREE----LEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2437 EAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEqlLQETQALQQSFLSEKDSLLQR-ERCIEQEKAKLEQLFQDEVAKAQ 2515
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSE--LEEEIEELQKELYALANEISRlEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2516 ALREeqqrqqqqmqqekqqLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAA 2595
Cdd:TIGR02168 324 QLEE---------------LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
....*...
gi 1920237970 2596 LARSEEIA 2603
Cdd:TIGR02168 389 AQLELQIA 396
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
606-698 |
1.22e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.16 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 606 HGFVAAATKELMWLSDREEEEVGFDWSDRNTNMAAKKEGYSALMHELELKEKKIKEIQSTGDRLLREDHPARPTAESFQA 685
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1920237970 686 ALQTQWSWMLQLC 698
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1469-1853 |
1.24e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1469 AEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAR---EKQRALQALEELRLQAEEAERRLRQAEAE 1545
Cdd:PRK10929 104 TDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRqlnEIERRLQTLGTPNTPLAQAQLTALQAESA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1546 RARQVQVALETAQRSAE-----AELQSEhaSFAEKTAQLERTLkeehvavvqlreeatrraqqqaeaeraraeaereler 1620
Cdd:PRK10929 184 ALKALVDELELAQLSANnrqelARLRSE--LAKKRSQQLDAYL------------------------------------- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1621 wqlkanEALRLRLQAEevaqqksltqaeaekqkeeaerearrrgkaeeqavRQRElAEQELEKQRQLAEGTAQQRLAAEQ 1700
Cdd:PRK10929 225 ------QALRNQLNSQ-----------------------------------RQRE-AERALESTELLAEQSGDLPKSIVA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1701 ELIRLRAETEQGEQQRQLLeEELARLQREAAAATQKRREleaELAKVRAEMEVLLASKARAE----EESRSTSEKSKQRL 1776
Cdd:PRK10929 263 QFKINRELSQALNQQAQRM-DLIASQQRQAASQTLQVRQ---ALNTLREQSQWLGVSNALGEalraQVARLPEMPKPQQL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1777 EAEAGRFRelaeeAARLR--ALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAA---------------ISEATRLK--- 1836
Cdd:PRK10929 339 DTEMAQLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTqrellnsllsggdtlILELTKLKvan 413
|
410
....*....|....*...
gi 1920237970 1837 TEAEIALKE-KEAENERL 1853
Cdd:PRK10929 414 SQLEDALKEvNEATHRYL 431
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1664-2046 |
1.26e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 45.00 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1664 GKAEEQAVRQRELAEQELEK-----QRQLAEGTAQQRLAAEQELIRLRAE--TEQGEQQRQLLEEELARLQREAAAATQK 1736
Cdd:NF033838 50 SSGNESQKEHAKEVESHLEKilseiQKSLDKRKHTQNVALNKKLSDIKTEylYELNVLKEKSEAELTSKTKKELDAAFEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1737 RRELEAELAKVRAEMEVLLA-----SKARAEEESRSTSEKSKQRLEAEAGRFrELAEEAARLRALAEEAKRQRqlaEEDA 1811
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEeaekkAKDQKEEDRRNYPTNTYKTLELEIAES-DVEVKKAELELVKEEAKEPR---DEEK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1812 VRQrAEAErVLAEKlaaiSEATRLKteaEIALKEKEAENERLRRLaedEAFQRRLLEEQAAQHKADIEARLAqlRKASES 1891
Cdd:NF033838 206 IKQ-AKAK-VESKK----AEATRLE---KIKTDREKAEEEAKRRA---DAKLKEAVEKNVATSEQDKPKRRA--KRGVLG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1892 ELERQKGLVEDTLRQRRQVEEEIL---ALKGSFEKAAAGKAELELElGRIRGTAEDTLR-----SKEQAEQEAARqrqla 1963
Cdd:NF033838 272 EPATPDKKENDAKSSDSSVGEETLpspSLKPEKKVAEAEKKVEEAK-KKAKDQKEEDRRnyptnTYKTLELEIAE----- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1964 aeEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKA---KVEEARRLRERAEQESARQLQLAQEAAQKrlQAEEKA 2040
Cdd:NF033838 346 --SDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAeatRLEKIKTDRKKAEEEAKRKAAEEDKVKEK--PAEQPQ 421
|
....*.
gi 1920237970 2041 HAFAVQ 2046
Cdd:NF033838 422 PAPAPQ 427
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1339-1466 |
1.29e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.11 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1339 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAqAEREaqglqRRMQEEVARREEVavEAQEQKRSIQEELQHLRQSSEA 1418
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKAEA-AEQE-----RKLLEEQQRELEQ--KLEDQERSYEEHLRQLKEKMEE 248
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1920237970 1419 EIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegELQALR 1466
Cdd:cd16269 249 ERENLLKEQERALESKLKEQEALLEEGFKEQAELLQE-----EIRSLK 291
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1410-1698 |
1.34e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1410 QHLRQSsEAEIQAKARQVEAAERSRLRIEEeirvvrlqleateRQrggaegelqalrARAEeaeaqkRQAQEEAERLRRQ 1489
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA-------------RQ------------ARLE------REKAAREARHKKA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1490 VQDETQRKRQAEAELALRVQAEAEAAREK----------QRALQALEELR-LQAEEAERRLRQAEAERARQVQVALETAQ 1558
Cdd:PRK05035 477 AEARAAKDKDAVAAALARVKAKKAAATQPivikagarpdNSAVIAAREARkAQARARQAEKQAAAAADPKKAAVAAAIAR 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1559 RSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERElerwqlkANEALRLRLQAEEV 1638
Cdd:PRK05035 557 AKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKA-------AVAAAIARAKAKKA 629
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1639 AQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1698
Cdd:PRK05035 630 EQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2753-2789 |
1.40e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.40e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1920237970 2753 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVREHG 2789
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1462-1561 |
1.43e-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: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1462 LQALRARAEEAE---AQKRQAQEEAERLRRQVQDEtQRKRQAEAElALRVQAEAEAAREKQRALQALEelrlqaEEAERR 1538
Cdd:COG0711 26 LKALDERQEKIAdglAEAERAKEEAEAALAEYEEK-LAEARAEAA-EIIAEARKEAEAIAEEAKAEAE------AEAERI 97
|
90 100
....*....|....*....|...
gi 1920237970 1539 LRQAEAERARQVQVALETAQRSA 1561
Cdd:COG0711 98 IAQAEAEIEQERAKALAELRAEV 120
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2144-2601 |
1.45e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.73 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2144 LRQKQAADAEMEKHKQFAEQALRQKAQV----EQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2219
Cdd:pfam05557 78 NRLKKKYLEALNKKLNEKESQLADAREVisclKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2220 LRVQMEELGKLKARIEAENRALVLRDKDSaqrllqEEAEKMKqvaEEAARLSVAAQEAARLRqlaeEDLAQQRALAEKML 2299
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQSQEQDS------EIVKNSK---SELARIPELEKELERLR----EHNKHLNENIENKL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2300 KEKMQAVQEATRLkaeaellqQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKT-------------LETERQRQLEMS 2366
Cdd:pfam05557 225 LLKEEVEDLKRKL--------EREEKYREEAATLELEKEKLEQELQSWVKLAQDTglnlrspedlsrrIEQLQQREIVLK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2367 AEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTE-----------LATQEKVMLVQTLE------TQRQQSD 2429
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKalvrrlqrrvlLLTKERDGYRAILEsydkelTMSNYSP 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2430 RDAERLREA----------IAELEHEKDKLKQEA----QLLQLKSEEMQTVRQeqllQETQALQQSFLSEKDSLLQRERC 2495
Cdd:pfam05557 377 QLLERIEEAedmtqkmqahNEEMEAQLSVAEEELggykQQAQTLERELQALRQ----QESLADPSYSKEEVDSLRRKLET 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2496 IEQEKAKLEQlfQDEVAKAQALREEQQRQQQQMQQEKQQLaasmeearrRQHEAEEGVRRQQEELQRLAqqqqqqeklla 2575
Cdd:pfam05557 453 LELERQRLRE--QKNELEMELERRCLQGDYDPKKTKVLHL---------SMNPAAEAYQQRKNQLEKLQ----------- 510
|
490 500
....*....|....*....|....*.
gi 1920237970 2576 EENQRLRERLQHLEEERRAALARSEE 2601
Cdd:pfam05557 511 AEIERLKRLLKKLEDDLEQVLRLPET 536
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1397-1750 |
1.47e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1397 EAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQK 1476
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1477 RQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERA---RQVQVA 1553
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEslqEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1554 LETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRL 1633
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1634 QAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGE 1713
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
330 340 350
....*....|....*....|....*....|....*..
gi 1920237970 1714 QQRQLLEEELARLQREAAAATQKRRELEAELAKVRAE 1750
Cdd:COG4372 330 LALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAG 366
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1766-1914 |
1.60e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1766 RSTSEKSKQRLEAEAGRFRELAEEAArlralaEEAKRQRQL-AEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALK 1844
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 1845 EKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKasesELERQKGLVEDTLRQR--RQVEEEI 1914
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEA 167
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1334-1579 |
1.60e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.50 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1334 EERLAEQQRaEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQ----------EEVARREEVAVEAQEQKR 1403
Cdd:pfam07888 33 QNRLEECLQ-ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAelkeelrqsrEKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1404 SIQEE---LQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQ 1480
Cdd:pfam07888 112 ELSEEkdaLLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1481 EEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVAleTAQRS 1560
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA--AQRDR 269
|
250
....*....|....*....
gi 1920237970 1561 AEAELQSEHASFAEKTAQL 1579
Cdd:pfam07888 270 TQAELHQARLQAAQLTLQL 288
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2197-2391 |
1.80e-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: 44.56 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2197 QRLKAEVTEAARQRGQVEEElfslrvqmeelgklkarieaenralvlrdkdsaQRLLQEEAEKMKQVAEEAARLSVAAQE 2276
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQ---------------------------------RRLQQEQLERAEKMREELELEQQRRFE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2277 AARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA---ELLQQQKELAQEQARRLQEDKE---QMAQQLAQETQG 2350
Cdd:pfam15709 388 EIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQELQRKKQQEEAERAEAEKQrqkELEMQLAEEQKR 467
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1920237970 2351 FQKTLETERQRQLEMSAEAERLRLRVAEMSRaqARAEEDAR 2391
Cdd:pfam15709 468 LMEMAEEERLEYQRQKQEAEEKARLEAEERR--QKEEEAAR 506
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1346-1597 |
1.84e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1346 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKAR 1425
Cdd:pfam13868 12 NSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1426 QVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1505
Cdd:pfam13868 92 EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1506 LRVQAEAEAAREKQRAlqaleELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELqsehasfAEKTAQLERTLKE 1585
Cdd:pfam13868 172 EAEREEIEEEKEREIA-----RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREE-------AEKKARQRQELQQ 239
|
250
....*....|..
gi 1920237970 1586 EHVAVVQLREEA 1597
Cdd:pfam13868 240 AREEQIELKERR 251
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
2307-2385 |
1.87e-03 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 43.93 E-value: 1.87e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 2307 QEATRLKAEAELLQQQKELAQEQArrlQEDKEQMAQQLAQETqgfqKTLETERQRQLEMSAEAERLRLRVAEMSRAQAR 2385
Cdd:PRK10920 60 QQAQNQTATNDALANQLTALQKAQ---ESQKQELEGILKQQA----KALDQANRQQAALAKQLDELQQKVATISGSDAK 131
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1447-1910 |
1.92e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1447 QLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALE 1526
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1527 ELRLQAEEAERRLRQAEAERARQVQValETAQRSAE--AELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQ 1604
Cdd:COG3064 97 KAKAAKEAEAAAAAEKAAAAAEKEKA--EEAKRKAEeeAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1605 AEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1684
Cdd:COG3064 175 AAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1685 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE 1764
Cdd:COG3064 255 AAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1765 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALK 1844
Cdd:COG3064 335 ASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEA 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 1845 EKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQV 1910
Cdd:COG3064 415 ASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADL 480
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1338-1591 |
1.98e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1338 AEQQRAEERERlaeVEAALEkqrqlaEAHAQAKAQAEREAQGL---------------------QRRMQEEVARREEVAV 1396
Cdd:PHA03247 1586 AKQQRAEATDR---VTAALR------EALAAHERRAQSEAESLanlktllrvaaipataaktldQARSVAEIVDQIELLL 1656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1397 EAQEQKRSIQEE----LQHLRQSSEAEIQAKARQVEAAERSRLRieeeirvVRLQLEATERQRggaegeLQALRARAEEA 1472
Cdd:PHA03247 1657 EQTEKAAELDVAavdwLEHARRVFEAHPLTAARGGGPDPLARLH-------ARLDALGETRRR------TEALRRSLEAA 1723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1473 EAQKRQAQEEAERLRRQvqdetqrkrqaeaelALRVQAEAEAAREKQRALQALEE--LRLQAEEAERRLrqaeAERARQV 1550
Cdd:PHA03247 1724 EAEWDEVWGRFGRVRGG---------------AWKSPEALRAAREQLRALQTATNtvLGLRADAHYERL----PAKYQGA 1784
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1920237970 1551 qVALETAQRSAEAElqsEHASFAEKTAQLERTLKEEHVAVV 1591
Cdd:PHA03247 1785 -LGAKSAERAGAVE---ELGAAVARHDGLLARLREEVVARV 1821
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1332-1596 |
2.20e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.09 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1332 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREA-----------QGL-----------QRRMQEEVA 1389
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELkpsgqggldeeEAFldrtakreerrQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1390 RREEVAVEAQEQKRSIQEELQHlRQSSEAEIQAKARQVEaAERSRLRIEEEIRVVRL---QLEATERQRGGAEGELQALR 1466
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKEN-NEEEENSSWEKEEKRD-SRLGRYKEEETEIREKEyqeNKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1467 ARAEEAEAQKRQAQEEAERLRRQVQDE---------------TQRKRQA--EAELALRVQAEAEAAREKQRALQALE-EL 1528
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDEKIKKEKKvkyeskvfldqkrghPEVKSQNgeEEVTKLKVTTKRRQGGLSQSQEREEEaEV 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1529 RLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAE--KTAQLERTLKEEHVAVVQLREE 1596
Cdd:pfam02029 243 FLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREErrKLLEEEEQRRKQEEAERKLREE 312
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1350-1557 |
2.21e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1350 AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQ--RRMQEEVARREEVAVEAQEQKRSIQE-----------ELQHLRQSS 1416
Cdd:PHA03247 1150 STVDAAVRAHGVLADAVAALSPAVRDPACPLAflVALADSAAGYVKATRLALDARRAIARlgalgaaaadlAVAVRRENP 1229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1417 EAE------IQAKARQVEAAERSRLRIEEEIRVVrLQLEATERQRGGAEGELQAL-------RARAEEAEAQkrqAQEEA 1483
Cdd:PHA03247 1230 QAEgdraalLEAAARAVTAAREGLAACEGEFGGL-LHAEGSAGDPSPSGRALQELgkvvgatRRRADELEAA---AADLA 1305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 1484 ERLRRQVQDETQRKRQAEAELAL-RVQAEAEAAREKQRALQALE-ELRLQAEEAERRLRQAEAERARQVQVALETA 1557
Cdd:PHA03247 1306 EKMAARRARASRERWAADVEAALdRVENRAEFDAVELRRLQALAaTHGYNPRDFRKRAEQALAANAKTATLALEAA 1381
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1462-1586 |
2.31e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1462 LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEaarekqralQALEELRLQAEEAERRLRQ 1541
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ---------QAIKEAKKEADEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1920237970 1542 AEAERARQVqvaletaqrsAEAELQSEHASFAEKTAQLERTLKEE 1586
Cdd:PRK00409 596 LQKGGYASV----------KAHELIEARKRLNKANEKKEKKKKKQ 630
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2023-2458 |
2.36e-03 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 44.19 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2023 LQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAE 2102
Cdd:COG4995 1 LLALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2103 RLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQL 2182
Cdd:COG4995 81 ALAALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2183 EETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQ 2262
Cdd:COG4995 161 AAAALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2263 VAEEAARLSvAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQ 2342
Cdd:COG4995 241 LALAAAAAA-LAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2343 QLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEM-SRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTL 2421
Cdd:COG4995 320 LAALLLLLAALALLALLLLLAAAALLAAALAAALALAaALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAA 399
|
410 420 430
....*....|....*....|....*....|....*..
gi 1920237970 2422 ETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQL 2458
Cdd:COG4995 400 LLALAAAQLLRLLLAALALLLALAAYAAARLALLALI 436
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1447-1562 |
2.39e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1447 QLEATERQR-GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQAL 1525
Cdd:PRK09039 67 DLLSLERQGnQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237970 1526 EELR---------LQAEEAERRLRQAE-AERARQVQVALetAQRSAE 1562
Cdd:PRK09039 147 AALRrqlaaleaaLDASEKRDRESQAKiADLGRRLNVAL--AQRVQE 191
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1701-2048 |
2.47e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1701 ELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAElaKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA 1780
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE--RQRRELESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1781 GRFRELAEEAARLRAlAEEAKRQRQLAEEDAVrqRAEAERVLaeklaaiseatrlkteaeialkEKEAENERLRRLAEDE 1860
Cdd:pfam07888 108 ASSEELSEEKDALLA-QRAAHEARIRELEEDI--KTLTQRVL----------------------ERETELERMKERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1861 AFQRRLLEEQAAQHKADIEARLAQLRKASeSELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRG 1940
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQQTEEELRSLS-KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1941 TAE-------------------DTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALE----- 1996
Cdd:pfam07888 242 LQErlnaserkveglgeelssmAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADkdrie 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237970 1997 ----EVERLKAKVEEARRLRERAEQESARQ--LQLAQEAAQKRLQAEEKAhAFAVQQK 2048
Cdd:pfam07888 322 klsaELQRLEERLQEERMEREKLEVELGREkdCNRVQLSESRRELQELKA-SLRVAQK 378
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1406-1596 |
2.49e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 42.73 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1406 QEELQHLRQSSEAEIQakarqveaaersrlRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1485
Cdd:pfam15665 13 EAEIQALKEAHEEEIQ--------------QILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1486 LRRQVQDetqRKRQAEAELALRVQAEA----EAAREKQRALQALEELRLQAE-EAERRLRQAEAERARQVQVALETaqrs 1560
Cdd:pfam15665 79 YKRRVEE---RELKAEAEHRQRVVELSreveEAKRAFEEKLESFEQLQAQFEqEKRKALEELRAKHRQEIQELLTT---- 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 1920237970 1561 aeaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREE 1596
Cdd:pfam15665 152 ----QRAQSASSLAEQEKLEELHKAELESLRKEVED 183
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2419-2602 |
2.60e-03 |
|
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: 43.96 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2419 QTLETQRQQSDR----DAERLREAIAELEHEKDKLKqeaqllqlKSEEMQTVRQEQLLQETQ--ALQQSFLSEKDSLLQR 2492
Cdd:pfam17380 281 QKAVSERQQQEKfekmEQERLRQEKEEKAREVERRR--------KLEEAEKARQAEMDRQAAiyAEQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2493 ERcIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEK 2572
Cdd:pfam17380 353 IR-QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190
....*....|....*....|....*....|.
gi 1920237970 2573 LLAEENQRL-RERLQHLEEERRAALARSEEI 2602
Cdd:pfam17380 432 ARQREVRRLeEERAREMERVRLEEQERQQQV 462
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1380-2045 |
2.65e-03 |
|
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: 43.97 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1380 LQRRMQeevARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRL---RIEEEIRVVR-LQLEATERQR 1455
Cdd:pfam07111 21 LERRLD---TQRPTVTMWEQDVSGDGQGPGRRGRSLELEGSQALSQQAELISRQLQelrRLEEEVRLLReTSLQQKMRLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1456 GGA-EGELQALRARAEEAEAQK-RQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKqralqALEELRLQAE 1533
Cdd:pfam07111 98 AQAmELDALAVAEKAGQAEAEGlRAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLTQAHEE-----ALSSLTSKAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1534 EAERRLRQAEAERARQVQvALETAQRsaEAELQSEHASFAEKTAQLERTLKEEHVAVV--QLREEATRRAQQQAEAERAR 1611
Cdd:pfam07111 173 GLEKSLNSLETKRAGEAK-QLAEAQK--EAELLRKQLSKTQEELEAQVTLVESLRKYVgeQVPPEVHSQTWELERQELLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1612 AEAERELERWQLKAN-EALRLRLQaeevaqqkSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEG 1690
Cdd:pfam07111 250 TMQHLQEDRADLQATvELLQVRVQ--------SLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1691 TAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQReaaAATQKRRELEAELAKVRA-EMEVLLASKARAEEESRSTS 1769
Cdd:pfam07111 322 LKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQR---ALQDKAAEVEVERMSAKGlQMELSRAQEARRRQQQQTAS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1770 EKSKQRLEAEAGRFRELAEEAARLRaLAEEAKRQRQLAEE--DAVRQRAEAERVLAEKLAAIS---EATRLKTEAEIALK 1844
Cdd:pfam07111 399 AEEQLKFVVNAMSSTQIWLETTMTR-VEQAVARIPSLSNRlsYAVRKVHTIKGLMARKVALAQlrqESCPPPPPAPPVDA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1845 EKEAENERLRRlaedeafQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKA 1924
Cdd:pfam07111 478 DLSLELEQLRE-------ERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVA 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1925 AAGKAELELELGRIRGTAEDTLRSKEQAEQEA-----ARQRQLAAEEERRRREAEERVQK---SLAAEEEAARQRKAALE 1996
Cdd:pfam07111 551 RQGQQESTEEAASLRQELTQQQEIYGQALQEKvaeveTRLREQLSDTKRRLNEARREQAKavvSLRQIQHRATQEKERNQ 630
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 1997 EVERLK--AKVEEARRLRERAEQ-ESARQLQLAQEAAQKRLQAEEKAHAFAV 2045
Cdd:pfam07111 631 ELRRLQdeARKEEGQRLARRVQElERDKNLMLATLQQEGLLSRYKQQRLLAV 682
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1356-1562 |
2.68e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1356 LEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEvaRREEVAVEAQEQKRSIQEELQHLrQSSEAEIQAKARQVEAaersrl 1435
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLE--AKELLLRERNQQRQEARREREEL-QREEERLVQKEEQLDA------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1436 RIEEeirvvrlqLEATERQRGGAEgelQALRARAEEAEAQKRQAQEEAERLrrqvqdETQRKRQAEAELALRVQAEAEaa 1515
Cdd:PRK12705 96 RAEK--------LDNLENQLEERE---KALSARELELEELEKQLDNELYRV------AGLTPEQARKLLLKLLDAELE-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1920237970 1516 REKQRALQALEelrlqaEEAerrlrQAEAERARQVQVAlETAQRSAE 1562
Cdd:PRK12705 157 EEKAQRVKKIE------EEA-----DLEAERKAQNILA-QAMQRIAS 191
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1326-1598 |
2.73e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.94 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1326 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEaHAQAKAQAEREAQGLQRRMQEevARREEVAVEAQEQKRSI 1405
Cdd:pfam03528 96 DEVKSQWQEEVASLQAIMKETVREYEVQFHRRLEQERAQ-WNQYRESAEREIADLRRRLSE--GQEEENLEDEMKKAQED 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1406 QEELQHLRQSSEAEIQA-KARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALraraeeaEAQKRQAQEEAE 1484
Cdd:pfam03528 173 AEKLRSVVMPMEKEIAAlKAKLTEAEDKIKELEASKMKELNHYLEAEKSCRTDLEMYVAVL-------NTQKSVLQEDAE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1485 RLRRQVQDETQRkrqaeaeLALRVQAEAEAAREKQRAL-QALEELRLQAEEAERRLRQAEAERARQVqvalETAQRSAEA 1563
Cdd:pfam03528 246 KLRKELHEVCHL-------LEQERQQHNQLKHTWQKANdQFLESQRLLMRDMQRMESVLTSEQLRQV----EEIKKKDQE 314
|
250 260 270
....*....|....*....|....*....|....*
gi 1920237970 1564 ELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAT 1598
Cdd:pfam03528 315 EHKRARTHKEKETLKSDREHTVSIHAVFSPAGVET 349
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1668-1812 |
2.85e-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: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1668 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1747
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237970 1748 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAV 1812
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAI 356
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2144-2308 |
2.91e-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: 42.60 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2144 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQ 2223
Cdd:COG1579 9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2224 mEELGKLKARIEAENRALVLRDkDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2303
Cdd:COG1579 89 -KEYEALQKEIESLKRRISDLE-DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*
gi 1920237970 2304 QAVQE 2308
Cdd:COG1579 167 ELAAK 171
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
851-1808 |
2.95e-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: 44.01 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 851 EAQEAIARLEAQHQALVAlwhQLHTEMKSLLAWQSLGRDMQLIRSWSLATFRTLKpEEQRQALRSLELHYQAFLRDSQDA 930
Cdd:pfam01576 219 DLQEQIAELQAQIAELRA---QLAKKEEELQAALARLEEETAQKNNALKKIRELE-AQISELQEDLESERAARNKAEKQR 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 931 GGFGPE-DRLQAEREYGSCSRHYQQLLQSleQGEQEESRCQRCISElkdirlqleacETRtVHRLRLPLDKEPARECAQR 1009
Cdd:pfam01576 295 RDLGEElEALKTELEDTLDTTAAQQELRS--KREQEVTELKKALEE-----------ETR-SHEAQLQEMRQKHTQALEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1010 ITEQQKaQAEVDGLGKGVARLSAEAEkVLALPEPSPAAPTLRSELELTLGKLE-QVRSLSAIYLEKLKtislvirstQEA 1088
Cdd:pfam01576 361 LTEQLE-QAKRNKANLEKAKQALESE-NAELQAELRTLQQAKQDSEHKRKKLEgQLQELQARLSESER---------QRA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1089 EEVLRAHEEQLkEAQAVPATLPELEATKAALKKLRAQAEAQ-QPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1167
Cdd:pfam01576 430 ELAEKLSKLQS-ELESVSSLLNEAEGKNIKLSKDVSSLESQlQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1168 VtlllerwqavlaqtdVRQRELEqlgRQLRyyresadPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIEr 1247
Cdd:pfam01576 509 E---------------EAKRNVE---RQLS-------TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE- 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1248 hgEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPK----VQSGSESIIQEYVDLRTRYS----ELSTLTSQ 1319
Cdd:pfam01576 563 --EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKkfdqMLAEEKAISARYAEERDRAEaearEKETRALS 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1320 YIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEreaqglqrRMQEEVARREEVAVEAQ 1399
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVE--------EMKTQLEELEDELQATE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1400 EQKRSIQEELQHLRQSSEAEIQAKArqvEAAERSRLRIEEEIRVVRLQLEATERQRGGA-------EGELQALRARAEEA 1472
Cdd:pfam01576 713 DAKLRLEVNMQALKAQFERDLQARD---EQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAA 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1473 EAQKRQAQEEAERLRRQVQDetqrkRQAEAELALRVQAEAEA-AREKQRALQALEELRLQAEE----AERRLRQAEAERA 1547
Cdd:pfam01576 790 NKGREEAVKQLKKLQAQMKD-----LQRELEEARASRDEILAqSKESEKKLKNLEAELLQLQEdlaaSERARRQAQQERD 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1548 R-QVQVALETAQRSAeaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQqaeaeraraeaerelerwqlkaN 1626
Cdd:pfam01576 865 ElADEIASGASGKSA---LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQ----------------------V 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1627 EALRLRLQAEEVAQQKSltqaeaekqkeeaerearrrgkaeEQAVRQRELAEQELEKQRQLAEGTAQQRLAAeqELIRLR 1706
Cdd:pfam01576 920 EQLTTELAAERSTSQKS------------------------ESARQQLERQNKELKAKLQEMEGTVKSKFKS--SIAALE 973
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1707 AETEQgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVRAEMEvllaSKARAEEESRSTSEKSKQRLEAEAGRFREL 1786
Cdd:pfam01576 974 AKIAQ-------LEEQLEQESRERQAANKLVRRTEKKLKEVLLQVE----DERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
970 980
....*....|....*....|..
gi 1920237970 1787 AEEAArlRALAEEAKRQRQLAE 1808
Cdd:pfam01576 1043 EEEAS--RANAARRKLQRELDD 1062
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1410-1899 |
3.00e-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: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1410 QHLRQSSEAEIQAKARqVEAAERSRLRIEEEIRVVRLQLEATERQRGGA--EGELQALRARAEEAEAQKRQAQEEAERLR 1487
Cdd:COG3064 2 QEALEEKAAEAAAQER-LEQAEAEKRAAAEAEQKAKEEAEEERLAELEAkrQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1488 RQVQDETQRKRQAEAELAlRVQAEAEAAREKQRALQALEELRLQAEEaerrlRQAEAERARQVQVALETAQRSAEAELQS 1567
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKA-KAAKEAEAAAAAEKAAAAAEKEKAEEAK-----RKAEEEAKRKAEEERKAAEAEAAAKAEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1568 EHASFAEKTAQLERTLKEEhVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQA 1647
Cdd:COG3064 155 EAARAAAAAAAAAAAAAAR-AAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1648 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQ 1727
Cdd:COG3064 234 LAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1728 REAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA 1807
Cdd:COG3064 314 EEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1808 EEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRK 1887
Cdd:COG3064 394 AAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDG 473
|
490
....*....|..
gi 1920237970 1888 ASESELERQKGL 1899
Cdd:COG3064 474 GAVLADLLLLGG 485
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
509-603 |
3.09e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.01 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 509 LRYLQDLLAWVEENQRRLDSAEWGVDLPSVEAQLGSHRGLHQSVEEFRTKIERARTDEGQL---SPATRGAYRDCLGRLD 585
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1920237970 586 LQYAKLLSSSKARLRSLE 603
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1335-1596 |
3.16e-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: 43.66 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1335 ERLAEQQRAEERERLAEVEaALEKQRQLAEAHAQAkaqaereaqgLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRq 1414
Cdd:pfam10174 453 ERLKEQREREDRERLEELE-SLKKENKDLKEKVSA----------LQPELTEKESSLIDLKEHASSLASSGLKKDSKLK- 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1415 SSEAEIQA-------------KARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQK----- 1476
Cdd:pfam10174 521 SLEIAVEQkkeecsklenqlkKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKndkdk 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1477 ----------RQAQEEAERLR--RQVQDETQRKRQAEAELALRVQ-AEAEAAREKQRA--LQALEELRLQAEEAERRLRQ 1541
Cdd:pfam10174 601 kiaelesltlRQMKEQNKKVAniKHGQQEMKKKGAQLLEEARRREdNLADNSQQLQLEelMGALEKTRQELDATKARLSS 680
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237970 1542 AE--------------AERARQVQVALETAQRSAEAELQSEHASFA--EKTAQLERTLKEEhvaVVQLREE 1596
Cdd:pfam10174 681 TQqslaekdghltnlrAERRKQLEEILEMKQEALLAAISEKDANIAllELSSSKKKKTQEE---VMALKRE 748
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2263-2506 |
3.19e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.56 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2263 VAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML--KEKMQAVQEATRLKAEAELLQQQKELAQEQAR--------- 2331
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYlaKEEDLKRQNAVLQEAQVELDALQNQLALARAEmenikavat 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2332 ----RLQEDKEQMAQQLAQETQGFQKTL-ETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRfrkqaedigerlyR 2406
Cdd:pfam03528 86 vsenTKQEAIDEVKSQWQEEVASLQAIMkETVREYEVQFHRRLEQERAQWNQYRESAEREIADLRR-------------R 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2407 TELATQEkvmlvQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQA--------- 2477
Cdd:pfam03528 153 LSEGQEE-----ENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKELNHYLEAekscrtdle 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1920237970 2478 -------LQQSFLSEKDSLLQRE-----RCIEQEKAKLEQL 2506
Cdd:pfam03528 228 myvavlnTQKSVLQEDAEKLRKElhevcHLLEQERQQHNQL 268
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2269-2387 |
3.62e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2269 RLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEA---TRLKAEAELLQQQKELaQEQARRLQEDKEQMAQQLA 2345
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEihkLRNEFEKELRERRNEL-QKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 2346 ------QETQGFQKTLETERQRQLEMSAEAERLR-------LRVAEMSRAQARAE 2387
Cdd:PRK12704 104 llekreEELEKKEKELEQKQQELEKKEEELEELIeeqlqelERISGLTAEEAKEI 158
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2716-2749 |
3.64e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.64e-03
10 20 30
....*....|....*....|....*....|....
gi 1920237970 2716 LLEAQAASGFLLDPVRNRRLAVNEAVKEGIVGPE 2749
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3747-3778 |
3.64e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.64e-03
10 20 30
....*....|....*....|....*....|..
gi 1920237970 3747 RLLSAERAVTGYRDPYTEQTISLFQAMKKDLI 3778
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1413-1566 |
3.65e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.80 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1413 RQSSEAEIQAKARQVEA-AERSRLRIE-EEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQV 1490
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-RRVL 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 1491 QDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQ 1566
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2249-2382 |
3.70e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.47 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2249 AQRLLQE-----EAEKMK-QVAEEAAR---LSVAAQEAARlrQLAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELL 2319
Cdd:PTZ00491 672 AELLEQEargrlERQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRI 748
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237970 2320 QQQKELAQEQARRLQEdkeqmaqqLAQETQgfQKTLETERQRQLeMSAEAERL--------RLRVAEMSRA 2382
Cdd:PTZ00491 749 EAEAELEKLRKRQELE--------LEYEQA--QNELEIAKAKEL-ADIEATKFerivealgRETLIAIARA 808
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1172-1445 |
3.88e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1172 LERWQAVLAQTDVRQRELEQLGRQLryyrESADplgawlRDAKQRQEQIQAVPLANSQAVREQLrqEKALLEDIERhgeK 1251
Cdd:PRK11281 65 LEQTLALLDKIDRQKEETEQLKQQL----AQAP------AKLRQAQAELEALKDDNDEETRETL--STLSLRQLES---R 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1252 VEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYVDLRTRYSelSTLTSQyiRFISETLR-R 1330
Cdd:PRK11281 130 LAQTLDQLQNAQNDLAEYNSQLVSLQTQPE---------RAQAALYANSQRLQQIRNLLK--GGKVGG--KALRPSQRvL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1331 MEEEERLAEQQRAEERERLA---EVEAALEKQRQLAEAHAQakaQAEREAQGLQRRM-QEEVARREEVAVEAQEQKRS-- 1404
Cdd:PRK11281 197 LQAEQALLNAQNDLQRKSLEgntQLQDLLQKQRDYLTARIQ---RLEHQLQLLQEAInSKRLTLSEKTVQEAQSQDEAar 273
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1405 ------IQEELQHLRQSSEAEIQAKAR-------------QVEAAERSRLRIEEEIRVVR 1445
Cdd:PRK11281 274 iqanplVAQELEINLQLSQRLLKATEKlntltqqnlrvknWLDRLTQSERNIKEQISVLK 333
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1461-1595 |
3.93e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1461 ELQALRARAEEAEAQKRQAQEEAERLRRQVQdetqrkrqaE-AELALRVQAEAEAAREKQRaLQALEELRLQAEEAERRL 1539
Cdd:COG0497 166 AWRALKKELEELRADEAERARELDLLRFQLE---------ElEAAALQPGEEEELEEERRR-LSNAEKLREALQEALEAL 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 1540 RQAEAerarQVQVALETAQRSAEaELQSEHASFAEKTAQLERtlkeehvAVVQLRE 1595
Cdd:COG0497 236 SGGEG----GALDLLGQALRALE-RLAEYDPSLAELAERLES-------ALIELEE 279
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1053-1269 |
3.95e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1053 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKAALkklraqaEAQQPV 1132
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-------DASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1133 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDvrqrELEQLGRQLRYYResadpLGAWLRD 1212
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE----AAEDLARLELRAL-----LEERFAA 757
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 1213 AKQRqeqiqavplANSQAVREQLRQE-KALLEDIERHGEKVEEC-QRFAKQYINAIKDY 1269
Cdd:COG4913 758 ALGD---------AVERELRENLEERiDALRARLNRAEEELERAmRAFNREWPAETADL 807
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1682-1955 |
4.01e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 42.92 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1682 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQllEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASK 1758
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQ--YDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1759 ARAEEESRSTSEK---SKQRLEAEAGRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAVRQRAEA 1818
Cdd:pfam03148 81 RRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAARHKLEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1819 ErvLAEKLAAI---SEATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRLLE--EQAAQHKADIEARLAQLRKASES 1891
Cdd:pfam03148 159 D--LSDKKEALeidEKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIEraEKERAASAQLRELIDSILEQTAN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 1892 ELERQKGLVEDTLRQRrqVEEeilalkgsFEKAaagKAELELELGRIRgtaedtlrsKEQAEQE 1955
Cdd:pfam03148 237 DLRAQADAVNFALRKR--IEE--------TEDA---KNKLEWQLKKTL---------QEIAELE 278
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2304-2601 |
4.13e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.32 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2304 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRvaemsrAQ 2383
Cdd:pfam02029 6 EAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQK------RL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2384 ARAEEDARRFRKQAEDIGErlyrtELATQEKVMLVQTLETQRQQSDRDAERLREAIAELE------------------HE 2445
Cdd:pfam02029 80 QEALERQKEFDPTIADEKE-----SVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEirekeyqenkwstevrqaEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2446 KDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQ 2525
Cdd:pfam02029 155 EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2526 QQMQQEKQQLAA--SMEEARRRQHEAEEgvrrqqEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRA-------AL 2596
Cdd:pfam02029 235 EREEEAEVFLEAeqKLEELRRRRQEKES------EEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRrkqeeaeRK 308
|
....*
gi 1920237970 2597 ARSEE 2601
Cdd:pfam02029 309 LREEE 313
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1798-2047 |
4.16e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1798 EEAKRQRQLAEEDAVRQRAEAERVLAEKLAA-ISEATRLKTEAEIALKEKEAENerlrrlaedeafqrrlLEEQAAQHKA 1876
Cdd:PRK07735 2 DPEKDLEDLKKEAARRAKEEARKRLVAKHGAeISKLEEENREKEKALPKNDDMT----------------IEEAKRRAAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1877 DIEARLAQLRKASESELERQkglvedtlrqrrqVEEEILALKGSFEKAAAGKAElELELGRIRGTAEDTLRSKEQAEQEA 1956
Cdd:PRK07735 66 AAKAKAAALAKQKREGTEEV-------------TEEEKAKAKAKAAAAAKAKAA-ALAKQKREGTEEVTEEEKAAAKAKA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1957 ARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQA 2036
Cdd:PRK07735 132 AAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAA 211
|
250
....*....|.
gi 1920237970 2037 EEKAHAFAVQQ 2047
Cdd:PRK07735 212 KAKAAALAKQK 222
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2261-2602 |
4.16e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2261 KQVAEEAARLSVAA--QEAARLRQLAEEDLAQQRALAEKmlkekmqavqEATRLKAEAELLQQQKELAQEQARR--LQED 2336
Cdd:PRK04863 260 KHLITESTNYVAADymRHANERRVHLEEALELRRELYTS----------RRQLAAEQYRLVEMARELAELNEAEsdLEQD 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2337 KEQMA--QQLAQETQGFQKTLE------TERQRQLEMSAEAERLRLRVAEMSRAQA-RAEEDARRFRKQAEDIGERL--- 2404
Cdd:PRK04863 330 YQAASdhLNLVQTALRQQEKIEryqadlEELEERLEEQNEVVEEADEQQEENEARAeAAEEEVDELKSQLADYQQALdvq 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2405 YRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEaqLLQLksEEMQTVRQEQLLQETQALQ--QSF 2482
Cdd:PRK04863 410 QTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEE--LLSL--EQKLSVAQAAHSQFEQAYQlvRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2483 LSEKDsllqRERCIEQEKAKLEQL--FQDEVAKAQALReeqqrqqqqmqqekqqlaASMEEARRRQHEAEEGVRRQQEEL 2560
Cdd:PRK04863 486 AGEVS----RSEAWDVARELLRRLreQRHLAEQLQQLR------------------MRLSELEQRLRQQQRAERLLAEFC 543
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1920237970 2561 QRLAQQQQQQEkLLAEENQRLRERLQHLEEERRAALARSEEI 2602
Cdd:PRK04863 544 KRLGKNLDDED-ELEQLQEELEARLESLSESVSEARERRMAL 584
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1474-1946 |
4.44e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1474 AQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQR--ALQALEELRLQAEEAERRLRQAEAERARQvQ 1551
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELeaKRQAEEEAREAKAEAEQRAAELAAEAAKK-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1552 VALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVA----VVQLREEATRRAQQQAEAERARAEAERELERWQLKANE 1627
Cdd:COG3064 80 AEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAekekAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1628 ALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRA 1707
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1708 ETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELA 1787
Cdd:COG3064 240 TEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1788 EEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLL 1867
Cdd:COG3064 320 AAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237970 1868 EEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTL 1946
Cdd:COG3064 400 LLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLA 478
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1362-1549 |
4.46e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.92 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1362 LAEAHAQAKAQAEREAQGLQRRMQEEVARreevaveAQEQKRSIQEELQHLRQsseaeiqakarqveaaERSRLRIEEEI 1441
Cdd:COG3524 160 LAESEELVNQLSERAREDAVRFAEEEVER-------AEERLRDAREALLAFRN----------------RNGILDPEATA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1442 RVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAL-RVQAEaeaarekqr 1520
Cdd:COG3524 217 EALLQLIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLaSLLAE--------- 287
|
170 180 190
....*....|....*....|....*....|.
gi 1920237970 1521 alqaLEELRLQAEEAERRLRQAEA--ERARQ 1549
Cdd:COG3524 288 ----YERLELEREFAEKAYTSALAalEQARI 314
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1428-1545 |
4.49e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1428 EAAerSRLRIE-----EEIRVVRLQLEATERqrggaegELQALRaraeeaEAQKRQAQEEAERLRRQVQDETQRKRQAEA 1502
Cdd:COG0542 397 EAA--ARVRMEidskpEELDELERRLEQLEI-------EKEALK------KEQDEASFERLAELRDELAELEEELEALKA 461
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237970 1503 elalRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAE 1545
Cdd:COG0542 462 ----RWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEE 500
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1436-1566 |
4.51e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1436 RIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAA 1515
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDLAREALERKAELEAQ 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 1516 REKQRAL-----QALEELRLQAEEAERRLRQAEAERArqvqvALETAQRSAEAELQ 1566
Cdd:COG1842 100 AEALEAQlaqleEQVEKLKEALRQLESKLEELKAKKD-----TLKARAKAAKAQEK 150
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1363-1551 |
4.55e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.35 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1363 AEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEir 1442
Cdd:PRK12678 67 AATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1443 vvRLQLEATERQRGGAEGELQALRARAEEAEA--QKRQAQEEAERLRRQVQDETQRKRQaEAELALRVQAEAEAAREKQR 1520
Cdd:PRK12678 145 --AGEGGEQPATEARADAAERTEEEERDERRRrgDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRREERGRR 221
|
170 180 190
....*....|....*....|....*....|.
gi 1920237970 1521 ALQALEELRLQAEEAERRLRQAEAERARQVQ 1551
Cdd:PRK12678 222 DGGDRRGRRRRRDRRDARGDDNREDRGDRDG 252
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2164-2597 |
4.66e-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: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2164 ALRQKAQVEQ-ELTALRLQLEEtdhQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEaeNRALV 2242
Cdd:pfam10174 335 AKEQRAAILQtEVDALRLRLEE---KESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE--NLQEQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2243 LRDKDsaqRLLQEEAEKMKQVAEEAARLSVA---AQEAARLRQLAEEDLAQQRALAEKMLKEKMQAV-QEATRLKAEAEL 2318
Cdd:pfam10174 410 LRDKD---KQLAGLKERVKSLQTDSSNTDTAlttLEEALSEKERIIERLKEQREREDRERLEELESLkKENKDLKEKVSA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2319 LQQQKelaQEQARRLQEDKEQmAQQLAQ---ETQGFQKTLETERQRQLEmsaEAERLrlrVAEMSRAQaRAEEDARrfrk 2395
Cdd:pfam10174 487 LQPEL---TEKESSLIDLKEH-ASSLASsglKKDSKLKSLEIAVEQKKE---ECSKL---ENQLKKAH-NAEEAVR---- 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2396 QAEDIGERLYRTELATQEKVMlvqtlETQRQQSDrdAERLREAIAELEHEK-DKLKQEAQLLQLKSEEMQTvrQEQLLQE 2474
Cdd:pfam10174 552 TNPEINDRIRLLEQEVARYKE-----ESGKAQAE--VERLLGILREVENEKnDKDKKIAELESLTLRQMKE--QNKKVAN 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2475 TQALQQsflsekdsllqrercieQEKAKLEQLFQDevakaqALREEQQRQQQQMQQEKQQLAASMEEARRrqhEAEEGVR 2554
Cdd:pfam10174 623 IKHGQQ-----------------EMKKKGAQLLEE------ARRREDNLADNSQQLQLEELMGALEKTRQ---ELDATKA 676
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1920237970 2555 RQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALA 2597
Cdd:pfam10174 677 RLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAAIS 719
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1871-2047 |
4.81e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1871 AAQHKADIEARLAQLRKasesELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKE 1950
Cdd:COG4942 18 QADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1951 QAEQEAARQRQLAAEEERRRREAEER--------------VQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRErAE 2016
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE-AE 172
|
170 180 190
....*....|....*....|....*....|.
gi 1920237970 2017 QESARQLQLAQEAAQKRLQAEEKAHAFAVQQ 2047
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLAR 203
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2093-2279 |
4.83e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.02 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2093 QSRRQVEEAERLKQsAEEQAQAQAQAQAAAEKLRKeaeqeaarraqaeqAALRQKQAADAEMEKHKQFAEQALRQKAQVE 2172
Cdd:pfam15709 360 QRRLQQEQLERAEK-MREELELEQQRRFEEIRLRK--------------QRLEEERQRQEEEERKQRLQLQAAQERARQQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2173 QEltALRLQLEETDHQKsildeelQRLKAEVTEAARQRGQVEEElfslrvQMEELGKLKARIEAENRALVLRDKDSAQRL 2252
Cdd:pfam15709 425 QE--EFRRKLQELQRKK-------QQEEAERAEAEKQRQKELEM------QLAEEQKRLMEMAEEERLEYQRQKQEAEEK 489
|
170 180 190
....*....|....*....|....*....|..
gi 1920237970 2253 LQEEAEKMKQVAEEAARLSVA-----AQEAAR 2279
Cdd:pfam15709 490 ARLEAEERRQKEEEAARLALEeamkqAQEQAR 521
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1666-1766 |
4.86e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1666 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELA 1745
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|.
gi 1920237970 1746 KvRAEMEVLLaskarAEEESR 1766
Cdd:PRK11448 223 D-QAAKRLEL-----SEEETR 237
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1708-1930 |
4.94e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 42.66 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1708 ETEQGEQQRQLLEEELARLQ-----------REAAAATQKRRELEAELAKVRAEMEV-----LLASKARAEEESRSTSEK 1771
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHgaeiskleeenREKEKALPKNDDMTIEEAKRRAAAAAkakaaALAKQKREGTEEVTEEEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1772 SKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED--AVRQRAEAERVLAEKLAAISEATRLKTEAEIAL---KEK 1846
Cdd:PRK07735 91 AKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAkaAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKakaKAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1847 EAENERLRRLAEDEAFQRRLLEEQAAQH-KADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEE-ILALKGSFEKA 1924
Cdd:PRK07735 171 AAAKAKAAALAKQKAAEAGEGTEEVTEEeKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKaIAAAKAKAAAA 250
|
....*.
gi 1920237970 1925 AAGKAE 1930
Cdd:PRK07735 251 ARAKTK 256
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2314-2557 |
4.94e-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: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2314 AEAELLQQQKEL--AQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDAR 2391
Cdd:COG3883 14 ADPQIQAKQKELseLQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2392 RFRKQ------------AEDIGE---RLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLL 2456
Cdd:COG3883 94 ALYRSggsvsyldvllgSESFSDfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2457 QLKSEEmqtvrQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLA 2536
Cdd:COG3883 174 EAQQAE-----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
250 260
....*....|....*....|.
gi 1920237970 2537 ASMEEARRRQHEAEEGVRRQQ 2557
Cdd:COG3883 249 AGAAGAAGAAAGSAGAAGAAA 269
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2225-2353 |
4.96e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2225 EELGKLKARIEAENRALVLRDKDSAQrlLQEeaekmkQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQ 2304
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQD------SVANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237970 2305 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ----------QLAQETQGFQK 2353
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAKiadlgrrlnvALAQRVQELNR 194
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2258-2352 |
4.98e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 42.27 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2258 EKMKQVAEEAARLSVAAQEAARLRQLAEEDL----AQQRALAE--KMLKEKMQAVQEatRLKAEAELLQQQKElaQEQAR 2331
Cdd:pfam02841 201 AKEKAIEAERAKAEAAEAEQELLREKQKEEEqmmeAQERSYQEhvKQLIEKMEAERE--QLLAEQERMLEHKL--QEQEE 276
|
90 100
....*....|....*....|.
gi 1920237970 2332 RLQEDKEQMAQQLAQETQGFQ 2352
Cdd:pfam02841 277 LLKEGFKTEAESLQKEIQDLK 297
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1332-1519 |
5.39e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.06 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1332 EEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAER--------EAQGLQRRMQ-----EEVARREEVAVEA 1398
Cdd:TIGR00927 649 GERPTEAEGENGEESGGEAEQE---GETETKGENESEGEIPAERkgeqegegEIEAKEADHKgeteaEEVEHEGETEAEG 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1399 QEQKRSIQ--EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQA---LRARAEEAE 1473
Cdd:TIGR00927 726 TEDEGEIEtgEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGE--------TEAEGKEDEDEGEIQAgedGEMKGDEGA 797
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1920237970 1474 AQKRQAQEEAERlRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ 1519
Cdd:TIGR00927 798 EGKVEHEGETEA-GEKDEHEGQSETQADDTEVKDETGEQELNAENQ 842
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1785-1913 |
5.48e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1785 ELAEEAARLRALAE-EAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 1863
Cdd:COG2268 196 EIIRDARIAEAEAErETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANA 275
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1920237970 1864 RRLLEEQAAQHKADIEARLAQLRKA-SESELERQKGLVEDTLRQRRQVEEE 1913
Cdd:COG2268 276 EREVQRQLEIAEREREIELQEKEAErEEAELEADVRKPAEAEKQAAEAEAE 326
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1330-1517 |
5.69e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.68 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1330 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQglqrrmQEEVARREEVAVEAQEQKRSIQEEL 1409
Cdd:pfam05262 206 RESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQ------QEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1410 QHLRQSSEAEIQAKARQVeaaersrlrieeeirvvrlqLEATERQRGGAEGElqalrARAEEAEAQKRqaQEEAERLRRQ 1489
Cdd:pfam05262 280 KREIEKAQIEIKKNDEEA--------------------LKAKDHKAFDLKQE-----SKASEKEAEDK--ELEAQKKREP 332
|
170 180
....*....|....*....|....*....
gi 1920237970 1490 VQDETQR-KRQAEAElalrVQAEAEAARE 1517
Cdd:pfam05262 333 VAEDLQKtKPQVEAQ----PTSLNEDAID 357
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1456-1596 |
5.78e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1456 GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQrkrqaEAELALRVQAEAEAAREKQralqaleelRLQAEEa 1535
Cdd:PRK12705 19 GVLVVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAK-----ELLLRERNQQRQEARRERE---------ELQREE- 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 1536 ERRLRQAEAERARQVQVALETAQRS-AEAELQSEHASFAEKTAQLERTLKEehvaVVQLREE 1596
Cdd:PRK12705 84 ERLVQKEEQLDARAEKLDNLENQLEeREKALSARELELEELEKQLDNELYR----VAGLTPE 141
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1305-1566 |
5.79e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 42.33 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1305 DLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQRAEERERLAEVEAAlekQRQLAEAHAQaKAQAEREAQGLQRRM 1384
Cdd:COG1538 77 EVAQAYFDLLAAQEQ-LALAEENLALAEELLELARARYEAGLASRLDVLQA---EAQLAQARAQ-LAQAEAQLAQARNAL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1385 QEEVARREEVAVEAQEQKRSIQEELQHLRQSSEA------EIQAKARQVEAAERsRLRIEEEIRVVRLQLEATERQRGGA 1458
Cdd:COG1538 152 ALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEalerrpDLRAAEAQLEAAEA-EIGVARAAFLPSLSLSASYGYSSSD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1459 EGELQ-------------------ALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ 1519
Cdd:COG1538 231 DLFSGgsdtwsvglslslplfdggRNRARVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEAAE 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 1520 RALQALEEL-------RLQAEEAERRLRQAEAERarqvqVALETAQRSAEAELQ 1566
Cdd:COG1538 311 EALELARARyraglasLLDVLDAQRELLQAQLNL-----IQARYDYLLALVQLY 359
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1779-1888 |
5.80e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1779 EAGRFRELAEEAARLRALAEEAKRQRQLAEE--------DAVRQRAEAERVLAEKLAAISEATRLKTEAEIA-LKEKEAE 1849
Cdd:PRK11448 130 KPGPFVPPEDPENLLHALQQEVLTLKQQLELqarekaqsQALAEAQQQELVALEGLAAELEEKQQELEAQLEqLQEKAAE 209
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237970 1850 NErlrrlAEDEAFQRRLLEEQAAQHKAD-IEARL---AQLRKA 1888
Cdd:PRK11448 210 TS-----QERKQKRKEITDQAAKRLELSeEETRIlidQQLRKA 247
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1458-1567 |
5.83e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1458 AEGELQALRARAE-EAEAQKR----QAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALE-ELRLQ 1531
Cdd:PRK12704 36 AEEEAKRILEEAKkEAEAIKKeallEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREeELEKK 115
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237970 1532 AEEAERRLRQAEAERARqvqvaLETAQRSAEAELQS 1567
Cdd:PRK12704 116 EKELEQKQQELEKKEEE-----LEELIEEQLQELER 146
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1329-1736 |
6.19e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.72 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1329 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAK-AQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQE 1407
Cdd:COG3064 24 EKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEqRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1408 ELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLR 1487
Cdd:COG3064 104 AEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1488 RQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQS 1567
Cdd:COG3064 184 AAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1568 EHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQA 1647
Cdd:COG3064 264 LAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1648 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQ 1727
Cdd:COG3064 344 LAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVL 423
|
....*....
gi 1920237970 1728 REAAAATQK 1736
Cdd:COG3064 424 LALAGAAGA 432
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1105-1517 |
6.21e-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: 42.36 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1105 VPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGaqevgerLQQRHGERDVEVERWRERvtllLERWQAVLAQTDV 1184
Cdd:pfam19220 36 IEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAG-------LTRRLSAAEGELEELVAR----LAKLEAALREAEA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1185 RQRELEQLGRQLRYYRESADplgawlRDAKQRQEQIQAVPLANsQAVREQLRQEKALLEDIERHGEKVEECQRFAKQyin 1264
Cdd:pfam19220 105 AKEELRIELRDKTAQAEALE------RQLAAETEQNRALEEEN-KALREEAQAAEKALQRAEGELATARERLALLEQ--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1265 aikdyelqlvtykaqlepvaspaKKPKVQSGSESIIQEYVDLRTRYSELSTL---TSQYIRFISETLRRMEEEERLAEQQ 1341
Cdd:pfam19220 175 -----------------------ENRRLQALSEEQAAELAELTRRLAELETQldaTRARLRALEGQLAAEQAERERAEAQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1342 RAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLrqssEAEIQ 1421
Cdd:pfam19220 232 LEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGL----EADLE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1422 AKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRqae 1501
Cdd:pfam19220 308 RRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRLKEELQRER--- 384
|
410
....*....|....*.
gi 1920237970 1502 AELALrVQAEAEAARE 1517
Cdd:pfam19220 385 AERAL-AQGALEIARE 399
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1324-1432 |
6.24e-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: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1324 ISETLRR----MEEEE-RLAeqqRAEERERLAEVEAALEKQRQLAEahaqakaqAEREAQGLQRRMQEEVARReevavEA 1398
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLL---IAEQHQKVVEKEAETERKRAVIE--------AEKDAEVAKIQMQQKIMEK-----EA 223
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237970 1399 QEQKRSIQEELQHLRQSS--EAEIQAKARQVEAAER 1432
Cdd:cd03406 224 EKKISEIEDEMHLAREKAraDAEYYRALREAEANKL 259
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2161-2414 |
6.43e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2161 AEQALRQKAQVEQELTALRLQLEETDHQK----------SILDEELQRLKAEVTEAARQRGQVEEELF-SLRVQMEELGK 2229
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLSETDARIklaaqekihvEILEEQLEKLRNELLIRGATEGLCVHSLSkELDVLKEENML 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2230 LKARIEAEnRALVLRDKDSAQRLLQEEAEKM---KQVAEEAARLSVAAQEAARLRQLAEED------------------- 2287
Cdd:PLN02939 238 LKDDIQFL-KAELIEVAETEERVFKLEKERSlldASLRELESKFIVAQEDVSKLSPLQYDCwwekvenlqdlldratnqv 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2288 ------LAQQRALAEK--MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTL---- 2355
Cdd:PLN02939 317 ekaalvLDQNQDLRDKvdKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLsklk 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237970 2356 ETERQRQLEMSAEA------ERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEK 2414
Cdd:PLN02939 397 EESKKRSLEHPADDmpsefwSRILLLIDGWLLEKKISNNDAKLLREMVWKRDGRIREAYLSCKGK 461
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1107-1550 |
6.60e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1107 ATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDVRQ 1186
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1187 RELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAI 1266
Cdd:COG5278 163 LALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1267 KDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEER 1346
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1347 ERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQ 1426
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1427 VEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAL 1506
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1920237970 1507 RVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV 1550
Cdd:COG5278 483 ALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3672-3710 |
6.71e-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: 6.71e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1920237970 3672 YLYGTGCVAGIYRPGSRQTLTIYQALKKGQLSAEVARQL 3710
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1418-1571 |
6.77e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.58 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1418 AEIQAKARQVEAAERSRLRIEEEIrvvrlqlEATERQRGGAEGElqALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1497
Cdd:PRK12678 29 PELRALAKQLGIKGTSGMRKGELI-------AAIKEARGGGAAA--AAATPAAPAAAARRAARAAAAARQAEQPAAEAAA 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237970 1498 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHAS 1571
Cdd:PRK12678 100 AKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERR 173
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1693-2104 |
6.95e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1693 QQRLAAEQELIRLRAETEQGEQQRQLL---EEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTS 1769
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLdelEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1770 EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAE 1849
Cdd:COG5278 163 LALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1850 NERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKA 1929
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1930 ELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEAR 2009
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2010 RLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAER 2089
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
410
....*....|....*
gi 1920237970 2090 EAAQSRRQVEEAERL 2104
Cdd:COG5278 483 ALAEAEAAAALAAAA 497
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1922-2404 |
6.99e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1922 EKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERvQKSLAAEEEAARQRKAALEEVERL 2001
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2002 KAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRseaeaARRAAEEAE 2081
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE-----LQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2082 AARERAEREAAQSRRQVEEAERLKQsAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFA 2161
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2162 EQAL---------RQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAArqrgqveEELFSLRVQMEELGKLKA 2232
Cdd:COG4717 282 VLGLlallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP-------EELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2233 RIE-AENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLkekmqAVQEATR 2311
Cdd:COG4717 355 EAEeLEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-----EALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2312 LKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQ-ETQGFQKTLETERQRQLEMSAEAER--LRLRVAE--MSRAQARA 2386
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAEewAALKLALelLEEAREEY 509
|
490
....*....|....*....
gi 1920237970 2387 EEDAR-RFRKQAEDIGERL 2404
Cdd:COG4717 510 REERLpPVLERASEYFSRL 528
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1716-2028 |
7.11e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1716 RQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESrstsEKSKQRLEAEAGRFRELAEEAARLRA 1795
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1796 LAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHK 1875
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1876 ADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQE 1955
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237970 1956 AARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2028
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2192-2287 |
7.41e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2192 LDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALvlrdkdsAQRLLQEEAEKMKQVAEEAARLS 2271
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQEL-------EAQLEQLQEKAAETSQERKQKRK 219
|
90
....*....|....*.
gi 1920237970 2272 VAAQEAARLRQLAEED 2287
Cdd:PRK11448 220 EITDQAAKRLELSEEE 235
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1001-1598 |
7.68e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.48 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1001 EPARECAQRITEQQKAQAEVDGLGKGVARLSaeaekvLALPepspaAPTLRSELEltlGKLEQVRSLSAIYlEKLKTISL 1080
Cdd:PRK10246 254 ELQQEASRRQQALQQALAAEEKAQPQLAALS------LAQP-----ARQLRPHWE---RIQEQSAALAHTR-QQIEEVNT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1081 VIRSTQEAEEVLRAHeeQLKEAQAVPATLPELeatkaalkklrAQAEAQQPVFDALRDELRG-----AQEVGERLQQRhg 1155
Cdd:PRK10246 319 RLQSTMALRARIRHH--AAKQSAELQAQQQSL-----------NTWLAEHDRFRQWNNELAGwraqfSQQTSDREQLR-- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1156 erdveveRWRERVTLLLERWQAVLAQT-----DVRQRELEQLGRQlRYYRESADPLGAWLRDAKQRQEQIQAvplANSQA 1230
Cdd:PRK10246 384 -------QWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQV---AIQNV 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1231 VREQLRQEKALLEDIERHGEKVEE-------CQRFAKqyinaIKDYELQ--------------------LVTYKAqLEPV 1283
Cdd:PRK10246 453 TQEQTQRNAALNEMRQRYKEKTQQladvktiCEQEAR-----IKDLEAQraqlqagqpcplcgstshpaVEAYQA-LEPG 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1284 ASPAKKPKVQSGSESIIQEYVDLRtrySELSTLTSQYIRFISETLRRMEEEERLAEQQRaeererlaEVEAALEKQRQLA 1363
Cdd:PRK10246 527 VNQSRLDALEKEVKKLGEEGAALR---GQLDALTKQLQRDESEAQSLRQEEQALTQQWQ--------AVCASLNITLQPQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1364 EAHAQ-AKAQAEREAQGLQRRMQEEVarrEEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQV--EAAERSRL--RIE 1438
Cdd:PRK10246 596 DDIQPwLDAQEEHERQLRLLSQRHEL---QGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLpqEDEEASWLatRQQ 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1439 EEIRVVRLQLEATERQRGGAE--------GELQALRARAEEAEAQK-RQAQEEAERLRRQVQ-------DETQRKRQAEA 1502
Cdd:PRK10246 673 EAQSWQQRQNELTALQNRIQQltplletlPQSDDLPHSEETVALDNwRQVHEQCLSLHSQLQtlqqqdvLEAQRLQKAQA 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1503 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLrqaeaERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERT 1582
Cdd:PRK10246 753 QFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNL-----ENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQI 827
|
650
....*....|....*.
gi 1920237970 1583 LKEEHVAVVQLREEAT 1598
Cdd:PRK10246 828 QQELAQLAQQLRENTT 843
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2162-2603 |
7.73e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2162 EQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQ-RGQVEEELFSLRVQMEELGKLKARIEAENRA 2240
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2241 LVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEE------DLAQQRALAEKMLKEKMQAVQEATRLKA 2314
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEyaelkeELEDLRAELEEVDKEFAETRDELKDYRE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2315 EAELLQQQKELAQEQARRLQEDKEQMAQQLAQetqgFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFR 2394
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2395 KQAEDIGERLYRTELATQEKVMLVQTLETQRQQSdRDAERLREAIAELEHEKDK--LKQEAQLLQLKSE----------- 2461
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARAS-EERVRGGRAVEEVLKASIQgvHGTVAQLGSVGERyataievaagn 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2462 ---------EMQTVRQEQLLQETQALQQSFL-------SEKD-SLLQRERCI----------EQEKAKLEQLFQDEV--- 2511
Cdd:TIGR02169 548 rlnnvvvedDAVAKEAIELLKRRKAGRATFLplnkmrdERRDlSILSEDGVIgfavdlvefdPKYEPAFKYVFGDTLvve 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2512 ----------------------------------------------AKAQALREEQQRQQQQMQQEKQQLA---ASMEEA 2542
Cdd:TIGR02169 628 dieaarrlmgkyrmvtlegelfeksgamtggsraprggilfsrsepAELQRLRERLEGLKRELSSLQSELRrieNRLDEL 707
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237970 2543 RRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEenqrLRERLQHLEEERRAALARSEEIA 2603
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE----LEEDLSSLEQEIENVKSELKELE 764
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
1739-1860 |
7.83e-03 |
|
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.
Pssm-ID: 461196 Cd Length: 835 Bit Score: 42.61 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1739 ELEAELAKVRAEM--EVLLASKARAEEesrstseKSKQRLEAEAGRFR---ELAEEAARLRALAEEAKRQRQLAEEDAVR 1813
Cdd:pfam04147 155 EEEPERKKSKKEVmeEVIAKSKLHKYE-------RQKAKEEDEELREEldkELKDLRSLLSGSKRPKPEQAKKPEEKPDR 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237970 1814 QRAEAE-----RVLA-EKLAAISEatRLKTEAEIALKEKE----AENERLRRLAEDE 1860
Cdd:pfam04147 228 KKPDDDydklvRELAfDKRAKPSD--RTKTEEELAEEEKErlekLEEERLRRMRGEE 282
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1165-1436 |
8.00e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1165 RERVTLLLERWQAVLAQTDVR---QRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKAL 1241
Cdd:COG4942 2 RKLLLLALLLALAAAAQADAAaeaEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1242 LEDIERHGEKVEECQRFAKQYINAIKdyELQLVTYKAQLEPvaspakKPKVQSGSESIIQEYvdlrtRYSELSTLTSQYI 1321
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELA--ELLRALYRLGRQP------PLALLLSPEDFLDAV-----RRLQYLKYLAPAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1322 RFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRqlaeahaQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQ 1401
Cdd:COG4942 149 REQAEELRADLAELAALRAELEAERAELEALLAELEEER-------AALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
250 260 270
....*....|....*....|....*....|....*
gi 1920237970 1402 KRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLR 1436
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2222-2517 |
8.16e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.59 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2222 VQMEE---LGKLKARIEAEN-RALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLA-EEDLAQQRALAE 2296
Cdd:pfam15964 341 VQMTEeanFEKTKALIQCEQlKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLAlSQNVAQLEAQVE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2297 KMLKEKMQAVQEATrlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLAQETQgfqKTLETERQRQLEMS-AEAERLRL 2374
Cdd:pfam15964 421 KVTREKNSLVSQLE--EAQKQLASQEMDVTKVCGEmRYQLNQTKMKKDEAEKEH---REYRTKTGRQLEIKdQEIEKLGL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2375 RVAEMSRAQARAEEDARRFRKQAEDIGERLYRTE----LATQEKVMLVQTL----ETQRQQSDRDAERLREAIAELE--H 2444
Cdd:pfam15964 496 ELSESKQRLEQAQQDAARAREECLKLTELLGESEhqlhLTRLEKESIQQSFsneaKAQALQAQQREQELTQKMQQMEaqH 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2445 EKD----------------KLKQEAQLLQLKSEEM-QTVRQE--QLLQETQALQQSFLSEK-------DSLLQRERCIEQ 2498
Cdd:pfam15964 576 DKTvneqyslltsqntfiaKLKEECCTLAKKLEEItQKSRSEveQLSQEKEYLQDRLEKLQkrneeleEQCVQHGRMHER 655
|
330
....*....|....*....
gi 1920237970 2499 EKAKLEQLFQDEVAKAQAL 2517
Cdd:pfam15964 656 MKQRLRQLDKHCQATAQQL 674
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1665-1805 |
8.44e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 41.51 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1665 KAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA-- 1742
Cdd:pfam12037 52 KKQEQ-TRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELlr 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237970 1743 ---ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA-GRFRELAE-EAARLRALAEEAKRQRQ 1805
Cdd:pfam12037 131 kqeESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAeARAKEEREnEDLNLEQLREKANEERE 198
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2174-2517 |
8.45e-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: 42.31 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2174 ELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELG----KLKARIEA-ENralvlrDKDS 2248
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNnkynDLKKQKEElEN------ELNL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2249 AQRLLQEEAEKMKQVAEEAAR----LSVAAQEAARLRQLAEE--DLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQ 2322
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKlellLSNLKKKIQKNKSLESQisELKKQNNQLKDNIEKKQQEINE---KTTEISNTQTQ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2323 -KELAQEQarrlQEDKEQMAQQLAQETQGFQKTLETERQRQlEMSAEAERLRlrvaemsraqaraeedarrfRKQAEDIG 2401
Cdd:TIGR04523 255 lNQLKDEQ----NKIKKQLSEKQKELEQNNKKIKELEKQLN-QLKSEISDLN--------------------NQKEQDWN 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2402 ERLyRTELATQEKVmlVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQlkseemqtvrqEQLLQETQALQQs 2481
Cdd:TIGR04523 310 KEL-KSELKNQEKK--LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQ-----------RELEEKQNEIEK- 374
|
330 340 350
....*....|....*....|....*....|....*.
gi 1920237970 2482 FLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQAL 2517
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK 410
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2096-2477 |
8.54e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2096 RQVEEAERlkqsaeeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAeQALRQKAQVEQEL 2175
Cdd:pfam07888 73 RQRRELES--------------------RVAELKEELRQSREKHEELEEKYKELSASSEELSEEKD-ALLAQRAAHEARI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2176 TALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRAL--VLRDKDSAQRLL 2253
Cdd:pfam07888 132 RELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELrnSLAQRDTQVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2254 QEEAEKMKQVAEEAARlSVAAQEAAR--LRQLAEEDLAQQRALAekMLKEKMQAVQeATRLKAEAELLQQQKELAQ---- 2327
Cdd:pfam07888 212 QDTITTLTQKLTTAHR-KEAENEALLeeLRSLQERLNASERKVE--GLGEELSSMA-AQRDRTQAELHQARLQAAQltlq 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2328 --EQARRLQEDKEQMaqqlAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEmsraqaraeedARRFRKQAEdigerly 2405
Cdd:pfam07888 288 laDASLALREGRARW----AQERETLQQSAEADKDRIEKLSAELQRLEERLQE-----------ERMEREKLE------- 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 2406 rTELATQEKVMLVQTLETQRQQSDrdaerLREAIAELEHEKDKLKQEAQllqlksEEMQTVRQEQLLQETQA 2477
Cdd:pfam07888 346 -VELGREKDCNRVQLSESRRELQE-----LKASLRVAQKEKEQLQAEKQ------ELLEYIRQLEQRLETVA 405
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3671-3707 |
8.83e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 36.69 E-value: 8.83e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1920237970 3671 RYLYGTGCVAGIYRPGSRQTLTIYQALKKGQLSAEVA 3707
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1205-1405 |
9.22e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1205 PLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKVEECQRfakqyinAIKDYELQLVTYKAQL-EPV 1283
Cdd:PRK11637 37 AFSAHASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASR-------KLRETQNTLNQLNKQIdELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1284 ASPAKKPKVQSGSESIIQEYVDLRTRYSE-------LSTLTSQ-------YIRFISE----------------TLRRMEE 1333
Cdd:PRK11637 110 ASIAKLEQQQAAQERLLAAQLDAAFRQGEhtglqliLSGEESQrgerilaYFGYLNQarqetiaelkqtreelAAQKAEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1334 EERLAEQQ----------------RAEERERLAEVEAALEK-QRQLAE--------------AHAQAKAQAEREAQGLQR 1382
Cdd:PRK11637 190 EEKQSQQKtllyeqqaqqqkleqaRNERKKTLTGLESSLQKdQQQLSElranesrlrdsiarAEREAKARAEREAREAAR 269
|
250 260
....*....|....*....|....
gi 1920237970 1383 -RMQEEVARREEVAVEAQEQKRSI 1405
Cdd:PRK11637 270 vRDKQKQAKRKGSTYKPTESERSL 293
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1470-1533 |
9.24e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.55 E-value: 9.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237970 1470 EEAEAQKRQAQEEAERLRrqvQDETQRKRQAE--AELALRVQAEAEAAREKQRALQALEELRLQAE 1533
Cdd:PLN02316 253 EKRRELEKLAKEEAERER---QAEEQRRREEEkaAMEADRAQAKAEVEKRREKLQNLLKKASRSAD 315
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1673-1766 |
9.47e-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: 39.13 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1673 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLraeteqgEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEME 1752
Cdd:pfam20492 21 ETKKAQEELEESEETAEELEEERRQAEEEAERL-------EQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIA 93
|
90
....*....|....
gi 1920237970 1753 VLLASKARAEEESR 1766
Cdd:pfam20492 94 RLEEEVERKEEEAR 107
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2172-2602 |
9.64e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2172 EQELTALRLQLEETDHQKSILDEELQRLKAEVTeAARQRGQV-EEELFSLRVQMEElgklKARIEAEnRALVLRDKDSAQ 2250
Cdd:pfam10174 302 ESELLALQTKLETLTNQNSDCKQHIEVLKESLT-AKEQRAAIlQTEVDALRLRLEE----KESFLNK-KTKQLQDLTEEK 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2251 RLLQEEAEKMKQVAEEAARLSVAAQEaaRLRQLAEEDLAQQRALAEkmLKEKMQAVQEATRLKAEAelLQQQKELAQEQA 2330
Cdd:pfam10174 376 STLAGEIRDLKDMLDVKERKINVLQK--KIENLQEQLRDKDKQLAG--LKERVKSLQTDSSNTDTA--LTTLEEALSEKE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2331 R---RLQEDKEQMAQQLAQEtqgfqktLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRT 2407
Cdd:pfam10174 450 RiieRLKEQREREDRERLEE-------LESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2408 ELATQEKVMLVQTLETQRQ--QSDRDAERLREAIAelehekDKLKQEAQLLQLKSEEMQTVRqeqllqetqalqqsflSE 2485
Cdd:pfam10174 523 EIAVEQKKEECSKLENQLKkaHNAEEAVRTNPEIN------DRIRLLEQEVARYKEESGKAQ----------------AE 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2486 KDSLLQRERCIEQEK-------AKLEQLFQDEVaKAQALREEQQRQQQQMQQEKQqlAASMEEARRRQHEAEEGVRRQQ- 2557
Cdd:pfam10174 581 VERLLGILREVENEKndkdkkiAELESLTLRQM-KEQNKKVANIKHGQQEMKKKG--AQLLEEARRREDNLADNSQQLQl 657
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1920237970 2558 ----EELQRLAQQQQQQEKLLAEENQRLRERLQHLEE---ERRAALarsEEI 2602
Cdd:pfam10174 658 eelmGALEKTRQELDATKARLSSTQQSLAEKDGHLTNlraERRKQL---EEI 706
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1326-1439 |
9.71e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.02 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1326 ETLRRMEEEERLAEQQRA-EERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGL-QRRMQEEVARREEVAVEAQEQKR 1403
Cdd:pfam05672 11 EAARILAEKRRQAREQRErEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEEREQ 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237970 1404 SIQEELQHLRQSSEAeiqAKARQVEAAERSRLRIEE 1439
Cdd:pfam05672 91 REQEEQERLQKQKEE---AEAKAREEAERQRQEREK 123
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1924-2425 |
9.79e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.15 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 1924 AAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKA 2003
Cdd:COG3899 736 PPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGEL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2004 KVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQ-----KEQELQQTLQQEQSVLERLRSEAEAARRAAE 2078
Cdd:COG3899 816 ALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAgletgDAALALLALAAAAAAAAAAAALAAAAAAAAR 895
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2079 EAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHK 2158
Cdd:COG3899 896 LLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAA 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2159 QFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAEN 2238
Cdd:COG3899 976 AAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAA 1055
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2239 RALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2318
Cdd:COG3899 1056 AAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAAL 1135
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237970 2319 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAE 2398
Cdd:COG3899 1136 LLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALL 1215
|
490 500
....*....|....*....|....*..
gi 1920237970 2399 DIGERLYRTELATQEKVMLVQTLETQR 2425
Cdd:COG3899 1216 ALEAAALLLLLLLAALALAAALLALRL 1242
|
|
| |
