|
Name |
Accession |
Description |
Interval |
E-value |
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
268-380 |
3.20e-71 |
|
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: 235.35 E-value: 3.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 268 EQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKR 347
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|...
gi 442626145 348 IKLVNINPADLVDGRPPVVLGLIWTIILYFQLR 380
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
433-541 |
1.29e-63 |
|
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: 213.33 E-value: 1.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 433 KWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAK 512
Cdd:cd21243 1 KFKGGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPR 80
|
90 100
....*....|....*....|....*....
gi 442626145 513 LLDAEDVDVPKPDEKSIMTYVAQFLHKYP 541
Cdd:cd21243 81 LLDPEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
268-379 |
2.85e-47 |
|
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: 166.98 E-value: 2.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 268 EQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKR 347
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 442626145 348 IKLVNINPADLVDGRPPVVLGLIWTIILYFQL 379
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
270-378 |
6.33e-44 |
|
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: 156.79 E-value: 6.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 270 ERVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASKRIK 349
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKA--RRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRM--RFHRLQNVQTALDFLKYRKIK 76
|
90 100
....*....|....*....|....*....
gi 442626145 350 LVNINPADLVDGRPPVVLGLIWTIILYFQ 378
Cdd:cd21188 77 LVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
268-380 |
4.21e-40 |
|
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: 146.13 E-value: 4.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 268 EQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGrvLRRPHFLSNANTALQFLASKR 347
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKG--HNVFQCRSNIETALSFLKNKS 78
|
90 100 110
....*....|....*....|....*....|...
gi 442626145 348 IKLVNINPADLVDGRPPVVLGLIWTIILYFQLR 380
Cdd:cd21242 79 IKLINIHVPDIIEGKPSIILGLIWTIILHFHIE 111
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
262-375 |
7.87e-39 |
|
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: 142.89 E-value: 7.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 262 ILQLQEEQERVQKKTFTNWINSYLlKRVPpLRIDDLINDLRDGTKLIALLEVLSGERLP-VEKGRVlrRPHFLSNANTAL 340
Cdd:cd21246 6 IKALADEREAVQKKTFTKWVNSHL-ARVG-CRINDLYTDLRDGRMLIKLLEVLSGERLPkPTKGKM--RIHCLENVDKAL 81
|
90 100 110
....*....|....*....|....*....|....*
gi 442626145 341 QFLASKRIKLVNINPADLVDGRPPVVLGLIWTIIL 375
Cdd:cd21246 82 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
261-375 |
9.20e-37 |
|
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: 137.04 E-value: 9.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 261 TILQLQEEQERVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLP-VEKGRVlrRPHFLSNANTA 339
Cdd:cd21193 5 RIRALQEERINIQKKTFTKWINSFLEKA--NLEIGDLFTDLSDGKLLLKLLEIISGEKLGkPNRGRL--RVQKIENVNKA 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 442626145 340 LQFLASKrIKLVNINPADLVDGRPPVVLGLIWTIIL 375
Cdd:cd21193 81 LAFLKTK-VRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
272-380 |
9.88e-37 |
|
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: 136.36 E-value: 9.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 272 VQKKTFTNWINSYLLKRVPPLrIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASKRIKLV 351
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKPP-IKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRM--RVHHLNNVNRALQVLEQNNVKLV 78
|
90 100
....*....|....*....|....*....
gi 442626145 352 NINPADLVDGRPPVVLGLIWTIILYFQLR 380
Cdd:cd21186 79 NISSNDIVDGNPKLTLGLVWSIILHWQVK 107
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
435-541 |
2.07e-36 |
|
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: 135.63 E-value: 2.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 435 KQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLL 514
Cdd:cd21192 1 QGSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLL 80
|
90 100
....*....|....*....|....*..
gi 442626145 515 DAEDVDVPKPDEKSIMTYVAQFLHKYP 541
Cdd:cd21192 81 EVEDVLVDKPDERSIMTYVSQFLRMFP 107
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
433-537 |
5.56e-35 |
|
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: 131.50 E-value: 5.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 433 KWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAK 512
Cdd:cd21244 1 RWKMSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPR 80
|
90 100
....*....|....*....|....*
gi 442626145 513 LLDAEDVDVPKPDEKSIMTYVAQFL 537
Cdd:cd21244 81 LLEPEDVDVVNPDEKSIMTYVAQFL 105
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
438-541 |
6.21e-34 |
|
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: 128.28 E-value: 6.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 517
Cdd:cd21189 2 AKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDPE 81
|
90 100
....*....|....*....|....
gi 442626145 518 DVDVPKPDEKSIMTYVAQFLHKYP 541
Cdd:cd21189 82 DVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
258-379 |
9.65e-34 |
|
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: 128.95 E-value: 9.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 258 YQMTILQLQEEQERVQKKTFTNWINSYLLKRVPplRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNAN 337
Cdd:cd21236 3 YENVLERYKDERDKVQKKTFTKWINQHLMKVRK--HVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRM--RFHRLQNVQ 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 442626145 338 TALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTIILYFQL 379
Cdd:cd21236 79 IALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQI 120
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
270-375 |
8.47e-33 |
|
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: 125.19 E-value: 8.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 270 ERVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLP-VEKGRVlrRPHFLSNANTALQFLASKRI 348
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKA--GTQIENIEEDFRDGLKLMLLLEVISGERLPkPERGKM--RFHKIANVNKALDFIASKGV 78
|
90 100
....*....|....*....|....*..
gi 442626145 349 KLVNINPADLVDGRPPVVLGLIWTIIL 375
Cdd:cd21214 79 KLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
438-540 |
1.32e-32 |
|
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: 124.45 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 517
Cdd:cd21194 3 AKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDAE 82
|
90 100
....*....|....*....|...
gi 442626145 518 DVDVPKPDEKSIMTYVAQFLHKY 540
Cdd:cd21194 83 DVDVARPDEKSIMTYVASYYHYF 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
267-379 |
2.23e-31 |
|
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: 121.67 E-value: 2.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 267 EEQERVQKKTFTNWINSYLLKrvPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASK 346
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLRHR 76
|
90 100 110
....*....|....*....|....*....|...
gi 442626145 347 RIKLVNINPADLVDGRPPVVLGLIWTIILYFQL 379
Cdd:cd21235 77 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 109
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
262-375 |
2.74e-31 |
|
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: 122.06 E-value: 2.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 262 ILQLQEEQERVQKKTFTNWINSYLLKrvPPLRIDDLINDLRDGTKLIALLEVLSGERLPV-EKGRVlrRPHFLSNANTAL 340
Cdd:cd21318 28 IKALADEREAVQKKTFTKWVNSHLAR--VPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRM--RIHSLENVDKAL 103
|
90 100 110
....*....|....*....|....*....|....*
gi 442626145 341 QFLASKRIKLVNINPADLVDGRPPVVLGLIWTIIL 375
Cdd:cd21318 104 QFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
438-541 |
2.97e-31 |
|
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: 120.67 E-value: 2.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKdSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 517
Cdd:cd21245 4 AIKALLNWVQRRTRK-YGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPE 82
|
90 100
....*....|....*....|....
gi 442626145 518 DVDVPKPDEKSIMTYVAQFLHKYP 541
Cdd:cd21245 83 DVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
264-564 |
6.37e-31 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 133.14 E-value: 6.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 264 QLQEEQERVQKKTFTNWINSYLLKRVPPlRIDDLINDLRDGTKLIALLEVLSGERLpVEKGRVLR-RPHFLSNANTALQF 342
Cdd:COG5069 1 MEAKKWQKVQKKTFTKWTNEKLISGGQK-EFGDLDTDLKDGVKLAQLLEALQKDNA-GEYNETPEtRIHVMENVSGRLEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 343 LASKRIKLVNINPADLVDGRPPVVLGLIWTIILYFQLRKkrrknlvvvINYApqiEENSRNLEYLghgiggsvssldSVG 422
Cdd:COG5069 79 IKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIAT---------INEE---GELTKHINLL------------LWC 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 423 NQKHGDLKAEkwkqgarktllnwvtnalpkdsgVEVKDFGASWRDGVAFLALI-----DAIKANLVNLAELKKTSNRQRl 497
Cdd:COG5069 135 DEDTGGYKPE-----------------------VDTFDFFRSWRDGLAFSALIhdsrpDTLDPNVLDLQKKNKALNNFQ- 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626145 498 etAFDVAESKLGIAKLLDAEDV-DVPKPDEKSIMTYVAQFLHKYpepkgasRDQSHVQQEADELRRFL 564
Cdd:COG5069 191 --AFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYIIRF-------GLLEKIDIALHRVYRLL 249
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
262-375 |
6.98e-31 |
|
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: 120.93 E-value: 6.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 262 ILQLQEEQERVQKKTFTNWINSYLlKRVPpLRIDDLINDLRDGTKLIALLEVLSGERLPV-EKGRVlrRPHFLSNANTAL 340
Cdd:cd21317 21 IKALADEREAVQKKTFTKWVNSHL-ARVT-CRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRM--RIHCLENVDKAL 96
|
90 100 110
....*....|....*....|....*....|....*
gi 442626145 341 QFLASKRIKLVNINPADLVDGRPPVVLGLIWTIIL 375
Cdd:cd21317 97 QFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
268-381 |
1.30e-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: 116.52 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 268 EQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKR 347
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 442626145 348 IKLVNINPADLVDGRPPVVLGLIWTIILYFQLRK 381
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
268-380 |
4.11e-29 |
|
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: 115.02 E-value: 4.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 268 EQERVQKKTFTNWINSYLLK-RVPPlrIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASK 346
Cdd:cd21231 2 EREDVQKKTFTKWINAQFAKfGKPP--IEDLFTDLQDGRRLLELLEGLTGQKLVKEKGST--RVHALNNVNKALQVLQKN 77
|
90 100 110
....*....|....*....|....*....|....
gi 442626145 347 RIKLVNINPADLVDGRPPVVLGLIWTIILYFQLR 380
Cdd:cd21231 78 NVDLVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
267-379 |
4.97e-29 |
|
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: 114.74 E-value: 4.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 267 EEQERVQKKTFTNWINSYLLKRVPplRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASK 346
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRK--HINDLYEDLRDGHNLISLLEVLSGVKLPREKGRM--RFHRLQNVQIALDFLKQR 76
|
90 100 110
....*....|....*....|....*....|...
gi 442626145 347 RIKLVNINPADLVDGRPPVVLGLIWTIILYFQL 379
Cdd:cd21237 77 QVKLVNIRNDDITDGNPKLTLGLIWTIILHFQI 109
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
438-538 |
5.06e-29 |
|
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: 114.41 E-value: 5.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNalpKDSG---VEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLL 514
Cdd:cd21248 3 AKDALLLWCQM---KTAGypnVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLL 79
|
90 100
....*....|....*....|....
gi 442626145 515 DAEDVDVPKPDEKSIMTYVAQFLH 538
Cdd:cd21248 80 DPEDVNVEQPDEKSIITYVVTYYH 103
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
270-377 |
3.46e-28 |
|
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: 112.11 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 270 ERVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLpvekGRVLRRP----HFLSNANTALQFLAS 345
Cdd:cd21215 2 VDVQKKTFTKWLNTKLSSR--GLSITDLVTDLSDGVRLIQLLEIIGDESL----GRYNKNPkmrvQKLENVNKALEFIKS 75
|
90 100 110
....*....|....*....|....*....|..
gi 442626145 346 KRIKLVNINPADLVDGRPPVVLGLIWTIILYF 377
Cdd:cd21215 76 RGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
435-538 |
1.24e-27 |
|
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: 110.72 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 435 KQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLL 514
Cdd:cd21249 2 LRSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLL 81
|
90 100
....*....|....*....|....
gi 442626145 515 DAEDVDVPKPDEKSIMTYVAQFLH 538
Cdd:cd21249 82 DPEDVAVPHPDERSIMTYVSLYYH 105
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
440-541 |
2.10e-27 |
|
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: 109.83 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 440 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDV 519
Cdd:cd21187 3 KTLLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDV 82
|
90 100
....*....|....*....|..
gi 442626145 520 DVPKPDEKSIMTYVAQFLHKYP 541
Cdd:cd21187 83 NVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
438-540 |
2.39e-27 |
|
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: 109.76 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 517
Cdd:cd21216 11 AKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKMLDAE 90
|
90 100
....*....|....*....|....
gi 442626145 518 D-VDVPKPDEKSIMTYVAQFLHKY 540
Cdd:cd21216 91 DiVNTPRPDERSVMTYVSCYYHAF 114
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
438-540 |
4.92e-27 |
|
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: 109.15 E-value: 4.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 517
Cdd:cd21291 11 AKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGIPQLLDVE 90
|
90 100
....*....|....*....|....
gi 442626145 518 DV-DVPKPDEKSIMTYVAQFLHKY 540
Cdd:cd21291 91 DVcDVAKPDERSIMTYVAYYFHAF 114
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
262-379 |
8.66e-27 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 108.69 E-value: 8.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 262 ILQLQEEQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLrRPHFLSNANTALQ 341
Cdd:cd21247 10 IRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQLPRPSRGKM-RVHFLENNSKAIT 88
|
90 100 110
....*....|....*....|....*....|....*....
gi 442626145 342 FLASK-RIKLvnINPADLVDGRPPVVLGLIWTIILYFQL 379
Cdd:cd21247 89 FLKTKvPVKL--IGPENIVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
436-544 |
9.18e-26 |
|
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: 105.47 E-value: 9.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 436 QGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLD 515
Cdd:cd21319 4 RSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLD 83
|
90 100
....*....|....*....|....*....
gi 442626145 516 AEDVDVPKPDEKSIMTYVAQFLHKYPEPK 544
Cdd:cd21319 84 PEDVFTENPDEKSIITYVVAFYHYFSKMK 112
|
|
| KASH |
pfam10541 |
Nuclear envelope localization domain; The KASH (for Klarsicht/ANC-1/Syne-1 homology) or KLS ... |
7906-7962 |
1.91e-25 |
|
Nuclear envelope localization domain; The KASH (for Klarsicht/ANC-1/Syne-1 homology) or KLS domain is a highly hydrophobic nuclear envelope localization domain of approximately 60 amino acids comprising a 20-amino-acid transmembrane region and a 30-35-residue C-terminal region that lies between the inner and the outer nuclear membranes. During meiotic prophase, telomeres cluster to form a bouquet arrangement of chromosomes. SUN and KASH domain proteins form complexes that span both membranes of the nuclear envelope. The KASH domain links the dynein motor complex of the microtubules, through the outer nuclear membrane to the Sad1 domain in the inner nuclear membrane which then interacts with the bouquet proteins Bqt1 and Bqt2 that are complexed with Bqt4, Rap1 and Taz1 and attached to the telomere. SUN domain-containing proteins are essential for recruiting KASH domain proteins at the outer nuclear membrane, and KASH domains provide a generic NE tethering device for functionally distinct proteins whose cytoplasmic domains mediate nuclear positioning, maintain physical connections with other cellular organelles, and possibly even influence chromosome dynamics.
Pssm-ID: 463142 Cd Length: 58 Bit Score: 102.29 E-value: 1.91e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 442626145 7906 FLGRVARASLPIQALMLLLLGVATLVPHG-EDYTCMFSNTFARSLEPMLSYPHGPPPT 7962
Cdd:pfam10541 1 FLGRVLRAALPLQLLLLLLLLLACLLPAGeEDYSCTLANNFARSFHPMLRYVNGPPPT 58
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
271-377 |
4.42e-25 |
|
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: 103.33 E-value: 4.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 271 RVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLpveKGRVLRRP----HFLSNANTALQFLASK 346
Cdd:cd21183 3 RIQANTFTRWCNEHLKER--GMQIHDLATDFSDGLCLIALLENLSTRPL---KRSYNRRPafqqHYLENVSTALKFIEAD 77
|
90 100 110
....*....|....*....|....*....|.
gi 442626145 347 RIKLVNINPADLVDGRPPVVLGLIWTIILYF 377
Cdd:cd21183 78 HIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
272-379 |
4.46e-25 |
|
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: 103.14 E-value: 4.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 272 VQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLpvekGRVLRRP----HFLSNANTALQFLASKR 347
Cdd:cd21227 4 IQKNTFTNWVNEQL--KPTGMSVEDLATDLEDGVKLIALVEILQGRKL----GRVIKKPlnqhQKLENVTLALKAMAEDG 77
|
90 100 110
....*....|....*....|....*....|..
gi 442626145 348 IKLVNINPADLVDGRPPVVLGLIWTIILYFQL 379
Cdd:cd21227 78 IKLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
272-380 |
5.87e-25 |
|
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: 102.78 E-value: 5.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 272 VQKKTFTNWINSYLLKRVPPlRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASKRIKLV 351
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKP-PIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGST--RVHALNNVNRVLQVLHQNNVELV 78
|
90 100
....*....|....*....|....*....
gi 442626145 352 NINPADLVDGRPPVVLGLIWTIILYFQLR 380
Cdd:cd21232 79 NIGGTDIVDGNHKLTLGLLWSIILHWQVK 107
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
433-545 |
8.34e-25 |
|
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: 102.83 E-value: 8.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 433 KWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAK 512
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100 110
....*....|....*....|....*....|...
gi 442626145 513 LLDAEDVDVPKPDEKSIMTYVAQFLHKYPEPKG 545
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKMKA 113
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
262-375 |
1.07e-24 |
|
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: 103.97 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 262 ILQLQEEQERVQKKTFTNWINSYLLKrvPPLRIDDLINDLRDGTKLIALLEVLSGERLPV-EKGRVlrRPHFLSNANTAL 340
Cdd:cd21316 43 IKALADEREAVQKKTFTKWVNSHLAR--VSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRM--RIHCLENVDKAL 118
|
90 100 110
....*....|....*....|....*....|....*
gi 442626145 341 QFLASKRIKLVNINPADLVDGRPPVVLGLIWTIIL 375
Cdd:cd21316 119 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
270-377 |
1.23e-23 |
|
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: 99.83 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 270 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLAS-KRI 348
Cdd:cd21311 13 KRIQQNTFTRWANEHL--KTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEEdEGI 90
|
90 100
....*....|....*....|....*....
gi 442626145 349 KLVNINPADLVDGRPPVVLGLIWTIILYF 377
Cdd:cd21311 91 KIVNIDSSDIVDGKLKLILGLIWTLILHY 119
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
438-541 |
1.73e-23 |
|
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: 98.52 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAEsKLGIAKLLDAE 517
Cdd:cd21239 2 AKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAE-KLGVTRLLDPE 80
|
90 100
....*....|....*....|....
gi 442626145 518 DVDVPKPDEKSIMTYVAQFLHKYP 541
Cdd:cd21239 81 DVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
438-541 |
2.61e-23 |
|
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: 98.19 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGIAKLLDAE 517
Cdd:cd21240 5 AKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAE 83
|
90 100
....*....|....*....|....
gi 442626145 518 DVDVPKPDEKSIMTYVAQFLHKYP 541
Cdd:cd21240 84 DVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
437-538 |
8.30e-23 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 96.54 E-value: 8.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 437 GARKTLLNWVTNALPKDSgveVKDFGASWRDGVAFLALIDAIKANL-VNLAELKKTSNRQRLETAFDVAESKLGIAKLLD 515
Cdd:cd21184 1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLiPDNESLDKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|...
gi 442626145 516 AEDVDVPKPDEKSIMTYVAQFLH 538
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSYFRN 100
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
440-540 |
1.17e-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: 96.00 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 440 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDV 519
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 442626145 520 DVPKPDEKSIMTYVAQFLHKY 540
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
438-541 |
5.81e-22 |
|
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: 94.32 E-value: 5.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 517
Cdd:cd21238 3 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 82
|
90 100
....*....|....*....|....
gi 442626145 518 DVDVPKPDEKSIMTYVAQFLHKYP 541
Cdd:cd21238 83 DVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
438-541 |
1.88e-21 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 92.73 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKD-SGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKT--SNRQRLETAFDVAESKLGIAK-L 513
Cdd:pfam00307 3 LEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVPKvL 82
|
90 100
....*....|....*....|....*...
gi 442626145 514 LDAEDVDvpKPDEKSIMTYVAQFLHKYP 541
Cdd:pfam00307 83 IEPEDLV--EGDNKSVLTYLASLFRRFQ 108
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
270-377 |
2.16e-21 |
|
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: 92.55 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 270 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVE-KGRVLRRPHFLSNANTALQFLASKRI 348
Cdd:cd21228 2 KKIQQNTFTRWCNEHL--KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKyNKRPTFRQMKLENVSVALEFLERESI 79
|
90 100
....*....|....*....|....*....
gi 442626145 349 KLVNINPADLVDGRPPVVLGLIWTIILYF 377
Cdd:cd21228 80 KLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
272-378 |
4.63e-21 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 91.58 E-value: 4.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 272 VQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKgRVLRRPHFLSNANTALQFLASK-RIKL 350
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK-LNKSEFDKLENINLALDVAEKKlGVPK 80
|
90 100
....*....|....*....|....*...
gi 442626145 351 VNINPADLVDGRPPVVLGLIWTIILYFQ 378
Cdd:pfam00307 81 VLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
455-540 |
1.01e-20 |
|
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: 90.87 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 455 GVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAED-VDVPKPDEKSIMTYV 533
Cdd:cd21253 19 DVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVALKVPDKLSILTYV 98
|
....*..
gi 442626145 534 AQFlHKY 540
Cdd:cd21253 99 SQY-YNY 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
436-545 |
1.59e-20 |
|
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: 90.88 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 436 QGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLD 515
Cdd:cd21322 16 RSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHLGLTKLLD 95
|
90 100 110
....*....|....*....|....*....|
gi 442626145 516 AEDVDVPKPDEKSIMTYVAQFLHKYPEPKG 545
Cdd:cd21322 96 PEDVNMEAPDEKSIITYVVSFYHYFSKMKA 125
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
436-540 |
4.33e-20 |
|
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: 89.00 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 436 QGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLD 515
Cdd:cd21320 1 KSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 80
|
90 100
....*....|....*....|....*
gi 442626145 516 AEDVDVPKPDEKSIMTYVAQFLHKY 540
Cdd:cd21320 81 PEDISVDHPDEKSIITYVVTYYHYF 105
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
438-540 |
4.71e-19 |
|
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: 86.70 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 517
Cdd:cd21289 11 AKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAE 90
|
90 100
....*....|....*....|....
gi 442626145 518 D-VDVPKPDEKSIMTYVAQFLHKY 540
Cdd:cd21289 91 DiVNTPKPDEKAIMTYVSCFYHAF 114
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
438-540 |
6.04e-19 |
|
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: 86.29 E-value: 6.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 517
Cdd:cd21287 11 AKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDAE 90
|
90 100
....*....|....*....|....
gi 442626145 518 D-VDVPKPDEKSIMTYVAQFLHKY 540
Cdd:cd21287 91 DiVGTARPDEKAIMTYVSSFYHAF 114
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
273-377 |
8.91e-19 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 84.94 E-value: 8.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 273 QKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPvekgRVLRRP----HFLSNANTALQFLASKRI 348
Cdd:cd21212 1 EIEIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVP----GIHSRPktraQKLENIQACLQFLAALGV 76
|
90 100
....*....|....*....|....*....
gi 442626145 349 KLVNINPADLVDGRPPVVLGLIWTIILYF 377
Cdd:cd21212 77 DVQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
438-540 |
9.80e-19 |
|
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: 84.90 E-value: 9.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 517
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAE 80
|
90 100
....*....|....*....|....
gi 442626145 518 D-VDVPKPDEKSIMTYVAQFLHKY 540
Cdd:cd21197 81 DmVTMHVPDRLSIITYVSQYYNHF 104
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
438-541 |
1.34e-18 |
|
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: 84.62 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 517
Cdd:cd21234 1 SEKILLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPE 80
|
90 100
....*....|....*....|....
gi 442626145 518 DVDVPKPDEKSIMTYVAQFLHKYP 541
Cdd:cd21234 81 DVAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
270-379 |
2.39e-18 |
|
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: 84.70 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 270 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLpveKGRVLRRPHF----LSNANTALQFLAS 345
Cdd:cd21310 14 KKIQQNTFTRWCNEHL--KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKM---YRKYHPRPNFrqmkLENVSVALEFLDR 88
|
90 100 110
....*....|....*....|....*....|....
gi 442626145 346 KRIKLVNINPADLVDGRPPVVLGLIWTIILYFQL 379
Cdd:cd21310 89 EHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 122
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
438-542 |
1.38e-17 |
|
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: 81.90 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNL-AELKKTSNRQRLETAFDVAESKLGIAKLLDA 516
Cdd:cd21233 1 SEKILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWnSVVSQQSATERLDHAFNIARQHLGIEKLLDP 80
|
90 100
....*....|....*....|....*.
gi 442626145 517 EDVDVPKPDEKSIMTYVAQFLHKYPE 542
Cdd:cd21233 81 EDVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
440-536 |
3.98e-17 |
|
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: 80.41 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 440 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTS---NRQRletAFDVAESKLGIAKLLDA 516
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENiaeNNQL---AFDVAEQELGIPPVMTG 79
|
90 100
....*....|....*....|.
gi 442626145 517 ED-VDVPKPDEKSIMTYVAQF 536
Cdd:cd22198 80 QEmASLAVPDKLSMVSYLSQF 100
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
438-540 |
6.81e-17 |
|
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: 80.51 E-value: 6.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 517
Cdd:cd21290 14 AKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAE 93
|
90 100
....*....|....*....|....
gi 442626145 518 D-VDVPKPDEKSIMTYVAQFLHKY 540
Cdd:cd21290 94 DiVNTARPDEKAIMTYVSSFYHAF 117
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
438-543 |
6.94e-17 |
|
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: 79.91 E-value: 6.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 517
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|....*..
gi 442626145 518 D-VDVPKPDEKSIMTYVAQFLHKYPEP 543
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYYNHFSNP 107
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
442-536 |
1.69e-16 |
|
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: 78.58 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 442 LLNWVTNALPKDSgveVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQR-LETAFDVAESKLGIAKLLDAEDVD 520
Cdd:cd21230 6 LLGWIQNKIPQLP---ITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDALEnATEAMQLAEDWLGVPQLITPEEII 82
|
90
....*....|....*.
gi 442626145 521 VPKPDEKSIMTYVAQF 536
Cdd:cd21230 83 NPNVDEMSVMTYLSQF 98
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
438-540 |
2.86e-16 |
|
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: 78.58 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 517
Cdd:cd21288 11 AKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAE 90
|
90 100
....*....|....*....|....
gi 442626145 518 D-VDVPKPDEKSIMTYVAQFLHKY 540
Cdd:cd21288 91 DiVNTPKPDERAIMTYVSCFYHAF 114
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
440-536 |
2.91e-16 |
|
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: 77.74 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 440 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNR----QRLETAFDVAESKLGIAKLLD 515
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 442626145 516 AEDVDVPKPDEKSIMTYVAQF 536
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
274-375 |
7.89e-16 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 76.61 E-value: 7.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 274 KKTFTNWINSyLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLAS-KRIKLVN 352
Cdd:cd00014 1 EEELLKWINE-VLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKlGLPELDL 79
|
90 100
....*....|....*....|....
gi 442626145 353 INPADLV-DGRPPVVLGLIWTIIL 375
Cdd:cd00014 80 FEPEDLYeKGNLKKVLGTLWALAL 103
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
270-380 |
9.68e-16 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 76.80 E-value: 9.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 270 ERVQKKTFTNWINSYLLKRVPPlRIDDLINDLRDGTKLIALLEVLSGERLPVE-----KGRVLRrphfLSNANTALQFLA 344
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGIP-KISDLATDLSDGVRLIFFLELVSGKKFPKKfdlepKNRIQM----IQNLHLAMLFIE 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 442626145 345 SK-RIKLVNINPADLVDGRPPVVLGLIWTiiLYFQLR 380
Cdd:cd21225 77 EDlKIRVQGIGAEDFVDNNKKLILGLLWT--LYRKYR 111
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
270-379 |
1.60e-15 |
|
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: 76.66 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 270 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLpveKGRVLRRPHF----LSNANTALQFLAS 345
Cdd:cd21309 15 KKIQQNTFTRWCNEHL--KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRM---YRKYHQRPTFrqmqLENVSVALEFLDR 89
|
90 100 110
....*....|....*....|....*....|....
gi 442626145 346 KRIKLVNINPADLVDGRPPVVLGLIWTIILYFQL 379
Cdd:cd21309 90 ESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSI 123
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
437-539 |
4.06e-15 |
|
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: 74.69 E-value: 4.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 437 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDA 516
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|....*
gi 442626145 517 EDVDV--PKPDEKSIMTYVAQFLHK 539
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLYRH 105
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
275-376 |
4.36e-15 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 74.27 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 275 KTFTNWINSYLLKRVPPlRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRP-HFLSNANTALQFLASKRIKLVNI 353
Cdd:smart00033 1 KTLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfKKIENINLALSFAEKLGGKVVLF 79
|
90 100
....*....|....*....|...
gi 442626145 354 NPADLVDGrPPVVLGLIWTIILY 376
Cdd:smart00033 80 EPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
270-379 |
5.64e-15 |
|
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: 75.12 E-value: 5.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 270 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLpveKGRVLRRPHF----LSNANTALQFLAS 345
Cdd:cd21308 18 KKIQQNTFTRWCNEHL--KCVSKRIANLQTDLSDGLRLIALLEVLSQKKM---HRKHNQRPTFrqmqLENVSVALEFLDR 92
|
90 100 110
....*....|....*....|....*....|....
gi 442626145 346 KRIKLVNINPADLVDGRPPVVLGLIWTIILYFQL 379
Cdd:cd21308 93 ESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 126
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
273-377 |
1.37e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 73.10 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 273 QKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLP----VEKGRVLRRphflSNANTALQFLASKRI 348
Cdd:cd21213 1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPgidwNPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 442626145 349 KLVNINPADLVDGRPPVVLGLIWTIILYF 377
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
440-535 |
1.16e-13 |
|
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: 70.53 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 440 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAEsKLGIAKLLDAED- 518
Cdd:cd21198 4 QDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAA-KLGIPRLLDPADm 82
|
90
....*....|....*..
gi 442626145 519 VDVPKPDEKSIMTYVAQ 535
Cdd:cd21198 83 VLLSVPDKLSVMTYLHQ 99
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
437-535 |
2.52e-13 |
|
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: 69.43 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 437 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGIAKLLDA 516
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|
gi 442626145 517 ED-VDVPKPDEKSIMTYVAQ 535
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQ 99
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
439-542 |
5.74e-13 |
|
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: 68.93 E-value: 5.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 439 RKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGIAKLLDAED 518
Cdd:cd21199 10 RNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAES-VGIPTTLTIDE 88
|
90 100
....*....|....*....|....*
gi 442626145 519 -VDVPKPDEKSIMTYVAQfLHKYPE 542
Cdd:cd21199 89 mVSMERPDWQSVMSYVTA-IYKHFE 112
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
439-539 |
6.20e-13 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 68.57 E-value: 6.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 439 RKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLvnLAELKKTSNRQRLET---AFDVAESKLGIAKLLD 515
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGL--CPNWRKLDPSNSLENcrrAMDLAKREFNIPMVLS 79
|
90 100
....*....|....*....|....
gi 442626145 516 AEDVDVPKPDEKSIMTYVAQFLHK 539
Cdd:cd21229 80 PEDLSSPHLDELSGMTYLSYFMKE 103
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
437-536 |
6.26e-13 |
|
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: 68.86 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 437 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDA 516
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80
|
90 100
....*....|....*....|.
gi 442626145 517 ED-VDVPKPDEKSIMTYVAQF 536
Cdd:cd21259 81 EDmVRMREPDWKCVYTYIQEF 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1994-2205 |
1.91e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 70.17 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1994 RWNDFAANKDKLEKWLNETETTLKvAPETKGELSEMKTLLERYKTLSNELKLKGNELEQLQSEARDLGTE--------VD 2065
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEghpdaeeiQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2066 AVNRLQSRCDKLKNDCSAHITALEQEMfDYNAYHQSLQDVEKWLLQISFQLMAHNslFISNREQTQEQIKQHEALLVEIQ 2145
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2146 KYQTNLDDLNAKGQAQIkryESSTPAIRPTVESQLKNIQDSYNSLLQTSVQIKNRLLESL 2205
Cdd:cd00176 157 AHEPRLKSLNELAEELL---EEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2148-3237 |
2.53e-12 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 75.09 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2148 QTNLDDLNAKGQAQIKRYESSTPAirpTVESQLKNIQDSYNSLLQTSVQIK--------NRLLESLAKFQEYEDTLDSIM 2219
Cdd:TIGR01612 695 KAKLDDLKSKIDKEYDKIQNMETA---TVELHLSNIENKKNELLDIIVEIKkhihgeinKDLNKILEDFKNKEKELSNKI 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2220 RNLETYepiiQTELDAPATSLELAQNQLRCAQEMQNkLNNEKSRLAAAVQACEAATASISR-PSSPLETAMQAIPERELI 2298
Cdd:TIGR01612 772 NDYAKE----KDELNKYKSKISEIKNHYNDQINIDN-IKDEDAKQNYDKSKEYIKTISIKEdEIFKIINEMKFMKDDFLN 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2299 VRAKLEDLLDQVQSHLGGLTASVSELEQQQKQRA---ELQDWVKKQQSSVS----------------------DWMMRPC 2353
Cdd:TIGR01612 847 KVDKFINFENNCKEKIDSEHEQFAELTNKIKAEIsddKLNDYEKKFNDSKSlineinksieeeyqnintlkkvDEYIKIC 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2354 KLRPEAAQQeLVSMNDLLNSIGDKRSQLMLE---MTGSLGDE-DTDLDDNIDKLESELMDA-IAKKQAGQNVIDGYRQGM 2428
Cdd:TIGR01612 927 ENTKESIEK-FHNKQNILKEILNKNIDTIKEsnlIEKSYKDKfDNTLIDKINELDKAFKDAsLNDYEAKNNELIKYFNDL 1005
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2429 ADV--QNWFDTLIKRMDVLDRGSGlNCAQKMAAINE---------------IKNEYELQGHPKIQELKGKAAQVAEV-IS 2490
Cdd:TIGR01612 1006 KANlgKNKENMLYHQFDEKEKATN-DIEQKIEDANKnipnieiaihtsiynIIDEIEKEIGKNIELLNKEILEEAEInIT 1084
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2491 NLDgqQVEEQMKSLDrrFADLGKR---------------IDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEELQAPKP 2555
Cdd:TIGR01612 1085 NFN--EIKEKLKHYN--FDDFGKEenikyadeinkikddIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVAD 1160
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2556 LGYTPKDAEARQQKIKSLMKDAEAKQSLADVLEKrvanMQQELEPVEYSQ--LESaLRNLN-TENRNLSGVLKAELDRAL 2632
Cdd:TIGR01612 1161 KAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKK----LLNEIAEIEKDKtsLEE-VKGINlSYGKNLGKLFLEKIDEEK 1235
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2633 EAS----KARKSLENDLDKarqwLKTKISEVRKLPVYHPLTSAEIEKKIQENRKYDD--DAKQFNDSVLTDVQRQAANIM 2706
Cdd:TIGR01612 1236 KKSehmiKAMEAYIEDLDE----IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDhhIISKKHDENISDIREKSLKII 1311
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2707 KD-----------------CDDADK--AALQQILDEIAADYQTLKDESSKrgKSLDDLLQGRKAFEDSMKNMGDWLNEME 2767
Cdd:TIGR01612 1312 EDfseesdindikkelqknLLDAQKhnSDINLYLNEIANIYNILKLNKIK--KIIDEVKEYTKEIEENNKNIKDELDKSE 1389
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2768 TATEGELRTTSLPVLEEQLahykKLLSDAENKGGLINDVSEQGKSILPTLSNADKLKLNDDIKN---------------- 2831
Cdd:TIGR01612 1390 KLIKKIKDDINLEECKSKI----ESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNenvlllfkniemadnk 1465
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2832 ----MKDRYGRIKNTIDDRVNALGDHIKKYKDAKSRlaecsqflGNIQQKLRELNRPIGSRI-EDVQDLLGAYEGI-LKE 2905
Cdd:TIGR01612 1466 sqhiLKIKKDNATNDHDFNINELKEHIDKSKGCKDE--------ADKNAKAIEKNKELFEQYkKDVTELLNKYSALaIKN 1537
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2906 LKDSKSKMGDMQMDDLPELQSILaqqddmikLIEDQLAHLRQLLLLREQFIalINEIIAFIMKYTDVIIDIENSPDSLED 2985
Cdd:TIGR01612 1538 KFAKTKKDSEIIIKEIKDAHKKF--------ILEAEKSEQKIKEIKKEKFR--IEDDAAKNDKSNKAAIDIQLSLENFEN 1607
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2986 KINKYDDVIVKIQEC-------EGVLASANDKGQKIASEGNAADKNSITEQLQSLKNQLQNLRKA------VESQRQKHQ 3052
Cdd:TIGR01612 1608 KFLKISDIKKKINDClketesiEKKISSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKkkeldeLDSEIEKIE 1687
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3053 LQLESHKKMaaelSEILDWLHSHEGAAKSRPLLDRDPESVERELQKHQSL--SQDIESY-----LNKFNkindgvkTEIG 3125
Cdd:TIGR01612 1688 IDVDQHKKN----YEIGIIEKIKEIAIANKEEIESIKELIEPTIENLISSfnTNDLEGIdpnekLEEYN-------TEIG 1756
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3126 MpssLLEMLSEGRSLVAS-LPHELEEREKY--LKNNR----DSRLEYMQLVAKFNDWVHEAEL----RLQNsqhgidyeH 3194
Cdd:TIGR01612 1757 D---IYEEFIELYNIIAGcLETVSKEPITYdeIKNTRinaqNEFLKIIEIEKKSKSYLDDIEAkefdRIIN--------H 1825
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|...
gi 442626145 3195 LVQDLDEHKIFFGNEapirnlvHKQIQEAADKIWSSLNNYEQS 3237
Cdd:TIGR01612 1826 FKKKLDHVNDKFTKE-------YSKINEGFDDISKSIENVKNS 1861
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
439-538 |
5.01e-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: 65.82 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 439 RKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSN---RQRLETAFDVAES-KLGIAKLL 514
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 442626145 515 DAEDVdVPKPDEKSIMTYVAQFLH 538
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
438-535 |
1.16e-11 |
|
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: 64.87 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 438 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAeSKLGIAKLLDAE 517
Cdd:cd21254 2 ASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGF-ASLGISRLLEPS 80
|
90
....*....|....*....
gi 442626145 518 D-VDVPKPDEKSIMTYVAQ 535
Cdd:cd21254 81 DmVLLAVPDKLTVMTYLYQ 99
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1989-2772 |
2.99e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1989 KQAQNRWNDFAANKDKLEKWLNETETTLKvapetkgELSEMKTLLERYKTLSNELK-----LKGNELEQLQSEARDLGTE 2063
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLK-------SLERQAEKAERYKELKAELRelelaLLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2064 VDAVNRLQSRCDKLKNDCSAHITALEQEMF-----------DYNAYHQSLQDVEKWLLQISFQLMAHNslfiSNREQTQE 2132
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSeleeeieelqkELYALANEISRLEQQKQILRERLANLE----RQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2133 QIKQHEAllvEIQKYQTNLDDLNAKGQAQIKRYES------STPAIRPTVESQLKNIQDSYNSLLQTSVQIKNRLLESLA 2206
Cdd:TIGR02168 324 QLEELES---KLDELAEELAELEEKLEELKEELESleaeleELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2207 KFQEYEDTLDSIMRNLETYEPIIQTELDapatslELAQNQLRCAQEMQNKLNNEKSRLAAAVQACEAATASISRPSSPLE 2286
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLK------KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2287 TAMQAIPERELIVRAKLeDLLDQVQSHLGGLTASVSELEQQQKQRAELQDWVKKQQSSVSDWMMRPCKLRPEAAQQELVS 2366
Cdd:TIGR02168 475 QALDAAERELAQLQARL-DSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2367 MND--------------------LLNSIGDKRSQLMLEMTGSLGDEDTDLDDNIDKLESELMDAIAKKQAGQNVIDGYRQ 2426
Cdd:TIGR02168 554 NLNaakkaiaflkqnelgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDN 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2427 GMADV------QNWF---DTLIKRMDVLDRGSGLNCAQKMAAINEIKNEYElqghpKIQELKGKAAQVAEVIsnldgQQV 2497
Cdd:TIGR02168 634 ALELAkklrpgYRIVtldGDLVRPGGVITGGSAKTNSSILERRREIEELEE-----KIEELEEKIAELEKAL-----AEL 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2498 EEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEELQApkplgYTPKDAEARQQKIKSLMKDA 2577
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE-----LEAEIEELEERLEEAEEELA 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2578 EAKQSLADvLEKRVANMQQELEpveysQLESALRNLNTENRNLSgvlkaelDRALEASKARKSLENDLDKARQWLKTKIS 2657
Cdd:TIGR02168 779 EAEAEIEE-LEAQIEQLKEELK-----ALREALDELRAELTLLN-------EEAANLRERLESLERRIAATERRLEDLEE 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2658 EVRKLpvyhpltSAEIEKKIQEnrkydddakqfndsvLTDVQRQAANIMKDCDdadkaALQQILDEIAADYQTLKDESSK 2737
Cdd:TIGR02168 846 QIEEL-------SEDIESLAAE---------------IEELEELIEELESELE-----ALLNERASLEEALALLRSELEE 898
|
810 820 830
....*....|....*....|....*....|....*
gi 442626145 2738 RGKSLDDLLQGRKAFEDSMKNMGDWLNEMETATEG 2772
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3247-3960 |
3.37e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.86 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3247 QTKLTNTLANAKTQQSELEKE--AERWREYQQSIDRVKATIERT-KFVDEPVQNLAGLHFNIQKLSHAIGNVQSQNSDLT 3323
Cdd:TIGR02168 208 QAEKAERYKELKAELRELELAllVLRLEELREELEELQEELKEAeEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3324 LVNQQAQSLI-------RQADARNRQLiEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDK 3396
Cdd:TIGR02168 288 KELYALANEIsrleqqkQILRERLANL-ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3397 FRNvdptvrSRRHLEDTKNAIQELREESNQLKsshKEIEALSKSIltflgEVHKPSAEAIQAKVDKLVEQQAKLNDTLrd 3476
Cdd:TIGR02168 367 LEE------LESRLEELEEQLETLRSKVAQLE---LQIASLNNEI-----ERLEARLERLEDRRERLQQEIEELLKKL-- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3477 KEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVhvyDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAHYQ---- 3552
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEEL---REELEEAEQALDAAERELAQLQARLDSLERLQENLEGfseg 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3553 -----AKQNQLPSDIAQ-----EF-----TALEL-LAERVQ-VTMETKEkdfkraktvrtEYVDGVD-----EVQRWLLQ 3610
Cdd:TIGR02168 508 vkallKNQSGLSGILGVlseliSVdegyeAAIEAaLGGRLQaVVVENLN-----------AAKKAIAflkqnELGRVTFL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3611 AEVQVQERSLTPTQMKEL------------------------------------LQRINHEITAIYERFTLVKTNGQLI- 3653
Cdd:TIGR02168 577 PLDSIKGTEIQGNDREILkniegflgvakdlvkfdpklrkalsyllggvlvvddLDNALELAKKLRPGYRIVTLDGDLVr 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3654 ----------------------IENCRnsEEKTLVQTTIDQLAASLAQVRGWLDEKKQAVGDSLDAWTRFmnlyQIVMSW 3711
Cdd:TIGR02168 657 pggvitggsaktnssilerrreIEELE--EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL----SRQISA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3712 ASEKRNFIDQTIELRTLPEARNKLndyvTSVKSIKPIVKHLSEMDKELEHIGQV-TTVGDLKDKLQEAEDAKISVEAVLL 3790
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSK----ELTELEAEIEELEERLEEAEEELAEAeAEIEELEAQIEQLKEELKALREALD 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3791 ERNSLLQEACEEWDQCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQLGFCEKTLADINVQKTKLRLSIEKLEVHFRNGM 3870
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3871 GGDPRLSENVDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRL-------VMAPTYLPHDRE 3943
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeysltleEAEALENKIEDD 966
|
810
....*....|....*...
gi 442626145 3944 RALAEQQ-DLITQELDEL 3960
Cdd:TIGR02168 967 EEEARRRlKRLENKIKEL 984
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
437-545 |
5.03e-11 |
|
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: 63.57 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 437 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDA 516
Cdd:cd21260 1 GVKNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEV 80
|
90 100 110
....*....|....*....|....*....|
gi 442626145 517 ED-VDVPKPDEKSIMTYVaQFLHKYPEPKG 545
Cdd:cd21260 81 EDmVRMSVPDSKCVYTYI-QELYRSLVQKG 109
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
442-536 |
7.60e-11 |
|
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: 62.75 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 442 LLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDV-D 520
Cdd:cd21195 9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEMaS 88
|
90
....*....|....*.
gi 442626145 521 VPKPDEKSIMTYVAQF 536
Cdd:cd21195 89 AQEPDKLSMVMYLSKF 104
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
443-538 |
8.36e-11 |
|
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: 62.32 E-value: 8.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 443 LNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGIAKLLDAEDVDVP 522
Cdd:cd21185 7 LRWVRQLLPD---VDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADP 82
|
90
....*....|....*.
gi 442626145 523 KPDEKSIMTYVAQFLH 538
Cdd:cd21185 83 EVEHLGIMAYAAQLQK 98
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7618-7796 |
9.41e-11 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 65.54 E-value: 9.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7618 WQQIDNDLWRLEQWLQfaESTQKAQSA-PPSNIELLEDVTQDHREFLLDLESHKSIISSLNVVGDHLAThtLDTEKARQL 7696
Cdd:cd00176 2 LQQFLRDADELEAWLS--EKEELLSSTdYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7697 RSRLEADNERWNNVCINATKWQGLLQTALMGNSEFHQTIgELVEWLQRTEQNIKASEPVDLTEErsvLETKFKKFKDLRA 7776
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLES---VEELLKKHKELEE 153
|
170 180
....*....|....*....|
gi 442626145 7777 ELERCEPRVVSLQDAADQLL 7796
Cdd:cd00176 154 ELEAHEPRLKSLNELAEELL 173
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3325-4125 |
1.04e-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: 69.32 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3325 VNQQAQSLIRQADARNR------QLIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFR 3398
Cdd:TIGR02168 198 LERQLKSLERQAEKAERykelkaELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3399 NVDPTVRSRRH-LEDTKNAI----QELREESNQLKSSHKEIEALSKSILTF----------LGEVHKPSAEaIQAKVDKL 3463
Cdd:TIGR02168 278 ELEEEIEELQKeLYALANEIsrleQQKQILRERLANLERQLEELEAQLEELeskldelaeeLAELEEKLEE-LKEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3464 VEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSvhvYDEHIAQTEQllitlnSQVQQAAEESKLL 3543
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER---LEARLERLED------RRERLQQEIEELL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3544 VAQTTAHYQAKQNQLPSDIAQEFTALELLaERVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPT 3623
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEEL-ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3624 QMKELLQRiNHEITAIYERFtlvktnGQLIieNCRNSEEKTLVQTtidqLAASLAQVrgwLDEKKQAVGD--SLDAWTRF 3701
Cdd:TIGR02168 507 GVKALLKN-QSGLSGILGVL------SELI--SVDEGYEAAIEAA----LGGRLQAV---VVENLNAAKKaiAFLKQNEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3702 MNLYQIVMSWASEKRNFIDQTIELRTLPEARNKLNDYVTSVKSIKPIVKHLS-------------EMDKELEHIGQ-VTT 3767
Cdd:TIGR02168 571 GRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLggvlvvddldnalELAKKLRPGYRiVTL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3768 VGDL--KDKLQEAEDAKisVEAVLLERNSLLQEACEEWDQCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQLGFCEKTL 3845
Cdd:TIGR02168 651 DGDLvrPGGVITGGSAK--TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3846 ADINVQKTKLRLSIEKLEVHFRNGMGGDPRLSENVDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQE 3925
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3926 EQQLRLVMAPTYLPHDRERALAEQQDLITQELDELLQSLSSVEDGIANMNQSSLDgmlhglklIQSNLEVHERDAIELKN 4005
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE--------LEELIEELESELEALLN 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 4006 QAKKLPTDPATERL--------LNDTVDRIDLLLRRTQQGITMIANAMHGQKKRQQEIDEYQQHLLELEQWIIEVSAELA 4077
Cdd:TIGR02168 881 ERASLEEALALLRSeleelseeLRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE 960
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626145 4078 SFEPTSDSSTDEQV--LKSQVER-------SQQLLRTLKDRQQSM----EDLVEQTRQLQS 4125
Cdd:TIGR02168 961 NKIEDDEEEARRRLkrLENKIKElgpvnlaAIEEYEELKERYDFLtaqkEDLTEAKETLEE 1021
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
431-542 |
1.23e-10 |
|
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: 62.35 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 431 AEKWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGI 510
Cdd:cd21257 2 AREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VGI 80
|
90 100 110
....*....|....*....|....*....|...
gi 442626145 511 AKLLDAED-VDVPKPDEKSIMTYVAQfLHKYPE 542
Cdd:cd21257 81 KPSLELSEmMYTDRPDWQSVMQYVAQ-IYKYFE 112
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
442-536 |
1.38e-10 |
|
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: 61.89 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 442 LLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDV-D 520
Cdd:cd21251 10 LLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPIMTGKEMaS 89
|
90
....*....|....*.
gi 442626145 521 VPKPDEKSIMTYVAQF 536
Cdd:cd21251 90 VGEPDKLSMVMYLTQF 105
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
439-533 |
1.61e-10 |
|
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: 61.99 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 439 RKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAED 518
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90
....*....|....*..
gi 442626145 519 VDV--PKPDEKSIMTYV 533
Cdd:cd21258 83 MMImgKKPDSKCVFTYV 99
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1565-2317 |
2.14e-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: 68.54 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1565 NQAYTETSDKLQALKGTQAVWSEFVDQKNDIFSMLQTAETELrsltplQTDPKNVSQDLkskRDLNVQLQQAS---HQLL 1641
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL------QKELYALANEI---SRLEQQKQILRerlANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1642 PKLHALKSELAPLAApdKRPILEKEVTEVEKMFFNTMEHVKDRVGYLEDYSAKWNNYKTRLAELQEWANKVAPKNIEALQ 1721
Cdd:TIGR02168 316 RQLEELEAQLEELES--KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1722 SEDLTpEERVVKVQAFKRILGDRMKQLD---LLAADASELAPKEGNIAEAKRLKGEITKLQEVLSAINRNVDHQAQAVQE 1798
Cdd:TIGR02168 394 QIASL-NNEIERLEARLERLEDRRERLQqeiEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1799 DLVNWQQFQAGLQQIKPAVE-----QSEVKKLLEEVLAEKDNVEDLNDNCELLMEQsactrirdqtIETQANYTK----- 1868
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDslerlQENLEGFSEGVKALLKNQSGLSGILGVLSEL----------ISVDEGYEAaieaa 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1869 ----------------------LLTSAQGLVAKIEKNLSDHTEFLNYKKEMDAWIEKAQQVLDDCSTDGDAA-------- 1918
Cdd:TIGR02168 543 lggrlqavvvenlnaakkaiafLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsyll 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1919 ---IIAQKLDTVNSLASRLPEGQHLLALVQDAYSKASNITPEDKQ------------EKLRELMTKVREDWDALGLAVKQ 1983
Cdd:TIGR02168 623 ggvLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKtnssilerrreiEELEEKIEELEEKIAELEKALAE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1984 KLSDLKQAQNRWNDFAANKDKLEKWLNETETTLKVAPETKGELSEMKTLLERyktLSNELKLKGNELEQLQSEARDLGTE 2063
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK---ELTELEAEIEELEERLEEAEEELAE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2064 VDAV-NRLQSRCDKLKNDCSAHITALEQEMFDYNAYHQSLQDVEKWLLQISFQLMAHNSLFISNREQTQEQIKQHEALLV 2142
Cdd:TIGR02168 780 AEAEiEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2143 EIQKYQTNLDDLNAKGQAQIKRYESSTPAIRpTVESQLKNIQDSYNSLLQTSVQIKNRLLESLAKFQEYEDTLDS----I 2218
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALA-LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlevrI 938
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2219 MRNLETYEPIIQTELDAPATSLELAQNQLRCAQEMQNKLNNEKSRL-----------AAAVQACEAATASISRPSSPLET 2287
Cdd:TIGR02168 939 DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaieeyEELKERYDFLTAQKEDLTEAKET 1018
|
810 820 830
....*....|....*....|....*....|
gi 442626145 2288 AMQAIPERELIVRAKLEDLLDQVQSHLGGL 2317
Cdd:TIGR02168 1019 LEEAIEEIDREARERFKDTFDQVNENFQRV 1048
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
274-374 |
2.51e-10 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 61.44 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 274 KKTFTNWINSYL-----LKRVPPLRI--DDLINDLRDGTKLIALLEVLSGERLPVekgRVLRRPHFLS------NANTAL 340
Cdd:cd21217 3 KEAFVEHINSLLaddpdLKHLLPIDPdgDDLFEALRDGVLLCKLINKIVPGTIDE---RKLNKKKPKNifeateNLNLAL 79
|
90 100 110
....*....|....*....|....*....|....
gi 442626145 341 QFLASKRIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21217 80 NAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
293-374 |
2.71e-10 |
|
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: 61.07 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 293 RIDDLINDLRDGTKLIALLEVLSGERLPVEKGRV--LRRPHFLSNANTALQFLASK----RIKLVNINPADLVDGRPPVV 366
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaISRLQKLHNVEVALKALKEAgvlrGGDGGGITAKDIVDGHREKT 104
|
....*...
gi 442626145 367 LGLIWTII 374
Cdd:cd21223 105 LALLWRII 112
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6617-7363 |
3.08e-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: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6617 EEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSseal 6696
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER---- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6697 rlwRQYLQHVQSFLSCAIPEDYSSLREQQQLCAihqnllisqqsvlsetplesELSEQYKALTNLHNETLSRIMQRNGEL 6776
Cdd:TIGR02168 311 ---LANLERQLEELEAQLEELESKLDELAEELA--------------------ELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6777 ERRVSGWNAYRQQL----AALLDWLRQREAERNALQLRYIHLKRVPHLKHRLDAMIQQLDQG--EQQSKALQEQQQELAR 6850
Cdd:TIGR02168 368 EELESRLEELEEQLetlrSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKleEAELKELQAELEELEE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6851 HCDDALATAMRMEQA--SIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKLLDAN----------SE 6918
Cdd:TIGR02168 448 ELEELQEELERLEEAleELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQsglsgilgvlSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6919 SLPTQP---AAIEQLLGSlRAQRV---QLGAQVSALESLT------VTQEELKecISPHDMKTIRQRNWLLWQQ------ 6980
Cdd:TIGR02168 528 LISVDEgyeAAIEAALGG-RLQAVvveNLNAAKKAIAFLKqnelgrVTFLPLD--SIKGTEIQGNDREILKNIEgflgva 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6981 ----------HADLDYQLANLI--NSIEERLSLLSNYQIRY-------DRIS-----------QWLQRLEQRVEKDADVT 7030
Cdd:TIGR02168 605 kdlvkfdpklRKALSYLLGGVLvvDDLDNALELAKKLRPGYrivtldgDLVRpggvitggsakTNSSILERRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7031 AMTNPEQAAKQLEQQVN---SELQLRDKEREWLLSTSRELLTLYSEPEVR-SQVQQQSDSLIDRWQRLKYLAKQKATKIG 7106
Cdd:TIGR02168 685 KIEELEEKIAELEKALAelrKELEELEEELEQLRKELEELSRQISALRKDlARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7107 ELKMTLLRLEERIALIRAWLFEVESQLDkplNFESYTPNVIEAKLKEHEQIQRsiehHSSNVGEVLNLVEMLLNDADSWR 7186
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIE---QLKEELKALREALDELRAELTL----LNEEAANLRERLESLERRIAATE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7187 TQvntsglaasAQNLEQRWKNVCSQSAERKARILTIWNLLQQLIKLTAEHKNWLGKQESQI--AGFERDQKSHSKHKLEE 7264
Cdd:TIGR02168 838 RR---------LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALalLRSELEELSEELRELES 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7265 RQMELRAKLEELESQ--SVNLR------QLEQIYAKLAMSAGVEPENIQKLTLPTKVMVSMWR----QLTPRCHAL---- 7328
Cdd:TIGR02168 909 KRSELRRELEELREKlaQLELRleglevRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARrrlkRLENKIKELgpvn 988
|
810 820 830
....*....|....*....|....*....|....*...
gi 442626145 7329 LDAID--KDAKLMREFNNAQLE-ATNSLNAIQKALEQL 7363
Cdd:TIGR02168 989 LAAIEeyEELKERYDFLTAQKEdLTEAKETLEEAIEEI 1026
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6750-6950 |
3.14e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6750 ELSEQYKALTNLHN---------ETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERnalqlryihlkrvphL 6820
Cdd:COG4913 229 ALVEHFDDLERAHEaledareqiELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL---------------L 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6821 KHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALAtamRMEQASiGQRISNLRAALKTWQGFLQRVTQLSESYEQRVN 6900
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEA---QIRGNG-GDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442626145 6901 QL-------QQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALES 6950
Cdd:COG4913 370 ALglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
427-536 |
3.87e-10 |
|
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: 60.95 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 427 GDLKAEKWKQGARKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLV-NLAELKKTSNRQRLETAFDVAE 505
Cdd:cd21315 6 DDGPDDGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAE 82
|
90 100 110
....*....|....*....|....*....|.
gi 442626145 506 SKLGIAKLLDAEDVDVPKPDEKSIMTYVAQF 536
Cdd:cd21315 83 DWLDVPQLIKPEEMVNPKVDELSMMTYLSQF 113
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
267-376 |
7.42e-10 |
|
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: 59.99 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 267 EEQErvqKKTFTNWINSYLLkrvpPLRIDDLINDLRDGtklIALLEVLsgERL---PVEKGRVLR-----RPHFLSNANT 338
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGL----DPLINNLYEDLRDG---LVLLQVL--DKIqpgCVNWKKVNKpkplnKFKKVENCNY 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 442626145 339 ALQfLASKR-IKLVNINPADLVDGRPPVVLGLIWTIILY 376
Cdd:cd21219 70 AVD-LAKKLgFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
431-542 |
1.58e-09 |
|
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: 59.32 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 431 AEKWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGI 510
Cdd:cd21256 8 AREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGI 86
|
90 100 110
....*....|....*....|....*....|...
gi 442626145 511 AKLLDAED-VDVPKPDEKSIMTYVAQfLHKYPE 542
Cdd:cd21256 87 KSTLDINEmVRTERPDWQSVMTYVTA-IYKYFE 118
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2845-3533 |
1.83e-09 |
|
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: 65.46 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2845 DRVNALGDHI----KKYKDAKSRLAECSQFLGNIQQKLRELNRPIGSRIEDVQDLLGAYEGILKELKDSKSkmgdmqmdD 2920
Cdd:TIGR02168 232 LRLEELREELeelqEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ--------Q 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2921 LPELQSILAQQDDMIKLIEDQLAHLRQLLLLREQFIALINEIIAFIMK-YTDVIIDIENSPDSLEDKINKYDDVIVKIQE 2999
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEeLESLEAELEELEAELEELESRLEELEEQLET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3000 CEGVLASANDKGQKIASE--GNAADKNSITEQLQSLK-NQLQNLRKAVESQRQKHQLQLESHKKMAAELSEILDWLHSH- 3075
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEieRLEARLERLEDRRERLQqEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAl 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3076 EGAAKSRPLLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEIgMPSSLLemlSEGRSLVASLPHELEEREKYL 3155
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL-KNQSGL---SGILGVLSELISVDEGYEAAI 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3156 KNNRDSRLEYMqLVAKFNDWVHEAELRLQNSQHGIDYehLVQDLDEHKIFFGNEAPIRNLVHKQIQEAAD--KIWSSLNN 3233
Cdd:TIGR02168 540 EAALGGRLQAV-VVENLNAAKKAIAFLKQNELGRVTF--LPLDSIKGTEIQGNDREILKNIEGFLGVAKDlvKFDPKLRK 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3234 YEQSELSaelaqfQTKLTNTLANAKTQQSELEKEA-------ERWR-----------------EYQQSIDRVKATIERT- 3288
Cdd:TIGR02168 617 ALSYLLG------GVLVVDDLDNALELAKKLRPGYrivtldgDLVRpggvitggsaktnssilERRREIEELEEKIEELe 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3289 --------------KFVDEPVQNLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIRQADARNRQLIEQDnAGLNRS 3354
Cdd:TIGR02168 691 ekiaelekalaelrKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI-EELEER 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3355 WQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFRNV-----DPTVRSRRHLEDTKNAIQELREESNQLKS 3429
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeaaNLRERLESLERRIAATERRLEDLEEQIEE 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3430 SHKEIEALSKSILTFlgevhKPSAEAIQAKVDKLVEQQAKLN---DTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALH 3506
Cdd:TIGR02168 850 LSEDIESLAAEIEEL-----EELIEELESELEALLNERASLEealALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
730 740
....*....|....*....|....*..
gi 442626145 3507 EQLQsvhvydEHIAQTEQLLITLNSQV 3533
Cdd:TIGR02168 925 AQLE------LRLEGLEVRIDNLQERL 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1775-2731 |
2.87e-09 |
|
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: 64.69 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1775 ITKLQEVLSAINRNVDH---QAQAVQEdlvnWQQFQAGLQQIKPAV-------EQSEVKKLLEEVLAEKDNVEDLNDNCE 1844
Cdd:TIGR02168 188 LDRLEDILNELERQLKSlerQAEKAER----YKELKAELRELELALlvlrleeLREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1845 LLMEQSACTRIRDQTIETQAN-YTKLLTSAQGLVAKIEKNLSDHTEFLNY----KKEMDAWIEKAQQVLDDCSTDGDA-- 1917
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEeLQKELYALANEISRLEQQKQILRERLANlerqLEELEAQLEELESKLDELAEELAEle 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1918 AIIAQKLDTVNSLASRLPEgqhLLALVQDAyskasnitpEDKQEKLRELMTKVREDWDALGLAVKQKLSDLKQAQNRWND 1997
Cdd:TIGR02168 344 EKLEELKEELESLEAELEE---LEAELEEL---------ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1998 FAANKDKL--EKWLNETETTLKVAPETKGELSEMKTLLE----RYKTLSNELKLKGNELEQLQSEARDLGTEVdavNRLQ 2071
Cdd:TIGR02168 412 LEDRRERLqqEIEELLKKLEEAELKELQAELEELEEELEelqeELERLEEALEELREELEEAEQALDAAEREL---AQLQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2072 SRCDKLKNdcsahitaLEQEmfdynayHQSLQDVEKWLLQISFQLMAHNSL---FISNREQTQEQIkqhEALLVE-IQKY 2147
Cdd:TIGR02168 489 ARLDSLER--------LQEN-------LEGFSEGVKALLKNQSGLSGILGVlseLISVDEGYEAAI---EAALGGrLQAV 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2148 QTNLDDLNAKGQAQIKRYESSTPAIRPtvesqLKNIQDSynsllqtsvQIKNRLLESLAKFQEYEDTLDSIMRNLETYEP 2227
Cdd:TIGR02168 551 VVENLNAAKKAIAFLKQNELGRVTFLP-----LDSIKGT---------EIQGNDREILKNIEGFLGVAKDLVKFDPKLRK 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2228 IIQTELD--APATSLELAQNQLrcaqemqnKLNNEKSRLAAAVQACEAATASISRPSSPLETAMQAiPERELivrAKLED 2305
Cdd:TIGR02168 617 ALSYLLGgvLVVDDLDNALELA--------KKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILE-RRREI---EELEE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2306 LLDQVQSHLGGLTASVSELEQQQKQRAELQDWVKKqqssvsdwmmrpcklRPEAAQQELVSMNDLLNSIGdKRSQLMLEM 2385
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRK---------------ELEELSRQISALRKDLARLE-AEVEQLEER 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2386 TGSLGDEDTDLDDNIDKLESELMDAIAKKQAGqnvidgyRQGMADVQNWFDTLIKRMDVLDRgsglncaqkmaAINEIKN 2465
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEA-------EAEIEELEAQIEQLKEELKALRE-----------ALDELRA 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2466 EYelqghpkiQELKGKAAQVAEVisnldgqqveeqMKSLDRRFADLGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQ 2545
Cdd:TIGR02168 811 EL--------TLLNEEAANLRER------------LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2546 QIEELQAPKplgytpKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELEPV--EYSQLESALRNLNTENRNLSGV 2623
Cdd:TIGR02168 871 LESELEALL------NERASLEEALALLRSELEELSEELRELESKRSELRRELEELreKLAQLELRLEGLEVRIDNLQER 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2624 LKAELDRALEASKARKS-LENDLDKARQWLKTKISEVRKLPVYHPLTSAEIEkkiQENRKYDDDAKQFNDsvLTDVQRQA 2702
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENkIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYE---ELKERYDFLTAQKED--LTEAKETL 1019
|
970 980
....*....|....*....|....*....
gi 442626145 2703 ANIMKDCDDADKAALQQILDEIAADYQTL 2731
Cdd:TIGR02168 1020 EEAIEEIDREARERFKDTFDQVNENFQRV 1048
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
437-536 |
3.74e-09 |
|
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: 57.75 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 437 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDA 516
Cdd:cd21196 3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSA 82
|
90 100
....*....|....*....|
gi 442626145 517 EDVdVPKPDEKSIMTYVAQF 536
Cdd:cd21196 83 QAV-VAGSDPLGLIAYLSHF 101
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
439-533 |
5.54e-09 |
|
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: 57.28 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 439 RKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAED 518
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90
....*....|....*..
gi 442626145 519 VDV--PKPDEKSIMTYV 533
Cdd:cd21261 83 MMVmgRKPDPMCVFTYV 99
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3356-4174 |
1.20e-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: 62.77 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3356 QDLVRSLEQRRDNLQ---QLAEHWDGFENSLHAWEKAL--GRLEDKFRNVDPTvrsrrhLEDTKNAIQELREESNQLKSS 3430
Cdd:TIGR02168 192 EDILNELERQLKSLErqaEKAERYKELKAELRELELALlvLRLEELREELEEL------QEELKEAEEELEELTAELQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3431 HKEIEALSKsiltFLGEVHKpSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQ 3510
Cdd:TIGR02168 266 EEKLEELRL----EVSELEE-EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3511 SVHvydehiAQTEQLLITLNSQVQQAAEESKLLVAQTTA--HYQAKQNQLPSDIAQEFTALELLAERVQVTMETKEkdfk 3588
Cdd:TIGR02168 341 ELE------EKLEELKEELESLEAELEELEAELEELESRleELEEQLETLRSKVAQLELQIASLNNEIERLEARLE---- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3589 raktvrteyvDGVDEVQRWllQAEVQVQERSLTPTQMKELLQRINHEITaiyERFTLVKTNGQLIIENCRNSEEKTLVQT 3668
Cdd:TIGR02168 411 ----------RLEDRRERL--QQEIEELLKKLEEAELKELQAELEELEE---ELEELQEELERLEEALEELREELEEAEQ 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3669 TIDQLAASLAQVRGWLDEKKQAVGdsldawtRFMNLYQ---IVMSWASEKRNFIDQTIELRTLPE---------ARNKLN 3736
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQE-------NLEGFSEgvkALLKNQSGLSGILGVLSELISVDEgyeaaieaaLGGRLQ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3737 DYVT-SVKSIKPIVKHLSEMDKELEHIGQVTTVGDlkDKLQEAEDAKISVEAVLLERNSLLQEACEEWdqceRKIKDIRS 3815
Cdd:TIGR02168 549 AVVVeNLNAAKKAIAFLKQNELGRVTFLPLDSIKG--TEIQGNDREILKNIEGFLGVAKDLVKFDPKL----RKALSYLL 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3816 WHEKTKQGLDSSQQQKKPLRDQLGFCekTLADINVQKtklRLSIEKLEVHFRNGMGGdprLSENVDDLVRVLDGLGELVK 3895
Cdd:TIGR02168 623 GGVLVVDDLDNALELAKKLRPGYRIV--TLDGDLVRP---GGVITGGSAKTNSSILE---RRREIEELEEKIEELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3896 AKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRLVMAPTYLPHDRERALAEQQDLITQELDELLQSLSSVEDGIANMN 3975
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3976 QSsldgmlhgLKLIQSNLEVHERDAIELKNQAKKLptdpatERLLNDTVDRIDLLLRRtqqgitmIANAMHGQKKRQQEI 4055
Cdd:TIGR02168 775 EE--------LAEAEAEIEELEAQIEQLKEELKAL------REALDELRAELTLLNEE-------AANLRERLESLERRI 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 4056 DEYQQHLLELEQWIIEVSAELASfeptsdsstdeqvLKSQVERSQQLLRTLKDRQQSMEDLVEQTRQLqshpdvspladt 4135
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEA------------ 888
|
810 820 830
....*....|....*....|....*....|....*....
gi 442626145 4136 lmeqlqsiITILREQVTVATKRIFTIEKRIVDLRKAKSE 4174
Cdd:TIGR02168 889 --------LALLRSELEELSEELRELESKRSELRRELEE 919
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2641-2852 |
1.36e-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: 59.00 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2641 LENDLDKARQWLKTKISEVRKLpvYHPLTSAEIEKKIQENRKYDDDAKQFNDSVlTDVQRQAANIMKDCDDaDKAALQQI 2720
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERV-EALNELGEQLIEEGHP-DAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2721 LDEIAADYQTLKDESSKRGKSLDDLLQGRKAFEDSMKnMGDWLNEMETATEGELRTTSLPVLEEQLAHYKKLLSDAENKG 2800
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442626145 2801 GLINDVSEQGKSILPTLSNADKLKLNDDIKNMKDRYGRIKNTIDDRVNALGD 2852
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2827-3502 |
2.06e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2827 DDIKNMKDRYGRIKNTIDDRVNALGDHIKKYKDAKSRLAECSQFLGNIQQKLRELNrpigSRIEDVQDLLGAYEGILKEL 2906
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEIS----SELPELREELEKLEKEVKEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2907 KDSKSKMGDMQMDDLPELQSILAQQDDmIKLIEDQLAHLRQLLLLREQFIALINEI----------IAFIMKYTDVIIDI 2976
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEK-IRELEERIEELKKEIEELEEKVKELKELkekaeeyiklSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2977 ENSPDSLEDKINkydDVIVKIQECEgvlasandkgqkiasegnaadknSITEQLQSLKNQLQNLRKAVESQRQKHQLqLE 3056
Cdd:PRK03918 313 EKRLSRLEEEIN---GIEERIKELE-----------------------EKEERLEELKKKLKELEKRLEELEERHEL-YE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3057 SHKKMAAELSEIldwlhshegaaKSRpLLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEIGMPSSLLEMLSE 3136
Cdd:PRK03918 366 EAKAKKEELERL-----------KKR-LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3137 GRSLVASLPHEL-EEREKYLKNnrdsrlEYMQLVAKFNDWVHEAELRLqnsqhgidyEHLVQDLDEHKIFFGNEAPIRNL 3215
Cdd:PRK03918 434 AKGKCPVCGRELtEEHRKELLE------EYTAELKRIEKELKEIEEKE---------RKLRKELRELEKVLKKESELIKL 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3216 vhKQIQEAADKIWSSLNNYEQSELSAELAQFQtKLTNTLANAKTQQSELEKEAERWREYQQSidrvKATIERTKfvDEPV 3295
Cdd:PRK03918 499 --KELAEQLKELEEKLKKYNLEELEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKL--DELE 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3296 QNLAGLHFNIQKLSHaignvqsqnSDLTLVNQQAQSLirqaDARNRQLIEQDNAglNRSWQDLVRSLEQRRDNLQQLAEH 3375
Cdd:PRK03918 570 EELAELLKELEELGF---------ESVEELEERLKEL----EPFYNEYLELKDA--EKELEREEKELKKLEEELDKAFEE 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3376 WDGFENSLhawEKALGRLEDKFRNVDPtvrsrrhlEDTKNAIQELREESNQLKSSHKEIEALSKSIltflgevhkpsaEA 3455
Cdd:PRK03918 635 LAETEKRL---EELRKELEELEKKYSE--------EEYEELREEYLELSRELAGLRAELEELEKRR------------EE 691
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 442626145 3456 IQAKVDKLVEQqaklndtlRDKEQQVSKDLEEIEQVFRRISQLQDKL 3502
Cdd:PRK03918 692 IKKTLEKLKEE--------LEEREKAKKELEKLEKALERVEELREKV 730
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
268-373 |
2.14e-08 |
|
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: 56.09 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 268 EQERVQKKTFTNWINSYllkRVPPlRIDDLINDLRDGTKLIALLEVLSgerlP--VEKGRVLRRPH-------FLSNANT 338
Cdd:cd21298 2 IEETREEKTYRNWMNSL---GVNP-FVNHLYSDLRDGLVLLQLYDKIK----PgvVDWSRVNKPFKklganmkKIENCNY 73
|
90 100 110
....*....|....*....|....*....|....*
gi 442626145 339 ALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTI 373
Cdd:cd21298 74 AVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQL 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2406-2755 |
2.15e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2406 ELMDAIA-------KKQAGQNVIDGYRQGMADVQNWFDTLIKRMDVLDRGSglNCAQKMAAINEIKNEYElqGHPKIQEL 2478
Cdd:TIGR02169 157 KIIDEIAgvaefdrKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER--EKAERYQALLKEKREYE--GYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2479 KGKAAQVAEVISNLDGQqvEEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEgAKGEIDQLQnwVKQQIEELQAP----- 2553
Cdd:TIGR02169 233 EALERQKEAIERQLASL--EEELEKLTEEISELEKRLEEIEQLLEELNKKIK-DLGEEEQLR--VKEKIGELEAEiasle 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2554 ---KPLGYTPKDAEARQQKIKSLMkdaEAKQSLADVLEKRVANMQQELEPV---------EYSQLESALRNLNTENRNLS 2621
Cdd:TIGR02169 308 rsiAEKERELEDAEERLAKLEAEI---DKLLAEIEELEREIEEERKRRDKLteeyaelkeELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2622 GVLKAELDRALEASKARKSLENDLDKARQWLKTKISEVRKLpvyhpltSAEIEKKIQENRKYDDDAKQFNDSVLTDVQRQ 2701
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL-------NAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 442626145 2702 AANImkdcddADKAALQQILDEIAADYQTLKDESSKRGKSLDDLLQGRKAFEDS 2755
Cdd:TIGR02169 458 EQLA------ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
435-536 |
2.16e-08 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 55.85 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 435 KQGARKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLV-NLAELKKTSNRQRLETAFDVAESKLGIAKL 513
Cdd:cd21314 9 KQTPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQV 85
|
90 100
....*....|....*....|...
gi 442626145 514 LDAEDVDVPKPDEKSIMTYVAQF 536
Cdd:cd21314 86 IAPEEIVDPNVDEHSVMTYLSQF 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2975-3118 |
2.99e-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: 57.84 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2975 DIENSPDSLEDKINKYDDVIVKIQECEGVLASANDKGQKIASEGnAADKNSITEQLQSLKNQLQNLRKAVESQRQKHQLQ 3054
Cdd:cd00176 27 DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQERLEELNQRWEELRELAEERRQRLEEA 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442626145 3055 LESHKKMaAELSEILDWLHSHEGAAKSRPlLDRDPESVERELQKHQSLSQDIESYLNKFNKIND 3118
Cdd:cd00176 106 LDLQQFF-RDADDLEQWLEEKEAALASED-LGKDLESVEELLKKHKELEEELEAHEPRLKSLNE 167
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
442-536 |
4.48e-08 |
|
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: 54.89 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 442 LLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDVD- 520
Cdd:cd21250 9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMAs 88
|
90
....*....|....*.
gi 442626145 521 VPKPDEKSIMTYVAQF 536
Cdd:cd21250 89 AEEPDKLSMVMYLSKF 104
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
435-536 |
4.70e-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: 54.71 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 435 KQGARKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLVNLAEL---KKTSNRQRleTAFDVAESKLGIA 511
Cdd:cd21313 6 KQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCPDWESwdpQKPVDNAR--EAMQQADDWLGVP 80
|
90 100
....*....|....*....|....*
gi 442626145 512 KLLDAEDVDVPKPDEKSIMTYVAQF 536
Cdd:cd21313 81 QVITPEEIIHPDVDEHSVMTYLSQF 105
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
950-1164 |
5.29e-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: 57.46 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 950 QEYKSGIEQLSRWLRGAESVLDQRQVLGNSEQVKEYGQQLQQLASEIDDNEELFKTISRNFQSLIQDLSRD--EVDKMMK 1027
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDaeEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1028 LLKQEKESLVRIRAQLpaKLHLFHQLQIQQESLEAgqKEIHQWLSEAEQLLGTHNLSGGRDAINEQLHKHKTYFSRTVYY 1107
Cdd:cd00176 83 ELNQRWEELRELAEER--RQRLEEALDLQQFFRDA--DDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442626145 1108 RSMLESKNKVFQNLLKAVSSDDKIDTApasQQMQQLNERFNYVIQNAQQWEQRLDSA 1164
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIE---EKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2535-2746 |
6.68e-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: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2535 EIDQLQNWVKQQIEELQAPKPlGYTPKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELePVEYSQLESALRNLN 2614
Cdd:cd00176 8 DADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2615 TENRNLSGvLKAELDRALEASKARKSLENDLDKARQWLKTKISEVRKLPVYHPLTsaEIEKKIQENRKYDDDAKQfNDSV 2694
Cdd:cd00176 86 QRWEELRE-LAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLE--SVEELLKKHKELEEELEA-HEPR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442626145 2695 LTDVQRQAANIMKDCDDADKAALQQILDEIAADYQTLKDESSKRGKSLDDLL 2746
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2496-3068 |
7.32e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 7.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2496 QVEEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNwVKQQIEELQapKPLGYTPKDAEARQQKIKSLMK 2575
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-LKEEIEELE--KELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2576 DAEAKQSLADVLEKRVANMqQELEPV--EYSQLESALRNLNTENRNLSgVLKAELDRALEASKARKSLENDLDKARQWLK 2653
Cdd:PRK03918 267 RIEELKKEIEELEEKVKEL-KELKEKaeEYIKLSEFYEEYLDELREIE-KRLSRLEEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2654 TKISEVRK----LPVYHPLTSaEIEKKIQENRKYDddaKQFNDSVLTDVQRQAANIMKdcddaDKAALQQILDEIAADYQ 2729
Cdd:PRK03918 345 KKLKELEKrleeLEERHELYE-EAKAKKEELERLK---KRLTGLTPEKLEKELEELEK-----AKEEIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2730 TLKDESSKRGKSLDDL--------LQGRKAFEDSMKN--------MGDWLNEMETATEGE--LRtTSLPVLEEQLAHYKK 2791
Cdd:PRK03918 416 ELKKEIKELKKAIEELkkakgkcpVCGRELTEEHRKElleeytaeLKRIEKELKEIEEKErkLR-KELRELEKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2792 LLSdaenkgglINDVSEQGKSILPTLSNADKLKLNDDIKNMKDRYGRIkNTIDDRVNALGDHIKKYKDAKSRLAECSQFL 2871
Cdd:PRK03918 495 LIK--------LKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKL-IKLKGEIKSLKKELEKLEELKKKLAELEKKL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2872 GNIQQKLRELNRPIGSR----IEDVQDLLGAYEGILK---ELKDSKSkmgdmqmddlpELQSILAQQDDMIKLIEDQLAH 2944
Cdd:PRK03918 566 DELEEELAELLKELEELgfesVEELEERLKELEPFYNeylELKDAEK-----------ELEREEKELKKLEEELDKAFEE 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2945 LRQLLLLREQfiaLINEIIAFIMKYTDviidienspdslEDKINKYDDVIVKIQECEGVLASAndkgqkiasEGNAADKN 3024
Cdd:PRK03918 635 LAETEKRLEE---LRKELEELEKKYSE------------EEYEELREEYLELSRELAGLRAEL---------EELEKRRE 690
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 442626145 3025 SITEQLQSLKNQLQNLRKAVEsqrqkhqlQLESHKKMAAELSEI 3068
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKK--------ELEKLEKALERVEEL 726
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3225-3512 |
7.87e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3225 DKIWSSLNNYEQSELSAELAQFQTKLTNTLANAKTQQSELEKEAERWREYQQSIDRVKATIE------RTKFVDEPVQ-- 3296
Cdd:TIGR02169 214 QALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEelnkkiKDLGEEEQLRvk 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3297 -NLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIRQADARNRQLIEQ--DNAGLNRSWQDLVRSLEQRRDNLQQLA 3373
Cdd:TIGR02169 294 eKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieEERKRRDKLTEEYAELKEELEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3374 EhwdgfenslhAWEKALGRLEDKFRNVdptvrsRRHLEDTKNAIQELR-------EESNQLKSSHKEIEALSKSILTFLG 3446
Cdd:TIGR02169 374 E----------EVDKEFAETRDELKDY------REKLEKLKREINELKreldrlqEELQRLSEELADLNAAIAGIEAKIN 437
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626145 3447 EVhKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSV 3512
Cdd:TIGR02169 438 EL-EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
268-371 |
8.05e-08 |
|
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: 54.35 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 268 EQERvQKKTFTNWINSYllkRVPPLrIDDLINDLRDGTKLI-ALLEVLSGErlpVEKGRV--------LRRPHFLSNANT 338
Cdd:cd21300 4 EGER-EARVFTLWLNSL---DVEPA-VNDLFEDLRDGLILLqAYDKVIPGS---VNWKKVnkapasaeISRFKAVENTNY 75
|
90 100 110
....*....|....*....|....*....|...
gi 442626145 339 ALQFLASKRIKLVNINPADLVDGRPPVVLGLIW 371
Cdd:cd21300 76 AVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
6572-7522 |
9.23e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.59 E-value: 9.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6572 TLANVAETQdKERKELDKEVTLAKAYFNNvqqDISREAPQNPKESEEQLAALRAhlqtLARTEEQLRQLKERHQN--SEV 6649
Cdd:PRK04863 245 TLEAIRVTQ-SDRDLFKHLITESTNYVAA---DYMRHANERRVHLEEALELRRE----LYTSRRQLAAEQYRLVEmaREL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6650 ApsvASSDDDGILEvlalwqkifqdtfQEYHRLSTRLARSQNsseALRLWRQYLQHVQSFLscaipEDYSSLREQQQLCA 6729
Cdd:PRK04863 317 A---ELNEAESDLE-------------QDYQAASDHLNLVQT---ALRQQEKIERYQADLE-----ELEERLEEQNEVVE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6730 IHQNLLISQQSVLSETPLE-SELSEQykaltnlhnetLSRIMQRNGELERRVSgwnAYRQQLAAL--------------- 6793
Cdd:PRK04863 373 EADEQQEENEARAEAAEEEvDELKSQ-----------LADYQQALDVQQTRAI---QYQQAVQALerakqlcglpdltad 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6794 --LDWLRQREAERNALQLRyihlkrVPHLKHRL---DAMIQQLDQGEQ----------QSKALQEQQQELARHCD----D 6854
Cdd:PRK04863 439 naEDWLEEFQAKEQEATEE------LLSLEQKLsvaQAAHSQFEQAYQlvrkiagevsRSEAWDVARELLRRLREqrhlA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6855 ALATAMRMEQASIGQRISNLRAALKTWQGFLQRvTQLSESYEQRVNQLQQEFGAAQKLLDANSESLPTQPAAIEQLLGSL 6934
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKR-LGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6935 RAQRVQLGAQVSALESLTVTQEELKECiSPHDMKTiRQRNWLLWQQHADLDYQLANLINSIEERLSLLsnyQIRYDRISQ 7014
Cdd:PRK04863 592 QARIQRLAARAPAWLAAQDALARLREQ-SGEEFED-SQDVTEYMQQLLERERELTVERDELAARKQAL---DEEIERLSQ 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7015 -------WLQRLEQRV------EKDADVTAMTNPEQAAkqLEQQVNSELQLRDkerewLLSTSRELLTLYSEPEVRSQVQ 7081
Cdd:PRK04863 667 pggsedpRLNALAERFggvllsEIYDDVSLEDAPYFSA--LYGPARHAIVVPD-----LSDAAEQLAGLEDCPEDLYLIE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7082 QQSDSLIDRWQRLKYLAKQKATKIGELKMTLLRL-----------EERIALIRAWLFEVESQLDKpLNFESytpnvieak 7150
Cdd:PRK04863 740 GDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFpevplfgraarEKRIEQLRAEREELAERYAT-LSFDV--------- 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7151 lkehEQIQRSIEHHSSNVGEVLNLV-----EMLLNDADSWRTQVNTSGLAASAQNLEQRwknvcsqSAERKARiltiwNL 7225
Cdd:PRK04863 810 ----QKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVELERALADHESQEQQQR-------SQLEQAK-----EG 873
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7226 LQQLIKLtaehknwlgkqESQIAGFERDQkshskhkLEERQMELRAKLEELE-------SQSVNLRQLEQIYAKLAmsag 7298
Cdd:PRK04863 874 LSALNRL-----------LPRLNLLADET-------LADRVEEIREQLDEAEeakrfvqQHGNALAQLEPIVSVLQ---- 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7299 VEPENIQKLTLPTKVMVSMWRQLTPRCHALLDAIDKDAKLMREFNNAQLEATNSLNaiqkalEQLPsaenqqtskaepka 7378
Cdd:PRK04863 932 SDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKNSDLN------EKLR-------------- 991
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7379 vlQRLESLEKKLQDAQQHVQQADNLAQEAKTRtkqqpqlkqLLELVSAYTTLWQTVQtrivtlkttwltRAAQAAASLPV 7458
Cdd:PRK04863 992 --QRLEQAEQERTRAREQLRQAQAQLAQYNQV---------LASLKSSYDAKRQMLQ------------ELKQELQDLGV 1048
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626145 7459 ----SEAANAAVQVNTLSQRkLRQAQQmQREtsitakdayimELQTAITECQNNLDELQRTVVDKTRK 7522
Cdd:PRK04863 1049 padsGAEERARARRDELHAR-LSANRS-RRN-----------QLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
268-379 |
9.79e-08 |
|
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: 54.22 E-value: 9.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 268 EQERVQKKTFTNWINSYllkRVPPLrIDDLINDLRDGTKLIALLEVLsgeRLPVEKGRVLRRPHFL--------SNANTA 339
Cdd:cd21329 2 EGESSEERTFRNWMNSL---GVNPY-VNHLYSDLCDALVIFQLYEMT---RVPVDWGHVNKPPYPAlggnmkkiENCNYA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 442626145 340 LQFLASK-RIKLVNINPADLVDGRPPVVLGLIWTIILYFQL 379
Cdd:cd21329 75 VELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTL 115
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
6747-7134 |
1.00e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6747 LESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHLK----------- 6815
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELReeleklekllq 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6816 ------RVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELAR------HCDDALATAMRMEQASIGQRISNLRAALKTWQG 6883
Cdd:COG4717 127 llplyqELEALEAELAELPERLEELEERLEELRELEEELEEleaelaELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6884 FLQRVTQLSESYEQRVNQLQQEFGAAQKllDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESL------------ 6951
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLEN--ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIltiagvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6952 -------------TVTQEELKECISPHDMKTIRQRNWLLWqqHADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQR 7018
Cdd:COG4717 285 llallflllarekASLGKEAEELQALPALEELEEEELEEL--LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7019 LEQRVEKD--------ADVTAMTNPEQAAKQLEQQVNSELQLRDKER--EWLLSTSRELLTLYSEPEVRSQVQQQSDSLI 7088
Cdd:COG4717 363 LQLEELEQeiaallaeAGVEDEEELRAALEQAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEELE 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 442626145 7089 DRWQRLKYLAKQKATKIGELKMtlLRLEERIALIRAWLFEVESQLD 7134
Cdd:COG4717 443 ELEEELEELREELAELEAELEQ--LEEDGELAELLQELEELKAELR 486
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2641-3870 |
1.73e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 58.91 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2641 LENDLDKARQWL---KTKISEVRKLPVY-HPLTSAEIEKKIQENrkydddAKQFNdsvltdVQRQAANIMKDCDDADKAA 2716
Cdd:TIGR01612 445 FKDDFDEFNKPIpksKLKALEKRFFEIFeEEWGSYDIKKDIDEN------SKQDN------TVKLILMRMKDFKDIIDFM 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2717 LQQILDEIAADYQTLKD-ESSKRGKSLDDLLQGRKAFEDSMKNMGDWLNEMETATEGElrttslpvlEEQLAHYKKLLSD 2795
Cdd:TIGR01612 513 ELYKPDEVPSKNIIGFDiDQNIKAKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEE---------NEDSIHLEKEIKD 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2796 AENKGGLINDVSeqgksilpTLSNADKLKLNDDIKNMKDRYGRIKNTID-----DRVNALGDHIKK-------------- 2856
Cdd:TIGR01612 584 LFDKYLEIDDEI--------IYINKLKLELKEKIKNISDKNEYIKKAIDlkkiiENNNAYIDELAKispyqvpehlknkd 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2857 --YKDAKSRLAECSQ--------FLGNIQQ-----------KLRELNRPIGSRIEDVQDLLGA-YEGILKELKDSKSKMG 2914
Cdd:TIGR01612 656 kiYSTIKSELSKIYEddidalynELSSIVKenaidntedkaKLDDLKSKIDKEYDKIQNMETAtVELHLSNIENKKNELL 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2915 DMQMDDLPELQSILAQqdDMIKLIEDQLAHLRQLLLLREQFIALINEIIAFIMKYTDV------IIDIENSPDslEDKIN 2988
Cdd:TIGR01612 736 DIIVEIKKHIHGEINK--DLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIknhyndQINIDNIKD--EDAKQ 811
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2989 KYDdvivKIQECEGVLASANDKGQKIASEGNAAdKNSITEQLQSLKNQLQNLRKAVESQrqkHQLQLESHKKMAAELSEi 3068
Cdd:TIGR01612 812 NYD----KSKEYIKTISIKEDEIFKIINEMKFM-KDDFLNKVDKFINFENNCKEKIDSE---HEQFAELTNKIKAEISD- 882
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3069 lDWLHSHEGAAK-SRPLLDRDPESVERELQKHQSL-------------SQDIESYLNKFNKINDGVKTEIGM--PSSLLE 3132
Cdd:TIGR01612 883 -DKLNDYEKKFNdSKSLINEINKSIEEEYQNINTLkkvdeyikicentKESIEKFHNKQNILKEILNKNIDTikESNLIE 961
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3133 MlSEGRSLVASLPHELEEREKYLKNNRDSRLEYM--QLVAKFNDWVHEAELRLQNSqhgidyehLVQDLDEhkiffgNEA 3210
Cdd:TIGR01612 962 K-SYKDKFDNTLIDKINELDKAFKDASLNDYEAKnnELIKYFNDLKANLGKNKENM--------LYHQFDE------KEK 1026
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3211 PIRNLVHKqiQEAADK--------IWSSLNNYEQsELSAELAQFQTKL-TNTLANAKTQQSELEKEAERWREYQQSiDRV 3281
Cdd:TIGR01612 1027 ATNDIEQK--IEDANKnipnieiaIHTSIYNIID-EIEKEIGKNIELLnKEILEEAEINITNFNEIKEKLKHYNFD-DFG 1102
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3282 KAtiERTKFVDEPVQNLAGLHFNIQKLSHAIGNVQS-QNSDLTLVNQQAQSLIRQADARNRQLIEQDNAGLNRSWQDLVR 3360
Cdd:TIGR01612 1103 KE--ENIKYADEINKIKDDIKNLDQKIDHHIKALEEiKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENIVT 1180
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3361 SLEQRR---DNLQQLAEHWDGFENSLHAWEKA---------------LGRLEDKFRNVDPTVRSR----RHLEDTKNAIQ 3418
Cdd:TIGR01612 1181 KIDKKKniyDEIKKLLNEIAEIEKDKTSLEEVkginlsygknlgklfLEKIDEEKKKSEHMIKAMeayiEDLDEIKEKSP 1260
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3419 ELREESNQLKSSHKEIEALSKSILTF-----LGEVHKPSAEAIQAKVDKLVE---QQAKLNDTLRDKEQQVS---KDLEE 3487
Cdd:TIGR01612 1261 EIENEMGIEMDIKAEMETFNISHDDDkdhhiISKKHDENISDIREKSLKIIEdfsEESDINDIKKELQKNLLdaqKHNSD 1340
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3488 IEQVFRRISQLQD--KLNALHEQLQSVHVYDEHIAQTeqllitlNSQVQQAAEESKLLVAQTtahyqakqnqlpsdiaQE 3565
Cdd:TIGR01612 1341 INLYLNEIANIYNilKLNKIKKIIDEVKEYTKEIEEN-------NKNIKDELDKSEKLIKKI----------------KD 1397
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3566 FTALELLAERVQVTMETKEKDfkraktvrtEYVDGVDEVQRWLLQAEVQVQersltpTQMKElLQRINHEITAIYERFTL 3645
Cdd:TIGR01612 1398 DINLEECKSKIESTLDDKDID---------ECIKKIKELKNHILSEESNID------TYFKN-ADENNENVLLLFKNIEM 1461
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3646 VKTNGQLIIENCRNSEEKTLvQTTIDQLAASLAQVRGWLDE---KKQAVGDSLDAWTRFMNLYQIVMS--WASEKRNFID 3720
Cdd:TIGR01612 1462 ADNKSQHILKIKKDNATNDH-DFNINELKEHIDKSKGCKDEadkNAKAIEKNKELFEQYKKDVTELLNkySALAIKNKFA 1540
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3721 QT-----IELRTLPEARNKLN-DYVTSVKSIKPIVKHLSEMDKELEH--------IGQVTTVGDLKDKLQEAEDAKISVE 3786
Cdd:TIGR01612 1541 KTkkdseIIIKEIKDAHKKFIlEAEKSEQKIKEIKKEKFRIEDDAAKndksnkaaIDIQLSLENFENKFLKISDIKKKIN 1620
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3787 AVLLERNSLLQEACE-EWDQCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQlgfcEKTLADINVQKTKLRLSIEKLEVH 3865
Cdd:TIGR01612 1621 DCLKETESIEKKISSfSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDK----KKELDELDSEIEKIEIDVDQHKKN 1696
|
....*
gi 442626145 3866 FRNGM 3870
Cdd:TIGR01612 1697 YEIGI 1701
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6555-7162 |
1.75e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6555 ELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDIsreapqnpkesEEQLAALRAHLQTLARTE 6634
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-----------EEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6635 EQLRQLKERHQNsevapsvASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEALRLwrqylqhvqsflscai 6714
Cdd:COG1196 302 QDIARLEERRRE-------LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA---------------- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6715 pedysSLREQQQLCAIHQNLLISQQSVLSEtpLESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALL 6794
Cdd:COG1196 359 -----ELAEAEEALLEAEAELAEAEEELEE--LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6795 DWLRQREAERNALQlryihlkrvphlkhRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALATAMRmEQASIGQRISNL 6874
Cdd:COG1196 432 ELEEEEEEEEEALE--------------EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE-ELAEAAARLLLL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6875 RAALKTWQGFLQRVTQLsesyeqrvnQLQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRV--QLGAQVSALESLT 6952
Cdd:COG1196 497 LEAEADYEGFLEGVKAA---------LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVveDDEVAAAAIEYLK 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6953 VTQEELKECISPHDMKTIRQRNWLLWQQHADLDYQL-ANLINSIEERLSLLSNY----QIRYDRISQWLQRLEQRVEKDA 7027
Cdd:COG1196 568 AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLvASDLREADARYYVLGDTllgrTLVAARLEAALRRAVTLAGRLR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7028 DVT-AMTNPEQAAKQLEQQVNSELQLRDKEREWLLSTSRELLtlysepEVRSQVQQQSDSLIDRWQRLKYLAKQKATKIG 7106
Cdd:COG1196 648 EVTlEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA------EEELELEEALLAEEEEERELAEAEEERLEEEL 721
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 442626145 7107 ELKMTLLRLEERIALIRAWLFEVESQLDKPLNFESYTPNVIEAKLKEHEQIQRSIE 7162
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2892-3436 |
3.43e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2892 VQDLLGAYEGILKELKDSKSKMGDMQMDD-LPELQSILAQQDDMIKLIEDQLAHLRQLLLLREQFIAL-------INEII 2963
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDLHErLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEheerreeLETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2964 AFIMKYTDVIIDIENSPDSLEDKINKYDDVIVKI-QECEGVLASAndkgqkiasEGNAADKNSITEQLQSLKNQLQNLRK 3042
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELeEERDDLLAEA---------GLDDADAEAVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3043 AVESQR---QKHQLQLESHKKMAAELSEILDWLHshEGAAKsrplLDRDPESVERELQKHQSLSQDIESYLNKFNKINDG 3119
Cdd:PRK02224 329 RLEECRvaaQAHNEEAESLREDADDLEERAEELR--EEAAE----LESELEEAREAVEDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3120 VKTEIGMPSSLLEMLSEGRSlvaSLPHELEEREKYLKNNRDSRLEYMQLVAKFNdwVHEAELRLQNSQH--GI-DYEHLV 3196
Cdd:PRK02224 403 APVDLGNAEDFLEELREERD---ELREREAELEATLRTARERVEEAEALLEAGK--CPECGQPVEGSPHveTIeEDRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3197 QDLDEHKIFFGNEAPIRNLVH---KQIQEAADKIWSSLNNYEQS-ELSAELAQFQTKLTNTLANAKTQQSELEKEAERWR 3272
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLeraEDLVEAEDRIERLEERREDLeELIAERRETIEEKRERAEELRERAAELEAEAEEKR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3273 E-YQQSIDRVKATIERTKFVD----------EPVQNLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIRQADARNR 3341
Cdd:PRK02224 558 EaAAEAEEEAEEAREEVAELNsklaelkeriESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKR 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3342 QLIEQ-DNAGLNRSWQDLVRS---LEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDkfrnvdptVRSRR-HLEDTKNA 3416
Cdd:PRK02224 638 ELEAEfDEARIEEAREDKERAeeyLEQVEEKLDELREERDDLQAEIGAVENELEELEE--------LRERReALENRVEA 709
|
570 580
....*....|....*....|
gi 442626145 3417 IQELREESNQLKSSHKEIEA 3436
Cdd:PRK02224 710 LEALYDEAEELESMYGDLRA 729
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
268-374 |
3.62e-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: 53.12 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 268 EQERVqkkTFTNWINSYL-----LKRVPPLRIDD--LINDLRDGT---KLIALLEVLSGERLPVEKGRVlrRPHFLS-NA 336
Cdd:cd21323 23 EEEKV---AFVNWINKALegdpdCKHVVPMNPTDesLFKSLADGIllcKMINLSQPDTIDERAINKKKL--TPFTISeNL 97
|
90 100 110
....*....|....*....|....*....|....*...
gi 442626145 337 NTALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21323 98 NLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQII 135
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3020-3686 |
3.75e-07 |
|
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: 57.76 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3020 AADKNSITEQLQSLKNQLQNLRKAVESQRQKHQlQLESHKKMAAEL-----SEILDWLHSHEGAAKSRPLLDRDPESVER 3094
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELE-ELESRLEELEEQletlrSKVAQLELQIASLNNEIERLEARLERLED 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3095 ELQKhqsLSQDIESYLNKFNKINdgvKTEIGMPSSLLEMLSEGrslvasLPHELEEREKYLKNNRDSRLEYMQLVAKFND 3174
Cdd:TIGR02168 415 RRER---LQQEIEELLKKLEEAE---LKELQAELEELEEELEE------LQEELERLEEALEELREELEEAEQALDAAER 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3175 WVHEAELRLqnsqhgidyeHLVQDLDEHKIFFGNEapIRNLVHKQIQEAADK--IWSSLNNYEQSELSAELA---QFQTK 3249
Cdd:TIGR02168 483 ELAQLQARL----------DSLERLQENLEGFSEG--VKALLKNQSGLSGILgvLSELISVDEGYEAAIEAAlggRLQAV 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3250 LTNTLANAKTQQSELeKEAERWREYQQSIDRVKAT------IERTKFVDEPVQNLAGLHFNIQKLSHAIGNVQSQnsdLT 3323
Cdd:TIGR02168 551 VVENLNAAKKAIAFL-KQNELGRVTFLPLDSIKGTeiqgndREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGG---VL 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3324 LVN--QQAQSLIRQADARNRqLIEQDNAGLNRSW------QDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLED 3395
Cdd:TIGR02168 627 VVDdlDNALELAKKLRPGYR-IVTLDGDLVRPGGvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRK 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3396 KFRNVDPTVRSRRHLEDTKNaiQELREESNQLKSSHKEIEALSKSILTFLGEVHKPSAE--AIQAKVDKLVEQQAKLNDT 3473
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELS--RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEieELEERLEEAEEELAEAEAE 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3474 LRDKEQQVSKDLEEIEQVFRRISQLQDKLNAL----HEQLQSVHVYDEHIAQTEQLLITLNSQVQQAAEESKLLVAQtta 3549
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELTLLneeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE--- 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3550 hyQAKQNQLPSDIAQEFTALELLAERVQVTMETKEKDfkraktvRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELL 3629
Cdd:TIGR02168 861 --IEELEELIEELESELEALLNERASLEEALALLRSE-------LEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 442626145 3630 QRINHEITAIYERFT-LVKTNGQLIIENCRNSEEKtlvqttIDQLAASLAQVRGWLDE 3686
Cdd:TIGR02168 932 EGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDD------EEEARRRLKRLENKIKE 983
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2094-2264 |
4.14e-07 |
|
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: 54.76 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2094 DYNAYHQSLQDVEKWLLQIsfQLMAHNSLFISNREQTQEQIKQHEALLVEIQKYQTNLDDLNAKGQAQIKRYESSTPAIR 2173
Cdd:cd00176 1 KLQQFLRDADELEAWLSEK--EELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2174 ptveSQLKNIQDSYNSLLQTSVQIKNRLLESLAKFQEYEDTLDsIMRNLETYEPIIQTELdaPATSLELAQNQLRCAQEM 2253
Cdd:cd00176 79 ----ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKEL 151
|
170
....*....|.
gi 442626145 2254 QNKLNNEKSRL 2264
Cdd:cd00176 152 EEELEAHEPRL 162
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
275-376 |
4.20e-07 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 51.95 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 275 KTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKRIKLVNIN 354
Cdd:cd21286 3 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 82
|
90 100
....*....|....*....|..
gi 442626145 355 PADLVDGRPPVVLGLIWTIILY 376
Cdd:cd21286 83 AEEIRNGNLKAILGLFFSLSRY 104
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
267-378 |
4.41e-07 |
|
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: 52.27 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 267 EEQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASK 346
Cdd:cd21285 5 EAENGFDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSFLAAK 84
|
90 100 110
....*....|....*....|....*....|..
gi 442626145 347 RIKLVNINPADLVDGRPPVVLGLIWTIILYFQ 378
Cdd:cd21285 85 GINIQGLSAEEIRNGNLKAILGLFFSLSRYKQ 116
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1894-2766 |
4.57e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.54 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1894 KKEMDAWIEKAQQVLDDCSTDGDAAIIAQKLDTVNSLASRLpegQHLLALVQDAYSKASnitpedkqeklrelmtkvred 1973
Cdd:pfam12128 220 RQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRL---SHLHFGYKSDETLIA--------------------- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1974 wdalglavkqklsdlkqaqnrwndfaankdklekwlnetettlkvapetkgelsemkTLLERYKTLSNELKlkgnelEQL 2053
Cdd:pfam12128 276 ---------------------------------------------------------SRQEERQETSAELN------QLL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2054 QSEARDLGTEVDAVNRLQSRCDKLKNDCSAHITALEQemfDYNAYHQSlqDVEKwllqisfqLMAHNSLFISNREQTQEQ 2133
Cdd:pfam12128 293 RTLDDQWKEKRDELNGELSAADAAVAKDRSELEALED---QHGAFLDA--DIET--------AAADQEQLPSWQSELENL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2134 IKQHEALLVEIQKYQTNLDDLNAKGQAQ----IKRYESSTPAIRPTVESQLKNIQDSYNSLLQtsvQIKNRLLESLAKFQ 2209
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQnnrdIAGIKDKLAKIREARDRQLAVAEDDLQALES---ELREQLEAGKLEFN 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2210 EYEDTLDSIMRNLETYEPIIQTEldaPATSLELAQNQLRC--AQEMQNKLNNEKSRLAAAVQACEAATASISRpssplet 2287
Cdd:pfam12128 437 EEEYRLKSRLGELKLRLNQATAT---PELLLQLENFDERIerAREEQEAANAEVERLQSELRQARKRRDQASE------- 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2288 AMQAIPERELIVRAKLEDLLDQVQSHLGGLTASVseleqqqkqRAELQDWVKKQQSSVSDWMMRPCKLRPEAAQQelvSM 2367
Cdd:pfam12128 507 ALRQASRRLEERQSALDELELQLFPQAGTLLHFL---------RKEAPDWEQSIGKVISPELLHRTDLDPEVWDG---SV 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2368 NDLLNSIGDKRSQLMLEMTGSLGDEDTdLDDNIDKLESELMDAIAKKQAGQNV-------IDGYRQGMAD----VQNWFD 2436
Cdd:pfam12128 575 GGELNLYGVKLDLKRIDVPEWAASEEE-LRERLDKAEEALQSAREKQAAAEEQlvqangeLEKASREETFartaLKNARL 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2437 TLIkRMDVLDRGSGLNCAQKMAAINEIKNE--YELQGHPKIQELKGKAAQVAEvisnlDGQQVEEQMKSLDRRFADLGKR 2514
Cdd:pfam12128 654 DLR-RLFDEKQSEKDKKNKALAERKDSANErlNSLEAQLKQLDKKHQAWLEEQ-----KEQKREARTEKQAYWQVVEGAL 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2515 IDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIeelqapKPLGYTPKDAEARQQKIKSLMKDAE-AKQSLADVLEKRVan 2593
Cdd:pfam12128 728 DAQLALLKAAIAARRSGAKAELKALETWYKRDL------ASLGVDPDVIAKLKREIRTLERKIErIAVRRQEVLRYFD-- 799
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2594 MQQELEPVEYSQLESALRNLNTENRNLSGVLK-----AELDRAlEASKARKSLENDLDKARQWLKTKISEVRKLPVYH-P 2667
Cdd:pfam12128 800 WYQETWLQRRPRLATQLSNIERAISELQQQLArliadTKLRRA-KLEMERKASEKQQVRLSENLRGLRCEMSKLATLKeD 878
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2668 LTSAEIEKKIQENRKYDDDAKQFNDSVLTDVQrqaanimKDCDDADKAALQQILDEIAADYQTLKDESSKRGKSLDDLLQ 2747
Cdd:pfam12128 879 ANSEQAQGSIGERLAQLEDLKLKRDYLSESVK-------KYVEHFKNVIADHSGSGLAETWESLREEDHYQNDKGIRLLD 951
|
890
....*....|....*....
gi 442626145 2748 GRKAFedsmKNMGDWLNEM 2766
Cdd:pfam12128 952 YRKLV----PYLEQWFDVR 966
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6792-7392 |
5.84e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6792 ALLDWLRQREAERNALQLRyihlkrvpHLKHRLDAMIQQLDQGEQQSKALQEQQQEL---------ARHCDDALATAMRM 6862
Cdd:COG1196 217 ELKEELKELEAELLLLKLR--------ELEAELEELEAELEELEAELEELEAELAELeaeleelrlELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6863 EQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKLLDANSESLptqpAAIEQLLGSLRAQRVQLG 6942
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL----EEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6943 AQVSALESLTVTQEELKEcisphdmktirqrnwLLWQQHADLDYQLANLINSIEERLSLLSNYQIRYDRisqwlqRLEQR 7022
Cdd:COG1196 365 EALLEAEAELAEAEEELE---------------ELAEELLEALRAAAELAAQLEELEEAEEALLERLER------LEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7023 VEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWLLSTSRELltLYSEPEVRSQVQQQSDSLIDRWQRLK------- 7095
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL--LEEAALLEAALAELLEELAEAAARLLllleaea 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7096 -YLAKQKATKIGELKMTLLRLEERIALIRAWLFEVESQLDKPLNfesytPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNL 7174
Cdd:COG1196 502 dYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA-----AALQNIVVEDDEVAAAAIEYLKAAKAGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7175 VEMLLNDADSWRTQVNTSGLAASAQNL---EQRWKNVCSQSAERKARILTIWNL-----------LQQLIKLTAEHKNWL 7240
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLvasDLREADARYYVLGDTLLGRTLVAArleaalrravtLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7241 GKQESQIAGFERDQKSHSKHKLEERQMELRAKLEELESQSVNLRQLE--QIYAKLAMSAGVEPENIQKLTLPTKVMVSMW 7318
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEeeERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626145 7319 RQLTPRCHALLDAIDKDAKLMREFNNAQLEAtnSLNAIQKALEQL----PSAENQQtskaepKAVLQRLESLEKKLQD 7392
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELER--ELERLEREIEALgpvnLLAIEEY------EELEERYDFLSEQRED 806
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6231-6997 |
6.10e-07 |
|
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: 56.99 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6231 EKVGELFSLSHKISTqIAEELEGASVLRDQLQAIQEGISNQRKHQAKISVILDECEAAERQGADVLEKAVADCQAAGEEL 6310
Cdd:TIGR02168 285 ELQKELYALANEISR-LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6311 VISWQEIMRIRQMLHTLPMRLKMSVSpvKLERDISQLQDDHAFLESKCTNI---MAILRSRLAVWLR--YERQLELVHGS 6385
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVA--QLELQIASLNNEIERLEARLERLedrRERLQQEIEELLKklEEAELKELQAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6386 VQETDFMMELIRVHGQVDYERLRKATERLEGLAGDLHNREQLIDELKGAAKPLiescdVQIVEQIESAvQEAVVAWNDTS 6465
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL-----ERLQENLEGF-SEGVKALLKNQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6466 ENLQQLRTRYQRAVELWDKYRNASAAVKNSIDQQMdAVKSLEQPLDALQHAKvcQDNLTTQNdrILELRDIVAKIAADVG 6545
Cdd:TIGR02168 516 SGLSGILGVLSELISVDEGYEAAIEAALGGRLQAV-VVENLNAAKKAIAFLK--QNELGRVT--FLPLDSIKGTEIQGND 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6546 LDASALMQGELDALgQRLAECKDAITT-----LANVAETQDkerkeLDKEVTLAKAY---FNNVQQD---ISREAPQNPK 6614
Cdd:TIGR02168 591 REILKNIEGFLGVA-KDLVKFDPKLRKalsylLGGVLVVDD-----LDNALELAKKLrpgYRIVTLDgdlVRPGGVITGG 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6615 ESEEQLAALrAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSE 6694
Cdd:TIGR02168 665 SAKTNSSIL-ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6695 ALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLCAIHQNLLISQQSVLSE-----TPLESELSEQYKALTNLhNETLSRI 6769
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeelKALREALDELRAELTLL-NEEAANL 822
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6770 MQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHLKRVphLKHRLDAMIQQLDQGEQQSKALQEQQQELA 6849
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE--LESELEALLNERASLEEALALLRSELEELS 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6850 RHCDDALATAMRMEQASIGQRISNLRAALKtWQGFLQRVTQLSEsyeqrvnQLQQEFGAAQKLLDANSESLPTQPAAIEQ 6929
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELR-LEGLEVRIDNLQE-------RLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626145 6930 LLGSLRAQRVQLGA-QVSALESLtvtqEELKEcisphdmktiRQRNwlLWQQHADLDYQLANLINSIEE 6997
Cdd:TIGR02168 973 RLKRLENKIKELGPvNLAAIEEY----EELKE----------RYDF--LTAQKEDLTEAKETLEEAIEE 1025
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
432-536 |
8.87e-07 |
|
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: 51.34 E-value: 8.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 432 EKWKQGARKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLV-NLAELKKTSNRQRLETAFDVAESKLGI 510
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*.
gi 442626145 511 AKLLDAEDVDVPKPDEKSIMTYVAQF 536
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQF 109
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
6582-7294 |
9.50e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.13 E-value: 9.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6582 KERKELDKEVTLAKAYFNNVQQDisreAPQNPKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSdddgi 6661
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLC----TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK----- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6662 levlalWQKIFQDTFQEYHRLSTRLARSQNSSEAL---RLWRQYLQHVQSFLSC--AIPEDYSSLREQQ----QLCAIHQ 6732
Cdd:TIGR00618 258 ------KQQLLKQLRARIEELRAQEAVLEETQERInraRKAAPLAAHIKAVTQIeqQAQRIHTELQSKMrsraKLLMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6733 NLLISQQSVLSETPLESELSEQYKALTNLHNETLSR--IMQRNGELERRVSGWnayRQQLAALLDWLRQREAERNALQlR 6810
Cdd:TIGR00618 332 AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIreISCQQHTLTQHIHTL---QQQKTTLTQKLQSLCKELDILQ-R 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6811 YIHLKRVPHLKHRldAMIQQLDQGEQQSKALQE--QQQELARHCDDALATAMRMEQASIGQRISNLRAALKTWQGFLQRV 6888
Cdd:TIGR00618 408 EQATIDTRTSAFR--DLQGQLAHAKKQQELQQRyaELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6889 TQLSESYEQRVNQLQQefgaaqklldanseslptQPAAIEQLLGSLRAQRVQLGaqvsaleSLTVTQEElkecisphdMK 6968
Cdd:TIGR00618 486 TRKKAVVLARLLELQE------------------EPCPLCGSCIHPNPARQDID-------NPGPLTRR---------MQ 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6969 TIRQRNWLLWQQHADLDYQLanliNSIEERLSLLSNYQIRYDRISQWLQRLEQRVEKDADVTamtnpeqaaKQLEQQVNS 7048
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQL----TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL---------QNITVRLQD 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7049 ELQLRDKEREWLLSTSRELLTlysepEVRSQVQQQSDSLIDRwQRLKYLAKQKATKIGELkMTLLRLEERIALIRAWLFE 7128
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLR-----KLQPEQDLQDVRLHLQ-QCSQELALKLTALHALQ-LTLTQERVREHALSIRVLP 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7129 VESqLDKPLNFESYTPNVIEA---KLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDADSWRT--QVNTSGLAASAQNLEQ 7203
Cdd:TIGR00618 672 KEL-LASRQLALQKMQSEKEQltyWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSdlAAREDALNQSLKELMH 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7204 RWKNVCSQSAERKARiltiwNLLQQLIKLT--AEHKNWLGKQESQIAGFERDQKShSKHKLEERQMELRAKLEELESQSV 7281
Cdd:TIGR00618 751 QARTVLKARTEAHFN-----NNEEVTAALQtgAELSHLAAEIQFFNRLREEDTHL-LKTLEAEIGQEIPSDEDILNLQCE 824
|
730
....*....|....
gi 442626145 7282 NLRQ-LEQIYAKLA 7294
Cdd:TIGR00618 825 TLVQeEEQFLSRLE 838
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6531-7094 |
1.02e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6531 LELRDIVAKIAADVGLDAS-ALMQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREA 6609
Cdd:COG1196 222 LKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6610 pqnpKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARS 6689
Cdd:COG1196 302 ----QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6690 QnsSEALRLWRQYLQHVQsflscaipEDYSSLREQQQLCAIHQNLLISQQSVLSEtplESELSEQYKALTNLHNETLSRI 6769
Cdd:COG1196 378 E--EELEELAEELLEALR--------AAAELAAQLEELEEAEEALLERLERLEEE---LEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6770 MQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHLKRvphLKHRLDAMIQQLDQGEQQSKALQ--EQQQE 6847
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA---RLLLLLEAEADYEGFLEGVKAALllAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6848 LARHCDDALATAMRMEQAsigqrisnLRAALKTWQgfLQRVTQLSESYEQRVNQLQQEFGAAQKLLDANSESLPTQPAAI 6927
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAA--------LEAALAAAL--QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6928 EQLLGSLRAQRVQLGAQVSALESLTVTQEELKEcispHDMKTIRQRNWLLWQQHADLDY--------------QLANLIN 6993
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLG----RTLVAARLEAALRRAVTLAGRLrevtlegeggsaggSLTGGSR 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6994 SIEERLSLLSNYQIRYDRISQWLQRLEQRVEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWLLSTSRELLTLYS- 7072
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEl 747
|
570 580 590
....*....|....*....|....*....|..
gi 442626145 7073 ----------EPEVRSQVQQQSDSLIDRWQRL 7094
Cdd:COG1196 748 leeealeelpEPPDLEELERELERLEREIEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2095-2908 |
1.45e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2095 YNAYHQSLQDVEKWLLQISFQlmahnslfisnreqtqEQIKQHEALLVEIQKYQTNLDDLnakgQAQIKRYESSTPAIRP 2174
Cdd:TIGR02168 215 YKELKAELRELELALLVLRLE----------------ELREELEELQEELKEAEEELEEL----TAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2175 TVeSQLKNIQDSYNSLLQTSVQIKNRLLESLAKFQEYEDTLdsimrnletyepiiQTELDAPATSLELAQNQLRCAQEMQ 2254
Cdd:TIGR02168 275 EV-SELEEEIEELQKELYALANEISRLEQQKQILRERLANL--------------ERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2255 NKLNNEKSRLAAAVQACEAATASISRPSSPLETAMQAIPERELIVRAKLEDLLDQVQSHLGGLTASVSELEQQQKQRAEL 2334
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2335 QDWVKKQQSSVSDWMMRPCKLRPEAAQQELvsmNDLLNSIGDKRSQLMLemtgslgdedtdLDDNIDKLESELMDAIAKK 2414
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEELEEEL---EELQEELERLEEALEE------------LREELEEAEQALDAAEREL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2415 QAGQNVIDGYRQGMADVQNWFDTLIKRMDVLDRGSGLncAQKMAAINEIKNEYELQghpkIQELKGKAAQVAEVISN--- 2491
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGI--LGVLSELISVDEGYEAA----IEAALGGRLQAVVVENLnaa 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2492 LDGQQVEEQMKSLDRRFADLGKRIDRKSQLLDV-TNKGVEGAKGEID-------QLQNWVK------------QQIEELQ 2551
Cdd:TIGR02168 559 KKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDReILKNIEGFLGVAKdlvkfdpKLRKALSyllggvlvvddlDNALELA 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2552 APKPLGY----------------TPKDAEA------RQQKIKSLMKDAEAKQSLADVLEKRVANMQQELEPVEySQLESA 2609
Cdd:TIGR02168 639 KKLRPGYrivtldgdlvrpggviTGGSAKTnssileRRREIEELEEKIEELEEKIAELEKALAELRKELEELE-EELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2610 LRNLNTENRNLSGvLKAELDRALEASKARKSLENDLDKARQWLKTKISEVRKLPVYHPLTSAEIEKKIQE-NRKYDDDAK 2688
Cdd:TIGR02168 718 RKELEELSRQISA-LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEElEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2689 QF--NDSVLTDVQRQAANIMKDCDDAdKAALQQILDEIAADYQTLKDESskrgKSLDDLLQGRKAFEDSMKNMGDWLNEM 2766
Cdd:TIGR02168 797 ELkaLREALDELRAELTLLNEEAANL-RERLESLERRIAATERRLEDLE----EQIEELSEDIESLAAEIEELEELIEEL 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2767 ETATEGELRttslpVLEEQLAHYKKLLSDAENKGGLINDVSEQGKSIlptlsNADKLKLNDDIKNMKDRYGRIKNTID-- 2844
Cdd:TIGR02168 872 ESELEALLN-----ERASLEEALALLRSELEELSEELRELESKRSEL-----RRELEELREKLAQLELRLEGLEVRIDnl 941
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2845 -DRVNA-----LGDHIKKYKDAKSRLAECSQFLGNIQQKLRELNRPIGSRIEDVQDLLGAYEGILKELKD 2908
Cdd:TIGR02168 942 qERLSEeysltLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKED 1011
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
268-379 |
1.87e-06 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 50.77 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 268 EQERVQKKTFTNWINSyllKRVPPlRIDDLINDLRDGTKLIALLEVLsgeRLPVEKGRVLRRPH--------FLSNANTA 339
Cdd:cd21331 18 EGETREERTFRNWMNS---LGVNP-HVNHLYGDLQDALVILQLYEKI---KVPVDWNKVNKPPYpklganmkKLENCNYA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 442626145 340 LQFLASK-RIKLVNINPADLVDGRPPVVLGLIWTIILYFQL 379
Cdd:cd21331 91 VELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
268-374 |
2.56e-06 |
|
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: 50.14 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 268 EQERVQkktFTNWINSYLL------KRVP-PLRIDDLINDLRDGTKLIALL----------EVLSgerLPVEKGRVLRRP 330
Cdd:cd21294 5 EDERRE---FTKHINAVLAgdpdvgSRLPfPTDTFQLFDECKDGLVLSKLIndsvpdtideRVLN---KPPRKNKPLNNF 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 442626145 331 HFLSNANTALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21294 79 QMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3270-3480 |
4.84e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 51.29 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3270 RWREYQQSIDRVKATIERTKFV---DEPVQNLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIrQADARNRQLIEQ 3346
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELlssTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3347 DNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFeNSLHAWEKALGRLEDKFRNVDPTvrsrRHLEDTKNAIQELREESNQ 3426
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALASEDLG----KDLESVEELLKKHKELEEE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442626145 3427 LKSSHKEIEALSKSILTFLGEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQ 3480
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKK 208
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
6395-6960 |
5.86e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6395 LIRVHGQVDYERLRKATERLEGLAGDLHNREQLIDEL----------KGAAKPLIESCD--VQIVEQIESAV---QEAVV 6459
Cdd:PRK02224 189 LDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYeeqreqaretRDEADEVLEEHEerREELETLEAEIedlRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6460 AWNDTSENL-QQLRTRYQRAVELWDKYRNASA------AVKNSIDQQMDAV-KSLEQPLDALQHAKVCQDNLTTQNDRIL 6531
Cdd:PRK02224 269 ETEREREELaEEVRDLRERLEELEEERDDLLAeaglddADAEAVEARREELeDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6532 ELRDIVAKIAADvgldasalMQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQqDISREAPQ 6611
Cdd:PRK02224 349 EDADDLEERAEE--------LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE-DFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6612 NPKESEEQLAALRAHLQTLARTEEQLRQLKER------HQNSEVAPSVASSDDDGilEVLALWQKIFQDTFQEYHRLSTR 6685
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEALLEAgkcpecGQPVEGSPHVETIEEDR--ERVEELEAELEDLEEEVEEVEER 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6686 LARSQNSSEALRlwrqylqhvqsflscaipeDYSSLREQ----QQLCAIHQNLLISQQSVLSE-----TPLESELSEQYK 6756
Cdd:PRK02224 498 LERAEDLVEAED-------------------RIERLEERredlEELIAERRETIEEKRERAEElreraAELEAEAEEKRE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6757 ALTNLHNETlSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQlryihlkrvpHLKHRLDAMIQQLDQGEQ 6836
Cdd:PRK02224 559 AAAEAEEEA-EEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIE----------RLREKREALAELNDERRE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6837 QSKALQEQQQELARHCDDAlatamrmeqasigqRISNLRAALKTWQGFLQRVT-QLSESYEQRvNQLQQEFGAAQKLLDA 6915
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEA--------------RIEEAREDKERAEEYLEQVEeKLDELREER-DDLQAEIGAVENELEE 692
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 442626145 6916 nseslptqpaaieqlLGSLRAQRVQLGAQVSALESLTVTQEELKE 6960
Cdd:PRK02224 693 ---------------LEELRERREALENRVEALEALYDEAEELES 722
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7005-7218 |
6.46e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 50.91 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7005 YQIRYDRISQWLQRLEQRVEKDADVTAMTNPEQAAKQLeQQVNSELQLRDKEREWLLSTSRELLTLYSEPEvrSQVQQQS 7084
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKH-EALEAELAAHEERVEALNELGEQLIEEGHPDA--EEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7085 DSLIDRWQRLKYLAKQKATKIGELKMTLLRLEErIALIRAWLFEVESQLDKPLNFESYTPnvIEAKLKEHEQIQRSIEHH 7164
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLES--VEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442626145 7165 SSNVGEVLNLVEMLLNDAdswrTQVNTSGLAASAQNLEQRWKNVCSQSAERKAR 7218
Cdd:cd00176 159 EPRLKSLNELAEELLEEG----HPDADEEIEEKLEELNERWEELLELAEERQKK 208
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7112-7321 |
6.64e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 50.91 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7112 LLRLEERIALIRAWLFEVESQLDKPLNfeSYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDAdswrtQVNT 7191
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDY--GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-----HPDA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7192 SGLAASAQNLEQRWKNVCSQSAERKARILTIWNLLQQLIKLTAEhKNWLGKQESQIAgfeRDQKSHSKHKLEERQMELRA 7271
Cdd:cd00176 75 EEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-EQWLEEKEAALA---SEDLGKDLESVEELLKKHKE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442626145 7272 KLEELESQSVNLRQLEQIYAKLAMSAgvEPENIQKLTLPTKVMVSMWRQL 7321
Cdd:cd00176 151 LEEELEAHEPRLKSLNELAEELLEEG--HPDADEEIEEKLEELNERWEEL 198
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
3028-3643 |
7.36e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3028 EQLQSLKNQLQNLRKAVESQRQKHQLQLES------HKKMAAELSEILDWLHSHEGAAKSRPLLDRDpesvERELQKHQS 3101
Cdd:TIGR00618 270 EELRAQEAVLEETQERINRARKAAPLAAHIkavtqiEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ----QSSIEEQRR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3102 LSQDIESYLNKFNKINDgvkteigMPSSLLEMLSEgrslvaslPHELEEREKYLKNNRDSRLEYMQLVAKFNDwvheael 3181
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAHE-------VATSIREISCQ--------QHTLTQHIHTLQQQKTTLTQKLQSLCKELD------- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3182 RLQNSQHGIDYEHLVQ-DLDEHKIFFGNEAPIRNLVHKQIQEAADKIWSSLN------NYEQSELSAELAQFQTKLTNTL 3254
Cdd:TIGR00618 404 ILQREQATIDTRTSAFrDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKlekihlQESAQSLKEREQQLQTKEQIHL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3255 ANAKTQQSE---LEKEAERWREYQQSIDRVKATIERTKFVDEPVQNLAGLHFNIQKLSHAIGNVQSQnsdLTLVNQQAQS 3331
Cdd:TIGR00618 484 QETRKKAVVlarLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQ---LTSERKQRAS 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3332 LIRQAdarnrQLIEQDNAGLNRSWQDLVRSLeqrrDNLQQLAEhwdgfenSLHAWEKALGRLEDKFRnvdptVRSRRHLE 3411
Cdd:TIGR00618 561 LKEQM-----QEIQQSFSILTQCDNRSKEDI----PNLQNITV-------RLQDLTEKLSEAEDMLA-----CEQHALLR 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3412 DTKNAIQELR---EESNQLKSSHKEIEALSKSILTFLGEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEI 3488
Cdd:TIGR00618 620 KLQPEQDLQDvrlHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3489 EQvfrrisqlqdKLNALHEQLQSVHVYDEHIAQTEQLLITLNSQVQQ------------AAEESKLLVAQTTAHYQAKQn 3556
Cdd:TIGR00618 700 AQ----------CQTLLRELETHIEEYDREFNEIENASSSLGSDLAAredalnqslkelMHQARTVLKARTEAHFNNNE- 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3557 QLPSDIaQEFTALELLAERVQVTMETKEKDFKRAKTVRTEYVDGVDE-VQRWLLQAEVQVQERSLTPTQMKELLQRInHE 3635
Cdd:TIGR00618 769 EVTAAL-QTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdEDILNLQCETLVQEEEQFLSRLEEKSATL-GE 846
|
....*...
gi 442626145 3636 ITAIYERF 3643
Cdd:TIGR00618 847 ITHQLLKY 854
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
6747-7422 |
1.13e-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: 52.66 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6747 LESELSEQYKALTNLHnETLSRIMQRNGELERRVSgWNAYRQQLAALLDWLRQREAE----RNALQLRYIHLKRVPHLKH 6822
Cdd:TIGR00618 224 LEKELKHLREALQQTQ-QSHAYLTQKREAQEEQLK-KQQLLKQLRARIEELRAQEAVleetQERINRARKAAPLAAHIKA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6823 rldamIQQLDQGEQQSKA-LQEQQQELARhcddalATAMRMEQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQ 6901
Cdd:TIGR00618 302 -----VTQIEQQAQRIHTeLQSKMRSRAK------LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6902 LQQEFGAAQKLLdanseSLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELK-ECISPHDMKTIRQRNWLLWQQ 6980
Cdd:TIGR00618 371 SCQQHTLTQHIH-----TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQgQLAHAKKQQELQQRYAELCAA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6981 HADLDYQLANLINSIEERLSllsnyqirydrisqwlQRLEQRVEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWL 7060
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESA----------------QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGS 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7061 LSTSRELLTLYSEPEVRSQVQQQsdsLIDRWQRLKYLAKQKATKIGELKMTLLRLEERIALIRAWLF-------EVESQL 7133
Cdd:TIGR00618 510 CIHPNPARQDIDNPGPLTRRMQR---GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSiltqcdnRSKEDI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7134 DKPLNFESYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDAD-SWRTQVNTSGLAASAQNLEQ-----RWKN 7207
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQcSQELALKLTALHALQLTLTQervreHALS 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7208 VCSQSAERKARILTIWNLLQQLIKLTAEHKNWLGKQESQIAGFERDQKSHSKHkLEERQMELRAKLEELESQSVNLRQLE 7287
Cdd:TIGR00618 667 IRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE-FNEIENASSSLGSDLAAREDALNQSL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7288 QIYAKLAMSAGVEPENIQKLTLPTKVMVSMwrqltprchalLDAIDKDAKLMREFNNAQLEATNSLNAIQKAL--EQLPS 7365
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFNNNEEVTAALQ-----------TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEigQEIPS 814
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626145 7366 AE-----NQQTSKAEPKAVLQRLESLEKKLQDAQQHVQQADNLAQEAKTRTKQQPQLKQLLE 7422
Cdd:TIGR00618 815 DEdilnlQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3596-3799 |
1.17e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 50.14 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3596 EYVDGVDEVQRWLLQAEVQVQERSL--TPTQMKELLQR---INHEITAIYERFTLVKTNGQLIIEncRNSEEKTLVQTTI 3670
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYgdDLESVEALLKKheaLEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3671 DQLAASLAQVRGWLDEKKQAVGDSLDAWtRFMNLYQIVMSWASEKRNFIDQTIELRTLPEARNKLN---DYVTSVKSIKP 3747
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKkhkELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442626145 3748 IVKHLSEMDKELEHIGQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEA 3799
Cdd:cd00176 161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3387-4125 |
1.18e-05 |
|
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: 52.76 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3387 EKALGRLEDKFRNVDptvRSRRHLEDTKNAIQELREESNQ------LKSSHKEIEA--LSKSIltflgEVHKPSAEAIQA 3458
Cdd:TIGR02169 173 EKALEELEEVEENIE---RLDLIIDEKRQQLERLRREREKaeryqaLLKEKREYEGyeLLKEK-----EALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3459 KVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQL-QDKLNALHEQLQSVHVydeHIAQTEQLLITLNSQVQQAA 3537
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEA---EIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3538 EESKLLVAQTTAhYQAKQNQLPSDIAQEFTALELLAERVQVTMETKEKDFKRAKTVRTEY---VDGVDEVQRWLLQAEVQ 3614
Cdd:TIGR02169 322 ERLAKLEAEIDK-LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFaetRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3615 VQERSLTPTQMKELLQRINHEITAIYERFTLVKtngqliiencrnsEEKTLVQTTIDQLAASLAQVRGWLDEKKQAVGDS 3694
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIE-------------AKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3695 LDAWTRFMNLYQIVMSWASEKRnfidqtielRTLPEARNKLNDYVTSVKSIKPIVKHLSEMDKELehIGQVTTVGDLKDK 3774
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQ---------RELAEAEAQARASEERVRGGRAVEEVLKASIQGV--HGTVAQLGSVGER 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3775 LQEAEDAKIS--VEAVLLERNSLLQEACEEWDQCE---------RKIKDIRSWHEKTKQG--------LDSSQQQKKP-- 3833
Cdd:TIGR02169 537 YATAIEVAAGnrLNNVVVEDDAVAKEAIELLKRRKagratflplNKMRDERRDLSILSEDgvigfavdLVEFDPKYEPaf 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3834 ---LRDQLGFCEKTLA-DINVQKTKLRLSIEKLEVH------FRNGMGGDPRLSENVDDLVRVLDGLGELVKAKSqSLEQ 3903
Cdd:TIGR02169 617 kyvFGDTLVVEDIEAArRLMGKYRMVTLEGELFEKSgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELS-SLQS 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3904 TLAQIdvyQQQMQSLRQRIIQEEQQLRLVMAPTYLPHDRERALAEQQDLITQELDELLQSLSSVEDGIANMNQ--SSLDG 3981
Cdd:TIGR02169 696 ELRRI---ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAriEELEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3982 MLHGLKLIQSNLEVHERDAI--ELKNQAKKLPTD--------PATERLLNDtVDRIDLLLRRTQQGITMIANAMHGQKK- 4050
Cdd:TIGR02169 773 DLHKLEEALNDLEARLSHSRipEIQAELSKLEEEvsriearlREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKs 851
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626145 4051 RQQEIDEYQQHLLELEQWIIEVSAELASFEptsDSSTDeqvLKSQVERSQQLLRTLKDRQQSMEDLVEQTRQLQS 4125
Cdd:TIGR02169 852 IEKEIENLNGKKEELEEELEELEAALRDLE---SRLGD---LKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3064-3267 |
1.28e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 50.14 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3064 ELSEILDWLHSHEGAAKSrPLLDRDPESVERELQKHQSLSQDIESYLNKFNKINDG----VKTEIGMPSSLLEMLSEGRS 3139
Cdd:cd00176 8 DADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELgeqlIEEGHPDAEEIQERLEELNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3140 LVASLPHELEEREKYLKNNRDsRLEYMQLVAKFNDWVHEAELRLQNSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLVhKQ 3219
Cdd:cd00176 87 RWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRL-KS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 442626145 3220 IQEAADKIWSSLNNYEQSELSAELAQFQTKLTNTLANAKTQQSELEKE 3267
Cdd:cd00176 165 LNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
6496-6960 |
1.35e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6496 IDQQMDAVKSLEQPLDALQHAkvcQDNLTTQNDRILELRDIVAKIAADVGLDASALMQGELDALGQRLAECKDAITTLAN 6575
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAEL---QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6576 VAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVAS 6655
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6656 SDDDGILEVLALWQKIfQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLCAihqnll 6735
Cdd:COG4717 230 EQLENELEAAALEERL-KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK------ 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6736 isqqsvlsetplESELSEQYKALTNLHNETLSRIMQRNG-ELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHL 6814
Cdd:COG4717 303 ------------EAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6815 KRVPHLKH-------RLDAMIQQLDQGEQQSKALQEQQQELARHCDDALATAMRMEQASIGQRISNLRAALktwqgflqr 6887
Cdd:COG4717 371 EIAALLAEagvedeeELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEEL--------- 441
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626145 6888 vtqlsESYEQRVNQLQQEFGAAQKLLDA--NSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELKE 6960
Cdd:COG4717 442 -----EELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3005-3975 |
1.61e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3005 ASANDKGQKIASEGNAADKNSITEQLQSLKNQLQNLRKAV-ESQRQKHQLQLESHKKmAAELSEILDWLHShegaaksrp 3083
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALLVLRLEELREELEELQEELkEAEEELEELTAELQEL-EEKLEELRLEVSE--------- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3084 lLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEIGMPSSLLEMLSEGRSLVASLPHELEEREKYLKNNRDSRL 3163
Cdd:TIGR02168 279 -LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3164 EymqLVAKFNDWVHEAELRLQNSQhgidyehlvqdldehkiffgneapirnlvhKQIQEAADKIwsslnnyeqselsAEL 3243
Cdd:TIGR02168 358 A---ELEELEAELEELESRLEELE------------------------------EQLETLRSKV-------------AQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3244 AQFQTKLTNTLANAKTQQSELEKEAERWREYQQSIDRVKATiertkfvdepvQNLAGLHFNIQKLSHAIGNVQSQNSDLt 3323
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE-----------AELKELQAELEELEEELEELQEELERL- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3324 lvnQQAQSLIRQADARNRQLIEQDNAGLNRSwQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFrNVDpt 3403
Cdd:TIGR02168 460 ---EEALEELREELEEAEQALDAAERELAQL-QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI-SVD-- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3404 vrsrrhlEDTKNAIQELREESNQ------LKSSHKEIEALSKSIL---TFLgEVHKPSAEAIQAKVDKLVEQQaklndtl 3474
Cdd:TIGR02168 533 -------EGYEAAIEAALGGRLQavvvenLNAAKKAIAFLKQNELgrvTFL-PLDSIKGTEIQGNDREILKNI------- 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3475 rDKEQQVSKDLEEIEqvfrriSQLQDKLNALheqLQSVHVYDEhIAQTEQLLITLNSQVQQAAEESKLL---------VA 3545
Cdd:TIGR02168 598 -EGFLGVAKDLVKFD------PKLRKALSYL---LGGVLVVDD-LDNALELAKKLRPGYRIVTLDGDLVrpggvitggSA 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3546 QTTAHYQAKQNQLpSDIAQEFTALELLAERVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQM 3625
Cdd:TIGR02168 667 KTNSSILERRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3626 KELLQRINHEITAIYERFTLVKTN-GQLIIENCRNSEEKTLVQTTIDQLAASLAQVRGWLDEKKQAVGDSLDAWTRFMNL 3704
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3705 YQivmswaSEKRNFIDQTIELRTLpearnklndyvtsVKSIKPIVKHLSEMDKELEHigQVTTVGDLKDKLQEAEDAKIS 3784
Cdd:TIGR02168 826 LE------SLERRIAATERRLEDL-------------EEQIEELSEDIESLAAEIEE--LEELIEELESELEALLNERAS 884
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3785 VEAVLLERNSLLQEACEEWDQCERKIKDirswhektkqgldssqqqkkpLRDQLGFCEKTLADINVQKTKLRLSIEKLEv 3864
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSE---------------------LRRELEELREKLAQLELRLEGLEVRIDNLQ- 942
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3865 hfrngmggdPRLSENVDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRlvmaptylphdrer 3944
Cdd:TIGR02168 943 ---------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELK-------------- 999
|
970 980 990
....*....|....*....|....*....|.
gi 442626145 3945 alaEQQDLITQELDELLQSLSSVEDGIANMN 3975
Cdd:TIGR02168 1000 ---ERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2124-2836 |
1.75e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2124 ISNREQTQEQ--IKQHEALLVEIQKYQTNLDDLNAKGQAQIKRYESSTPAIRpTVESQLKNIqdsyNSLLQTSVQIKNRL 2201
Cdd:TIGR04523 27 IANKQDTEEKqlEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIK-ILEQQIKDL----NDKLKKNKDKINKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2202 LESLAKFQEYEDTLDSIMRNLETYEPIIQTELDAPATSLELAQNQLRCAQEMQNKLNNEKSRLAAAVQACEAATASISRP 2281
Cdd:TIGR04523 102 NSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2282 SSPLETAMQAIPERELIVRAKLEDLLDQVQSHlGGLTASVSELEQQQKQraeLQDWVKKQQSSVSDwmmrpCKLRPEAAQ 2361
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSLESQISELKKQNNQ---LKDNIEKKQQEINE-----KTTEISNTQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2362 QELVSMNDLLNSIGD--KRSQLMLEMTGSLGDEdtdLDDNIDKLESELMDaiAKKQAGQNVIDGYRQGMADVQNWFDTLI 2439
Cdd:TIGR04523 253 TQLNQLKDEQNKIKKqlSEKQKELEQNNKKIKE---LEKQLNQLKSEISD--LNNQKEQDWNKELKSELKNQEKKLEEIQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2440 KRMDVLDRG-SGLNcaQKMAAINEIKNEYELQGHPKIQELKGKAAQVAEVISnlDGQQVEEQMKSLDRRFADLGKRI--- 2515
Cdd:TIGR04523 328 NQISQNNKIiSQLN--EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK--ENQSYKQEIKNLESQINDLESKIqnq 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2516 DRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEELQAP-KPLgyTPKDAeARQQKIKSLMKDAEAKQSLADVLEKRVANM 2594
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEiKDL--TNQDS-VKELIIKNLDNTRESLETQLKVLSRSINKI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2595 QQELEPV--EYSQLESALRNLNTENRNLSGVLKAELDRALEASKARKSLENDLDKARQWLKTKISEVRKLPvyHPLTSAE 2672
Cdd:TIGR04523 481 KQNLEQKqkELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD--FELKKEN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2673 IEKKIQENRKYDDDAKQFNDSvLTDVQRQAANIMKDCDDADKAALQQI-------------LDEIAADYQTLKDESSKRG 2739
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKS-LKKKQEEKQELIDQKEKEKKDLIKEIeekekkisslekeLEKAKKENEKLSSIIKNIK 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2740 KSLDDLLQGRKAFEDSMKNMGDWLNEMETATE------GELRTTSLPVLEEQLAHYKKLLSD--AENKGGLINDVSEQGK 2811
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKesktkiDDIIELMKDWLKELSLHYKKYITRmiRIKDLPKLEEKYKEIE 717
|
730 740
....*....|....*....|....*
gi 442626145 2812 SILPTLSNADKlKLNDDIKNMKDRY 2836
Cdd:TIGR04523 718 KELKKLDEFSK-ELENIIKNFNKKF 741
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1065-1263 |
1.90e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 49.75 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1065 KEIHQWLSEAEQLLGTHNLSGGRDAINEQLHKHKTYfsrtvyYRSMLESKNKV--FQNLLKAVSSDDKIDTAPASQQMQQ 1142
Cdd:cd00176 10 DELEAWLSEKEELLSSTDYGDDLESVEALLKKHEAL------EAELAAHEERVeaLNELGEQLIEEGHPDAEEIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1143 LNERFNYVIQNAQQWEQRLDSAAGGWSNFKDnERVVSEWLTQAESMLV-EKHIESKTTIETQKYFFEQV------NDRWM 1215
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALAsEDLGKDLESVEELLKKHKELeeeleaHEPRL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 442626145 1216 NDLVQSAQQLLTTLPAQEQPAVVHSVEQLQSRWKNVLSQAPLHLLKLE 1263
Cdd:cd00176 163 KSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
273-374 |
2.20e-05 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 48.04 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 273 QKKTFTNWINSYL-----LKRVPPLR--IDDLINDLRDGTKLIALLEVLS----GERLPVEKGRVLRRPHflSNANTALQ 341
Cdd:cd21292 25 EKVAFVNWINKNLgddpdCKHLLPMDpnTDDLFEKVKDGILLCKMINLSVpdtiDERAINKKKLTVFTIH--ENLTLALN 102
|
90 100 110
....*....|....*....|....*....|...
gi 442626145 342 FLASKRIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21292 103 SASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3416-3642 |
2.63e-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: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3416 AIQELREESNQLKSSHKEIEALSKSIltflgEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRI 3495
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKEL-----AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3496 SQLQDKLNALHEQLQSVHVYDEHIAQTEQLLITLNSQ-VQQAAEESKLLvaqttAHYQAKQNQLPSDIAQEFTALELLAE 3574
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEdFLDAVRRLQYL-----KYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626145 3575 RVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELLQRINHEITAIYER 3642
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2474-2834 |
4.33e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2474 KIQELKgKAAQV--AEVISNLDGQQVEEQMKSLDRRFADLGKRIDRKsQLLDVTNKGVEGAKGEIDQLQnwvKQQIEELQ 2551
Cdd:PTZ00121 1547 KADELK-KAEELkkAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA-RIEEVMKLYEEEKKMKAEEAK---KAEEAKIK 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2552 APKPlgytpKDAEARQQKIKSLMKDAEAKQSLADVLEK-----RVANMQQELEPVEYSQLESALRNLNTENRNLSGVLKA 2626
Cdd:PTZ00121 1622 AEEL-----KKAEEEKKKVEQLKKKEAEEKKKAEELKKaeeenKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2627 ELDRALEASKARKSLENDLDKARQWLKTKisEVRKLPVYHPLTSAEIEKKIQENRKYDDDAKQFNDSVLTDVQRQAANIM 2706
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAE--EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2707 KDcddaDKAALQQILDEIAADYQTLKDESSKRGKSLDDLLQgrkafEDSMKN--MGDWLNEMETATEGELRTTSLPVLEE 2784
Cdd:PTZ00121 1775 KE----KEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANII-----EGGKEGnlVINDSKEMEDSAIKEVADSKNMQLEE 1845
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 442626145 2785 QLAHYKkllsdaeNKGGLINDVSEQGKSilPTLSNADKLKLNDDIKNMKD 2834
Cdd:PTZ00121 1846 ADAFEK-------HKFNKNNENGEDGNK--EADFNKEKDLKEDDEEEIEE 1886
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
3023-3689 |
4.94e-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: 50.49 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3023 KNSITEQLQSLKNQLQNLRKAVESQRQKHQ-LQLESHK---KMAAELSEILDWLHSH-----------EGAAKSRPLLDR 3087
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKAIQeLQFENEKvslKLEEEIQENKDLIKENnatrhlcnllkETCARSAEKTKK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3088 DPESVERELQKHQSLSQDIESYLNKFNKIN-DGVKTEIGMPSSLLEMLSEGRSLVASLPHELEEREKYL---------KN 3157
Cdd:pfam05483 174 YEYEREETRQVYMDLNNNIEKMILAFEELRvQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVsllliqiteKE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3158 NRDSRLEYM--QLVAKFNDWVHEAELRLQNSQHGIDYE-HLVQDLDEHKIFFGNEAPIRNLVHKQIQEAADKIWsSLNNY 3234
Cdd:pfam05483 254 NKMKDLTFLleESRDKANQLEEKTKLQDENLKELIEKKdHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIC-QLTEE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3235 EQSELSaELAQFQTKLTNTLANAKTQQSELEkeaERWREYQQsidRVKATIERTKFVDEPVQNLAGlhfNIQKLSHAIGN 3314
Cdd:pfam05483 333 KEAQME-ELNKAKAAHSFVVTEFEATTCSLE---ELLRTEQQ---RLEKNEDQLKIITMELQKKSS---ELEEMTKFKNN 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3315 VQSQNSDLTLVNQQAQSLIRQadarNRQlIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLE 3394
Cdd:pfam05483 403 KEVELEELKKILAEDEKLLDE----KKQ-FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3395 -----DKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKSSHKEI-------EALSKSILTfLGEVHKPSAEAIQAKVDK 3462
Cdd:pfam05483 478 telekEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIinckkqeERMLKQIEN-LEEKEMNLRDELESVREE 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3463 LVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVHVYDEHIAQTEQLLitlnsqVQQAAEESKL 3542
Cdd:pfam05483 557 FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL------KKKGSAENKQ 630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3543 LVAqttahYQAKQNQLPSDIAQEFTALELLAERVQVTMETKE-------KDFKRAKTVrteyvdgVDEVQRWLLQAEVQV 3615
Cdd:pfam05483 631 LNA-----YEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKiseekllEEVEKAKAI-------ADEAVKLQKEIDKRC 698
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626145 3616 QERSltpTQMKELLQRINHEITAIYErftlvKTNGQLIIENCRNSEEKTL---VQTTIDQLAASLAQVRGWLDEKKQ 3689
Cdd:pfam05483 699 QHKI---AEMVALMEKHKHQYDKIIE-----ERDSELGLYKNKEQEQSSAkaaLEIELSNIKAELLSLKKQLEIEKE 767
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
6819-7420 |
5.44e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6819 HLKHRLDAMIQQLDQGEQQSKALQEQQQELARhcddalatamrmeqasIGQRISNLRAALKTWQGFLQRVTQLSESYEQr 6898
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEE----------------VLREINEISSELPELREELEKLEKEVKELEE- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6899 vnqLQQEFGAAQKLLdansESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELKECISPHdMKTIRQRNWLLw 6978
Cdd:PRK03918 236 ---LKEEIEELEKEL----ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY-IKLSEFYEEYL- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6979 QQHADLDYQLANL---INSIEERLSLLSNYQIRYDRISQWLQRLEQRVEKdadvtamtnPEQAAKQLEQQVNSELQLRDK 7055
Cdd:PRK03918 307 DELREIEKRLSRLeeeINGIEERIKELEEKEERLEELKKKLKELEKRLEE---------LEERHELYEEAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7056 EREWLLSTSRELLTLYSEPEVR-SQVQQQSDSLIDRWQRLKYLAKQKATKIGELKMT---------LLRLEERIALIRAW 7125
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAkEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrELTEEHRKELLEEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7126 LFEVESqldkplnfesytpnvIEAKLKEHEQIQRSIEhhssnvgEVLNLVEMLLNDADSWRTQVNtsgLAASAQNLEQRW 7205
Cdd:PRK03918 458 TAELKR---------------IEKELKEIEEKERKLR-------KELRELEKVLKKESELIKLKE---LAEQLKELEEKL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7206 KNVCSQSAERKARILTiwNLLQQLIKLTAEHKNwLGKQESQIAGFERDQKS--HSKHKLEERQMELRAKLEELESQSVN- 7282
Cdd:PRK03918 513 KKYNLEELEKKAEEYE--KLKEKLIKLKGEIKS-LKKELEKLEELKKKLAEleKKLDELEEELAELLKELEELGFESVEe 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7283 ----LRQLEQIYAKLAMSAGVEPEniqkltlptkvmvsmWRQLTPRCHALLDAIDKDAKLMREFNNAQLEATNSLNAIQK 7358
Cdd:PRK03918 590 leerLKELEPFYNEYLELKDAEKE---------------LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626145 7359 AL--EQLPSAENQQTSKA-EPKAVLQRLESLEKKLQDAQqhvQQADNLAQEAKTRTKQQPQLKQL 7420
Cdd:PRK03918 655 KYseEEYEELREEYLELSrELAGLRAELEELEKRREEIK---KTLEKLKEELEEREKAKKELEKL 716
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3330-4123 |
5.82e-05 |
|
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: 50.45 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3330 QSLIRQADARNRQL--IEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGF-ENSLHAWEKALGRLEDKFRNVDPTVR- 3405
Cdd:TIGR02169 233 EALERQKEAIERQLasLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAe 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3406 SRRHLEDTKNAIQELREESNQLKSshkEIEALSKSILTFLGEVHKPSAE--AIQAKVDKLV---EQQAKLNDTLRDKEQQ 3480
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLA---EIEELEREIEEERKRRDKLTEEyaELKEELEDLRaelEEVDKEFAETRDELKD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3481 VSKDLE----EIEQVFRRISQLQDKLNALHEQLQSVH----VYDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAhYQ 3552
Cdd:TIGR02169 390 YREKLEklkrEINELKRELDRLQEELQRLSEELADLNaaiaGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK-YE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3553 AKQNQLPSDIAQ---EFTALELLAERVQVT---METKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQ------------ 3614
Cdd:TIGR02169 469 QELYDLKEEYDRvekELSKLQRELAEAEAQaraSEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERyataievaagnr 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3615 ----VQERSLTPTQMKELLQRINheitaiYERFTLVKTNG-QLIIENCRNSEEKTLVQTTID------QLAASLAQVRGw 3683
Cdd:TIGR02169 549 lnnvVVEDDAVAKEAIELLKRRK------AGRATFLPLNKmRDERRDLSILSEDGVIGFAVDlvefdpKYEPAFKYVFG- 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3684 ldekKQAVGDSLDAWTRFMNLYQIVM--------SWA------SEKRNFIDQTIELRTLPEARNKLNDyvtsvksikpIV 3749
Cdd:TIGR02169 622 ----DTLVVEDIEAARRLMGKYRMVTlegelfekSGAmtggsrAPRGGILFSRSEPAELQRLRERLEG----------LK 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3750 KHLSEMDKELEHIGQvttvgDLKDKLQEAEDAKISVEAVLLERNSLLQEAceewDQCERKIKDIRSWHEKTKQGLDSSQQ 3829
Cdd:TIGR02169 688 RELSSLQSELRRIEN-----RLDELSQELSDASRKIGEIEKEIEQLEQEE----EKLKERLEELEEDLSSLEQEIENVKS 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3830 QKKPLRDQLGFCEKTLAdinvqktKLRLSIEKLEVHFRNgmggdprlsENVDDLVRVLDGLGELVKAKSQSLEQTLAQID 3909
Cdd:TIGR02169 759 ELKELEARIEELEEDLH-------KLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSRIEARLREIEQKLN 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3910 VYQQQMQSLRQRIIQEEQQLRLVmaptylpHDRERALAEQQDLITQELDELLQSLSSVEDGIANmnqssLDGMLHGLKLI 3989
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDL-------KEQIKSIEKEIENLNGKKEELEEELEELEAALRD-----LESRLGDLKKE 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3990 QSNLEVHERDAIELKNQAKklptdpATERLLNDTVDRIDLLLRRTQQGITMIANAmhgqKKRQQEIDEYQQHLLELEQWI 4069
Cdd:TIGR02169 891 RDELEAQLRELERKIEELE------AQIEKKRKRLSELKAKLEALEEELSEIEDP----KGEDEEIPEEELSLEDVQAEL 960
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 442626145 4070 IEVSAELASFEPTSDSSTD--EQVLKSQVERSQQlLRTLKDRQQSMEDLVEQTRQL 4123
Cdd:TIGR02169 961 QRVEEEIRALEPVNMLAIQeyEEVLKRLDELKEK-RAKLEEERKAILERIEEYEKK 1015
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3232-3502 |
6.99e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3232 NNYEQSE-LSAELAQfqtkLTNTLANAKTQQSELEKEAERWREYQQSIDRVKAtiertkfVDEPVQNLAGLHFNIQKLSH 3310
Cdd:COG4913 607 DNRAKLAaLEAELAE----LEEELAEAEERLEALEAELDALQERREALQRLAE-------YSWDEIDVASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3311 AIGNVQSQNSDLTLVNQQAQSLIRQADArnrqlIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKAl 3390
Cdd:COG4913 676 ELERLDASSDDLAALEEQLEELEAELEE-----LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA- 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3391 gRLEDKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKsshkeiEALSKSILTFLGEVHKPSAE------------AIQA 3458
Cdd:COG4913 750 -LLEERFAAALGDAVERELRENLEERIDALRARLNRAE------EELERAMRAFNREWPAETADldadleslpeylALLD 822
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 442626145 3459 KV--DKLVEQQAKLNDTLRDKEQQVSKDL-----EEIEQVFRRISQLQDKL 3502
Cdd:COG4913 823 RLeeDGLPEYEERFKELLNENSIEFVADLlsklrRAIREIKERIDPLNDSL 873
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6405-7058 |
7.20e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6405 ERLRKATERLEGLAGDLHNREQLIDELKG---AAKPLIESCDVQIVEQIES--AVQEAVVAWNDTSENLQQLRTRYQRAV 6479
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERlaNLERQLEELEAQLEELESKLDELAEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6480 ELWDKYRNASAAVKNSIDQQMDAVKSLEQplDALQHAKVCQDNLTTQNDRILELRDIVAKIAADVgldasALMQGELDAL 6559
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELE--ELESRLEELEEQLETLRSKVAQLELQIASLNNEI-----ERLEARLERL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6560 GQRLAECKDAITTLANVAETQDKER-----KELDKEVTLAKAYFNNVQ------QDISREAPQNPKESEEQLAALRAHLQ 6628
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLEealeelREELEEAEQALDAAERELAQLQARLD 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6629 TLARTEEQLRQ--------LKERHQNSEVAPSVAS--------------------------SDDDGILEVLAL-WQKIFQ 6673
Cdd:TIGR02168 493 SLERLQENLEGfsegvkalLKNQSGLSGILGVLSElisvdegyeaaieaalggrlqavvveNLNAAKKAIAFLkQNELGR 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6674 DTFQEYHRLSTRLARSQNssealrlwRQYLQHVQSFLSCAIPEDYSSLREQQQLCAIHQNLLISQqSVLSETPLESELSE 6753
Cdd:TIGR02168 573 VTFLPLDSIKGTEIQGND--------REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVD-DLDNALELAKKLRP 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6754 QYK-------------ALTNLHNETLSRIMQRNGELERrvsgwnaYRQQLAALLDWLRQREAERNAL-QLRYIHLKRVPH 6819
Cdd:TIGR02168 644 GYRivtldgdlvrpggVITGGSAKTNSSILERRREIEE-------LEEKIEELEEKIAELEKALAELrKELEELEEELEQ 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6820 LKHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALAtamrmEQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRV 6899
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK-----ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6900 NQLQQEFGAAQKLLDANS-----------------ESLPTQPAAIEQLLGSLRAQRVQLGAQVSAL----ESLTVTQEEL 6958
Cdd:TIGR02168 792 EQLKEELKALREALDELRaeltllneeaanlrerlESLERRIAATERRLEDLEEQIEELSEDIESLaaeiEELEELIEEL 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6959 KECISPH---------DMKTIRQRNWLLWQQHADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQRLEQRVEKDADV 7029
Cdd:TIGR02168 872 ESELEALlnerasleeALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
730 740
....*....|....*....|....*....
gi 442626145 7030 TAMTNPEQAAKQLEQQVNSELQLRDKERE 7058
Cdd:TIGR02168 952 TLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1889-2083 |
8.33e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 47.83 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1889 EFLNYKKEMDAWIEKAQQVLDDCSTDGDAAIIAQKLDTVNSLASRLPEGQHLLALVQDAYSKASNITPEDKqEKLRELMT 1968
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA-EEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1969 KVREDWDALGLAVKQKLSDLKQAQNRWNDFaANKDKLEKWLNETETTLKvAPETKGELSEMKTLLERYKTLSNELKLKGN 2048
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 442626145 2049 ELEQLQSEARDLGTEV--DAVNRLQSRCDKLKNDCSA 2083
Cdd:cd00176 161 RLKSLNELAEELLEEGhpDADEEIEEKLEELNERWEE 197
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
6787-7156 |
8.41e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.91 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6787 RQQLAALLDwLRQREAERNALQ------LRYihLKRVPHLKHRLDAMIQQLDQGEQQskaLQEQQQELARHCDDALATAm 6860
Cdd:PRK11281 42 QAQLDALNK-QKLLEAEDKLVQqdleqtLAL--LDKIDRQKEETEQLKQQLAQAPAK---LRQAQAELEALKDDNDEET- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6861 rmeqasiGQRISNLRaalktwqgflqrVTQLsesyEQRVNQLQQEFGAAQK-LLDANSE--SLPTQPAaieqllgslRAQ 6937
Cdd:PRK11281 115 -------RETLSTLS------------LRQL----ESRLAQTLDQLQNAQNdLAEYNSQlvSLQTQPE---------RAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6938 RVQLGAQVSALE--SLTVTQEELKECISPhdmktiRQRNWLLWQQHAdLDYQLANLINSIEERLSLLSNYQIRYDRISQW 7015
Cdd:PRK11281 163 AALYANSQRLQQirNLLKGGKVGGKALRP------SQRVLLQAEQAL-LNAQNDLQRKSLEGNTQLQDLLQKQRDYLTAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7016 LQRLEQRVEKDADVTAMTNPEQAAKQLEQQVNS--------------ELQLRDKEREWLLSTSRELLTLySEPEVRsqVQ 7081
Cdd:PRK11281 236 IQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQdeaariqanplvaqELEINLQLSQRLLKATEKLNTL-TQQNLR--VK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7082 QQSDSLIDRWQRLKylakqkaTKIGELKMTLL-------------------RLEERIALIRAWLFEVESQLDKPLNFESY 7142
Cdd:PRK11281 313 NWLDRLTQSERNIK-------EQISVLKGSLLlsrilyqqqqalpsadlieGLADRIADLRLEQFEINQQRDALFQPDAY 385
|
410
....*....|....
gi 442626145 7143 tpnvIEAKLKEHEQ 7156
Cdd:PRK11281 386 ----IDKLEAGHKS 395
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
268-379 |
8.80e-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: 45.75 E-value: 8.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 268 EQERVQKKTFTNWINSYllkRVPPlRIDDLINDLRDGTKLIALLEVLsgeRLPVEKGRVLRRPH--------FLSNANTA 339
Cdd:cd21330 9 EGETREERTFRNWMNSL---GVNP-RVNHLYSDLSDALVIFQLYEKI---KVPVDWNRVNKPPYpklgenmkKLENCNYA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 442626145 340 LQFLASK-RIKLVNINPADLVDGRPPVVLGLIWTIILYFQL 379
Cdd:cd21330 82 VELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTL 122
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3164-3371 |
8.89e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 47.83 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3164 EYMQLVAKFNDWVHEAELRLQNSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLVhKQIQEAADKIwSSLNNYEQSELSAEL 3243
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERV-EALNELGEQL-IEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3244 AQFQTKLTNTLANAKTQQSELEKEAERWREYQQSIDRVKATIERTKFV--DEPVQNLAGLHFNIQKLSHAIGNVQSQNSD 3321
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALasEDLGKDLESVEELLKKHKELEEELEAHEPR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442626145 3322 LTLVNQQAQSLIRQADARNRQLIEQDNAGLNRSWQDLVRSLEQRRDNLQQ 3371
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
5112-5239 |
9.33e-05 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 48.78 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 5112 QQTTPRIPSPTEKSEVEQDIKSVQTSPQHQPKLDETAVQTSLEVQP------DNQENESQTLIVEITETEA--------- 5176
Cdd:PRK10905 82 QGQTPVATDGQQRVEVQGDLNNALTQPQNQQQLNNVAVNSTLPTEPatvapvRNGNASRQTAKTQTAERPAttrparkqa 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 5177 -------QTTPRSEEQSVAVEISTTEIQTDVSGQPAETVEISSQTTVTTTIEKELQTTPKDSPRAPEAGS 5239
Cdd:PRK10905 162 viepkkpQATAKTEPKPVAQTPKRTEPAAPVASTKAPAATSTPAPKETATTAPVQTASPAQTTATPAAGG 231
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3441-3642 |
9.44e-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: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3441 ILTFLGEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVhvyDEHIA 3520
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---EAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3521 QTEQLLITLNSQV-QQAAEESKLLVAQTTAHYQAKQNQL-----PSDIAQEFTALELLAERVQVTMETKEKDFKRAKTVR 3594
Cdd:COG4942 87 ELEKEIAELRAELeAQKEELAELLRALYRLGRQPPLALLlspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 442626145 3595 TEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELLQRINHEITAIYER 3642
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2752-2936 |
9.66e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 47.44 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2752 FEDSMKNMGDWLNEMETATEGELRTTSLPVLEEQLAHYKKLLSDAENKGGLINDVSEQGKSILpTLSNADKLKLNDDIKN 2831
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2832 MKDRYGRIKNTIDDRVNALGDHIKKYKdaksRLAECSQFLGNIQQKLRELNR-PIGSRIEDVQDLLGAYEGILKELKDSK 2910
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQ----FFRDADDLEQWLEEKEAALASeDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180
....*....|....*....|....*.
gi 442626145 2911 skmgdmqmddlPELQSILAQQDDMIK 2936
Cdd:cd00176 160 -----------PRLKSLNELAEELLE 174
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
3037-3838 |
1.07e-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: 49.66 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3037 LQNLRKAVESQRQK---HQLQLESHKKMAAELSEILDWLHSHEGAAKSRPLLDRdpeSVERELQKHQSLSQDIESYLNKF 3113
Cdd:TIGR00606 188 LETLRQVRQTQGQKvqeHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVK---SYENELDPLKNRLKEIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3114 NKINDGVKT----------------------EIGMPSSLLEMLSEGRSLVASLPHELEEREKYLKNNRDSRLEYMQLVAK 3171
Cdd:TIGR00606 265 MKLDNEIKAlksrkkqmekdnselelkmekvFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3172 FNDWVHEAELRLQNSQ-HGIDYEHLVQDLDEHKIFFGNEapirnlvHKQIQEAADKIWSSLNNYEQSELSAELAQFQTKL 3250
Cdd:TIGR00606 345 LLVEQGRLQLQADRHQeHIRARDSLIQSLATRLELDGFE-------RGPFSERQIKNFHTLVIERQEDEAKTAAQLCADL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3251 TNTLANAKTQQSELE-KEAERWREYQQSIDRVKATIERTKFVDEPVQNLAGLHFNIQKLSHAIGNVQS------QNSDLT 3323
Cdd:TIGR00606 418 QSKERLKQEQADEIRdEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERelskaeKNSLTE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3324 LVNQQAQSL-IRQADA-RNRQLIEQDNAGLNRSWQDLVRSL----------EQRRDNLQQLAEHWDG----------FEN 3381
Cdd:TIGR00606 498 TLKKEVKSLqNEKADLdRKLRKLDQEMEQLNHHTTTRTQMEmltkdkmdkdEQIRKIKSRHSDELTSllgyfpnkkqLED 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3382 SLHAWEKALGRLEDKFRNVDPTVRSrrhLEDTKNAIQelreesNQLKSSHKEIEALSKSILTFLG-EVHKPSAEAIQAKV 3460
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELAS---LEQNKNHIN------NELESKEEQLSSYEDKLFDVCGsQDEESDLERLKEEI 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3461 DKLVEQQAKLNDTLRDKEQQVSKDLEEIEQ---VFRRISQLQDKLNALHEQLQS-VHVYDEHIAQTEQLLitlnSQVQQA 3536
Cdd:TIGR00606 649 EKSSKQRAMLAGATAVYSQFITQLTDENQSccpVCQRVFQTEAELQEFISDLQSkLRLAPDKLKSTESEL----KKKEKR 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3537 AEESKLLVAQTTAHYQAKQNQLP----------SDIAQEFTALELLAERVQVTMETKE--KDFKRAKTVRTEYVDGVDEV 3604
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPelrnklqkvnRDIQRLKNDIEEQETLLGTIMPEEEsaKVCLTDVTIMERFQMELKDV 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3605 QRWLLQ--AEVQVQERSLTPTQMKELLQRINHEITAIYERFTLvktNGQLIIENcrnSEEKTLVQTTIDQLAASLAQVRG 3682
Cdd:TIGR00606 805 ERKIAQqaAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIEL---NRKLIQDQ---QEQIQHLKSKTNELKSEKLQIGT 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3683 WLDEKKQAVGDSLDAWTRFMNLYQIVmswaSEKRNfidQTIELRTLPEARNKLNDYVTSVK--SIKPIVKHLSEMDKELE 3760
Cdd:TIGR00606 879 NLQRRQQFEEQLVELSTEVQSLIREI----KDAKE---QDSPLETFLEKDQQEKEELISSKetSNKKAQDKVNDIKEKVK 951
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626145 3761 HIgqVTTVGDLKDKLQEA-EDAKISVEAVLLERNSLLQEaceewdqCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQL 3838
Cdd:TIGR00606 952 NI--HGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEE-------CEKHQEKINEDMRLMRQDIDTQKIQERWLQDNL 1021
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6470-7069 |
1.21e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6470 QLRTRYQRAVELWDKYRNASAAVKNsIDQQMDAVKSLEQPLDALQHAKvcqdnlttqnDRILELRDIVAKIAADVGLDAS 6549
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALED-AREQIELLEPIRELAERYAAAR----------ERLAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6550 ALMQGELDALGQRLAECKDAITTLANVAETQDKERKELdkevtlAKAYFNNVQQDIsreapqnpKESEEQLAALRAHL-- 6627
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDEL------EAQIRGNGGDRL--------EQLEREIERLERELee 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6628 --QTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQdtfQEYHRLSTRLARSQNSSEALRLWRQYLQH 6705
Cdd:COG4913 357 reRRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAEIASLER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6706 VQSflscAIPEDYSSLREQqqlcaihqnllISQQSVLSETPL--------------------ESEL----------SEQY 6755
Cdd:COG4913 434 RKS----NIPARLLALRDA-----------LAEALGLDEAELpfvgelievrpeeerwrgaiERVLggfaltllvpPEHY 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6756 KALT----NLHNET---LSRIMQRNGELERRvsgwNAYRQQLAALLD--------WLRQREAERNAL-------QLRY-- 6811
Cdd:COG4913 499 AAALrwvnRLHLRGrlvYERVRTGLPDPERP----RLDPDSLAGKLDfkphpfraWLEAELGRRFDYvcvdspeELRRhp 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6812 --------IHLKRVPHLKHRLDAMIQQLDQG---EQQSKALQEQQQELARHCDDALATAMRMEQASigQRISNLRAALKT 6880
Cdd:COG4913 575 raitragqVKGNGTRHEKDDRRRIRSRYVLGfdnRAKLAALEAELAELEEELAEAEERLEALEAEL--DALQERREALQR 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6881 WQGFLQRVTQLsESYEQRVNQLQQEfgaAQKLLDANSE--SLPTQPAAIEQLLGSLRAQRVQLGAQVSALES-LTVTQEE 6957
Cdd:COG4913 653 LAEYSWDEIDV-ASAEREIAELEAE---LERLDASSDDlaALEEQLEELEAELEELEEELDELKGEIGRLEKeLEQAEEE 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6958 LKECISPHDMKTIRQRNWLlwqqHADLDYQLANLINSiEERLSLLSNYQIRYDRISQWLQRLEQRVEK------------ 7025
Cdd:COG4913 729 LDELQDRLEAAEDLARLEL----RALLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERamrafnrewpae 803
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 442626145 7026 --DADVTAMTNPEqAAKQLEQQVNSEL-QLRDKEREWLLSTSRELLT 7069
Cdd:COG4913 804 taDLDADLESLPE-YLALLDRLEEDGLpEYEERFKELLNENSIEFVA 849
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3805-4153 |
1.22e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3805 QCERKIKDIRSWHEKtkqgLDSSQQQKKPLRDQLGFCEKTLADINVQKTKLRLSIEKLEvhfrngmggdprlsENVDDLV 3884
Cdd:COG1196 219 KEELKELEAELLLLK----LRELEAELEELEAELEELEAELEELEAELAELEAELEELR--------------LELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3885 RVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRLVMAptylphdRERALAEQQDLITQELDELLQSL 3964
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE-------ELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3965 SSVEDGIANMNQSSLDgMLHGLKLIQSNLEVHERDAIELKNQAKKLptdpatERLLNDTVDRIDLLLRRTQQGITMIANA 4044
Cdd:COG1196 354 EEAEAELAEAEEALLE-AEAELAEAEEELEELAEELLEALRAAAEL------AAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 4045 MHGQKKRQQEIDEYQQHLLELEQWIIEVSAELASFEptsDSSTDEQVLKSQVERSQQLLRTLKDRQQSMEDLVEQTRQLQ 4124
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL---ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
330 340
....*....|....*....|....*....
gi 442626145 4125 SHPDVSPLADTLMEQLQSIITILREQVTV 4153
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3359-3802 |
1.57e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3359 VRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKSSHKEIEALS 3438
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3439 KSILTFlgevhKPSAEAIQAKVDKLVEQQAKLNDTLRD----KEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVhv 3514
Cdd:COG4717 153 ERLEEL-----RELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEEL-- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3515 yDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAHYQAKQNQLPSDIAQEFTALELLAE--RVQVTMETKEKDFKRAKT 3592
Cdd:COG4717 226 -EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGllALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3593 VRTEYVDGVDEVQRWLLQAEVQVQ--ERSLTPTQMKELLQRINHEITAIYERFTLVKtngQLIIENCRNSEEKTLVQ--- 3667
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALglPPDLSPEELLELLDRIEELQELLREAEELEE---ELQLEELEQEIAALLAEagv 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3668 TTIDQLAASLAQVRGWLDEKKQavgdsLDAWTRFMNLYQIVMSWASEKRNFIDQTIEL----RTLPEARNKLNDYVTSVK 3743
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEE-----LEELEEQLEELLGELEELLEALDEEELEEELeeleEELEELEEELEELREELA 456
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 442626145 3744 SIKPIVKHLSEmDKELEHIGQVttVGDLKDKLQEAEDAKISVEAVLlernSLLQEACEE 3802
Cdd:COG4717 457 ELEAELEQLEE-DGELAELLQE--LEELKAELRELAEEWAALKLAL----ELLEEAREE 508
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
5077-5236 |
2.02e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 48.50 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 5077 EDAVVSSP--SESPRTPMVELVIPTEVVELA--LVEDEEQQTTPRIPSPTEKSEVEQDIKSVQTSPQHQPKLDETAV--- 5149
Cdd:PRK10811 861 AEEVQVQPvvAEVPVAAAVEPVVSAPVVEAVaeVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDVAvaq 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 5150 QTSLEVQPDNQENESQTLIVEITETEAQTTPRSEEQSVAVEISTTEIQTDVSGQPAETVEISSQTTVTTTIEKELQTTPK 5229
Cdd:PRK10811 941 EVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVEHNHATAPM 1020
|
....*..
gi 442626145 5230 DSPRAPE 5236
Cdd:PRK10811 1021 TRAPAPE 1027
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6390-6950 |
2.14e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6390 DFMMELIRVHGQVdyERLRKATERLEGLAGD------LHNREQLIDELKGAAKPLIescDVQIVEQIESAVQEAVVAWND 6463
Cdd:COG4913 232 EHFDDLERAHEAL--EDAREQIELLEPIRELaeryaaARERLAELEYLRAALRLWF---AQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6464 TSENLQQLRTRYQRAVELWDKYRNASAAVKNsidqqmDAVKSLEQPLDALQHAkvcqdnLTTQNDRILELRDIVAKIAAD 6543
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERE------LEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6544 VGLDASAL------MQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVT-LAK------AYFNNVQQDISREAP 6610
Cdd:COG4913 375 LPASAEEFaalraeAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAsLERrksnipARLLALRDALAEALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6611 Q--------------NPKESEEQLAALRAhLQTLART----EEQLRQ---------LKERHQNSEVAPSVASS-----DD 6658
Cdd:COG4913 455 LdeaelpfvgelievRPEEERWRGAIERV-LGGFALTllvpPEHYAAalrwvnrlhLRGRLVYERVRTGLPDPerprlDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6659 DGILEVLAlwqkiFQDT-FQEYhrLSTRLARSQNssealrlwrqylqhvqsFLSCAIPEDyssLREQQQlcAIHQNLLIS 6737
Cdd:COG4913 534 DSLAGKLD-----FKPHpFRAW--LEAELGRRFD-----------------YVCVDSPEE---LRRHPR--AITRAGQVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6738 QQSVLSETPLESELSEQY-------KALtnlhnETLSRIMQrngELERRVSGWNAYRQQLAALLDWLRQREAERNALQLR 6810
Cdd:COG4913 585 GNGTRHEKDDRRRIRSRYvlgfdnrAKL-----AALEAELA---ELEEELAEAEERLEALEAELDALQERREALQRLAEY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6811 YIHLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHcdDALATAMRMEQASIGQRISNLRAALKTWQGFLQRVTQ 6890
Cdd:COG4913 657 SWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEEL--EAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6891 LSESYEQRVnQLQQEFGAAQKLLDANseslptQPAAIEQLLGSLRAQRVQLGAQVSALES 6950
Cdd:COG4913 735 RLEAAEDLA-RLELRALLEERFAAAL------GDAVERELRENLEERIDALRARLNRAEE 787
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
266-374 |
2.45e-04 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 45.05 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 266 QEEQERVQKKTFTNWINSYL-----LKRVPPLR--IDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFL--SNA 336
Cdd:cd21325 18 QHSYSEEEKYAFVNWINKALendpdCRHVIPMNpnTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFIiqENL 97
|
90 100 110
....*....|....*....|....*....|....*...
gi 442626145 337 NTALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21325 98 NLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 135
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3362-3646 |
2.47e-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: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3362 LEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKSSHKEIEALSKSI 3441
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3442 ltflgevhkpsaEAIQAKVDKLVEQQAKLNdtlrdkeqqvskdleeieqvfRRISQLQDKLNALHEQLQSVHvydehiAQ 3521
Cdd:COG4913 695 ------------EELEAELEELEEELDELK---------------------GEIGRLEKELEQAEEELDELQ------DR 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3522 TEQLLITLNSQVQQAAEEsKLLVAQTTAHYQAKQNQLPSDIAQEFTALELLAERVQVTMETKEKDFK-RAKTVRTEyVDG 3600
Cdd:COG4913 736 LEAAEDLARLELRALLEE-RFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPaETADLDAD-LES 813
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 442626145 3601 VDEVQRWL--LQAE--VQVQER------SLTPTQMKELLQRINHEITAIYERFTLV 3646
Cdd:COG4913 814 LPEYLALLdrLEEDglPEYEERfkellnENSIEFVADLLSKLRRAIREIKERIDPL 869
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2474-2671 |
3.02e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2474 KIQELKGKAAQVAEVISNLDGQQ--VEEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEEL- 2550
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELa 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2551 -------------------------QAPKPLGYTPKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELEpvEYSQ 2605
Cdd:COG4942 108 ellralyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA--ELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626145 2606 LESALRNLNTENRNLSGVLKAELDRALEASKARKSLENDLDKARQWLKTKISEVRKLPVYHPLTSA 2671
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
3386-3548 |
3.03e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.00 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3386 WEKALGRLEDKFRNVDPTVRSRRH-LEDTKNAIQELREESNQLKSSHK---EIEAL--SKSILTFLGEVHKPSAEAIQAK 3459
Cdd:PRK05771 84 LEELIKDVEEELEKIEKEIKELEEeISELENEIKELEQEIERLEPWGNfdlDLSLLlgFKYVSVFVGTVPEDKLEELKLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3460 VDKLVEQ---QAKLND-----TLRDKEQQVSKDL-----------------EEIEQVFRRISQLQDKLNALHEQLQSV-- 3512
Cdd:PRK05771 164 SDVENVEyisTDKGYVyvvvvVLKELSDEVEEELkklgferleleeegtpsELIREIKEELEEIEKERESLLEELKELak 243
|
170 180 190
....*....|....*....|....*....|....*.
gi 442626145 3513 HVYDEHIAQTEQLLItlnsQVQQAAEESKLLVAQTT 3548
Cdd:PRK05771 244 KYLEELLALYEYLEI----ELERAEALSKFLKTDKT 275
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
6404-7073 |
3.28e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.91 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6404 YERLRKATERLEGLAGDLHNREQLIDELKGAAKPLIEScDVQIVEQIEsAVQEAVVAWNdtsenlQQLRTryqraveLWD 6483
Cdd:pfam12128 233 IAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSD-ETLIASRQE-ERQETSAELN------QLLRT-------LDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6484 KYRNASAAVKNSIDQQMDAVKSLEQPLDAL--QHAKVCQDNLTTqndrilelrdivakIAADvgLDASALMQGELDALGQ 6561
Cdd:pfam12128 298 QWKEKRDELNGELSAADAAVAKDRSELEALedQHGAFLDADIET--------------AAAD--QEQLPSWQSELENLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6562 RLaeckDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREApqnpkeSEEQLAALRAHLQTL-----ARTEEQ 6636
Cdd:pfam12128 362 RL----KALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREA------RDRQLAVAEDDLQALeselrEQLEAG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6637 LRQLKERHQNSEVAPSVASS--DDDGILEVLALWQKIFQD-----------TFQEYHRLSTRLA----RSQNSSEALRLW 6699
Cdd:pfam12128 432 KLEFNEEEYRLKSRLGELKLrlNQATATPELLLQLENFDErierareeqeaANAEVERLQSELRqarkRRDQASEALRQA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6700 RQYLQHVQSFLSCA----IPEDYS---SLREQQQLCAIHQNLLISQQsVLSETPLESELSE-QYKALTNLHNETLsrimq 6771
Cdd:pfam12128 512 SRRLEERQSALDELelqlFPQAGTllhFLRKEAPDWEQSIGKVISPE-LLHRTDLDPEVWDgSVGGELNLYGVKL----- 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6772 rngELER-RVSGWNAYRQQLAALLDWL---------RQREAERNALQLRyihlKRVPHLKHRLDAMIQQLDQGEQQSKAL 6841
Cdd:pfam12128 586 ---DLKRiDVPEWAASEEELRERLDKAeealqsareKQAAAEEQLVQAN----GELEKASREETFARTALKNARLDLRRL 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6842 QEQQQELARHCDDALATAMRMEQASIGQRISNLRAALKTWQGFLQRVT-QLSESYEQRVNQLQQEFGAAQklldansesl 6920
Cdd:pfam12128 659 FDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKeQKREARTEKQAYWQVVEGALD---------- 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6921 ptqpAAIEQLLGSLRAQRVQLGAQVSALesltvtQEELKECISPHDMKTIRQrnwllwqqhADLDYQLANLINSIEerls 7000
Cdd:pfam12128 729 ----AQLALLKAAIAARRSGAKAELKAL------ETWYKRDLASLGVDPDVI---------AKLKREIRTLERKIE---- 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7001 llsnyQIRYDR--ISQWLQRLEQR--VEKDADVTAMTNPEQAAKQLEQQV---NSELQLRDKEREWLLSTSRELLTLYSE 7073
Cdd:pfam12128 786 -----RIAVRRqeVLRYFDWYQETwlQRRPRLATQLSNIERAISELQQQLarlIADTKLRRAKLEMERKASEKQQVRLSE 860
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
6553-6804 |
3.29e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6553 QGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVtlakayfNNVQQDIsreapqnpKESEEQLAALRAHLQTLAR 6632
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------AALARRI--------RALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6633 TEEQLRQLKERHQNsEVAPSVASSDDDGILEVLALwqkifqdtfqeyhrlstrLARSQNSSEALRLwRQYLQHVQSFLSC 6712
Cdd:COG4942 91 EIAELRAELEAQKE-ELAELLRALYRLGRQPPLAL------------------LLSPEDFLDAVRR-LQYLKYLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6713 AIpedySSLREQQQLCAIHQNLLISQQSVLSEtpLESELSEQYKALTNL---HNETLSRIMQRNGELERRVSGWNAYRQQ 6789
Cdd:COG4942 151 QA----EELRADLAELAALRAELEAERAELEA--LLAELEEERAALEALkaeRQKLLARLEKELAELAAELAELQQEAEE 224
|
250
....*....|....*
gi 442626145 6790 LAALLDWLRQREAER 6804
Cdd:COG4942 225 LEALIARLEAEAAAA 239
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
2098-2201 |
3.53e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 43.47 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2098 YHQSLQDVEKWLLQISFQLMAHNslFISNREQTQEQIKQHEALLVEIQKYQTNLDDLNAKGQAQIKRYESSTPAIrptvE 2177
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASED--LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEI----E 76
|
90 100
....*....|....*....|....
gi 442626145 2178 SQLKNIQDSYNSLLQTSVQIKNRL 2201
Cdd:smart00150 77 ERLEELNERWEELKELAEERRQKL 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3325-3964 |
3.75e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3325 VNQQAQSLIRQADArnrqlieqdnAglnRSWQDLVRSLEQRRDNLQQLaeHWDGFENSLHAWEKALGRLEDKFRnvdptv 3404
Cdd:COG1196 198 LERQLEPLERQAEK----------A---ERYRELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELE------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3405 RSRRHLEDTKNAIQELREESNQLKsshKEIEALSKSIltflgevhkpsaEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKD 3484
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELE---LELEEAQAEE------------YELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3485 LEEIEQVFRRISQLQDKLNALHEQLQSVhvyDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAHYQAKQNQLpsdiaQ 3564
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEA---EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-----R 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3565 EFTALELLAERVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELLQRINHEITAIYERFT 3644
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3645 LVKTNGQLIIEncRNSEEKTLVQTTIDQLAASLAQVRGWLDEKKQA----VGDSLDAWTRFMNLYQIVMSWASEKRNFID 3720
Cdd:COG1196 474 LLEAALAELLE--ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrgLAGAVAVLIGVEAAYEAALEAALAAALQNI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3721 QTIELRTLPEARNKLNDYVTSVKSIKPIVK-HLSEMDKELEHIGQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEA 3799
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3800 CEEWDqcERKIKDIRSWHEKTKQGLDSSQQQkkplrDQLGFCEKTLADINVQKTKLRLSIEKLEVHfrngmggdpRLSEN 3879
Cdd:COG1196 632 LEAAL--RRAVTLAGRLREVTLEGEGGSAGG-----SLTGGSRRELLAALLEAEAELEELAERLAE---------EELEL 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3880 VDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRLVMAPTYLPHDRERALAEQQdlitQELDE 3959
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE----RELER 771
|
....*
gi 442626145 3960 LLQSL 3964
Cdd:COG1196 772 LEREI 776
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
442-535 |
4.52e-04 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 43.44 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 442 LLNWVTNALPKDSG--VEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQ----RLETAFDVAEsKLGIAKLLD 515
Cdd:cd21218 15 LLRWVNYHLKKAGPtkKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEdlekRAEKVLQAAE-KLGCKYFLT 93
|
90 100
....*....|....*....|
gi 442626145 516 AEdvDVPKPDEKSIMTYVAQ 535
Cdd:cd21218 94 PE--DIVSGNPRLNLAFVAT 111
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
7145-7480 |
4.91e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 47.44 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7145 NVIEAKLKEHEQIQRSiehHSSNVGEVLNLVEMLLNDADSwrtqvNTSGLAASAQNLEQRWKNVCSQ--SAERKARIL-- 7220
Cdd:pfam07111 133 NLEEGSQRELEEIQRL---HQEQLSSLTQAHEEALSSLTS-----KAEGLEKSLNSLETKRAGEAKQlaEAQKEAELLrk 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7221 ---TIWNLLQQLIKLTAEHKNWLGKQ-----ESQIAGFERDQKSHSKHKLEERQMELRAKLEELESQSVNLR-----QLE 7287
Cdd:pfam07111 205 qlsKTQEELEAQVTLVESLRKYVGEQvppevHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLThmlalQEE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7288 QIYAKLAMSAGVEPENIQKltlpTKVMVSMWRQltprchalldaidKDAKLMREFNNAQLEATNSLNAIQkalEQLPSAE 7367
Cdd:pfam07111 285 ELTRKIQPSDSLEPEFPKK----CRSLLNRWRE-------------KVFALMVQLKAQDLEHRDSVKQLR---GQVAELQ 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7368 NQQTSKAEPKAVLQRleSLEKKLQDAQ------QHVQQADNLAQEAKTRTKQQPQL--KQLLELVSAYTTLWQTVQTRiv 7439
Cdd:pfam07111 345 EQVTSQSQEQAILQR--ALQDKAAEVEvermsaKGLQMELSRAQEARRRQQQQTASaeEQLKFVVNAMSSTQIWLETT-- 420
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 442626145 7440 tlkttwLTRAAQAAASLP-----VSEAANAAVQVNTLSQRKLRQAQ 7480
Cdd:pfam07111 421 ------MTRVEQAVARIPslsnrLSYAVRKVHTIKGLMARKVALAQ 460
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2474-2773 |
5.01e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2474 KIQELKGKAAQVAEVisnldgqqVEEQMKSLDRRFAD-LGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEELQa 2552
Cdd:PTZ00121 1419 KADEAKKKAEEKKKA--------DEAKKKAEEAKKADeAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK- 1489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2553 pkplgytpKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELEPVEYSQLESALRNLNtENRNLSGVLKAE-LDRA 2631
Cdd:PTZ00121 1490 --------KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE-EKKKADELKKAEeLKKA 1560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2632 LEASKARKSLENDLDK---------ARQWLKTKISEVRKLPVYHPLTSAEIEKKIQENRKYDDDAKQfNDSVLTDVQRQA 2702
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKnmalrkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLK 1639
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626145 2703 ANIMKDCDDADKAALQQILDEIAADYQTLKDESSKRGKSlddllQGRKAFEDSMKNMGDWLNEMETATEGE 2773
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE-----EAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1663-2223 |
5.26e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1663 LEKEVTEVEKMFFNTMEHVKDRVGYLEDYSAKWNNYKTRLAELQEWANKvapknIEALQSEDLTPEERVVKVQAFKRILG 1742
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE-----IEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1743 DRMKQLDllaADASELAPKEGNIAEAKRLKGEITKLQEVLSAINRnvdhQAQAVQEDLVNWQQFQAGLQ-QIKPAVEQS- 1820
Cdd:PRK03918 266 ERIEELK---KEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLD----ELREIEKRLSRLEEEINGIEeRIKELEEKEe 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1821 ---EVKKLLEEVLAE----KDNVEDLNDNCELLME-QSACTRIRDQTIETQANYTKLLTSAQGLVAKIEKNLSDH-TEFL 1891
Cdd:PRK03918 339 rleELKKKLKELEKRleelEERHELYEEAKAKKEElERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARiGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1892 NYKKEMDAWIEKAQQVLDDCSTDGdaaiiaqkldtvnslasRLPEGQHLLALVQDAYSKASNITPEDKQ--EKLRELMTK 1969
Cdd:PRK03918 419 KEIKELKKAIEELKKAKGKCPVCG-----------------RELTEEHRKELLEEYTAELKRIEKELKEieEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1970 VREDWDALG-----LAVKQKLSDLKQAQNRWNDFaaNKDKLEKWLNETETTLKVAPETKGELSEMKTLLERYKTLSNELK 2044
Cdd:PRK03918 482 LRELEKVLKkeselIKLKELAEQLKELEEKLKKY--NLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2045 LKGNELEQLQSEARDLgtevdaVNRLQSRCDKLKNDCSAHITALEQEmfdYNAYhQSLQDVEKWLlqisfqlmahnslfi 2124
Cdd:PRK03918 560 ELEKKLDELEEELAEL------LKELEELGFESVEELEERLKELEPF---YNEY-LELKDAEKEL--------------- 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2125 snrEQTQEQIKQHEALLVEIQKYqtnLDDLNAKGQAQIKRYEsstpairptvESQLKNIQDSYNSLLQTSVQIKNRLLES 2204
Cdd:PRK03918 615 ---EREEKELKKLEEELDKAFEE---LAETEKRLEELRKELE----------ELEKKYSEEEYEELREEYLELSRELAGL 678
|
570
....*....|....*....
gi 442626145 2205 LAKFQEYEDTLDSIMRNLE 2223
Cdd:PRK03918 679 RAELEELEKRREEIKKTLE 697
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
273-374 |
5.83e-04 |
|
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409142 Cd Length: 116 Bit Score: 43.29 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 273 QKKTFTNWINSYL-----LKRVPPL--RIDDLINDLRDGTKLIALLEV-LSG---ERlPVEKGRVLRRphFLSNANTALQ 341
Cdd:cd21293 2 EKGSYVDHINRYLgddpfLKQFLPIdpSTNDLFDLVKDGVLLCKLINVaVPGtidER-AINTKKVLNP--WERNENHTLC 78
|
90 100 110
....*....|....*....|....*....|....*
gi 442626145 342 FLASKRI--KLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21293 79 LNSAKAIgcSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
865-1052 |
5.83e-04 |
|
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: 45.13 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 865 EEWLQLAEQKVNQSEDERL------------DFFQDIPVWKDKFDALASSANYLIASCEEPiAQQLRQRHGALSERFERL 932
Cdd:cd00176 13 EAWLSEKEELLSSTDYGDDlesveallkkheALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQERLEELNQRWEEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 933 FANTKQYMHAGDIIRSRQEYKSGIEQLSRWLRGAESVLDQRQVLGNSEQVKEYGQQLQQLASEIDDNEELFKTISRNFQS 1012
Cdd:cd00176 92 RELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442626145 1013 LIQDLSRDEVDKMMKLLKQEKESLVRIRAQLPAKLHLFHQ 1052
Cdd:cd00176 172 LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3750-4193 |
6.03e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3750 KHLSEMDKELEHIG-QVTTVGDLKDKLQEAEDAKISVEAVLLERNSL-LQEACEEWDQCERKIKDIRSWHEKTKQGLDSS 3827
Cdd:COG4913 235 DDLERAHEALEDAReQIELLEPIRELAERYAAARERLAELEYLRAALrLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3828 QQQKKPLRDQLGFCEKTLADINVQ-KTKLRLSIEKLEVHFRngmggdpRLSENVDDLVRVLDGLGELVKAKSQSLEQTLA 3906
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELE-------ERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3907 QIDVYQQQMQSLRQRIIQEEQQLRlvmaptylphDRERALAEQQDLITQELDELLQSLSSVEDGIANMN----------- 3975
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAE----------AALRDLRRELRELEAEIASLERRKSNIPARLLALRdalaealglde 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3976 -------------------QSSLDGMLHGLKLiqsNLEV---HERDAIELKNQ-----------AKKLPTDPATERLLND 4022
Cdd:COG4913 458 aelpfvgelievrpeeerwRGAIERVLGGFAL---TLLVppeHYAAALRWVNRlhlrgrlvyerVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 4023 TV--------------------DRIDLL-------LRRTQQGIT---MI-ANAMHGQKKRQQEIDEY-------QQHLLE 4064
Cdd:COG4913 535 SLagkldfkphpfrawleaelgRRFDYVcvdspeeLRRHPRAITragQVkGNGTRHEKDDRRRIRSRyvlgfdnRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 4065 LEQWIIEVSAELASFEPTSDSSTDEQvlkSQVERSQQLLRTLKDRQQSMEDLVEQTRQLQ-----------SHPDVSPLA 4133
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAEL---DALQERREALQRLAEYSWDEIDVASAEREIAeleaelerldaSSDDLAALE 691
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 4134 DTLmEQLQSIITILREQVTVATKRIFTIEKRIVDLRKAKsEEAQRQRVLADSLIKPPTEA 4193
Cdd:COG4913 692 EQL-EELEAELEELEEELDELKGEIGRLEKELEQAEEEL-DELQDRLEAAEDLARLELRA 749
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2716-3541 |
6.53e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2716 ALQQILDEIAadyqtlkdESSKRGKSLDDLLQGRKAFEDSMKNMGDWLNEMETATEGELRT-TSLPVLEEQLAHYKKLLS 2794
Cdd:TIGR00606 170 ALKQKFDEIF--------SATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIrDQITSKEAQLESSREIVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2795 DAENKgglINDVSEQGKSILPTLSNAdkLKLNDDIKNMKDRYGRIKNT--------------IDDRVNAL-GDHIKKYKD 2859
Cdd:TIGR00606 242 SYENE---LDPLKNRLKEIEHNLSKI--MKLDNEIKALKSRKKQMEKDnselelkmekvfqgTDEQLNDLyHNHQRTVRE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2860 AKSRLAECSQFLGNIQQKLRELNRPiGSRIEDVQDLLGA-----YEGILKELKDSKSKMGDMQMDDLPELQSILAQQDDM 2934
Cdd:TIGR00606 317 KERELVDCQRELEKLNKERRLLNQE-KTELLVEQGRLQLqadrhQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNF 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2935 IKLI----EDQLAHLRQLLLLREQFIALINEIIAFI-MKYTDVIIDIENSPDSLEDKINKYDDVIVKIQECEGVLASAND 3009
Cdd:TIGR00606 396 HTLVierqEDEAKTAAQLCADLQSKERLKQEQADEIrDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3010 KGQ---KIASEGNAADKNSITEQLQSLKNQLQNlrkavesqrqkHQLQLESHKKMAAELSEILDwlhSHEGAAKSRPLLD 3086
Cdd:TIGR00606 476 LDQelrKAERELSKAEKNSLTETLKKEVKSLQN-----------EKADLDRKLRKLDQEMEQLN---HHTTTRTQMEMLT 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3087 RDPESVERELQKHQSL-SQDIESYLNKFNKINDGVKTEigmpSSLLEMLSEGRSLVASLPHELE--EREKYLKNNRDSRL 3163
Cdd:TIGR00606 542 KDKMDKDEQIRKIKSRhSDELTSLLGYFPNKKQLEDWL----HSKSKEINQTRDRLAKLNKELAslEQNKNHINNELESK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3164 EYMQLvaKFNDWVHEAelrLQNSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLVHKQIQEAADKIWSSLNNYEQS-ELSAE 3242
Cdd:TIGR00606 618 EEQLS--SYEDKLFDV---CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVfQTEAE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3243 LAQFQTKLTNTLANAKTQQSELEKEAERwREYQQSIDRVKATIeRTKFVDEPVQNLAGLHFNIQKLSHAIgnvQSQNSDL 3322
Cdd:TIGR00606 693 LQEFISDLQSKLRLAPDKLKSTESELKK-KEKRRDEMLGLAPG-RQSIIDLKEKEIPELRNKLQKVNRDI---QRLKNDI 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3323 TLVNQQAQSLIRQADARNrqlIEQDNAGLNRSWQDLVRSLEQRrdnLQQLAEHWDGFENSLhAWEKALGRLEDKFRNVDP 3402
Cdd:TIGR00606 768 EEQETLLGTIMPEEESAK---VCLTDVTIMERFQMELKDVERK---IAQQAAKLQGSDLDR-TVQQVNQEKQEKQHELDT 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3403 TVRS----RRHLEDTKNAIQELREESNQLKSSHKEI-------EALSKSILTFLGEVHKPSAEAIQAKVDKLVEQQAKlN 3471
Cdd:TIGR00606 841 VVSKielnRKLIQDQQEQIQHLKSKTNELKSEKLQIgtnlqrrQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFL-E 919
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626145 3472 DTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVHVY-----DEHIAQTEQLLITLNSQVQQAAEESK 3541
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgkDDYLKQKETELNTVNAQLEECEKHQE 994
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3296-3512 |
6.75e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3296 QNLAGLHFNIQKLSHAIGNVQSQ----NSDLTLVNQQAQSLIRQADARNRQL--IEQDNAGLNRSWQDLVRSLEQRRDNL 3369
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEekalLKQLAALERRIAALARRIRALEQELaaLEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3370 QQLAEHWdgFENSLHAWEKALGRLEDKFRNVdptvrsrRHLEDTKNAIQELREESNQLKSSHKEIEALSKSILTflgevh 3449
Cdd:COG4942 107 AELLRAL--YRLGRQPPLALLLSPEDFLDAV-------RRLQYLKYLAPARREQAEELRADLAELAALRAELEA------ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626145 3450 kpSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSV 3512
Cdd:COG4942 172 --ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
6573-7017 |
6.78e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 46.89 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6573 LANVAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPS 6652
Cdd:COG4995 8 ALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6653 VASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLCAIHQ 6732
Cdd:COG4995 88 ALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6733 NLLISQQSVLSETPLESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYI 6812
Cdd:COG4995 168 LALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6813 HLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALATAMRMEQASIGQRISNLRAALKTWQGFLQRVTQLS 6892
Cdd:COG4995 248 AALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6893 ESYEQRVNQLQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELKECISPHDMKTIRQ 6972
Cdd:COG4995 328 AALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQ 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 442626145 6973 RNWLLWQQHADLDYQLANLInsIEERLSLLSNYQIRYDRISQWLQ 7017
Cdd:COG4995 408 LLRLLLAALALLLALAAYAA--ARLALLALIEYIILPDRLYAFVQ 450
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
4620-4845 |
7.07e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 47.00 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 4620 APVE-------LPAPQVDVEQPVVVATTSP-VHVPTADVV-EPKDSSPTSTTAAVVDVEavvediNEIWPLEHHLKPTNI 4690
Cdd:PRK10263 335 APVEpvtqtppVASVDVPPAQPTVAWQPVPgPQTGEPVIApAPEGYPQQSQYAQPAVQY------NEPLQQPVQPQQPYY 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 4691 DFSQHVEELAAPAAVTAETEASMPVEEIWPTSPETGNSLTLEQYE--------FEPQSPHEESTKSD--LVKPQETEPQV 4760
Cdd:PRK10263 409 APAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQstfapqstYQTEQTYQQPAAQEplYQQPQPVEQQP 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 4761 VAETKPEGITTGSITITKTTTTITSSTEVPE-ETLV---QNVPADEQQPPANKIKTDIQSfleaeqtlAAALKEQSSTPT 4836
Cdd:PRK10263 489 VVEPEPVVEETKPARPPLYYFEEVEEKRARErEQLAawyQPIPEPVKEPEPIKSSLKAPS--------VAAVPPVEAAAA 560
|
....*....
gi 442626145 4837 GASVAEDVQ 4845
Cdd:PRK10263 561 VSPLASGVK 569
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
273-374 |
9.02e-04 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 43.46 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 273 QKKTFTNWINSYL-----LKRVPPL--RIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFL--SNANTALQFL 343
Cdd:cd21324 25 EKYAFVNWINKALendpdCKHVIPMnpNTDDLFKAVGDGIVLCKMINFSVPDTIDERTINKKKLTPFTiqENLNLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 442626145 344 ASKRIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 135
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
3162-3975 |
9.88e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.37 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3162 RLEYMQLVAKFNDwVHEAELRLQnSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLV---HKQIQEAADKIwsslnNYEQSE 3238
Cdd:pfam12128 240 RPEFTKLQQEFNT-LESAELRLS-HLHFGYKSDETLIASRQEERQETSAELNQLLrtlDDQWKEKRDEL-----NGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3239 LSAELAQFQtkltntlanaktqqSELEKEAERWREYQQS-IDRVKATIERTKFVDEPVQNLAGLHfniQKLSHAIGNVQs 3317
Cdd:pfam12128 313 ADAAVAKDR--------------SELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERL---KALTGKHQDVT- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3318 qnsdltlvnQQAQSLIRQADARNRQLIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHW----DGFENSLHAWEKAL-GR 3392
Cdd:pfam12128 375 ---------AKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELreqlEAGKLEFNEEEYRLkSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3393 LED-KFRNVDPTVRSrrhledtknaiqelrEESNQLKSSHKEIEALSKSIltflgevhkpsaEAIQAKVDKLVEQQAKLn 3471
Cdd:pfam12128 446 LGElKLRLNQATATP---------------ELLLQLENFDERIERAREEQ------------EAANAEVERLQSELRQA- 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3472 DTLRDKEqqvskdLEEIEQVFRRISQLQDKLNALHEQLqsvhvydehIAQTEQLLITLNSQVQQAAEE-----SKLLVAQ 3546
Cdd:pfam12128 498 RKRRDQA------SEALRQASRRLEERQSALDELELQL---------FPQAGTLLHFLRKEAPDWEQSigkviSPELLHR 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3547 TTAHYQAKQNQlPSDiAQEFTALELLAERVQV------TMETKEKDFKRAKTVRTEYvDGVDEVQRWLLQAEVQVQERSL 3620
Cdd:pfam12128 563 TDLDPEVWDGS-VGG-ELNLYGVKLDLKRIDVpewaasEEELRERLDKAEEALQSAR-EKQAAAEEQLVQANGELEKASR 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3621 TPTQMKELLQriNHEITAIyeRFTLVKTNGQLIIENCRnSEEKTLVQTTIDQLAASLAQV----RGWLDEKKqavGDSLD 3696
Cdd:pfam12128 640 EETFARTALK--NARLDLR--RLFDEKQSEKDKKNKAL-AERKDSANERLNSLEAQLKQLdkkhQAWLEEQK---EQKRE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3697 AWTRFMNLYQIVMSWASEKRNFIDQTIE-LRTLPEARNKL--NDYVTSVKSIKPIVKHLSEMDKELEHIgqVTTVGDLKD 3773
Cdd:pfam12128 712 ARTEKQAYWQVVEGALDAQLALLKAAIAaRRSGAKAELKAleTWYKRDLASLGVDPDVIAKLKREIRTL--ERKIERIAV 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3774 KLQEAEDAKISVEAVLLERNSLLQEACEEwdqCERKIKDIRSwhEKTKQGLDSSQQQKKpLRDQLGFCEKTLADINVQKT 3853
Cdd:pfam12128 790 RRQEVLRYFDWYQETWLQRRPRLATQLSN---IERAISELQQ--QLARLIADTKLRRAK-LEMERKASEKQQVRLSENLR 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3854 KLRLSIEKL--------------EVHFRNGMGGD-----PRLSENVDDLVRVLDGlgeLVKAKS--------QSLEQTLA 3906
Cdd:pfam12128 864 GLRCEMSKLatlkedanseqaqgSIGERLAQLEDlklkrDYLSESVKKYVEHFKN---VIADHSgsglaetwESLREEDH 940
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626145 3907 QIDVYQQQMQSLRQrIIQEEQQLRLVMAPtylphDRERALAEQQDLITQELDELLQSLSSVEDGIANMN 3975
Cdd:pfam12128 941 YQNDKGIRLLDYRK-LVPYLEQWFDVRVP-----QSIMVLREQVSILGVDLTEFYDVLADFDRRIASFS 1003
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
6533-7294 |
1.11e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.37 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6533 LRDIVAKIAAD--VGLDASALMQGELDA------LGQRLAECKDAITTLANVAETQDKERKELDkevTLAKAYFNnvqqD 6604
Cdd:pfam12128 198 VKSMIVAILEDdgVVPPKSRLNRQQVEHwirdiqAIAGIMKIRPEFTKLQQEFNTLESAELRLS---HLHFGYKS----D 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6605 ISREAPQNpKESEEQLAALRAHLQTLartEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTfqeyhRLST 6684
Cdd:pfam12128 271 ETLIASRQ-EERQETSAELNQLLRTL---DDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDA-----DIET 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6685 RLARSQNsseaLRLWRQYLQHVQsflscaipedysslreqqqlcAIHQNLLISQQSVLSET-PLESELSEQYKALTNLHN 6763
Cdd:pfam12128 342 AAADQEQ----LPSWQSELENLE---------------------ERLKALTGKHQDVTAKYnRRRSKIKEQNNRDIAGIK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6764 ETLSRImqRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIhlKRVPHLKHRLDAMIQQLDQGEQQskalqE 6843
Cdd:pfam12128 397 DKLAKI--REARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLK--SRLGELKLRLNQATATPELLLQL-----E 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6844 QQQELARHCDDALaTAMRMEQASIGQRISNLRAALKTWQGFLQRVtqlsesyEQRVNQLQQEFGAAQKLLDANSES---- 6919
Cdd:pfam12128 468 NFDERIERAREEQ-EAANAEVERLQSELRQARKRRDQASEALRQA-------SRRLEERQSALDELELQLFPQAGTllhf 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6920 LPTQPAAIEQLLGSLRAQ----RVQL-----GAQVSALESLTVTQEELKECISP--HDM-KTIRQRNWLL-------WQQ 6980
Cdd:pfam12128 540 LRKEAPDWEQSIGKVISPellhRTDLdpevwDGSVGGELNLYGVKLDLKRIDVPewAASeEELRERLDKAeealqsaREK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6981 HADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQRL--EQRVEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKE-R 7057
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLfdEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKhQ 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7058 EWLLSTSRELLTLYSEpevrsqvqqqsdslidRWQRLKYLAKQKATKIGELKMTLLRLEERIAlirAWLFEVESQLDKPL 7137
Cdd:pfam12128 700 AWLEEQKEQKREARTE----------------KQAYWQVVEGALDAQLALLKAAIAARRSGAK---AELKALETWYKRDL 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7138 NFESYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLnlvemllndadSWRtqvntsglaasaQNLEQRWKNVCSQSAERKA 7217
Cdd:pfam12128 761 ASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVL-----------RYF------------DWYQETWLQRRPRLATQLS 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7218 RILT-IWNLLQQLIKLTAEHKNWLGKQESQIAGFERDQ----KSHSKHKLEERQM---ELRAKLEELE-SQSVNLRQLEQ 7288
Cdd:pfam12128 818 NIERaISELQQQLARLIADTKLRRAKLEMERKASEKQQvrlsENLRGLRCEMSKLatlKEDANSEQAQgSIGERLAQLED 897
|
....*.
gi 442626145 7289 IYAKLA 7294
Cdd:pfam12128 898 LKLKRD 903
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3388-3539 |
1.43e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3388 KALGRLEDKFRNVdptvrsRRHLEDTKNAIQELREESNQLKSSHKEIEALSKSILTFLGEVHKP-SAEAIQAKVDKLVEQ 3466
Cdd:COG1579 31 AELAELEDELAAL------EARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkEYEALQKEIESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626145 3467 QAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLqsvhvyDEHIAQTEQLLITLNSQVQQAAEE 3539
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL------DEELAELEAELEELEAEREELAAK 171
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1823-1991 |
1.46e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 43.97 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1823 KKLLEEVLAEKDNVEDLNDNCELLMEQS--ACTRIRDQTIETQANYTKLLTSAQGLVAKIEKNLSDHtEFLNYKKEMDAW 1900
Cdd:cd00176 43 EALEAELAAHEERVEALNELGEQLIEEGhpDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQW 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1901 IEKAQQVLDDCSTDGDAAIIAQKLDTVNSLASRLPEGQHLLALVQDAYSKASNITPEDKQEKLRELMTKVREDWDALGLA 1980
Cdd:cd00176 122 LEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLEL 201
|
170
....*....|.
gi 442626145 1981 VKQKLSDLKQA 1991
Cdd:cd00176 202 AEERQKKLEEA 212
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
3451-3564 |
1.55e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3451 PSAEAIQAKVDKLVEQ----------QAKLNDTLR--DKEQQVSKDLEE----IEQVFRRISQLQDKLNALHEQLQSVHV 3514
Cdd:PRK11281 36 PTEADVQAQLDALNKQklleaedklvQQDLEQTLAllDKIDRQKEETEQlkqqLAQAPAKLRQAQAELEALKDDNDEETR 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 442626145 3515 YD---EHIAQTEQLLITLNSQVQQA----AEESKLLVAQTTAHYQAkQNQLPSDIAQ 3564
Cdd:PRK11281 116 ETlstLSLRQLESRLAQTLDQLQNAqndlAEYNSQLVSLQTQPERA-QAALYANSQR 171
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1271-1462 |
1.89e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 43.59 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1271 FYQSLKDVEKELQLEQQALNRNEDVDSILQRNQQF----LLQQDVVPRLERcLQNMQRLAQAHRQQQPGDIS-LDQAYDN 1345
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLkkheALEAELAAHEER-VEALNELGEQLIEEGHPDAEeIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1346 AKSQWQLLSNKLGDMRQTLQQIPAQWQgYHLKFNDMVDWMNGVDQSLKNIVNeVNTMEEFEKEKVVFQKICQDADNKRED 1425
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEAHEPR 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 442626145 1426 MKWLVKTLDSLLSYATEDEANLEQKKLEDLIARYKNL 1462
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEEL 198
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6798-7520 |
1.91e-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: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6798 RQREAERNaLQLRYIHLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELaRHCDDALAT-----------AMRMEQAS 6866
Cdd:TIGR02168 173 RRKETERK-LERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAEL-RELELALLVlrleelreeleELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6867 IGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKLLDAnsesLPTQPAAIEQLLGSLRAQRVQLGAQVS 6946
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR----LEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6947 ALESltvTQEELKEcisphDMKTIRQRNWLLWQQHADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQRLEQRVekd 7026
Cdd:TIGR02168 327 ELES---KLDELAE-----ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI--- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7027 advtamtnpEQAAKQLEQQVnSELQLRDKEREWLLSTSRELLTLYSEPEVRsQVQQQSDSLIdrwQRLKYLAKQKATKIG 7106
Cdd:TIGR02168 396 ---------ASLNNEIERLE-ARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELE---EELEELQEELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7107 ELKmtllRLEERIALIRAWLFEVESQLDKpLNFESYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDADSWR 7186
Cdd:TIGR02168 462 ALE----ELREELEEAEQALDAAERELAQ-LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7187 TQVNTSgLAASAQ-----NLEQRWKNVCSQSAERKARILTIWNLLQQLIKLTAEHKNWLGKQEsqiaGFERDQKSHSKHK 7261
Cdd:TIGR02168 537 AAIEAA-LGGRLQavvveNLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIE----GFLGVAKDLVKFD 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7262 LEERQ------------------MELRAKLEELESqSVNLrQLEQIYAKLAMSAGVEPENIQKLTLPTKVmvsmwRQLTP 7323
Cdd:TIGR02168 612 PKLRKalsyllggvlvvddldnaLELAKKLRPGYR-IVTL-DGDLVRPGGVITGGSAKTNSSILERRREI-----EELEE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7324 RCHALLDAIdkdaklmREFNNAQLEATNSLNAIQKALEQLPSAENQQTSK-AEPKAVLQRLESLEKKLQDAQQhvQQADN 7402
Cdd:TIGR02168 685 KIEELEEKI-------AELEKALAELRKELEELEEELEQLRKELEELSRQiSALRKDLARLEAEVEQLEERIA--QLSKE 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7403 LAQEAKTRTKQQPQLKQLLELVSAYTTLWQTVQTRIVTLKTTWLT-----RAAQAAASLPVSEAANAAVQVNTLSQRKLR 7477
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealDELRAELTLLNEEAANLRERLESLERRIAA 835
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 442626145 7478 QAQQMQRETSITAKDAYIME-LQTAITECQNNLDELQRTVVDKT 7520
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIEsLAAEIEELEELIEELESELEALL 879
|
|
| PRK13914 |
PRK13914 |
invasion associated endopeptidase; |
5074-5235 |
2.00e-03 |
|
invasion associated endopeptidase;
Pssm-ID: 237555 [Multi-domain] Cd Length: 481 Bit Score: 45.18 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 5074 KIVEDAVVSSPSeSPRTPMVELVIPTEVVELALVEDEEQQTTPRIPsPTEKSEVEQDIKSV-QTSPQHQPKLDET----A 5148
Cdd:PRK13914 137 KYLTDKVTSTPV-APTQEVKKETTTQQAAPAAETKTEVKQTTQATT-PAPKVAETKETPVVdQNATTHAVKSGDTiwalS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 5149 VQTSLEVQP-DNQENESQTLI-----VEITETEAQTTPRSEeqsVAVEISTTEIQTdvsgqpAETVEISSQTTVTTTIEK 5222
Cdd:PRK13914 215 VKYGVSVQDiMSWNNLSSSSIyvgqkLAIKQTANTATPKAE---VKTEAPAAEKQA------APVVKENTNTNTATTEKK 285
|
170
....*....|...
gi 442626145 5223 ELQTTPKDSPRAP 5235
Cdd:PRK13914 286 ETTTQQQTAPKAP 298
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
6824-7050 |
2.32e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6824 LDAMIQQLDQGEQQSKALQEQQQELarhcDD--ALATAMRMEQASIGQRISNLRAALKTwQGFLQRVTQLSESYEQRVNQ 6901
Cdd:PRK10929 50 LQSALNWLEERKGSLERAKQYQQVI----DNfpKLSAELRQQLNNERDEPRSVPPNMST-DALEQEILQVSSQLLEKSRQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6902 LQQEFGAAQKLLDANSEsLPTQPAA-------IEQLLGSL--------RAQRVQLGAQVSALESLtVTQEELKECISPHD 6966
Cdd:PRK10929 125 AQQEQDRAREISDSLSQ-LPQQQTEarrqlneIERRLQTLgtpntplaQAQLTALQAESAALKAL-VDELELAQLSANNR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6967 MKTIRQRNWLLWQQHADLDYQLANLINSIeerlsllsNYQiRYDRISQWLQRLEQRVEKDADVtamtnPEQAAKQLeqQV 7046
Cdd:PRK10929 203 QELARLRSELAKKRSQQLDAYLQALRNQL--------NSQ-RQREAERALESTELLAEQSGDL-----PKSIVAQF--KI 266
|
....
gi 442626145 7047 NSEL 7050
Cdd:PRK10929 267 NREL 270
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6405-6650 |
2.32e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6405 ERLRKATERLEGLAGDLHNREQLIDELKGAAKPLIESCDV-QIVEQIEsAVQEAVVAWNDTSENLQQLRTRYQRAVELWD 6483
Cdd:COG4913 624 EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVaSAEREIA-ELEAELERLDASSDDLAALEEQLEELEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6484 KYRNAsaavknsIDQQMDAVKSLEQPLDALQhakvcqdnlttqnDRILELRDIVAKIAADVGLDASALMQGELDALGQRL 6563
Cdd:COG4913 703 ELEEE-------LDELKGEIGRLEKELEQAE-------------EELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6564 AEcKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPkESEEQLAALRAHLQT--LARTEEQLRQLK 6641
Cdd:COG4913 763 VE-RELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADL-ESLPEYLALLDRLEEdgLPEYEERFKELL 840
|
....*....
gi 442626145 6642 ERHQNSEVA 6650
Cdd:COG4913 841 NENSIEFVA 849
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2923-3525 |
2.43e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2923 ELQSILAQQDDMIKLIEDQLAHLRQLLLLREQFIALINEIiafiMKYTDVIIDIENSPDSLEDKINKYDDVIVKIQ---- 2998
Cdd:PRK01156 191 KLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNA----MDDYNNLKSALNELSSLEDMKNRYESEIKTAEsdls 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2999 ---ECEGVLASANDKGQKIASEGNAADKNSITEQLqSLKNQLQNLRKAVESQRQKHQLQLESHKKMA---AELSEILDWL 3072
Cdd:PRK01156 267 melEKNNYYKELEERHMKIINDPVYKNRNYINDYF-KYKNDIENKKQILSNIDAEINKYHAIIKKLSvlqKDYNDYIKKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3073 HSHEGAAKSRPLLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEIGM----PSSLLEMLSEGRSLVASLPHE- 3147
Cdd:PRK01156 346 SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIqeidPDAIKKELNEINVKLQDISSKv 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3148 --LEEREKYLKNNRDSRLEYMQLVA---------------KFNDWVHEAELRLQNSQHGIDY-EHLVQDLDEHKiffgne 3209
Cdd:PRK01156 426 ssLNQRIRALRENLDELSRNMEMLNgqsvcpvcgttlgeeKSNHIINHYNEKKSRLEEKIREiEIEVKDIDEKI------ 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3210 apiRNLVHKQIQEAADKIWSSLNNYEQ-SELSAELAQFQTKLtNTLANAKTQqselekeaerwreYQQSIDRVKatiert 3288
Cdd:PRK01156 500 ---VDLKKRKEYLESEEINKSINEYNKiESARADLEDIKIKI-NELKDKHDK-------------YEEIKNRYK------ 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3289 kfvdepvqnlaglhfniqklSHAIGNVQSQNSDLTLVNQQaqslirqadarnRQLIEQDNaglNRSWQDLVRSleQRRDN 3368
Cdd:PRK01156 557 --------------------SLKLEDLDSKRTSWLNALAV------------ISLIDIET---NRSRSNEIKK--QLNDL 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3369 LQQLAEHWDGFENSLHAWEKALGRLEDKFRNVDPtvrSRRHLEDTKNAIQELREESNQLKSSHKEIEALSKSILTFlgev 3448
Cdd:PRK01156 600 ESRLQEIEIGFPDDKSYIDKSIREIENEANNLNN---KYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEI---- 672
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626145 3449 hkpSAEAIQAKvDKLVEQQAKLNDTLRDKEQQVSKdleeIEQVFRRISQLQDKLNALHEQLQSVHVYDEHIAQTEQL 3525
Cdd:PRK01156 673 ---TSRINDIE-DNLKKSRKALDDAKANRARLEST----IEILRTRINELSDRINDINETLESMKKIKKAIGDLKRL 741
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6257-6879 |
2.43e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6257 LRDQLQAIQEGISNQRKHQAKISVILDECEAAERQGADVLEKAVADCQAAGEELVISWQEIMRirqmlhtlpmrlkmsvs 6336
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR----------------- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6337 pvkLERDISQLQDDHAFLESKctniMAILRSRLAVWlryERQLELVHGSVQETDfmmelirvhgqvdyERLRKATERLEG 6416
Cdd:COG1196 300 ---LEQDIARLEERRRELEER----LEELEEELAEL---EEELEELEEELEELE--------------EELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6417 LAGDLHNREQLIDELKGAAKPLIEScdvqiVEQIESAVQEAVVAWNDTSENLQQLRTRYQRAVELWDKYRNASAAVKNSI 6496
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEE-----LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6497 DQQMDAVKSLEQPLDALQHAKVCQDNLTTQNDRIL-----ELRDIVAKIAADVGLDASALMQGELDALGQRLAECKDAIT 6571
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLaelleEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6572 TLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPKESEEQLAALRAHLQTL---ARTEEQLRQLKERHQNSE 6648
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagRATFLPLDKIRARAALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6649 VAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEALRlwrqylqhvqsflscaipedysslreqqqlc 6728
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA------------------------------- 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6729 aihQNLLISQQSVLSETPLESELSEQYKALTNLHNETLSRIMQRNGELERRVSgwnayRQQLAALLDWLRQREAERNALQ 6808
Cdd:COG1196 640 ---VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA-----EEELELEEALLAEEEEERELAE 711
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626145 6809 LRyihlKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHcDDALATAMRMEQASIGQRISNLRAALK 6879
Cdd:COG1196 712 AE----EERLEEELEEEALEEQLEAEREELLEELLEEEELLEE-EALEELPEPPDLEELERELERLEREIE 777
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
6403-6835 |
2.80e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6403 DYERLRKATERLEGLAGDLHNREQLIDELKGAAKpLIESCDVQIVEQIESAVQEAVVAWNDTSENLQQLRTRYQRAVELW 6482
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEE-ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6483 DKYRNASAAVKNSIDQQMDAVKSLEQPLDALQHAKVCQDNLTTqndrILELRDIVAKIAADVGLDASALMQGELDALGQR 6562
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL----LLIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6563 LAECKDAITTLANVAETQDKER-KELDKEVTLAKAYFNNVQQDISREAPQNPKESEE---QLAALRAHLQTLARTEEQLR 6638
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEElQALPALEELEEEELEELLAALGLPPDLSPEELLElldRIEELQELLREAEELEEELQ 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6639 QLKERHQNSEVAPSVASSDDDGILEVLALWQKiFQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQhvqsflscaIPEDY 6718
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEE---------LEEEL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6719 SSLREQQQLcaihqnllisqqsvlsetpLESELSEQYKALTNLHNETlsRIMQRNGELERRvsgwnayRQQLAALLDWLR 6798
Cdd:COG4717 435 EELEEELEE-------------------LEEELEELREELAELEAEL--EQLEEDGELAEL-------LQELEELKAELR 486
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 442626145 6799 QREAERNALQL---------RYIHLKRVPHLKHRLDAMIQQLDQGE 6835
Cdd:COG4717 487 ELAEEWAALKLalelleearEEYREERLPPVLERASEYFSRLTDGR 532
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
2389-2789 |
3.07e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 44.67 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2389 LGDEDTDLDDNIDKLESELMDAIAK-KQAGQNVIDGYRQGMADVQNWFDTLIKRM------DVLDRGSGLNcaqkmaaiN 2461
Cdd:pfam13166 87 LGEESIEIQEKIAKLKKEIKDHEEKlDAAEANLQKLDKEKEKLEADFLDECWKKIkrkknsALSEALNGFK--------Y 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2462 EIKNEYELqghpkIQELKGKAAQVAEVisnLDGQQVEEQMKSLDRR-FADLGKRIDRKSQLLDVTNKGVEGAK-----GE 2535
Cdd:pfam13166 159 EANFKSRL-----LREIEKDNFNAGVL---LSDEDRKAALATVFSDnKPEIAPLTFNVIDFDALEKAEILIQKvigksSA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2536 IDQLQN------WVKQQIEELQApkplgyTPKDAEARQQKIkslmkDAEAKQSLADVLEKRVANMQQelepveysQLESA 2609
Cdd:pfam13166 231 IEELIKnpdladWVEQGLELHKA------HLDTCPFCGQPL-----PAERKAALEAHFDDEFTEFQN--------RLQKL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2610 LRNLNTENRNLSGVLKA--ELDRALEASK-ARKSLENDLDKARQWLKT---KISEVRKLPVyhplTSAEIEKKIQENRKY 2683
Cdd:pfam13166 292 IEKVESAISSLLAQLPAvsDLASLLSAFElDVEDIESEAEVLNSQLDGlrrALEAKRKDPF----KSIELDSVDAKIESI 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2684 DDDAKQFNDSVlTDVQRQAANIMKDCDDADKAALQQILDEIAADYQTLKDESSKRGKSLDDLLQGRKAFEDSMKNMGDWL 2763
Cdd:pfam13166 368 NDLVASINELI-AKHNEITDNFEEEKNKAKKKLRLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEI 446
|
410 420
....*....|....*....|....*.
gi 442626145 2764 NEMETATEGELRTTSlpVLEEQLAHY 2789
Cdd:pfam13166 447 KELEAQLRDHKPGAD--EINKLLKAF 470
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6783-6973 |
3.30e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.82 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6783 WNAYRQQLAALLDWLRQREAERNALQLRyIHLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDAlATAMRM 6862
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6863 EQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQrVNQLQQEFGAAQKLLdaNSESLPTQPAAIEQLLGSLRAQRVQLG 6942
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAAL--ASEDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190
....*....|....*....|....*....|.
gi 442626145 6943 AQVSALESLTVTQEELKECISPHDMKTIRQR 6973
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEK 187
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3351-3570 |
3.75e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3351 LNRSWQDLVRsLEQRRDNLQQLAEHWDgfenslhAWEKALGRLE--DKFRNVDPTVRSRRHLEDTKNAIQELREESNQLK 3428
Cdd:COG4913 237 LERAHEALED-AREQIELLEPIRELAE-------RYAAARERLAelEYLRAALRLWFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3429 sshKEIEALSKSIltflgevhkpsaEAIQAKVDKLVEQQAKL-NDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHE 3507
Cdd:COG4913 309 ---AELERLEARL------------DALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442626145 3508 QL-QSVHVYDEHIAQTEQLLITLNSQVQQAAEEsklLVAQTTAHYQAKQNQlpSDIAQEFTALE 3570
Cdd:COG4913 374 PLpASAEEFAALRAEAAALLEALEEELEALEEA---LAEAEAALRDLRREL--RELEAEIASLE 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
6734-6998 |
3.80e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6734 LLISQQSVLSETPLESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLryih 6813
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6814 lkrvphlkhRLDAMIQQLDQGEQQskaLQEQQQELARHcddaLATAMRMEQASIGQRISNLRAALKtwqgfLQRVTQLSE 6893
Cdd:COG4942 84 ---------ELAELEKEIAELRAE---LEAQKEELAEL----LRALYRLGRQPPLALLLSPEDFLD-----AVRRLQYLK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6894 SYEQRVNQLQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLtvtQEELKEcisphDMKTIRQR 6973
Cdd:COG4942 143 YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEK-----ELAELAAE 214
|
250 260
....*....|....*....|....*
gi 442626145 6974 NWLLWQQHADLDYQLANLINSIEER 6998
Cdd:COG4942 215 LAELQQEAEELEALIARLEAEAAAA 239
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
6764-7063 |
4.00e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6764 ETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALqLRYIHLKRVPHLKHRLDAMIQQLDQgeqqskaLQE 6843
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKL-LPQANLLADETLADRLEELREELDA-------AQE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6844 QQQELARHcddalatamrmeqasiGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQefgaAQKLLDANSEslptq 6923
Cdd:COG3096 908 AQAFIQQH----------------GKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRR----LKQQIFALSE----- 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6924 paaieqllgsLRAQRVQLGAQVSAlESLTVTQ---EELKECISphDMKTIRQRNWLLWQQHADlDYQLANlinsiEERLS 7000
Cdd:COG3096 963 ----------VVQRRPHFSYEDAV-GLLGENSdlnEKLRARLE--QAEEARREAREQLRQAQA-QYSQYN-----QVLAS 1023
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626145 7001 LLSNYQIRYdrisQWLQRLEQRVEkDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWLLST 7063
Cdd:COG3096 1024 LKSSRDAKQ----QTLQELEQELE-ELGVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQ 1081
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
6724-7021 |
4.32e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6724 QQQLCAIHQNLLISQQSVLSETPLESELseqykaltnlhnETLSRIMQRNGELErrvsgwnAYRQQLAALLDWLRQREAE 6803
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQTL------------ALLDKIDRQKEETE-------QLKQQLAQAPAKLRQAQAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6804 RNALQLryihlKRVPHLKHRLDAM-IQQL-DQGEQQSKALQEQQQELARHCDDALATAMRME--QASIG---QRISNLRA 6876
Cdd:PRK11281 103 LEALKD-----DNDEETRETLSTLsLRQLeSRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPEraQAALYansQRLQQIRN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6877 ALKTwqgflQRVTQLSESYEQRvNQLQQEfgaaQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALES------ 6950
Cdd:PRK11281 178 LLKG-----GKVGGKALRPSQR-VLLQAE----QALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHqlqllq 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626145 6951 -------LTVTQEELKECISPHDMKTIrQRNWLLwQQHADLDYQLAN-LINSIeERLSLLSNYQIrydRISQWLQRLEQ 7021
Cdd:PRK11281 248 eainskrLTLSEKTVQEAQSQDEAARI-QANPLV-AQELEINLQLSQrLLKAT-EKLNTLTQQNL---RVKNWLDRLTQ 320
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3763-3976 |
5.51e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3763 GQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEACEEWDQCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQLgfcE 3842
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI---A 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3843 KTLADINVQKTKLRlsiEKLEVHFRNGMGGDPRL---SENVDDLVRVLDGLGELV----------KAKSQSLEQTLAQID 3909
Cdd:COG4942 94 ELRAELEAQKEELA---ELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAparreqaeelRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3910 VYQQQMQSLRQRIIQEEQQLRLVMAptylphDRERALAE---QQDLITQELDELLQSLSSVEDGIANMNQ 3976
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA------ERQKLLARlekELAELAAELAELQQEAEELEALIARLEA 234
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1663-2210 |
6.41e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1663 LEKEVTEVEKMFFNTMEHVKDRVGYLEDYSAKWNNYKTRLAELQEWANKVApKNIEALQSEDLTPEERVVKVQAFKRILG 1742
Cdd:TIGR04523 129 LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLE-KEKLNIQKNIDKIKNKLLKLELLLSNLK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1743 DRMKQLDLLAADASELAPKEGNIAEAKRLKGEitKLQEVLSAINRNVDHQAQAVQEDLVNWQQFQAGLQQIKPAVEQ-SE 1821
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKDNIEKKQQ--EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKiKE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1822 VKKLLEEVLAEkdnVEDLNDNCELLMEQSACTRIRDQ-----TIETQ-ANYTKLLTSAQGLVAKIEKNLSDHTeflNYKK 1895
Cdd:TIGR04523 286 LEKQLNQLKSE---ISDLNNQKEQDWNKELKSELKNQekkleEIQNQiSQNNKIISQLNEQISQLKKELTNSE---SENS 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1896 EMDAWIEKAQQVLDDCSTDGDaaiiaQKLDTVNSLASRLPE-GQHLLALVQDAYSKASNItpeDKQEKLRELMTKVREDW 1974
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQ-----SYKQEIKNLESQINDlESKIQNQEKLNQQKDEQI---KKLQQEKELLEKEIERL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1975 DALGLAVKQKLSDLKqaqNRWNDFAANKDKLEKWLNETETTLKVapeTKGELSEMKTLLERYKTlsnELKLKGNELEQLQ 2054
Cdd:TIGR04523 432 KETIIKNNSEIKDLT---NQDSVKELIIKNLDNTRESLETQLKV---LSRSINKIKQNLEQKQK---ELKSKEKELKKLN 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2055 SEARDLGTEVDAVNRLQSRCDKLKNDCSAHITALEQEMFDYNAYHQSLQDVEKWLL----------QISfQLMAHNSLFI 2124
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENlekeideknkEIE-ELKQTQKSLK 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2125 SNREQTQEQIKQHEALLVEIQKYQTNLDDLNAKGQAQIKRYESSTPAIrptvESQLKNIQDSYNSLLQTSVQIKNRLLES 2204
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKL----SSIIKNIKSKKNKLKQEVKQIKETIKEI 657
|
....*.
gi 442626145 2205 LAKFQE 2210
Cdd:TIGR04523 658 RNKWPE 663
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1508-2254 |
6.47e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1508 SLDRVNRLIEEQQYAINQLDHQRPHIMSMLQRGRDLIKDVhapafvNAEVKNLETGWNQAYTETSDKLQA-LKGTQAVWS 1586
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL------NKKIKDLGEEEQLRVKEKIGELEAeIASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1587 EFVDQKNDIFSMLQTAETELRSLTPLQTDPKNVSQDLKSKRDlnvqlqqashqllpklhALKSELAPLAapDKRPILEKE 1666
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD-----------------KLTEEYAELK--EELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1667 VTEVEKMFFNTMEHVKDRVGYLEDYSAKWNNYKTRLAELQEwankvapkniealqsedltpeervVKVQAFKRILGDRMK 1746
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE------------------------ELQRLSEELADLNAA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1747 QLDLLAADASELAPKEGNIAEAKRLKGEITKLQEVLSAINRnvdhQAQAVQEDLVNWQQFQAGLQQIKPAVEqSEVKKLL 1826
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ----ELYDLKEEYDRVEKELSKLQRELAEAE-AQARASE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1827 EEVLAEKDNVEDLNDNCELLMEQSActrirdQTIETQANYTKLLTSAQG--LVAKIEKNLSDHTEFLNYKKEMDAW---- 1900
Cdd:TIGR02169 504 ERVRGGRAVEEVLKASIQGVHGTVA------QLGSVGERYATAIEVAAGnrLNNVVVEDDAVAKEAIELLKRRKAGratf 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1901 -----IEKAQQVLDDCSTDGD--------------AAIIAQKL-DT--VNSL--ASRLPEGQHLLALVQDAYSKASNITP 1956
Cdd:TIGR02169 578 lplnkMRDERRDLSILSEDGVigfavdlvefdpkyEPAFKYVFgDTlvVEDIeaARRLMGKYRMVTLEGELFEKSGAMTG 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 1957 EDKQEKLRELMTKVREDwdalglAVKQKLSDLKQAQNRWNDFAANKDKLEKWLNETETTLKVAPETKGELS-EMKTLLER 2035
Cdd:TIGR02169 658 GSRAPRGGILFSRSEPA------ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkEIEQLEQE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2036 YKTLSNELKLKGNELEQLQSEARDLGTEVDAVN----RLQSRCDKLK---NDCSAH-----ITALEQEMFDYNAYHQS-- 2101
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEarieELEEDLHKLEealNDLEARlshsrIPEIQAELSKLEEEVSRie 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2102 --LQDVEKWLLQISFQLMAHNSL---FISNREQTQEQIKQHEALLVEIQKYQTNLDDLNAKGQAQIKRYESSTPAI---R 2173
Cdd:TIGR02169 812 arLREIEQKLNRLTLEKEYLEKEiqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLkkeR 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 2174 PTVESQLKNIQDSYNSLLQTSVQIKNRLLESLAKFQEYEDTLDSIMRNLETYEPIIQTELDAPatslELAQNQLRCAQEM 2253
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE----DVQAELQRVEEEI 967
|
.
gi 442626145 2254 Q 2254
Cdd:TIGR02169 968 R 968
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
7067-7312 |
6.61e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7067 LLTLYSEPEVRSQVQQQSDSLIDRWQRLKYLAKQKATKIGELKMTLLRLEERIALIRAWLFEVESQLdkplnfesytpNV 7146
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL-----------AA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7147 IEAKL----KEHEQIQRSIEHHSSNVGEVL---------NLVEMLLNDADSWRTQVNTSGLAASAQNLEQRWKNVCSQSA 7213
Cdd:COG4942 81 LEAELaeleKEIAELRAELEAQKEELAELLralyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7214 ERKARILTIWNLLQQLIKLTAEHKNWLGKQESQIAgfERDQKShskHKLEERQMELRAKLEELESQSVNLRQL------E 7287
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKA--ERQKLL---ARLEKELAELAAELAELQQEAEELEALiarleaE 235
|
250 260
....*....|....*....|....*
gi 442626145 7288 QIYAKLAMSAGVEPENIQKLTLPTK 7312
Cdd:COG4942 236 AAAAAERTPAAGFAALKGKLPWPVS 260
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
6542-6948 |
7.89e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6542 ADVGLDASALMQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDIsreapqnpkESEEQLA 6621
Cdd:COG3096 280 RRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTAL---------RQQEKIE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6622 ALRAHLQTLA-RTEEQLRQLKERHqnsevapsvassdddgilEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEAL-RLW 6699
Cdd:COG3096 351 RYQEDLEELTeRLEEQEEVVEEAA------------------EQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqTRA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6700 RQYLQHVQSflscaipedyssLREQQQLCAI----------HQNLLISQQSVLSETPLESE--LSEQyKALTNLHNETLS 6767
Cdd:COG3096 413 IQYQQAVQA------------LEKARALCGLpdltpenaedYLAAFRAKEQQATEEVLELEqkLSVA-DAARRQFEKAYE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6768 RIMQRNGELERRvSGWNAYRQQLAallDWLRQR-EAER-NALQLRYIHLKRVPHLKHRLDAMIQQLDQGEQQS------- 6838
Cdd:COG3096 480 LVCKIAGEVERS-QAWQTARELLR---RYRSQQaLAQRlQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQldaaeel 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 6839 KALQEQQQELARHCDDALATA------MRMEQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKL 6912
Cdd:COG3096 556 EELLAELEAQLEELEEQAAEAveqrseLRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQL 635
|
410 420 430
....*....|....*....|....*....|....*.
gi 442626145 6913 LDANSEslptqpaaIEQLLGSLRAQRVQLGAQVSAL 6948
Cdd:COG3096 636 LERERE--------ATVERDELAARKQALESQIERL 663
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
279-363 |
8.25e-03 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 39.97 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 279 NWINSYLLKR-VPPLRIDDLINDLRDGTKLIALLEVLSGER-LPVEKGRVLRRPHFLSNANTALQFLasKRIKLVN-INP 355
Cdd:cd21218 17 RWVNYHLKKAgPTKKRVTNFSSDLKDGEVYALLLHSLAPELcDKELVLEVLSEEDLEKRAEKVLQAA--EKLGCKYfLTP 94
|
....*...
gi 442626145 356 ADLVDGRP 363
Cdd:cd21218 95 EDIVSGNP 102
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3322-3512 |
8.62e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3322 LTLVNQQAQSLIRQADARNRQliEQDNAGLnRSWQDlVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFRNVd 3401
Cdd:COG4913 254 LEPIRELAERYAAARERLAEL--EYLRAAL-RLWFA-QRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3402 ptvrSRRHLEDTKNAIQELREESNQLKSSHKEIEALSKSILTFLGEVHKPSAEAIQAkvdkLVEQQAKLNDTLRDKEQQV 3481
Cdd:COG4913 329 ----EAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE----FAALRAEAAALLEALEEEL 400
|
170 180 190
....*....|....*....|....*....|.
gi 442626145 3482 SKDLEEIEQVFRRISQLQDKLNALHEQLQSV 3512
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3146-3559 |
8.88e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3146 HELEEREKYLKNNRDSRLEYMQLVAKFNDWVHEAELRLQNSQHGIDYEHLVQDLDEHKiFFGNEAPIRNLVHKQIQEAAD 3225
Cdd:COG4717 102 EELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3226 KIWSSLNNYEQSELSaelaqfqtKLTNTLANAKTQQSELEKEAERWREYQQSIDRVKATIERTKFVDEPVQNL------- 3298
Cdd:COG4717 181 ELLEQLSLATEEELQ--------DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLkearlll 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3299 --AGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIRQADARNRQLIEQDNAGLNRSWqdlvrsleqRRDNLQQLaehw 3376
Cdd:COG4717 253 liAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALP---------ALEELEEE---- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3377 dgfenSLHAWEKALGRLEDkfRNVDPTVRSRRHLEDTKNAIQELREESNQLksshkEIEALSKSILTFLGEVHKPSAEAI 3456
Cdd:COG4717 320 -----ELEELLAALGLPPD--LSPEELLELLDRIEELQELLREAEELEEEL-----QLEELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 3457 QAKVDKLVEQQAKLN-------------------------DTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQS 3511
Cdd:COG4717 388 RAALEQAEEYQELKEeleeleeqleellgeleellealdeEELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 442626145 3512 VHVYDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAHYQAKQNQLP 3559
Cdd:COG4717 468 DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
7730-7798 |
9.29e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 39.24 E-value: 9.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7730 EFHQTIGELVEWLQRTEQNIKASE-PVDLTEersvLETKFKKFKDLRAELERCEPRVVSLQDAADQLLRS 7798
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASEDlGKDLES----VEALLKKHEAFEAELEAHEERVEALNELGEQLIEE 67
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
7114-7219 |
9.56e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 39.24 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626145 7114 RLEERIALIRAWLFEVESQLDKPLNFESytPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDADSwrtqvNTSG 7193
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASEDLGKD--LESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-----DAEE 74
|
90 100
....*....|....*....|....*.
gi 442626145 7194 LAASAQNLEQRWKNVCSQSAERKARI 7219
Cdd:smart00150 75 IEERLEELNERWEELKELAEERRQKL 100
|
|
| |
