|
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 |
2.26e-72 |
|
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: 239.20 E-value: 2.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 268 EQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKR 347
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|...
gi 320544548 348 IKLVNINPADLVDGRPPVVLGLIWTIILYFQIE 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 ... |
415-523 |
3.81e-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: 212.56 E-value: 3.81e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 415 KWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAK 494
Cdd:cd21243 1 KFKGGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPR 80
|
90 100
....*....|....*....|....*....
gi 320544548 495 LLDAEDVDVPKPDEKSIMTYVAQFLHKYP 523
Cdd:cd21243 81 LLDPEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
268-380 |
2.82e-48 |
|
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: 170.06 E-value: 2.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 268 EQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKR 347
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|...
gi 320544548 348 IKLVNINPADLVDGRPPVVLGLIWTIILYFQIE 380
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQIE 113
|
|
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
270-378 |
2.40e-43 |
|
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: 155.64 E-value: 2.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 270 ERVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASKRIK 349
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKA--RRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRM--RFHRLQNVQTALDFLKYRKIK 76
|
90 100
....*....|....*....|....*....
gi 320544548 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 |
2.73e-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: 147.28 E-value: 2.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 268 EQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGrvLRRPHFLSNANTALQFLASKR 347
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKG--HNVFQCRSNIETALSFLKNKS 78
|
90 100 110
....*....|....*....|....*....|...
gi 320544548 348 IKLVNINPADLVDGRPPVVLGLIWTIILYFQIE 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 |
2.49e-38 |
|
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: 141.74 E-value: 2.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 262 ILQLQEEQERVQKKTFTNWINSYLlKRVPpLRIDDLINDLRDGTKLIALLEVLSGERLP-VEKGRVlrRPHFLSNANTAL 340
Cdd:cd21246 6 IKALADEREAVQKKTFTKWVNSHL-ARVG-CRINDLYTDLRDGRMLIKLLEVLSGERLPkPTKGKM--RIHCLENVDKAL 81
|
90 100 110
....*....|....*....|....*....|....*
gi 320544548 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 |
2.77e-36 |
|
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: 135.89 E-value: 2.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 261 TILQLQEEQERVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLP-VEKGRVlrRPHFLSNANTA 339
Cdd:cd21193 5 RIRALQEERINIQKKTFTKWINSFLEKA--NLEIGDLFTDLSDGKLLLKLLEIISGEKLGkPNRGRL--RVQKIENVNKA 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 320544548 340 LQFLASKrIKLVNINPADLVDGRPPVVLGLIWTIIL 375
Cdd:cd21193 81 LAFLKTK-VRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
417-523 |
3.54e-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: 135.24 E-value: 3.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 417 KQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLL 496
Cdd:cd21192 1 QGSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLL 80
|
90 100
....*....|....*....|....*..
gi 320544548 497 DAEDVDVPKPDEKSIMTYVAQFLHKYP 523
Cdd:cd21192 81 EVEDVLVDKPDERSIMTYVSQFLRMFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
272-379 |
4.10e-36 |
|
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: 135.20 E-value: 4.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 272 VQKKTFTNWINSYLLKRVPPLrIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASKRIKLV 351
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKPP-IKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRM--RVHHLNNVNRALQVLEQNNVKLV 78
|
90 100
....*....|....*....|....*...
gi 320544548 352 NINPADLVDGRPPVVLGLIWTIILYFQI 379
Cdd:cd21186 79 NISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
415-519 |
9.71e-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: 9.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 415 KWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAK 494
Cdd:cd21244 1 RWKMSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPR 80
|
90 100
....*....|....*....|....*
gi 320544548 495 LLDAEDVDVPKPDEKSIMTYVAQFL 519
Cdd:cd21244 81 LLEPEDVDVVNPDEKSIMTYVAQFL 105
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
420-523 |
1.05e-33 |
|
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: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21189 2 AKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDPE 81
|
90 100
....*....|....*....|....
gi 320544548 500 DVDVPKPDEKSIMTYVAQFLHKYP 523
Cdd:cd21189 82 DVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
258-381 |
1.52e-33 |
|
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: 128.56 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 258 YQMTILQLQEEQERVQKKTFTNWINSYLLKRVPplRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNAN 337
Cdd:cd21236 3 YENVLERYKDERDKVQKKTFTKWINQHLMKVRK--HVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRM--RFHRLQNVQ 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 320544548 338 TALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTIILYFQIEE 381
Cdd:cd21236 79 IALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISD 122
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
264-546 |
1.10e-32 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 139.31 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 264 QLQEEQERVQKKTFTNWINSYLLKRVPPlRIDDLINDLRDGTKLIALLEVLSGERLpVEKGRVLR-RPHFLSNANTALQF 342
Cdd:COG5069 1 MEAKKWQKVQKKTFTKWTNEKLISGGQK-EFGDLDTDLKDGVKLAQLLEALQKDNA-GEYNETPEtRIHVMENVSGRLEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 343 LASKRIKLVNINPADLVDGRPPVVLGLIWTIILYFQIEENSRNLEYLGHgiggsvSSLDSVGNQKHGDLKAEkwkqgark 422
Cdd:COG5069 79 IKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGELTKH------INLLLWCDEDTGGYKPE-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 423 tllnwvtnalpkdsgVEVKDFGASWRDGVAFLALI-----DAIKANLVNLAELKKTSNRQRletAFDVAESKLGIAKLLD 497
Cdd:COG5069 145 ---------------VDTFDFFRSWRDGLAFSALIhdsrpDTLDPNVLDLQKKNKALNNFQ---AFENANKVIGIARLIG 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 320544548 498 AEDV-DVPKPDEKSIMTYVAQFLHKYpepkgasRDQSHVQQEADELRRFL 546
Cdd:COG5069 207 VEDIvNVSIPDERSIMTYVSWYIIRF-------GLLEKIDIALHRVYRLL 249
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
420-522 |
1.99e-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: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21194 3 AKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDAE 82
|
90 100
....*....|....*....|...
gi 320544548 500 DVDVPKPDEKSIMTYVAQFLHKY 522
Cdd:cd21194 83 DVDVARPDEKSIMTYVASYYHYF 105
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
270-375 |
3.34e-32 |
|
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: 124.04 E-value: 3.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 270 ERVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLP-VEKGRVlrRPHFLSNANTALQFLASKRI 348
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKA--GTQIENIEEDFRDGLKLMLLLEVISGERLPkPERGKM--RFHKIANVNKALDFIASKGV 78
|
90 100
....*....|....*....|....*..
gi 320544548 349 KLVNINPADLVDGRPPVVLGLIWTIIL 375
Cdd:cd21214 79 KLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
420-523 |
2.96e-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: 121.44 E-value: 2.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKdSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21245 4 AIKALLNWVQRRTRK-YGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPE 82
|
90 100
....*....|....*....|....
gi 320544548 500 DVDVPKPDEKSIMTYVAQFLHKYP 523
Cdd:cd21245 83 DVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
267-379 |
2.99e-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: 2.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 267 EEQERVQKKTFTNWINSYLLKrvPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASK 346
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLRHR 76
|
90 100 110
....*....|....*....|....*....|...
gi 320544548 347 RIKLVNINPADLVDGRPPVVLGLIWTIILYFQI 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 |
4.88e-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: 4.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 262 ILQLQEEQERVQKKTFTNWINSYLLKrvPPLRIDDLINDLRDGTKLIALLEVLSGERLPV-EKGRVlrRPHFLSNANTAL 340
Cdd:cd21318 28 IKALADEREAVQKKTFTKWVNSHLAR--VPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRM--RIHSLENVDKAL 103
|
90 100 110
....*....|....*....|....*....|....*
gi 320544548 341 QFLASKRIKLVNINPADLVDGRPPVVLGLIWTIIL 375
Cdd:cd21318 104 QFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
262-375 |
1.83e-30 |
|
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: 120.16 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 262 ILQLQEEQERVQKKTFTNWINSYLlKRVPpLRIDDLINDLRDGTKLIALLEVLSGERLPV-EKGRVlrRPHFLSNANTAL 340
Cdd:cd21317 21 IKALADEREAVQKKTFTKWVNSHL-ARVT-CRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRM--RIHCLENVDKAL 96
|
90 100 110
....*....|....*....|....*....|....*
gi 320544548 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 |
3.31e-30 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 118.45 E-value: 3.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 268 EQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKR 347
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 320544548 348 IKLVNINPADLVDGRPPVVLGLIWTIILYFQIEE 381
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
267-381 |
4.07e-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: 115.52 E-value: 4.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 267 EEQERVQKKTFTNWINSYLLKRVPplRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASK 346
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRK--HINDLYEDLRDGHNLISLLEVLSGVKLPREKGRM--RFHRLQNVQIALDFLKQR 76
|
90 100 110
....*....|....*....|....*....|....*
gi 320544548 347 RIKLVNINPADLVDGRPPVVLGLIWTIILYFQIEE 381
Cdd:cd21237 77 QVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISD 111
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
420-520 |
1.60e-28 |
|
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: 113.26 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21248 3 AKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDPE 82
|
90 100
....*....|....*....|.
gi 320544548 500 DVDVPKPDEKSIMTYVAQFLH 520
Cdd:cd21248 83 DVNVEQPDEKSIITYVVTYYH 103
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
268-380 |
1.72e-28 |
|
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: 113.48 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 268 EQERVQKKTFTNWINSYLLK-RVPPlrIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASK 346
Cdd:cd21231 2 EREDVQKKTFTKWINAQFAKfGKPP--IEDLFTDLQDGRRLLELLEGLTGQKLVKEKGST--RVHALNNVNKALQVLQKN 77
|
90 100 110
....*....|....*....|....*....|....
gi 320544548 347 RIKLVNINPADLVDGRPPVVLGLIWTIILYFQIE 380
Cdd:cd21231 78 NVDLVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
270-377 |
1.29e-27 |
|
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: 110.95 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 270 ERVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLpvekGRVLRRP----HFLSNANTALQFLAS 345
Cdd:cd21215 2 VDVQKKTFTKWLNTKLSSR--GLSITDLVTDLSDGVRLIQLLEIIGDESL----GRYNKNPkmrvQKLENVNKALEFIKS 75
|
90 100 110
....*....|....*....|....*....|..
gi 320544548 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) ... |
417-520 |
2.98e-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: 109.95 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 417 KQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLL 496
Cdd:cd21249 2 LRSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLL 81
|
90 100
....*....|....*....|....
gi 320544548 497 DAEDVDVPKPDEKSIMTYVAQFLH 520
Cdd:cd21249 82 DPEDVAVPHPDERSIMTYVSLYYH 105
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
262-379 |
3.50e-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: 110.23 E-value: 3.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 262 ILQLQEEQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPV-EKGRVlrRPHFLSNANTAL 340
Cdd:cd21247 10 IRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKM--RVHFLENNSKAI 87
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 320544548 341 QFLASK-RIKLvnINPADLVDGRPPVVLGLIWTIILYFQI 379
Cdd:cd21247 88 TFLKTKvPVKL--IGPENIVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
422-523 |
4.16e-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: 109.44 E-value: 4.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 422 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDV 501
Cdd:cd21187 3 KTLLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDV 82
|
90 100
....*....|....*....|..
gi 320544548 502 DVPKPDEKSIMTYVAQFLHKYP 523
Cdd:cd21187 83 NVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
420-522 |
6.73e-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: 108.99 E-value: 6.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21216 11 AKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKMLDAE 90
|
90 100
....*....|....*....|....
gi 320544548 500 D-VDVPKPDEKSIMTYVAQFLHKY 522
Cdd:cd21216 91 DiVNTPRPDERSVMTYVSCYYHAF 114
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
420-522 |
1.48e-26 |
|
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: 108.38 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21291 11 AKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGIPQLLDVE 90
|
90 100
....*....|....*....|....
gi 320544548 500 DV-DVPKPDEKSIMTYVAQFLHKY 522
Cdd:cd21291 91 DVcDVAKPDERSIMTYVAYYFHAF 114
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
418-526 |
1.39e-25 |
|
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: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 418 QGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLD 497
Cdd:cd21319 4 RSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLD 83
|
90 100
....*....|....*....|....*....
gi 320544548 498 AEDVDVPKPDEKSIMTYVAQFLHKYPEPK 526
Cdd:cd21319 84 PEDVFTENPDEKSIITYVVAFYHYFSKMK 112
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
272-379 |
1.65e-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: 105.06 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 272 VQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKRIKLV 351
Cdd:cd21227 4 IQKNTFTNWVNEQL--KPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIKLV 81
|
90 100
....*....|....*....|....*...
gi 320544548 352 NINPADLVDGRPPVVLGLIWTIILYFQI 379
Cdd:cd21227 82 NIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| KASH |
pfam10541 |
Nuclear envelope localization domain; The KASH (for Klarsicht/ANC-1/Syne-1 homology) or KLS ... |
11943-11999 |
2.89e-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: 2.89e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 320544548 11943 FLGRVARASLPIQALMLLLLGVATLVPHG-EDYTCMFSNTFARSLEPMLSYPHGPPPT 11999
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 |
1.48e-24 |
|
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: 102.17 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 271 RVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLpveKGRVLRRP----HFLSNANTALQFLASK 346
Cdd:cd21183 3 RIQANTFTRWCNEHLKER--GMQIHDLATDFSDGLCLIALLENLSTRPL---KRSYNRRPafqqHYLENVSTALKFIEAD 77
|
90 100 110
....*....|....*....|....*....|.
gi 320544548 347 RIKLVNINPADLVDGRPPVVLGLIWTIILYF 377
Cdd:cd21183 78 HIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
272-380 |
1.51e-24 |
|
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: 102.39 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 272 VQKKTFTNWINSYLLKRVPPlRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASKRIKLV 351
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKP-PIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGST--RVHALNNVNRVLQVLHQNNVELV 78
|
90 100
....*....|....*....|....*....
gi 320544548 352 NINPADLVDGRPPVVLGLIWTIILYFQIE 380
Cdd:cd21232 79 NIGGTDIVDGNHKLTLGLLWSIILHWQVK 107
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
262-375 |
2.71e-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: 103.20 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 262 ILQLQEEQERVQKKTFTNWINSYLLKrvPPLRIDDLINDLRDGTKLIALLEVLSGERLPV-EKGRVlrRPHFLSNANTAL 340
Cdd:cd21316 43 IKALADEREAVQKKTFTKWVNSHLAR--VSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRM--RIHCLENVDKAL 118
|
90 100 110
....*....|....*....|....*....|....*
gi 320544548 341 QFLASKRIKLVNINPADLVDGRPPVVLGLIWTIIL 375
Cdd:cd21316 119 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
415-527 |
2.90e-24 |
|
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: 101.67 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 415 KWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAK 494
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100 110
....*....|....*....|....*....|...
gi 320544548 495 LLDAEDVDVPKPDEKSIMTYVAQFLHKYPEPKG 527
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKMKA 113
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
270-379 |
7.81e-24 |
|
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: 100.60 E-value: 7.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 270 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLAS-KRI 348
Cdd:cd21311 13 KRIQQNTFTRWANEHL--KTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEEdEGI 90
|
90 100 110
....*....|....*....|....*....|.
gi 320544548 349 KLVNINPADLVDGRPPVVLGLIWTIILYFQI 379
Cdd:cd21311 91 KIVNIDSSDIVDGKLKLILGLIWTLILHYSI 121
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
420-523 |
2.61e-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: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAEsKLGIAKLLDAE 499
Cdd:cd21239 2 AKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAE-KLGVTRLLDPE 80
|
90 100
....*....|....*....|....
gi 320544548 500 DVDVPKPDEKSIMTYVAQFLHKYP 523
Cdd:cd21239 81 DVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
420-523 |
3.94e-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: 3.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGIAKLLDAE 499
Cdd:cd21240 5 AKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAE 83
|
90 100
....*....|....*....|....
gi 320544548 500 DVDVPKPDEKSIMTYVAQFLHKYP 523
Cdd:cd21240 84 DVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
419-520 |
1.45e-22 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 96.15 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 419 GARKTLLNWVTNALPKDSgveVKDFGASWRDGVAFLALIDAIKANL-VNLAELKKTSNRQRLETAFDVAESKLGIAKLLD 497
Cdd:cd21184 1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLiPDNESLDKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|...
gi 320544548 498 AEDVDVPKPDEKSIMTYVAQFLH 520
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSYFRN 100
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
422-522 |
3.17e-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: 95.22 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 422 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDV 501
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 320544548 502 DVPKPDEKSIMTYVAQFLHKY 522
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
420-523 |
7.73e-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: 7.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21238 3 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 82
|
90 100
....*....|....*....|....
gi 320544548 500 DVDVPKPDEKSIMTYVAQFLHKYP 523
Cdd:cd21238 83 DVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
270-377 |
6.51e-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: 91.78 E-value: 6.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 270 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVE-KGRVLRRPHFLSNANTALQFLASKRI 348
Cdd:cd21228 2 KKIQQNTFTRWCNEHL--KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKyNKRPTFRQMKLENVSVALEFLERESI 79
|
90 100
....*....|....*....|....*....
gi 320544548 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 ... |
420-523 |
8.10e-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: 8.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKD-SGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKT--SNRQRLETAFDVAESKLGIAK-L 495
Cdd:pfam00307 3 LEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVPKvL 82
|
90 100
....*....|....*....|....*...
gi 320544548 496 LDAEDVDvpKPDEKSIMTYVAQFLHKYP 523
Cdd:pfam00307 83 IEPEDLV--EGDNKSVLTYLASLFRRFQ 108
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
272-379 |
9.74e-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: 91.19 E-value: 9.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 272 VQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKgRVLRRPHFLSNANTALQFLASK-RIKL 350
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK-LNKSEFDKLENINLALDVAEKKlGVPK 80
|
90 100
....*....|....*....|....*....
gi 320544548 351 VNINPADLVDGRPPVVLGLIWTIILYFQI 379
Cdd:pfam00307 81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
437-522 |
2.17e-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: 90.10 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 437 GVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAED-VDVPKPDEKSIMTYV 515
Cdd:cd21253 19 DVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVALKVPDKLSILTYV 98
|
....*..
gi 320544548 516 AQFlHKY 522
Cdd:cd21253 99 SQY-YNY 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
418-527 |
2.98e-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: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 418 QGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLD 497
Cdd:cd21322 16 RSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHLGLTKLLD 95
|
90 100 110
....*....|....*....|....*....|
gi 320544548 498 AEDVDVPKPDEKSIMTYVAQFLHKYPEPKG 527
Cdd:cd21322 96 PEDVNMEAPDEKSIITYVVSFYHYFSKMKA 125
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
418-522 |
1.16e-19 |
|
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: 88.23 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 418 QGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLD 497
Cdd:cd21320 1 KSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 80
|
90 100
....*....|....*....|....*
gi 320544548 498 AEDVDVPKPDEKSIMTYVAQFLHKY 522
Cdd:cd21320 81 PEDISVDHPDEKSIITYVVTYYHYF 105
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
420-522 |
9.06e-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: 86.32 E-value: 9.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21289 11 AKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAE 90
|
90 100
....*....|....*....|....
gi 320544548 500 D-VDVPKPDEKSIMTYVAQFLHKY 522
Cdd:cd21289 91 DiVNTPKPDEKAIMTYVSCFYHAF 114
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
420-522 |
1.11e-18 |
|
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: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21287 11 AKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDAE 90
|
90 100
....*....|....*....|....
gi 320544548 500 D-VDVPKPDEKSIMTYVAQFLHKY 522
Cdd:cd21287 91 DiVGTARPDEKAIMTYVSSFYHAF 114
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
420-523 |
1.58e-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: 85.01 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21234 1 SEKILLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPE 80
|
90 100
....*....|....*....|....
gi 320544548 500 DVDVPKPDEKSIMTYVAQFLHKYP 523
Cdd:cd21234 81 DVAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
420-522 |
1.60e-18 |
|
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: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAE 80
|
90 100
....*....|....*....|....
gi 320544548 500 D-VDVPKPDEKSIMTYVAQFLHKY 522
Cdd:cd21197 81 DmVTMHVPDRLSIITYVSQYYNHF 104
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
270-379 |
1.83e-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: 85.47 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 270 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLpveKGRVLRRPHF----LSNANTALQFLAS 345
Cdd:cd21310 14 KKIQQNTFTRWCNEHL--KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKM---YRKYHPRPNFrqmkLENVSVALEFLDR 88
|
90 100 110
....*....|....*....|....*....|....
gi 320544548 346 KRIKLVNINPADLVDGRPPVVLGLIWTIILYFQI 379
Cdd:cd21310 89 EHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 122
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
273-377 |
2.56e-18 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 84.17 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 273 QKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPvekgRVLRRP----HFLSNANTALQFLASKRI 348
Cdd:cd21212 1 EIEIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVP----GIHSRPktraQKLENIQACLQFLAALGV 76
|
90 100
....*....|....*....|....*....
gi 320544548 349 KLVNINPADLVDGRPPVVLGLIWTIILYF 377
Cdd:cd21212 77 DVQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
420-524 |
1.97e-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: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNL-AELKKTSNRQRLETAFDVAESKLGIAKLLDA 498
Cdd:cd21233 1 SEKILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWnSVVSQQSATERLDHAFNIARQHLGIEKLLDP 80
|
90 100
....*....|....*....|....*.
gi 320544548 499 EDVDVPKPDEKSIMTYVAQFLHKYPE 524
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 ... |
422-518 |
6.06e-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: 6.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 422 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTS---NRQRletAFDVAESKLGIAKLLDA 498
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENiaeNNQL---AFDVAEQELGIPPVMTG 79
|
90 100
....*....|....*....|.
gi 320544548 499 ED-VDVPKPDEKSIMTYVAQF 518
Cdd:cd22198 80 QEmASLAVPDKLSMVSYLSQF 100
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
420-525 |
1.05e-16 |
|
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: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|....*..
gi 320544548 500 D-VDVPKPDEKSIMTYVAQFLHKYPEP 525
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYYNHFSNP 107
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
420-522 |
1.29e-16 |
|
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: 80.13 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21290 14 AKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAE 93
|
90 100
....*....|....*....|....
gi 320544548 500 D-VDVPKPDEKSIMTYVAQFLHKY 522
Cdd:cd21290 94 DiVNTARPDEKAIMTYVSSFYHAF 117
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
424-518 |
2.39e-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: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 424 LLNWVTNALPKDSgveVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQR-LETAFDVAESKLGIAKLLDAEDVD 502
Cdd:cd21230 6 LLGWIQNKIPQLP---ITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDALEnATEAMQLAEDWLGVPQLITPEEII 82
|
90
....*....|....*.
gi 320544548 503 VPKPDEKSIMTYVAQF 518
Cdd:cd21230 83 NPNVDEMSVMTYLSQF 98
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
420-522 |
4.63e-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: 4.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21288 11 AKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAE 90
|
90 100
....*....|....*....|....
gi 320544548 500 D-VDVPKPDEKSIMTYVAQFLHKY 522
Cdd:cd21288 91 DiVNTPKPDERAIMTYVSCFYHAF 114
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
422-518 |
1.06e-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: 76.59 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 422 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNR----QRLETAFDVAESKLGIAKLLD 497
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 320544548 498 AEDVDVPKPDEKSIMTYVAQF 518
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
270-379 |
1.21e-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: 77.81 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 270 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLpveKGRVLRRPHF----LSNANTALQFLAS 345
Cdd:cd21309 15 KKIQQNTFTRWCNEHL--KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRM---YRKYHQRPTFrqmqLENVSVALEFLDR 89
|
90 100 110
....*....|....*....|....*....|....
gi 320544548 346 KRIKLVNINPADLVDGRPPVVLGLIWTIILYFQI 379
Cdd:cd21309 90 ESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSI 123
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
274-375 |
2.72e-15 |
|
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: 75.45 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 274 KKTFTNWINSyLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLAS-KRIKLVN 352
Cdd:cd00014 1 EEELLKWINE-VLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKlGLPELDL 79
|
90 100
....*....|....*....|....
gi 320544548 353 INPADLV-DGRPPVVLGLIWTIIL 375
Cdd:cd00014 80 FEPEDLYeKGNLKKVLGTLWALAL 103
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
270-379 |
4.63e-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: 75.89 E-value: 4.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 270 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLpveKGRVLRRPHF----LSNANTALQFLAS 345
Cdd:cd21308 18 KKIQQNTFTRWCNEHL--KCVSKRIANLQTDLSDGLRLIALLEVLSQKKM---HRKHNQRPTFrqmqLENVSVALEFLDR 92
|
90 100 110
....*....|....*....|....*....|....
gi 320544548 346 KRIKLVNINPADLVDGRPPVVLGLIWTIILYFQI 379
Cdd:cd21308 93 ESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 126
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
270-373 |
4.88e-15 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 75.26 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 270 ERVQKKTFTNWINSYLLKRVPPlRIDDLINDLRDGTKLIALLEVLSGERLPVE-----KGRVLRrphfLSNANTALQFLA 344
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGIP-KISDLATDLSDGVRLIFFLELVSGKKFPKKfdlepKNRIQM----IQNLHLAMLFIE 76
|
90 100 110
....*....|....*....|....*....|
gi 320544548 345 SK-RIKLVNINPADLVDGRPPVVLGLIWTI 373
Cdd:cd21225 77 EDlKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
419-521 |
6.14e-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: 6.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 419 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDA 498
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|....*
gi 320544548 499 EDVDV--PKPDEKSIMTYVAQFLHK 521
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLYRH 105
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
275-376 |
1.52e-14 |
|
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: 73.50 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 275 KTFTNWINSYLLKRVPPlRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRP-HFLSNANTALQFLASKRIKLVNI 353
Cdd:smart00033 1 KTLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfKKIENINLALSFAEKLGGKVVLF 79
|
90 100
....*....|....*....|...
gi 320544548 354 NPADLVDGrPPVVLGLIWTIILY 376
Cdd:smart00033 80 EPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
273-377 |
1.79e-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: 73.49 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 273 QKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLP----VEKGRVLRRphflSNANTALQFLASKRI 348
Cdd:cd21213 1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPgidwNPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 320544548 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 ... |
422-517 |
1.74e-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: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 422 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAEsKLGIAKLLDAED- 500
Cdd:cd21198 4 QDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAA-KLGIPRLLDPADm 82
|
90
....*....|....*..
gi 320544548 501 VDVPKPDEKSIMTYVAQ 517
Cdd:cd21198 83 VLLSVPDKLSVMTYLHQ 99
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
419-517 |
3.80e-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: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 419 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGIAKLLDA 498
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|
gi 320544548 499 ED-VDVPKPDEKSIMTYVAQ 517
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQ 99
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
421-524 |
8.67e-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: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 421 RKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGIAKLLDAED 500
Cdd:cd21199 10 RNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAES-VGIPTTLTIDE 88
|
90 100
....*....|....*....|....*
gi 320544548 501 -VDVPKPDEKSIMTYVAQfLHKYPE 524
Cdd:cd21199 89 mVSMERPDWQSVMSYVTA-IYKHFE 112
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
421-521 |
9.37e-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: 9.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 421 RKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLvnLAELKKTSNRQRLET---AFDVAESKLGIAKLLD 497
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGL--CPNWRKLDPSNSLENcrrAMDLAKREFNIPMVLS 79
|
90 100
....*....|....*....|....
gi 320544548 498 AEDVDVPKPDEKSIMTYVAQFLHK 521
Cdd:cd21229 80 PEDLSSPHLDELSGMTYLSYFMKE 103
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
419-518 |
1.07e-12 |
|
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: 68.48 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 419 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDA 498
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80
|
90 100
....*....|....*....|.
gi 320544548 499 ED-VDVPKPDEKSIMTYVAQF 518
Cdd:cd21259 81 EDmVRMREPDWKCVYTYIQEF 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5962-6173 |
4.31e-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: 69.78 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5962 RWNDFAANKDKLEKWLNETETTLKvAPETKGELSEMKTLLERYKTLSNELKLKGNELEQLQSEARDLGTE--------VD 6033
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEghpdaeeiQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6034 AVNRLQSRCDKLKNDCSAHITALEQEMfDYNAYHQSLQDVEKWLLQISFQLMAHNslFISNREQTQEQIKQHEALLVEIQ 6113
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6114 KYQTNLDDLNAKGQAQIkryESSTPAIRPTVESQLKNIQDSYNSLLQTSVQIKNRLLESL 6173
Cdd:cd00176 157 AHEPRLKSLNELAEELL---EEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
421-520 |
1.66e-11 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 64.67 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 421 RKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSN---RQRLETAFDVAES-KLGIAKLL 496
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 320544548 497 DAEDVdVPKPDEKSIMTYVAQFLH 520
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
420-517 |
1.76e-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: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAeSKLGIAKLLDAE 499
Cdd:cd21254 2 ASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGF-ASLGISRLLEPS 80
|
90
....*....|....*....
gi 320544548 500 D-VDVPKPDEKSIMTYVAQ 517
Cdd:cd21254 81 DmVLLAVPDKLTVMTYLYQ 99
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5326-5539 |
6.04e-11 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 66.32 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5326 KWSDYQDQYTEALEWLSKTEALVQSYNKLQDsLIQKKVVLEQFQGHLQTLFDWQKTLDDLNMKAQVLLETCSD--TRISN 5403
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPdaEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5404 AIMQLTTKYNALLTLAKEVMRRLEMHYQEHQQHHSLYEECQsWIEKTREKLSEcEQIPGTLNEVQIKLNTVKNLRQGFET 5483
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQ-WLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 320544548 5484 GQNKLRYLLELKEKVIMNTEQNGAAKIQEDTEALKQDFDKLLVDLNDVRQKLANRL 5539
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7284-7997 |
7.32e-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: 70.47 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7284 QTKLTNTLANAKTQQSELEKE--AERWREYQQSIDRVKATIERT-KFVDEPVQNLAGLHFNIQKLSHAIGNVQSQNSDLT 7360
Cdd:TIGR02168 208 QAEKAERYKELKAELRELELAllVLRLEELREELEELQEELKEAeEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7361 LVNQQAQSLI-------RQADARNRQLiEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDK 7433
Cdd:TIGR02168 288 KELYALANEIsrleqqkQILRERLANL-ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7434 FRNvdptvrSRRHLEDTKNAIQELREESNQLKsshKEIEALSKSIltflgEVHKPSAEAIQAKVDKLVEQQAKLNDTLrd 7513
Cdd:TIGR02168 367 LEE------LESRLEELEEQLETLRSKVAQLE---LQIASLNNEI-----ERLEARLERLEDRRERLQQEIEELLKKL-- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7514 KEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVhvyDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAHYQ---- 7589
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEEL---REELEEAEQALDAAERELAQLQARLDSLERLQENLEGfseg 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7590 -----AKQNQLPSDIAQ-----EF-----TALEL-LAERVQ-VTMETKEkdfkraktvrtEYVDGVD-----EVQRWLLQ 7647
Cdd:TIGR02168 508 vkallKNQSGLSGILGVlseliSVdegyeAAIEAaLGGRLQaVVVENLN-----------AAKKAIAflkqnELGRVTFL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7648 AEVQVQERSLTPTQMKEL------------------------------------LQRINHEITAIYERFTLVKTNGQLI- 7690
Cdd:TIGR02168 577 PLDSIKGTEIQGNDREILkniegflgvakdlvkfdpklrkalsyllggvlvvddLDNALELAKKLRPGYRIVTLDGDLVr 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7691 ----------------------IENCRnsEEKTLVQTTIDQLAASLAQVRGWLDEKKQAVGDSLDAWTRFmnlyQIVMSW 7748
Cdd:TIGR02168 657 pggvitggsaktnssilerrreIEELE--EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL----SRQISA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7749 ASEKRNFIDQTIELRTLPEARNKLndyvTSVKSIKPIVKHLSEMDKELEHIGQV-TTVGDLKDKLQEAEDAKISVEAVLL 7827
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSK----ELTELEAEIEELEERLEEAEEELAEAeAEIEELEAQIEQLKEELKALREALD 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7828 ERNSLLQEACEEWDQCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQLGFCEKTLADINVQKTKLRLSIEKLEVHFRNGM 7907
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7908 GGDPRLSENVDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRL-------VMAPTYLPHDRE 7980
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeysltleEAEALENKIEDD 966
|
810
....*....|....*...
gi 320544548 7981 RALAEQQ-DLITQELDEL 7997
Cdd:TIGR02168 967 EEEARRRlKRLENKIKEL 984
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
419-527 |
7.60e-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: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 419 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDA 498
Cdd:cd21260 1 GVKNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEV 80
|
90 100 110
....*....|....*....|....*....|
gi 320544548 499 ED-VDVPKPDEKSIMTYVaQFLHKYPEPKG 527
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), ... |
424-518 |
1.15e-10 |
|
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: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 424 LLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDV-D 502
Cdd:cd21195 9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEMaS 88
|
90
....*....|....*.
gi 320544548 503 VPKPDEKSIMTYVAQF 518
Cdd:cd21195 89 AQEPDKLSMVMYLSKF 104
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
425-520 |
1.26e-10 |
|
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: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 425 LNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGIAKLLDAEDVDVP 504
Cdd:cd21185 7 LRWVRQLLPD---VDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADP 82
|
90
....*....|....*.
gi 320544548 505 KPDEKSIMTYVAQFLH 520
Cdd:cd21185 83 EVEHLGIMAYAAQLQK 98
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2588-3747 |
1.78e-10 |
|
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: 69.31 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2588 NEIDNI--KQKVDELRNLYPTFSESIIPKELNNVQKRYENVDLYAKKIESSLLQFLKKFHADKVGMLKRIIATQREKvaw 2665
Cdd:TIGR01612 687 NAIDNTedKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILEDFKNK--- 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2666 cQPESSSD-----KYN--LDVKKSSLQEVSK------SIDDCKARHAET--LKSLEMLKAVESPQN-LAELTSDAELLRK 2729
Cdd:TIGR01612 764 -EKELSNKindyaKEKdeLNKYKSKISEIKNhyndqiNIDNIKDEDAKQnyDKSKEYIKTISIKEDeIFKIINEMKFMKD 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2730 DMQALQDSFDQIKGILDENVDlwSQYEQSNEQISnwlrdvegRVKAETSSQvnlsevpqklqELSILQQDVLAHEPIINN 2809
Cdd:TIGR01612 843 DFLNKVDKFINFENNCKEKID--SEHEQFAELTN--------KIKAEISDD-----------KLNDYEKKFNDSKSLINE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2810 LEQTsqqlIEKNPearigQFVTHL--VQRYQAVSKALTSYIDKIRGAQ-------------LSNAN-FAKAAKD-FNEWF 2872
Cdd:TIGR01612 902 INKS----IEEEY-----QNINTLkkVDEYIKICENTKESIEKFHNKQnilkeilnknidtIKESNlIEKSYKDkFDNTL 972
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2873 GDAKIEFQELARMGSPGSSSATAQQLqtvknyIKTFDNgqILLNNAVDIGEALYpvvspdnreriradlrqmrEKFDYLR 2952
Cdd:TIGR01612 973 IDKINELDKAFKDASLNDYEAKNNEL------IKYFND--LKANLGKNKENMLY-------------------HQFDEKE 1025
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2953 DEANAFMQQVEGVLIQKTSIEES-YTQVSHYLNESKAKVPTTDELYPTLATKKAALQnyKTQLQEItlhKNALKqlHDKA 3031
Cdd:TIGR01612 1026 KATNDIEQKIEDANKNIPNIEIAiHTSIYNIIDEIEKEIGKNIELLNKEILEEAEIN--ITNFNEI---KEKLK--HYNF 1098
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3032 VTLCDDESERKTDESiqeyntlsKKISDRITTVGNHVVKH-EAYDQVLEKAQDWLNTIKSEAIDI--LNETTFEKEGAEE 3108
Cdd:TIGR01612 1099 DDFGKEENIKYADEI--------NKIKDDIKNLDQKIDHHiKALEEIKKKSENYIDEIKAQINDLedVADKAISNDDPEE 1170
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3109 KLLVVENLLQHKPEGDSIFDTCHKLL---------ETVLTQTH-------PSGHPALLKGFEEPKQSWEDFMTLCQDSLV 3172
Cdd:TIGR01612 1171 IEKKIENIVTKIDKKKNIYDEIKKLLneiaeiekdKTSLEEVKginlsygKNLGKLFLEKIDEEKKKSEHMIKAMEAYIE 1250
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3173 KLKQLCSKWDEFDTIIEELDNWMKNVEA------------VVKNQNLKSTAEAKNAHLKQLQDISkdierRGAAINELMD 3240
Cdd:TIGR01612 1251 DLDEIKEKSPEIENEMGIEMDIKAEMETfnishdddkdhhIISKKHDENISDIREKSLKIIEDFS-----EESDINDIKK 1325
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3241 --QGREIEGE---TDLNLKLSRLNTRYQTLKnlcKESIAKYVNYVKDhesFDKDFDSFKQNLQSSVDELAKTNEIVGDQS 3315
Cdd:TIGR01612 1326 elQKNLLDAQkhnSDINLYLNEIANIYNILK---LNKIKKIIDEVKE---YTKEIEENNKNIKDELDKSEKLIKKIKDDI 1399
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3316 VLQDQQNKLREMSDKRILDstlfeGLIDRGEKLYGHTSPEGREIirqqlralrtlwDNYtddLNSATQKIDQCLLQFNEF 3395
Cdd:TIGR01612 1400 NLEECKSKIESTLDDKDID-----ECIKKIKELKNHILSEESNI------------DTY---FKNADENNENVLLLFKNI 1459
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3396 SIAQDQLTKWLK-------------------DVDKAMQSHTEPKttlQEKRAQLQNHKLLHQEITTHNVLVDNVCDKA-Q 3455
Cdd:TIGR01612 1460 EMADNKSQHILKikkdnatndhdfninelkeHIDKSKGCKDEAD---KNAKAIEKNKELFEQYKKDVTELLNKYSALAiK 1536
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3456 ILVDQIKDNSlNVYLTSIKQLFQSIV-------QKSDEILH---NLDDCVQKHNELNNALSSAKTWISNEKAKLL----- 3520
Cdd:TIGR01612 1537 NKFAKTKKDS-EIIIKEIKDAHKKFIleaekseQKIKEIKKekfRIEDDAAKNDKSNKAAIDIQLSLENFENKFLkisdi 1615
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3521 --ECDDAYGEKADIKRKIETLG------QLAQNKPQAMKIISDIRDLFEKVKATTSEKGN-EVLDKEIEELETTMKSHFD 3591
Cdd:TIGR01612 1616 kkKINDCLKETESIEKKISSFSidsqdtELKENGDNLNSLQEFLESLKDQKKNIEDKKKElDELDSEIEKIEIDVDQHKK 1695
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3592 DIE-GIEGKQKDV-LAQWDKFEKALEELTKWCRSAEAVFREQQLQSTlhEKVEQLEKYKIQRELILQKEKEIdafgdaaH 3669
Cdd:TIGR01612 1696 NYEiGIIEKIKEIaIANKEEIESIKELIEPTIENLISSFNTNDLEGI--DPNEKLEEYNTEIGDIYEEFIEL-------Y 1766
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3670 ALLNNCgadrLKTLT-----------TQITNRYQLLQVLskEVVNRWSNLVDDhqfyqDKYNEVDLWLQPIESQMAKVLL 3738
Cdd:TIGR01612 1767 NIIAGC----LETVSkepitydeiknTRINAQNEFLKII--EIEKKSKSYLDD-----IEAKEFDRIINHFKKKLDHVND 1835
|
....*....
gi 320544548 3739 DEPTQSSNI 3747
Cdd:TIGR01612 1836 KFTKEYSKI 1844
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
413-524 |
1.99e-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: 61.97 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 413 AEKWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGI 492
Cdd:cd21257 2 AREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VGI 80
|
90 100 110
....*....|....*....|....*....|...
gi 320544548 493 AKLLDAED-VDVPKPDEKSIMTYVAQfLHKYPE 524
Cdd:cd21257 81 KPSLELSEmMYTDRPDWQSVMQYVAQ-IYKYFE 112
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
11655-11833 |
2.06e-10 |
|
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: 64.77 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11655 WQQIDNDLWRLEQWLQfaESTQKAQSA-PPSNIELLEDVTQDHREFLLDLESHKSIISSLNVVGDHLAThtLDTEKARQL 11733
Cdd:cd00176 2 LQQFLRDADELEAWLS--EKEELLSSTdYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11734 RSRLEADNERWNNVCINATKWQGLLQTALMGNSEFHQTIgELVEWLQRTEQNIKASEPVDLTEErsvLETKFKKFKDLRA 11813
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLES---VEELLKKHKELEE 153
|
170 180
....*....|....*....|
gi 320544548 11814 ELERCEPRVVSLQDAADQLL 11833
Cdd:cd00176 154 ELEAHEPRLKSLNELAEELL 173
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
424-518 |
2.30e-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: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 424 LLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDV-D 502
Cdd:cd21251 10 LLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPIMTGKEMaS 89
|
90
....*....|....*.
gi 320544548 503 VPKPDEKSIMTYVAQF 518
Cdd:cd21251 90 VGEPDKLSMVMYLTQF 105
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
421-515 |
2.43e-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: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 421 RKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAED 500
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90
....*....|....*..
gi 320544548 501 VDV--PKPDEKSIMTYV 515
Cdd:cd21258 83 MMImgKKPDSKCVFTYV 99
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7362-8162 |
2.50e-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: 68.93 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7362 VNQQAQSLIRQADARNR------QLIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFR 7435
Cdd:TIGR02168 198 LERQLKSLERQAEKAERykelkaELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7436 NVDPTVRSRRH-LEDTKNAI----QELREESNQLKSSHKEIEALSKSILTF----------LGEVHKPSAEaIQAKVDKL 7500
Cdd:TIGR02168 278 ELEEEIEELQKeLYALANEIsrleQQKQILRERLANLERQLEELEAQLEELeskldelaeeLAELEEKLEE-LKEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7501 VEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSvhvYDEHIAQTEQllitlnSQVQQAAEESKLL 7580
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER---LEARLERLED------RRERLQQEIEELL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7581 VAQTTAHYQAKQNQLPSDIAQEFTALELLaERVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPT 7660
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEEL-ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7661 QMKELLQRiNHEITAIYERFtlvktnGQLIieNCRNSEEKTLVQTtidqLAASLAQVrgwLDEKKQAVGD--SLDAWTRF 7738
Cdd:TIGR02168 507 GVKALLKN-QSGLSGILGVL------SELI--SVDEGYEAAIEAA----LGGRLQAV---VVENLNAAKKaiAFLKQNEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7739 MNLYQIVMSWASEKRNFIDQTIELRTLPEARNKLNDYVTSVKSIKPIVKHLS-------------EMDKELEHIGQ-VTT 7804
Cdd:TIGR02168 571 GRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLggvlvvddldnalELAKKLRPGYRiVTL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7805 VGDL--KDKLQEAEDAKisVEAVLLERNSLLQEACEEWDQCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQLGFCEKTL 7882
Cdd:TIGR02168 651 DGDLvrPGGVITGGSAK--TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7883 ADINVQKTKLRLSIEKLEVHFRNGMGGDPRLSENVDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQE 7962
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7963 EQQLRLVMAPTYLPHDRERALAEQQDLITQELDELLQSLSSVEDGIANMNQSSLDgmlhglklIQSNLEVHERDAIELKN 8042
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE--------LEELIEELESELEALLN 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 8043 QAKKLPTDPATERL--------LNDTVDRIDLLLRRTQQGITMIANAMHGQKKRQQEIDEYQQHLLELEQWIIEVSAELA 8114
Cdd:TIGR02168 881 ERASLEEALALLRSeleelseeLRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE 960
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320544548 8115 SFEPTSDSSTDEQV--LKSQVER-------SQQLLRTLKDRQQSM----EDLVEQTRQLQS 8162
Cdd:TIGR02168 961 NKIEDDEEEARRRLkrLENKIKElgpvnlaAIEEYEELKERYDFLtaqkEDLTEAKETLEE 1021
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
6496-7097 |
2.59e-10 |
|
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: 68.92 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6496 AINEIKNEYELQGHPKIQELKGKAAQVAEV-ISNLDgqQVEEQMKSLDrrFADLGKR---------------IDRKSQLL 6559
Cdd:TIGR01612 1052 SIYNIIDEIEKEIGKNIELLNKEILEEAEInITNFN--EIKEKLKHYN--FDDFGKEenikyadeinkikddIKNLDQKI 1127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6560 DVTNKGVEGAKGEIDQLQNWVKQQIEELQAPKPLGYTPKDAEARQQKIKSLMKDAEAKQSLADVLEKrvanMQQELEPVE 6639
Cdd:TIGR01612 1128 DHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKK----LLNEIAEIE 1203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6640 YSQ--LESaLRNLN-TENRNLSGVLKAELDRALEAS----KARKSLENDLDKarqwLKTKISEVRKLPVYHPLTSAEIEK 6712
Cdd:TIGR01612 1204 KDKtsLEE-VKGINlSYGKNLGKLFLEKIDEEKKKSehmiKAMEAYIEDLDE----IKEKSPEIENEMGIEMDIKAEMET 1278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6713 KIQENRKYDD--DAKQFNDSVLTDVQRQAANIMKD-----------------CDDADK--AALQQILDEIAADYQTLKDE 6771
Cdd:TIGR01612 1279 FNISHDDDKDhhIISKKHDENISDIREKSLKIIEDfseesdindikkelqknLLDAQKhnSDINLYLNEIANIYNILKLN 1358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6772 SSKrgKSLDDLLQGRKAFEDSMKNMGDWLNEMETATEGELRTTSLPVLEEQLahykKLLSDAENKGGLINDVSEQGKSIL 6851
Cdd:TIGR01612 1359 KIK--KIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKI----ESTLDDKDIDECIKKIKELKNHIL 1432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6852 PTLSNADKLKLNDDIKN--------------------MKDRYGRIKNTIDDRVNALGDHIKKYKDAKSRlaecsqflGNI 6911
Cdd:TIGR01612 1433 SEESNIDTYFKNADENNenvlllfkniemadnksqhiLKIKKDNATNDHDFNINELKEHIDKSKGCKDE--------ADK 1504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6912 QQKLRELNRPIGSRI-EDVQDLLGAYEGI-LKELKDSKSKMGDMQMDDLPELQSILaqqddmikLIEDQLAHLRQLLLLR 6989
Cdd:TIGR01612 1505 NAKAIEKNKELFEQYkKDVTELLNKYSALaIKNKFAKTKKDSEIIIKEIKDAHKKF--------ILEAEKSEQKIKEIKK 1576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6990 EQFIalINEIIAFIMKYTDVIIDIENSPDSLEDKINKYDDVIVKIQEC-------EGVLASANDKGQKIASEGNAADKNS 7062
Cdd:TIGR01612 1577 EKFR--IEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDClketesiEKKISSFSIDSQDTELKENGDNLNS 1654
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 320544548 7063 ITEQLQSLKNQLQNLRKA------VESQRQKHQLQLESHKK 7097
Cdd:TIGR01612 1655 LQEFLESLKDQKKNIEDKkkeldeLDSEIEKIEIDVDQHKK 1695
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
293-374 |
4.34e-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: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 293 RIDDLINDLRDGTKLIALLEVLSGERLPVEKGRV--LRRPHFLSNANTALQFLASK----RIKLVNINPADLVDGRPPVV 366
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaISRLQKLHNVEVALKALKEAgvlrGGDGGGITAKDIVDGHREKT 104
|
....*...
gi 320544548 367 LGLIWTII 374
Cdd:cd21223 105 LALLWRII 112
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
10787-10987 |
4.64e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.02 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10787 ELSEQYKALTNLHN---------ETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERnalqlryihlkrvphL 10857
Cdd:COG4913 229 ALVEHFDDLERAHEaledareqiELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL---------------L 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10858 KHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALAtamRMEQASiGQRISNLRAALKTWQGFLQRVTQLSESYEQRVN 10937
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEA---QIRGNG-GDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 320544548 10938 QL-------QQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALES 10987
Cdd:COG4913 370 ALglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10654-11400 |
6.75e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 6.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10654 EEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSseal 10733
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER---- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10734 rlwRQYLQHVQSFLSCAIPEDYSSLREQQQLCAihqnllisqqsvlsetplesELSEQYKALTNLHNETLSRIMQRNGEL 10813
Cdd:TIGR02168 311 ---LANLERQLEELEAQLEELESKLDELAEELA--------------------ELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10814 ERRVSGWNAYRQQL----AALLDWLRQREAERNALQLRYIHLKRVPHLKHRLDAMIQQLDQG--EQQSKALQEQQQELAR 10887
Cdd:TIGR02168 368 EELESRLEELEEQLetlrSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKleEAELKELQAELEELEE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10888 HCDDALATAMRMEQA--SIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKLLDAN----------SE 10955
Cdd:TIGR02168 448 ELEELQEELERLEEAleELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQsglsgilgvlSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10956 SLPTQP---AAIEQLLGSlRAQRV---QLGAQVSALESLT------VTQEELKecISPHDMKTIRQRNWLLWQQ------ 11017
Cdd:TIGR02168 528 LISVDEgyeAAIEAALGG-RLQAVvveNLNAAKKAIAFLKqnelgrVTFLPLD--SIKGTEIQGNDREILKNIEgflgva 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11018 ----------HADLDYQLANLI--NSIEERLSLLSNYQIRY-------DRIS-----------QWLQRLEQRVEKDADVT 11067
Cdd:TIGR02168 605 kdlvkfdpklRKALSYLLGGVLvvDDLDNALELAKKLRPGYrivtldgDLVRpggvitggsakTNSSILERRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11068 AMTNPEQAAKQLEQQVN---SELQLRDKEREWLLSTSRELLTLYSEPEVR-SQVQQQSDSLIDRWQRLKYLAKQKATKIG 11143
Cdd:TIGR02168 685 KIEELEEKIAELEKALAelrKELEELEEELEQLRKELEELSRQISALRKDlARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11144 ELKMTLLRLEERIALIRAWLFEVESQLDkplNFESYTPNVIEAKLKEHEQIQRsiehHSSNVGEVLNLVEMLLNDADSWR 11223
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIE---QLKEELKALREALDELRAELTL----LNEEAANLRERLESLERRIAATE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11224 TQvntsglaasAQNLEQRWKNVCSQSAERKARILTIWNLLQQLIKLTAEHKNWLGKQESQI--AGFERDQKSHSKHKLEE 11301
Cdd:TIGR02168 838 RR---------LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALalLRSELEELSEELRELES 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11302 RQMELRAKLEELESQ--SVNLR------QLEQIYAKLAMSAGVEPENIQKLTLPTKVMVSMWR----QLTPRCHAL---- 11365
Cdd:TIGR02168 909 KRSELRRELEELREKlaQLELRleglevRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARrrlkRLENKIKELgpvn 988
|
810 820 830
....*....|....*....|....*....|....*...
gi 320544548 11366 LDAID--KDAKLMREFNNAQLE-ATNSLNAIQKALEQL 11400
Cdd:TIGR02168 989 LAAIEeyEELKERYDFLTAQKEdLTEAKETLEEAIEEI 1026
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
409-518 |
7.17e-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: 60.57 E-value: 7.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 409 GDLKAEKWKQGARKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLV-NLAELKKTSNRQRLETAFDVAE 487
Cdd:cd21315 6 DDGPDDGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAE 82
|
90 100 110
....*....|....*....|....*....|.
gi 320544548 488 SKLGIAKLLDAEDVDVPKPDEKSIMTYVAQF 518
Cdd:cd21315 83 DWLDVPQLIKPEEMVNPKVDELSMMTYLSQF 113
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
274-374 |
7.27e-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: 60.67 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 274 KKTFTNWINSYL-----LKRVPPLRI--DDLINDLRDGTKLIALLEVLSGERLPVekgRVLRRPHFLS------NANTAL 340
Cdd:cd21217 3 KEAFVEHINSLLaddpdLKHLLPIDPdgDDLFEALRDGVLLCKLINKIVPGTIDE---RKLNKKKPKNifeateNLNLAL 79
|
90 100 110
....*....|....*....|....*....|....
gi 320544548 341 QFLASKRIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21217 80 NAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
267-376 |
1.89e-09 |
|
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: 59.22 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 267 EEQErvqKKTFTNWINSYLLkrvpPLRIDDLINDLRDGtklIALLEVLsgERL---PVEKGRVLR-----RPHFLSNANT 338
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGL----DPLINNLYEDLRDG---LVLLQVL--DKIqpgCVNWKKVNKpkplnKFKKVENCNY 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 320544548 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 ... |
413-524 |
2.50e-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: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 413 AEKWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGI 492
Cdd:cd21256 8 AREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGI 86
|
90 100 110
....*....|....*....|....*....|...
gi 320544548 493 AKLLDAED-VDVPKPDEKSIMTYVAQfLHKYPE 524
Cdd:cd21256 87 KSTLDINEmVRTERPDWQSVMTYVTA-IYKYFE 118
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5957-6768 |
3.42e-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: 65.08 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5957 KQAQNRWNDFAANKDKLEKWLNETETTLKvapetkgELSEMKTLLERYKTLSNELK------------LKGNELEQLQSE 6024
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLK-------SLERQAEKAERYKELKAELRelelallvlrleELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6025 ARDLGTEVDAVNRLQSRCDKLKNDCSAHITALEQEMFD----YNAYHQSLQDVEKWLLQISFQLMAHNslfiSNREQTQE 6100
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkeLYALANEISRLEQQKQILRERLANLE----RQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6101 QIKQHE-----------ALLVEIQKYQTNLDDLNAKGQAQIKRYESSTPAIRpTVESQLKNIQDSYNSLLQTSVQIKNRL 6169
Cdd:TIGR02168 324 QLEELEskldelaeelaELEEKLEELKEELESLEAELEELEAELEELESRLE-ELEEQLETLRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6170 ------LESLAKFQEYEDT-------------LDSIMRNLETYEPII---QTELDAPATSLELAQNQLRCAQEMQNKLNN 6227
Cdd:TIGR02168 403 erlearLERLEDRRERLQQeieellkkleeaeLKELQAELEELEEELeelQEELERLEEALEELREELEEAEQALDAAER 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6228 EKSRLAAAVQACEAATASISRPSSPLETAMQAIPERELIVrAKLEDLLdqKPPPKTRSST----GG-----VSTDDDKDE 6298
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGIL-GVLSELI--SVDEGYEAAIeaalGGrlqavVVENLNAAK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6299 ADVEIQVE----------LSDVNEALLDPIAHERVKNYRRIVRLNSAHVGKLNELVAKVQSHLGGLtASVSELEQQQKQR 6368
Cdd:TIGR02168 560 KAIAFLKQnelgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV-LVVDDLDNALELA 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6369 AELqdwvKKQQSSVSdwmmrpcklrpeaAQQELVSMNDLLNSIGDKRSQLMLEmtgslgdedtdLDDNIDKLESELMDAI 6448
Cdd:TIGR02168 639 KKL----RPGYRIVT-------------LDGDLVRPGGVITGGSAKTNSSILE-----------RRREIEELEEKIEELE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6449 AKKQAGQNVIDGYRQGMADVQNWFDTLIKRMDVLDRGSGLNCAQKMAAINEIKNEYEL--QGHPKIQELKGKAAQVAEVI 6526
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaQLSKELTELEAEIEELEERL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6527 SNLDG---------QQVEEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEELQApkpLGYTP 6597
Cdd:TIGR02168 771 EEAEEelaeaeaeiEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED---LEEQI 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6598 KDAEARQQKIKSLMKDAEAK----QSLADVLEKRVANMQQELEpveysQLESALRNLNTENRNLSGVLKAELDRALEASK 6673
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELieelESELEALLNERASLEEALA-----LLRSELEELSEELRELESKRSELRRELEELRE 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6674 ARKSLENDLDKARQWLKTKISEVR-----------KLPVYHPLTSAEIEKKI----------------------QENRKY 6720
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDNLQERLSeeysltleeaeALENKIEDDEEEARRRLkrlenkikelgpvnlaaieeyeELKERY 1002
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 320544548 6721 DDDAKQFNDsvLTDVQRQAANIMKDCDDADKAALQQILDEIAADYQTL 6768
Cdd:TIGR02168 1003 DFLTAQKED--LTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRV 1048
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6882-7570 |
4.30e-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: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6882 DRVNALGDHI----KKYKDAKSRLAECSQFLGNIQQKLRELNRPIGSRIEDVQDLLGAYEGILKELKDSKSkmgdmqmdD 6957
Cdd:TIGR02168 232 LRLEELREELeelqEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ--------Q 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6958 LPELQSILAQQDDMIKLIEDQLAHLRQLLLLREQFIALINEIIAFIMK-YTDVIIDIENSPDSLEDKINKYDDVIVKIQE 7036
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEeLESLEAELEELEAELEELESRLEELEEQLET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7037 CEGVLASANDKGQKIASE--GNAADKNSITEQLQSLK-NQLQNLRKAVESQRQKHQLQLESHKKMAAELSEILDWLHSH- 7112
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEieRLEARLERLEDRRERLQqEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAl 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7113 EGAAKSRPLLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEIgMPSSLLemlSEGRSLVASLPHELEEREKYL 7192
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL-KNQSGL---SGILGVLSELISVDEGYEAAI 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7193 KNNRDSRLEYMqLVAKFNDWVHEAELRLQNSQHGIDYehLVQDLDEHKIFFGNEAPIRNLVHKQIQEAAD--KIWSSLNN 7270
Cdd:TIGR02168 540 EAALGGRLQAV-VVENLNAAKKAIAFLKQNELGRVTF--LPLDSIKGTEIQGNDREILKNIEGFLGVAKDlvKFDPKLRK 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7271 YEQSELSaelaqfQTKLTNTLANAKTQQSELEKEA-------ERWR-----------------EYQQSIDRVKATIERT- 7325
Cdd:TIGR02168 617 ALSYLLG------GVLVVDDLDNALELAKKLRPGYrivtldgDLVRpggvitggsaktnssilERRREIEELEEKIEELe 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7326 --------------KFVDEPVQNLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIRQADARNRQLIEQDnAGLNRS 7391
Cdd:TIGR02168 691 ekiaelekalaelrKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI-EELEER 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7392 WQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFRNV-----DPTVRSRRHLEDTKNAIQELREESNQLKS 7466
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeaaNLRERLESLERRIAATERRLEDLEEQIEE 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7467 SHKEIEALSKSILTFlgevhKPSAEAIQAKVDKLVEQQAKLN---DTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALH 7543
Cdd:TIGR02168 850 LSEDIESLAAEIEEL-----EELIEELESELEALLNERASLEealALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
730 740
....*....|....*....|....*..
gi 320544548 7544 EQLQsvhvydEHIAQTEQLLITLNSQV 7570
Cdd:TIGR02168 925 AQLE------LRLEGLEVRIDNLQERL 945
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2751-2963 |
4.58e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.92 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2751 LWSQYEQSNEQISNWLRDVEGRVKAETSSQvNLSEVPQKLQELSILQQDVLAHEPIINNLEQTSQQLIEKNPEA--RIGQ 2828
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDaeEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2829 FVTHLVQRYQAVSKALTSYIDKIRGAQLSnANFAKAAKDFNEWFGDAKiefQELARMGSPGSSSATAQQLQTVKNYIKTF 2908
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLEEKE---AALASEDLGKDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 320544548 2909 DNGQILLNNAVDIGEALYPVVSPDNRERIRADLRQMREKFDYLRDEANAFMQQVE 2963
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
419-518 |
5.65e-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: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 419 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDA 498
Cdd:cd21196 3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSA 82
|
90 100
....*....|....*....|
gi 320544548 499 EDVdVPKPDEKSIMTYVAQF 518
Cdd:cd21196 83 QAV-VAGSDPLGLIAYLSHF 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4391-4560 |
5.96e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.54 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4391 LDRLKNLKASLADEFPRVDQVRALGEKVIPGTVDVGQvNIKSQIDTTQQEWESLLTTISSTIEAIEARLQHWSEYEQLrD 4470
Cdd:cd00176 39 LKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-D 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4471 QCLAWIRDTDNNLHAIDLKEDLPKKRAQLDALKALQGDVRAKELEVDNVTEKAQTLLKGPSSNRAsgpelvtkyQQIFHK 4550
Cdd:cd00176 117 DLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDAD---------EEIEEK 187
|
170
....*....|
gi 320544548 4551 VKELNNRWQQ 4560
Cdd:cd00176 188 LEELNERWEE 197
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3815-4032 |
7.05e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.54 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3815 QLSSYQDILNQTVNWLDQVEKLIHNENPASwtSAQEIRSKLYKYKATNQDINSHKRIVEAVNEKAAALLgSAAPANADEI 3894
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGD--DLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3895 SKAVAEVNKRYDQVGQDCAKLVADLDGAFDVYQQFSELQKAQQDYQKNlwDRLTGYSDYSGNKAALQARLQKINEIQDAL 3974
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEK--EAALASEDLGKDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 320544548 3975 PEGVAKLKSLEDHIEQQASNIPARSKEVMARDLANLHADFEKFGASLSDVKSGLENRL 4032
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
421-515 |
8.37e-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: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 421 RKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAED 500
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90
....*....|....*..
gi 320544548 501 VDV--PKPDEKSIMTYV 515
Cdd:cd21261 83 MMVmgRKPDPMCVFTYV 99
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3606-3811 |
9.89e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.15 E-value: 9.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3606 QWDKFEKALEELTKWCRSAEAVFREQQLQSTLHEKVEQLEKYKIQRELILQKEKEIDAFGDAAHALLNNCG--ADRLKTL 3683
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHpdAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3684 TTQITNRYQLLQVLSKEVVNRWSNLVDDHQFYQDKYnEVDLWLQPIESQMAKVLLDEPTQSSNIL----QVLLSEKEQAE 3759
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLESVEELlkkhKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 320544548 3760 SLFAALNAAGEKALPETSTQGREKIRKDLRDIRDRWDKLDEGIRNLEKRQEA 3811
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
417-518 |
2.21e-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: 56.23 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 417 KQGARKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLV-NLAELKKTSNRQRLETAFDVAESKLGIAKL 495
Cdd:cd21314 9 KQTPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQV 85
|
90 100
....*....|....*....|...
gi 320544548 496 LDAEDVDVPKPDEKSIMTYVAQF 518
Cdd:cd21314 86 IAPEEIVDPNVDEHSVMTYLSQF 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7393-8211 |
2.60e-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: 62.00 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7393 QDLVRSLEQRRDNLQ---QLAEHWDGFENSLHAWEKAL--GRLEDKFRNVDPTvrsrrhLEDTKNAIQELREESNQLKSS 7467
Cdd:TIGR02168 192 EDILNELERQLKSLErqaEKAERYKELKAELRELELALlvLRLEELREELEEL------QEELKEAEEELEELTAELQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7468 HKEIEALSKsiltFLGEVHKpSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQ 7547
Cdd:TIGR02168 266 EEKLEELRL----EVSELEE-EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7548 SVHvydehiAQTEQLLITLNSQVQQAAEESKLLVAQTTA--HYQAKQNQLPSDIAQEFTALELLAERVQVTMETKEkdfk 7625
Cdd:TIGR02168 341 ELE------EKLEELKEELESLEAELEELEAELEELESRleELEEQLETLRSKVAQLELQIASLNNEIERLEARLE---- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7626 raktvrteyvDGVDEVQRWllQAEVQVQERSLTPTQMKELLQRINHEITaiyERFTLVKTNGQLIIENCRNSEEKTLVQT 7705
Cdd:TIGR02168 411 ----------RLEDRRERL--QQEIEELLKKLEEAELKELQAELEELEE---ELEELQEELERLEEALEELREELEEAEQ 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7706 TIDQLAASLAQVRGWLDEKKQAVGdsldawtRFMNLYQ---IVMSWASEKRNFIDQTIELRTLPE---------ARNKLN 7773
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQE-------NLEGFSEgvkALLKNQSGLSGILGVLSELISVDEgyeaaieaaLGGRLQ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7774 DYVT-SVKSIKPIVKHLSEMDKELEHIGQVTTVGDlkDKLQEAEDAKISVEAVLLERNSLLQEACEEWdqceRKIKDIRS 7852
Cdd:TIGR02168 549 AVVVeNLNAAKKAIAFLKQNELGRVTFLPLDSIKG--TEIQGNDREILKNIEGFLGVAKDLVKFDPKL----RKALSYLL 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7853 WHEKTKQGLDSSQQQKKPLRDQLGFCekTLADINVQKtklRLSIEKLEVHFRNGMGGdprLSENVDDLVRVLDGLGELVK 7932
Cdd:TIGR02168 623 GGVLVVDDLDNALELAKKLRPGYRIV--TLDGDLVRP---GGVITGGSAKTNSSILE---RRREIEELEEKIEELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7933 AKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRLVMAPTYLPHDRERALAEQQDLITQELDELLQSLSSVEDGIANMN 8012
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 8013 QSsldgmlhgLKLIQSNLEVHERDAIELKNQAKKLptdpatERLLNDTVDRIDLLLRRtqqgitmIANAMHGQKKRQQEI 8092
Cdd:TIGR02168 775 EE--------LAEAEAEIEELEAQIEQLKEELKAL------REALDELRAELTLLNEE-------AANLRERLESLERRI 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 8093 DEYQQHLLELEQWIIEVSAELASfeptsdsstdeqvLKSQVERSQQLLRTLKDRQQSMEDLVEQTRQLqshpdvspladt 8172
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEA------------ 888
|
810 820 830
....*....|....*....|....*....|....*....
gi 320544548 8173 lmeqlqsiITILREQVTVATKRIFTIEKRIVDLRKAKSE 8211
Cdd:TIGR02168 889 --------LALLRSELEELSEELRELESKRSELRRELEE 919
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6678-6889 |
2.73e-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: 58.61 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6678 LENDLDKARQWLKTKISEVRKLpvYHPLTSAEIEKKIQENRKYDDDAKQFNDSVlTDVQRQAANIMKDCDDaDKAALQQI 6757
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERV-EALNELGEQLIEEGHP-DAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6758 LDEIAADYQTLKDESSKRGKSLDDLLQGRKAFEDSMKnMGDWLNEMETATEGELRTTSLPVLEEQLAHYKKLLSDAENKG 6837
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 320544548 6838 GLINDVSEQGKSILPTLSNADKLKLNDDIKNMKDRYGRIKNTIDDRVNALGD 6889
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6443-6792 |
3.98e-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: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6443 ELMDAIA-------KKQAGQNVIDGYRQGMADVQNWFDTLIKRMDVLDRGSglNCAQKMAAINEIKNEYElqGHPKIQEL 6515
Cdd:TIGR02169 157 KIIDEIAgvaefdrKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER--EKAERYQALLKEKREYE--GYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6516 KGKAAQVAEVISNLDGQqvEEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEgAKGEIDQLQnwVKQQIEELQAP----- 6590
Cdd:TIGR02169 233 EALERQKEAIERQLASL--EEELEKLTEEISELEKRLEEIEQLLEELNKKIK-DLGEEEQLR--VKEKIGELEAEiasle 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6591 ---KPLGYTPKDAEARQQKIKSLMkdaEAKQSLADVLEKRVANMQQELEPV---------EYSQLESALRNLNTENRNLS 6658
Cdd:TIGR02169 308 rsiAEKERELEDAEERLAKLEAEI---DKLLAEIEELEREIEEERKRRDKLteeyaelkeELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6659 GVLKAELDRALEASKARKSLENDLDKARQWLKTKISEVRKLpvyhpltSAEIEKKIQENRKYDDDAKQFNDSVLTDVQRQ 6738
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL-------NAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 320544548 6739 AANImkdcddADKAALQQILDEIAADYQTLKDESSKRGKSLDDLLQGRKAFEDS 6792
Cdd:TIGR02169 458 EQLA------ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5541-5749 |
4.48e-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: 58.23 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5541 QLEEIFKLYKILIEWLEDVEPSVkTSDEFLNDLSEKRAALEKFRVIQRDINGHNDIVEKIN---QRLKEDNSLDLKDFQP 5617
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNelgEQLIEEGHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5618 GL----TKFDDLQTQVNKIIESLENQVNSHEKYKQAYnELQDWLRRTRIEVEQCADCHgEKDQVESRLNRLGDIQSSSLE 5693
Cdd:cd00176 80 RLeelnQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 320544548 5694 GKALLEACEELSQAVIATSGSEGQDNVAQEIKHLTSEWETLQTISRDARSSLESCL 5749
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
10609-11559 |
4.49e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.51 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10609 TLANVAETQdKERKELDKEVTLAKAYFNNvqqDISREAPQNPKESEEQLAALRAhlqtLARTEEQLRQLKERHQN--SEV 10686
Cdd:PRK04863 245 TLEAIRVTQ-SDRDLFKHLITESTNYVAA---DYMRHANERRVHLEEALELRRE----LYTSRRQLAAEQYRLVEmaREL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10687 ApsvASSDDDGILEvlalwqkifqdtfQEYHRLSTRLARSQNsseALRLWRQYLQHVQSFLscaipEDYSSLREQQQLCA 10766
Cdd:PRK04863 317 A---ELNEAESDLE-------------QDYQAASDHLNLVQT---ALRQQEKIERYQADLE-----ELEERLEEQNEVVE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10767 IHQNLLISQQSVLSETPLE-SELSEQykaltnlhnetLSRIMQRNGELERRVSgwnAYRQQLAAL--------------- 10830
Cdd:PRK04863 373 EADEQQEENEARAEAAEEEvDELKSQ-----------LADYQQALDVQQTRAI---QYQQAVQALerakqlcglpdltad 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10831 --LDWLRQREAERNALQLRyihlkrVPHLKHRL---DAMIQQLDQGEQQSKAL-----QEQQQELARhcdDALATAMrmE 10900
Cdd:PRK04863 439 naEDWLEEFQAKEQEATEE------LLSLEQKLsvaQAAHSQFEQAYQLVRKIagevsRSEAWDVAR---ELLRRLR--E 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10901 QASIGQRISNLRAALKTWQGFL---QRVTQLSESYEQRVNQ---LQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQ 10974
Cdd:PRK04863 508 QRHLAEQLQQLRMRLSELEQRLrqqQRAERLLAEFCKRLGKnldDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10975 RVQLGAQVSALESLT----VTQ---EELKECiSPHDMKTiRQRNWLLWQQHADLDYQLANLINSIEERLSLLsnyQIRYD 11047
Cdd:PRK04863 588 LEQLQARIQRLAARApawlAAQdalARLREQ-SGEEFED-SQDVTEYMQQLLERERELTVERDELAARKQAL---DEEIE 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11048 RISQ-------WLQRLEQRV------EKDADVTAMTNPEQAAkqLEQQVNSELQLRDkerewLLSTSRELLTLYSEPEVR 11114
Cdd:PRK04863 663 RLSQpggsedpRLNALAERFggvllsEIYDDVSLEDAPYFSA--LYGPARHAIVVPD-----LSDAAEQLAGLEDCPEDL 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11115 SQVQQQSDSLIDRWQRLKYLAKQKATKIGELKMTLLRL-----------EERIALIRAWLFEVESQLDKpLNFESytpnv 11183
Cdd:PRK04863 736 YLIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFpevplfgraarEKRIEQLRAEREELAERYAT-LSFDV----- 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11184 ieaklkehEQIQRSIEHHSSNVGEVLNLV-----EMLLNDADSWRTQVNTSGLAASAQNLEQRwknvcsqSAERKARilt 11258
Cdd:PRK04863 810 --------QKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVELERALADHESQEQQQR-------SQLEQAK--- 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11259 iwNLLQQLIKLtaehknwlgkqESQIAGFERDQkshskhkLEERQMELRAKLEELE-------SQSVNLRQLEQIYAKLA 11331
Cdd:PRK04863 872 --EGLSALNRL-----------LPRLNLLADET-------LADRVEEIREQLDEAEeakrfvqQHGNALAQLEPIVSVLQ 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11332 msagVEPENIQKLTLPTKVMVSMWRQLTPRCHALLDAIDKDAKLMREFNNAQLEATNSLNaiqkalEQLPsaenqqtska 11411
Cdd:PRK04863 932 ----SDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKNSDLN------EKLR---------- 991
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11412 epkavlQRLESLEKKLQDAQQHVQQADNLAQEAKTRtkqqpqlkqLLELVSAYTTLWQTVQtrivtlkttwltRAAQAAA 11491
Cdd:PRK04863 992 ------QRLEQAEQERTRAREQLRQAQAQLAQYNQV---------LASLKSSYDAKRQMLQ------------ELKQELQ 1044
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 320544548 11492 SLPV----SEAANAAVQVNTLSQRkLRQAQQmQREtsitakdayimELQTAITECQNNLDELQRTVVDKTRK 11559
Cdd:PRK04863 1045 DLGVpadsGAEERARARRDELHAR-LSANRS-RRN-----------QLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
268-373 |
4.58e-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: 55.32 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 268 EQERVQKKTFTNWINSYllkRVPPlRIDDLINDLRDGTKLIALLEVLSgerlP--VEKGRVLRRPH-------FLSNANT 338
Cdd:cd21298 2 IEETREEKTYRNWMNSL---GVNP-FVNHLYSDLRDGLVLLQLYDKIK----PgvVDWSRVNKPFKklganmkKIENCNY 73
|
90 100 110
....*....|....*....|....*....|....*
gi 320544548 339 ALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTI 373
Cdd:cd21298 74 AVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQL 108
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
417-518 |
5.63e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 55.10 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 417 KQGARKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLVNLAEL---KKTSNRQRleTAFDVAESKLGIA 493
Cdd:cd21313 6 KQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCPDWESwdpQKPVDNAR--EAMQQADDWLGVP 80
|
90 100
....*....|....*....|....*
gi 320544548 494 KLLDAEDVDVPKPDEKSIMTYVAQF 518
Cdd:cd21313 81 QVITPEEIIHPDVDEHSVMTYLSQF 105
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7012-7155 |
6.34e-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: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7012 DIENSPDSLEDKINKYDDVIVKIQECEGVLASANDKGQKIASEGnAADKNSITEQLQSLKNQLQNLRKAVESQRQKHQLQ 7091
Cdd:cd00176 27 DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQERLEELNQRWEELRELAEERRQRLEEA 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320544548 7092 LESHKKMaAELSEILDWLHSHEGAAKSRPlLDRDPESVERELQKHQSLSQDIESYLNKFNKIND 7155
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 ... |
424-518 |
7.47e-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: 54.50 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 424 LLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDVD- 502
Cdd:cd21250 9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMAs 88
|
90
....*....|....*.
gi 320544548 503 VPKPDEKSIMTYVAQF 518
Cdd:cd21250 89 AEEPDKLSMVMYLSKF 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
932-1146 |
1.11e-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: 56.69 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 932 QEYKSGIEQLSRWLRGAESVLDQRQVLGNSEQVKEYGQQLQQLASEIDDNEELFKTISRNFQSLIQDLSRD--EVDKMMK 1009
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDaeEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 1010 LLKQEKESLVRIRAQLpaKLHLFHQLQIQQESLEAgqKEIHQWLSEAEQLLGTHNLSGGRDAINEQLHKHKTYFSRTVYY 1089
Cdd:cd00176 83 ELNQRWEELRELAEER--RQRLEEALDLQQFFRDA--DDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 320544548 1090 RSMLESKNKVFQNLLKAVSSDDKIDTApasQQMQQLNERFNYVIQNAQQWEQRLDSA 1146
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIE---EKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5432-5645 |
1.27e-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: 56.69 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5432 EHQQHHSLYEECQSWIEKTREKLSEcEQIPGTLNEVQIKLNTVKNLRQGFETGQNKLRYLLELKEKVImNTEQNGAAKIQ 5511
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5512 EDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILiEWLEDVEPSVKtSDEFLNDLSEKRAALEKFRVIQRDIN 5591
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 320544548 5592 GHNDIVEKINQRLKEdnsLDLKDFQPGLTKFDDLQTQVNKIIESLENQVNSHEK 5645
Cdd:cd00176 157 AHEPRLKSLNELAEE---LLEEGHPDADEEIEEKLEELNERWEELLELAEERQK 207
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
6864-7539 |
1.28e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6864 DDIKNMKDRYGRIKNTIDDRVNALGDHIKKYKDAKSRLAECSQFLGNIQQKLRELNrpigSRIEDVQDLLGAYEGILKEL 6943
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEIS----SELPELREELEKLEKEVKEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6944 KDSKSKMGDMQMDDLPELQSILAQQDDmIKLIEDQLAHLRQLLLLREQFIALINEI----------IAFIMKYTDVIIDI 7013
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEK-IRELEERIEELKKEIEELEEKVKELKELkekaeeyiklSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7014 ENSPDSLEDKINkydDVIVKIQECEgvlasandkgqkiasegnaadknSITEQLQSLKNQLQNLRKAVESQRQKHQLqLE 7093
Cdd:PRK03918 313 EKRLSRLEEEIN---GIEERIKELE-----------------------EKEERLEELKKKLKELEKRLEELEERHEL-YE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7094 SHKKMAAELSEIldwlhshegaaKSRpLLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEIGMPSSLLEMLSE 7173
Cdd:PRK03918 366 EAKAKKEELERL-----------KKR-LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7174 GRSLVASLPHEL-EEREKYLKNnrdsrlEYMQLVAKFNDWVHEAELRLqnsqhgidyEHLVQDLDEHKIFFGNEAPIRNL 7252
Cdd:PRK03918 434 AKGKCPVCGRELtEEHRKELLE------EYTAELKRIEKELKEIEEKE---------RKLRKELRELEKVLKKESELIKL 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7253 vhKQIQEAADKIWSSLNNYEQSELSAELAQFQtKLTNTLANAKTQQSELEKEAERWREYQQSidrvKATIERTKfvDEPV 7332
Cdd:PRK03918 499 --KELAEQLKELEEKLKKYNLEELEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKL--DELE 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7333 QNLAGLHFNIQKLSHaignvqsqnSDLTLVNQQAQSLirqaDARNRQLIEQDNAglNRSWQDLVRSLEQRRDNLQQLAEH 7412
Cdd:PRK03918 570 EELAELLKELEELGF---------ESVEELEERLKEL----EPFYNEYLELKDA--EKELEREEKELKKLEEELDKAFEE 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7413 WDGFENSLhawEKALGRLEDKFRNVDPtvrsrrhlEDTKNAIQELREESNQLKSSHKEIEALSKSIltflgevhkpsaEA 7492
Cdd:PRK03918 635 LAETEKRL---EELRKELEELEKKYSE--------EEYEELREEYLELSRELAGLRAELEELEKRR------------EE 691
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 320544548 7493 IQAKVDKLVEQqaklndtlRDKEQQVSKDLEEIEQVFRRISQLQDKL 7539
Cdd:PRK03918 692 IKKTLEKLKEE--------LEEREKAKKELEKLEKALERVEELREKV 730
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7262-7549 |
1.40e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7262 DKIWSSLNNYEQSELSAELAQFQTKLTNTLANAKTQQSELEKEAERWREYQQSIDRVKATIE------RTKFVDEPVQ-- 7333
Cdd:TIGR02169 214 QALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEelnkkiKDLGEEEQLRvk 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7334 -NLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIRQADARNRQLIEQ--DNAGLNRSWQDLVRSLEQRRDNLQQLA 7410
Cdd:TIGR02169 294 eKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieEERKRRDKLTEEYAELKEELEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7411 EhwdgfenslhAWEKALGRLEDKFRNVdptvrsRRHLEDTKNAIQELR-------EESNQLKSSHKEIEALSKSILTFLG 7483
Cdd:TIGR02169 374 E----------EVDKEFAETRDELKDY------REKLEKLKREINELKreldrlqEELQRLSEELADLNAAIAGIEAKIN 437
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320544548 7484 EVhKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSV 7549
Cdd:TIGR02169 438 EL-EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
268-371 |
1.41e-07 |
|
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: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 268 EQERvQKKTFTNWINSYllkRVPPlRIDDLINDLRDGTKLI-ALLEVLSGErlpVEKGRV--------LRRPHFLSNANT 338
Cdd:cd21300 4 EGER-EARVFTLWLNSL---DVEP-AVNDLFEDLRDGLILLqAYDKVIPGS---VNWKKVnkapasaeISRFKAVENTNY 75
|
90 100 110
....*....|....*....|....*....|...
gi 320544548 339 ALQFLASKRIKLVNINPADLVDGRPPVVLGLIW 371
Cdd:cd21300 76 AVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6572-6783 |
1.46e-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: 56.69 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6572 EIDQLQNWVKQQIEELQAPKPlGYTPKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELePVEYSQLESALRNLN 6651
Cdd:cd00176 8 DADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6652 TENRNLSGvLKAELDRALEASKARKSLENDLDKARQWLKTKISEVRKLPVYHPLTsaEIEKKIQENRKYDDDAKQfNDSV 6731
Cdd:cd00176 86 QRWEELRE-LAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLE--SVEELLKKHKELEEELEA-HEPR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 320544548 6732 LTDVQRQAANIMKDCDDADKAALQQILDEIAADYQTLKDESSKRGKSLDDLL 6783
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
10784-11171 |
1.49e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10784 LESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHLK----------- 10852
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELReeleklekllq 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10853 ------RVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELAR------HCDDALATAMRMEQASIGQRISNLRAALKTWQG 10920
Cdd:COG4717 127 llplyqELEALEAELAELPERLEELEERLEELRELEEELEEleaelaELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10921 FLQRVTQLSESYEQRVNQLQQEFGAAQKllDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESL------------ 10988
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLEN--ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIltiagvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10989 -------------TVTQEELKECISPHDMKTIRQRNWLLWqqHADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQR 11055
Cdd:COG4717 285 llallflllarekASLGKEAEELQALPALEELEEEELEEL--LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11056 LEQRVEKD--------ADVTAMTNPEQAAKQLEQQVNSELQLRDKER--EWLLSTSRELLTLYSEPEVRSQVQQQSDSLI 11125
Cdd:COG4717 363 LQLEELEQeiaallaeAGVEDEEELRAALEQAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEELE 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 320544548 11126 DRWQRLKYLAKQKATKIGELKMtlLRLEERIALIRAWLFEVESQLD 11171
Cdd:COG4717 443 ELEEELEELREELAELEAELEQ--LEEDGELAELLQELEELKAELR 486
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3180-3373 |
1.68e-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: 56.30 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3180 KWDEFDTIIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINELMDQGREI-----EGETDLNLK 3254
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeghPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3255 LSRLNTRYQTLKNLCKESIAKYVNYVKDHEsFDKDFDSFKQNLQsSVDELAKTNEIVGDQSVLQDQQNKLREMSDKRILD 3334
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLE-EKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 320544548 3335 STLFEGLIDRGEKLYGHTSPEGREIIRQQLRALRTLWDN 3373
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEE 197
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10592-11199 |
2.27e-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: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10592 ELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDIsreapqnpkesEEQLAALRAHLQTLARTE 10671
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-----------EEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10672 EQLRQLKERHQNsevapsvASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEALRLwrqylqhvqsflscai 10751
Cdd:COG1196 302 QDIARLEERRRE-------LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA---------------- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10752 pedysSLREQQQLCAIHQNLLISQQSVLSEtpLESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALL 10831
Cdd:COG1196 359 -----ELAEAEEALLEAEAELAEAEEELEE--LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10832 DWLRQREAERNALQlryihlkrvphlkhRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALATAMRmEQASIGQRISNL 10911
Cdd:COG1196 432 ELEEEEEEEEEALE--------------EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE-ELAEAAARLLLL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10912 RAALKTWQGFLQRVTQLsesyeqrvnQLQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRV--QLGAQVSALESLT 10989
Cdd:COG1196 497 LEAEADYEGFLEGVKAA---------LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVveDDEVAAAAIEYLK 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10990 VTQEELKECISPHDMKTIRQRNWLLWQQHADLDYQL-ANLINSIEERLSLLSNY----QIRYDRISQWLQRLEQRVEKDA 11064
Cdd:COG1196 568 AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLvASDLREADARYYVLGDTllgrTLVAARLEAALRRAVTLAGRLR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11065 DVT-AMTNPEQAAKQLEQQVNSELQLRDKEREWLLSTSRELLtlysepEVRSQVQQQSDSLIDRWQRLKYLAKQKATKIG 11143
Cdd:COG1196 648 EVTlEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA------EEELELEEALLAEEEEERELAEAEEERLEEEL 721
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 320544548 11144 ELKMTLLRLEERIALIRAWLFEVESQLDKPLNFESYTPNVIEAKLKEHEQIQRSIE 11199
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4470-4672 |
2.31e-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: 55.91 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4470 DQCLAWIRDTDNNLHAIDLKEDLPKKRAQLDALKALQGDVRAKELEVDNVTEKAQTLLkgpSSNRASGPELVTKYQQIFH 4549
Cdd:cd00176 10 DELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI---EEGHPDAEEIQERLEELNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4550 KVKELNNRWQQYVTSHED------FDNAISDCSSWINEIKEKL---DYCSDMSSMspKELDKKLATIQDVILLKDEgsaR 4620
Cdd:cd00176 87 RWEELRELAEERRQRLEEaldlqqFFRDADDLEQWLEEKEAALaseDLGKDLESV--EELLKKHKELEEELEAHEP---R 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 320544548 4621 VLKILEQAQHVLANTAPGGHEAINKELTDLQDLWSGIALRIMDVKSNLDDSI 4672
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
268-380 |
2.35e-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: 54.28 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 268 EQERVqkkTFTNWINSYL-----LKRVPPLRIDD--LINDLRDGT---KLIALLEVLSGERLPVEKGRVlrRPHFLS-NA 336
Cdd:cd21323 23 EEEKV---AFVNWINKALegdpdCKHVVPMNPTDesLFKSLADGIllcKMINLSQPDTIDERAINKKKL--TPFTISeNL 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 320544548 337 NTALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTII---LYFQIE 380
Cdd:cd21323 98 NLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIkvgLFADIE 144
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
268-374 |
2.81e-07 |
|
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: 53.45 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 268 EQERVQKKTFTNWINSYllkRVPPLrIDDLINDLRDGTKLIALLEVLsgeRLPVEKGRVLRRPHFL--------SNANTA 339
Cdd:cd21329 2 EGESSEERTFRNWMNSL---GVNPY-VNHLYSDLCDALVIFQLYEMT---RVPVDWGHVNKPPYPAlggnmkkiENCNYA 74
|
90 100 110
....*....|....*....|....*....|....*.
gi 320544548 340 LQFLASK-RIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21329 75 VELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLM 110
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5441-6232 |
2.84e-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: 58.53 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5441 EECQSWIEKTREKLSECEQIpgtLNEVQIKLNTVKnlRQG-----FETGQNKLR------YLLELKEKV----IMNTEQN 5505
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDI---LNELERQLKSLE--RQAekaerYKELKAELRelelalLVLRLEELReeleELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5506 GAAKIQEDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDVEPSVKTSDEFLND----LSEKRAALE 5581
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERqleeLEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5582 KFRVIQRDIngHNDIVEKINQRLKEDNSLDLKdfqpgLTKFDDLQTQVNKIIESLENQvnsHEKYKQAYNELQDWLRRTR 5661
Cdd:TIGR02168 330 SKLDELAEE--LAELEEKLEELKEELESLEAE-----LEELEAELEELESRLEELEEQ---LETLRSKVAQLELQIASLN 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5662 IEVEQCADchgEKDQVESRLNRLGDIQSSslEGKALLEACEELSQAVIATsgsegqdnVAQEIKHLTSEWETLQTISRDA 5741
Cdd:TIGR02168 400 NEIERLEA---RLERLEDRRERLQQEIEE--LLKKLEEAELKELQAELEE--------LEEELEELQEELERLEEALEEL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5742 RSSLESCLAAWQTFLQKFNKINLWIETMNKRVTKsQEGENKTPEDLVNAKKLLEE---VLAEKDNVEDlndNCELLMEQS 5818
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQEN-LEGFSEGVKALLKNQSGLSGilgVLSELISVDE---GYEAAIEAA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5819 ACTRIRDQTIETQANYTK----LLTSAQGLVAKIEKNLSDHTEFLNYKKEMDAWIEKAQQVLDDCSTDGDAA-------- 5886
Cdd:TIGR02168 543 LGGRLQAVVVENLNAAKKaiafLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsyll 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5887 ---IIAQKLDTVNSLASRLPEGqhllalvqdayskASNITPEDKQEKLRELMTKVREDWDALGLAVKQKLSDLKQaqnrw 5963
Cdd:TIGR02168 623 ggvLVVDDLDNALELAKKLRPG-------------YRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEE----- 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5964 ndfaankdklekwlnetettlkvapetkgelsEMKTLLERYKTLSNELKLKGNELEQLQSEARDLGTEVDAVNRLQSRCD 6043
Cdd:TIGR02168 685 --------------------------------KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6044 KLKNDCSAHITALEQEMFDYNAYHQSLQDVEKWLLQISFQLMAHNSLFISNREQTQEQIKQHEALLV----EIQKYQTNL 6119
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalreALDELRAEL 812
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6120 DDLNAKGQAQIKRYESStpairptvESQLKNIQDSYNSLLQTSVQIKNRLLESLAKFQEYEDTLDSIMRNLEtyepIIQT 6199
Cdd:TIGR02168 813 TLLNEEAANLRERLESL--------ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE----ALLN 880
|
810 820 830
....*....|....*....|....*....|...
gi 320544548 6200 ELDAPATSLELAQNQLRCAQEMQNKLNNEKSRL 6232
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSEL 913
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
6533-7105 |
3.67e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6533 QVEEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNwVKQQIEELQapKPLGYTPKDAEARQQKIKSLMK 6612
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-LKEEIEELE--KELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6613 DAEAKQSLADVLEKRVANMqQELEPV--EYSQLESALRNLNTENRNLSgVLKAELDRALEASKARKSLENDLDKARQWLK 6690
Cdd:PRK03918 267 RIEELKKEIEELEEKVKEL-KELKEKaeEYIKLSEFYEEYLDELREIE-KRLSRLEEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6691 TKISEVRK----LPVYHPLTSaEIEKKIQENRKYDddaKQFNDSVLTDVQRQAANIMKdcddaDKAALQQILDEIAADYQ 6766
Cdd:PRK03918 345 KKLKELEKrleeLEERHELYE-EAKAKKEELERLK---KRLTGLTPEKLEKELEELEK-----AKEEIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6767 TLKDESSKRGKSLDDL--------LQGRKAFEDSMKN--------MGDWLNEMETATEGE--LRtTSLPVLEEQLAHYKK 6828
Cdd:PRK03918 416 ELKKEIKELKKAIEELkkakgkcpVCGRELTEEHRKElleeytaeLKRIEKELKEIEEKErkLR-KELRELEKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6829 LLSdaenkgglINDVSEQGKSILPTLSNADKLKLNDDIKNMKDRYGRIkNTIDDRVNALGDHIKKYKDAKSRLAECSQFL 6908
Cdd:PRK03918 495 LIK--------LKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKL-IKLKGEIKSLKKELEKLEELKKKLAELEKKL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6909 GNIQQKLRELNRPIGSR----IEDVQDLLGAYEGILK---ELKDSKSkmgdmqmddlpELQSILAQQDDMIKLIEDQLAH 6981
Cdd:PRK03918 566 DELEEELAELLKELEELgfesVEELEERLKELEPFYNeylELKDAEK-----------ELEREEKELKKLEEELDKAFEE 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6982 LRQLLLLREQfiaLINEIIAFIMKYTDviidienspdslEDKINKYDDVIVKIQECEGVLASAndkgqkiasEGNAADKN 7061
Cdd:PRK03918 635 LAETEKRLEE---LRKELEELEKKYSE------------EEYEELREEYLELSRELAGLRAEL---------EELEKRRE 690
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 320544548 7062 SITEQLQSLKNQLQNLRKAVEsqrqkhqlQLESHKKMAAELSEI 7105
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKK--------ELEKLEKALERVEEL 726
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
6929-7473 |
5.36e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6929 VQDLLGAYEGILKELKDSKSKMGDMQMDD-LPELQSILAQQDDMIKLIEDQLAHLRQLLLLREQFIAL-------INEII 7000
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDLHErLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEheerreeLETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7001 AFIMKYTDVIIDIENSPDSLEDKINKYDDVIVKI-QECEGVLASAndkgqkiasEGNAADKNSITEQLQSLKNQLQNLRK 7079
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELeEERDDLLAEA---------GLDDADAEAVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7080 AVESQR---QKHQLQLESHKKMAAELSEILDWLHshEGAAKsrplLDRDPESVERELQKHQSLSQDIESYLNKFNKINDG 7156
Cdd:PRK02224 329 RLEECRvaaQAHNEEAESLREDADDLEERAEELR--EEAAE----LESELEEAREAVEDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7157 VKTEIGMPSSLLEMLSEGRSlvaSLPHELEEREKYLKNNRDSRLEYMQLVAKFNdwVHEAELRLQNSQH--GI-DYEHLV 7233
Cdd:PRK02224 403 APVDLGNAEDFLEELREERD---ELREREAELEATLRTARERVEEAEALLEAGK--CPECGQPVEGSPHveTIeEDRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7234 QDLDEHKIFFGNEAPIRNLVH---KQIQEAADKIWSSLNNYEQS-ELSAELAQFQTKLTNTLANAKTQQSELEKEAERWR 7309
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLeraEDLVEAEDRIERLEERREDLeELIAERRETIEEKRERAEELRERAAELEAEAEEKR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7310 E-YQQSIDRVKATIERTKFVD----------EPVQNLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIRQADARNR 7378
Cdd:PRK02224 558 EaAAEAEEEAEEAREEVAELNsklaelkeriESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKR 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7379 QLIEQ-DNAGLNRSWQDLVRS---LEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDkfrnvdptVRSRR-HLEDTKNA 7453
Cdd:PRK02224 638 ELEAEfDEARIEEAREDKERAeeyLEQVEEKLDELREERDDLQAEIGAVENELEELEE--------LRERReALENRVEA 709
|
570 580
....*....|....*....|
gi 320544548 7454 IQELREESNQLKSSHKEIEA 7473
Cdd:PRK02224 710 LEALYDEAEELESMYGDLRA 729
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10829-11429 |
7.08e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10829 ALLDWLRQREAERNALQLRyihlkrvpHLKHRLDAMIQQLDQGEQQSKALQEQQQEL---------ARHCDDALATAMRM 10899
Cdd:COG1196 217 ELKEELKELEAELLLLKLR--------ELEAELEELEAELEELEAELEELEAELAELeaeleelrlELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10900 EQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKLLDANSESLptqpAAIEQLLGSLRAQRVQLG 10979
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL----EEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10980 AQVSALESLTVTQEELKEcisphdmktirqrnwLLWQQHADLDYQLANLINSIEERLSLLSNYQIRYDRisqwlqRLEQR 11059
Cdd:COG1196 365 EALLEAEAELAEAEEELE---------------ELAEELLEALRAAAELAAQLEELEEAEEALLERLER------LEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11060 VEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWLLSTSRELltLYSEPEVRSQVQQQSDSLIDRWQRLK------- 11132
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL--LEEAALLEAALAELLEELAEAAARLLllleaea 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11133 -YLAKQKATKIGELKMTLLRLEERIALIRAWLFEVESQLDKPLNfesytPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNL 11211
Cdd:COG1196 502 dYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA-----AALQNIVVEDDEVAAAAIEYLKAAKAGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11212 VEMLLNDADSWRTQVNTSGLAASAQNL---EQRWKNVCSQSAERKARILTIWNL-----------LQQLIKLTAEHKNWL 11277
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLvasDLREADARYYVLGDTLLGRTLVAArleaalrravtLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11278 GKQESQIAGFERDQKSHSKHKLEERQMELRAKLEELESQSVNLRQLE--QIYAKLAMSAGVEPENIQKLTLPTKVMVSMW 11355
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEeeERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320544548 11356 RQLTPRCHALLDAIDKDAKLMREFNNAQLEAtnSLNAIQKALEQL----PSAENQQtskaepKAVLQRLESLEKKLQD 11429
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELER--ELERLEREIEALgpvnLLAIEEY------EELEERYDFLSEQRED 806
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
267-383 |
7.48e-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: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 267 EEQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASK 346
Cdd:cd21285 5 EAENGFDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSFLAAK 84
|
90 100 110
....*....|....*....|....*....|....*..
gi 320544548 347 RIKLVNINPADLVDGRPPVVLGLIWTIILYFQIEENS 383
Cdd:cd21285 85 GINIQGLSAEEIRNGNLKAILGLFFSLSRYKQQQQQP 121
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7057-7723 |
7.53e-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: 57.37 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7057 AADKNSITEQLQSLKNQLQNLRKAVESQRQKHQlQLESHKKMAAEL-----SEILDWLHSHEGAAKSRPLLDRDPESVER 7131
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELE-ELESRLEELEEQletlrSKVAQLELQIASLNNEIERLEARLERLED 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7132 ELQKhqsLSQDIESYLNKFNKINdgvKTEIGMPSSLLEMLSEgrslvaSLPHELEEREKYLKNNRDSRLEYMQLVAKFND 7211
Cdd:TIGR02168 415 RRER---LQQEIEELLKKLEEAE---LKELQAELEELEEELE------ELQEELERLEEALEELREELEEAEQALDAAER 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7212 WVHEAELRLqnsqhgidyeHLVQDLDEHKIFFGNEapIRNLVHKQIQEAADK--IWSSLNNYEQSELSAELA---QFQTK 7286
Cdd:TIGR02168 483 ELAQLQARL----------DSLERLQENLEGFSEG--VKALLKNQSGLSGILgvLSELISVDEGYEAAIEAAlggRLQAV 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7287 LTNTLANAKTQQSELeKEAERWREYQQSIDRVKAT------IERTKFVDEPVQNLAGLHFNIQKLSHAIGNVQSQnsdLT 7360
Cdd:TIGR02168 551 VVENLNAAKKAIAFL-KQNELGRVTFLPLDSIKGTeiqgndREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGG---VL 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7361 LVN--QQAQSLIRQADARNRqLIEQDNAGLNRSW------QDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLED 7432
Cdd:TIGR02168 627 VVDdlDNALELAKKLRPGYR-IVTLDGDLVRPGGvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRK 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7433 KFRNVDPTVRSRRHLEDTKNaiQELREESNQLKSSHKEIEALSKSILTFLGEVHKPSAE--AIQAKVDKLVEQQAKLNDT 7510
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELS--RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEieELEERLEEAEEELAEAEAE 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7511 LRDKEQQVSKDLEEIEQVFRRISQLQDKLNAL----HEQLQSVHVYDEHIAQTEQLLITLNSQVQQAAEESKLLVAQtta 7586
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELTLLneeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE--- 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7587 hyQAKQNQLPSDIAQEFTALELLAERVQVTMETKEKDfkraktvRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELL 7666
Cdd:TIGR02168 861 --IEELEELIEELESELEALLNERASLEEALALLRSE-------LEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 320544548 7667 QRINHEITAIYERFT-LVKTNGQLIIENCRNSEEKtlvqttIDQLAASLAQVRGWLDE 7723
Cdd:TIGR02168 932 EGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDD------EEEARRRLKRLENKIKE 983
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
10619-11331 |
7.69e-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: 57.29 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10619 KERKELDKEVTLAKAYFNNVQQDisreAPQNPKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSdddgi 10698
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLC----TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK----- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10699 levlalWQKIFQDTFQEYHRLSTRLARSQNSSEAL---RLWRQYLQHVQSFLSC--AIPEDYSSLREQQ----QLCAIHQ 10769
Cdd:TIGR00618 258 ------KQQLLKQLRARIEELRAQEAVLEETQERInraRKAAPLAAHIKAVTQIeqQAQRIHTELQSKMrsraKLLMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10770 NLLISQQSVLSETPLESELSEQYKALTNLHNETLSR--IMQRNGELERRVSGWnayRQQLAALLDWLRQREAERNALQlR 10847
Cdd:TIGR00618 332 AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIreISCQQHTLTQHIHTL---QQQKTTLTQKLQSLCKELDILQ-R 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10848 YIHLKRVPHLKHRldAMIQQLDQGEQQSKALQE--QQQELARHCDDALATAMRMEQASIGQRISNLRAALKTWQGFLQRV 10925
Cdd:TIGR00618 408 EQATIDTRTSAFR--DLQGQLAHAKKQQELQQRyaELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10926 TQLSESYEQRVNQLQQefgaaqklldanseslptQPAAIEQLLGSLRAQRVQLGaqvsalesltvtqeelkecISPHD-- 11003
Cdd:TIGR00618 486 TRKKAVVLARLLELQE------------------EPCPLCGSCIHPNPARQDID-------------------NPGPLtr 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11004 -MKTIRQRNWLLWQQHADLDYQLanliNSIEERLSLLSNYQIRYDRISQWLQRLEQRVEKDADVTamtnpeqaaKQLEQQ 11082
Cdd:TIGR00618 529 rMQRGEQTYAQLETSEEDVYHQL----TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL---------QNITVR 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11083 VNSELQLRDKEREWLLSTSRELLTlysepEVRSQVQQQSDSLIDRwQRLKYLAKQKATKIGELkMTLLRLEERIALIRAW 11162
Cdd:TIGR00618 596 LQDLTEKLSEAEDMLACEQHALLR-----KLQPEQDLQDVRLHLQ-QCSQELALKLTALHALQ-LTLTQERVREHALSIR 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11163 LFEVESqLDKPLNFESYTPNVIEA---KLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDADSWRT--QVNTSGLAASAQN 11237
Cdd:TIGR00618 669 VLPKEL-LASRQLALQKMQSEKEQltyWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSdlAAREDALNQSLKE 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11238 LEQRWKNVCSQSAERKARiltiwNLLQQLIKLT--AEHKNWLGKQESQIAGFERDQKShSKHKLEERQMELRAKLEELES 11315
Cdd:TIGR00618 748 LMHQARTVLKARTEAHFN-----NNEEVTAALQtgAELSHLAAEIQFFNRLREEDTHL-LKTLEAEIGQEIPSDEDILNL 821
|
730
....*....|....*..
gi 320544548 11316 QSVNLRQ-LEQIYAKLA 11331
Cdd:TIGR00618 822 QCETLVQeEEQFLSRLE 838
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6062-6232 |
8.62e-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: 54.37 E-value: 8.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6062 DYNAYHQSLQDVEKWLLQIsfQLMAHNSLFISNREQTQEQIKQHEALLVEIQKYQTNLDDLNAKGQAQIKRYESSTPAIR 6141
Cdd:cd00176 1 KLQQFLRDADELEAWLSEK--EELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6142 ptveSQLKNIQDSYNSLLQTSVQIKNRLLESLAKFQEYEDTLDsIMRNLETYEPIIQTELdaPATSLELAQNQLRCAQEM 6221
Cdd:cd00176 79 ----ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKEL 151
|
170
....*....|.
gi 320544548 6222 QNKLNNEKSRL 6232
Cdd:cd00176 152 EEELEAHEPRL 162
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
275-376 |
9.37e-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: 51.57 E-value: 9.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 275 KTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKRIKLVNIN 354
Cdd:cd21286 3 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 82
|
90 100
....*....|....*....|..
gi 320544548 355 PADLVDGRPPVVLGLIWTIILY 376
Cdd:cd21286 83 AEEIRNGNLKAILGLFFSLSRY 104
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
414-518 |
1.12e-06 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 51.34 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 414 EKWKQGARKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLV-NLAELKKTSNRQRLETAFDVAESKLGI 492
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*.
gi 320544548 493 AKLLDAEDVDVPKPDEKSIMTYVAQF 518
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQF 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10268-11034 |
1.32e-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: 56.60 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10268 EKVGELFSLSHKISTqIAEELEGASVLRDQLQAIQEGISNQRKHQAKISVILDECEAAERQGADVLEKAVADCQAAGEEL 10347
Cdd:TIGR02168 285 ELQKELYALANEISR-LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10348 VISWQEIMRIRQMLHTLPMRLKMSVSpvKLERDISQLQDDHAFLESKCTNI---MAILRSRLAVWLR--YERQLELVHGS 10422
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVA--QLELQIASLNNEIERLEARLERLedrRERLQQEIEELLKklEEAELKELQAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10423 VQETDFMMELIRVHGQVDYERLRKATERLEGLAGDLHNREQLIDELKGAAKPLiescdVQIVEQIESAvQEAVVAWNDTS 10502
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL-----ERLQENLEGF-SEGVKALLKNQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10503 ENLQQLRTRYQRAVELWDKYRNASAAVKNSIDQQMdAVKSLEQPLDALQHAKvcQDNLTTQNdrILELRDIVAKIAADVG 10582
Cdd:TIGR02168 516 SGLSGILGVLSELISVDEGYEAAIEAALGGRLQAV-VVENLNAAKKAIAFLK--QNELGRVT--FLPLDSIKGTEIQGND 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10583 LDASALMQGELDALgQRLAECKDAITT-----LANVAETQDkerkeLDKEVTLAKAY---FNNVQQD---ISREAPQNPK 10651
Cdd:TIGR02168 591 REILKNIEGFLGVA-KDLVKFDPKLRKalsylLGGVLVVDD-----LDNALELAKKLrpgYRIVTLDgdlVRPGGVITGG 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10652 ESEEQLAALrAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSE 10731
Cdd:TIGR02168 665 SAKTNSSIL-ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10732 ALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLCAIHQNLLISQQSVLSE-----TPLESELSEQYKALTNLhNETLSRI 10806
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeelKALREALDELRAELTLL-NEEAANL 822
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10807 MQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHLKRVphLKHRLDAMIQQLDQGEQQSKALQEQQQELA 10886
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE--LESELEALLNERASLEEALALLRSELEELS 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10887 RHCDDALATAMRMEQASIGQRISNLRAALKtWQGFLQRVTQLSEsyeqrvnQLQQEFGAAQKLLDANSESLPTQPAAIEQ 10966
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELR-LEGLEVRIDNLQE-------RLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320544548 10967 LLGSLRAQRVQLGA-QVSALESLtvtqEELKEcisphdmktiRQRNwlLWQQHADLDYQLANLINSIEE 11034
Cdd:TIGR02168 973 RLKRLENKIKELGPvNLAAIEEY----EELKE----------RYDF--LTAQKEDLTEAKETLEEAIEE 1025
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10568-11131 |
1.40e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10568 LELRDIVAKIAADVGLDAS-ALMQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREA 10646
Cdd:COG1196 222 LKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10647 pqnpKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARS 10726
Cdd:COG1196 302 ----QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10727 QnsSEALRLWRQYLQHVQsflscaipEDYSSLREQQQLCAIHQNLLISQQSVLSEtplESELSEQYKALTNLHNETLSRI 10806
Cdd:COG1196 378 E--EELEELAEELLEALR--------AAAELAAQLEELEEAEEALLERLERLEEE---LEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10807 MQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHLKRvphLKHRLDAMIQQLDQGEQQSKALQ--EQQQE 10884
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA---RLLLLLEAEADYEGFLEGVKAALllAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10885 LARHCDDALATAMRMEQAsigqrisnLRAALKTWQgfLQRVTQLSESYEQRVNQLQQEFGAAQKLLDANSESLPTQPAAI 10964
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAA--------LEAALAAAL--QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10965 EQLLGSLRAQRVQLGAQVSALESLTVTQEELKEcispHDMKTIRQRNWLLWQQHADLDY--------------QLANLIN 11030
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLG----RTLVAARLEAALRRAVTLAGRLrevtlegeggsaggSLTGGSR 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11031 SIEERLSLLSNYQIRYDRISQWLQRLEQRVEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWLLSTSRELLTLYS- 11109
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEl 747
|
570 580 590
....*....|....*....|....*....|..
gi 320544548 11110 ----------EPEVRSQVQQQSDSLIDRWQRL 11131
Cdd:COG1196 748 leeealeelpEPPDLEELERELERLEREIEAL 779
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3282-3494 |
1.78e-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: 53.22 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3282 DHESFDKDFDSFKQNLqSSVDELAKTNEIVGDQSVLQDQQNKLREMSDKRILDSTLFEGLIDRGEKLyGHTSPEGREIIR 3361
Cdd:cd00176 1 KLQQFLRDADELEAWL-SEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQL-IEEGHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3362 QQLRALRTLWDNYTDDLNSATQKIDQCLLQFNEFSIAqDQLTKWLKDVDKAMQSHtEPKTTLQEKRAQLQNHKLLHQEIT 3441
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 320544548 3442 THNVLVDNVCDKAQILVDQIKDNSLNVY---LTSIKQLFQSIVQKSDEILHNLDDC 3494
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIeekLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4248-4445 |
1.80e-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: 53.22 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4248 KWSGFDEIADSLKSWLDETENALpADIELKTTLDEKRNKLQTYRDILNDINNHQVELGNLQEIAANL----PEKTELVDQ 4323
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieegHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4324 IIKDISDRFGKLQKRAQNYVERYEGIVSAHQQYSKAvMDAQEFIDATLNTV-HYWGDLDLEQISLHtnLDRLKNLKASLA 4402
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALaSEDLGKDLESVEEL--LKKHKELEEELE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 320544548 4403 DEFPRVDQVRALGEKVIPGTVDVGQVNIKSQIDTTQQEWESLL 4445
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELL 199
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3545-3811 |
2.27e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3545 NKPQAMKIISDIRDLFEkvkattsekgNEVLD-KEIEELETTMKSHFDDIEGIEG------KQKDVL----AQWDKFEKA 3613
Cdd:COG4913 198 HKTQSFKPIGDLDDFVR----------EYMLEePDTFEAADALVEHFDDLERAHEaledarEQIELLepirELAERYAAA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3614 LEELTKW--CRSAEAVFREQQLQSTLHEKVEQLEK-YKIQRELILQKEKEIDAFG---DAAHALLNNCGADRLKTLTTQI 3687
Cdd:COG4913 268 RERLAELeyLRAALRLWFAQRRLELLEAELEELRAeLARLEAELERLEARLDALReelDELEAQIRGNGGDRLEQLEREI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3688 TNryqlLQVLSKEVVNRWSNLvddhqfyqdkynevDLWLQPIEsqmakvlldeptqssniLQVLLSEKEqaeslFAALNA 3767
Cdd:COG4913 348 ER----LERELEERERRRARL--------------EALLAALG-----------------LPLPASAEE-----FAALRA 387
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 320544548 3768 AGeKALPETSTQGREKIRKDLRDIRDRWDKLDEGIRNLEKRQEA 3811
Cdd:COG4913 388 EA-AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
3161-4328 |
2.89e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 55.44 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3161 EDFMTLCQDSLVKLKQLCSKWDEFDTIIEELDNWMKNVEAVVKNQNLKSTAE-AKNAHLKQLQDISKDI--------ERR 3231
Cdd:TIGR01612 751 KDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDnIKDEDAKQNYDKSKEYiktisikeDEI 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3232 GAAINELMDQGREIegetdlnlkLSRLNtRYQTLKNLCKESI-------AKYVNYVKDHESfDKDFDSFKQNLQSSVDEL 3304
Cdd:TIGR01612 831 FKIINEMKFMKDDF---------LNKVD-KFINFENNCKEKIdseheqfAELTNKIKAEIS-DDKLNDYEKKFNDSKSLI 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3305 AKTNeivgdQSVLQDQQN--KLREMSDK-RILDSTL--FEGLIDRGEKLyghtspegREIIRQQLRALR---TLWDNYTD 3376
Cdd:TIGR01612 900 NEIN-----KSIEEEYQNinTLKKVDEYiKICENTKesIEKFHNKQNIL--------KEILNKNIDTIKesnLIEKSYKD 966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3377 DL-NSATQKIDQCLLQFNEFSiaqdqLTKWLKDVDKAMQSHTEPKTTLQEKRAQLQNHKLLHQEITTHNVLvdnvcdkaQ 3455
Cdd:TIGR01612 967 KFdNTLIDKINELDKAFKDAS-----LNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFDEKEKATNDIE--------Q 1033
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3456 ILVDqIKDNSLNVYLTsikqLFQSIVQKSDEILHNLDDCVQKHNElnNALSSAKTWISN-----EKAKLLECDDaYGEKA 3530
Cdd:TIGR01612 1034 KIED-ANKNIPNIEIA----IHTSIYNIIDEIEKEIGKNIELLNK--EILEEAEINITNfneikEKLKHYNFDD-FGKEE 1105
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3531 DIKRKIETLGQLAQNKPQAMKIISDIRDLfEKVKATTSEKGNEvLDKEIEELETTMKSHF--DDIEGIEGKQKDVLAQWD 3608
Cdd:TIGR01612 1106 NIKYADEINKIKDDIKNLDQKIDHHIKAL-EEIKKKSENYIDE-IKAQINDLEDVADKAIsnDDPEEIEKKIENIVTKID 1183
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3609 KFEKALEELTKWCRSAEAVFREQqlqsTLHEKV----------------EQLEKYKIQRELILQKE----KEIDAFGDAA 3668
Cdd:TIGR01612 1184 KKKNIYDEIKKLLNEIAEIEKDK----TSLEEVkginlsygknlgklflEKIDEEKKKSEHMIKAMeayiEDLDEIKEKS 1259
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3669 HALLNNCGADRLKTLTTQITN----RYQLLQVLSKEVVNRWSNLVDDH-QFYQDKYNEVDlwLQPIESQMAKVLLDEPTQ 3743
Cdd:TIGR01612 1260 PEIENEMGIEMDIKAEMETFNishdDDKDHHIISKKHDENISDIREKSlKIIEDFSEESD--INDIKKELQKNLLDAQKH 1337
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3744 SSNILQVLlsekEQAESLFAALNAAGEKALPETSTQGREKIRKDLRDIRDRWDKLDEGIRNLEkrqeaQGVQLSSYQDIL 3823
Cdd:TIGR01612 1338 NSDINLYL----NEIANIYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIK-----DDINLEECKSKI 1408
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3824 NQTVNWLDQVEKLIHNENPASWTSAQEIRSKLY--KYKATNQDINSHKRIVEAVNEKAAALLG-------SAAPANADEI 3894
Cdd:TIGR01612 1409 ESTLDDKDIDECIKKIKELKNHILSEESNIDTYfkNADENNENVLLLFKNIEMADNKSQHILKikkdnatNDHDFNINEL 1488
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3895 SKAVAEVNKRYDQVGQDcAKLVADLDGAFDVYQQ--------FSELQ-KAQQDYQKNLWDRLTGYSDYSGNKAALQARL- 3964
Cdd:TIGR01612 1489 KEHIDKSKGCKDEADKN-AKAIEKNKELFEQYKKdvtellnkYSALAiKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKs 1567
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3965 -QKINEIqdalpegvaklKSLEDHIEQQASNIPARSKEVMarDLANLHADFEKFGASLSDVKSGLENRLQQWNDYEINLD 4043
Cdd:TIGR01612 1568 eQKIKEI-----------KKEKFRIEDDAAKNDKSNKAAI--DIQLSLENFENKFLKISDIKKKINDCLKETESIEKKIS 1634
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4044 RL--------ITWLGEAENSLKNY-----NLKSSFEEKEEQLNGFQSlaqNLRQNEADFDKVKDDTS-ELVQSSGETRIA 4109
Cdd:TIGR01612 1635 SFsidsqdteLKENGDNLNSLQEFleslkDQKKNIEDKKKELDELDS---EIEKIEIDVDQHKKNYEiGIIEKIKEIAIA 1711
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4110 vNVQQVSSRFQSIQATAKEILKKC-----------EQAVQDHGHFNDKYKQCADwLANAQARYddccdLSTVAsrddllK 4178
Cdd:TIGR01612 1712 -NKEEIESIKELIEPTIENLISSFntndlegidpnEKLEEYNTEIGDIYEEFIE-LYNIIAGC-----LETVS------K 1778
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4179 KQVVIQELLAQQPTATQLLNSTVELGEKCygstategreaiRSQLDDLT---FDQL-------FDNIAITARKIQDKIAK 4248
Cdd:TIGR01612 1779 EPITYDEIKNTRINAQNEFLKIIEIEKKS------------KSYLDDIEakeFDRIinhfkkkLDHVNDKFTKEYSKINE 1846
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4249 wsGFDEIADSLKSWLDETENALPADIeLKTTLDEKRN----KLQTYRDILNDINNHQVELGNLQEIAANLPEKTELVDQI 4324
Cdd:TIGR01612 1847 --GFDDISKSIENVKNSTDENLLFDI-LNKTKDAYAGiigkKYYSYKDEAEKIFINISKLANSINIQIQNNSGIDLFDNI 1923
|
....
gi 320544548 4325 IKDI 4328
Cdd:TIGR01612 1924 NIAI 1927
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3712-3910 |
2.92e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 52.83 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3712 HQFYQDkYNEVDLWLQPIESQMAKVLLDEPTQSSNIL----QVLLSEKEQAESLFAALNAAGEKaLPETSTQGREKIRKD 3787
Cdd:cd00176 3 QQFLRD-ADELEAWLSEKEELLSSTDYGDDLESVEALlkkhEALEAELAAHEERVEALNELGEQ-LIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3788 LRDIRDRWDKLDEGIRNLEKRQEAQGVQLSSYQDILnQTVNWLDQVEKLIHNENPASwtSAQEIRSKLYKYKATNQDINS 3867
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK--DLESVEELLKKHKELEEELEA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 320544548 3868 HKRIVEAVNEKAAALLGSAAPANADEISKAVAEVNKRYDQVGQ 3910
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLE 200
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5195-5684 |
5.46e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5195 DKYENLTKQAKDLYEKQKNTIESYQSLIDAGNEFATWLRNAKERlskcseptgdkqaLAEKTHQLKILQGELPEGAQKLK 5274
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKE-------------LEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5275 NAleqgeiacrSAEPEDCEIIEQEVALLQEEfdayREALNKAKDYLEVGIVKWSDYQDQYTEALEWLSKTEALVQSYNKL 5354
Cdd:PRK03918 225 KL---------EKEVKELEELKEEIEELEKE----LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5355 QDSLIQKKVVLEQFqghLQTLFDWQKTLDDLNMKAQVLLETCSDtrisnaIMQLTTKYNALLTLAKEVMRRLEmhyqEHQ 5434
Cdd:PRK03918 292 AEEYIKLSEFYEEY---LDELREIEKRLSRLEEEINGIEERIKE------LEEKEERLEELKKKLKELEKRLE----ELE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5435 QHHSLYEECQSW---------------IEKTREKLSECE----QIPGTLNEVQIKLNTVKNLRQGFETGQNKL------- 5488
Cdd:PRK03918 359 ERHELYEEAKAKkeelerlkkrltgltPEKLEKELEELEkakeEIEEEISKITARIGELKKEIKELKKAIEELkkakgkc 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5489 ----RYLLELKEKVIMNTEQNGAAKIQEDtealKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILiEWLEDVEPSVK 5564
Cdd:PRK03918 439 pvcgRELTEEHRKELLEEYTAELKRIEKE----LKEIEEKERKLRKELRELEKVLKKESELIKLKELA-EQLKELEEKLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5565 TSDefLNDLSEK----RAALEKFRVIQRDINGHNDIVEKINQRLKEDNSLD--LKDFQPGLTKF-DDLQTQVNKIIESLE 5637
Cdd:PRK03918 514 KYN--LEELEKKaeeyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEkkLDELEEELAELlKELEELGFESVEELE 591
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 320544548 5638 NQVNSHEKYKQAYNELQDWLRRTRIEVEQCADCHGEKDQVESRLNRL 5684
Cdd:PRK03918 592 ERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAET 638
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
268-374 |
5.53e-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: 49.75 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 268 EQERVQkktFTNWINSYLL------KRVP-PLRIDDLINDLRDGTKLIALL----------EVLSgerLPVEKGRVLRRP 330
Cdd:cd21294 5 EDERRE---FTKHINAVLAgdpdvgSRLPfPTDTFQLFDECKDGLVLSKLIndsvpdtideRVLN---KPPRKNKPLNNF 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 320544548 331 HFLSNANTALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21294 79 QMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
7065-7680 |
5.80e-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: 54.20 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7065 EQLQSLKNQLQNLRKAVESQRQKHQLQLES------HKKMAAELSEILDWLHSHEGAAKSRPLLDRDpesvERELQKHQS 7138
Cdd:TIGR00618 270 EELRAQEAVLEETQERINRARKAAPLAAHIkavtqiEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ----QSSIEEQRR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7139 LSQDIESYLNKFNKINDgvkteigMPSSLLEMLSEgrslvaslPHELEEREKYLKNNRDSRLEYMQLVAKFNDwvheael 7218
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAHE-------VATSIREISCQ--------QHTLTQHIHTLQQQKTTLTQKLQSLCKELD------- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7219 RLQNSQHGIDYEHLVQ-DLDEHKIFFGNEAPIRNLVHKQIQEAADKIWSSLN------NYEQSELSAELAQFQTKLTNTL 7291
Cdd:TIGR00618 404 ILQREQATIDTRTSAFrDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKlekihlQESAQSLKEREQQLQTKEQIHL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7292 ANAKTQQSE---LEKEAERWREYQQSIDRVKATIERTKFVDEPVQNLAGLHFNIQKLSHAIGNVQSQnsdLTLVNQQAQS 7368
Cdd:TIGR00618 484 QETRKKAVVlarLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQ---LTSERKQRAS 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7369 LIRQAdarnrQLIEQDNAGLNRSWQDLVRSLeqrrDNLQQLAEhwdgfenSLHAWEKALGRLEDKFRnvdptVRSRRHLE 7448
Cdd:TIGR00618 561 LKEQM-----QEIQQSFSILTQCDNRSKEDI----PNLQNITV-------RLQDLTEKLSEAEDMLA-----CEQHALLR 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7449 DTKNAIQELR---EESNQLKSSHKEIEALSKSILTFLGEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEI 7525
Cdd:TIGR00618 620 KLQPEQDLQDvrlHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7526 EQvfrrisqlqdKLNALHEQLQSVHVYDEHIAQTEQLLITLNSQVQQ------------AAEESKLLVAQTTAHYQAKQn 7593
Cdd:TIGR00618 700 AQ----------CQTLLRELETHIEEYDREFNEIENASSSLGSDLAAredalnqslkelMHQARTVLKARTEAHFNNNE- 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7594 QLPSDIaQEFTALELLAERVQVTMETKEKDFKRAKTVRTEYVDGVDE-VQRWLLQAEVQVQERSLTPTQMKELLQRInHE 7672
Cdd:TIGR00618 769 EVTAAL-QTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdEDILNLQCETLVQEEEQFLSRLEEKSATL-GE 846
|
....*...
gi 320544548 7673 ITAIYERF 7680
Cdd:TIGR00618 847 ITHQLLKY 854
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
268-374 |
6.67e-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: 50.00 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 268 EQERVQKKTFTNWINSyllKRVPPlRIDDLINDLRDGTKLIALLEVLsgeRLPVEKGRVLRRPH--------FLSNANTA 339
Cdd:cd21331 18 EGETREERTFRNWMNS---LGVNP-HVNHLYGDLQDALVILQLYEKI---KVPVDWNKVNKPPYpklganmkKLENCNYA 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 320544548 340 LQFLASK-RIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21331 91 VELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLM 126
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
10432-10997 |
8.76e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10432 LIRVHGQVDYERLRKATERLEGLAGDLHNREQLIDEL----------KGAAKPLIESCD--VQIVEQIESAV---QEAVV 10496
Cdd:PRK02224 189 LDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYeeqreqaretRDEADEVLEEHEerREELETLEAEIedlRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10497 AWNDTSENL-QQLRTRYQRAVELWDKYRNASA------AVKNSIDQQMDAV-KSLEQPLDALQHAKVCQDNLTTQNDRIL 10568
Cdd:PRK02224 269 ETEREREELaEEVRDLRERLEELEEERDDLLAeaglddADAEAVEARREELeDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10569 ELRDIVAKIAADvgldasalMQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQqDISREAPQ 10648
Cdd:PRK02224 349 EDADDLEERAEE--------LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE-DFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10649 NPKESEEQLAALRAHLQTLARTEEQLRQLKER------HQNSEVAPSVASSDDDGilEVLALWQKIFQDTFQEYHRLSTR 10722
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEALLEAgkcpecGQPVEGSPHVETIEEDR--ERVEELEAELEDLEEEVEEVEER 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10723 LARSQNSSEALRlwrqylqhvqsflscaipeDYSSLREQ----QQLCAIHQNLLISQQSVLSE-----TPLESELSEQYK 10793
Cdd:PRK02224 498 LERAEDLVEAED-------------------RIERLEERredlEELIAERRETIEEKRERAEElreraAELEAEAEEKRE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10794 ALTNLHNETlSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQlryihlkrvpHLKHRLDAMIQQLDQGEQ 10873
Cdd:PRK02224 559 AAAEAEEEA-EEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIE----------RLREKREALAELNDERRE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10874 QSKALQEQQQELARHCDDAlatamrmeqasigqRISNLRAALKTWQGFLQRVT-QLSESYEQRvNQLQQEFGAAQKLLDA 10952
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEA--------------RIEEAREDKERAEEYLEQVEeKLDELREER-DDLQAEIGAVENELEE 692
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 320544548 10953 nseslptqpaaieqlLGSLRAQRVQLGAQVSALESLTVTQEELKE 10997
Cdd:PRK02224 693 ---------------LEELRERREALENRVEALEALYDEAEELES 722
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7307-7517 |
9.70e-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: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7307 RWREYQQSIDRVKATIERTKFV---DEPVQNLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIrQADARNRQLIEQ 7383
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELlssTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7384 DNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFeNSLHAWEKALGRLEDKFRNVDPTvrsrRHLEDTKNAIQELREESNQ 7463
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALASEDLG----KDLESVEELLKKHKELEEE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 320544548 7464 LKSSHKEIEALSKSILTFLGEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQ 7517
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKK 208
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
10784-11459 |
1.02e-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: 53.43 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10784 LESELSEQYKALTNLHnETLSRIMQRNGELERRVSgWNAYRQQLAALLDWLRQREAE----RNALQLRYIHLKRVPHLKH 10859
Cdd:TIGR00618 224 LEKELKHLREALQQTQ-QSHAYLTQKREAQEEQLK-KQQLLKQLRARIEELRAQEAVleetQERINRARKAAPLAAHIKA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10860 rldamIQQLDQGEQQSKA-LQEQQQELARhcddalATAMRMEQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQ 10938
Cdd:TIGR00618 302 -----VTQIEQQAQRIHTeLQSKMRSRAK------LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10939 LQQEFGAAQKLLdanseSLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELK-ECISPHDMKTIRQRNWLLWQQ 11017
Cdd:TIGR00618 371 SCQQHTLTQHIH-----TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQgQLAHAKKQQELQQRYAELCAA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11018 HADLDYQLANLINSIEERLSllsnyqirydrisqwlQRLEQRVEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWL 11097
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESA----------------QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGS 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11098 LSTSRELLTLYSEPEVRSQVQQQsdsLIDRWQRLKYLAKQKATKIGELKMTLLRLEERIALIRAWLF-------EVESQL 11170
Cdd:TIGR00618 510 CIHPNPARQDIDNPGPLTRRMQR---GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSiltqcdnRSKEDI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11171 DKPLNFESYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDAD-SWRTQVNTSGLAASAQNLEQ-----RWKN 11244
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQcSQELALKLTALHALQLTLTQervreHALS 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11245 VCSQSAERKARILTIWNLLQQLIKLTAEHKNWLGKQESQIAGFERDQKSHSKHkLEERQMELRAKLEELESQSVNLRQLE 11324
Cdd:TIGR00618 667 IRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE-FNEIENASSSLGSDLAAREDALNQSL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11325 QIYAKLAMSAGVEPENIQKLTLPTKVMVSMwrqltprchalLDAIDKDAKLMREFNNAQLEATNSLNAIQKAL--EQLPS 11402
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFNNNEEVTAALQ-----------TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEigQEIPS 814
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 320544548 11403 AE-----NQQTSKAEPKAVLQRLESLEKKLQDAQQHVQQADNLAQEAKTRTKQQPQLKQLLE 11459
Cdd:TIGR00618 815 DEdilnlQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
11042-11255 |
1.34e-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: 50.52 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11042 YQIRYDRISQWLQRLEQRVEKDADVTAMTNPEQAAKQLeQQVNSELQLRDKEREWLLSTSRELLTLYSEPEvrSQVQQQS 11121
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKH-EALEAELAAHEERVEALNELGEQLIEEGHPDA--EEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11122 DSLIDRWQRLKYLAKQKATKIGELKMTLLRLEErIALIRAWLFEVESQLDKPLNFESYTPnvIEAKLKEHEQIQRSIEHH 11201
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLES--VEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 320544548 11202 SSNVGEVLNLVEMLLNDAdswrTQVNTSGLAASAQNLEQRWKNVCSQSAERKAR 11255
Cdd:cd00176 159 EPRLKSLNELAEELLEEG----HPDADEEIEEKLEELNERWEELLELAEERQKK 208
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
11149-11358 |
1.59e-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: 50.52 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11149 LLRLEERIALIRAWLFEVESQLDKPLNfeSYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDAdswrtQVNT 11228
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDY--GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-----HPDA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11229 SGLAASAQNLEQRWKNVCSQSAERKARILTIWNLLQQLIKLTAEhKNWLGKQESQIAgfeRDQKSHSKHKLEERQMELRA 11308
Cdd:cd00176 75 EEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-EQWLEEKEAALA---SEDLGKDLESVEELLKKHKE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 320544548 11309 KLEELESQSVNLRQLEQIYAKLAMSAgvEPENIQKLTLPTKVMVSMWRQL 11358
Cdd:cd00176 151 LEEELEAHEPRLKSLNELAEELLEEG--HPDADEEIEEKLEELNERWEEL 198
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3360-4146 |
1.63e-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: 52.75 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3360 IRQQLRALRtlWDNYTDDLNSATQKIDQCLLQFNEfsiaqdqltkwlkdvdkAMQSHTEPKTTLQEKRAQLQNHKLLHQE 3439
Cdd:TIGR02168 218 LKAELRELE--LALLVLRLEELREELEELQEELKE-----------------AEEELEELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3440 I-TTHNVLVDNVCDKAQILvdQIKDNSLNVYLTSIKQLFQSIVQKSDEILHNLddcvQKHNELNNALSSAKTWISNEKAK 3518
Cdd:TIGR02168 279 LeEEIEELQKELYALANEI--SRLEQQKQILRERLANLERQLEELEAQLEELE----SKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3519 LLECDDAYGEKADIKRKIETLGQLAQNKPQAMKiiSDIRDLFEKVkattsekgnEVLDKEIEELETTmkshfddIEGIEG 3598
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLR--SKVAQLELQI---------ASLNNEIERLEAR-------LERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3599 KQKDVLAQWDKFEKALEELTKWCRSAEAVFREQQLQSTLHEKVEQLEKYKIQRELILQKEKEIDAFGDAAHALLNncgad 3678
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA----- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3679 RLKTLTTqITNRYQLLQVLSKEVVNRWSNLVDDHQFYQDKYnEVDlwlQPIESQMAKVLldeptqSSNILQVLLSEKEQA 3758
Cdd:TIGR02168 490 RLDSLER-LQENLEGFSEGVKALLKNQSGLSGILGVLSELI-SVD---EGYEAAIEAAL------GGRLQAVVVENLNAA 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3759 ESLFAAL--NAAGEKALPETSTQGREKIRKDLRDIRDRWDKLDEGIRNLEKRQEAqgvqlssYQDILNqtvNWLDQVekL 3836
Cdd:TIGR02168 559 KKAIAFLkqNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK-------LRKALS---YLLGGV--L 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3837 IHNenpaSWTSAQEIRSKL-YKYKATNQD---INSHKRIVEAVNEKAAALLG------------SAAPANADEISKAVAE 3900
Cdd:TIGR02168 627 VVD----DLDNALELAKKLrPGYRIVTLDgdlVRPGGVITGGSAKTNSSILErrreieeleekiEELEEKIAELEKALAE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3901 VNKRYDQVGQDCAKLVADLDgafDVYQQFSELQKaqqDYQKNLWDRLTGYSDYSGNKAALQARLQKINEIQDALPEGVAK 3980
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELE---ELSRQISALRK---DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3981 LKSLEDHIEQQASNIparskEVMARDLANLHADFEKFGASLSDVKSGLENRLQQWNDYEINLDRLITWLGEAENSLknyn 4060
Cdd:TIGR02168 777 LAEAEAEIEELEAQI-----EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI---- 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4061 lkssfEEKEEQLngfQSLAQNLRQNEADFDKVKDDTSELVQSSGEtrIAVNVQQVSSRFQSIQATAKEILKKCEQAVQDH 4140
Cdd:TIGR02168 848 -----EELSEDI---ESLAAEIEELEELIEELESELEALLNERAS--LEEALALLRSELEELSEELRELESKRSELRREL 917
|
....*.
gi 320544548 4141 GHFNDK 4146
Cdd:TIGR02168 918 EELREK 923
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5752-5959 |
1.87e-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: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5752 WQTFLQKFNKINLWIETMNKRVTKSQegenkTPEDLVNAKKLLE-------EVLAEKDNVEDLNDNCELLMEQS--ACTR 5822
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTD-----YGDDLESVEALLKkhealeaELAAHEERVEALNELGEQLIEEGhpDAEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5823 IRDQTIETQANYTKLLTSAQGLVAKIEKNLSDHtEFLNYKKEMDAWIEKAQQVLDDCSTDGDAAIIAQKLDTVNSLASRL 5902
Cdd:cd00176 77 IQERLEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 320544548 5903 PEGQHLLALVQDAYSKASNITPEDKQEKLRELMTKVREDWDALGLAVKQKLSDLKQA 5959
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
10533-10997 |
2.03e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10533 IDQQMDAVKSLEQPLDALQHAkvcQDNLTTQNDRILELRDIVAKIAADVGLDASALMQGELDALGQRLAECKDAITTLAN 10612
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAEL---QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10613 VAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVAS 10692
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10693 SDDDGILEVLALWQKIfQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLCAihqnll 10772
Cdd:COG4717 230 EQLENELEAAALEERL-KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK------ 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10773 isqqsvlsetplESELSEQYKALTNLHNETLSRIMQRNG-ELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHL 10851
Cdd:COG4717 303 ------------EAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10852 KRVPHLKH-------RLDAMIQQLDQGEQQSKALQEQQQELARHCDDALATAMRMEQASIGQRISNLRAALktwqgflqr 10924
Cdd:COG4717 371 EIAALLAEagvedeeELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEEL--------- 441
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320544548 10925 vtqlsESYEQRVNQLQQEFGAAQKLLDA--NSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELKE 10997
Cdd:COG4717 442 -----EELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
273-380 |
2.06e-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: 48.82 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 273 QKKTFTNWINSYL-----LKRVPPLR--IDDLINDLRDGTKLIALLEVLS----GERLPVEKGRVLRRPHflSNANTALQ 341
Cdd:cd21292 25 EKVAFVNWINKNLgddpdCKHLLPMDpnTDDLFEKVKDGILLCKMINLSVpdtiDERAINKKKLTVFTIH--ENLTLALN 102
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 320544548 342 FLASKRIKLVNINPADLVDGRPPVVLGLIWTII---LYFQIE 380
Cdd:cd21292 103 SASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIrigLFADIE 144
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7633-7836 |
2.48e-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: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7633 EYVDGVDEVQRWLLQAEVQVQERSL--TPTQMKELLQR---INHEITAIYERFTLVKTNGQLIIEncRNSEEKTLVQTTI 7707
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYgdDLESVEALLKKheaLEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7708 DQLAASLAQVRGWLDEKKQAVGDSLDAWtRFMNLYQIVMSWASEKRNFIDQTIELRTLPEARNKLN---DYVTSVKSIKP 7784
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKkhkELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 320544548 7785 IVKHLSEMDKELEHIGQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEA 7836
Cdd:cd00176 161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7101-7304 |
2.62e-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: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7101 ELSEILDWLHSHEGAAKSrPLLDRDPESVERELQKHQSLSQDIESYLNKFNKINDG----VKTEIGMPSSLLEMLSEGRS 7176
Cdd:cd00176 8 DADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELgeqlIEEGHPDAEEIQERLEELNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7177 LVASLPHELEEREKYLKNNRDsRLEYMQLVAKFNDWVHEAELRLQNSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLVhKQ 7256
Cdd:cd00176 87 RWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRL-KS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 320544548 7257 IQEAADKIWSSLNNYEQSELSAELAQFQTKLTNTLANAKTQQSELEKE 7304
Cdd:cd00176 165 LNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7424-8162 |
2.66e-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: 52.38 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7424 EKALGRLEDKFRNVDptvRSRRHLEDTKNAIQELREESNQ------LKSSHKEIEA--LSKSIltflgEVHKPSAEAIQA 7495
Cdd:TIGR02169 173 EKALEELEEVEENIE---RLDLIIDEKRQQLERLRREREKaeryqaLLKEKREYEGyeLLKEK-----EALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7496 KVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQL-QDKLNALHEQLQSVHVydeHIAQTEQLLITLNSQVQQAA 7574
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEA---EIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7575 EESKLLVAQTTAhYQAKQNQLPSDIAQEFTALELLAERVQVTMETKEKDFKRAKTVRTEY---VDGVDEVQRWLLQAEVQ 7651
Cdd:TIGR02169 322 ERLAKLEAEIDK-LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFaetRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7652 VQERSLTPTQMKELLQRINHEITAIYERFTLVKtngqliiencrnsEEKTLVQTTIDQLAASLAQVRGWLDEKKQAVGDS 7731
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIE-------------AKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7732 LDAWTRFMNLYQIVMSWASEKRnfidqtielRTLPEARNKLNDYVTSVKSIKPIVKHLSEMDKELehIGQVTTVGDLKDK 7811
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQ---------RELAEAEAQARASEERVRGGRAVEEVLKASIQGV--HGTVAQLGSVGER 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7812 LQEAEDAKIS--VEAVLLERNSLLQEACEEWDQCE---------RKIKDIRSWHEKTKQG--------LDSSQQQKKP-- 7870
Cdd:TIGR02169 537 YATAIEVAAGnrLNNVVVEDDAVAKEAIELLKRRKagratflplNKMRDERRDLSILSEDgvigfavdLVEFDPKYEPaf 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7871 ---LRDQLGFCEKTLA-DINVQKTKLRLSIEKLEVH------FRNGMGGDPRLSENVDDLVRVLDGLGELVKAKSqSLEQ 7940
Cdd:TIGR02169 617 kyvFGDTLVVEDIEAArRLMGKYRMVTLEGELFEKSgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELS-SLQS 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7941 TLAQIdvyQQQMQSLRQRIIQEEQQLRLVMAPTYLPHDRERALAEQQDLITQELDELLQSLSSVEDGIANMNQ--SSLDG 8018
Cdd:TIGR02169 696 ELRRI---ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAriEELEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 8019 MLHGLKLIQSNLEVHERDAI--ELKNQAKKLPTD--------PATERLLNDtVDRIDLLLRRTQQGITMIANAMHGQKK- 8087
Cdd:TIGR02169 773 DLHKLEEALNDLEARLSHSRipEIQAELSKLEEEvsriearlREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKs 851
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320544548 8088 RQQEIDEYQQHLLELEQWIIEVSAELASFEptsDSSTDeqvLKSQVERSQQLLRTLKDRQQSMEDLVEQTRQLQS 8162
Cdd:TIGR02169 852 IEKEIENLNGKKEELEEELEELEAALRDLE---SRLGD---LKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1785-1996 |
2.74e-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: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 1785 WQQFQAGLQQIKPAVEQSEVKVNNVVSkPISLEEAVAMQQNAQQFETQCQEQLDKLHGISNISHKmLCKTNAPD------ 1858
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQ-LIEEGHPDaeeiqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 1859 ELDAMHSRWTAVHENAKQASAKLEKLVANWKsFDADAAKLEDWVGQGEQQMSRRPavlNTPHIDKLEKELVKLKSFNNEI 1938
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASED---LGKDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 320544548 1939 SQQQAKLVTLGQNADQISLHLAPEGAAALKDRVNQMKGKLQKLSEATRGHINEVSDAI 1996
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1921-3326 |
3.19e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.98 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 1921 IDKLEKELVK-LKSFNNEISQQQAKLVTlgqNADQISLHL--------APEGAAALKDRVNQMKGKLQKLSEATRGHINE 1991
Cdd:TIGR01612 1057 IDEIEKEIGKnIELLNKEILEEAEINIT---NFNEIKEKLkhynfddfGKEENIKYADEINKIKDDIKNLDQKIDHHIKA 1133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 1992 VSDaiISRQDfnaklvnfSNWMEQLRNQVTQVEEI--------NPERVETSLHVIHALLqehaDKKPSfnaIYDEVKQL- 2062
Cdd:TIGR01612 1134 LEE--IKKKS--------ENYIDEIKAQINDLEDVadkaisndDPEEIEKKIENIVTKI----DKKKN---IYDEIKKLl 1196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2063 -ALGATPEESNALNDAYTALVVNYQNLETNMLQ------KKA-----ALEKWTELL--------------GWKNDTESHL 2116
Cdd:TIGR01612 1197 nEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEkideekKKSehmikAMEAYIEDLdeikekspeienemGIEMDIKAEM 1276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2117 NYLK--HQLDKPEGPAAEELSKVIDEIDN----LGQGIgYWKGQAKEIDENPAIQLRDALSRRPLIaTQIVNDVENKLEN 2190
Cdd:TIGR01612 1277 ETFNisHDDDKDHHIISKKHDENISDIREkslkIIEDF-SEESDINDIKKELQKNLLDAQKHNSDI-NLYLNEIANIYNI 1354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2191 LKLRSQSQQQQIQqmtvrKDKFHALEHNFGQALQE--NRAKLDEILRQHPTLNNIDQIIADLV---ALNDALKYQADLKN 2265
Cdd:TIGR01612 1355 LKLNKIKKIIDEV-----KEYTKEIEENNKNIKDEldKSEKLIKKIKDDINLEECKSKIESTLddkDIDECIKKIKELKN 1429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2266 RI----------------HDEGSLLMREDIASMPAIQESLLIMDKN-----YDSLQNEIADRIQKYNlisqalrEYADSK 2324
Cdd:TIGR01612 1430 HIlseesnidtyfknadeNNENVLLLFKNIEMADNKSQHILKIKKDnatndHDFNINELKEHIDKSK-------GCKDEA 1502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2325 DKFSKELKKAEDLY--------------------NAIPQQPRDET-------ELHQA----SEKTRKTMEQLRKSKLSLD 2373
Cdd:TIGR01612 1503 DKNAKAIEKNKELFeqykkdvtellnkysalaikNKFAKTKKDSEiiikeikDAHKKfileAEKSEQKIKEIKKEKFRIE 1582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2374 ELERRGNNVGKlfSAIGEPIPQEvPQEVTAAKqhwqdLHD-KTAKNAHVYETEAV--------IWSQIEDAKK--DLLPW 2442
Cdd:TIGR01612 1583 DDAAKNDKSNK--AAIDIQLSLE-NFENKFLK-----ISDiKKKINDCLKETESIekkissfsIDSQDTELKEngDNLNS 1654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2443 LSETNQGLCDAADNsieIEFGPMRLSKYRTELPSYQALKDS--------IVEKTNDLVKINKGaEIPALSALNKLLSEQF 2514
Cdd:TIGR01612 1655 LQEFLESLKDQKKN---IEDKKKELDELDSEIEKIEIDVDQhkknyeigIIEKIKEIAIANKE-EIESIKELIEPTIENL 1730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2515 AEVNNNAD--------RLSAITTSFNDQEQELRRRSKEAGERVSKLREQLIKCDDMSGD----NNKIMERLQQCRALRGE 2582
Cdd:TIGR01612 1731 ISSFNTNDlegidpneKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITYDEIKNTrinaQNEFLKIIEIEKKSKSY 1810
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2583 LDN-SGNEIDNI----KQKVDELRNLYpTFSESIIPKELNNVQKRYENVDLYAKkiESSLLQFLKKFHADKVGMLKRIIA 2657
Cdd:TIGR01612 1811 LDDiEAKEFDRIinhfKKKLDHVNDKF-TKEYSKINEGFDDISKSIENVKNSTD--ENLLFDILNKTKDAYAGIIGKKYY 1887
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2658 TQREKVAWCQPESSSDKYNLDVKKSSlqevSKSIDDCKARHAETLKSL-----EMLKAVESPQNLAEL-----TSDAELL 2727
Cdd:TIGR01612 1888 SYKDEAEKIFINISKLANSINIQIQN----NSGIDLFDNINIAILSSLdsekeDTLKFIPSPEKEPEIytkirDSYDTLL 1963
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2728 R--KDMQALQDSFDQIKGILDENVDLWSQYEQSNEqisnwLRDVEGRVKAETSSQVN-LSEVPQKLQELSILQQDVLAHE 2804
Cdd:TIGR01612 1964 DifKKSQDLHKKEQDTLNIIFENQQLYEKIQASNE-----LKDTLSDLKYKKEKILNdVKLLLHKFDELNKLSCDSQNYD 2038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2805 PIinnLEQTSQQLI-------EKNPEARIGQF-VTHLVQRYQAVSKALTSYIDKIRGAQLSNANFAKaAKDFNEWFGDAK 2876
Cdd:TIGR01612 2039 TI---LELSKQDKIkekidnyEKEKEKFGIDFdVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDFSE-EKDNIIQSKKKL 2114
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2877 IEFQELARMGSPGSSSATAQQLQTVKNYIKTfdNGQILLNNAVDIGEALYPVVSpDNRERIRADLRQMREKFDYLRDEAN 2956
Cdd:TIGR01612 2115 KELTEAFNTEIKIIEDKIIEKNDLIDKLIEM--RKECLLFSYATLVETLKSKVI-NHSEFITSAAKFSKDFFEFIEDISD 2191
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2957 AFMQQVEGVliqktsieesytQVSHYLNESKAKVPT-----TDELYPTLATKKAALQ--NYKTQLQEITLHKNALKQLHD 3029
Cdd:TIGR01612 2192 SLNDDIDAL------------QIKYNLNQTKKHMISiladaTKDHNNLIEKEKEATKiiNNLTELFTIDFNNADADILHN 2259
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3030 KAVTLCDDESE-RKTDESIQE-------------------YNTLSKKIsDRITTVGNHVVKHEAYDqvLEKAQDWLNTIK 3089
Cdd:TIGR01612 2260 NKIQIIYFNSElHKSIESIKKlykkinafkllnishinekYFDISKEF-DNIIQLQKHKLTENLND--LKEIDQYISDKK 2336
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3090 SEAIDILNETT-FEKEGAEEkllVVENLLQHKPEGDSIFDTCHKLLETVLTQTHPsghpalLKGFEEPKQSWEDFMTLCQ 3168
Cdd:TIGR01612 2337 NIFLHALNENTnFNFNALKE---IYDDIINRENKADEIENINNKENENIMQYIDT------ITKLTEKIQDILIFVTTYE 2407
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3169 DSLVKLKQLCSKWDEFDtIIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINELMDQGREIEGE 3248
Cdd:TIGR01612 2408 NDNNIIKQHIQDNDEND-VSKIKDNLKKTIQSFQEILNKIDEIKAQFYGGNNINNIIITISQNANDVKNHFSKDLTIENE 2486
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3249 tdlnlkLSRLNTRYQTLKNLC----KESIAKYVNYVKDHesFDKDFDSFKQNlqSSVDELAKTNEIvgdQSVLQDQQNKL 3324
Cdd:TIGR01612 2487 ------LIQIQKRLEDIKNAAheirSEQITKYTNAIHNH--IEEQFKKIENN--SNKDEVYKINEI---DNIIEKIINYN 2553
|
..
gi 320544548 3325 RE 3326
Cdd:TIGR01612 2554 KE 2555
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5072-5802 |
3.70e-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: 51.60 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5072 RDAINTEMKELQTEWDRLVKKMStaKVQLETNLLQWADYSssYSQLQQWITDREAKLQQACEQKIVKSKRGQPGLSSGLS 5151
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVS--ELEEEIEELQKELYA--LANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5152 ERKANLRQTNNIVQDIVSFEPMIQSVTSKASVLQQGAPGTE--ISDKYENLTKQAKDLYEKQK------NTIESYQSLI- 5222
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELEsrLEELEEQLETLRSKVAQLELqiaslnNEIERLEARLe 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5223 DAGNEFATWLRNAKERLSKCSEPTGDKQA--LAEKTHQLKILQGELPEGAQKLKNA---LEQGEIACRSAEPE------D 5291
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELKELQaeLEELEEELEELQEELERLEEALEELreeLEEAEQALDAAERElaqlqaR 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5292 CEIIEQEVALLQEEFDAYREALNKAK----------DYLEVG------------------IVKWSDYQDQYTEALEWLSK 5343
Cdd:TIGR02168 491 LDSLERLQENLEGFSEGVKALLKNQSglsgilgvlsELISVDegyeaaieaalggrlqavVVENLNAAKKAIAFLKQNEL 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5344 TEALVQSYNKLQDSLIQKK--VVLEQFQGHLQTLFDWQKTLDDLNMKAQVLLETC---SDTRISNAIMQLTTKYNALLTL 5418
Cdd:TIGR02168 571 GRVTFLPLDSIKGTEIQGNdrEILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvDDLDNALELAKKLRPGYRIVTL 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5419 AKEVMRRLEMHYQEHQQHHSLYEECQSWIEKTREKLsecEQIPGTLNEVQIKLNTVKNLRQGFETGQNKLRYLLELKEKV 5498
Cdd:TIGR02168 651 DGDLVRPGGVITGGSAKTNSSILERRREIEELEEKI---EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5499 IMNTEQNgAAKIQEDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDVEPSVKTSDEFLND----LS 5574
Cdd:TIGR02168 728 ISALRKD-LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlreaLD 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5575 EKRAAL----EKFRVIQRDINGHNDIVEKINQRL------KEDNSLDLKDFQPGLTKFDDLQTQVNKIIESLENQVNSHE 5644
Cdd:TIGR02168 807 ELRAELtllnEEAANLRERLESLERRIAATERRLedleeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5645 KYKQAYNELQDWLRRTRIEVEQcadchgEKDQVESRLNRLGDIQSSSLEGKALLEACEELSQAVIAtsgSEGQDNvAQEI 5724
Cdd:TIGR02168 887 EALALLRSELEELSEELRELES------KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS---EEYSLT-LEEA 956
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320544548 5725 KHLTSEWETLQTISRDARSSLESCLAAwqtflqkFNKINLWIETMNKRVTKSQEGENKTPEDLVNAKKLLEEVLAEKD 5802
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKE-------LGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7042-8012 |
3.79e-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: 51.60 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7042 ASANDKGQKIASEGNAADKNSITEQLQSLKNQLQNLRKAV-ESQRQKHQLQLESHKKmAAELSEILDWLHShegaaksrp 7120
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALLVLRLEELREELEELQEELkEAEEELEELTAELQEL-EEKLEELRLEVSE--------- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7121 lLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEIGMPSSLLEMLSEGRSLVASLPHELEEREKYLKNNRDSRL 7200
Cdd:TIGR02168 279 -LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7201 EymqLVAKFNDWVHEAELRLQNSQhgidyehlvqdldehkiffgneapirnlvhKQIQEAADKIwsslnnyeqselsAEL 7280
Cdd:TIGR02168 358 A---ELEELEAELEELESRLEELE------------------------------EQLETLRSKV-------------AQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7281 AQFQTKLTNTLANAKTQQSELEKEAERWREYQQSIDRVKATiertkfvdepvQNLAGLHFNIQKLSHAIGNVQSQNSDLt 7360
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE-----------AELKELQAELEELEEELEELQEELERL- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7361 lvnQQAQSLIRQADARNRQLIEQDNAGLNRSwQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFrNVDpt 7440
Cdd:TIGR02168 460 ---EEALEELREELEEAEQALDAAERELAQL-QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI-SVD-- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7441 vrsrrhlEDTKNAIQELREESNQ------LKSSHKEIEALSKSIL---TFLgEVHKPSAEAIQAKVDKLVEQQaklndtl 7511
Cdd:TIGR02168 533 -------EGYEAAIEAALGGRLQavvvenLNAAKKAIAFLKQNELgrvTFL-PLDSIKGTEIQGNDREILKNI------- 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7512 rDKEQQVSKDLEEIEqvfrriSQLQDKLNALheqLQSVHVYDEhIAQTEQLLITLNSQVQQAAEESKLL---------VA 7582
Cdd:TIGR02168 598 -EGFLGVAKDLVKFD------PKLRKALSYL---LGGVLVVDD-LDNALELAKKLRPGYRIVTLDGDLVrpggvitggSA 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7583 QTTAHYQAKQNQLpSDIAQEFTALELLAERVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQM 7662
Cdd:TIGR02168 667 KTNSSILERRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7663 KELLQRINHEITAIYERFTLVKTN-GQLIIENCRNSEEKTLVQTTIDQLAASLAQVRGWLDEKKQAVGDSLDAWTRFMNL 7741
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7742 YQivmswaSEKRNFIDQTIELRTLpearnklndyvtsVKSIKPIVKHLSEMDKELEHigQVTTVGDLKDKLQEAEDAKIS 7821
Cdd:TIGR02168 826 LE------SLERRIAATERRLEDL-------------EEQIEELSEDIESLAAEIEE--LEELIEELESELEALLNERAS 884
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7822 VEAVLLERNSLLQEACEEWDQCERKIKDirswhektkqgldssqqqkkpLRDQLGFCEKTLADINVQKTKLRLSIEKLEv 7901
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSE---------------------LRRELEELREKLAQLELRLEGLEVRIDNLQ- 942
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7902 hfrngmggdPRLSENVDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRlvmaptylphdrer 7981
Cdd:TIGR02168 943 ---------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELK-------------- 999
|
970 980 990
....*....|....*....|....*....|.
gi 320544548 7982 alaEQQDLITQELDELLQSLSSVEDGIANMN 8012
Cdd:TIGR02168 1000 ---ERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1047-1245 |
3.79e-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: 49.37 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 1047 KEIHQWLSEAEQLLGTHNLSGGRDAINEQLHKHKTYfsrtvyYRSMLESKNKV--FQNLLKAVSSDDKIDTAPASQQMQQ 1124
Cdd:cd00176 10 DELEAWLSEKEELLSSTDYGDDLESVEALLKKHEAL------EAELAAHEERVeaLNELGEQLIEEGHPDAEEIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 1125 LNERFNYVIQNAQQWEQRLDSAAGGWSNFKDnERVVSEWLTQAESMLV-EKHIESKTTIETQKYFFEQV------NDRWM 1197
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALAsEDLGKDLESVEELLKKHKELeeeleaHEPRL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 320544548 1198 NDLVQSAQQLLTTLPAQEQPAVVHSVEQLQSRWKNVLSQAPLHLLKLE 1245
Cdd:cd00176 163 KSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
7453-7679 |
3.90e-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: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7453 AIQELREESNQLKSSHKEIEALSKSIltflgEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRI 7532
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKEL-----AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7533 SQLQDKLNALHEQLQSVHVYDEHIAQTEQLLITLNSQ-VQQAAEESKLLvaqttAHYQAKQNQLPSDIAQEFTALELLAE 7611
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEdFLDAVRRLQYL-----KYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320544548 7612 RVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELLQRINHEITAIYER 7679
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6511-6731 |
4.25e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6511 KIQELKGKAAQVAEVISNLDGQ--QVEEQMKSLDRRFADLGKRIDRKSQLLDVtnkgvEGAKGEIDQLQnwvkQQIEELQ 6588
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERleALEAELDALQERREALQRLAEYSWDEIDV-----ASAEREIAELE----AELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6589 ApkplgyTPKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELEpveysQLESALRNLNTENRNLSGVLKAELDRA 6668
Cdd:COG4913 682 A------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELE-----QAEEELDELQDRLEAAEDLARLELRAL 750
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320544548 6669 LEASKARKSLENDLDKARQWLKTKISEVRKLPVYHpltSAEIEKKIQE-NRKYDDDAKQFNDSV 6731
Cdd:COG4913 751 LEERFAAALGDAVERELRENLEERIDALRARLNRA---EEELERAMRAfNREWPAETADLDADL 811
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
6856-7907 |
5.45e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.21 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6856 NADKLKLNDDIKNMKDRYGRIKNTID-----DRVNALGDHIKK----------------YKDAKSRLAECSQ-------- 6906
Cdd:TIGR01612 599 NKLKLELKEKIKNISDKNEYIKKAIDlkkiiENNNAYIDELAKispyqvpehlknkdkiYSTIKSELSKIYEddidalyn 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6907 FLGNIQQ-----------KLRELNRPIGSRIEDVQDLLGA-YEGILKELKDSKSKMGDMQMDDLPELQSILAQqdDMIKL 6974
Cdd:TIGR01612 679 ELSSIVKenaidntedkaKLDDLKSKIDKEYDKIQNMETAtVELHLSNIENKKNELLDIIVEIKKHIHGEINK--DLNKI 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6975 IEDQLAHLRQLLLLREQFIALINEIIAFIMKYTDV------IIDIENSPDslEDKINKYDdvivKIQECEGVLASANDKG 7048
Cdd:TIGR01612 757 LEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIknhyndQINIDNIKD--EDAKQNYD----KSKEYIKTISIKEDEI 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7049 QKIASEGNAAdKNSITEQLQSLKNQLQNLRKAVESQrqkHQLQLESHKKMAAELSEilDWLHSHEGAAK-SRPLLDRDPE 7127
Cdd:TIGR01612 831 FKIINEMKFM-KDDFLNKVDKFINFENNCKEKIDSE---HEQFAELTNKIKAEISD--DKLNDYEKKFNdSKSLINEINK 904
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7128 SVERELQKHQSL-------------SQDIESYLNKFNKINDGVKTEIGM--PSSLLEMlSEGRSLVASLPHELEEREKYL 7192
Cdd:TIGR01612 905 SIEEEYQNINTLkkvdeyikicentKESIEKFHNKQNILKEILNKNIDTikESNLIEK-SYKDKFDNTLIDKINELDKAF 983
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7193 KNNRDSRLEYM--QLVAKFNDWVHEAELRLQNSqhgidyehLVQDLDEHKIFFGN-EAPIRNlVHKQIQEAADKIWSSLN 7269
Cdd:TIGR01612 984 KDASLNDYEAKnnELIKYFNDLKANLGKNKENM--------LYHQFDEKEKATNDiEQKIED-ANKNIPNIEIAIHTSIY 1054
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7270 NYEQsELSAELAQFQTKL-TNTLANAKTQQSELEKEAERWREYQQSiDRVKAtiERTKFVDEPVQNLAGLHFNIQKLSHA 7348
Cdd:TIGR01612 1055 NIID-EIEKEIGKNIELLnKEILEEAEINITNFNEIKEKLKHYNFD-DFGKE--ENIKYADEINKIKDDIKNLDQKIDHH 1130
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7349 IGNVQS-QNSDLTLVNQQAQSLIRQADARNRQLIEQDNAGLNRSWQDLVRSLEQRR---DNLQQLAEHWDGFENSLHAWE 7424
Cdd:TIGR01612 1131 IKALEEiKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKniyDEIKKLLNEIAEIEKDKTSLE 1210
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7425 KA---------------LGRLEDKFRNVDPTVRSR----RHLEDTKNAIQELREESNQLKSSHKEIEALSKSILTF---- 7481
Cdd:TIGR01612 1211 EVkginlsygknlgklfLEKIDEEKKKSEHMIKAMeayiEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDkdhh 1290
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7482 -LGEVHKPSAEAIQAKVDKLVE---QQAKLNDTLRDKEQQVS---KDLEEIEQVFRRISQLQD--KLNALHEQLQSVHVY 7552
Cdd:TIGR01612 1291 iISKKHDENISDIREKSLKIIEdfsEESDINDIKKELQKNLLdaqKHNSDINLYLNEIANIYNilKLNKIKKIIDEVKEY 1370
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7553 DEHIAQTeqllitlNSQVQQAAEESKLLVAQTtahyqakqnqlpsdiaQEFTALELLAERVQVTMETKEKDfkraktvrt 7632
Cdd:TIGR01612 1371 TKEIEEN-------NKNIKDELDKSEKLIKKI----------------KDDINLEECKSKIESTLDDKDID--------- 1418
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7633 EYVDGVDEVQRWLLQAEVQVQersltpTQMKElLQRINHEITAIYERFTLVKTNGQLIIENCRNSEEKTLvQTTIDQLAA 7712
Cdd:TIGR01612 1419 ECIKKIKELKNHILSEESNID------TYFKN-ADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDH-DFNINELKE 1490
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7713 SLAQVRGWLDE---KKQAVGDSLDAWTRFMNLYQIVMS--WASEKRNFIDQT-----IELRTLPEARNKLN-DYVTSVKS 7781
Cdd:TIGR01612 1491 HIDKSKGCKDEadkNAKAIEKNKELFEQYKKDVTELLNkySALAIKNKFAKTkkdseIIIKEIKDAHKKFIlEAEKSEQK 1570
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7782 IKPIVKHLSEMDKELEH--------IGQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEACE-EWDQCERKIKDIRS 7852
Cdd:TIGR01612 1571 IKEIKKEKFRIEDDAAKndksnkaaIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSfSIDSQDTELKENGD 1650
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*
gi 320544548 7853 WHEKTKQGLDSSQQQKKPLRDQlgfcEKTLADINVQKTKLRLSIEKLEVHFRNGM 7907
Cdd:TIGR01612 1651 NLNSLQEFLESLKDQKKNIEDK----KKELDELDSEIEKIEIDVDQHKKNYEIGI 1701
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3183-3271 |
5.90e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 46.17 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3183 EFDTIIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINELMDQGREI-----EGETDLNLKLSR 3257
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeghPDAEEIEERLEE 81
|
90
....*....|....
gi 320544548 3258 LNTRYQTLKNLCKE 3271
Cdd:smart00150 82 LNERWEELKELAEE 95
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4034-4226 |
6.08e-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: 48.60 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4034 QWNDYEINLDRLITWLGEAENSLKNYNLKSSFEEKEEQLNGFQSLAQNLRQNEADFDKVKDDTSELVQSSGE--TRIAVN 4111
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPdaEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4112 VQQVSSRFQSIQATAKEILKKCEQAVQDHGHFNDkYKQCADWLANAQARYDDCCDLSTVASRDDLLKKQvviQELLAQQP 4191
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLESVEELLKKH---KELEEELE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 320544548 4192 TATQLLNSTVELGEKCYGSTATEGREAIRSQLDDL 4226
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEEL 191
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
9149-9276 |
6.65e-05 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 49.94 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 9149 QQTTPRIPSPTEKSEVEQDIKSVQTSPQHQPKLDETAVQTSLEVQP------DNQENESQTLIVEITETEA--------- 9213
Cdd:PRK10905 82 QGQTPVATDGQQRVEVQGDLNNALTQPQNQQQLNNVAVNSTLPTEPatvapvRNGNASRQTAKTQTAERPAttrparkqa 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 9214 -------QTTPRSEEQSVAVEISTTEIQTDVSGQPAETVEISSQTTVTTTIEKELQTTPKDSPRAPEAGS 9276
Cdd:PRK10905 162 viepkkpQATAKTEPKPVAQTPKRTEPAAPVASTKAPAATSTPAPKETATTAPVQTASPAQTTATPAAGG 231
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2067-3607 |
7.01e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.82 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2067 TPEESNALNDAYTalvvnyQNLETNMLQKKAALEKW-------------TELLGWKNDTESHL-----NYLKHQLDKPEg 2128
Cdd:TIGR01612 953 TIKESNLIEKSYK------DKFDNTLIDKINELDKAfkdaslndyeaknNELIKYFNDLKANLgknkeNMLYHQFDEKE- 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2129 paaEELSKVIDEIDNLGQGIgywkgqakeidenPAIQLrdalsrrpLIATQIVNDVEnKLENL------KLRSQSQQQQI 2202
Cdd:TIGR01612 1026 ---KATNDIEQKIEDANKNI-------------PNIEI--------AIHTSIYNIID-EIEKEigknieLLNKEILEEAE 1080
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2203 QQMTVRKDKFHALEH-NFGQALQENRAKL-DEILRQHPTLNNIDQII-ADLVAL----NDALKYQADLKNRIHD----EG 2271
Cdd:TIGR01612 1081 INITNFNEIKEKLKHyNFDDFGKEENIKYaDEINKIKDDIKNLDQKIdHHIKALeeikKKSENYIDEIKAQINDledvAD 1160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2272 SLLMREDIASMPAIQESLLI-MDK------NYDSLQNEIA---------DRIQKYNL-----ISQALREYADSKDKFSKE 2330
Cdd:TIGR01612 1161 KAISNDDPEEIEKKIENIVTkIDKkkniydEIKKLLNEIAeiekdktslEEVKGINLsygknLGKLFLEKIDEEKKKSEH 1240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2331 LKKA-----EDLYNAIPQQPRDETEL-----------------------HQASEKTRKTMEQLRKSKLSLDELERRGNNV 2382
Cdd:TIGR01612 1241 MIKAmeayiEDLDEIKEKSPEIENEMgiemdikaemetfnishdddkdhHIISKKHDENISDIREKSLKIIEDFSEESDI 1320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2383 GKlfsaigepIPQEVPQEVTAAKQHWQDLHDKTAKNAHVYETEAV-IWSQIEDAKKDLLPWLSETNQGLCDAADNSieie 2461
Cdd:TIGR01612 1321 ND--------IKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLnKIKKIIDEVKEYTKEIEENNKNIKDELDKS---- 1388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2462 fgpMRLSKYRTELPSYQALKdSIVEKTNDLVKINKGAEIPALSAlNKLLSEqfaEVNN-----NADRLSA-ITTSFNDQE 2535
Cdd:TIGR01612 1389 ---EKLIKKIKDDINLEECK-SKIESTLDDKDIDECIKKIKELK-NHILSE---ESNIdtyfkNADENNEnVLLLFKNIE 1460
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2536 ------QELRRRSKEAGE-----RVSKLREQLIK---CDDMSGDNNKIMER----LQQCRALRGELDNSGNEIDnIKQKV 2597
Cdd:TIGR01612 1461 madnksQHILKIKKDNATndhdfNINELKEHIDKskgCKDEADKNAKAIEKnkelFEQYKKDVTELLNKYSALA-IKNKF 1539
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2598 DELRNlyptfSESIIPKELNNVQKRYEnvdLYAKKIEssllQFLKKFHADKVGMLKRIIATQREKVAWCQPESSSDkyNL 2677
Cdd:TIGR01612 1540 AKTKK-----DSEIIIKEIKDAHKKFI---LEAEKSE----QKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLE--NF 1605
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2678 DVKKSSLQEVSKSIDDCKARHAETLKSLEMLKAVESPQNLAELTSDAELLRKDMQALQDsfdQIKGILDENVDLwsqyEQ 2757
Cdd:TIGR01612 1606 ENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKENGDNLNSLQEFLESLKD---QKKNIEDKKKEL----DE 1678
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2758 SNEQISNWLRDVEGRVKaetSSQVNLSEvpqKLQELSILQQdvlahepiiNNLEQTsQQLIEKNPEARIGQFVTHlvqry 2837
Cdd:TIGR01612 1679 LDSEIEKIEIDVDQHKK---NYEIGIIE---KIKEIAIANK---------EEIESI-KELIEPTIENLISSFNTN----- 1737
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2838 qavskaltsyidkirgaQLSNANFAKAAKDFNEWFGDAKIEFQELARMgspgsssaTAQQLQTVKNYIKTFDNgqiLLNN 2917
Cdd:TIGR01612 1738 -----------------DLEGIDPNEKLEEYNTEIGDIYEEFIELYNI--------IAGCLETVSKEPITYDE---IKNT 1789
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2918 AVDIGEALYPVVSPDNRERIRADLRQMREkFDYLRDEANAFMQQVEGVLIQKTS-IEESYTQVSHYLNESKAkvpTTDE- 2995
Cdd:TIGR01612 1790 RINAQNEFLKIIEIEKKSKSYLDDIEAKE-FDRIINHFKKKLDHVNDKFTKEYSkINEGFDDISKSIENVKN---STDEn 1865
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2996 -LYPTLATKKAALQN--------YKTQLQEITLHK-----------------NALKQLHDKAVTLCDDESER--KTDESI 3047
Cdd:TIGR01612 1866 lLFDILNKTKDAYAGiigkkyysYKDEAEKIFINIsklansiniqiqnnsgiDLFDNINIAILSSLDSEKEDtlKFIPSP 1945
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3048 QEYNTLSKKISDRITTVGNhVVKHEAYDQvlEKAQDWLNTI------------KSEAIDILNETTFEKEgaeeKLLVVEN 3115
Cdd:TIGR01612 1946 EKEPEIYTKIRDSYDTLLD-IFKKSQDLH--KKEQDTLNIIfenqqlyekiqaSNELKDTLSDLKYKKE----KILNDVK 2018
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3116 LLQHKpegdsiFDTCHKL------LETVLTQTHPSGHPALLKGFEEPKQSwedfmtLCQDSLVKLKQlcSKWDEFDTIIE 3189
Cdd:TIGR01612 2019 LLLHK------FDELNKLscdsqnYDTILELSKQDKIKEKIDNYEKEKEK------FGIDFDVKAME--EKFDNDIKDIE 2084
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3190 ELDNWMKNVEA------------VVKNQNLKSTAEAKNAHLKQLQDisKDIERrgaaiNELMDQGREIEGETdlnlklsr 3257
Cdd:TIGR01612 2085 KFENNYKHSEKdnhdfseekdniIQSKKKLKELTEAFNTEIKIIED--KIIEK-----NDLIDKLIEMRKEC-------- 2149
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3258 LNTRYQTLKNLCKESIAKYVNYVKDHESFDKDFDSFKQNLQSSVDElaktneivgDQSVLQDQQNkLREMsdKRILDSTL 3337
Cdd:TIGR01612 2150 LLFSYATLVETLKSKVINHSEFITSAAKFSKDFFEFIEDISDSLND---------DIDALQIKYN-LNQT--KKHMISIL 2217
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3338 FEGLIDRGEklyghtspegreIIRQQLRALRTLwDNYTDDLNSATQKIDQCLLQFNEFsiaqdQLTKWLKDVDKAMQSht 3417
Cdd:TIGR01612 2218 ADATKDHNN------------LIEKEKEATKII-NNLTELFTIDFNNADADILHNNKI-----QIIYFNSELHKSIES-- 2277
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3418 ePKTTLQEKRA-QLQNHKLLHQEITTHNVLVDNVCdkaqilvdQIKDNSLNVYLTSIKQLFQSIVQKSDEILHNLDDCVq 3496
Cdd:TIGR01612 2278 -IKKLYKKINAfKLLNISHINEKYFDISKEFDNII--------QLQKHKLTENLNDLKEIDQYISDKKNIFLHALNENT- 2347
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3497 khNELNNALSSAKTWISNEKAKLLECDDAYG-EKADIKRKIETLGQLAQNkpqamkiisdIRDLFEKVkaTTSEKGNEVL 3575
Cdd:TIGR01612 2348 --NFNFNALKEIYDDIINRENKADEIENINNkENENIMQYIDTITKLTEK----------IQDILIFV--TTYENDNNII 2413
|
1690 1700 1710 1720
....*....|....*....|....*....|....*....|
gi 320544548 3576 DKEIEE--------LETTMKSHFDDIEGIEGKQKDVLAQW 3607
Cdd:TIGR01612 2414 KQHIQDndendvskIKDNLKKTIQSFQEILNKIDEIKAQF 2453
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
10824-11193 |
9.68e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.30 E-value: 9.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10824 RQQLAALLDwLRQREAERNALQ------LRYihLKRVPHLKHRLDAMIQQLDQGEQQskaLQEQQQELARHCDDALATAm 10897
Cdd:PRK11281 42 QAQLDALNK-QKLLEAEDKLVQqdleqtLAL--LDKIDRQKEETEQLKQQLAQAPAK---LRQAQAELEALKDDNDEET- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10898 rmeqasiGQRISNLRaalktwqgflqrVTQLsesyEQRVNQLQQEFGAAQK-LLDANSE--SLPTQPAaieqllgslRAQ 10974
Cdd:PRK11281 115 -------RETLSTLS------------LRQL----ESRLAQTLDQLQNAQNdLAEYNSQlvSLQTQPE---------RAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10975 RVQLGAQVSALE--SLTVTQEELKECISPhdmktiRQRNWLLWQQHAdLDYQLANLINSIEERLSLLSNYQIRYDRISQW 11052
Cdd:PRK11281 163 AALYANSQRLQQirNLLKGGKVGGKALRP------SQRVLLQAEQAL-LNAQNDLQRKSLEGNTQLQDLLQKQRDYLTAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11053 LQRLEQRVEKDADVTAMTNPEQAAKQLEQQVNS--------------ELQLRDKEREWLLSTSRELLTLySEPEVRsqVQ 11118
Cdd:PRK11281 236 IQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQdeaariqanplvaqELEINLQLSQRLLKATEKLNTL-TQQNLR--VK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11119 QQSDSLIDRWQRLKylakqkaTKIGELKMTLL-------------------RLEERIALIRAWLFEVESQLDKPLNFESY 11179
Cdd:PRK11281 313 NWLDRLTQSERNIK-------EQISVLKGSLLlsrilyqqqqalpsadlieGLADRIADLRLEQFEINQQRDALFQPDAY 385
|
410
....*....|....
gi 320544548 11180 tpnvIEAKLKEHEQ 11193
Cdd:PRK11281 386 ----IDKLEAGHKS 395
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7269-7539 |
1.04e-04 |
|
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: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7269 NNYEQSE-LSAELAQfqtkLTNTLANAKTQQSELEKEAERWREYQQSIDRVKAtiertkfVDEPVQNLAGLHFNIQKLSH 7347
Cdd:COG4913 607 DNRAKLAaLEAELAE----LEEELAEAEERLEALEAELDALQERREALQRLAE-------YSWDEIDVASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7348 AIGNVQSQNSDLTLVNQQAQSLIRQADArnrqlIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKAl 7427
Cdd:COG4913 676 ELERLDASSDDLAALEEQLEELEAELEE-----LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA- 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7428 gRLEDKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKsshkeiEALSKSILTFLGEVHKPSAE------------AIQA 7495
Cdd:COG4913 750 -LLEERFAAALGDAVERELRENLEERIDALRARLNRAE------EELERAMRAFNREWPAETADldadleslpeylALLD 822
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 320544548 7496 KV--DKLVEQQAKLNDTLRDKEQQVSKDL-----EEIEQVFRRISQLQDKL 7539
Cdd:COG4913 823 RLeeDGLPEYEERFKELLNENSIEFVADLlsklrRAIREIKERIDPLNDSL 873
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4890-5101 |
1.15e-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: 47.83 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4890 QWRAYKEEYERLMEWLQQIDILVKNhkLNLCPNLPEKEKQVADMKEVMSRLEKGKDDIDKFNASAASLLKSHLD--TYVN 4967
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPdaEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4968 NQLRHLSSVYQVQVNLAKDVLKKVETNRDQHREYDaNMKSAKDWIANAKATIQSAGEGaGSKEALQRRLEQIQDLIRNRE 5047
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLG-KDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 320544548 5048 LGQNLVHTAINNGEKIIRNTRSDGRDAINTEMKELQTEWDRLVKKMSTAKVQLE 5101
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
2754-2844 |
1.19e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 45.40 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2754 QYEQSNEQISNWLRDVEgRVKAETSSQVNLSEVPQKLQELSILQQDVLAHEPIINNLEQTSQQLIEKNPEAR--IGQFVT 2831
Cdd:smart00150 2 QFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAeeIEERLE 80
|
90
....*....|...
gi 320544548 2832 HLVQRYQAVSKAL 2844
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
7478-7679 |
1.28e-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: 48.99 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7478 ILTFLGEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVhvyDEHIA 7557
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---EAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7558 QTEQLLITLNSQV-QQAAEESKLLVAQTTAHYQAKQNQL-----PSDIAQEFTALELLAERVQVTMETKEKDFKRAKTVR 7631
Cdd:COG4942 87 ELEKEIAELRAELeAQKEELAELLRALYRLGRQPPLALLlspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 320544548 7632 TEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELLQRINHEITAIYER 7679
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5644-5842 |
1.29e-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: 47.83 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5644 EKYKQAYNELQDWLRRTRIEVEQcADCHGEKDQVESRLNRLGDIQSSSLEGKALLEACEELSQAVIAtSGSEGQDNVAQE 5723
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5724 IKHLTSEWETLQTISRDARSSLESCLAAWQtFLQKFNKINLWIETMNKRVTKSQEGENKTP-EDLVNA-KKLLEEVLAEK 5801
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDLGKDLESvEELLKKhKELEEELEAHE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 320544548 5802 DNVEDLNDNCELLMEQS---ACTRIRDQTIETQANYTKLLTSAQ 5842
Cdd:cd00176 160 PRLKSLNELAEELLEEGhpdADEEIEEKLEELNERWEELLELAE 203
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7367-8160 |
1.29e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7367 QSLIRQADARNRQL--IEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGF-ENSLHAWEKALGRLEDKFRNVDPTVR- 7442
Cdd:TIGR02169 233 EALERQKEAIERQLasLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAe 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7443 SRRHLEDTKNAIQELREESNQLKSshkEIEALSKSILTFLGEVHKPSAE--AIQAKVDKLV---EQQAKLNDTLRDKEQQ 7517
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLA---EIEELEREIEEERKRRDKLTEEyaELKEELEDLRaelEEVDKEFAETRDELKD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7518 VSKDLE----EIEQVFRRISQLQDKLNALHEQLQSVH----VYDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAhYQ 7589
Cdd:TIGR02169 390 YREKLEklkrEINELKRELDRLQEELQRLSEELADLNaaiaGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK-YE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7590 AKQNQLPSDIAQ---EFTALELLAERVQVT---METKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQ------------ 7651
Cdd:TIGR02169 469 QELYDLKEEYDRvekELSKLQRELAEAEAQaraSEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERyataievaagnr 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7652 ----VQERSLTPTQMKELLQRINheitaiYERFTLVKTNG-QLIIENCRNSEEKTLVQTTID------QLAASLAQVRGw 7720
Cdd:TIGR02169 549 lnnvVVEDDAVAKEAIELLKRRK------AGRATFLPLNKmRDERRDLSILSEDGVIGFAVDlvefdpKYEPAFKYVFG- 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7721 ldekKQAVGDSLDAWTRFMNLYQIVM--------SWA------SEKRNFIDQTIELRTLPEARNKLNDyvtsvksikpIV 7786
Cdd:TIGR02169 622 ----DTLVVEDIEAARRLMGKYRMVTlegelfekSGAmtggsrAPRGGILFSRSEPAELQRLRERLEG----------LK 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7787 KHLSEMDKELEHIGQvttvgDLKDKLQEAEDAKISVEAVLLERNSLLQEAceewDQCERKIKDIRSWHEKTKQGLDSSQQ 7866
Cdd:TIGR02169 688 RELSSLQSELRRIEN-----RLDELSQELSDASRKIGEIEKEIEQLEQEE----EKLKERLEELEEDLSSLEQEIENVKS 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7867 QKKPLRDQLGFCEKTLAdinvqktKLRLSIEKLEVHFRNgmggdprlsENVDDLVRVLDGLGELVKAKSQSLEQTLAQID 7946
Cdd:TIGR02169 759 ELKELEARIEELEEDLH-------KLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSRIEARLREIEQKLN 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7947 VYQQQMQSLRQRIIQEEQQLRLVmaptylpHDRERALAEQQDLITQELDELLQSLSSVEDGIANmnqssLDGMLHGLKLI 8026
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDL-------KEQIKSIEKEIENLNGKKEELEEELEELEAALRD-----LESRLGDLKKE 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 8027 QSNLEVHERDAIELKNQAKklptdpATERLLNDTVDRIDLLLRRTQQGITMIANAmhgqKKRQQEIDEYQQHLLELEQWI 8106
Cdd:TIGR02169 891 RDELEAQLRELERKIEELE------AQIEKKRKRLSELKAKLEALEEELSEIEDP----KGEDEEIPEEELSLEDVQAEL 960
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 320544548 8107 IEVSAELASFEPTSDSSTD--EQVLKSQVERSQQlLRTLKDRQQSMEDLVEQTRQL 8160
Cdd:TIGR02169 961 QRVEEEIRALEPVNMLAIQeyEEVLKRLDELKEK-RAKLEEERKAILERIEEYEKK 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10442-11095 |
1.40e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10442 ERLRKATERLEGLAGDLHNREQLIDELKG---AAKPLIESCDVQIVEQIES--AVQEAVVAWNDTSENLQQLRTRYQRAV 10516
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERlaNLERQLEELEAQLEELESKLDELAEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10517 ELWDKYRNASAAVKNSIDQQMDAVKSLEQplDALQHAKVCQDNLTTQNDRILELRDIVAKIAADVgldasALMQGELDAL 10596
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELE--ELESRLEELEEQLETLRSKVAQLELQIASLNNEI-----ERLEARLERL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10597 GQRLAECKDAITTLANVAETQDKER-----KELDKEVTLAKAYFNNVQ------QDISREAPQNPKESEEQLAALRAHLQ 10665
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLEealeelREELEEAEQALDAAERELAQLQARLD 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10666 TLARTEEQLRQ--------LKERHQNSEVAPSVAS--------------------------SDDDGILEVLAL-WQKIFQ 10710
Cdd:TIGR02168 493 SLERLQENLEGfsegvkalLKNQSGLSGILGVLSElisvdegyeaaieaalggrlqavvveNLNAAKKAIAFLkQNELGR 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10711 DTFQEYHRLSTRLARSQNssealrlwRQYLQHVQSFLSCAIPEDYSSLREQQQLCAIHQNLLISQqSVLSETPLESELSE 10790
Cdd:TIGR02168 573 VTFLPLDSIKGTEIQGND--------REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVD-DLDNALELAKKLRP 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10791 QYK-------------ALTNLHNETLSRIMQRNGELERrvsgwnaYRQQLAALLDWLRQREAERNAL-QLRYIHLKRVPH 10856
Cdd:TIGR02168 644 GYRivtldgdlvrpggVITGGSAKTNSSILERRREIEE-------LEEKIEELEEKIAELEKALAELrKELEELEEELEQ 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10857 LKHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALAtamrmEQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRV 10936
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK-----ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10937 NQLQQEFGAAQKLLDANS-----------------ESLPTQPAAIEQLLGSLRAQRVQLGAQVSAL----ESLTVTQEEL 10995
Cdd:TIGR02168 792 EQLKEELKALREALDELRaeltllneeaanlrerlESLERRIAATERRLEDLEEQIEELSEDIESLaaeiEELEELIEEL 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10996 KECISPH---------DMKTIRQRNWLLWQQHADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQRLEQRVEKDADV 11066
Cdd:TIGR02168 872 ESELEALlnerasleeALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
730 740
....*....|....*....|....*....
gi 320544548 11067 TAMTNPEQAAKQLEQQVNSELQLRDKERE 11095
Cdd:TIGR02168 952 TLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5645-6554 |
1.54e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5645 KYKQAYNELQDWLRRTRIEVEQCADCHGEkdqVESRLNRLgDIQSSSLEgkALLEACEELSQAVIATSgsegqdnvAQEI 5724
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNE---LERQLKSL-ERQAEKAE--RYKELKAELRELELALL--------VLRL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5725 KHLTSEWETLQTISRDARSSLESCLAAWQTFLQKFNKINLWIETMNKRVTKSQEGENKTPEDLVNAKKLLEEVLAEKDNV 5804
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5805 EDLNDNCELLMEQSACTRIRDQTIETQANytKLLTSAQGLVAKIEKnlsDHTEFLNYKKEMDAWIEKAQQVLDDCSTDgd 5884
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELE--EKLEELKEELESLEA---ELEELEAELEELESRLEELEEQLETLRSK-- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5885 aaiIAQKLDTVNSLASRLpegQHLLALVQDAyskasnitpEDKQEKLRElmtkvredwdalglavkQKLSDLKQAQNrwn 5964
Cdd:TIGR02168 388 ---VAQLELQIASLNNEI---ERLEARLERL---------EDRRERLQQ-----------------EIEELLKKLEE--- 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5965 dfaANKDKLEKWLNETETTLKvapETKGELSemkTLLERYKTLSNELKLKGNELEQLQSEARDLGTEVDAVNRLQSRCDK 6044
Cdd:TIGR02168 433 ---AELKELQAELEELEEELE---ELQEELE---RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6045 LkndcSAHITALEQEMFDYNAYHQSLQDV----EKWLLQISFQLMAH-NSLFISNRE---QTQEQIKQHEALLVEIQKYQ 6116
Cdd:TIGR02168 504 F----SEGVKALLKNQSGLSGILGVLSELisvdEGYEAAIEAALGGRlQAVVVENLNaakKAIAFLKQNELGRVTFLPLD 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6117 TNLDDLNAKGQAQIKRYESSTPAIRPTVESQLKNIQDSYNSLLQ-----TSVQIKNRLLESLaKFQEYEDTLD------- 6184
Cdd:TIGR02168 580 SIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGgvlvvDDLDNALELAKKL-RPGYRIVTLDgdlvrpg 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6185 ------SIMRNLETYEPiiQTELDAPATSLELAQNQLRCAQEMQNKLNNEKSRLAAAVQACEAATASISRPSSPLETAMQ 6258
Cdd:TIGR02168 659 gvitggSAKTNSSILER--RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6259 AIPERElivrAKLEDLLDQkpppktrsstggvsTDDDKDEADVEIQVELSDVNEALLDPIAHErvknyrrivrlnsAHVG 6338
Cdd:TIGR02168 737 RLEAEV----EQLEERIAQ--------------LSKELTELEAEIEELEERLEEAEEELAEAE-------------AEIE 785
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6339 KLNELVAKVQSHLGGLTASVSELEQQ-QKQRAELQDWVKKQQSSVSDwmMRPCKLRPEAAQQELvsmndllnsigDKRSQ 6417
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAElTLLNEEAANLRERLESLERR--IAATERRLEDLEEQI-----------EELSE 852
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6418 LMLEMTGSLgdedTDLDDNIDKLESELMDAIAKKQAGQNVIDGYRQGMADVQNWFDTLIKRMDVLDRGSGlNCAQKMAAI 6497
Cdd:TIGR02168 853 DIESLAAEI----EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE-ELREKLAQL 927
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 320544548 6498 NEIKNEYELQGHPKIQELKGKAAQVAEVISNLDgQQVEEQMKSLDRRFADLGKRIDR 6554
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE-NKIEDDEEEARRRLKRLENKIKE 983
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
11182-11517 |
1.55e-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: 49.36 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11182 NVIEAKLKEHEQIQRSiehHSSNVGEVLNLVEMLLNDADSwrtqvNTSGLAASAQNLEQRWKNVCSQ--SAERKARIL-- 11257
Cdd:pfam07111 133 NLEEGSQRELEEIQRL---HQEQLSSLTQAHEEALSSLTS-----KAEGLEKSLNSLETKRAGEAKQlaEAQKEAELLrk 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11258 ---TIWNLLQQLIKLTAEHKNWLGKQ-----ESQIAGFERDQKSHSKHKLEERQMELRAKLEELESQSVNLR-----QLE 11324
Cdd:pfam07111 205 qlsKTQEELEAQVTLVESLRKYVGEQvppevHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLThmlalQEE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11325 QIYAKLAMSAGVEPENIQKltlpTKVMVSMWRQltprchalldaidKDAKLMREFNNAQLEATNSLNAIQkalEQLPSAE 11404
Cdd:pfam07111 285 ELTRKIQPSDSLEPEFPKK----CRSLLNRWRE-------------KVFALMVQLKAQDLEHRDSVKQLR---GQVAELQ 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11405 NQQTSKAEPKAVLQRleSLEKKLQDAQ------QHVQQADNLAQEAKTRTKQQPQL--KQLLELVSAYTTLWQTVQTRiv 11476
Cdd:pfam07111 345 EQVTSQSQEQAILQR--ALQDKAAEVEvermsaKGLQMELSRAQEARRRQQQQTASaeEQLKFVVNAMSSTQIWLETT-- 420
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 320544548 11477 tlkttwLTRAAQAAASLP-----VSEAANAAVQVNTLSQRKLRQAQ 11517
Cdd:pfam07111 421 ------MTRVEQAVARIPslsnrLSYAVRKVHTIKGLMARKVALAQ 460
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7842-8190 |
1.58e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7842 QCERKIKDIRSWHEKtkqgLDSSQQQKKPLRDQLGFCEKTLADINVQKTKLRLSIEKLEvhfrngmggdprlsENVDDLV 7921
Cdd:COG1196 219 KEELKELEAELLLLK----LRELEAELEELEAELEELEAELEELEAELAELEAELEELR--------------LELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7922 RVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRLVMAptylphdRERALAEQQDLITQELDELLQSL 8001
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE-------ELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 8002 SSVEDGIANMNQSSLDgMLHGLKLIQSNLEVHERDAIELKNQAKKLptdpatERLLNDTVDRIDLLLRRTQQGITMIANA 8081
Cdd:COG1196 354 EEAEAELAEAEEALLE-AEAELAEAEEELEELAEELLEALRAAAEL------AAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 8082 MHGQKKRQQEIDEYQQHLLELEQWIIEVSAELASfepTSDSSTDEQVLKSQVERSQQLLRTLKDRQQSMEDLVEQTRQLQ 8161
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEA---LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
330 340
....*....|....*....|....*....
gi 320544548 8162 SHPDVSPLADTLMEQLQSIITILREQVTV 8190
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3158-3271 |
1.61e-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: 47.44 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3158 QSWEDFMTLCQDSLVKLKQLCSKWDEFDTiIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINE 3237
Cdd:cd00176 86 QRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKS 164
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 320544548 3238 LMDQGREIE------GETDLNLKLSRLNTRYQTLKNLCKE 3271
Cdd:cd00176 165 LNELAEELLeeghpdADEEIEEKLEELNERWEELLELAEE 204
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5857-6051 |
1.65e-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: 47.44 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5857 EFLNYKKEMDAWIEKAQQVLDDCSTDGDAAIIAQKLDTVNSLASRLPEGQHLLALVQDAYSKASNITPEDKqEKLRELMT 5936
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA-EEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5937 KVREDWDALGLAVKQKLSDLKQAQNRWNDFaANKDKLEKWLNETETTLKvAPETKGELSEMKTLLERYKTLSNELKLKGN 6016
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 320544548 6017 ELEQLQSEARDLGTEV--DAVNRLQSRCDKLKNDCSA 6051
Cdd:cd00176 161 RLKSLNELAEELLEEGhpDADEEIEEKLEELNERWEE 197
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
10507-11106 |
1.73e-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: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10507 QLRTRYQRAVELWDKYRNASAAVKNsIDQQMDAVKSLEQPLDALQHAKvcqdnlttqnDRILELRDIVAKIAADVGLDAS 10586
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALED-AREQIELLEPIRELAERYAAAR----------ERLAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10587 ALMQGELDALGQRLAECKDAITTLANVAETQDKERKELdkevtlAKAYFNNVQQDIsreapqnpKESEEQLAALRAHL-- 10664
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDEL------EAQIRGNGGDRL--------EQLEREIERLERELee 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10665 --QTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQdtfQEYHRLSTRLARSQNSSEALRLWRQYLQH 10742
Cdd:COG4913 357 reRRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAEIASLER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10743 VQSflscAIPEDYSSLREQqqlcaihqnllISQQSVLSETPL--------------------ESEL----------SEQY 10792
Cdd:COG4913 434 RKS----NIPARLLALRDA-----------LAEALGLDEAELpfvgelievrpeeerwrgaiERVLggfaltllvpPEHY 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10793 KALT----NLHNET---LSRIMQRNGELERRvsgwNAYRQQLAALLD--------WLRQREAERNAL-------QLRY-- 10848
Cdd:COG4913 499 AAALrwvnRLHLRGrlvYERVRTGLPDPERP----RLDPDSLAGKLDfkphpfraWLEAELGRRFDYvcvdspeELRRhp 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10849 --------IHLKRVPHLKHRLDAMIQQLDQG---EQQSKALQEQQQELARHCDDALATAMRMEQASigQRISNLRAALKT 10917
Cdd:COG4913 575 raitragqVKGNGTRHEKDDRRRIRSRYVLGfdnRAKLAALEAELAELEEELAEAEERLEALEAEL--DALQERREALQR 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10918 WQGFLQRVTQLsESYEQRVNQLQQEfgaAQKLLDANSE--SLPTQPAAIEQLLGSLRAQRVQLGAQVSALES-LTVTQEE 10994
Cdd:COG4913 653 LAEYSWDEIDV-ASAEREIAELEAE---LERLDASSDDlaALEEQLEELEAELEELEEELDELKGEIGRLEKeLEQAEEE 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10995 LKECISPHDMKTIRQRNWLlwqqHADLDYQLANLINSiEERLSLLSNYQIRYDRISQWLQRLEQRVEK------------ 11062
Cdd:COG4913 729 LDELQDRLEAAEDLARLEL----RALLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERamrafnrewpae 803
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 320544548 11063 --DADVTAMTNPEqAAKQLEQQVNSEL-QLRDKEREWLLSTSRELLT 11106
Cdd:COG4913 804 taDLDADLESLPE-YLALLDRLEEDGLpEYEERFKELLNENSIEFVA 849
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7201-7408 |
1.79e-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: 47.44 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7201 EYMQLVAKFNDWVHEAELRLQNSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLVhKQIQEAADKIwSSLNNYEQSELSAEL 7280
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERV-EALNELGEQL-IEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7281 AQFQTKLTNTLANAKTQQSELEKEAERWREYQQSIDRVKATIERTKFV--DEPVQNLAGLHFNIQKLSHAIGNVQSQNSD 7358
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALasEDLGKDLESVEELLKKHKELEEELEAHEPR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 320544548 7359 LTLVNQQAQSLIRQADARNRQLIEQDNAGLNRSWQDLVRSLEQRRDNLQQ 7408
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
9114-9273 |
1.84e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 49.27 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 9114 EDAVVSSP--SESPRTPMVELVIPTEVVELA--LVEDEEQQTTPRIPSPTEKSEVEQDIKSVQTSPQHQPKLDETAV--- 9186
Cdd:PRK10811 861 AEEVQVQPvvAEVPVAAAVEPVVSAPVVEAVaeVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDVAvaq 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 9187 QTSLEVQPDNQENESQTLIVEITETEAQTTPRSEEQSVAVEISTTEIQTDVSGQPAETVEISSQTTVTTTIEKELQTTPK 9266
Cdd:PRK10811 941 EVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVEHNHATAPM 1020
|
....*..
gi 320544548 9267 DSPRAPE 9273
Cdd:PRK10811 1021 TRAPAPE 1027
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
5441-6230 |
1.85e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 49.66 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5441 EECQSWIEKTREKLSECEQipgtlnevqiklNTVKNLRQGFETGQNKLRYLLELKEKVIMNTEQNGAAKIQEDTEALKQD 5520
Cdd:TIGR01612 699 DDLKSKIDKEYDKIQNMET------------ATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILEDFKNKEKE 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5521 FDKLLVDLNDVRQKLANRLAQLEEIFKLY--KILIEWL--EDVEPSVKTSDEFLNDLSEKRAalEKFRVIQRDINGHNDI 5596
Cdd:TIGR01612 767 LSNKINDYAKEKDELNKYKSKISEIKNHYndQINIDNIkdEDAKQNYDKSKEYIKTISIKED--EIFKIINEMKFMKDDF 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5597 VEKINQRLKEDNSLDlKDFQPGLTKFDDLQTQVNKII---------------ESLENQVN-SHEKYKQAYNELQ---DWL 5657
Cdd:TIGR01612 845 LNKVDKFINFENNCK-EKIDSEHEQFAELTNKIKAEIsddklndyekkfndsKSLINEINkSIEEEYQNINTLKkvdEYI 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5658 RRTRIEVEQCADCHGEKDQVESRLNR-LGDIQSSSLEGKA--------LLEACEELSQAVIATSGSEGQDNVAQEIKHLT 5728
Cdd:TIGR01612 924 KICENTKESIEKFHNKQNILKEILNKnIDTIKESNLIEKSykdkfdntLIDKINELDKAFKDASLNDYEAKNNELIKYFN 1003
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5729 SEWETLQTISRDArsslesclaAWQTFLQK---FNKINLWIETMNKRVTK------------SQEGENKTPEdlvNAKKL 5793
Cdd:TIGR01612 1004 DLKANLGKNKENM---------LYHQFDEKekaTNDIEQKIEDANKNIPNieiaihtsiyniIDEIEKEIGK---NIELL 1071
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5794 LEEVLAEKD-NVEDLNDNCELLMEQSACTRIRDQTIETQANYTKLLTSAQGLVAKIEKNLSDHTEFL----NYKKEMDAW 5868
Cdd:TIGR01612 1072 NKEILEEAEiNITNFNEIKEKLKHYNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKkkseNYIDEIKAQ 1151
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5869 IEKAQQVLDDCSTDGDAAIIAQKLDTVnslasrlpegqhllalvqdayskasnITPEDKQEKLRELMTKVREDWDalglA 5948
Cdd:TIGR01612 1152 INDLEDVADKAISNDDPEEIEKKIENI--------------------------VTKIDKKKNIYDEIKKLLNEIA----E 1201
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5949 VKQKLSDLKQAQNRWNDFAANKDKLekwlnetetTLKVAPETKGELSEMKTLLERYKTLSNELKLKGNELEQLQSEARDL 6028
Cdd:TIGR01612 1202 IEKDKTSLEEVKGINLSYGKNLGKL---------FLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDI 1272
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6029 GTEVDAVNRLQSRCDKL-----KNDCS-AHITALEQEMFDYNAYHQSLQDVEKWLLQISFQLMAHNS------------- 6089
Cdd:TIGR01612 1273 KAEMETFNISHDDDKDHhiiskKHDENiSDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSdinlylneianiy 1352
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6090 --LFISNREQTQEQIKQHEAllvEIQKYQTNLDDLNAKGQAQIK--RYESSTPAIRPTVESQL--KNIqdsyNSLLQTSV 6163
Cdd:TIGR01612 1353 niLKLNKIKKIIDEVKEYTK---EIEENNKNIKDELDKSEKLIKkiKDDINLEECKSKIESTLddKDI----DECIKKIK 1425
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320544548 6164 QIKNRLLESlakfqeyEDTLDSIMRNLETYEPIIQTELDapatSLELAQNQLRcaQEMQNKLNNEKS 6230
Cdd:TIGR01612 1426 ELKNHILSE-------ESNIDTYFKNADENNENVLLLFK----NIEMADNKSQ--HILKIKKDNATN 1479
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6789-6954 |
1.95e-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: 47.06 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6789 FEDSMKNMGDWLNEMETATEGELRTTSLPVLEEQLAHYKKLLSDAENKGGLINDVSEQGKSILpTLSNADKLKLNDDIKN 6868
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6869 MKDRYGRIKNTIDDRVNALGDHIKKYKdaksRLAECSQFLGNIQQKLRELNR-PIGSRIEDVQDLLGAYEGILKELKDSK 6947
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQ----FFRDADDLEQWLEEKEAALASeDLGKDLESVEELLKKHKELEEELEAHE 159
|
....*..
gi 320544548 6948 SKMGDMQ 6954
Cdd:cd00176 160 PRLKSLN 166
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7396-7839 |
2.28e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7396 VRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKSSHKEIEALS 7475
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7476 KSILTFlgevhKPSAEAIQAKVDKLVEQQAKLNDTLRD----KEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVhv 7551
Cdd:COG4717 153 ERLEEL-----RELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEEL-- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7552 yDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAHYQAKQNQLPSDIAQEFTALELLAE--RVQVTMETKEKDFKRAKT 7629
Cdd:COG4717 226 -EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGllALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7630 VRTEYVDGVDEVQRWLLQAEVQVQ--ERSLTPTQMKELLQRINHEITAIYERFTLVKtngQLIIENCRNSEEKTLVQ--- 7704
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALglPPDLSPEELLELLDRIEELQELLREAEELEE---ELQLEELEQEIAALLAEagv 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7705 TTIDQLAASLAQVRGWLDEKKQavgdsLDAWTRFMNLYQIVMSWASEKRNFIDQTIEL----RTLPEARNKLNDYVTSVK 7780
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEE-----LEELEEQLEELLGELEELLEALDEEELEEELeeleEELEELEEELEELREELA 456
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 320544548 7781 SIKPIVKHLSEmDKELEHIGQVttVGDLKDKLQEAEDAKISVEAVLlernSLLQEACEE 7839
Cdd:COG4717 457 ELEAELEQLEE-DGELAELLQE--LEELKAELRELAEEWAALKLAL----ELLEEAREE 508
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1888-2100 |
2.30e-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: 47.06 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 1888 WKSFDADAAKLEDWVGQGEQQMSRRPAVlntPHIDKLEKELVKLKSFNNEISQQQAKLVTLGQNADQIsLHLAPEGAAAL 1967
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYG---DDLESVEALLKKHEALEAELAAHEERVEALNELGEQL-IEEGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 1968 KDRVNQMKGKLQKLSEATRGHINEVSDAIiSRQDFNAKLVNFSNWMEQLRNQVTQVEeinperVETSLHVIHALLQEHAD 2047
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASED------LGKDLESVEELLKKHKE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2048 -------KKPSFNAIYDEVKQLALGATPEESNALNDAYTALVVNYQNLETNMLQKKAALE 2100
Cdd:cd00176 151 leeeleaHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4566-4777 |
2.34e-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: 47.06 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4566 EDFDNAISDCSSWINEIKEKL---DYCSDMSSMspKELDKKLATIQDVILLKDEgsaRVLKILEQAQHvLANTAPGGHEA 4642
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLsstDYGDDLESV--EALLKKHEALEAELAAHEE---RVEALNELGEQ-LIEEGHPDAEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4643 INKELTDLQDLWSGIALRIMDVKSNLDDSITQWSGFLDqvqnVRKFNEWLDGQVKELS--EHQTTMTEKRAQLDRVKSTE 4720
Cdd:cd00176 77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD----ADDLEQWLEEKEAALAseDLGKDLESVEELLKKHKELE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 320544548 4721 EKVRVEKIDVDALKIQAKEMIASGQQSQAAFQAQKvLDTFDELFAKTQKLLSHRQDQ 4777
Cdd:cd00176 153 EELEAHEPRLKSLNELAEELLEEGHPDADEEIEEK-LEELNERWEELLELAEERQKK 208
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
7060-7726 |
2.35e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.95 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7060 KNSITEQLQSLKNQLQNLRKAVESQRQKHQ-LQLESHK---KMAAELSEILDWLHSH-----------EGAAKSRPLLDR 7124
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKAIQeLQFENEKvslKLEEEIQENKDLIKENnatrhlcnllkETCARSAEKTKK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7125 DPESVERELQKHQSLSQDIESYLNKFNKIN-DGVKTEIGMPSSLLEMLSEGRSLVASLPHELEEREKYL---------KN 7194
Cdd:pfam05483 174 YEYEREETRQVYMDLNNNIEKMILAFEELRvQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVsllliqiteKE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7195 NRDSRLEYM--QLVAKFNDWVHEAELRLQNSQHGIDYE-HLVQDLDEHKIFFGNEAPIRNLVHKQIQEAADKIWsSLNNY 7271
Cdd:pfam05483 254 NKMKDLTFLleESRDKANQLEEKTKLQDENLKELIEKKdHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIC-QLTEE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7272 EQSELSaELAQFQTKLTNTLANAKTQQSELEkeaERWREYQQsidRVKATIERTKFVDEPVQNLAGlhfNIQKLSHAIGN 7351
Cdd:pfam05483 333 KEAQME-ELNKAKAAHSFVVTEFEATTCSLE---ELLRTEQQ---RLEKNEDQLKIITMELQKKSS---ELEEMTKFKNN 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7352 VQSQNSDLTLVNQQAQSLIRQadarNRQlIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLE 7431
Cdd:pfam05483 403 KEVELEELKKILAEDEKLLDE----KKQ-FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7432 -----DKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKSSHKEI-------EALSKSILTfLGEVHKPSAEAIQAKVDK 7499
Cdd:pfam05483 478 telekEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIinckkqeERMLKQIEN-LEEKEMNLRDELESVREE 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7500 LVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVHVYDEHIAQTEQLLitlnsqVQQAAEESKL 7579
Cdd:pfam05483 557 FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL------KKKGSAENKQ 630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7580 LVAqttahYQAKQNQLPSDIAQEFTALELLAERVQVTMETKE-------KDFKRAKTVrteyvdgVDEVQRWLLQAEVQV 7652
Cdd:pfam05483 631 LNA-----YEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKiseekllEEVEKAKAI-------ADEAVKLQKEIDKRC 698
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320544548 7653 QERSltpTQMKELLQRINHEITAIYErftlvKTNGQLIIENCRNSEEKTL---VQTTIDQLAASLAQVRGWLDEKKQ 7726
Cdd:pfam05483 699 QHKI---AEMVALMEKHKHQYDKIIE-----ERDSELGLYKNKEQEQSSAkaaLEIELSNIKAELLSLKKQLEIEKE 767
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6511-6871 |
2.47e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6511 KIQELKgKAAQV--AEVISNLDGQQVEEQMKSLDRRFADLGKRIDRKsQLLDVTNKGVEGAKGEIDQLQnwvKQQIEELQ 6588
Cdd:PTZ00121 1547 KADELK-KAEELkkAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA-RIEEVMKLYEEEKKMKAEEAK---KAEEAKIK 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6589 APKPlgytpKDAEARQQKIKSLMKDAEAKQSLADVLEK-----RVANMQQELEPVEYSQLESALRNLNTENRNLSGVLKA 6663
Cdd:PTZ00121 1622 AEEL-----KKAEEEKKKVEQLKKKEAEEKKKAEELKKaeeenKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6664 ELDRALEASKARKSLENDLDKARQWLKTKisEVRKLPVYHPLTSAEIEKKIQENRKYDDDAKQFNDSVLTDVQRQAANIM 6743
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAE--EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6744 KDcddaDKAALQQILDEIAADYQTLKDESSKRGKSLDDLLQgrkafEDSMKN--MGDWLNEMETATEGELRTTSLPVLEE 6821
Cdd:PTZ00121 1775 KE----KEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANII-----EGGKEGnlVINDSKEMEDSAIKEVADSKNMQLEE 1845
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 320544548 6822 QLAHYKkllsdaeNKGGLINDVSEQGKSilPTLSNADKLKLNDDIKNMKD 6871
Cdd:PTZ00121 1846 ADAFEK-------HKFNKNNENGEDGNK--EADFNKEKDLKEDDEEEIEE 1886
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
10856-11457 |
3.00e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10856 HLKHRLDAMIQQLDQGEQQSKALQEQQQELARhcddalatamrmeqasIGQRISNLRAALKTWQGFLQRVTQLSESYEQr 10935
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEE----------------VLREINEISSELPELREELEKLEKEVKELEE- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10936 vnqLQQEFGAAQKLLdansESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELKECISPHdMKTIRQRNWLLw 11015
Cdd:PRK03918 236 ---LKEEIEELEKEL----ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY-IKLSEFYEEYL- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11016 QQHADLDYQLANL---INSIEERLSLLSNYQIRYDRISQWLQRLEQRVEKdadvtamtnPEQAAKQLEQQVNSELQLRDK 11092
Cdd:PRK03918 307 DELREIEKRLSRLeeeINGIEERIKELEEKEERLEELKKKLKELEKRLEE---------LEERHELYEEAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11093 EREWLLSTSRELLTLYSEPEVR-SQVQQQSDSLIDRWQRLKYLAKQKATKIGELKMT---------LLRLEERIALIRAW 11162
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAkEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrELTEEHRKELLEEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11163 LFEVESqldkplnfesytpnvIEAKLKEHEQIQRSIEhhssnvgEVLNLVEMLLNDADSWRTQVNtsgLAASAQNLEQRW 11242
Cdd:PRK03918 458 TAELKR---------------IEKELKEIEEKERKLR-------KELRELEKVLKKESELIKLKE---LAEQLKELEEKL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11243 KNVCSQSAERKARILTiwNLLQQLIKLTAEHKNwLGKQESQIAGFERDQKS--HSKHKLEERQMELRAKLEELESQSVN- 11319
Cdd:PRK03918 513 KKYNLEELEKKAEEYE--KLKEKLIKLKGEIKS-LKKELEKLEELKKKLAEleKKLDELEEELAELLKELEELGFESVEe 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11320 ----LRQLEQIYAKLAMSAGVEPEniqkltlptkvmvsmWRQLTPRCHALLDAIDKDAKLMREFNNAQLEATNSLNAIQK 11395
Cdd:PRK03918 590 leerLKELEPFYNEYLELKDAEKE---------------LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320544548 11396 AL--EQLPSAENQQTSKA-EPKAVLQRLESLEKKLQDAQqhvQQADNLAQEAKTRTKQQPQLKQL 11457
Cdd:PRK03918 655 KYseEEYEELREEYLELSrELAGLRAELEELEKRREEIK---KTLEKLKEELEEREKAKKELEKL 716
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
10427-10987 |
3.12e-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: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10427 DFMMELIRVHGQVdyERLRKATERLEGLAGD------LHNREQLIDELKGAAKPLIescDVQIVEQIESAVQEAVVAWND 10500
Cdd:COG4913 232 EHFDDLERAHEAL--EDAREQIELLEPIRELaeryaaARERLAELEYLRAALRLWF---AQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10501 TSENLQQLRTRYQRAVELWDKYRNASAAVKNsidqqmDAVKSLEQPLDALQHAkvcqdnLTTQNDRILELRDIVAKIAAD 10580
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERE------LEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10581 VGLDASAL------MQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVT-LAK------AYFNNVQQDISREAP 10647
Cdd:COG4913 375 LPASAEEFaalraeAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAsLERrksnipARLLALRDALAEALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10648 Q--------------NPKESEEQLAALRAhLQTLART----EEQLRQ---------LKERHQNSEVAPSVASS-----DD 10695
Cdd:COG4913 455 LdeaelpfvgelievRPEEERWRGAIERV-LGGFALTllvpPEHYAAalrwvnrlhLRGRLVYERVRTGLPDPerprlDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10696 DGILEVLAlwqkiFQDT-FQEYhrLSTRLARSQNssealrlwrqylqhvqsFLSCAIPEDyssLREQQQlcAIHQNLLIS 10774
Cdd:COG4913 534 DSLAGKLD-----FKPHpFRAW--LEAELGRRFD-----------------YVCVDSPEE---LRRHPR--AITRAGQVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10775 QQSVLSETPLESELSEQY-------KALtnlhnETLSRIMQrngELERRVSGWNAYRQQLAALLDWLRQREAERNALQLR 10847
Cdd:COG4913 585 GNGTRHEKDDRRRIRSRYvlgfdnrAKL-----AALEAELA---ELEEELAEAEERLEALEAELDALQERREALQRLAEY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10848 YIHLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHcdDALATAMRMEQASIGQRISNLRAALKTWQGFLQRVTQ 10927
Cdd:COG4913 657 SWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEEL--EAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10928 LSESYEQRVnQLQQEFGAAQKLLDANseslptQPAAIEQLLGSLRAQRVQLGAQVSALES 10987
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 ... |
266-385 |
3.56e-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: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 266 QEEQERVQKKTFTNWINSYL-----LKRVPPLR--IDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFL--SNA 336
Cdd:cd21325 18 QHSYSEEEKYAFVNWINKALendpdCRHVIPMNpnTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFIiqENL 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 320544548 337 NTALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTII---LYFQIEEnSRN 385
Cdd:cd21325 98 NLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIkigLFADIEL-SRN 148
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7399-7683 |
3.63e-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: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7399 LEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKSSHKEIEALSKSI 7478
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7479 ltflgevhkpsaEAIQAKVDKLVEQQAKLNdtlrdkeqqvskdleeieqvfRRISQLQDKLNALHEQLQSVHvydehiAQ 7558
Cdd:COG4913 695 ------------EELEAELEELEEELDELK---------------------GEIGRLEKELEQAEEELDELQ------DR 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7559 TEQLLITLNSQVQQAAEEsKLLVAQTTAHYQAKQNQLPSDIAQEFTALELLAERVQVTMETKEKDFK-RAKTVRTEyVDG 7637
Cdd:COG4913 736 LEAAEDLARLELRALLEE-RFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPaETADLDAD-LES 813
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 320544548 7638 VDEVQRWL--LQAE--VQVQER------SLTPTQMKELLQRINHEITAIYERFTLV 7683
Cdd:COG4913 814 LPEYLALLdrLEEDglPEYEERfkellnENSIEFVADLLSKLRRAIREIKERIDPL 869
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
268-374 |
3.66e-04 |
|
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: 44.60 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 268 EQERVQKKTFTNWINSYllkRVPPlRIDDLINDLRDGTKLIALLEVLsgeRLPVEKGRVLRRPH--------FLSNANTA 339
Cdd:cd21330 9 EGETREERTFRNWMNSL---GVNP-RVNHLYSDLSDALVIFQLYEKI---KVPVDWNRVNKPPYpklgenmkKLENCNYA 81
|
90 100 110
....*....|....*....|....*....|....*.
gi 320544548 340 LQFLASK-RIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21330 82 VELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLM 117
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4256-4347 |
3.89e-04 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 43.85 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4256 ADSLKSWLDETENALpADIELKTTLDEKRNKLQTYRDILNDINNHQVELGNLQEIAANL----PEKTELVDQIIKDISDR 4331
Cdd:pfam00435 10 ADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLidegHYASEEIQERLEELNER 88
|
90
....*....|....*.
gi 320544548 4332 FGKLQKRAQNYVERYE 4347
Cdd:pfam00435 89 WEQLLELAAERKQKLE 104
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
7074-7875 |
3.97e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7074 LQNLRKAVESQRQK---HQLQLESHKKMAAELSEILDWLHSHEGAAKSRPLLDRdpeSVERELQKHQSLSQDIESYLNKF 7150
Cdd:TIGR00606 188 LETLRQVRQTQGQKvqeHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVK---SYENELDPLKNRLKEIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7151 NKINDG----------------------VKTEIGMPSSLLEMLSEGRSLVASLPHELEEREKYLKNNRDSRLEYMQLVAK 7208
Cdd:TIGR00606 265 MKLDNEikalksrkkqmekdnselelkmEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7209 FNDWVHEAELRLQNSQ-HGIDYEHLVQDLDEHKIFFGNEapirnlvHKQIQEAADKIWSSLNNYEQSELSAELAQFQTKL 7287
Cdd:TIGR00606 345 LLVEQGRLQLQADRHQeHIRARDSLIQSLATRLELDGFE-------RGPFSERQIKNFHTLVIERQEDEAKTAAQLCADL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7288 TNTLANAKTQQSELE-KEAERWREYQQSIDRVKATIERTKFVDEPVQNLAGLHFNIQKLSHAIGNVQS------QNSDLT 7360
Cdd:TIGR00606 418 QSKERLKQEQADEIRdEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERelskaeKNSLTE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7361 LVNQQAQSL-IRQADA-RNRQLIEQDNAGLNRSWQDLVRSL----------EQRRDNLQQLAEHWDG----------FEN 7418
Cdd:TIGR00606 498 TLKKEVKSLqNEKADLdRKLRKLDQEMEQLNHHTTTRTQMEmltkdkmdkdEQIRKIKSRHSDELTSllgyfpnkkqLED 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7419 SLHAWEKALGRLEDKFRNVDPTVRSrrhLEDTKNAIQelreesNQLKSSHKEIEALSKSILTFLG-EVHKPSAEAIQAKV 7497
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELAS---LEQNKNHIN------NELESKEEQLSSYEDKLFDVCGsQDEESDLERLKEEI 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7498 DKLVEQQAKLNDTLRDKEQQVSKDLEEIEQ---VFRRISQLQDKLNALHEQLQS-VHVYDEHIAQTEQLLitlnSQVQQA 7573
Cdd:TIGR00606 649 EKSSKQRAMLAGATAVYSQFITQLTDENQSccpVCQRVFQTEAELQEFISDLQSkLRLAPDKLKSTESEL----KKKEKR 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7574 AEESKLLVAQTTAHYQAKQNQLP----------SDIAQEFTALELLAERVQVTMETKE--KDFKRAKTVRTEYVDGVDEV 7641
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPelrnklqkvnRDIQRLKNDIEEQETLLGTIMPEEEsaKVCLTDVTIMERFQMELKDV 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7642 QRWLLQ--AEVQVQERSLTPTQMKELLQRINHEITAIYERFTLvktNGQLIIENcrnSEEKTLVQTTIDQLAASLAQVRG 7719
Cdd:TIGR00606 805 ERKIAQqaAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIEL---NRKLIQDQ---QEQIQHLKSKTNELKSEKLQIGT 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7720 WLDEKKQAVGDSLDAWTRFMNLYQIVmswaSEKRNfidQTIELRTLPEARNKLNDYVTSVK--SIKPIVKHLSEMDKELE 7797
Cdd:TIGR00606 879 NLQRRQQFEEQLVELSTEVQSLIREI----KDAKE---QDSPLETFLEKDQQEKEELISSKetSNKKAQDKVNDIKEKVK 951
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320544548 7798 HIgqVTTVGDLKDKLQEA-EDAKISVEAVLLERNSLLQEaceewdqCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQL 7875
Cdd:TIGR00606 952 NI--HGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEE-------CEKHQEKINEDMRLMRQDIDTQKIQERWLQDNL 1021
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
8657-8882 |
4.09e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 48.16 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 8657 APVE-------LPAPQVDVEQPVVVATTSP-VHVPTADVV-EPKDSSPTSTTAAVVDVEavvediNEIWPLEHHLKPTNI 8727
Cdd:PRK10263 335 APVEpvtqtppVASVDVPPAQPTVAWQPVPgPQTGEPVIApAPEGYPQQSQYAQPAVQY------NEPLQQPVQPQQPYY 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 8728 DFSQHVEELAAPAAVTAETEASMPVEEIWPTSPETGNSLTLEQYE--------FEPQSPHEESTKSD--LVKPQETEPQV 8797
Cdd:PRK10263 409 APAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQstfapqstYQTEQTYQQPAAQEplYQQPQPVEQQP 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 8798 VAETKPEGITTGSITITKTTTTITSSTEVPE-ETLV---QNVPADEQQPPANKIKTDIQSfleaeqtlAAALKEQSSTPT 8873
Cdd:PRK10263 489 VVEPEPVVEETKPARPPLYYFEEVEEKRARErEQLAawyQPIPEPVKEPEPIKSSLKAPS--------VAAVPPVEAAAA 560
|
....*....
gi 320544548 8874 GASVAEDVQ 8882
Cdd:PRK10263 561 VSPLASGVK 569
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3819-3914 |
4.14e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 43.86 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3819 YQDILNQTVNWLDQVEKLIHNENPASwtSAQEIRSKLYKYKATNQDINSHKRIVEAVNEKAAALLgSAAPANADEISKAV 3898
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASEDLGK--DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI-EEGHPDAEEIEERL 79
|
90
....*....|....*.
gi 320544548 3899 AEVNKRYDQVGQDCAK 3914
Cdd:smart00150 80 EELNERWEELKELAEE 95
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
6511-6708 |
4.16e-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: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6511 KIQELKGKAAQVAEVISNLDGQQ--VEEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEEL- 6587
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELa 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6588 -------------------------QAPKPLGYTPKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELEpvEYSQ 6642
Cdd:COG4942 108 ellralyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA--ELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320544548 6643 LESALRNLNTENRNLSGVLKAELDRALEASKARKSLENDLDKARQWLKTKISEVRKLPVYHPLTSA 6708
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
5507-6255 |
4.25e-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: 48.30 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5507 AAKIQEDTEALKQDFDKLL---VDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDvepSVKTS-DEFLNDLSEKRAALEK 5582
Cdd:pfam12128 243 FTKLQQEFNTLESAELRLShlhFGYKSDETLIASRQEERQETSAELNQLLRTLDD---QWKEKrDELNGELSAADAAVAK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5583 FRviqrdinghnDIVEKINQRLKEDNSLDLKDFQPGLTKFDDLQTQVNKIIESLENQVNSHEKYKQAYNelqdwlRRTRI 5662
Cdd:pfam12128 320 DR----------SELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYN------RRRSK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5663 EVEQCADchgekdqvesRLNRLGDIQSSSLEGKALLEACEElsqAVIATSGSEGQDNVAQEIKHLTSEWETLQTISRDAR 5742
Cdd:pfam12128 384 IKEQNNR----------DIAGIKDKLAKIREARDRQLAVAE---DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5743 SSLESCLAAWQTFLQKFNKINLwIETMNKRVTKSQEGENKTPEDLVNAKKLLEEVLaekdnvEDLND-NCELLMEQSACT 5821
Cdd:pfam12128 451 LRLNQATATPELLLQLENFDER-IERAREEQEAANAEVERLQSELRQARKRRDQAS------EALRQaSRRLEERQSALD 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5822 RIRDQTIETQANYTKLL-TSAQGLVAKIEKNLSdhTEFLnYKKEMDAwiekaqqVLDDCSTDGDAAIIAQKLDT----VN 5896
Cdd:pfam12128 524 ELELQLFPQAGTLLHFLrKEAPDWEQSIGKVIS--PELL-HRTDLDP-------EVWDGSVGGELNLYGVKLDLkridVP 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5897 SLASRLPEGQHLLALVQDAYSKASnitpeDKQEKLRELMTKVREDWDALGLAVKQKLSDLKQA---QNRWNDFAAN-KDK 5972
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAR-----EKQAAAEEQLVQANGELEKASREETFARTALKNArldLRRLFDEKQSeKDK 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5973 LEKWLNE-----TETTLKVAPETKGELSEMKTLLERYKTLSNELKLKGNELEQLQSEARDlgtevDAVNRLQSRCDKLKN 6047
Cdd:pfam12128 669 KNKALAErkdsaNERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALD-----AQLALLKAAIAARRS 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6048 DCSAHITALEQEmfdynaYHQSLQDvekwlLQISFQLMAHNSLFISNREQTQEQIKQ--HEAL----------LVEIQKY 6115
Cdd:pfam12128 744 GAKAELKALETW------YKRDLAS-----LGVDPDVIAKLKREIRTLERKIERIAVrrQEVLryfdwyqetwLQRRPRL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6116 QTNLDDLNAKG---QAQIKRYESSTPAIRPTVESQLKNIQDSynsllqtsvqiKNRLLESLAKfqeyedtLDSIMRNLET 6192
Cdd:pfam12128 813 ATQLSNIERAIselQQQLARLIADTKLRRAKLEMERKASEKQ-----------QVRLSENLRG-------LRCEMSKLAT 874
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320544548 6193 YepiiqtELDAPATSLEL-AQNQLRCAQEMQNKLNNEKSRLAAAVQACEAATASISRpSSPLET 6255
Cdd:pfam12128 875 L------KEDANSEQAQGsIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADHSG-SGLAET 931
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
10590-10841 |
4.50e-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: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10590 QGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVtlakayfNNVQQDIsreapqnpKESEEQLAALRAHLQTLAR 10669
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------AALARRI--------RALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10670 TEEQLRQLKERHQNsEVAPSVASSDDDGILEVLALwqkifqdtfqeyhrlstrLARSQNSSEALRLwRQYLQHVQSFLSC 10749
Cdd:COG4942 91 EIAELRAELEAQKE-ELAELLRALYRLGRQPPLAL------------------LLSPEDFLDAVRR-LQYLKYLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10750 AIpedySSLREQQQLCAIHQNLLISQQSVLSEtpLESELSEQYKALTNL---HNETLSRIMQRNGELERRVSGWNAYRQQ 10826
Cdd:COG4942 151 QA----EELRADLAELAALRAELEAERAELEA--LLAELEEERAALEALkaeRQKLLARLEKELAELAAELAELQQEAEE 224
|
250
....*....|....*
gi 320544548 10827 LAALLDWLRQREAER 10841
Cdd:COG4942 225 LEALIARLEAEAAAA 239
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3173-3839 |
4.53e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3173 KLKQLCSKWDEFDTIIEELDnwMKNVEAVVKNQNLKSTAEAKNAHLK----QLQDISKDIERRGAAINELmdQGREIEGE 3248
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELE--EEIEELQKELYALANEISRLEQQKQilreRLANLERQLEELEAQLEEL--ESKLDELA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3249 TDLNL---KLSRLNTRYQTLKNLCKESIAKYVNYV-------KDHESFDKDFDSFKQN-----------------LQSSV 3301
Cdd:TIGR02168 337 EELAEleeKLEELKEELESLEAELEELEAELEELEsrleeleEQLETLRSKVAQLELQiaslnneierlearlerLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3302 DELAKTNEIVGDQSVLQDQQNKLREMSDKRILDSTLFEGLIDRGEKLyghtspegrEIIRQQLRALRTLWDNYTDDLNSA 3381
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL---------EELREELEEAEQALDAAERELAQL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3382 TQKIDQCLLQFNEFSIAQDQLtKWLKDVDKAMQSHTEPKTTLQEKRAQLQNHKLLHQEITTHNVLVDNVcDKAQILVDQI 3461
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEGV-KALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENL-NAAKKAIAFL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3462 KDNSLN----VYLTSIKQlfQSIVQKSDEILHNLDDCVQKHNELNNALSSAKTWISNEKAKLLECDDaygekadikrkIE 3537
Cdd:TIGR02168 566 KQNELGrvtfLPLDSIKG--TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDD-----------LD 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3538 TLGQLAQNKPQAMKIISDIRDLFEKVKATT--SEKGNEVL---DKEIEELETTMKSHFDDIEGIEGKQKDVLAQWDKFEK 3612
Cdd:TIGR02168 633 NALELAKKLRPGYRIVTLDGDLVRPGGVITggSAKTNSSIlerRREIEELEEKIEELEEKIAELEKALAELRKELEELEE 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3613 ALEELTKWCRSAEAVFREQQLQ-STLHEKVEQLEKYKIQR-----ELILQKEKEIDAFGDAAHALLNncGADRLKTLTTQ 3686
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDlARLEAEVEQLEERIAQLskeltELEAEIEELEERLEEAEEELAE--AEAEIEELEAQ 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3687 ITNRYQLLQVLSKEVVNRWSNLVDDHQFYQDKYNEVDLWLQPIES--QMAKVLLDEPTQSSNILQVLLSEKEQAESLFAA 3764
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAteRRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320544548 3765 LNAAGEKALPEtstqgREKIRKDLRDIRDRWDKLDEGIRNLEKRQEAQGVQLSSYQDILNQTVNWLDQVEKLIHN 3839
Cdd:TIGR02168 871 LESELEALLNE-----RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
7423-7585 |
4.61e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.00 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7423 WEKALGRLEDKFRNVDPTVRSRRH-LEDTKNAIQELREESNQLKSSHK---EIEAL--SKSILTFLGEVHKPSAEAIQAK 7496
Cdd:PRK05771 84 LEELIKDVEEELEKIEKEIKELEEeISELENEIKELEQEIERLEPWGNfdlDLSLLlgFKYVSVFVGTVPEDKLEELKLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7497 VDKLVEQ---QAKLND-----TLRDKEQQVSKDL-----------------EEIEQVFRRISQLQDKLNALHEQLQSV-- 7549
Cdd:PRK05771 164 SDVENVEyisTDKGYVyvvvvVLKELSDEVEEELkklgferleleeegtpsELIREIKEELEEIEKERESLLEELKELak 243
|
170 180 190
....*....|....*....|....*....|....*.
gi 320544548 7550 HVYDEHIAQTEQLLItlnsQVQQAAEESKLLVAQTT 7585
Cdd:PRK05771 244 KYLEELLALYEYLEI----ELERAEALSKFLKTDKT 275
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7362-8001 |
4.85e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7362 VNQQAQSLIRQADArnrqlieqdnAglnRSWQDLVRSLEQRRDNLQQLaeHWDGFENSLHAWEKALGRLEDKFRnvdptv 7441
Cdd:COG1196 198 LERQLEPLERQAEK----------A---ERYRELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELE------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7442 RSRRHLEDTKNAIQELREESNQLKsshKEIEALSKSIltflgevhkpsaEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKD 7521
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELE---LELEEAQAEE------------YELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7522 LEEIEQVFRRISQLQDKLNALHEQLQSVhvyDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAHYQAKQNQLpsdiaQ 7601
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEA---EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-----R 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7602 EFTALELLAERVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELLQRINHEITAIYERFT 7681
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7682 LVKTNGQLIIEncRNSEEKTLVQTTIDQLAASLAQVRGWLDEKKQA----VGDSLDAWTRFMNLYQIVMSWASEKRNFID 7757
Cdd:COG1196 474 LLEAALAELLE--ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrgLAGAVAVLIGVEAAYEAALEAALAAALQNI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7758 QTIELRTLPEARNKLNDYVTSVKSIKPIVK-HLSEMDKELEHIGQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEA 7836
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7837 CEEWDqcERKIKDIRSWHEKTKQGLDSSQQQkkplrDQLGFCEKTLADINVQKTKLRLSIEKLEVHfrngmggdpRLSEN 7916
Cdd:COG1196 632 LEAAL--RRAVTLAGRLREVTLEGEGGSAGG-----SLTGGSRRELLAALLEAEAELEELAERLAE---------EELEL 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7917 VDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRLVMAPTYLPHDRERALAEQQdlitQELDE 7996
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE----RELER 771
|
....*
gi 320544548 7997 LLQSL 8001
Cdd:COG1196 772 LEREI 776
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
10441-11110 |
6.21e-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: 47.53 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10441 YERLRKATERLEGLAGDLHNREQLIDELKGAAKPLIEScDVQIVEQIEsAVQEAVVAWNdtsenlQQLRTryqraveLWD 10520
Cdd:pfam12128 233 IAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSD-ETLIASRQE-ERQETSAELN------QLLRT-------LDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10521 KYRNASAAVKNSIDQQMDAVKSLEQPLDAL--QHAKVCQDNLTTqndrilelrdivakIAADvgLDASALMQGELDALGQ 10598
Cdd:pfam12128 298 QWKEKRDELNGELSAADAAVAKDRSELEALedQHGAFLDADIET--------------AAAD--QEQLPSWQSELENLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10599 RLaeckDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREApqnpkeSEEQLAALRAHLQTL-----ARTEEQ 10673
Cdd:pfam12128 362 RL----KALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREA------RDRQLAVAEDDLQALeselrEQLEAG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10674 LRQLKERHQNSEVAPSVASS--DDDGILEVLALWQKIFQD-----------TFQEYHRLSTRLA----RSQNSSEALRLW 10736
Cdd:pfam12128 432 KLEFNEEEYRLKSRLGELKLrlNQATATPELLLQLENFDErierareeqeaANAEVERLQSELRqarkRRDQASEALRQA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10737 RQYLQHVQSFLSCA----IPEDYS---SLREQQQLCAIHQNLLISQQsVLSETPLESELSE-QYKALTNLHNETLsrimq 10808
Cdd:pfam12128 512 SRRLEERQSALDELelqlFPQAGTllhFLRKEAPDWEQSIGKVISPE-LLHRTDLDPEVWDgSVGGELNLYGVKL----- 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10809 rngELER-RVSGWNAYRQQLAALLDWL---------RQREAERNALQLRyihlKRVPHLKHRLDAMIQQLDQGEQQSKAL 10878
Cdd:pfam12128 586 ---DLKRiDVPEWAASEEELRERLDKAeealqsareKQAAAEEQLVQAN----GELEKASREETFARTALKNARLDLRRL 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10879 QEQQQELARHCDDALATAMRMEQASIGQRISNLRAALKTWQGFLQRVT-QLSESYEQRVNQLQQEFGAAQklldansesl 10957
Cdd:pfam12128 659 FDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKeQKREARTEKQAYWQVVEGALD---------- 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10958 ptqpAAIEQLLGSLRAQRVQLGAQVSALesltvtQEELKECISPHDMKTIRQrnwllwqqhADLDYQLANLINSIEerls 11037
Cdd:pfam12128 729 ----AQLALLKAAIAARRSGAKAELKAL------ETWYKRDLASLGVDPDVI---------AKLKREIRTLERKIE---- 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11038 llsnyQIRYDR--ISQWLQRLEQR--VEKDADVTAMTNPEQAAKQLEQQV---NSELQLRDKEREWLLSTSRELLTLYSE 11110
Cdd:pfam12128 786 -----RIAVRRqeVLRYFDWYQETwlQRRPRLATQLSNIERAISELQQQLarlIADTKLRRAKLEMERKASEKQQVRLSE 860
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6066-6169 |
6.80e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 43.09 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6066 YHQSLQDVEKWLLQISFQLMAHNslFISNREQTQEQIKQHEALLVEIQKYQTNLDDLNAKGQAQIKRYESSTPAIrptvE 6145
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASED--LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEI----E 76
|
90 100
....*....|....*....|....
gi 320544548 6146 SQLKNIQDSYNSLLQTSVQIKNRL 6169
Cdd:smart00150 77 ERLEELNERWEELKELAEERRQKL 100
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5226-5427 |
7.35e-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: 45.51 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5226 NEFATWLRNAKERLSKcSEPTGDKQALAEKTHQLKILQGELPEGAQKLKNALEQGEiACRSAEPEDCEIIEQEVALLQEE 5305
Cdd:cd00176 10 DELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGE-QLIEEGHPDAEEIQERLEELNQR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5306 FDAYREALNKAKDYLEVGIVKWSDYQDQyTEALEWLSKTEALVQSYNKLQDsLIQKKVVLEQFQGHLQTLFDWQKTLDDL 5385
Cdd:cd00176 88 WEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 320544548 5386 NMKAQVLLETC---SDTRISNAIMQLTTKYNALLTLAKEVMRRLE 5427
Cdd:cd00176 166 NELAEELLEEGhpdADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
424-517 |
8.61e-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: 43.06 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 424 LLNWVTNALPKDSG--VEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQ----RLETAFDVAEsKLGIAKLLD 497
Cdd:cd21218 15 LLRWVNYHLKKAGPtkKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEdlekRAEKVLQAAE-KLGCKYFLT 93
|
90 100
....*....|....*....|
gi 320544548 498 AEdvDVPKPDEKSIMTYVAQ 517
Cdd:cd21218 94 PE--DIVSGNPRLNLAFVAT 111
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7787-8230 |
9.01e-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: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7787 KHLSEMDKELEHIG-QVTTVGDLKDKLQEAEDAKISVEAVLLERNSL-LQEACEEWDQCERKIKDIRSWHEKTKQGLDSS 7864
Cdd:COG4913 235 DDLERAHEALEDAReQIELLEPIRELAERYAAARERLAELEYLRAALrLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7865 QQQKKPLRDQLGFCEKTLADINVQ-KTKLRLSIEKLEVHFRngmggdpRLSENVDDLVRVLDGLGELVKAKSQSLEQTLA 7943
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELE-------ERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7944 QIDVYQQQMQSLRQRIIQEEQQLRlvmaptylphDRERALAEQQDLITQELDELLQSLSSVEDGIANMN----------- 8012
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAE----------AALRDLRRELRELEAEIASLERRKSNIPARLLALRdalaealglde 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 8013 -------------------QSSLDGMLHGLKLiqsNLEV---HERDAIELKNQ-----------AKKLPTDPATERLLND 8059
Cdd:COG4913 458 aelpfvgelievrpeeerwRGAIERVLGGFAL---TLLVppeHYAAALRWVNRlhlrgrlvyerVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 8060 TV--------------------DRIDLL-------LRRTQQGIT---MI-ANAMHGQKKRQQEIDEY-------QQHLLE 8101
Cdd:COG4913 535 SLagkldfkphpfrawleaelgRRFDYVcvdspeeLRRHPRAITragQVkGNGTRHEKDDRRRIRSRyvlgfdnRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 8102 LEQWIIEVSAELASFEPTSDSSTDEQvlkSQVERSQQLLRTLKDRQQSMEDLVEQTRQLQ-----------SHPDVSPLA 8170
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAEL---DALQERREALQRLAEYSWDEIDVASAEREIAeleaelerldaSSDDLAALE 691
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 8171 DTLmEQLQSIITILREQVTVATKRIFTIEKRIVDLRKAKsEEAQRQRVLADSLIKPPTEA 8230
Cdd:COG4913 692 EQL-EELEAELEELEEELDELKGEIGRLEKELEQAEEEL-DELQDRLEAAEDLARLELRA 749
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
7333-7549 |
9.64e-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: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7333 QNLAGLHFNIQKLSHAIGNVQSQ----NSDLTLVNQQAQSLIRQADARNRQL--IEQDNAGLNRSWQDLVRSLEQRRDNL 7406
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEekalLKQLAALERRIAALARRIRALEQELaaLEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7407 QQLAEHWdgFENSLHAWEKALGRLEDKFRNVdptvrsrRHLEDTKNAIQELREESNQLKSSHKEIEALSKSILTflgevh 7486
Cdd:COG4942 107 AELLRAL--YRLGRQPPLALLLSPEDFLDAV-------RRLQYLKYLAPARREQAEELRADLAELAALRAELEA------ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320544548 7487 kpSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSV 7549
Cdd:COG4942 172 --ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
10610-11054 |
1.03e-03 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 46.89 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10610 LANVAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPS 10689
Cdd:COG4995 8 ALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10690 VASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLCAIHQ 10769
Cdd:COG4995 88 ALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10770 NLLISQQSVLSETPLESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYI 10849
Cdd:COG4995 168 LALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10850 HLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALATAMRMEQASIGQRISNLRAALKTWQGFLQRVTQLS 10929
Cdd:COG4995 248 AALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10930 ESYEQRVNQLQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELKECISPHDMKTIRQ 11009
Cdd:COG4995 328 AALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQ 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 320544548 11010 RNWLLWQQHADLDYQLANLInsIEERLSLLSNYQIRYDRISQWLQ 11054
Cdd:COG4995 408 LLRLLLAALALLLALAAYAA--ARLALLALIEYIILPDRLYAFVQ 450
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6302-7137 |
1.05e-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: 46.97 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6302 EIQVELSDVNEALLDPIAHERVKNYRRivrLNSahvgKLNELVAKVQSHLGGLTASVSELEQQQKQRAELQDwvkkqqss 6381
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEELREELEE---LQE----ELKEAEEELEELTAELQELEEKLEELRLEVSELEE-------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6382 vsdwmmrpcklRPEAAQQELvsmNDLLNSIGDKRSQLMLemtgsLGDEDTDLDDNIDKLESELMDAIAKKQAgqnvidgY 6461
Cdd:TIGR02168 282 -----------EIEELQKEL---YALANEISRLEQQKQI-----LRERLANLERQLEELEAQLEELESKLDE-------L 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6462 RQGMADVQNWFDTLIKRMDvldrgsglNCAQKMAAINEIKNEYELQGHPKIQELKGKAAQVAEVisNLDGQQVEEQMKSL 6541
Cdd:TIGR02168 336 AEELAELEEKLEELKEELE--------SLEAELEELEAELEELESRLEELEEQLETLRSKVAQL--ELQIASLNNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6542 DRRFADLGKRIDR-KSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEELQApkplgytpkDAEARQQKIKSLMKDAEAKQSL 6620
Cdd:TIGR02168 406 EARLERLEDRRERlQQEIEELLKKLEEAELKELQAELEELEEELEELQE---------ELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6621 ADVLEKRVANMQQELEpveysQLESALRNLNTENRNLSGVLKAELDRALE----------ASKARKSLENDLDKARQWLK 6690
Cdd:TIGR02168 477 LDAAERELAQLQARLD-----SLERLQENLEGFSEGVKALLKNQSGLSGIlgvlselisvDEGYEAAIEAALGGRLQAVV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6691 TKISEVRKLPVYHPLTSAEIEKKIQENRKYDDDAKQFNDSVLTDVQRQAANIMKDCDDADKA---ALQQILDE--IAADY 6765
Cdd:TIGR02168 552 VENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkALSYLLGGvlVVDDL 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6766 QT-LKDESSKRGK----SLDDLL---QGRKAFEDSMKNMGDWLNEMETAtegELRTTsLPVLEEQLAHYKKLLSDAENKG 6837
Cdd:TIGR02168 632 DNaLELAKKLRPGyrivTLDGDLvrpGGVITGGSAKTNSSILERRREIE---ELEEK-IEELEEKIAELEKALAELRKEL 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6838 GLINDVSEQGKSILPTLSnadklklnDDIKNMKDRYGRIKNTIDDRVNALGDHIKKYKDAKSRLAECSQFLGNIQQKLRE 6917
Cdd:TIGR02168 708 EELEEELEQLRKELEELS--------RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6918 LNRPIGS---RIEDVQDLLGAYEGILKELKDSKSKMGDMQMDDLPELQSILAQQDDMIKLIEDqlahlrqllllREQFIA 6994
Cdd:TIGR02168 780 AEAEIEEleaQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED-----------LEEQIE 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6995 LINEIIAfimKYTDVIIDIENSPDSLEDKINKYDDVIVKIQEcegVLASANDKGQKIASEGNAADKnsiteQLQSLKNQL 7074
Cdd:TIGR02168 849 ELSEDIE---SLAAEIEELEELIEELESELEALLNERASLEE---ALALLRSELEELSEELRELES-----KRSELRREL 917
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320544548 7075 QNLRKAVEsqrqKHQLQLESHKKMAAELSEIL--DWLHSHEGAAKSRPLLDRDPESVERELQKHQ 7137
Cdd:TIGR02168 918 EELREKLA----QLELRLEGLEVRIDNLQERLseEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
847-1034 |
1.05e-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: 45.13 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 847 EEWLQLAEQKVNQSEDERL------------DFFQDIPVWKDKFDALASSANYLIASCEEPiAQQLRQRHGALSERFERL 914
Cdd:cd00176 13 EAWLSEKEELLSSTDYGDDlesveallkkheALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQERLEELNQRWEEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 915 FANTKQYMHAGDIIRSRQEYKSGIEQLSRWLRGAESVLDQRQVLGNSEQVKEYGQQLQQLASEIDDNEELFKTISRNFQS 994
Cdd:cd00176 92 RELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 320544548 995 LIQDLSRDEVDKMMKLLKQEKESLVRIRAQLPAKLHLFHQ 1034
Cdd:cd00176 172 LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
273-374 |
1.20e-03 |
|
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409142 Cd Length: 116 Bit Score: 42.90 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 273 QKKTFTNWINSYL-----LKRVPPL--RIDDLINDLRDGTKLIALLEV-LSG---ERlPVEKGRVLRRphFLSNANTALQ 341
Cdd:cd21293 2 EKGSYVDHINRYLgddpfLKQFLPIdpSTNDLFDLVKDGVLLCKLINVaVPGtidER-AINTKKVLNP--WERNENHTLC 78
|
90 100 110
....*....|....*....|....*....|....*
gi 320544548 342 FLASKRI--KLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21293 79 LNSAKAIgcSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3180-3271 |
1.45e-03 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 42.31 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3180 KWDEFDTIIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINELMDQGREI-----EGETDLNLK 3254
Cdd:pfam00435 2 LLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLideghYASEEIQER 81
|
90
....*....|....*..
gi 320544548 3255 LSRLNTRYQTLKNLCKE 3271
Cdd:pfam00435 82 LEELNERWEQLLELAAE 98
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
5492-6212 |
1.50e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5492 LELKEKVIMNTEQNGAAKIQEDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDVEPSVKTSDEFLN 5571
Cdd:TIGR00618 181 LALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5572 DLSEKRAALEKFrviQRDINGHNDIVEKINQRLKEDNSLDL--------KDFQPGLTKFDDLQTQVNKIIESLENQVNSH 5643
Cdd:TIGR00618 261 LLKQLRARIEEL---RAQEAVLEETQERINRARKAAPLAAHikavtqieQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5644 EKYKQAYNELQDWLR---RTRIEVEQCADCHGEKDQVESRLNRLGDIQSSslegkalLEACEELSQavIATSGSEGQDNV 5720
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSqeiHIRDAHEVATSIREISCQQHTLTQHIHTLQQQ-------KTTLTQKLQ--SLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5721 AQEIKHLTSEWETLQTISRDARSSLESCLaAWQTFLQKFNKINLWIETMNKRVTKSQEGENKTPEDLVNAKKLLEEVLAE 5800
Cdd:TIGR00618 409 QATIDTRTSAFRDLQGQLAHAKKQQELQQ-RYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETR 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5801 KDNVEDLNDNCELLMEQSACTRIRDQTIETQANY-----TKLLTSAQGLVAKIEKNLSDH----TEFLNYKKEMDAWIEK 5871
Cdd:TIGR00618 488 KKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDnpgplTRRMQRGEQTYAQLETSEEDVyhqlTSERKQRASLKEQMQE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5872 AQQvlddcstdgDAAIIAQKldtVNSLASRLPEGQHLLALVQ---DAYSKASNITPEDKQEKLRELMTKVREDWDALGLA 5948
Cdd:TIGR00618 568 IQQ---------SFSILTQC---DNRSKEDIPNLQNITVRLQdltEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5949 VKQK-LSDLKQAQNRWNDFAANKDKLEKWLNETETTLKVAPETKGELSEMKTLLEryktlsnELKLKGNELEQLQSEARD 6027
Cdd:TIGR00618 636 QCSQeLALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKE-------QLTYWKEMLAQCQTLLRE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6028 LGTEVDAVNRLQsrcDKLKNDCSAHITALEQEMFDYNAYHQSLQDVEKWLLQisfqlmahnslfisnrEQTQEQIKQHEA 6107
Cdd:TIGR00618 709 LETHIEEYDREF---NEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK----------------ARTEAHFNNNEE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6108 LLVEIQKyQTNLDDLNAKGQAQIKRYESSTPAIRPTVESQLKNIQDSYNSLLQTSVQIKNRLLESLAKFQEYEDTLDSIM 6187
Cdd:TIGR00618 770 VTAALQT-GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEIT 848
|
730 740
....*....|....*....|....*
gi 320544548 6188 RNLETYEPIIQTELDAPATSLELAQ 6212
Cdd:TIGR00618 849 HQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
273-374 |
1.70e-03 |
|
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: 43.07 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 273 QKKTFTNWINSYL-----LKRVPPL--RIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFL--SNANTALQFL 343
Cdd:cd21324 25 EKYAFVNWINKALendpdCKHVIPMnpNTDDLFKAVGDGIVLCKMINFSVPDTIDERTINKKKLTPFTiqENLNLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 320544548 344 ASKRIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 135
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2712-2844 |
1.81e-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: 44.36 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2712 ESPQNLAELTSDAELLRKDMQALQDSFDQIKGILDENVDLWSQYEQSnEQISNWLRDVEGRVKAETSSQvNLSEVPQKLQ 2791
Cdd:cd00176 69 EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGK-DLESVEELLK 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 320544548 2792 ELSILQQDVLAHEPIINNLEQTSQQLIEKNPEAR---IGQFVTHLVQRYQAVSKAL 2844
Cdd:cd00176 147 KHKELEEELEAHEPRLKSLNELAEELLEEGHPDAdeeIEEKLEELNERWEELLELA 202
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
7199-8012 |
1.93e-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: 45.98 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7199 RLEYMQLVAKFNDwVHEAELRLQnSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLV---HKQIQEAADKIwsslnNYEQSE 7275
Cdd:pfam12128 240 RPEFTKLQQEFNT-LESAELRLS-HLHFGYKSDETLIASRQEERQETSAELNQLLrtlDDQWKEKRDEL-----NGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7276 LSAELAQFQtkltntlanaktqqSELEKEAERWREYQQS-IDRVKATIERTKFVDEPVQNLAGLHfniQKLSHAIGNVQs 7354
Cdd:pfam12128 313 ADAAVAKDR--------------SELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERL---KALTGKHQDVT- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7355 qnsdltlvnQQAQSLIRQADARNRQLIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHW----DGFENSLHAWEKAL-GR 7429
Cdd:pfam12128 375 ---------AKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELreqlEAGKLEFNEEEYRLkSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7430 LED-KFRNVDPTVRSrrhledtknaiqelrEESNQLKSSHKEIEALSKSIltflgevhkpsaEAIQAKVDKLVEQQAKLn 7508
Cdd:pfam12128 446 LGElKLRLNQATATP---------------ELLLQLENFDERIERAREEQ------------EAANAEVERLQSELRQA- 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7509 DTLRDKEqqvskdLEEIEQVFRRISQLQDKLNALHEQLqsvhvydehIAQTEQLLITLNSQVQQAAEE-----SKLLVAQ 7583
Cdd:pfam12128 498 RKRRDQA------SEALRQASRRLEERQSALDELELQL---------FPQAGTLLHFLRKEAPDWEQSigkviSPELLHR 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7584 TTAHYQAKQNQlPSDiAQEFTALELLAERVQV------TMETKEKDFKRAKTVRTEYvDGVDEVQRWLLQAEVQVQERSL 7657
Cdd:pfam12128 563 TDLDPEVWDGS-VGG-ELNLYGVKLDLKRIDVpewaasEEELRERLDKAEEALQSAR-EKQAAAEEQLVQANGELEKASR 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7658 TPTQMKELLQriNHEITAIyeRFTLVKTNGQLIIENCRnSEEKTLVQTTIDQLAASLAQV----RGWLDEKKqavGDSLD 7733
Cdd:pfam12128 640 EETFARTALK--NARLDLR--RLFDEKQSEKDKKNKAL-AERKDSANERLNSLEAQLKQLdkkhQAWLEEQK---EQKRE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7734 AWTRFMNLYQIVMSWASEKRNFIDQTIE-LRTLPEARNKL--NDYVTSVKSIKPIVKHLSEMDKELEHIgqVTTVGDLKD 7810
Cdd:pfam12128 712 ARTEKQAYWQVVEGALDAQLALLKAAIAaRRSGAKAELKAleTWYKRDLASLGVDPDVIAKLKREIRTL--ERKIERIAV 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7811 KLQEAEDAKISVEAVLLERNSLLQEACEEwdqCERKIKDIRSwhEKTKQGLDSSQQQKKpLRDQLGFCEKTLADINVQKT 7890
Cdd:pfam12128 790 RRQEVLRYFDWYQETWLQRRPRLATQLSN---IERAISELQQ--QLARLIADTKLRRAK-LEMERKASEKQQVRLSENLR 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7891 KLRLSIEKL--------------EVHFRNGMGGD-----PRLSENVDDLVRVLDGlgeLVKAKS--------QSLEQTLA 7943
Cdd:pfam12128 864 GLRCEMSKLatlkedanseqaqgSIGERLAQLEDlklkrDYLSESVKKYVEHFKN---VIADHSgsglaetwESLREEDH 940
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320544548 7944 QIDVYQQQMQSLRQrIIQEEQQLRLVMAPtylphDRERALAEQQDLITQELDELLQSLSSVEDGIANMN 8012
Cdd:pfam12128 941 YQNDKGIRLLDYRK-LVPYLEQWFDVRVP-----QSIMVLREQVSILGVDLTEFYDVLADFDRRIASFS 1003
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6603-7395 |
1.99e-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: 46.20 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6603 RQQKIKSLMKDAEAKQSLADV------LEKRVANMQQELEPVE-YSQLESALRNLNtenRNLSGV----LKAELDRALEA 6671
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLedilneLERQLKSLERQAEKAErYKELKAELRELE---LALLVLrleeLREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6672 SKARKSLENDLDKARQWLKTKISEVRKLpvYHPL-------------TSAEIEKKIQENRKYDDDAKQFNDS-VLTDVQR 6737
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLE--VSELeeeieelqkelyaLANEISRLEQQKQILRERLANLERQlEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6738 QAANIMKDCDDADKAALQQILDEIAADYQTLKDESSKRGKSLDDLLQGRKAFEDSMKNMGDWLNEMEtategelrtTSLP 6817
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE---------LQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6818 VLEEQLAHYKKLLSDAE-NKGGLINDVSEQGKSILPTlsnadklklndDIKNMKDRYGRIKNTIDDRVNALGDHIKKYKD 6896
Cdd:TIGR02168 397 SLNNEIERLEARLERLEdRRERLQQEIEELLKKLEEA-----------ELKELQAELEELEEELEELQEELERLEEALEE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6897 AKSRLAECSQflgNIQQKLRELNRpIGSRIEDVQDLLGAYEGI---LKELKDSKSKMGD--------MQMD--------- 6956
Cdd:TIGR02168 466 LREELEEAEQ---ALDAAERELAQ-LQARLDSLERLQENLEGFsegVKALLKNQSGLSGilgvlselISVDegyeaaiea 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6957 DLPE-LQSILAQQDDMIKLI----------------------EDQLAHLRQLLLLREQFIALINEIIAFIMKYTDVIID- 7012
Cdd:TIGR02168 542 ALGGrLQAVVVENLNAAKKAiaflkqnelgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYl 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7013 -----IENSPDSLEDKINKYD---------------------------------------------DVIVKIQECEGVLA 7042
Cdd:TIGR02168 622 lggvlVVDDLDNALELAKKLRpgyrivtldgdlvrpggvitggsaktnssilerrreieeleekieELEEKIAELEKALA 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7043 SANDKGQKIASEGNAADK--NSITEQLQSLKNQLQNLRKAVESQRQKHQLQLESHKKMAAELSEILDWLHSHEGAAKSrp 7120
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE-- 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7121 lLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEIGMPSSLLEMLsegRSLVASLPHELEEREKYLKNNRDSRL 7200
Cdd:TIGR02168 780 -AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL---ERRIAATERRLEDLEEQIEELSEDIE 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7201 EYMQLVAKFndWVHEAELRLQNSQHGIDYEHLVQDLDEHKIFFGN-EAPIRNLVHK------QIQEAADKIwSSLNNyEQ 7273
Cdd:TIGR02168 856 SLAAEIEEL--EELIEELESELEALLNERASLEEALALLRSELEElSEELRELESKrselrrELEELREKL-AQLEL-RL 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7274 SELSAELAQFQTKLTN----TLANAKTQQSELEKEAERWREyqqSIDRVKATIERTKFVdepvqNLAGLHfNIQKLSHAI 7349
Cdd:TIGR02168 932 EGLEVRIDNLQERLSEeyslTLEEAEALENKIEDDEEEARR---RLKRLENKIKELGPV-----NLAAIE-EYEELKERY 1002
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 320544548 7350 GNVQSQNSDLTLVNQQAQSLIRQADARNRQL----IEQDNAGLNRSWQDL 7395
Cdd:TIGR02168 1003 DFLTAQKEDLTEAKETLEEAIEEIDREARERfkdtFDQVNENFQRVFPKL 1052
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6511-6810 |
2.08e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6511 KIQELKGKAAQVAEVisnldgqqVEEQMKSLDRRFAD-LGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEELQa 6589
Cdd:PTZ00121 1419 KADEAKKKAEEKKKA--------DEAKKKAEEAKKADeAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK- 1489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6590 pkplgytpKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELEPVEYSQLESALRNLNtENRNLSGVLKAE-LDRA 6668
Cdd:PTZ00121 1490 --------KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE-EKKKADELKKAEeLKKA 1560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6669 LEASKARKSLENDLDK---------ARQWLKTKISEVRKLPVYHPLTSAEIEKKIQENRKYDDDAKQfNDSVLTDVQRQA 6739
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKnmalrkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLK 1639
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320544548 6740 ANIMKDCDDADKAALQQILDEIAADYQTLKDESSKRGKSlddllQGRKAFEDSMKNMGDWLNEMETATEGE 6810
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE-----EAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
7488-7601 |
2.12e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7488 PSAEAIQAKVDKLVEQ----------QAKLNDTLR--DKEQQVSKDLEE----IEQVFRRISQLQDKLNALHEQLQSVHV 7551
Cdd:PRK11281 36 PTEADVQAQLDALNKQklleaedklvQQDLEQTLAllDKIDRQKEETEQlkqqLAQAPAKLRQAQAELEALKDDNDEETR 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 320544548 7552 YD---EHIAQTEQLLITLNSQVQQA----AEESKLLVAQTTAHYQAkQNQLPSDIAQ 7601
Cdd:PRK11281 116 ETlstLSLRQLESRLAQTLDQLQNAqndlAEYNSQLVSLQTQPERA-QAALYANSQR 171
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
10861-11087 |
2.20e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.82 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10861 LDAMIQQLDQGEQQSKALQEQQQELarhcDD--ALATAMRMEQASIGQRISNLRAALKTwQGFLQRVTQLSESYEQRVNQ 10938
Cdd:PRK10929 50 LQSALNWLEERKGSLERAKQYQQVI----DNfpKLSAELRQQLNNERDEPRSVPPNMST-DALEQEILQVSSQLLEKSRQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10939 LQQEFGAAQKLLDANSEsLPTQPAA-------IEQLLGSL--------RAQRVQLGAQVSALESLtVTQEELKECISPHD 11003
Cdd:PRK10929 125 AQQEQDRAREISDSLSQ-LPQQQTEarrqlneIERRLQTLgtpntplaQAQLTALQAESAALKAL-VDELELAQLSANNR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11004 MKTIRQRNWLLWQQHADLDYQLANLINSIeerlsllsNYQiRYDRISQWLQRLEQRVEKDADVtamtnPEQAAKQLeqQV 11083
Cdd:PRK10929 203 QELARLRSELAKKRSQQLDAYLQALRNQL--------NSQ-RQREAERALESTELLAEQSGDL-----PKSIVAQF--KI 266
|
....
gi 320544548 11084 NSEL 11087
Cdd:PRK10929 267 NREL 270
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
10570-11331 |
2.23e-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: 45.98 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10570 LRDIVAKIAAD--VGLDASALMQGELDA------LGQRLAECKDAITTLANVAETQDKERKELDkevTLAKAYFNnvqqD 10641
Cdd:pfam12128 198 VKSMIVAILEDdgVVPPKSRLNRQQVEHwirdiqAIAGIMKIRPEFTKLQQEFNTLESAELRLS---HLHFGYKS----D 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10642 ISREAPQNpKESEEQLAALRAHLQTLartEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTfqeyhRLST 10721
Cdd:pfam12128 271 ETLIASRQ-EERQETSAELNQLLRTL---DDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDA-----DIET 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10722 RLARSQNsseaLRLWRQYLQHVQsflscaipedysslreqqqlcAIHQNLLISQQSVLSET-PLESELSEQYKALTNLHN 10800
Cdd:pfam12128 342 AAADQEQ----LPSWQSELENLE---------------------ERLKALTGKHQDVTAKYnRRRSKIKEQNNRDIAGIK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10801 ETLSRImqRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIhlKRVPHLKHRLDAMIQQLDQGEQQskalqE 10880
Cdd:pfam12128 397 DKLAKI--REARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLK--SRLGELKLRLNQATATPELLLQL-----E 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10881 QQQELARHCDDALaTAMRMEQASIGQRISNLRAALKTWQGFLQRVtqlsesyEQRVNQLQQEFGAAQKLLDANSES---- 10956
Cdd:pfam12128 468 NFDERIERAREEQ-EAANAEVERLQSELRQARKRRDQASEALRQA-------SRRLEERQSALDELELQLFPQAGTllhf 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10957 LPTQPAAIEQLLGSLRAQ----RVQL-----GAQVSALESLTVTQEELKECISP--HDM-KTIRQRNWLL-------WQQ 11017
Cdd:pfam12128 540 LRKEAPDWEQSIGKVISPellhRTDLdpevwDGSVGGELNLYGVKLDLKRIDVPewAASeEELRERLDKAeealqsaREK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11018 HADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQRL--EQRVEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKE-R 11094
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLfdEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKhQ 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11095 EWLLSTSRELLTLYSEpevrsqvqqqsdslidRWQRLKYLAKQKATKIGELKMTLLRLEERIAlirAWLFEVESQLDKPL 11174
Cdd:pfam12128 700 AWLEEQKEQKREARTE----------------KQAYWQVVEGALDAQLALLKAAIAARRSGAK---AELKALETWYKRDL 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11175 NFESYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLnlvemllndadSWRtqvntsglaasaQNLEQRWKNVCSQSAERKA 11254
Cdd:pfam12128 761 ASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVL-----------RYF------------DWYQETWLQRRPRLATQLS 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11255 RILT-IWNLLQQLIKLTAEHKNWLGKQESQIAGFERDQ----KSHSKHKLEERQM---ELRAKLEELE-SQSVNLRQLEQ 11325
Cdd:pfam12128 818 NIERaISELQQQLARLIADTKLRRAKLEMERKASEKQQvrlsENLRGLRCEMSKLatlKEDANSEQAQgSIGERLAQLED 897
|
....*.
gi 320544548 11326 IYAKLA 11331
Cdd:pfam12128 898 LKLKRD 903
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5626-6191 |
2.27e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5626 QTQVNKIIESLE------NQVNSHEKYKQAYNELQDWLRRTRIeveqcadchgEKDQVESRLNRLGDIQssslegKALLE 5699
Cdd:PRK03918 134 QGEIDAILESDEsrekvvRQILGLDDYENAYKNLGEVIKEIKR----------RIERLEKFIKRTENIE------ELIKE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5700 ACEELSQaviatsgsegqdnVAQEIKHLTSEwetlqtisrdaRSSLESCLAAWQTFLQKFNKINLWIETMNKRVTKSQEG 5779
Cdd:PRK03918 198 KEKELEE-------------VLREINEISSE-----------LPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5780 ENKTPEDLVNAKKLLEEVLAE----KDNVEDLNDNCELLMEQSACTRIRDQTIETQANYTKLLTSAQGLVAKIEKNLSDH 5855
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEieelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5856 TEFLNYKKEMDAWIEKAQQVLDDCSTDgdaaiiAQKLDTVNSLASRLpegqhllalvQDAYSKASNITPEDKQEKLRELM 5935
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEER------HELYEEAKAKKEEL----------ERLKKRLTGLTPEKLEKELEELE 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5936 TKVREDWDALgLAVKQKLSDLKQAQNRwndfaankdkLEKWLNETETTLKVAPETKGELSE--MKTLLERY----KTLSN 6009
Cdd:PRK03918 398 KAKEEIEEEI-SKITARIGELKKEIKE----------LKKAIEELKKAKGKCPVCGRELTEehRKELLEEYtaelKRIEK 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6010 ELKLKGNELEQLQSEARdlgtEVDAVNRLQSRCDKLKnDCSAHITALEQEMFDYNA--YHQSLQDVEKwLLQISFQLMAH 6087
Cdd:PRK03918 467 ELKEIEEKERKLRKELR----ELEKVLKKESELIKLK-ELAEQLKELEEKLKKYNLeeLEKKAEEYEK-LKEKLIKLKGE 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6088 NSLFISNREQTQEQIKQHEALLVEIQKYQTNLDDLNakgqaqiKRYESSTPAIRPTVESQLKNIQDSYNSLLqTSVQIKN 6167
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEELAELL-------KELEELGFESVEELEERLKELEPFYNEYL-ELKDAEK 612
|
570 580
....*....|....*....|....
gi 320544548 6168 RLLESLAKFQEYEDTLDSIMRNLE 6191
Cdd:PRK03918 613 ELEREEKELKKLEEELDKAFEELA 636
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4460-4560 |
2.30e-03 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 41.54 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4460 QHWSEYEQLRDQCLAWIRDTDNNLHAIDLKEDLPKKRAQLDALKALQGDVRAKELEVDNVTEKAQTLLkgpsSNRASGPE 4539
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI----DEGHYASE 76
|
90 100
....*....|....*....|.
gi 320544548 4540 LVTKyqqifhKVKELNNRWQQ 4560
Cdd:pfam00435 77 EIQE------RLEELNERWEQ 91
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3952-4136 |
2.45e-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: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3952 DYSGNKAALQARLQKINEIQDALPEGVAKLKSLEDHIEQQASNIPARSKEVMARdLANLHADFEKFGASLSDVKSGLENR 4031
Cdd:cd00176 27 DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER-LEELNQRWEELRELAEERRQRLEEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4032 LQQWNDYEiNLDRLITWLGEAENSLKNYNLKSSFEEKEEQLNGFQSLAQNLRQNEADFDKVKDDTSELVQSS---GETRI 4108
Cdd:cd00176 106 LDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGhpdADEEI 184
|
170 180
....*....|....*....|....*...
gi 320544548 4109 AVNVQQVSSRFQSIQATAKEILKKCEQA 4136
Cdd:cd00176 185 EEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5418-6024 |
2.54e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5418 LAKEVMRRLEMHYQEHQQHHSLYEECQSWIEKTREKLSECEQIPGTLNEVQIKLNTVKNLRQGFETGQNKLRYLLELKEK 5497
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5498 VIMNTEQNGA--AKIQEDTEALKQdFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDVEPSVKTSDEFLNDLSE 5575
Cdd:PRK03918 274 EIEELEEKVKelKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5576 KRAALEKFRVIQRDINGHNDIVEKINQRLKEDNSLDLKDfqpgltKFDDLQTQVNKIIESLENQVNSHEKYKQAYNELQD 5655
Cdd:PRK03918 353 RLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK------ELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5656 WLRRTRIEVEQCADC------HGEKDQVESRLNRLGDIQSSSLEGKALLEAC----EELSQAVIATSGSEGQDNVAQEIK 5725
Cdd:PRK03918 427 AIEELKKAKGKCPVCgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLrkelRELEKVLKKESELIKLKELAEQLK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5726 HLTSEWE--TLQTISRDARSslesclaaWQTFLQKFNKINLWIETMNKRVTKSQEGENKTpEDLVNAKKLLEEVLAE-KD 5802
Cdd:PRK03918 507 ELEEKLKkyNLEELEKKAEE--------YEKLKEKLIKLKGEIKSLKKELEKLEELKKKL-AELEKKLDELEEELAElLK 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5803 NVEDLNDNCELLMEQsactRIRDqtietqanytklltsaqglvakIEKNLSDHTEFLNYKKEmdawIEKAQQVLDDCSTD 5882
Cdd:PRK03918 578 ELEELGFESVEELEE----RLKE----------------------LEPFYNEYLELKDAEKE----LEREEKELKKLEEE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5883 GDAAI--IAQKLDTVNSLASRLPEgqhllalVQDAYSkasnitpEDKQEKLRELMTKVREdwdalglAVKQKLSDLKQAQ 5960
Cdd:PRK03918 628 LDKAFeeLAETEKRLEELRKELEE-------LEKKYS-------EEEYEELREEYLELSR-------ELAGLRAELEELE 686
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320544548 5961 NRWNDFAANKDKLEKWLNETETTLKVAPETKGELSEMKTLLERYKTLSNELKLKG-NELEQLQSE 6024
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERAlSKVGEIASE 751
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
6753-7578 |
2.63e-03 |
|
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: 45.81 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6753 ALQQILDEIAadyqtlkdESSKRGKSLDDLLQGRKAFEDSMKNMGDWLNEMETATEGELRT-TSLPVLEEQLAHYKKLLS 6831
Cdd:TIGR00606 170 ALKQKFDEIF--------SATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIrDQITSKEAQLESSREIVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6832 DAENKgglINDVSEQGKSILPTLSNAdkLKLNDDIKNMKDRYGRIKNT--------------IDDRVNAL-GDHIKKYKD 6896
Cdd:TIGR00606 242 SYENE---LDPLKNRLKEIEHNLSKI--MKLDNEIKALKSRKKQMEKDnselelkmekvfqgTDEQLNDLyHNHQRTVRE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6897 AKSRLAECSQFLGNIQQKLRELNRPiGSRIEDVQDLLGA-----YEGILKELKDSKSKMGDMQMDDLPELQSILAQQDDM 6971
Cdd:TIGR00606 317 KERELVDCQRELEKLNKERRLLNQE-KTELLVEQGRLQLqadrhQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNF 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 6972 IKLI----EDQLAHLRQLLLLREQFIALINEIIAFI-MKYTDVIIDIENSPDSLEDKINKYDDVIVKIQECEGVLASAND 7046
Cdd:TIGR00606 396 HTLVierqEDEAKTAAQLCADLQSKERLKQEQADEIrDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7047 KGQ---KIASEGNAADKNSITEQLQSLKNQLQNlrkavesqrqkHQLQLESHKKMAAELSEILDwlhSHEGAAKSRPLLD 7123
Cdd:TIGR00606 476 LDQelrKAERELSKAEKNSLTETLKKEVKSLQN-----------EKADLDRKLRKLDQEMEQLN---HHTTTRTQMEMLT 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7124 RDPESVERELQKHQSL-SQDIESYLNKFNKINDGVKTEigmpSSLLEMLSEGRSLVASLPHELE--EREKYLKNNRDSRL 7200
Cdd:TIGR00606 542 KDKMDKDEQIRKIKSRhSDELTSLLGYFPNKKQLEDWL----HSKSKEINQTRDRLAKLNKELAslEQNKNHINNELESK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7201 EYMQLvaKFNDWVHEAelrLQNSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLVHKQIQEAADKIWSSLNNYEQS-ELSAE 7279
Cdd:TIGR00606 618 EEQLS--SYEDKLFDV---CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVfQTEAE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7280 LAQFQTKLTNTLANAKTQQSELEKEAERwREYQQSIDRVKATIeRTKFVDEPVQNLAGLHFNIQKLSHAIgnvQSQNSDL 7359
Cdd:TIGR00606 693 LQEFISDLQSKLRLAPDKLKSTESELKK-KEKRRDEMLGLAPG-RQSIIDLKEKEIPELRNKLQKVNRDI---QRLKNDI 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7360 TLVNQQAQSLIRQADARNrqlIEQDNAGLNRSWQDLVRSLEQRrdnLQQLAEHWDGFENSLhAWEKALGRLEDKFRNVDP 7439
Cdd:TIGR00606 768 EEQETLLGTIMPEEESAK---VCLTDVTIMERFQMELKDVERK---IAQQAAKLQGSDLDR-TVQQVNQEKQEKQHELDT 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7440 TVRS----RRHLEDTKNAIQELREESNQLKSSHKEI-------EALSKSILTFLGEVHKPSAEAIQAKVDKLVEQQAKlN 7508
Cdd:TIGR00606 841 VVSKielnRKLIQDQQEQIQHLKSKTNELKSEKLQIgtnlqrrQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFL-E 919
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320544548 7509 DTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVHVY-----DEHIAQTEQLLITLNSQVQQAAEESK 7578
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgkDDYLKQKETELNTVNAQLEECEKHQE 994
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
7425-7576 |
2.75e-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: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7425 KALGRLEDKFRNVdptvrsRRHLEDTKNAIQELREESNQLKSSHKEIEALSKSILTFLGEVHKP-SAEAIQAKVDKLVEQ 7503
Cdd:COG1579 31 AELAELEDELAAL------EARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkEYEALQKEIESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320544548 7504 QAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLqsvhvyDEHIAQTEQLLITLNSQVQQAAEE 7576
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL------DEELAELEAELEELEAEREELAAK 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7798-8217 |
2.81e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7798 HIGQVTTVGDLKDKLQEAEDAKISVEAVLLErnslLQEACEEWDQCERKIKDIRSWHEKTKQgldssQQQKKPLRDQLGF 7877
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEE----LEELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7878 CEKTLADINVQKTKLRLSIEKLEVHFRNGmggdPRLSENVDDLVRVLDGLGELVK-AKSQSLEQTLAQIDVYQQQMQSLR 7956
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEEL----EELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7957 QRIIQEEQQLRLVMAPTYLPHDRERALAEQQDLitQELDELLQSLSSVEdGIANMNQSSLDGMLHGLKLIQSNLEV---- 8032
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERL--KEARLLLLIAAALL-ALLGLGGSLLSLILTIAGVLFLVLGLlall 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 8033 ---HERDAIELKNQAKKLPTDPATERL----LNDTVDRIDLLLRRTQQGITMIANAMHGQKKRQQEIDEYQQHLLeleqw 8105
Cdd:COG4717 290 fllLAREKASLGKEAEELQALPALEELeeeeLEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ----- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 8106 IIEVSAELASFEPTSDSSTDEQVLK--SQVERSQQLLRTLKDRQQSMEDLVEQTRQLQSHPDVSPLADTLmEQLQSIITI 8183
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEEL-EELEEELEE 443
|
410 420 430
....*....|....*....|....*....|....
gi 320544548 8184 LREQVTVATKRIFTIEKRIVDLRKAKSEEAQRQR 8217
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELLQE 477
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3828-3913 |
2.97e-03 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 41.54 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3828 NWLDQVEKLIHNENPASwtSAQEIRSKLYKYKATNQDINSHKRIVEAVNEKAAALLGSAAPAnADEISKAVAEVNKRYDQ 3907
Cdd:pfam00435 15 SWIEEKEALLSSEDYGK--DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYA-SEEIQERLEELNERWEQ 91
|
....*.
gi 320544548 3908 VGQDCA 3913
Cdd:pfam00435 92 LLELAA 97
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10294-10916 |
3.37e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10294 LRDQLQAIQEGISNQRKHQAKISVILDECEAAERQGADVLEKAVADCQAAGEELVISWQEIMRirqmlhtlpmrlkmsvs 10373
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR----------------- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10374 pvkLERDISQLQDDHAFLESKctniMAILRSRLAVWlryERQLELVHGSVQETDfmmelirvhgqvdyERLRKATERLEG 10453
Cdd:COG1196 300 ---LEQDIARLEERRRELEER----LEELEEELAEL---EEELEELEEELEELE--------------EELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10454 LAGDLHNREQLIDELKGAAKPLIEScdvqiVEQIESAVQEAVVAWNDTSENLQQLRTRYQRAVELWDKYRNASAAVKNSI 10533
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEE-----LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10534 DQQMDAVKSLEQPLDALQHAKVCQDNLTTQNDRIL-----ELRDIVAKIAADVGLDASALMQGELDALGQRLAECKDAIT 10608
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLaelleEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10609 TLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPKESEEQLAALRAHLQTL---ARTEEQLRQLKERHQNSE 10685
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagRATFLPLDKIRARAALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10686 VAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEALRlwrqylqhvqsflscaipedysslreqqqlc 10765
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA------------------------------- 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10766 aihQNLLISQQSVLSETPLESELSEQYKALTNLHNETLSRIMQRNGELERRVSgwnayRQQLAALLDWLRQREAERNALQ 10845
Cdd:COG1196 640 ---VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA-----EEELELEEALLAEEEEERELAE 711
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320544548 10846 LRyihlKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHcDDALATAMRMEQASIGQRISNLRAALK 10916
Cdd:COG1196 712 AE----EERLEEELEEEALEEQLEAEREELLEELLEEEELLEE-EALEELPEPPDLEELERELERLEREIE 777
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
10442-10687 |
3.52e-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: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10442 ERLRKATERLEGLAGDLHNREQLIDELKGAAKPLIESCDV-QIVEQIEsAVQEAVVAWNDTSENLQQLRTRYQRAVELWD 10520
Cdd:COG4913 624 EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVaSAEREIA-ELEAELERLDASSDDLAALEEQLEELEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10521 KYRNAsaavknsIDQQMDAVKSLEQPLDALQhakvcqdnlttqnDRILELRDIVAKIAADVGLDASALMQGELDALGQRL 10600
Cdd:COG4913 703 ELEEE-------LDELKGEIGRLEKELEQAE-------------EELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10601 AEcKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPkESEEQLAALRAHLQT--LARTEEQLRQLK 10678
Cdd:COG4913 763 VE-RELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADL-ESLPEYLALLDRLEEdgLPEYEERFKELL 840
|
....*....
gi 320544548 10679 ERHQNSEVA 10687
Cdd:COG4913 841 NENSIEFVA 849
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1253-1444 |
3.80e-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: 43.20 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 1253 FYQSLKDVEKELQLEQQALNRNEDVDSILQRNQQF----LLQQDVVPRLERcLQNMQRLAQAHRQQQPGDIS-LDQAYDN 1327
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLkkheALEAELAAHEER-VEALNELGEQLIEEGHPDAEeIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 1328 AKSQWQLLSNKLGDMRQTLQQIPAQWQgYHLKFNDMVDWMNGVDQSLKNIVNeVNTMEEFEKEKVVFQKICQDADNKRED 1407
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEAHEPR 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 320544548 1408 MKWLVKTLDSLLSYATEDEANLEQKKLEDLIARYKNL 1444
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEEL 198
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4252-4347 |
3.92e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.78 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4252 FDEIADSLKSWLDETENALpADIELKTTLDEKRNKLQTYRDILNDINNHQVELGNLQEIAANL----PEKTELVDQIIKD 4327
Cdd:smart00150 3 FLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieegHPDAEEIEERLEE 81
|
90 100
....*....|....*....|
gi 320544548 4328 ISDRFGKLQKRAQNYVERYE 4347
Cdd:smart00150 82 LNERWEELKELAEERRQKLE 101
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
10801-11100 |
3.92e-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: 44.94 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10801 ETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALqLRYIHLKRVPHLKHRLDAMIQQLDQgeqqskaLQE 10880
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKL-LPQANLLADETLADRLEELREELDA-------AQE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10881 QQQELARHcddalatamrmeqasiGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQefgaAQKLLDANSEslptq 10960
Cdd:COG3096 908 AQAFIQQH----------------GKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRR----LKQQIFALSE----- 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10961 paaieqllgsLRAQRVQLGAQVSAlESLTVTQ---EELKECISphDMKTIRQRNWLLWQQHADlDYQLANlinsiEERLS 11037
Cdd:COG3096 963 ----------VVQRRPHFSYEDAV-GLLGENSdlnEKLRARLE--QAEEARREAREQLRQAQA-QYSQYN-----QVLAS 1023
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320544548 11038 LLSNYQIRYdrisQWLQRLEQRVEkDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWLLST 11100
Cdd:COG3096 1024 LKSSRDAKQ----QTLQELEQELE-ELGVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQ 1081
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2209-3597 |
4.13e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.04 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2209 KDKFHALEHNFGQALQE------NRAKLDEILRQHPTLNNIDQIIADLVALNDALK-YQAD---------------LKNR 2266
Cdd:TIGR01612 458 KSKLKALEKRFFEIFEEewgsydIKKDIDENSKQDNTVKLILMRMKDFKDIIDFMElYKPDevpskniigfdidqnIKAK 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2267 IHDEGSLLMREDIASMPAIQESLLIMDK-----NYDS--LQNEIADRIQKY----------NLISQALREYADSKDKFSK 2329
Cdd:TIGR01612 538 LYKEIEAGLKESYELAKNWKKLIHEIKKeleeeNEDSihLEKEIKDLFDKYleiddeiiyiNKLKLELKEKIKNISDKNE 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2330 ELKKAEDLYNAIPQQPRDETEL-----HQASE--KTRKTMEQLRKSKLSldelERRGNNVGKLFSAIGEpIPQEVPQEVT 2402
Cdd:TIGR01612 618 YIKKAIDLKKIIENNNAYIDELakispYQVPEhlKNKDKIYSTIKSELS----KIYEDDIDALYNELSS-IVKENAIDNT 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2403 AAKQHWQDLH---DKTAKNAHVYETEAVI--WSQIEDAKKDLLPWLSETNQGLCDAADNSIEiefgpmrlskyrTELPSY 2477
Cdd:TIGR01612 693 EDKAKLDDLKskiDKEYDKIQNMETATVElhLSNIENKKNELLDIIVEIKKHIHGEINKDLN------------KILEDF 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2478 QALKDSIVEKTNDLVKINkgaeipalSALNKLLSeQFAEVNNNADRLSAITTSFNDQEQELRRRSKEAGERVSKLREQLI 2557
Cdd:TIGR01612 761 KNKEKELSNKINDYAKEK--------DELNKYKS-KISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIF 831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2558 KC--------DDMSGDNNKIMERLQQCRalrgELDNSGNE-----IDNIKQKV-DELRNLYPTF---SESIIPKELNNVQ 2620
Cdd:TIGR01612 832 KIinemkfmkDDFLNKVDKFINFENNCK----EKIDSEHEqfaelTNKIKAEIsDDKLNDYEKKfndSKSLINEINKSIE 907
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2621 KRYENVDLYAK-----KIESSLLQFLKKFHaDKVGMLKRIIATQREKVAWCQ--PESSSDKYN--LDVKKSSLQEVSK-- 2689
Cdd:TIGR01612 908 EEYQNINTLKKvdeyiKICENTKESIEKFH-NKQNILKEILNKNIDTIKESNliEKSYKDKFDntLIDKINELDKAFKda 986
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2690 SIDDCKARHAETLKSLEMLKA---VESPQNLAELTSDAELLRKDMQalQDSFDQIKGILDENVDLWSQYEQSNEQISNWL 2766
Cdd:TIGR01612 987 SLNDYEAKNNELIKYFNDLKAnlgKNKENMLYHQFDEKEKATNDIE--QKIEDANKNIPNIEIAIHTSIYNIIDEIEKEI 1064
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2767 -RDVEGR----VKAETSSQVNLSEVPQKLQELSIlqQDVLAHEpiinNLEQTSQQLIEKNPEARIGQFVTHLVQRYQAVS 2841
Cdd:TIGR01612 1065 gKNIELLnkeiLEEAEINITNFNEIKEKLKHYNF--DDFGKEE----NIKYADEINKIKDDIKNLDQKIDHHIKALEEIK 1138
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2842 KALTSYIDKIRgAQLSNANFAKAAKDFNEwfgdakiefqelarmgSPGSSSATAQQLQT---VKNYIktFDNGQILLNNA 2918
Cdd:TIGR01612 1139 KKSENYIDEIK-AQINDLEDVADKAISND----------------DPEEIEKKIENIVTkidKKKNI--YDEIKKLLNEI 1199
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2919 VDIgealypvvspdnrERIRADLRQMRE-KFDYLRDEANAFMQQVEGvliQKTSIEESYTQVSHY---LNESKAKVPTTD 2994
Cdd:TIGR01612 1200 AEI-------------EKDKTSLEEVKGiNLSYGKNLGKLFLEKIDE---EKKKSEHMIKAMEAYiedLDEIKEKSPEIE 1263
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2995 ELYPTLATKKAALQ-------NYKTQLQEITLHKNALKQLHDKAVTLCDDESERKTDESIQEynTLSKKISDrittvgnh 3067
Cdd:TIGR01612 1264 NEMGIEMDIKAEMEtfnishdDDKDHHIISKKHDENISDIREKSLKIIEDFSEESDINDIKK--ELQKNLLD-------- 1333
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3068 VVKHEA-YDQVLEKAQDWLNTIK----SEAIDILNETTFEKE----GAEEKLLVVENLLQhKPEGDSIFDTCHKLLETVL 3138
Cdd:TIGR01612 1334 AQKHNSdINLYLNEIANIYNILKlnkiKKIIDEVKEYTKEIEennkNIKDELDKSEKLIK-KIKDDINLEECKSKIESTL 1412
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3139 TQTHPSGhpallkgfeepkqswedfmtlCQDSLVKLKQ-LCSKWDEFDTIIEELDNWMKNVEAVVKNQNLkstAEAKNAH 3217
Cdd:TIGR01612 1413 DDKDIDE---------------------CIKKIKELKNhILSEESNIDTYFKNADENNENVLLLFKNIEM---ADNKSQH 1468
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3218 LKQLQ--DISKDIERRGAAINELMDQGREIEGETDLNLKLSRLNTR-YQTLKNLCKESIAKYVNYV---------KDHES 3285
Cdd:TIGR01612 1469 ILKIKkdNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKElFEQYKKDVTELLNKYSALAiknkfaktkKDSEI 1548
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3286 FDKDFDSFKQN--LQSSVDElAKTNEIVGDQSVLQDQQNKlREMSDKRILDStlfeglidrgeklygHTSPEGREIIRQQ 3363
Cdd:TIGR01612 1549 IIKEIKDAHKKfiLEAEKSE-QKIKEIKKEKFRIEDDAAK-NDKSNKAAIDI---------------QLSLENFENKFLK 1611
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3364 LRALRTlwdnYTDDLNSATQKIDQcllQFNEFSI-AQDQLTKWLKDVDKAMQSHTEP----KTTLQEKRAQLQNhkllhq 3438
Cdd:TIGR01612 1612 ISDIKK----KINDCLKETESIEK---KISSFSIdSQDTELKENGDNLNSLQEFLESlkdqKKNIEDKKKELDE------ 1678
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3439 eitthnvlVDNVCDKAQILVDQIKDNslnvYLTSIKQLFQSIVQKSDEILHNLDDCVQkhNELNNALSSAKT-----WIS 3513
Cdd:TIGR01612 1679 --------LDSEIEKIEIDVDQHKKN----YEIGIIEKIKEIAIANKEEIESIKELIE--PTIENLISSFNTndlegIDP 1744
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 3514 NEKaklleCDDAYGEKADIKRKIETLGQLAQNkpqAMKIISDIRDLFEKVKATTSEKGNEVLdkEIEELETTMKSHFDDI 3593
Cdd:TIGR01612 1745 NEK-----LEEYNTEIGDIYEEFIELYNIIAG---CLETVSKEPITYDEIKNTRINAQNEFL--KIIEIEKKSKSYLDDI 1814
|
....
gi 320544548 3594 EGIE 3597
Cdd:TIGR01612 1815 EAKE 1818
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
10440-10872 |
4.18e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10440 DYERLRKATERLEGLAGDLHNREQLIDELKGAAKpLIESCDVQIVEQIESAVQEAVVAWNDTSENLQQLRTRYQRAVELW 10519
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEE-ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10520 DKYRNASAAVKNSIDQQMDAVKSLEQPLDALQHAKVCQDNLTTqndrILELRDIVAKIAADVGLDASALMQGELDALGQR 10599
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL----LLIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10600 LAECKDAITTLANVAETQDKER-KELDKEVTLAKAYFNNVQQDISREAPQNPKESEE---QLAALRAHLQTLARTEEQLR 10675
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEElQALPALEELEEEELEELLAALGLPPDLSPEELLElldRIEELQELLREAEELEEELQ 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10676 QLKERHQNSEVAPSVASSDDDGILEVLALWQKiFQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQhvqsflscaIPEDY 10755
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEE---------LEEEL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10756 SSLREQQQLcaihqnllisqqsvlsetpLESELSEQYKALTNLHNETlsRIMQRNGELERRvsgwnayRQQLAALLDWLR 10835
Cdd:COG4717 435 EELEEELEE-------------------LEEELEELREELAELEAEL--EQLEEDGELAEL-------LQELEELKAELR 486
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 320544548 10836 QREAERNALQL---------RYIHLKRVPHLKHRLDAMIQQLDQGE 10872
Cdd:COG4717 487 ELAEEWAALKLalelleearEEYREERLPPVLERASEYFSRLTDGR 532
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10835-11557 |
4.31e-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: 45.05 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10835 RQREAERNaLQLRYIHLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELaRHCDDALAT-----------AMRMEQAS 10903
Cdd:TIGR02168 173 RRKETERK-LERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAEL-RELELALLVlrleelreeleELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10904 IGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKLLDAnsesLPTQPAAIEQLLGSLRAQRVQLGAQVS 10983
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR----LEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10984 ALESltvTQEELKEcisphDMKTIRQRNWLLWQQHADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQRLEQRVekd 11063
Cdd:TIGR02168 327 ELES---KLDELAE-----ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI--- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11064 advtamtnpEQAAKQLEQQVnSELQLRDKEREWLLSTSRELLTLYSEPEVRsQVQQQSDSLIdrwQRLKYLAKQKATKIG 11143
Cdd:TIGR02168 396 ---------ASLNNEIERLE-ARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELE---EELEELQEELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11144 ELKmtllRLEERIALIRAWLFEVESQLDKpLNFESYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDADSWR 11223
Cdd:TIGR02168 462 ALE----ELREELEEAEQALDAAERELAQ-LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11224 TQVNTSgLAASAQ-----NLEQRWKNVCSQSAERKARILTIWNLLQQLIKLTAEHKNWLGKQEsqiaGFERDQKSHSKHK 11298
Cdd:TIGR02168 537 AAIEAA-LGGRLQavvveNLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIE----GFLGVAKDLVKFD 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11299 LEERQ------------------MELRAKLEELESqSVNLrQLEQIYAKLAMSAGVEPENIQKLTLPTKVmvsmwRQLTP 11360
Cdd:TIGR02168 612 PKLRKalsyllggvlvvddldnaLELAKKLRPGYR-IVTL-DGDLVRPGGVITGGSAKTNSSILERRREI-----EELEE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11361 RCHALLDAIdkdaklmREFNNAQLEATNSLNAIQKALEQLPSAENQQTSK-AEPKAVLQRLESLEKKLQDAQQhvQQADN 11439
Cdd:TIGR02168 685 KIEELEEKI-------AELEKALAELRKELEELEEELEQLRKELEELSRQiSALRKDLARLEAEVEQLEERIA--QLSKE 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11440 LAQEAKTRTKQQPQLKQLLELVSAYTTLWQTVQTRIVTLKTTWLT-----RAAQAAASLPVSEAANAAVQVNTLSQRKLR 11514
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealDELRAELTLLNEEAANLRERLESLERRIAA 835
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 320544548 11515 QAQQMQRETSITAKDAYIME-LQTAITECQNNLDELQRTVVDKT 11557
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIEsLAAEIEELEELIEELESELEALL 879
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2538-2873 |
4.50e-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: 44.66 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2538 LRRRSKEAGERVSKLREQLIKCDDMSGDNNKIMERLQ-------QCRALRGELDN-----SGNEIDNIKQKVDELRNLYP 2605
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLErqaekaeRYKELKAELRElelalLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2606 TFSESI--IPKELNNVQKRYENVDLYAKKIESSLLQFLKKFHA--DKVGMLKRIIATQREKVAWCQPESSSDKYNLDVKK 2681
Cdd:TIGR02168 250 EAEEELeeLTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaNEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2682 SSLQEVSKSIDDCKARHAETLKSLEMLKA--VESPQNLAELTSDAELLRKDMQALQDSFDQIKGILDEN----VDLWSQY 2755
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLnneiERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2756 EQSNEQISNWLRDVEGRVKAETSSQvnLSEVPQKLQELSILQQDVLAHEPIINNLEQTSQQLIEKNPEARigQFVTHLVQ 2835
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL--DAAERELA 485
|
330 340 350
....*....|....*....|....*....|....*...
gi 320544548 2836 RYQAVSKALTSYIDKIRGAQLSNANFAKAAKDFNEWFG 2873
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILG 523
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2512-2810 |
5.14e-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: 44.67 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2512 EQFAEVNNNADRLSAITTSFNDQEQELRRRSKEAGERVSKLREqlikCDDMSGDNNKIMERL-QQCRALRGELDNSGNEI 2590
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD----ASRKIGEIEKEIEQLeQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2591 DNIKQKVDELRNLYPTFSESIIPKELNNVQKRYENVDLYAKKIESSL------LQFLKKFHADKVGMLKRIIA-----TQ 2659
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpeiqaeLSKLEEEVSRIEARLREIEQklnrlTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 2660 REKVAwcQPESSSDKYNLDVKKSSLQEVSKSIDDCKARHAETLKSLEMLKAVESP--QNLAELTSDAELLRKDMQALQDS 2737
Cdd:TIGR02169 827 EKEYL--EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDleSRLGDLKKERDELEAQLRELERK 904
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320544548 2738 FDQIKGILDENVDLWSQYEQSNEQISNWLRDVEGRVKAETSSQVNLSEVPQKLQELSILQQDVLAHEPiINNL 2810
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEP-VNML 976
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4780-4992 |
5.19e-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: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4780 DHRLFKEAYDDLVSWIGRAREKFPSlkQSSLSDKLAIENAVQATEALLNKQAQGELLVEHLVHTGEvVLASTSAQGQEII 4859
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGE-QLIEEGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4860 RNDIRALRDSFEGLFREINQQKENLEVTMVQWRAYKEEYErLMEWLQQIDILVKNHKlnLCPNLPEKEKQVADMKEVMSR 4939
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 320544548 4940 LEKGKDDIDKFNASAASLLKSH---LDTYVNNQLRHLSSVYQVQVNLAKDVLKKVE 4992
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGhpdADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
10761-11058 |
5.26e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10761 QQQLCAIHQNLLISQQSVLSETPLESELseqykaltnlhnETLSRIMQRNGELErrvsgwnAYRQQLAALLDWLRQREAE 10840
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQTL------------ALLDKIDRQKEETE-------QLKQQLAQAPAKLRQAQAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10841 RNALQLryihlKRVPHLKHRLDAM-IQQL-DQGEQQSKALQEQQQELARHCDDALATAMRME--QASIG---QRISNLRA 10913
Cdd:PRK11281 103 LEALKD-----DNDEETRETLSTLsLRQLeSRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPEraQAALYansQRLQQIRN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10914 ALKTwqgflQRVTQLSESYEQRvNQLQQEfgaaQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALES------ 10987
Cdd:PRK11281 178 LLKG-----GKVGGKALRPSQR-VLLQAE----QALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHqlqllq 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320544548 10988 -------LTVTQEELKECISPHDMKTIrQRNWLLwQQHADLDYQLAN-LINSIeERLSLLSNYQIrydRISQWLQRLEQ 11058
Cdd:PRK11281 248 eainskrLTLSEKTVQEAQSQDEAARI-QANPLV-AQELEINLQLSQrLLKAT-EKLNTLTQQNL---RVKNWLDRLTQ 320
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7388-7607 |
5.45e-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: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7388 LNRSWQDLVRsLEQRRDNLQQLAEHWDgfenslhAWEKALGRLE--DKFRNVDPTVRSRRHLEDTKNAIQELREESNQLK 7465
Cdd:COG4913 237 LERAHEALED-AREQIELLEPIRELAE-------RYAAARERLAelEYLRAALRLWFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7466 sshKEIEALSKSIltflgevhkpsaEAIQAKVDKLVEQQAKL-NDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHE 7544
Cdd:COG4913 309 ---AELERLEARL------------DALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320544548 7545 QL-QSVHVYDEHIAQTEQLLITLNSQVQQAAEEsklLVAQTTAHYQAKQNQlpSDIAQEFTALE 7607
Cdd:COG4913 374 PLpASAEEFAALRAEAAALLEALEEELEALEEA---LAEAEAALRDLRREL--RELEAEIASLE 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
10771-11035 |
5.48e-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: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10771 LLISQQSVLSETPLESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLryih 10850
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10851 lkrvphlkhRLDAMIQQLDQGEQQskaLQEQQQELARHcddaLATAMRMEQASIGQRISNLRAALKtwqgfLQRVTQLSE 10930
Cdd:COG4942 84 ---------ELAELEKEIAELRAE---LEAQKEELAEL----LRALYRLGRQPPLALLLSPEDFLD-----AVRRLQYLK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10931 SYEQRVNQLQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLtvtQEELKEcisphDMKTIRQR 11010
Cdd:COG4942 143 YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEK-----ELAELAAE 214
|
250 260
....*....|....*....|....*
gi 320544548 11011 NWLLWQQHADLDYQLANLINSIEER 11035
Cdd:COG4942 215 LAELQQEAEELEALIARLEAEAAAA 239
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
5088-5870 |
5.51e-03 |
|
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: 44.65 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5088 RLVKKMSTAKVQLETNLLQwaDYSSSYSQLQQWITDREAklQQACEQKIVKSKRGQpglssgLSERKANLRQTNNIVQDI 5167
Cdd:TIGR00606 195 RQTQGQKVQEHQMELKYLK--QYKEKACEIRDQITSKEA--QLESSREIVKSYENE------LDPLKNRLKEIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5168 VSFEPMIQSVTSKAsvLQQGAPGTEISDK----YENLTKQAKDLYEKQKNTIESY-QSLIDAGNEFATWLRNAKERLSKC 5242
Cdd:TIGR00606 265 MKLDNEIKALKSRK--KQMEKDNSELELKmekvFQGTDEQLNDLYHNHQRTVREKeRELVDCQRELEKLNKERRLLNQEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5243 SE---PTGDKQALAEKTH----------QLKILQGEL------PEGAQKLKNALE---QGEIACRSAEPEDCEIIEQEVA 5300
Cdd:TIGR00606 343 TEllvEQGRLQLQADRHQehirardsliQSLATRLELdgfergPFSERQIKNFHTlviERQEDEAKTAAQLCADLQSKER 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5301 LLQEEFDAYREALNKAKDYLEVGIVKWSDYQDQYTEALEWLSKTEALVQSYNKLQDSLIQKKVVLEQFQGHLQTLFDWQK 5380
Cdd:TIGR00606 423 LKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5381 TLDDLNMKAQVLLETCSDTRISNAIMQLTTKYNALLTLAKEVMRRLEMHYQEHQQHHSLYEECQSWIEKTREKLSECEQI 5460
Cdd:TIGR00606 503 VKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5461 PGTLNEVQIKLNTVKNLRQGFETGQNKLRYLLELKEKVIMNTEQN-----GAAKIQEDTEALKQDFDKLLVDLNDVRQKL 5535
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcGSQDEESDLERLKEEIEKSSKQRAMLAGAT 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5536 ANRLAQLEE--------------IFKLYKILIEWLEDVEPSVKTSDEFLNDLSEKRAALEKFR------------VIQRD 5589
Cdd:TIGR00606 663 AVYSQFITQltdenqsccpvcqrVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRdemlglapgrqsIIDLK 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5590 INGHNDIVEKIN------QRLK---EDNSLDLKDFQPGLTKFDDLQTQVNkIIESLENQVNSHE-KYKQAYNELQDW-LR 5658
Cdd:TIGR00606 743 EKEIPELRNKLQkvnrdiQRLKndiEEQETLLGTIMPEEESAKVCLTDVT-IMERFQMELKDVErKIAQQAAKLQGSdLD 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5659 RTRIEVEQcadchgekdQVESRLNRLGDIQSSSLEGKALLEACEELSQAVIATSGSEGQDNV------------AQEIKH 5726
Cdd:TIGR00606 822 RTVQQVNQ---------EKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLqigtnlqrrqqfEEQLVE 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5727 LTSEWETLQTISRDARSSlescLAAWQTFLQKFnkinlwiETMNKRVTKSQEGENKTPEDLVN--AKKLLEEVLAEKDNV 5804
Cdd:TIGR00606 893 LSTEVQSLIREIKDAKEQ----DSPLETFLEKD-------QQEKEELISSKETSNKKAQDKVNdiKEKVKNIHGYMKDIE 961
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320544548 5805 EDLNDNCEllmeqsactrirDQTIETQANYTKL---LTSAQGLVAKIEKNLSDHTEFLNYKKEMDAWIE 5870
Cdd:TIGR00606 962 NKIQDGKD------------DYLKQKETELNTVnaqLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQ 1018
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
10579-10985 |
6.27e-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: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10579 ADVGLDASALMQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDIsreapqnpkESEEQLA 10658
Cdd:COG3096 280 RRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTAL---------RQQEKIE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10659 ALRAHLQTLA-RTEEQLRQLKERHqnsevapsvassdddgilEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEAL-RLW 10736
Cdd:COG3096 351 RYQEDLEELTeRLEEQEEVVEEAA------------------EQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqTRA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10737 RQYLQHVQSflscaipedyssLREQQQLCAI----------HQNLLISQQSVLSETPLESE--LSEQyKALTNLHNETLS 10804
Cdd:COG3096 413 IQYQQAVQA------------LEKARALCGLpdltpenaedYLAAFRAKEQQATEEVLELEqkLSVA-DAARRQFEKAYE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10805 RIMQRNGELERRvSGWNAYRQQLAallDWLRQR-EAER-NALQLRYIHLKRVPHLKHRLDAMIQQLDQGEQQS------- 10875
Cdd:COG3096 480 LVCKIAGEVERS-QAWQTARELLR---RYRSQQaLAQRlQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQldaaeel 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10876 KALQEQQQELARHCDDALATA------MRMEQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKL 10949
Cdd:COG3096 556 EELLAELEAQLEELEEQAAEAveqrseLRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQL 635
|
410 420 430
....*....|....*....|....*....|....*.
gi 320544548 10950 LDANSEslptqpaaIEQLLGSLRAQRVQLGAQVSAL 10985
Cdd:COG3096 636 LERERE--------ATVERDELAARKQALESQIERL 663
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
10820-11010 |
6.40e-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: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10820 WNAYRQQLAALLDWLRQREAERNALQLRyIHLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDAlATAMRM 10899
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10900 EQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQrVNQLQQEFGAAQKLLdaNSESLPTQPAAIEQLLGSLRAQRVQLG 10979
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAAL--ASEDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190
....*....|....*....|....*....|.
gi 320544548 10980 AQVSALESLTVTQEELKECISPHDMKTIRQR 11010
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEK 187
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
7800-8013 |
7.80e-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: 43.60 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7800 GQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEACEEWDQCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQLgfcE 7879
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI---A 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7880 KTLADINVQKTKLRlsiEKLEVHFRNGMGGDPRL---SENVDDLVRVLDGLGELV----------KAKSQSLEQTLAQID 7946
Cdd:COG4942 94 ELRAELEAQKEELA---ELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAparreqaeelRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 7947 VYQQQMQSLRQRIIQEEQQLRLVMAptylphDRERALAE---QQDLITQELDELLQSLSSVEDGIANMNQ 8013
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA------ERQKLLARlekELAELAAELAELQQEAEELEALIARLEA 234
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
11104-11349 |
9.27e-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: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11104 LLTLYSEPEVRSQVQQQSDSLIDRWQRLKYLAKQKATKIGELKMTLLRLEERIALIRAWLFEVESQLdkplnfesytpNV 11183
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL-----------AA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11184 IEAKL----KEHEQIQRSIEHHSSNVGEVL---------NLVEMLLNDADSWRTQVNTSGLAASAQNLEQRWKNVCSQSA 11250
Cdd:COG4942 81 LEAELaeleKEIAELRAELEAQKEELAELLralyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 11251 ERKARILTIWNLLQQLIKLTAEHKNWLGKQESQIAgfERDQKShskHKLEERQMELRAKLEELESQSVNLRQL------E 11324
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKA--ERQKLL---ARLEKELAELAAELAELQQEAEELEALiarleaE 235
|
250 260
....*....|....*....|....*
gi 320544548 11325 QIYAKLAMSAGVEPENIQKLTLPTK 11349
Cdd:COG4942 236 AAAAAERTPAAGFAALKGKLPWPVS 260
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5488-6047 |
9.30e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5488 LRYLLELKEKVIMNTEQngaakIQEDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDVEPSVKtsd 5567
Cdd:PRK03918 174 IKRRIERLEKFIKRTEN-----IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEK--- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5568 EFLNDLSEKRAALEKFRVIQRDINGHNDIVEKINQRLKEDNSLD------------LKDFQPGLTKFDDLQTQVNKIIES 5635
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekaeeyiklsefYEEYLDELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5636 LENQVNSHEKYKQAYNELQDWLRRTRIEVEQCADCHGEKDQVESRLNRLGDIqSSSLEGKALLEACEELSQAviatsgSE 5715
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERL-KKRLTGLTPEKLEKELEEL------EK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5716 GQDNVAQEIKHLTSEWETLQTISRDARSSLESCLAAWQ---------TFLQKFNKINLWIETMNKRVTKSQEGENKTpED 5786
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKE-RK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5787 LVNAKKLLEEVLAEKDNVEDLNDNCELLME-QSACTRIRDQTIETQAN-YTKLLTSAQGLVAKIEKNLSDHTEFLNYKKE 5864
Cdd:PRK03918 478 LRKELRELEKVLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKAEeYEKLKEKLIKLKGEIKSLKKELEKLEELKKK 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5865 MDAwIEKAQQVLDDCSTDGDAAIIAQKLDTVNSLASRLPEgqhlLALVQDAYSKASNITPE-----DKQEKLRELMTKVR 5939
Cdd:PRK03918 558 LAE-LEKKLDELEEELAELLKELEELGFESVEELEERLKE----LEPFYNEYLELKDAEKElereeKELKKLEEELDKAF 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5940 EDWDALGLAVKQKLSDLKQAQNRWNDfaankdklEKWLNETETTLKVAPETKGELSEMKTLLERYKTLSNELKLKGNELE 6019
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYSE--------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
570 580 590
....*....|....*....|....*....|.
gi 320544548 6020 QLQS---EARDLGTEVDAVNRLQSRCDKLKN 6047
Cdd:PRK03918 705 EREKakkELEKLEKALERVEELREKVKKYKA 735
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
10485-10891 |
9.41e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.64 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10485 EQIESAVQEAVVAWNDTSENLQQLRTRYqravelwdKYRNASAAVKNSIDQQMDAVKSLEQPLDALQHAKVCQDNLTTQN 10564
Cdd:PRK10246 443 AQLQVAIQNVTQEQTQRNAALNEMRQRY--------KEKTQQLADVKTICEQEARIKDLEAQRAQLQAGQPCPLCGSTSH 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10565 DRI-----LEL------RDIVAKIAADVGlDASALMQGELDALGQRLAECKDAITTLANVAETQDKERKEL--DKEVTLa 10631
Cdd:PRK10246 515 PAVeayqaLEPgvnqsrLDALEKEVKKLG-EEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVcaSLNITL- 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10632 kayfnNVQQDISrEAPQNPKESEEQL----------AALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGilev 10701
Cdd:PRK10246 593 -----QPQDDIQ-PWLDAQEEHERQLrllsqrhelqGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDE---- 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10702 LALWQKIFQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLC-AIHQNLLISQQSVLS 10780
Cdd:PRK10246 663 EASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQClSLHSQLQTLQQQDVL 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 10781 ETPLESELSEQYK-ALTN-------------LHNETLSRIMQRNGELERRvsgwnayRQQLAALLDWLRQREAERNALQL 10846
Cdd:PRK10246 743 EAQRLQKAQAQFDtALQAsvfddqqaflaalLDEETLTQLEQLKQNLENQ-------RQQAQTLVTQTAQALAQHQQHRP 815
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320544548 10847 RYIHLK-RVPHLKHRLDAMIQQL-----DQGE------------QQSKALQEQQQELARHCDD 10891
Cdd:PRK10246 816 DGLDLTvTVEQIQQELAQLAQQLrenttRQGEirqqlkqdadnrQQQQALMQQIAQATQQVED 878
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4868-5166 |
9.73e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4868 DSFEGLFREINQQKENLEVTmvqwRAYKEEYERLMEWLQQIDILVKNHKLN-LCPNLPEKEKQVADMKEVMSRLEKGKDD 4946
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKEKEaLERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 4947 IDKFNASAASLLKShldtyVNNQLRHLSSVYQVQVNLA-KDVLKKVETNRDQHREYDANMKSAKDWIANAKATIQS---- 5021
Cdd:TIGR02169 263 LEKRLEEIEQLLEE-----LNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKllae 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544548 5022 AGEGAGSKEALQRRLEQIQDLIRNRELGQNLVHTAINNGEKIIRNTR---SDGR---DAINTEMKELQTEWDRLVKKMST 5095
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRdelKDYReklEKLKREINELKRELDRLQEELQR 417
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320544548 5096 AKVQLETNLLQWADYSSSYSQLQQWITDREAKLQQAcEQKIvksKRGQPGLSSgLSERKANLRQTNNIVQD 5166
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ-EWKL---EQLAADLSK-YEQELYDLKEEYDRVEK 483
|
|
| |
