|
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 |
2.33e-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: 2.33e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 268 EQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKR 347
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|...
gi 442626147 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 |
3.78e-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: 3.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 415 KWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAK 494
Cdd:cd21243 1 KFKGGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPR 80
|
90 100
....*....|....*....|....*....
gi 442626147 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 |
3.00e-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: 3.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 268 EQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKR 347
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|...
gi 442626147 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 |
2.39e-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: 2.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 270 ERVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASKRIK 349
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKA--RRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRM--RFHRLQNVQTALDFLKYRKIK 76
|
90 100
....*....|....*....|....*....
gi 442626147 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 |
2.87e-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: 2.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 268 EQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGrvLRRPHFLSNANTALQFLASKR 347
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKG--HNVFQCRSNIETALSFLKNKS 78
|
90 100 110
....*....|....*....|....*....|...
gi 442626147 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 |
2.47e-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: 2.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 262 ILQLQEEQERVQKKTFTNWINSYLlKRVPpLRIDDLINDLRDGTKLIALLEVLSGERLP-VEKGRVlrRPHFLSNANTAL 340
Cdd:cd21246 6 IKALADEREAVQKKTFTKWVNSHL-ARVG-CRINDLYTDLRDGRMLIKLLEVLSGERLPkPTKGKM--RIHCLENVDKAL 81
|
90 100 110
....*....|....*....|....*....|....*
gi 442626147 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 |
2.89e-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: 2.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 261 TILQLQEEQERVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLP-VEKGRVlrRPHFLSNANTA 339
Cdd:cd21193 5 RIRALQEERINIQKKTFTKWINSFLEKA--NLEIGDLFTDLSDGKLLLKLLEIISGEKLGkPNRGRL--RVQKIENVNKA 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 442626147 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 |
3.59e-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: 3.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 417 KQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLL 496
Cdd:cd21192 1 QGSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLL 80
|
90 100
....*....|....*....|....*..
gi 442626147 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 |
4.23e-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: 4.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 272 VQKKTFTNWINSYLLKRVPPLrIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASKRIKLV 351
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKPP-IKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRM--RVHHLNNVNRALQVLEQNNVKLV 78
|
90 100
....*....|....*....|....*...
gi 442626147 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 |
9.83e-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: 9.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 415 KWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAK 494
Cdd:cd21244 1 RWKMSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPR 80
|
90 100
....*....|....*....|....*
gi 442626147 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 |
1.06e-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: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21189 2 AKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDPE 81
|
90 100
....*....|....*....|....
gi 442626147 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 |
1.54e-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: 1.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 258 YQMTILQLQEEQERVQKKTFTNWINSYLLKRVPplRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNAN 337
Cdd:cd21236 3 YENVLERYKDERDKVQKKTFTKWINQHLMKVRK--HVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRM--RFHRLQNVQ 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 442626147 338 TALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTIILYFQIEE 381
Cdd:cd21236 79 IALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISD 122
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
264-546 |
1.24e-32 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 138.92 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 264 QLQEEQERVQKKTFTNWINSYLLKRVPPlRIDDLINDLRDGTKLIALLEVLSGERLpVEKGRVLR-RPHFLSNANTALQF 342
Cdd:COG5069 1 MEAKKWQKVQKKTFTKWTNEKLISGGQK-EFGDLDTDLKDGVKLAQLLEALQKDNA-GEYNETPEtRIHVMENVSGRLEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 343 LASKRIKLVNINPADLVDGRPPVVLGLIWTIILYFQIEENSRNLEYLGHgiggsvSSLDSVGNQKHGDLKAEkwkqgark 422
Cdd:COG5069 79 IKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGELTKH------INLLLWCDEDTGGYKPE-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 423 tllnwvtnalpkdsgVEVKDFGASWRDGVAFLALI-----DAIKANLVNLAELKKTSNRQRletAFDVAESKLGIAKLLD 497
Cdd:COG5069 145 ---------------VDTFDFFRSWRDGLAFSALIhdsrpDTLDPNVLDLQKKNKALNNFQ---AFENANKVIGIARLIG 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 442626147 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 |
1.97e-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: 1.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21194 3 AKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDAE 82
|
90 100
....*....|....*....|...
gi 442626147 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 |
3.35e-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: 3.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 270 ERVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLP-VEKGRVlrRPHFLSNANTALQFLASKRI 348
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKA--GTQIENIEEDFRDGLKLMLLLEVISGERLPkPERGKM--RFHKIANVNKALDFIASKGV 78
|
90 100
....*....|....*....|....*..
gi 442626147 349 KLVNINPADLVDGRPPVVLGLIWTIIL 375
Cdd:cd21214 79 KLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
267-379 |
2.95e-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: 2.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 267 EEQERVQKKTFTNWINSYLLKrvPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASK 346
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLRHR 76
|
90 100 110
....*....|....*....|....*....|...
gi 442626147 347 RIKLVNINPADLVDGRPPVVLGLIWTIILYFQI 379
Cdd:cd21235 77 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 109
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
420-523 |
3.02e-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: 3.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKdSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21245 4 AIKALLNWVQRRTRK-YGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPE 82
|
90 100
....*....|....*....|....
gi 442626147 500 DVDVPKPDEKSIMTYVAQFLHKYP 523
Cdd:cd21245 83 DVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
262-375 |
4.85e-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: 4.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 262 ILQLQEEQERVQKKTFTNWINSYLLKrvPPLRIDDLINDLRDGTKLIALLEVLSGERLPV-EKGRVlrRPHFLSNANTAL 340
Cdd:cd21318 28 IKALADEREAVQKKTFTKWVNSHLAR--VPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRM--RIHSLENVDKAL 103
|
90 100 110
....*....|....*....|....*....|....*
gi 442626147 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 |
1.86e-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: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 262 ILQLQEEQERVQKKTFTNWINSYLlKRVPpLRIDDLINDLRDGTKLIALLEVLSGERLPV-EKGRVlrRPHFLSNANTAL 340
Cdd:cd21317 21 IKALADEREAVQKKTFTKWVNSHL-ARVT-CRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRM--RIHCLENVDKAL 96
|
90 100 110
....*....|....*....|....*....|....*
gi 442626147 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 |
3.39e-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: 3.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 268 EQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKR 347
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 442626147 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 |
4.12e-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: 4.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 267 EEQERVQKKTFTNWINSYLLKRVPplRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASK 346
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRK--HINDLYEDLRDGHNLISLLEVLSGVKLPREKGRM--RFHRLQNVQIALDFLKQR 76
|
90 100 110
....*....|....*....|....*....|....*
gi 442626147 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 |
1.59e-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: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21248 3 AKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDPE 82
|
90 100
....*....|....*....|.
gi 442626147 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 442626147 268 EQERVQKKTFTNWINSYLLK-RVPPlrIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASK 346
Cdd:cd21231 2 EREDVQKKTFTKWINAQFAKfGKPP--IEDLFTDLQDGRRLLELLEGLTGQKLVKEKGST--RVHALNNVNKALQVLQKN 77
|
90 100 110
....*....|....*....|....*....|....
gi 442626147 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 |
1.31e-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: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 270 ERVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLpvekGRVLRRP----HFLSNANTALQFLAS 345
Cdd:cd21215 2 VDVQKKTFTKWLNTKLSSR--GLSITDLVTDLSDGVRLIQLLEIIGDESL----GRYNKNPkmrvQKLENVNKALEFIKS 75
|
90 100 110
....*....|....*....|....*....|..
gi 442626147 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 |
2.94e-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: 2.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 417 KQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLL 496
Cdd:cd21249 2 LRSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLL 81
|
90 100
....*....|....*....|....
gi 442626147 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 |
3.72e-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: 3.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 262 ILQLQEEQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPV-EKGRVlrRPHFLSNANTAL 340
Cdd:cd21247 10 IRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKM--RVHFLENNSKAI 87
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 442626147 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 |
4.13e-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: 4.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 422 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDV 501
Cdd:cd21187 3 KTLLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDV 82
|
90 100
....*....|....*....|..
gi 442626147 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 |
6.50e-27 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 109.37 E-value: 6.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21216 11 AKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKMLDAE 90
|
90 100
....*....|....*....|....
gi 442626147 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 |
1.47e-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: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21291 11 AKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGIPQLLDVE 90
|
90 100
....*....|....*....|....
gi 442626147 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 |
1.38e-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: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 418 QGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLD 497
Cdd:cd21319 4 RSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLD 83
|
90 100
....*....|....*....|....*....
gi 442626147 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 |
1.77e-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: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 272 VQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKRIKLV 351
Cdd:cd21227 4 IQKNTFTNWVNEQL--KPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIKLV 81
|
90 100
....*....|....*....|....*...
gi 442626147 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 ... |
11861-11917 |
2.87e-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: 2.87e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 442626147 11861 FLGRVARASLPIQALMLLLLGVATLVPHG-EDYTCMFSNTFARSLEPMLSYPHGPPPT 11917
Cdd:pfam10541 1 FLGRVLRAALPLQLLLLLLLLLACLLPAGeEDYSCTLANNFARSFHPMLRYVNGPPPT 58
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
272-380 |
1.49e-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: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 272 VQKKTFTNWINSYLLKRVPPlRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASKRIKLV 351
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKP-PIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGST--RVHALNNVNRVLQVLHQNNVELV 78
|
90 100
....*....|....*....|....*....
gi 442626147 352 NINPADLVDGRPPVVLGLIWTIILYFQIE 380
Cdd:cd21232 79 NIGGTDIVDGNHKLTLGLLWSIILHWQVK 107
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
271-377 |
1.53e-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: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 271 RVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLpveKGRVLRRP----HFLSNANTALQFLASK 346
Cdd:cd21183 3 RIQANTFTRWCNEHLKER--GMQIHDLATDFSDGLCLIALLENLSTRPL---KRSYNRRPafqqHYLENVSTALKFIEAD 77
|
90 100 110
....*....|....*....|....*....|.
gi 442626147 347 RIKLVNINPADLVDGRPPVVLGLIWTIILYF 377
Cdd:cd21183 78 HIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
415-527 |
2.88e-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: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 415 KWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAK 494
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100 110
....*....|....*....|....*....|...
gi 442626147 495 LLDAEDVDVPKPDEKSIMTYVAQFLHKYPEPKG 527
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKMKA 113
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
262-375 |
2.94e-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: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 262 ILQLQEEQERVQKKTFTNWINSYLLKrvPPLRIDDLINDLRDGTKLIALLEVLSGERLPV-EKGRVlrRPHFLSNANTAL 340
Cdd:cd21316 43 IKALADEREAVQKKTFTKWVNSHLAR--VSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRM--RIHCLENVDKAL 118
|
90 100 110
....*....|....*....|....*....|....*
gi 442626147 341 QFLASKRIKLVNINPADLVDGRPPVVLGLIWTIIL 375
Cdd:cd21316 119 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
270-379 |
7.76e-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: 7.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 270 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLAS-KRI 348
Cdd:cd21311 13 KRIQQNTFTRWANEHL--KTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEEdEGI 90
|
90 100 110
....*....|....*....|....*....|.
gi 442626147 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 |
2.54e-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: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAEsKLGIAKLLDAE 499
Cdd:cd21239 2 AKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAE-KLGVTRLLDPE 80
|
90 100
....*....|....*....|....
gi 442626147 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 |
4.23e-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: 4.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGIAKLLDAE 499
Cdd:cd21240 5 AKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAE 83
|
90 100
....*....|....*....|....
gi 442626147 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 |
1.47e-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: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 419 GARKTLLNWVTNALPKDSgveVKDFGASWRDGVAFLALIDAIKANL-VNLAELKKTSNRQRLETAFDVAESKLGIAKLLD 497
Cdd:cd21184 1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLiPDNESLDKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|...
gi 442626147 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 |
3.18e-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: 3.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 422 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDV 501
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 442626147 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 |
7.76e-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: 7.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21238 3 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 82
|
90 100
....*....|....*....|....
gi 442626147 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 |
6.66e-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: 6.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 270 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVE-KGRVLRRPHFLSNANTALQFLASKRI 348
Cdd:cd21228 2 KKIQQNTFTRWCNEHL--KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKyNKRPTFRQMKLENVSVALEFLERESI 79
|
90 100
....*....|....*....|....*....
gi 442626147 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 |
8.12e-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: 8.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKD-SGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKT--SNRQRLETAFDVAESKLGIAK-L 495
Cdd:pfam00307 3 LEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVPKvL 82
|
90 100
....*....|....*....|....*...
gi 442626147 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 |
9.96e-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: 9.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 272 VQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKgRVLRRPHFLSNANTALQFLASK-RIKL 350
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK-LNKSEFDKLENINLALDVAEKKlGVPK 80
|
90 100
....*....|....*....|....*....
gi 442626147 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 |
2.16e-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: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 437 GVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAED-VDVPKPDEKSIMTYV 515
Cdd:cd21253 19 DVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVALKVPDKLSILTYV 98
|
....*..
gi 442626147 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 |
2.99e-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: 2.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 418 QGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLD 497
Cdd:cd21322 16 RSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHLGLTKLLD 95
|
90 100 110
....*....|....*....|....*....|
gi 442626147 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 |
1.15e-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: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 418 QGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLD 497
Cdd:cd21320 1 KSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 80
|
90 100
....*....|....*....|....*
gi 442626147 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 |
9.00e-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: 9.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21289 11 AKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAE 90
|
90 100
....*....|....*....|....
gi 442626147 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 |
1.10e-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: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21287 11 AKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDAE 90
|
90 100
....*....|....*....|....
gi 442626147 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 |
1.60e-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: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21234 1 SEKILLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPE 80
|
90 100
....*....|....*....|....
gi 442626147 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 |
1.62e-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: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAE 80
|
90 100
....*....|....*....|....
gi 442626147 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 |
1.88e-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: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 270 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLpveKGRVLRRPHF----LSNANTALQFLAS 345
Cdd:cd21310 14 KKIQQNTFTRWCNEHL--KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKM---YRKYHPRPNFrqmkLENVSVALEFLDR 88
|
90 100 110
....*....|....*....|....*....|....
gi 442626147 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 |
2.54e-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: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 273 QKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPvekgRVLRRP----HFLSNANTALQFLASKRI 348
Cdd:cd21212 1 EIEIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVP----GIHSRPktraQKLENIQACLQFLAALGV 76
|
90 100
....*....|....*....|....*....
gi 442626147 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 |
1.95e-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: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNL-AELKKTSNRQRLETAFDVAESKLGIAKLLDA 498
Cdd:cd21233 1 SEKILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWnSVVSQQSATERLDHAFNIARQHLGIEKLLDP 80
|
90 100
....*....|....*....|....*.
gi 442626147 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 |
6.26e-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: 6.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 422 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTS---NRQRletAFDVAESKLGIAKLLDA 498
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENiaeNNQL---AFDVAEQELGIPPVMTG 79
|
90 100
....*....|....*....|.
gi 442626147 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 442626147 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|....*..
gi 442626147 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 |
1.28e-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: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21290 14 AKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAE 93
|
90 100
....*....|....*....|....
gi 442626147 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 |
2.42e-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: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 424 LLNWVTNALPKDSgveVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQR-LETAFDVAESKLGIAKLLDAEDVD 502
Cdd:cd21230 6 LLGWIQNKIPQLP---ITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDALEnATEAMQLAEDWLGVPQLITPEEII 82
|
90
....*....|....*.
gi 442626147 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 |
4.59e-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: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 499
Cdd:cd21288 11 AKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAE 90
|
90 100
....*....|....*....|....
gi 442626147 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 442626147 422 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNR----QRLETAFDVAESKLGIAKLLD 497
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 442626147 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 |
1.22e-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: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 270 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLpveKGRVLRRPHF----LSNANTALQFLAS 345
Cdd:cd21309 15 KKIQQNTFTRWCNEHL--KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRM---YRKYHQRPTFrqmqLENVSVALEFLDR 89
|
90 100 110
....*....|....*....|....*....|....
gi 442626147 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 |
2.76e-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: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 274 KKTFTNWINSyLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLAS-KRIKLVN 352
Cdd:cd00014 1 EEELLKWINE-VLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKlGLPELDL 79
|
90 100
....*....|....*....|....
gi 442626147 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 |
4.87e-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: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 270 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLpveKGRVLRRPHF----LSNANTALQFLAS 345
Cdd:cd21308 18 KKIQQNTFTRWCNEHL--KCVSKRIANLQTDLSDGLRLIALLEVLSQKKM---HRKHNQRPTFrqmqLENVSVALEFLDR 92
|
90 100 110
....*....|....*....|....*....|....
gi 442626147 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 |
5.14e-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: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 270 ERVQKKTFTNWINSYLLKRVPPlRIDDLINDLRDGTKLIALLEVLSGERLPVE-----KGRVLRrphfLSNANTALQFLA 344
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGIP-KISDLATDLSDGVRLIFFLELVSGKKFPKKfdlepKNRIQM----IQNLHLAMLFIE 76
|
90 100 110
....*....|....*....|....*....|
gi 442626147 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 |
6.09e-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: 6.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 419 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDA 498
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|....*
gi 442626147 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 |
1.51e-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: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 275 KTFTNWINSYLLKRVPPlRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRP-HFLSNANTALQFLASKRIKLVNI 353
Cdd:smart00033 1 KTLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfKKIENINLALSFAEKLGGKVVLF 79
|
90 100
....*....|....*....|...
gi 442626147 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 |
1.78e-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: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 273 QKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLP----VEKGRVLRRphflSNANTALQFLASKRI 348
Cdd:cd21213 1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPgidwNPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 442626147 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 |
1.73e-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: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 422 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAEsKLGIAKLLDAED- 500
Cdd:cd21198 4 QDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAA-KLGIPRLLDPADm 82
|
90
....*....|....*..
gi 442626147 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 |
3.78e-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: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 419 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGIAKLLDA 498
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|
gi 442626147 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 |
8.61e-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: 8.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 421 RKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGIAKLLDAED 500
Cdd:cd21199 10 RNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAES-VGIPTTLTIDE 88
|
90 100
....*....|....*....|....*
gi 442626147 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 |
9.30e-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: 9.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 421 RKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLvnLAELKKTSNRQRLET---AFDVAESKLGIAKLLD 497
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGL--CPNWRKLDPSNSLENcrrAMDLAKREFNIPMVLS 79
|
90 100
....*....|....*....|....
gi 442626147 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 442626147 419 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDA 498
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80
|
90 100
....*....|....*....|.
gi 442626147 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 |
4.75e-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: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5962 RWNDFAANKDKLEKWLNETETTLKvAPETKGELSEMKTLLERYKTLSNELKLKGNELEQLQSEARDLGTE--------VD 6033
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEghpdaeeiQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6034 AVNRLQSRCDKLKNDCSAHITALEQEMfDYNAYHQSLQDVEKWLLQISFQLMAHNslFISNREQTQEQIKQHEALLVEIQ 6113
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 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 |
1.67e-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: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 421 RKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSN---RQRLETAFDVAES-KLGIAKLL 496
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 442626147 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 |
1.75e-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: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 420 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAeSKLGIAKLLDAE 499
Cdd:cd21254 2 ASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGF-ASLGISRLLEPS 80
|
90
....*....|....*....
gi 442626147 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 |
6.41e-11 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 66.32 E-value: 6.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5326 KWSDYQDQYTEALEWLSKTEALVQSYNKLQDsLIQKKVVLEQFQGHLQTLFDWQKTLDDLNMKAQVLLETCSD--TRISN 5403
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPdaEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5404 AIMQLTTKYNALLTLAKEVMRRLEMHYQEHQQHHSLYEECQsWIEKTREKLSEcEQIPGTLNEVQIKLNTVKNLRQGFET 5483
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQ-WLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442626147 5484 GQNKLRYLLELKEKVIMNTEQNGAAKIQEDTEALKQDFDKLLVDLNDVRQKLANRL 5539
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
419-527 |
7.55e-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: 7.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 419 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDA 498
Cdd:cd21260 1 GVKNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEV 80
|
90 100 110
....*....|....*....|....*....|
gi 442626147 499 ED-VDVPKPDEKSIMTYVaQFLHKYPEPKG 527
Cdd:cd21260 81 EDmVRMSVPDSKCVYTYI-QELYRSLVQKG 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7215-7928 |
8.74e-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: 70.09 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7215 QTKLTNTLANAKTQQSELEKE--AERWREYQQSIDRVKATIERT-KFVDEPVQNLAGLHFNIQKLSHAIGNVQSQNSDLT 7291
Cdd:TIGR02168 208 QAEKAERYKELKAELRELELAllVLRLEELREELEELQEELKEAeEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7292 LVNQQAQSLI-------RQADARNRQLiEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDK 7364
Cdd:TIGR02168 288 KELYALANEIsrleqqkQILRERLANL-ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7365 FRNvdptvrSRRHLEDTKNAIQELREESNQLKsshKEIEALSKSIltflgEVHKPSAEAIQAKVDKLVEQQAKLNDTLrd 7444
Cdd:TIGR02168 367 LEE------LESRLEELEEQLETLRSKVAQLE---LQIASLNNEI-----ERLEARLERLEDRRERLQQEIEELLKKL-- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7445 KEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVhvyDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAHYQ---- 7520
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEEL---REELEEAEQALDAAERELAQLQARLDSLERLQENLEGfseg 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7521 -----AKQNQLPSDIAQ-----EF-----TALEL-LAERVQ-VTMETKEkdfkraktvrtEYVDGVD-----EVQRWLLQ 7578
Cdd:TIGR02168 508 vkallKNQSGLSGILGVlseliSVdegyeAAIEAaLGGRLQaVVVENLN-----------AAKKAIAflkqnELGRVTFL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7579 AEVQVQERSLTPTQMKEL------------------------------------LQRINHEITAIYERFTLVKTNGQLI- 7621
Cdd:TIGR02168 577 PLDSIKGTEIQGNDREILkniegflgvakdlvkfdpklrkalsyllggvlvvddLDNALELAKKLRPGYRIVTLDGDLVr 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7622 ----------------------IENCRnsEEKTLVQTTIDQLAASLAQVRGWLDEKKQAVGDSLDAWTRFmnlyQIVMSW 7679
Cdd:TIGR02168 657 pggvitggsaktnssilerrreIEELE--EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL----SRQISA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7680 ASEKRNFIDQTIELRTLPEARNKLndyvTSVKSIKPIVKHLSEMDKELEHIGQV-TTVGDLKDKLQEAEDAKISVEAVLL 7758
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSK----ELTELEAEIEELEERLEEAEEELAEAeAEIEELEAQIEQLKEELKALREALD 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7759 ERNSLLQEACEEWDQCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQLGFCEKTLADINVQKTKLRLSIEKLEVHFRNGM 7838
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7839 GGDPRLSENVDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRL-------VMAPTYLPHDRE 7911
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeysltleEAEALENKIEDD 966
|
810
....*....|....*...
gi 442626147 7912 RALAEQQ-DLITQELDEL 7928
Cdd:TIGR02168 967 EEEARRRlKRLENKIKEL 984
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
424-518 |
1.13e-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: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 424 LLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDV-D 502
Cdd:cd21195 9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEMaS 88
|
90
....*....|....*.
gi 442626147 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 |
1.25e-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: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 425 LNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGIAKLLDAEDVDVP 504
Cdd:cd21185 7 LRWVRQLLPD---VDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADP 82
|
90
....*....|....*.
gi 442626147 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 |
1.92e-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: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2588 NEIDNI--KQKVDELRNLYPTFSESIIPKELNNVQKRYENVDLYAKKIESSLLQFLKKFHADKVGMLKRIIATQREKvaw 2665
Cdd:TIGR01612 687 NAIDNTedKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILEDFKNK--- 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2666 cQPESSSD-----KYN--LDVKKSSLQEVSK------SIDDCKARHAET--LKSLEMLKAVESPQN-LAELTSDAELLRK 2729
Cdd:TIGR01612 764 -EKELSNKindyaKEKdeLNKYKSKISEIKNhyndqiNIDNIKDEDAKQnyDKSKEYIKTISIKEDeIFKIINEMKFMKD 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2730 DMQALQDSFDQIKGILDENVDlwSQYEQSNEQISnwlrdvegRVKAETSSQvnlsevpqklqELSILQQDVLAHEPIINN 2809
Cdd:TIGR01612 843 DFLNKVDKFINFENNCKEKID--SEHEQFAELTN--------KIKAEISDD-----------KLNDYEKKFNDSKSLINE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2810 LEQTsqqlIEKNPearigQFVTHL--VQRYQAVSKALTSYIDKIRGAQ-------------LSNAN-FAKAAKD-FNEWF 2872
Cdd:TIGR01612 902 INKS----IEEEY-----QNINTLkkVDEYIKICENTKESIEKFHNKQnilkeilnknidtIKESNlIEKSYKDkFDNTL 972
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2873 GDAKIEFQELARMGSPGSSSATAQQLqtvknyIKTFDNgqILLNNAVDIGEALYpvvspdnreriradlrqmrEKFDYLR 2952
Cdd:TIGR01612 973 IDKINELDKAFKDASLNDYEAKNNEL------IKYFND--LKANLGKNKENMLY-------------------HQFDEKE 1025
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2953 DEANAFMQQVEGVLIQKTSIEES-YTQVSHYLNESKAKVPTTDELYPTLATKKAALQnyKTQLQEItlhKNALKqlHDKA 3031
Cdd:TIGR01612 1026 KATNDIEQKIEDANKNIPNIEIAiHTSIYNIIDEIEKEIGKNIELLNKEILEEAEIN--ITNFNEI---KEKLK--HYNF 1098
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3032 VTLCDDESERKTDESiqeyntlsKKISDRITTVGNHVVKH-EAYDQVLEKAQDWLNTIKSEAIDI--LNETTFEKEGAEE 3108
Cdd:TIGR01612 1099 DDFGKEENIKYADEI--------NKIKDDIKNLDQKIDHHiKALEEIKKKSENYIDEIKAQINDLedVADKAISNDDPEE 1170
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3109 KLLVVENLLQHKPEGDSIFDTCHKLL---------ETVLTQTH-------PSGHPALLKGFEEPKQSWEDFMTLCQDSLV 3172
Cdd:TIGR01612 1171 IEKKIENIVTKIDKKKNIYDEIKKLLneiaeiekdKTSLEEVKginlsygKNLGKLFLEKIDEEKKKSEHMIKAMEAYIE 1250
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3173 KLKQLCSKWDEFDTIIEELDNWMKNVEA------------VVKNQNLKSTAEAKNAHLKQLQDISkdierRGAAINELMD 3240
Cdd:TIGR01612 1251 DLDEIKEKSPEIENEMGIEMDIKAEMETfnishdddkdhhIISKKHDENISDIREKSLKIIEDFS-----EESDINDIKK 1325
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3241 --QGREIEGE---TDLNLKLSRLNTRYQTLKnlcKESIAKYVNYVKDhesFDKDFDSFKQNLQSSVDELAKTNEIVGDQS 3315
Cdd:TIGR01612 1326 elQKNLLDAQkhnSDINLYLNEIANIYNILK---LNKIKKIIDEVKE---YTKEIEENNKNIKDELDKSEKLIKKIKDDI 1399
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3316 VLQDQQNKLREMSDKRILDstlfeGLIDRGEKLYGHTSPEGREIirqqlralrtlwDNYtddLNSATQKIDQCLLQFNEF 3395
Cdd:TIGR01612 1400 NLEECKSKIESTLDDKDID-----ECIKKIKELKNHILSEESNI------------DTY---FKNADENNENVLLLFKNI 1459
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3396 SIAQDQLTKWLK-------------------DVDKAMQSHTEPKttlQEKRAQLQNHKLLHQEITTHNVLVDNVCDKA-Q 3455
Cdd:TIGR01612 1460 EMADNKSQHILKikkdnatndhdfninelkeHIDKSKGCKDEAD---KNAKAIEKNKELFEQYKKDVTELLNKYSALAiK 1536
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3456 ILVDQIKDNSlNVYLTSIKQLFQSIV-------QKSDEILH---NLDDCVQKHNELNNALSSAKTWISNEKAKLL----- 3520
Cdd:TIGR01612 1537 NKFAKTKKDS-EIIIKEIKDAHKKFIleaekseQKIKEIKKekfRIEDDAAKNDKSNKAAIDIQLSLENFENKFLkisdi 1615
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3521 --ECDDAYGEKADIKRKIETLG------QLAQNKPQAMKIISDIRDLFEKVKATTSEKGN-EVLDKEIEELETTMKSHFD 3591
Cdd:TIGR01612 1616 kkKINDCLKETESIEKKISSFSidsqdtELKENGDNLNSLQEFLESLKDQKKNIEDKKKElDELDSEIEKIEIDVDQHKK 1695
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3592 DIE-GIEGKQKDV-LAQWDKFEKALEELTKWCRSAEAVFREQQLQSTlhEKVEQLEKYKIQRELILQKEKEIdafgdaaH 3669
Cdd:TIGR01612 1696 NYEiGIIEKIKEIaIANKEEIESIKELIEPTIENLISSFNTNDLEGI--DPNEKLEEYNTEIGDIYEEFIEL-------Y 1766
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3670 ALLNNCgadrLKTLT-----------TQITNRYQLLQVLskEVVNRWSNLVDDhqfyqDKYNEVDLWLQPIESQMAKVLL 3738
Cdd:TIGR01612 1767 NIIAGC----LETVSkepitydeiknTRINAQNEFLKII--EIEKKSKSYLDD-----IEAKEFDRIINHFKKKLDHVND 1835
|
....*....
gi 442626147 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 442626147 413 AEKWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGI 492
Cdd:cd21257 2 AREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VGI 80
|
90 100 110
....*....|....*....|....*....|...
gi 442626147 493 AKLLDAED-VDVPKPDEKSIMTYVAQfLHKYPE 524
Cdd:cd21257 81 KPSLELSEmMYTDRPDWQSVMQYVAQ-IYKYFE 112
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
424-518 |
2.37e-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: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 424 LLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDV-D 502
Cdd:cd21251 10 LLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPIMTGKEMaS 89
|
90
....*....|....*.
gi 442626147 503 VPKPDEKSIMTYVAQF 518
Cdd:cd21251 90 VGEPDKLSMVMYLTQF 105
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
11573-11751 |
2.40e-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: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11573 WQQIDNDLWRLEQWLQfaESTQKAQSA-PPSNIELLEDVTQDHREFLLDLESHKSIISSLNVVGDHLAThtLDTEKARQL 11651
Cdd:cd00176 2 LQQFLRDADELEAWLS--EKEELLSSTdYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11652 RSRLEADNERWNNVCINATKWQGLLQTALMGNSEFHQTIgELVEWLQRTEQNIKASEPVDLTEErsvLETKFKKFKDLRA 11731
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLES---VEELLKKHKELEE 153
|
170 180
....*....|....*....|
gi 442626147 11732 ELERCEPRVVSLQDAADQLL 11751
Cdd:cd00176 154 ELEAHEPRLKSLNELAEELL 173
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
421-515 |
2.42e-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: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 421 RKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAED 500
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90
....*....|....*..
gi 442626147 501 VDV--PKPDEKSIMTYV 515
Cdd:cd21258 83 MMImgKKPDSKCVFTYV 99
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
6427-7028 |
2.62e-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: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6427 AINEIKNEYELQGHPKIQELKGKAAQVAEV-ISNLDgqQVEEQMKSLDrrFADLGKR---------------IDRKSQLL 6490
Cdd:TIGR01612 1052 SIYNIIDEIEKEIGKNIELLNKEILEEAEInITNFN--EIKEKLKHYN--FDDFGKEenikyadeinkikddIKNLDQKI 1127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6491 DVTNKGVEGAKGEIDQLQNWVKQQIEELQAPKPLGYTPKDAEARQQKIKSLMKDAEAKQSLADVLEKrvanMQQELEPVE 6570
Cdd:TIGR01612 1128 DHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKK----LLNEIAEIE 1203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6571 YSQ--LESaLRNLN-TENRNLSGVLKAELDRALEAS----KARKSLENDLDKarqwLKTKISEVRKLPVYHPLTSAEIEK 6643
Cdd:TIGR01612 1204 KDKtsLEE-VKGINlSYGKNLGKLFLEKIDEEKKKSehmiKAMEAYIEDLDE----IKEKSPEIENEMGIEMDIKAEMET 1278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6644 KIQENRKYDD--DAKQFNDSVLTDVQRQAANIMKD-----------------CDDADK--AALQQILDEIAADYQTLKDE 6702
Cdd:TIGR01612 1279 FNISHDDDKDhhIISKKHDENISDIREKSLKIIEDfseesdindikkelqknLLDAQKhnSDINLYLNEIANIYNILKLN 1358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6703 SSKrgKSLDDLLQGRKAFEDSMKNMGDWLNEMETATEGELRTTSLPVLEEQLahykKLLSDAENKGGLINDVSEQGKSIL 6782
Cdd:TIGR01612 1359 KIK--KIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKI----ESTLDDKDIDECIKKIKELKNHIL 1432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6783 PTLSNADKLKLNDDIKN--------------------MKDRYGRIKNTIDDRVNALGDHIKKYKDAKSRlaecsqflGNI 6842
Cdd:TIGR01612 1433 SEESNIDTYFKNADENNenvlllfkniemadnksqhiLKIKKDNATNDHDFNINELKEHIDKSKGCKDE--------ADK 1504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6843 QQKLRELNRPIGSRI-EDVQDLLGAYEGI-LKELKDSKSKMGDMQMDDLPELQSILaqqddmikLIEDQLAHLRQLLLLR 6920
Cdd:TIGR01612 1505 NAKAIEKNKELFEQYkKDVTELLNKYSALaIKNKFAKTKKDSEIIIKEIKDAHKKF--------ILEAEKSEQKIKEIKK 1576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6921 EQFIalINEIIAFIMKYTDVIIDIENSPDSLEDKINKYDDVIVKIQEC-------EGVLASANDKGQKIASEGNAADKNS 6993
Cdd:TIGR01612 1577 EKFR--IEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDClketesiEKKISSFSIDSQDTELKENGDNLNS 1654
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 442626147 6994 ITEQLQSLKNQLQNLRKA------VESQRQKHQLQLESHKK 7028
Cdd:TIGR01612 1655 LQEFLESLKDQKKNIEDKkkeldeLDSEIEKIEIDVDQHKK 1695
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7293-8093 |
2.89e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7293 VNQQAQSLIRQADARNR------QLIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFR 7366
Cdd:TIGR02168 198 LERQLKSLERQAEKAERykelkaELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7367 NVDPTVRSRRH-LEDTKNAI----QELREESNQLKSSHKEIEALSKSILTF----------LGEVHKPSAEaIQAKVDKL 7431
Cdd:TIGR02168 278 ELEEEIEELQKeLYALANEIsrleQQKQILRERLANLERQLEELEAQLEELeskldelaeeLAELEEKLEE-LKEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7432 VEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSvhvYDEHIAQTEQllitlnSQVQQAAEESKLL 7511
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER---LEARLERLED------RRERLQQEIEELL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7512 VAQTTAHYQAKQNQLPSDIAQEFTALELLaERVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPT 7591
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEEL-ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7592 QMKELLQRiNHEITAIYERFtlvktnGQLIieNCRNSEEKTLVQTtidqLAASLAQVrgwLDEKKQAVGD--SLDAWTRF 7669
Cdd:TIGR02168 507 GVKALLKN-QSGLSGILGVL------SELI--SVDEGYEAAIEAA----LGGRLQAV---VVENLNAAKKaiAFLKQNEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7670 MNLYQIVMSWASEKRNFIDQTIELRTLPEARNKLNDYVTSVKSIKPIVKHLS-------------EMDKELEHIGQ-VTT 7735
Cdd:TIGR02168 571 GRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLggvlvvddldnalELAKKLRPGYRiVTL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7736 VGDL--KDKLQEAEDAKisVEAVLLERNSLLQEACEEWDQCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQLGFCEKTL 7813
Cdd:TIGR02168 651 DGDLvrPGGVITGGSAK--TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7814 ADINVQKTKLRLSIEKLEVHFRNGMGGDPRLSENVDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQE 7893
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7894 EQQLRLVMAPTYLPHDRERALAEQQDLITQELDELLQSLSSVEDGIANMNQSSLDgmlhglklIQSNLEVHERDAIELKN 7973
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE--------LEELIEELESELEALLN 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7974 QAKKLPTDPATERL--------LNDTVDRIDLLLRRTQQGITMIANAMHGQKKRQQEIDEYQQHLLELEQWIIEVSAELA 8045
Cdd:TIGR02168 881 ERASLEEALALLRSeleelseeLRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE 960
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626147 8046 SFEPTSDSSTDEQV--LKSQVER-------SQQLLRTLKDRQQSM----EDLVEQTRQLQS 8093
Cdd:TIGR02168 961 NKIEDDEEEARRRLkrLENKIKElgpvnlaAIEEYEELKERYDFLtaqkEDLTEAKETLEE 1021
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
293-374 |
4.31e-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: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 293 RIDDLINDLRDGTKLIALLEVLSGERLPVEKGRV--LRRPHFLSNANTALQFLASK----RIKLVNINPADLVDGRPPVV 366
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaISRLQKLHNVEVALKALKEAgvlrGGDGGGITAKDIVDGHREKT 104
|
....*...
gi 442626147 367 LGLIWTII 374
Cdd:cd21223 105 LALLWRII 112
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
10718-10918 |
4.76e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10718 ELSEQYKALTNLHN---------ETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERnalqlryihlkrvphL 10788
Cdd:COG4913 229 ALVEHFDDLERAHEaledareqiELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL---------------L 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10789 KHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALAtamRMEQASiGQRISNLRAALKTWQGFLQRVTQLSESYEQRVN 10868
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEA---QIRGNG-GDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442626147 10869 QL-------QQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALES 10918
Cdd:COG4913 370 ALglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
409-518 |
7.12e-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: 7.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 409 GDLKAEKWKQGARKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLV-NLAELKKTSNRQRLETAFDVAE 487
Cdd:cd21315 6 DDGPDDGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAE 82
|
90 100 110
....*....|....*....|....*....|.
gi 442626147 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 |
7.22e-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: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 274 KKTFTNWINSYL-----LKRVPPLRI--DDLINDLRDGTKLIALLEVLSGERLPVekgRVLRRPHFLS------NANTAL 340
Cdd:cd21217 3 KEAFVEHINSLLaddpdLKHLLPIDPdgDDLFEALRDGVLLCKLINKIVPGTIDE---RKLNKKKPKNifeateNLNLAL 79
|
90 100 110
....*....|....*....|....*....|....
gi 442626147 341 QFLASKRIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21217 80 NAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10585-11331 |
7.80e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 7.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10585 EEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSseal 10664
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER---- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10665 rlwRQYLQHVQSFLSCAIPEDYSSLREQQQLCAihqnllisqqsvlsetplesELSEQYKALTNLHNETLSRIMQRNGEL 10744
Cdd:TIGR02168 311 ---LANLERQLEELEAQLEELESKLDELAEELA--------------------ELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10745 ERRVSGWNAYRQQL----AALLDWLRQREAERNALQLRYIHLKRVPHLKHRLDAMIQQLDQG--EQQSKALQEQQQELAR 10818
Cdd:TIGR02168 368 EELESRLEELEEQLetlrSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKleEAELKELQAELEELEE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10819 HCDDALATAMRMEQA--SIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKLLDAN----------SE 10886
Cdd:TIGR02168 448 ELEELQEELERLEEAleELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQsglsgilgvlSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10887 SLPTQP---AAIEQLLGSlRAQRV---QLGAQVSALESLT------VTQEELKecISPHDMKTIRQRNWLLWQQ------ 10948
Cdd:TIGR02168 528 LISVDEgyeAAIEAALGG-RLQAVvveNLNAAKKAIAFLKqnelgrVTFLPLD--SIKGTEIQGNDREILKNIEgflgva 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10949 ----------HADLDYQLANLI--NSIEERLSLLSNYQIRY-------DRIS-----------QWLQRLEQRVEKDADVT 10998
Cdd:TIGR02168 605 kdlvkfdpklRKALSYLLGGVLvvDDLDNALELAKKLRPGYrivtldgDLVRpggvitggsakTNSSILERRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10999 AMTNPEQAAKQLEQQVN---SELQLRDKEREWLLSTSRELLTLYSEPEVR-SQVQQQSDSLIDRWQRLKYLAKQKATKIG 11074
Cdd:TIGR02168 685 KIEELEEKIAELEKALAelrKELEELEEELEQLRKELEELSRQISALRKDlARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11075 ELKMTLLRLEERIALIRAWLFEVESQLDkplNFESYTPNVIEAKLKEHEQIQRsiehHSSNVGEVLNLVEMLLNDADSWR 11154
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIE---QLKEELKALREALDELRAELTL----LNEEAANLRERLESLERRIAATE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11155 TQvntsglaasAQNLEQRWKNVCSQSAERKARILTIWNLLQQLIKLTAEHKNWLGKQESQI--AGFERDQKSHSKHKLEE 11232
Cdd:TIGR02168 838 RR---------LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALalLRSELEELSEELRELES 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11233 RQMELRAKLEELESQ--SVNLR------QLEQIYAKLAMSAGVEPENIQKLTLPTKVMVSMWR----QLTPRCHAL---- 11296
Cdd:TIGR02168 909 KRSELRRELEELREKlaQLELRleglevRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARrrlkRLENKIKELgpvn 988
|
810 820 830
....*....|....*....|....*....|....*...
gi 442626147 11297 LDAID--KDAKLMREFNNAQLE-ATNSLNAIQKALEQL 11331
Cdd:TIGR02168 989 LAAIEeyEELKERYDFLTAQKEdLTEAKETLEEAIEEI 1026
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
267-376 |
1.96e-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: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 267 EEQErvqKKTFTNWINSYLLkrvpPLRIDDLINDLRDGtklIALLEVLsgERL---PVEKGRVLR-----RPHFLSNANT 338
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGL----DPLINNLYEDLRDG---LVLLQVL--DKIqpgCVNWKKVNKpkplnKFKKVENCNY 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 442626147 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 |
2.51e-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: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 413 AEKWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGI 492
Cdd:cd21256 8 AREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGI 86
|
90 100 110
....*....|....*....|....*....|...
gi 442626147 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 ... |
6813-7501 |
4.76e-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: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6813 DRVNALGDHI----KKYKDAKSRLAECSQFLGNIQQKLRELNRPIGSRIEDVQDLLGAYEGILKELKDSKSkmgdmqmdD 6888
Cdd:TIGR02168 232 LRLEELREELeelqEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ--------Q 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6889 LPELQSILAQQDDMIKLIEDQLAHLRQLLLLREQFIALINEIIAFIMK-YTDVIIDIENSPDSLEDKINKYDDVIVKIQE 6967
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEeLESLEAELEELEAELEELESRLEELEEQLET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6968 CEGVLASANDKGQKIASE--GNAADKNSITEQLQSLK-NQLQNLRKAVESQRQKHQLQLESHKKMAAELSEILDWLHSH- 7043
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEieRLEARLERLEDRRERLQqEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAl 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7044 EGAAKSRPLLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEIgMPSSLLemlSEGRSLVASLPHELEEREKYL 7123
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL-KNQSGL---SGILGVLSELISVDEGYEAAI 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7124 KNNRDSRLEYMqLVAKFNDWVHEAELRLQNSQHGIDYehLVQDLDEHKIFFGNEAPIRNLVHKQIQEAAD--KIWSSLNN 7201
Cdd:TIGR02168 540 EAALGGRLQAV-VVENLNAAKKAIAFLKQNELGRVTF--LPLDSIKGTEIQGNDREILKNIEGFLGVAKDlvKFDPKLRK 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7202 YEQSELSaelaqfQTKLTNTLANAKTQQSELEKEA-------ERWR-----------------EYQQSIDRVKATIERT- 7256
Cdd:TIGR02168 617 ALSYLLG------GVLVVDDLDNALELAKKLRPGYrivtldgDLVRpggvitggsaktnssilERRREIEELEEKIEELe 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7257 --------------KFVDEPVQNLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIRQADARNRQLIEQDnAGLNRS 7322
Cdd:TIGR02168 691 ekiaelekalaelrKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI-EELEER 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7323 WQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFRNV-----DPTVRSRRHLEDTKNAIQELREESNQLKS 7397
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeaaNLRERLESLERRIAATERRLEDLEEQIEE 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7398 SHKEIEALSKSILTFlgevhKPSAEAIQAKVDKLVEQQAKLN---DTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALH 7474
Cdd:TIGR02168 850 LSEDIESLAAEIEEL-----EELIEELESELEALLNERASLEealALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
730 740
....*....|....*....|....*..
gi 442626147 7475 EQLQsvhvydEHIAQTEQLLITLNSQV 7501
Cdd:TIGR02168 925 AQLE------LRLEGLEVRIDNLQERL 945
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2751-2963 |
4.81e-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: 4.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2751 LWSQYEQSNEQISNWLRDVEGRVKAETSSQvNLSEVPQKLQELSILQQDVLAHEPIINNLEQTSQQLIEKNPEA--RIGQ 2828
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDaeEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2829 FVTHLVQRYQAVSKALTSYIDKIRGAQLSnANFAKAAKDFNEWFGDAKiefQELARMGSPGSSSATAQQLQTVKNYIKTF 2908
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLEEKE---AALASEDLGKDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 442626147 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 |
5.61e-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: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 419 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDA 498
Cdd:cd21196 3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSA 82
|
90 100
....*....|....*....|
gi 442626147 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 |
6.75e-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: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4391 LDRLKNLKASLADEFPRVDQVRALGEKVIPGTVDVGQvNIKSQIDTTQQEWESLLTTISSTIEAIEARLQHWSEYEQLrD 4470
Cdd:cd00176 39 LKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-D 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4471 QCLAWIRDTDNNLHAIDLKEDLPKKRAQLDALKALQGDVRAKELEVDNVTEKAQTLLKGPSSNRAsgpelvtkyQQIFHK 4550
Cdd:cd00176 117 DLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDAD---------EEIEEK 187
|
170
....*....|
gi 442626147 4551 VKELNNRWQQ 4560
Cdd:cd00176 188 LEELNERWEE 197
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3815-4032 |
7.34e-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: 7.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3815 QLSSYQDILNQTVNWLDQVEKLIHNENPASwtSAQEIRSKLYKYKATNQDINSHKRIVEAVNEKAAALLgSAAPANADEI 3894
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGD--DLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3895 SKAVAEVNKRYDQVGQDCAKLVADLDGAFDVYQQFSELQKAQQDYQKNlwDRLTGYSDYSGNKAALQARLQKINEIQDAL 3974
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEK--EAALASEDLGKDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442626147 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 |
8.31e-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: 8.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 421 RKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAED 500
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90
....*....|....*..
gi 442626147 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 |
1.03e-08 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 59.77 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3606 QWDKFEKALEELTKWCRSAEAVFREQQLQSTLHEKVEQLEKYKIQRELILQKEKEIDAFGDAAHALLNNCG--ADRLKTL 3683
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHpdAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3684 TTQITNRYQLLQVLSKEVVNRWSNLVDDHQFYQDKYnEVDLWLQPIESQMAKVLLDEPTQSSNIL----QVLLSEKEQAE 3759
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLESVEELlkkhKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442626147 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 |
2.24e-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: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 417 KQGARKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLV-NLAELKKTSNRQRLETAFDVAESKLGIAKL 495
Cdd:cd21314 9 KQTPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQV 85
|
90 100
....*....|....*....|...
gi 442626147 496 LDAEDVDVPKPDEKSIMTYVAQF 518
Cdd:cd21314 86 IAPEEIVDPNVDEHSVMTYLSQF 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7324-8142 |
2.91e-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: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7324 QDLVRSLEQRRDNLQ---QLAEHWDGFENSLHAWEKAL--GRLEDKFRNVDPTvrsrrhLEDTKNAIQELREESNQLKSS 7398
Cdd:TIGR02168 192 EDILNELERQLKSLErqaEKAERYKELKAELRELELALlvLRLEELREELEEL------QEELKEAEEELEELTAELQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7399 HKEIEALSKsiltFLGEVHKpSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQ 7478
Cdd:TIGR02168 266 EEKLEELRL----EVSELEE-EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7479 SVHvydehiAQTEQLLITLNSQVQQAAEESKLLVAQTTA--HYQAKQNQLPSDIAQEFTALELLAERVQVTMETKEkdfk 7556
Cdd:TIGR02168 341 ELE------EKLEELKEELESLEAELEELEAELEELESRleELEEQLETLRSKVAQLELQIASLNNEIERLEARLE---- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7557 raktvrteyvDGVDEVQRWllQAEVQVQERSLTPTQMKELLQRINHEITaiyERFTLVKTNGQLIIENCRNSEEKTLVQT 7636
Cdd:TIGR02168 411 ----------RLEDRRERL--QQEIEELLKKLEEAELKELQAELEELEE---ELEELQEELERLEEALEELREELEEAEQ 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7637 TIDQLAASLAQVRGWLDEKKQAVGdsldawtRFMNLYQ---IVMSWASEKRNFIDQTIELRTLPE---------ARNKLN 7704
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQE-------NLEGFSEgvkALLKNQSGLSGILGVLSELISVDEgyeaaieaaLGGRLQ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7705 DYVT-SVKSIKPIVKHLSEMDKELEHIGQVTTVGDlkDKLQEAEDAKISVEAVLLERNSLLQEACEEWdqceRKIKDIRS 7783
Cdd:TIGR02168 549 AVVVeNLNAAKKAIAFLKQNELGRVTFLPLDSIKG--TEIQGNDREILKNIEGFLGVAKDLVKFDPKL----RKALSYLL 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7784 WHEKTKQGLDSSQQQKKPLRDQLGFCekTLADINVQKtklRLSIEKLEVHFRNGMGGdprLSENVDDLVRVLDGLGELVK 7863
Cdd:TIGR02168 623 GGVLVVDDLDNALELAKKLRPGYRIV--TLDGDLVRP---GGVITGGSAKTNSSILE---RRREIEELEEKIEELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7864 AKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRLVMAPTYLPHDRERALAEQQDLITQELDELLQSLSSVEDGIANMN 7943
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7944 QSsldgmlhgLKLIQSNLEVHERDAIELKNQAKKLptdpatERLLNDTVDRIDLLLRRtqqgitmIANAMHGQKKRQQEI 8023
Cdd:TIGR02168 775 EE--------LAEAEAEIEELEAQIEQLKEELKAL------REALDELRAELTLLNEE-------AANLRERLESLERRI 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 8024 DEYQQHLLELEQWIIEVSAELASfeptsdsstdeqvLKSQVERSQQLLRTLKDRQQSMEDLVEQTRQLqshpdvspladt 8103
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEA------------ 888
|
810 820 830
....*....|....*....|....*....|....*....
gi 442626147 8104 lmeqlqsiITILREQVTVATKRIFTIEKRIVDLRKAKSE 8142
Cdd:TIGR02168 889 --------LALLRSELEELSEELRELESKRSELRRELEE 919
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6609-6820 |
3.06e-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: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6609 LENDLDKARQWLKTKISEVRKLpvYHPLTSAEIEKKIQENRKYDDDAKQFNDSVlTDVQRQAANIMKDCDDaDKAALQQI 6688
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERV-EALNELGEQLIEEGHP-DAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6689 LDEIAADYQTLKDESSKRGKSLDDLLQGRKAFEDSMKnMGDWLNEMETATEGELRTTSLPVLEEQLAHYKKLLSDAENKG 6768
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442626147 6769 GLINDVSEQGKSILPTLSNADKLKLNDDIKNMKDRYGRIKNTIDDRVNALGD 6820
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5441-6298 |
3.50e-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: 61.61 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5441 EECQSWIEKTREKLSECEQIpgtLNEVQIKLNTVKnlRQG-----FETGQNKLR------YLLELKEKV----IMNTEQN 5505
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDI---LNELERQLKSLE--RQAekaerYKELKAELRelelalLVLRLEELReeleELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5506 GAAKIQEDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDVEPSVKTSDEFLND----LSEKRAALE 5581
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERqleeLEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5582 KFRVIQRDINghNDIVEKINQRLKEDNSLDLKdfqpgLTKFDDLQTQVNKIIESLENQvnsHEKYKQAYNELQDWLRRTR 5661
Cdd:TIGR02168 330 SKLDELAEEL--AELEEKLEELKEELESLEAE-----LEELEAELEELESRLEELEEQ---LETLRSKVAQLELQIASLN 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5662 IEVEQCADchgEKDQVESRLNRLGDIQSSslEGKALLEACEELSQAVIATsgsegqdnVAQEIKHLTSEWETLQTISRDA 5741
Cdd:TIGR02168 400 NEIERLEA---RLERLEDRRERLQQEIEE--LLKKLEEAELKELQAELEE--------LEEELEELQEELERLEEALEEL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5742 RSSLESCLAAWQTFLQKFNKINLWIETMNKRVTKsQEGENKTPEDLVNAKKLLEE---VLAEKDNVEDlndNCELLMEQS 5818
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQEN-LEGFSEGVKALLKNQSGLSGilgVLSELISVDE---GYEAAIEAA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5819 ACTRIRDQTIETQANYTK----LLTSAQGLVAKIEKNLSDHTEFLNYKKEMDAWIEKAQQVLDDCSTDGDAA-------- 5886
Cdd:TIGR02168 543 LGGRLQAVVVENLNAAKKaiafLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsyll 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5887 ---IIAQKLDTVNSLASRLPEGqhllalvqdayskASNITPEDKQEKLRELMTKVREDWDALGLAVKQKLSDLKQaqnrw 5963
Cdd:TIGR02168 623 ggvLVVDDLDNALELAKKLRPG-------------YRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEE----- 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5964 ndfaankdklekwlnetettlkvapetkgelsEMKTLLERYKTLSNELKLKGNELEQLQSEARDLGTEVDAVNRLQSRCD 6043
Cdd:TIGR02168 685 --------------------------------KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6044 KLKNDCSAHITALEQEMFDYNAYHQSLQDVEKWLLQISFQLMAHNSLFISNREQTQEQIKQHEALLV----EIQKYQTNL 6119
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalreALDELRAEL 812
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6120 DDLNAKGQAQIKRYESStpairptvESQLKNIQDSYNSLLQTSVQIKNRLLESLAKFQEYEDTLDSIMRNLEtyepIIQT 6199
Cdd:TIGR02168 813 TLLNEEAANLRERLESL--------ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE----ALLN 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6200 ELDAPATSLELAQNQLRCAQEMQNKLNNEKSRLAAAVQACEAATASISRPSSPLETAMQAIPEReliVRAKLEDLLDQVQ 6279
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER---LSEEYSLTLEEAE 957
|
890
....*....|....*....
gi 442626147 6280 SHLGGLTASVSELEQQQKQ 6298
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKR 976
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6374-6723 |
4.34e-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: 61.24 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6374 ELMDAIA-------KKQAGQNVIDGYRQGMADVQNWFDTLIKRMDVLDRGSglNCAQKMAAINEIKNEYElqGHPKIQEL 6446
Cdd:TIGR02169 157 KIIDEIAgvaefdrKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER--EKAERYQALLKEKREYE--GYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6447 KGKAAQVAEVISNLDGQqvEEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEgAKGEIDQLQnwVKQQIEELQAP----- 6521
Cdd:TIGR02169 233 EALERQKEAIERQLASL--EEELEKLTEEISELEKRLEEIEQLLEELNKKIK-DLGEEEQLR--VKEKIGELEAEiasle 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6522 ---KPLGYTPKDAEARQQKIKSLMkdaEAKQSLADVLEKRVANMQQELEPV---------EYSQLESALRNLNTENRNLS 6589
Cdd:TIGR02169 308 rsiAEKERELEDAEERLAKLEAEI---DKLLAEIEELEREIEEERKRRDKLteeyaelkeELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6590 GVLKAELDRALEASKARKSLENDLDKARQWLKTKISEVRKLpvyhpltSAEIEKKIQENRKYDDDAKQFNDSVLTDVQRQ 6669
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL-------NAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 442626147 6670 AANImkdcddADKAALQQILDEIAADYQTLKDESSKRGKSLDDLLQGRKAFEDS 6723
Cdd:TIGR02169 458 EQLA------ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
268-373 |
4.46e-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: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 268 EQERVQKKTFTNWINSYllkRVPPlRIDDLINDLRDGTKLIALLEVLSgerlP--VEKGRVLRRPH-------FLSNANT 338
Cdd:cd21298 2 IEETREEKTYRNWMNSL---GVNP-FVNHLYSDLRDGLVLLQLYDKIK----PgvVDWSRVNKPFKklganmkKIENCNY 73
|
90 100 110
....*....|....*....|....*....|....*
gi 442626147 339 ALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTI 373
Cdd:cd21298 74 AVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQL 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5541-5749 |
4.84e-08 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 57.84 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5541 QLEEIFKLYKILIEWLEDVEPSVkTSDEFLNDLSEKRAALEKFRVIQRDINGHNDIVEKIN---QRLKEDNSLDLKDFQP 5617
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNelgEQLIEEGHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5618 GL----TKFDDLQTQVNKIIESLENQVNSHEKYKQAYnELQDWLRRTRIEVEQCADCHgEKDQVESRLNRLGDIQSSSLE 5693
Cdd:cd00176 80 RLeelnQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442626147 5694 GKALLEACEELSQAVIATSGSEGQDNVAQEIKHLTSEWETLQTISRDARSSLESCL 5749
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
10540-11490 |
4.97e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.13 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10540 TLANVAETQdKERKELDKEVTLAKAYFNNvqqDISREAPQNPKESEEQLAALRAhlqtLARTEEQLRQLKERHQN--SEV 10617
Cdd:PRK04863 245 TLEAIRVTQ-SDRDLFKHLITESTNYVAA---DYMRHANERRVHLEEALELRRE----LYTSRRQLAAEQYRLVEmaREL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10618 ApsvASSDDDGILEvlalwqkifqdtfQEYHRLSTRLARSQNsseALRLWRQYLQHVQSFLscaipEDYSSLREQQQLCA 10697
Cdd:PRK04863 317 A---ELNEAESDLE-------------QDYQAASDHLNLVQT---ALRQQEKIERYQADLE-----ELEERLEEQNEVVE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10698 IHQNLLISQQSVLSETPLE-SELSEQykaltnlhnetLSRIMQRNGELERRVSgwnAYRQQLAAL--------------- 10761
Cdd:PRK04863 373 EADEQQEENEARAEAAEEEvDELKSQ-----------LADYQQALDVQQTRAI---QYQQAVQALerakqlcglpdltad 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10762 --LDWLRQREAERNALQLRyihlkrVPHLKHRL---DAMIQQLDQGEQQSKAL-----QEQQQELARhcdDALATAMrmE 10831
Cdd:PRK04863 439 naEDWLEEFQAKEQEATEE------LLSLEQKLsvaQAAHSQFEQAYQLVRKIagevsRSEAWDVAR---ELLRRLR--E 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10832 QASIGQRISNLRAALKTWQGFL---QRVTQLSESYEQRVNQ---LQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQ 10905
Cdd:PRK04863 508 QRHLAEQLQQLRMRLSELEQRLrqqQRAERLLAEFCKRLGKnldDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10906 RVQLGAQVSALESLT----VTQ---EELKECiSPHDMKTiRQRNWLLWQQHADLDYQLANLINSIEERLSLLsnyQIRYD 10978
Cdd:PRK04863 588 LEQLQARIQRLAARApawlAAQdalARLREQ-SGEEFED-SQDVTEYMQQLLERERELTVERDELAARKQAL---DEEIE 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10979 RISQ-------WLQRLEQRV------EKDADVTAMTNPEQAAkqLEQQVNSELQLRDkerewLLSTSRELLTLYSEPEVR 11045
Cdd:PRK04863 663 RLSQpggsedpRLNALAERFggvllsEIYDDVSLEDAPYFSA--LYGPARHAIVVPD-----LSDAAEQLAGLEDCPEDL 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11046 SQVQQQSDSLIDRWQRLKYLAKQKATKIGELKMTLLRL-----------EERIALIRAWLFEVESQLDKpLNFESytpnv 11114
Cdd:PRK04863 736 YLIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFpevplfgraarEKRIEQLRAEREELAERYAT-LSFDV----- 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11115 ieaklkehEQIQRSIEHHSSNVGEVLNLV-----EMLLNDADSWRTQVNTSGLAASAQNLEQRwknvcsqSAERKARilt 11189
Cdd:PRK04863 810 --------QKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVELERALADHESQEQQQR-------SQLEQAK--- 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11190 iwNLLQQLIKLtaehknwlgkqESQIAGFERDQkshskhkLEERQMELRAKLEELE-------SQSVNLRQLEQIYAKLA 11262
Cdd:PRK04863 872 --EGLSALNRL-----------LPRLNLLADET-------LADRVEEIREQLDEAEeakrfvqQHGNALAQLEPIVSVLQ 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11263 msagVEPENIQKLTLPTKVMVSMWRQLTPRCHALLDAIDKDAKLMREFNNAQLEATNSLNaiqkalEQLPsaenqqtska 11342
Cdd:PRK04863 932 ----SDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKNSDLN------EKLR---------- 991
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11343 epkavlQRLESLEKKLQDAQQHVQQADNLAQEAKTRtkqqpqlkqLLELVSAYTTLWQTVQtrivtlkttwltRAAQAAA 11422
Cdd:PRK04863 992 ------QRLEQAEQERTRAREQLRQAQAQLAQYNQV---------LASLKSSYDAKRQMLQ------------ELKQELQ 1044
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626147 11423 SLPV----SEAANAAVQVNTLSQRkLRQAQQmQREtsitakdayimELQTAITECQNNLDELQRTVVDKTRK 11490
Cdd:PRK04863 1045 DLGVpadsGAEERARARRDELHAR-LSANRS-RRN-----------QLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
417-518 |
5.59e-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: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 417 KQGARKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLVNLAEL---KKTSNRQRleTAFDVAESKLGIA 493
Cdd:cd21313 6 KQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCPDWESwdpQKPVDNAR--EAMQQADDWLGVP 80
|
90 100
....*....|....*....|....*
gi 442626147 494 KLLDAEDVDVPKPDEKSIMTYVAQF 518
Cdd:cd21313 81 QVITPEEIIHPDVDEHSVMTYLSQF 105
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6943-7086 |
6.92e-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: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6943 DIENSPDSLEDKINKYDDVIVKIQECEGVLASANDKGQKIASEGnAADKNSITEQLQSLKNQLQNLRKAVESQRQKHQLQ 7022
Cdd:cd00176 27 DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQERLEELNQRWEELRELAEERRQRLEEA 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442626147 7023 LESHKKMaAELSEILDWLHSHEGAAKSRPlLDRDPESVERELQKHQSLSQDIESYLNKFNKIND 7086
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 |
7.71e-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: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 424 LLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDVD- 502
Cdd:cd21250 9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMAs 88
|
90
....*....|....*.
gi 442626147 503 VPKPDEKSIMTYVAQF 518
Cdd:cd21250 89 AEEPDKLSMVMYLSKF 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
932-1146 |
1.20e-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: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 932 QEYKSGIEQLSRWLRGAESVLDQRQVLGNSEQVKEYGQQLQQLASEIDDNEELFKTISRNFQSLIQDLSRD--EVDKMMK 1009
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDaeEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 1010 LLKQEKESLVRIRAQLpaKLHLFHQLQIQQESLEAgqKEIHQWLSEAEQLLGTHNLSGGRDAINEQLHKHKTYFSRTVYY 1089
Cdd:cd00176 83 ELNQRWEELRELAEER--RQRLEEALDLQQFFRDA--DDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442626147 1090 RSMLESKNKVFQNLLKAVSSDDKIDTApasQQMQQLNERFNYVIQNAQQWEQRLDSA 1146
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIE---EKLEELNERWEELLELAEERQKKLEEA 212
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
6795-7470 |
1.26e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6795 DDIKNMKDRYGRIKNTIDDRVNALGDHIKKYKDAKSRLAECSQFLGNIQQKLRELNrpigSRIEDVQDLLGAYEGILKEL 6874
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEIS----SELPELREELEKLEKEVKEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6875 KDSKSKMGDMQMDDLPELQSILAQQDDmIKLIEDQLAHLRQLLLLREQFIALINEI----------IAFIMKYTDVIIDI 6944
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEK-IRELEERIEELKKEIEELEEKVKELKELkekaeeyiklSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6945 ENSPDSLEDKINkydDVIVKIQECEgvlasandkgqkiasegnaadknSITEQLQSLKNQLQNLRKAVESQRQKHQLqLE 7024
Cdd:PRK03918 313 EKRLSRLEEEIN---GIEERIKELE-----------------------EKEERLEELKKKLKELEKRLEELEERHEL-YE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7025 SHKKMAAELSEIldwlhshegaaKSRpLLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEIGMPSSLLEMLSE 7104
Cdd:PRK03918 366 EAKAKKEELERL-----------KKR-LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7105 GRSLVASLPHEL-EEREKYLKNnrdsrlEYMQLVAKFNDWVHEAELRLqnsqhgidyEHLVQDLDEHKIFFGNEAPIRNL 7183
Cdd:PRK03918 434 AKGKCPVCGRELtEEHRKELLE------EYTAELKRIEKELKEIEEKE---------RKLRKELRELEKVLKKESELIKL 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7184 vhKQIQEAADKIWSSLNNYEQSELSAELAQFQtKLTNTLANAKTQQSELEKEAERWREYQQSidrvKATIERTKfvDEPV 7263
Cdd:PRK03918 499 --KELAEQLKELEEKLKKYNLEELEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKL--DELE 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7264 QNLAGLHFNIQKLSHaignvqsqnSDLTLVNQQAQSLirqaDARNRQLIEQDNAglNRSWQDLVRSLEQRRDNLQQLAEH 7343
Cdd:PRK03918 570 EELAELLKELEELGF---------ESVEELEERLKEL----EPFYNEYLELKDA--EKELEREEKELKKLEEELDKAFEE 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7344 WDGFENSLhawEKALGRLEDKFRNVDPtvrsrrhlEDTKNAIQELREESNQLKSSHKEIEALSKSIltflgevhkpsaEA 7423
Cdd:PRK03918 635 LAETEKRL---EELRKELEELEKKYSE--------EEYEELREEYLELSRELAGLRAELEELEKRR------------EE 691
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 442626147 7424 IQAKVDKLVEQqaklndtlRDKEQQVSKDLEEIEQVFRRISQLQDKL 7470
Cdd:PRK03918 692 IKKTLEKLKEE--------LEEREKAKKELEKLEKALERVEELREKV 730
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5432-5645 |
1.42e-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: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5432 EHQQHHSLYEECQSWIEKTREKLSEcEQIPGTLNEVQIKLNTVKNLRQGFETGQNKLRYLLELKEKVImNTEQNGAAKIQ 5511
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5512 EDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILiEWLEDVEPSVKtSDEFLNDLSEKRAALEKFRVIQRDIN 5591
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442626147 5592 GHNDIVEKINQRLKEdnsLDLKDFQPGLTKFDDLQTQVNKIIESLENQVNSHEK 5645
Cdd:cd00176 157 AHEPRLKSLNELAEE---LLEEGHPDADEEIEEKLEELNERWEELLELAEERQK 207
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
268-371 |
1.42e-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: 53.97 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 268 EQERvQKKTFTNWINSYllkRVPPlRIDDLINDLRDGTKLI-ALLEVLSGErlpVEKGRV--------LRRPHFLSNANT 338
Cdd:cd21300 4 EGER-EARVFTLWLNSL---DVEP-AVNDLFEDLRDGLILLqAYDKVIPGS---VNWKKVnkapasaeISRFKAVENTNY 75
|
90 100 110
....*....|....*....|....*....|...
gi 442626147 339 ALQFLASKRIKLVNINPADLVDGRPPVVLGLIW 371
Cdd:cd21300 76 AVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7193-7480 |
1.48e-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: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7193 DKIWSSLNNYEQSELSAELAQFQTKLTNTLANAKTQQSELEKEAERWREYQQSIDRVKATIE------RTKFVDEPVQ-- 7264
Cdd:TIGR02169 214 QALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEelnkkiKDLGEEEQLRvk 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7265 -NLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIRQADARNRQLIEQ--DNAGLNRSWQDLVRSLEQRRDNLQQLA 7341
Cdd:TIGR02169 294 eKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieEERKRRDKLTEEYAELKEELEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7342 EhwdgfenslhAWEKALGRLEDKFRNVdptvrsRRHLEDTKNAIQELR-------EESNQLKSSHKEIEALSKSILTFLG 7414
Cdd:TIGR02169 374 E----------EVDKEFAETRDELKDY------REKLEKLKREINELKreldrlqEELQRLSEELADLNAAIAGIEAKIN 437
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626147 7415 EVhKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSV 7480
Cdd:TIGR02169 438 EL-EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
10715-11102 |
1.65e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10715 LESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHLK----------- 10783
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELReeleklekllq 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10784 ------RVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELAR------HCDDALATAMRMEQASIGQRISNLRAALKTWQG 10851
Cdd:COG4717 127 llplyqELEALEAELAELPERLEELEERLEELRELEEELEEleaelaELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10852 FLQRVTQLSESYEQRVNQLQQEFGAAQKllDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESL------------ 10919
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLEN--ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIltiagvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10920 -------------TVTQEELKECISPHDMKTIRQRNWLLWqqHADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQR 10986
Cdd:COG4717 285 llallflllarekASLGKEAEELQALPALEELEEEELEEL--LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10987 LEQRVEKD--------ADVTAMTNPEQAAKQLEQQVNSELQLRDKER--EWLLSTSRELLTLYSEPEVRSQVQQQSDSLI 11056
Cdd:COG4717 363 LQLEELEQeiaallaeAGVEDEEELRAALEQAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEELE 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 442626147 11057 DRWQRLKYLAKQKATKIGELKMtlLRLEERIALIRAWLFEVESQLD 11102
Cdd:COG4717 443 ELEEELEELREELAELEAELEQ--LEEDGELAELLQELEELKAELR 486
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6503-6714 |
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 442626147 6503 EIDQLQNWVKQQIEELQAPKPlGYTPKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELePVEYSQLESALRNLN 6582
Cdd:cd00176 8 DADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6583 TENRNLSGvLKAELDRALEASKARKSLENDLDKARQWLKTKISEVRKLPVYHPLTsaEIEKKIQENRKYDDDAKQfNDSV 6662
Cdd:cd00176 86 QRWEELRE-LAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLE--SVEELLKKHKELEEELEA-HEPR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442626147 6663 LTDVQRQAANIMKDCDDADKAALQQILDEIAADYQTLKDESSKRGKSLDDLL 6714
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5399-6285 |
1.74e-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: 59.30 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5399 TRISNAIMQLTTKYNALLTLAKEVMRRLEMHYQEHQQHHSLY----EECQSWIEKTREKL----SECEQIPGTLNEVQIK 5470
Cdd:TIGR02168 189 DRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLvlrlEELREELEELQEELkeaeEELEELTAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5471 LNTVKNLRQGFETGQNKLRYLLELKEKVIMNTEQNgAAKIQEDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYK 5550
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELYALANEISRLEQQ-KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5551 ILIEWLEDVEPSVKTSDEFLNDLSEKRAALEK-FRVIQRDINGHNDIVEKIN-----------------QRLKEDNSLDL 5612
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEqLETLRSKVAQLELQIASLNneierlearlerledrrERLQQEIEELL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5613 KDFQPglTKFDDLQTQVNKIIESLENQVNSHEKYKQAYNELQDWLRRTRIEVEQCADchgEKDQVESRLNRLGDIQsSSL 5692
Cdd:TIGR02168 428 KKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER---ELAQLQARLDSLERLQ-ENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5693 EGKAlleacEELSQAVIATSGSEGQDNVAQEIKHLTSEWETlqtisrdarsSLESCLAawqtflqkfnkinlwiETMNKR 5772
Cdd:TIGR02168 502 EGFS-----EGVKALLKNQSGLSGILGVLSELISVDEGYEA----------AIEAALG----------------GRLQAV 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5773 VTKSQEGENKTPEDLVNAKKLLEEVLAEKDNVEDL--NDNCELLMEQSACTRIRDQTIETQANYTKLLTSAQGLVAkIEK 5850
Cdd:TIGR02168 551 VVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEiqGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVL-VVD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5851 NLSDHTEFLNYKKEMDAWIekaqqVLDDCSTDGDAAIIAQKLDTVNSLASRLPEGQHLLALVQDAYSKASNITPE----- 5925
Cdd:TIGR02168 630 DLDNALELAKKLRPGYRIV-----TLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKAlaelr 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5926 DKQEKLRELMTKVREDWDALGLAVKQKLSDLKQAQNRWNDFAANKDKLEKWLNETETTLKVAPETKGELS--------EM 5997
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEeelaeaeaEI 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5998 KTLLERYKTLSNELKLKGNELEQLQSEARDLGTEVDAVNRLQSRCDKLKNDCSAHITALEQEmfdynayhqslqdvekwL 6077
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ-----------------I 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6078 LQISFQLMAHNSLFISNREQTQEQIKQHEALLVEIQKYQTNLDDLNakgqaqiKRYESSTPAIRpTVESQLKNIQDSYNS 6157
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR-------SELEELSEELR-ELESKRSELRRELEE 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6158 LLQTSVQIKNRLLESLAKFQ--------EYEDTLDSIMRNLETYEPIIQtELDAPATSLE-----------LAQNQLRCA 6218
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDnlqerlseEYSLTLEEAEALENKIEDDEE-EARRRLKRLEnkikelgpvnlAAIEEYEEL 998
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626147 6219 QEMQNKLNNEKSRLAaavqaceaatasisrpsSPLETAMQAIPERELIVRAKLEDLLDQVQSHLGGL 6285
Cdd:TIGR02168 999 KERYDFLTAQKEDLT-----------------EAKETLEEAIEEIDREARERFKDTFDQVNENFQRV 1048
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3180-3373 |
1.81e-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: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3180 KWDEFDTIIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINELMDQGREI-----EGETDLNLK 3254
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeghPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3255 LSRLNTRYQTLKNLCKESIAKYVNYVKDHEsFDKDFDSFKQNLQsSVDELAKTNEIVGDQSVLQDQQNKLREMSDKRILD 3334
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLE-EKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 442626147 3335 STLFEGLIDRGEKLYGHTSPEGREIIRQQLRALRTLWDN 3373
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEE 197
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5792-6699 |
2.17e-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: 58.91 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5792 KLLEEVLAEKDNVEDLNDNCELLMEQSACTRIRDQTIETQAN-YTKLLTSAQGLVAKIEKNLSDHTEFLNY----KKEMD 5866
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEeLQKELYALANEISRLEQQKQILRERLANlerqLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5867 AWIEKAQQVLDDCSTDGDA--AIIAQKLDTVNSLASRLPEgqhLLALVQDAyskasnitpEDKQEKLRELMTKVREDWDA 5944
Cdd:TIGR02168 323 AQLEELESKLDELAEELAEleEKLEELKEELESLEAELEE---LEAELEEL---------ESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5945 LGLAVKQKLSDLKQAQNRWNDFAANKDKL--EKWLNETETTLKVAPETKGELSEMKTLLE----RYKTLSNELKLKGNEL 6018
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLqqEIEELLKKLEEAELKELQAELEELEEELEelqeELERLEEALEELREEL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6019 EQLQSEARDLGTEVdavNRLQSRCDKLKNdcsahitaLEQEmfdynayHQSLQDVEKWLLQISFQLMAHNSL---FISNR 6095
Cdd:TIGR02168 471 EEAEQALDAAEREL---AQLQARLDSLER--------LQEN-------LEGFSEGVKALLKNQSGLSGILGVlseLISVD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6096 EQTQEQIkqhEALLVE-IQKYQTNLDDLNAKGQAQIKRYESSTPAIRPtvesqLKNIQDSynsllqtsvQIKNRLLESLA 6174
Cdd:TIGR02168 533 EGYEAAI---EAALGGrLQAVVVENLNAAKKAIAFLKQNELGRVTFLP-----LDSIKGT---------EIQGNDREILK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6175 KFQEYEDTLDSIMRNLETYEPIIQTELD--APATSLELAQNQLrcaqemqnKLNNEKSRLAAAVQACEAATASISRPSSP 6252
Cdd:TIGR02168 596 NIEGFLGVAKDLVKFDPKLRKALSYLLGgvLVVDDLDNALELA--------KKLRPGYRIVTLDGDLVRPGGVITGGSAK 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6253 LETAMQAiPERELivrAKLEDLLDQVQSHLGGLTASVSELEQQQKQRAELQDWVKKqqssvsdwmmrpcklRPEAAQQEL 6332
Cdd:TIGR02168 668 TNSSILE-RRREI---EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK---------------ELEELSRQI 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6333 VSMNDLLNSIGdKRSQLMLEMTGSLGDEDTDLDDNIDKLESELMDAIAKKQAGqnvidgyRQGMADVQNWFDTLIKRMDV 6412
Cdd:TIGR02168 729 SALRKDLARLE-AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA-------EAEIEELEAQIEQLKEELKA 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6413 LDRgsglncaqkmaAINEIKNEYelqghpkiQELKGKAAQVAEVisnldgqqveeqMKSLDRRFADLGKRIDRKSQLLDV 6492
Cdd:TIGR02168 801 LRE-----------ALDELRAEL--------TLLNEEAANLRER------------LESLERRIAATERRLEDLEEQIEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6493 TNKGVEGAKGEIDQLQNWVKQQIEELQAPKplgytpKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELEPV--E 6570
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALL------NERASLEEALALLRSELEELSEELRELESKRSELRRELEELreK 923
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6571 YSQLESALRNLNTENRNLSGVLKAELDRALEASKARKS-LENDLDKARQWLKTKISEVRKLPVYHPLTSAEIEkkiQENR 6649
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENkIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYE---ELKE 1000
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 442626147 6650 KYDDDAKQFNDsvLTDVQRQAANIMKDCDDADKAALQQILDEIAADYQTL 6699
Cdd:TIGR02168 1001 RYDFLTAQKED--LTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRV 1048
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
268-380 |
2.33e-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: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 268 EQERVqkkTFTNWINSYL-----LKRVPPLRIDD--LINDLRDGT---KLIALLEVLSGERLPVEKGRVlrRPHFLS-NA 336
Cdd:cd21323 23 EEEKV---AFVNWINKALegdpdCKHVVPMNPTDesLFKSLADGIllcKMINLSQPDTIDERAINKKKL--TPFTISeNL 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 442626147 337 NTALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTII---LYFQIE 380
Cdd:cd21323 98 NLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIkvgLFADIE 144
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10523-11130 |
2.43e-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: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10523 ELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDIsreapqnpkesEEQLAALRAHLQTLARTE 10602
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-----------EEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10603 EQLRQLKERHQNsevapsvASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEALRLwrqylqhvqsflscai 10682
Cdd:COG1196 302 QDIARLEERRRE-------LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA---------------- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10683 pedysSLREQQQLCAIHQNLLISQQSVLSEtpLESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALL 10762
Cdd:COG1196 359 -----ELAEAEEALLEAEAELAEAEEELEE--LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10763 DWLRQREAERNALQlryihlkrvphlkhRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALATAMRmEQASIGQRISNL 10842
Cdd:COG1196 432 ELEEEEEEEEEALE--------------EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE-ELAEAAARLLLL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10843 RAALKTWQGFLQRVTQLsesyeqrvnQLQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRV--QLGAQVSALESLT 10920
Cdd:COG1196 497 LEAEADYEGFLEGVKAA---------LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVveDDEVAAAAIEYLK 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10921 VTQEELKECISPHDMKTIRQRNWLLWQQHADLDYQL-ANLINSIEERLSLLSNY----QIRYDRISQWLQRLEQRVEKDA 10995
Cdd:COG1196 568 AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLvASDLREADARYYVLGDTllgrTLVAARLEAALRRAVTLAGRLR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10996 DVT-AMTNPEQAAKQLEQQVNSELQLRDKEREWLLSTSRELLtlysepEVRSQVQQQSDSLIDRWQRLKYLAKQKATKIG 11074
Cdd:COG1196 648 EVTlEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA------EEELELEEALLAEEEEERELAEAEEERLEEEL 721
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 442626147 11075 ELKMTLLRLEERIALIRAWLFEVESQLDKPLNFESYTPNVIEAKLKEHEQIQRSIE 11130
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4470-4672 |
2.61e-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: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4470 DQCLAWIRDTDNNLHAIDLKEDLPKKRAQLDALKALQGDVRAKELEVDNVTEKAQTLLkgpSSNRASGPELVTKYQQIFH 4549
Cdd:cd00176 10 DELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI---EEGHPDAEEIQERLEELNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4550 KVKELNNRWQQYVTSHED------FDNAISDCSSWINEIKEKL---DYCSDMSSMspKELDKKLATIQDVILLKDEgsaR 4620
Cdd:cd00176 87 RWEELRELAEERRQRLEEaldlqqFFRDADDLEQWLEEKEAALaseDLGKDLESV--EELLKKHKELEEELEAHEP---R 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442626147 4621 VLKILEQAQHVLANTAPGGHEAINKELTDLQDLWSGIALRIMDVKSNLDDSI 4672
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
268-374 |
2.79e-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: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 268 EQERVQKKTFTNWINSYllkRVPPLrIDDLINDLRDGTKLIALLEVLsgeRLPVEKGRVLRRPHFL--------SNANTA 339
Cdd:cd21329 2 EGESSEERTFRNWMNSL---GVNPY-VNHLYSDLCDALVIFQLYEMT---RVPVDWGHVNKPPYPAlggnmkkiENCNYA 74
|
90 100 110
....*....|....*....|....*....|....*.
gi 442626147 340 LQFLASK-RIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21329 75 VELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLM 110
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
6464-7036 |
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 442626147 6464 QVEEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNwVKQQIEELQapKPLGYTPKDAEARQQKIKSLMK 6543
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-LKEEIEELE--KELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6544 DAEAKQSLADVLEKRVANMqQELEPV--EYSQLESALRNLNTENRNLSgVLKAELDRALEASKARKSLENDLDKARQWLK 6621
Cdd:PRK03918 267 RIEELKKEIEELEEKVKEL-KELKEKaeEYIKLSEFYEEYLDELREIE-KRLSRLEEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6622 TKISEVRK----LPVYHPLTSaEIEKKIQENRKYDddaKQFNDSVLTDVQRQAANIMKdcddaDKAALQQILDEIAADYQ 6697
Cdd:PRK03918 345 KKLKELEKrleeLEERHELYE-EAKAKKEELERLK---KRLTGLTPEKLEKELEELEK-----AKEEIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6698 TLKDESSKRGKSLDDL--------LQGRKAFEDSMKN--------MGDWLNEMETATEGE--LRtTSLPVLEEQLAHYKK 6759
Cdd:PRK03918 416 ELKKEIKELKKAIEELkkakgkcpVCGRELTEEHRKElleeytaeLKRIEKELKEIEEKErkLR-KELRELEKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6760 LLSdaenkgglINDVSEQGKSILPTLSNADKLKLNDDIKNMKDRYGRIkNTIDDRVNALGDHIKKYKDAKSRLAECSQFL 6839
Cdd:PRK03918 495 LIK--------LKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKL-IKLKGEIKSLKKELEKLEELKKKLAELEKKL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6840 GNIQQKLRELNRPIGSR----IEDVQDLLGAYEGILK---ELKDSKSkmgdmqmddlpELQSILAQQDDMIKLIEDQLAH 6912
Cdd:PRK03918 566 DELEEELAELLKELEELgfesVEELEERLKELEPFYNeylELKDAEK-----------ELEREEKELKKLEEELDKAFEE 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6913 LRQLLLLREQfiaLINEIIAFIMKYTDviidienspdslEDKINKYDDVIVKIQECEGVLASAndkgqkiasEGNAADKN 6992
Cdd:PRK03918 635 LAETEKRLEE---LRKELEELEKKYSE------------EEYEELREEYLELSRELAGLRAEL---------EELEKRRE 690
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 442626147 6993 SITEQLQSLKNQLQNLRKAVEsqrqkhqlQLESHKKMAAELSEI 7036
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKK--------ELEKLEKALERVEEL 726
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
6860-7404 |
5.32e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6860 VQDLLGAYEGILKELKDSKSKMGDMQMDD-LPELQSILAQQDDMIKLIEDQLAHLRQLLLLREQFIAL-------INEII 6931
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDLHErLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEheerreeLETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6932 AFIMKYTDVIIDIENSPDSLEDKINKYDDVIVKI-QECEGVLASAndkgqkiasEGNAADKNSITEQLQSLKNQLQNLRK 7010
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELeEERDDLLAEA---------GLDDADAEAVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7011 AVESQR---QKHQLQLESHKKMAAELSEILDWLHshEGAAKsrplLDRDPESVERELQKHQSLSQDIESYLNKFNKINDG 7087
Cdd:PRK02224 329 RLEECRvaaQAHNEEAESLREDADDLEERAEELR--EEAAE----LESELEEAREAVEDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7088 VKTEIGMPSSLLEMLSEGRSlvaSLPHELEEREKYLKNNRDSRLEYMQLVAKFNdwVHEAELRLQNSQH--GI-DYEHLV 7164
Cdd:PRK02224 403 APVDLGNAEDFLEELREERD---ELREREAELEATLRTARERVEEAEALLEAGK--CPECGQPVEGSPHveTIeEDRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7165 QDLDEHKIFFGNEAPIRNLVH---KQIQEAADKIWSSLNNYEQS-ELSAELAQFQTKLTNTLANAKTQQSELEKEAERWR 7240
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLeraEDLVEAEDRIERLEERREDLeELIAERRETIEEKRERAEELRERAAELEAEAEEKR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7241 E-YQQSIDRVKATIERTKFVD----------EPVQNLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIRQADARNR 7309
Cdd:PRK02224 558 EaAAEAEEEAEEAREEVAELNsklaelkeriESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKR 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7310 QLIEQ-DNAGLNRSWQDLVRS---LEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDkfrnvdptVRSRR-HLEDTKNA 7384
Cdd:PRK02224 638 ELEAEfDEARIEEAREDKERAeeyLEQVEEKLDELREERDDLQAEIGAVENELEELEE--------LRERReALENRVEA 709
|
570 580
....*....|....*....|
gi 442626147 7385 IQELREESNQLKSSHKEIEA 7404
Cdd:PRK02224 710 LEALYDEAEELESMYGDLRA 729
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
267-383 |
7.50e-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: 7.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 267 EEQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASK 346
Cdd:cd21285 5 EAENGFDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSFLAAK 84
|
90 100 110
....*....|....*....|....*....|....*..
gi 442626147 347 RIKLVNINPADLVDGRPPVVLGLIWTIILYFQIEENS 383
Cdd:cd21285 85 GINIQGLSAEEIRNGNLKAILGLFFSLSRYKQQQQQP 121
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10760-11360 |
8.11e-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: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10760 ALLDWLRQREAERNALQLRyihlkrvpHLKHRLDAMIQQLDQGEQQSKALQEQQQEL---------ARHCDDALATAMRM 10830
Cdd:COG1196 217 ELKEELKELEAELLLLKLR--------ELEAELEELEAELEELEAELEELEAELAELeaeleelrlELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10831 EQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKLLDANSESLptqpAAIEQLLGSLRAQRVQLG 10910
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL----EEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10911 AQVSALESLTVTQEELKEcisphdmktirqrnwLLWQQHADLDYQLANLINSIEERLSLLSNYQIRYDRisqwlqRLEQR 10990
Cdd:COG1196 365 EALLEAEAELAEAEEELE---------------ELAEELLEALRAAAELAAQLEELEEAEEALLERLER------LEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10991 VEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWLLSTSRELltLYSEPEVRSQVQQQSDSLIDRWQRLK------- 11063
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL--LEEAALLEAALAELLEELAEAAARLLllleaea 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11064 -YLAKQKATKIGELKMTLLRLEERIALIRAWLFEVESQLDKPLNfesytPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNL 11142
Cdd:COG1196 502 dYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA-----AALQNIVVEDDEVAAAAIEYLKAAKAGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11143 VEMLLNDADSWRTQVNTSGLAASAQNL---EQRWKNVCSQSAERKARILTIWNL-----------LQQLIKLTAEHKNWL 11208
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLvasDLREADARYYVLGDTLLGRTLVAArleaalrravtLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11209 GKQESQIAGFERDQKSHSKHKLEERQMELRAKLEELESQSVNLRQLE--QIYAKLAMSAGVEPENIQKLTLPTKVMVSMW 11286
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEeeERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626147 11287 RQLTPRCHALLDAIDKDAKLMREFNNAQLEAtnSLNAIQKALEQL----PSAENQQtskaepKAVLQRLESLEKKLQD 11360
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELER--ELERLEREIEALgpvnLLAIEEY------EELEERYDFLSEQRED 806
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6988-7654 |
8.13e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 8.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6988 AADKNSITEQLQSLKNQLQNLRKAVESQRQKHQlQLESHKKMAAEL-----SEILDWLHSHEGAAKSRPLLDRDPESVER 7062
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELE-ELESRLEELEEQletlrSKVAQLELQIASLNNEIERLEARLERLED 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7063 ELQKhqsLSQDIESYLNKFNKINdgvKTEIGMPSSLLEMLSEgrslvaSLPHELEEREKYLKNNRDSRLEYMQLVAKFND 7142
Cdd:TIGR02168 415 RRER---LQQEIEELLKKLEEAE---LKELQAELEELEEELE------ELQEELERLEEALEELREELEEAEQALDAAER 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7143 WVHEAELRLqnsqhgidyeHLVQDLDEHKIFFGNEapIRNLVHKQIQEAADK--IWSSLNNYEQSELSAELA---QFQTK 7217
Cdd:TIGR02168 483 ELAQLQARL----------DSLERLQENLEGFSEG--VKALLKNQSGLSGILgvLSELISVDEGYEAAIEAAlggRLQAV 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7218 LTNTLANAKTQQSELeKEAERWREYQQSIDRVKAT------IERTKFVDEPVQNLAGLHFNIQKLSHAIGNVQSQnsdLT 7291
Cdd:TIGR02168 551 VVENLNAAKKAIAFL-KQNELGRVTFLPLDSIKGTeiqgndREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGG---VL 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7292 LVN--QQAQSLIRQADARNRqLIEQDNAGLNRSW------QDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLED 7363
Cdd:TIGR02168 627 VVDdlDNALELAKKLRPGYR-IVTLDGDLVRPGGvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRK 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7364 KFRNVDPTVRSRRHLEDTKNaiQELREESNQLKSSHKEIEALSKSILTFLGEVHKPSAE--AIQAKVDKLVEQQAKLNDT 7441
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELS--RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEieELEERLEEAEEELAEAEAE 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7442 LRDKEQQVSKDLEEIEQVFRRISQLQDKLNAL----HEQLQSVHVYDEHIAQTEQLLITLNSQVQQAAEESKLLVAQtta 7517
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELTLLneeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE--- 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7518 hyQAKQNQLPSDIAQEFTALELLAERVQVTMETKEKDfkraktvRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELL 7597
Cdd:TIGR02168 861 --IEELEELIEELESELEALLNERASLEEALALLRSE-------LEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 442626147 7598 QRINHEITAIYERFT-LVKTNGQLIIENCRNSEEKtlvqttIDQLAASLAQVRGWLDE 7654
Cdd:TIGR02168 932 EGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDD------EEEARRRLKRLENKIKE 983
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
275-376 |
9.31e-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: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 275 KTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKRIKLVNIN 354
Cdd:cd21286 3 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 82
|
90 100
....*....|....*....|..
gi 442626147 355 PADLVDGRPPVVLGLIWTIILY 376
Cdd:cd21286 83 AEEIRNGNLKAILGLFFSLSRY 104
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
10550-11262 |
9.42e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.90 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10550 KERKELDKEVTLAKAYFNNVQQDisreAPQNPKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSdddgi 10629
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLC----TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK----- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10630 levlalWQKIFQDTFQEYHRLSTRLARSQNSSEAL---RLWRQYLQHVQSFLSC--AIPEDYSSLREQQ----QLCAIHQ 10700
Cdd:TIGR00618 258 ------KQQLLKQLRARIEELRAQEAVLEETQERInraRKAAPLAAHIKAVTQIeqQAQRIHTELQSKMrsraKLLMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10701 NLLISQQSVLSETPLESELSEQYKALTNLHNETLSR--IMQRNGELERRVSGWnayRQQLAALLDWLRQREAERNALQlR 10778
Cdd:TIGR00618 332 AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIreISCQQHTLTQHIHTL---QQQKTTLTQKLQSLCKELDILQ-R 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10779 YIHLKRVPHLKHRldAMIQQLDQGEQQSKALQE--QQQELARHCDDALATAMRMEQASIGQRISNLRAALKTWQGFLQRV 10856
Cdd:TIGR00618 408 EQATIDTRTSAFR--DLQGQLAHAKKQQELQQRyaELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10857 TQLSESYEQRVNQLQQefgaaqklldanseslptQPAAIEQLLGSLRAQRVQLGaqvsalesltvtqeelkecISPHD-- 10934
Cdd:TIGR00618 486 TRKKAVVLARLLELQE------------------EPCPLCGSCIHPNPARQDID-------------------NPGPLtr 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10935 -MKTIRQRNWLLWQQHADLDYQLanliNSIEERLSLLSNYQIRYDRISQWLQRLEQRVEKDADVTamtnpeqaaKQLEQQ 11013
Cdd:TIGR00618 529 rMQRGEQTYAQLETSEEDVYHQL----TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL---------QNITVR 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11014 VNSELQLRDKEREWLLSTSRELLTlysepEVRSQVQQQSDSLIDRwQRLKYLAKQKATKIGELkMTLLRLEERIALIRAW 11093
Cdd:TIGR00618 596 LQDLTEKLSEAEDMLACEQHALLR-----KLQPEQDLQDVRLHLQ-QCSQELALKLTALHALQ-LTLTQERVREHALSIR 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11094 LFEVESqLDKPLNFESYTPNVIEA---KLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDADSWRT--QVNTSGLAASAQN 11168
Cdd:TIGR00618 669 VLPKEL-LASRQLALQKMQSEKEQltyWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSdlAAREDALNQSLKE 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11169 LEQRWKNVCSQSAERKARiltiwNLLQQLIKLT--AEHKNWLGKQESQIAGFERDQKShSKHKLEERQMELRAKLEELES 11246
Cdd:TIGR00618 748 LMHQARTVLKARTEAHFN-----NNEEVTAALQtgAELSHLAAEIQFFNRLREEDTHL-LKTLEAEIGQEIPSDEDILNL 821
|
730
....*....|....*..
gi 442626147 11247 QSVNLRQ-LEQIYAKLA 11262
Cdd:TIGR00618 822 QCETLVQeEEQFLSRLE 838
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6062-6232 |
9.66e-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: 53.99 E-value: 9.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6062 DYNAYHQSLQDVEKWLLQIsfQLMAHNSLFISNREQTQEQIKQHEALLVEIQKYQTNLDDLNAKGQAQIKRYESSTPAIR 6141
Cdd:cd00176 1 KLQQFLRDADELEAWLSEK--EELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6142 ptveSQLKNIQDSYNSLLQTSVQIKNRLLESLAKFQEYEDTLDsIMRNLETYEPIIQTELdaPATSLELAQNQLRCAQEM 6221
Cdd:cd00176 79 ----ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKEL 151
|
170
....*....|.
gi 442626147 6222 QNKLNNEKSRL 6232
Cdd:cd00176 152 EEELEAHEPRL 162
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5645-6485 |
9.70e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 9.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5645 KYKQAYNELQDWLRRTRIEVEQCADCHGEkdqVESRLNRLgDIQSSSLEgkALLEACEELSQAVIATSgsegqdnvAQEI 5724
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNE---LERQLKSL-ERQAEKAE--RYKELKAELRELELALL--------VLRL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5725 KHLTSEWETLQTISRDARSSLESCLAAWQTFLQKFNKINLWIETMNKRVTKSQEGENKTPEDLVNAKKLLEEVLAEKDNV 5804
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5805 EDLNDNCELLMEQSACTRIRDQTIETQANytKLLTSAQGLVAKIEKnlsDHTEFLNYKKEMDAWIEKAQQVLDDCSTDgd 5884
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELE--EKLEELKEELESLEA---ELEELEAELEELESRLEELEEQLETLRSK-- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5885 aaiIAQKLDTVNSLASRLpegQHLLALVQDAYSKASNItpedKQEKLRELMTKVREDWDALGLAVKQKLSDLKQAQNRWN 5964
Cdd:TIGR02168 388 ---VAQLELQIASLNNEI---ERLEARLERLEDRRERL----QQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5965 DFAANKDKLEKWLNETETTLKVA----PETKGELSEMKTLLERYKTLSN---ELKLKGNELEQLQSEARDL-------GT 6030
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAerelAQLQARLDSLERLQENLEGFSEgvkALLKNQSGLSGILGVLSELisvdegyEA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6031 EVDAV--NRLQSRCDKLKNDCSAHITALEQEmfdynayhqslqDVEKWLLqISFQLMAHNSLFISNRE--QTQEQIKQHE 6106
Cdd:TIGR02168 538 AIEAAlgGRLQAVVVENLNAAKKAIAFLKQN------------ELGRVTF-LPLDSIKGTEIQGNDREilKNIEGFLGVA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6107 ALLVEIQ-KYQTNLDDL---------NAKGQAQIKRYESSTPAIrpTVESQLKNIQDSY--------NSLLQTSVQIKNr 6168
Cdd:TIGR02168 605 KDLVKFDpKLRKALSYLlggvlvvddLDNALELAKKLRPGYRIV--TLDGDLVRPGGVItggsaktnSSILERRREIEE- 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6169 lLEslAKFQEYEDTLDSIMRNLETYEpiiqTELDAPATSLELAQNQLRCAQEMQNKLNNEKSRLAAAVQACEAATASISR 6248
Cdd:TIGR02168 682 -LE--EKIEELEEKIAELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6249 PSSPLETAMQAIPERelivRAKLEDLLDQVQSHLGGLTASV----SELEQQQKQRAELQDWVKKQQSSVSDWMMRPCKLR 6324
Cdd:TIGR02168 755 ELTELEAEIEELEER----LEEAEEELAEAEAEIEELEAQIeqlkEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6325 PEAAQQElVSMNDLLNSIGDKRSQlMLEMTGSLgdedTDLDDNIDKLESELMDAIAKKQAGQNVIDGYRQGMADVQNWFD 6404
Cdd:TIGR02168 831 RRIAATE-RRLEDLEEQIEELSED-IESLAAEI----EELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6405 TLIKRMDVLDRGSGlNCAQKMAAINEIKNEYELQGHPKIQELKGKAAQVAEVISNLDgQQVEEQMKSLDRRFADLGKRID 6484
Cdd:TIGR02168 905 ELESKRSELRRELE-ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE-NKIEDDEEEARRRLKRLENKIK 982
|
.
gi 442626147 6485 R 6485
Cdd:TIGR02168 983 E 983
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
5862-6734 |
9.91e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 56.77 E-value: 9.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5862 KKEMDAWIEKAQQVLDDCSTDGDAAIIAQKLDTVNSLASRLpegQHLLALVQDAYSKASnitpedkqeklrelmtkvred 5941
Cdd:pfam12128 220 RQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRL---SHLHFGYKSDETLIA--------------------- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5942 wdalglavkqklsdlkqaqnrwndfaankdklekwlnetettlkvapetkgelsemkTLLERYKTLSNELKlkgnelEQL 6021
Cdd:pfam12128 276 ---------------------------------------------------------SRQEERQETSAELN------QLL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6022 QSEARDLGTEVDAVNRLQSRCDKLKNDCSAHITALEQemfDYNAYHQSlqDVEKwllqisfqLMAHNSLFISNREQTQEQ 6101
Cdd:pfam12128 293 RTLDDQWKEKRDELNGELSAADAAVAKDRSELEALED---QHGAFLDA--DIET--------AAADQEQLPSWQSELENL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6102 IKQHEALLVEIQKYQTNLDDLNAKGQAQ----IKRYESSTPAIRPTVESQLKNIQDSYNSLLQtsvQIKNRLLESLAKFQ 6177
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQnnrdIAGIKDKLAKIREARDRQLAVAEDDLQALES---ELREQLEAGKLEFN 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6178 EYEDTLDSIMRNLETYEPIIQTEldaPATSLELAQNQLRC--AQEMQNKLNNEKSRLAAAVQACEAATASISRpssplet 6255
Cdd:pfam12128 437 EEEYRLKSRLGELKLRLNQATAT---PELLLQLENFDERIerAREEQEAANAEVERLQSELRQARKRRDQASE------- 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6256 AMQAIPERELIVRAKLEDLLDQVQSHLGGLTASVseleqqqkqRAELQDWVKKQQSSVSDWMMRPCKLRPEAAQQelvSM 6335
Cdd:pfam12128 507 ALRQASRRLEERQSALDELELQLFPQAGTLLHFL---------RKEAPDWEQSIGKVISPELLHRTDLDPEVWDG---SV 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6336 NDLLNSIGDKRSQLMLEMTGSLGDEDTdLDDNIDKLESELMDAIAKKQAGQNV-------IDGYRQGMAD----VQNWFD 6404
Cdd:pfam12128 575 GGELNLYGVKLDLKRIDVPEWAASEEE-LRERLDKAEEALQSAREKQAAAEEQlvqangeLEKASREETFartaLKNARL 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6405 TLIkRMDVLDRGSGLNCAQKMAAINEIKNE--YELQGHPKIQELKGKAAQVAEvisnlDGQQVEEQMKSLDRRFADLGKR 6482
Cdd:pfam12128 654 DLR-RLFDEKQSEKDKKNKALAERKDSANErlNSLEAQLKQLDKKHQAWLEEQ-----KEQKREARTEKQAYWQVVEGAL 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6483 IDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIeelqapKPLGYTPKDAEARQQKIKSLMKDAE-AKQSLADVLEKRVan 6561
Cdd:pfam12128 728 DAQLALLKAAIAARRSGAKAELKALETWYKRDL------ASLGVDPDVIAKLKREIRTLERKIErIAVRRQEVLRYFD-- 799
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6562 MQQELEPVEYSQLESALRNLNTENRNLSGVLK-----AELDRAlEASKARKSLENDLDKARQWLKTKISEVRKLPVYH-P 6635
Cdd:pfam12128 800 WYQETWLQRRPRLATQLSNIERAISELQQQLArliadTKLRRA-KLEMERKASEKQQVRLSENLRGLRCEMSKLATLKeD 878
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6636 LTSAEIEKKIQENRKYDDDAKQFNDSVLTDVQrqaanimKDCDDADKAALQQILDEIAADYQTLKDESSKRGKSLDDLLQ 6715
Cdd:pfam12128 879 ANSEQAQGSIGERLAQLEDLKLKRDYLSESVK-------KYVEHFKNVIADHSGSGLAETWESLREEDHYQNDKGIRLLD 951
|
890
....*....|....*....
gi 442626147 6716 GRKAFedsmKNMGDWLNEM 6734
Cdd:pfam12128 952 YRKLV----PYLEQWFDVR 966
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
414-518 |
1.13e-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: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 414 EKWKQGARKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLV-NLAELKKTSNRQRLETAFDVAESKLGI 492
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*.
gi 442626147 493 AKLLDAEDVDVPKPDEKSIMTYVAQF 518
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQF 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10199-10965 |
1.40e-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: 56.22 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10199 EKVGELFSLSHKISTqIAEELEGASVLRDQLQAIQEGISNQRKHQAKISVILDECEAAERQGADVLEKAVADCQAAGEEL 10278
Cdd:TIGR02168 285 ELQKELYALANEISR-LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10279 VISWQEIMRIRQMLHTLPMRLKMSVSpvKLERDISQLQDDHAFLESKCTNI---MAILRSRLAVWLR--YERQLELVHGS 10353
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVA--QLELQIASLNNEIERLEARLERLedrRERLQQEIEELLKklEEAELKELQAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10354 VQETDFMMELIRVHGQVDYERLRKATERLEGLAGDLHNREQLIDELKGAAKPLiescdVQIVEQIESAvQEAVVAWNDTS 10433
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL-----ERLQENLEGF-SEGVKALLKNQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10434 ENLQQLRTRYQRAVELWDKYRNASAAVKNSIDQQMdAVKSLEQPLDALQHAKvcQDNLTTQNdrILELRDIVAKIAADVG 10513
Cdd:TIGR02168 516 SGLSGILGVLSELISVDEGYEAAIEAALGGRLQAV-VVENLNAAKKAIAFLK--QNELGRVT--FLPLDSIKGTEIQGND 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10514 LDASALMQGELDALgQRLAECKDAITT-----LANVAETQDkerkeLDKEVTLAKAY---FNNVQQD---ISREAPQNPK 10582
Cdd:TIGR02168 591 REILKNIEGFLGVA-KDLVKFDPKLRKalsylLGGVLVVDD-----LDNALELAKKLrpgYRIVTLDgdlVRPGGVITGG 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10583 ESEEQLAALrAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSE 10662
Cdd:TIGR02168 665 SAKTNSSIL-ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10663 ALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLCAIHQNLLISQQSVLSE-----TPLESELSEQYKALTNLhNETLSRI 10737
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeelKALREALDELRAELTLL-NEEAANL 822
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10738 MQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHLKRVphLKHRLDAMIQQLDQGEQQSKALQEQQQELA 10817
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE--LESELEALLNERASLEEALALLRSELEELS 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10818 RHCDDALATAMRMEQASIGQRISNLRAALKtWQGFLQRVTQLSEsyeqrvnQLQQEFGAAQKLLDANSESLPTQPAAIEQ 10897
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELR-LEGLEVRIDNLQE-------RLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626147 10898 LLGSLRAQRVQLGA-QVSALESLtvtqEELKEcisphdmktiRQRNwlLWQQHADLDYQLANLINSIEE 10965
Cdd:TIGR02168 973 RLKRLENKIKELGPvNLAAIEEY----EELKE----------RYDF--LTAQKEDLTEAKETLEEAIEE 1025
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10499-11062 |
1.50e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10499 LELRDIVAKIAADVGLDAS-ALMQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREA 10577
Cdd:COG1196 222 LKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10578 pqnpKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARS 10657
Cdd:COG1196 302 ----QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10658 QnsSEALRLWRQYLQHVQsflscaipEDYSSLREQQQLCAIHQNLLISQQSVLSEtplESELSEQYKALTNLHNETLSRI 10737
Cdd:COG1196 378 E--EELEELAEELLEALR--------AAAELAAQLEELEEAEEALLERLERLEEE---LEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10738 MQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHLKRvphLKHRLDAMIQQLDQGEQQSKALQ--EQQQE 10815
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA---RLLLLLEAEADYEGFLEGVKAALllAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10816 LARHCDDALATAMRMEQAsigqrisnLRAALKTWQgfLQRVTQLSESYEQRVNQLQQEFGAAQKLLDANSESLPTQPAAI 10895
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAA--------LEAALAAAL--QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10896 EQLLGSLRAQRVQLGAQVSALESLTVTQEELKEcispHDMKTIRQRNWLLWQQHADLDY--------------QLANLIN 10961
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLG----RTLVAARLEAALRRAVTLAGRLrevtlegeggsaggSLTGGSR 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10962 SIEERLSLLSNYQIRYDRISQWLQRLEQRVEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWLLSTSRELLTLYS- 11040
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEl 747
|
570 580 590
....*....|....*....|....*....|..
gi 442626147 11041 ----------EPEVRSQVQQQSDSLIDRWQRL 11062
Cdd:COG1196 748 leeealeelpEPPDLEELERELERLEREIEAL 779
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4248-4445 |
1.91e-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: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4248 KWSGFDEIADSLKSWLDETENALpADIELKTTLDEKRNKLQTYRDILNDINNHQVELGNLQEIAANL----PEKTELVDQ 4323
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieegHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4324 IIKDISDRFGKLQKRAQNYVERYEGIVSAHQQYSKAvMDAQEFIDATLNTV-HYWGDLDLEQISLHtnLDRLKNLKASLA 4402
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALaSEDLGKDLESVEEL--LKKHKELEEELE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442626147 4403 DEFPRVDQVRALGEKVIPGTVDVGQVNIKSQIDTTQQEWESLL 4445
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELL 199
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3282-3494 |
2.00e-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: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3282 DHESFDKDFDSFKQNLqSSVDELAKTNEIVGDQSVLQDQQNKLREMSDKRILDSTLFEGLIDRGEKLyGHTSPEGREIIR 3361
Cdd:cd00176 1 KLQQFLRDADELEAWL-SEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQL-IEEGHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3362 QQLRALRTLWDNYTDDLNSATQKIDQCLLQFNEFSIAqDQLTKWLKDVDKAMQSHtEPKTTLQEKRAQLQNHKLLHQEIT 3441
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442626147 3442 THNVLVDNVCDKAQILVDQIKDNSLNVY---LTSIKQLFQSIVQKSDEILHNLDDC 3494
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIeekLEELNERWEELLELAEERQKKLEEA 212
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3545-3811 |
2.39e-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: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3545 NKPQAMKIISDIRDLFEkvkattsekgNEVLD-KEIEELETTMKSHFDDIEGIEG------KQKDVL----AQWDKFEKA 3613
Cdd:COG4913 198 HKTQSFKPIGDLDDFVR----------EYMLEePDTFEAADALVEHFDDLERAHEaledarEQIELLepirELAERYAAA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3614 LEELTKW--CRSAEAVFREQQLQSTLHEKVEQLE----KYKIQRELILQKEKEIDAFGDAAHALLNNCGADRLKTLTTQI 3687
Cdd:COG4913 268 RERLAELeyLRAALRLWFAQRRLELLEAELEELRaelaRLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3688 TNryqlLQVLSKEVVNRWSNLvddhqfyqdkynevDLWLQPIEsqmakvlldeptqssniLQVLLSEKEqaeslFAALNA 3767
Cdd:COG4913 348 ER----LERELEERERRRARL--------------EALLAALG-----------------LPLPASAEE-----FAALRA 387
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 442626147 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 |
2.87e-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: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3161 EDFMTLCQDSLVKLKQLCSKWDEFDTIIEELDNWMKNVEAVVKNQNLKSTAE-AKNAHLKQLQDISKDI--------ERR 3231
Cdd:TIGR01612 751 KDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDnIKDEDAKQNYDKSKEYiktisikeDEI 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3232 GAAINELMDQGREIegetdlnlkLSRLNtRYQTLKNLCKESI-------AKYVNYVKDHESfDKDFDSFKQNLQSSVDEL 3304
Cdd:TIGR01612 831 FKIINEMKFMKDDF---------LNKVD-KFINFENNCKEKIdseheqfAELTNKIKAEIS-DDKLNDYEKKFNDSKSLI 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3305 AKTNeivgdQSVLQDQQN--KLREMSDK-RILDSTL--FEGLIDRGEKLyghtspegREIIRQQLRALR---TLWDNYTD 3376
Cdd:TIGR01612 900 NEIN-----KSIEEEYQNinTLKKVDEYiKICENTKesIEKFHNKQNIL--------KEILNKNIDTIKesnLIEKSYKD 966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3377 DL-NSATQKIDQCLLQFNEFSiaqdqLTKWLKDVDKAMQSHTEPKTTLQEKRAQLQNHKLLHQEITTHNVLvdnvcdkaQ 3455
Cdd:TIGR01612 967 KFdNTLIDKINELDKAFKDAS-----LNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFDEKEKATNDIE--------Q 1033
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3456 ILVDqIKDNSLNVYLTsikqLFQSIVQKSDEILHNLDDCVQKHNElnNALSSAKTWISN-----EKAKLLECDDaYGEKA 3530
Cdd:TIGR01612 1034 KIED-ANKNIPNIEIA----IHTSIYNIIDEIEKEIGKNIELLNK--EILEEAEINITNfneikEKLKHYNFDD-FGKEE 1105
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3531 DIKRKIETLGQLAQNKPQAMKIISDIRDLfEKVKATTSEKGNEvLDKEIEELETTMKSHF--DDIEGIEGKQKDVLAQWD 3608
Cdd:TIGR01612 1106 NIKYADEINKIKDDIKNLDQKIDHHIKAL-EEIKKKSENYIDE-IKAQINDLEDVADKAIsnDDPEEIEKKIENIVTKID 1183
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3609 KFEKALEELTKWCRSAEAVFREQqlqsTLHEKV----------------EQLEKYKIQRELILQKE----KEIDAFGDAA 3668
Cdd:TIGR01612 1184 KKKNIYDEIKKLLNEIAEIEKDK----TSLEEVkginlsygknlgklflEKIDEEKKKSEHMIKAMeayiEDLDEIKEKS 1259
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3669 HALLNNCGADRLKTLTTQITN----RYQLLQVLSKEVVNRWSNLVDDH-QFYQDKYNEVDlwLQPIESQMAKVLLDEPTQ 3743
Cdd:TIGR01612 1260 PEIENEMGIEMDIKAEMETFNishdDDKDHHIISKKHDENISDIREKSlKIIEDFSEESD--INDIKKELQKNLLDAQKH 1337
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3744 SSNILQVLlsekEQAESLFAALNAAGEKALPETSTQGREKIRKDLRDIRDRWDKLDEGIRNLEkrqeaQGVQLSSYQDIL 3823
Cdd:TIGR01612 1338 NSDINLYL----NEIANIYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIK-----DDINLEECKSKI 1408
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3824 NQTVNWLDQVEKLIHNENPASWTSAQEIRSKLY--KYKATNQDINSHKRIVEAVNEKAAALLG-------SAAPANADEI 3894
Cdd:TIGR01612 1409 ESTLDDKDIDECIKKIKELKNHILSEESNIDTYfkNADENNENVLLLFKNIEMADNKSQHILKikkdnatNDHDFNINEL 1488
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3895 SKAVAEVNKRYDQVGQDcAKLVADLDGAFDVYQQ--------FSELQ-KAQQDYQKNLWDRLTGYSDYSGNKAALQARL- 3964
Cdd:TIGR01612 1489 KEHIDKSKGCKDEADKN-AKAIEKNKELFEQYKKdvtellnkYSALAiKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKs 1567
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3965 -QKINEIqdalpegvaklKSLEDHIEQQASNIPARSKEVMarDLANLHADFEKFGASLSDVKSGLENRLQQWNDYEINLD 4043
Cdd:TIGR01612 1568 eQKIKEI-----------KKEKFRIEDDAAKNDKSNKAAI--DIQLSLENFENKFLKISDIKKKINDCLKETESIEKKIS 1634
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4044 RL--------ITWLGEAENSLKNY-----NLKSSFEEKEEQLNGFQSlaqNLRQNEADFDKVKDDTS-ELVQSSGETRIA 4109
Cdd:TIGR01612 1635 SFsidsqdteLKENGDNLNSLQEFleslkDQKKNIEDKKKELDELDS---EIEKIEIDVDQHKKNYEiGIIEKIKEIAIA 1711
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4110 vNVQQVSSRFQSIQATAKEILKKC-----------EQAVQDHGHFNDKYKQCADwLANAQARYddccdLSTVAsrddllK 4178
Cdd:TIGR01612 1712 -NKEEIESIKELIEPTIENLISSFntndlegidpnEKLEEYNTEIGDIYEEFIE-LYNIIAGC-----LETVS------K 1778
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4179 KQVVIQELLAQQPTATQLLNSTVELGEKCygstategreaiRSQLDDLT---FDQL-------FDNIAITARKIQDKIAK 4248
Cdd:TIGR01612 1779 EPITYDEIKNTRINAQNEFLKIIEIEKKS------------KSYLDDIEakeFDRIinhfkkkLDHVNDKFTKEYSKINE 1846
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4249 wsGFDEIADSLKSWLDETENALPADIeLKTTLDEKRN----KLQTYRDILNDINNHQVELGNLQEIAANLPEKTELVDQI 4324
Cdd:TIGR01612 1847 --GFDDISKSIENVKNSTDENLLFDI-LNKTKDAYAGiigkKYYSYKDEAEKIFINISKLANSINIQIQNNSGIDLFDNI 1923
|
....
gi 442626147 4325 IKDI 4328
Cdd:TIGR01612 1924 NIAI 1927
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3712-3910 |
3.21e-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: 52.45 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3712 HQFYQDkYNEVDLWLQPIESQMAKVLLDEPTQSSNIL----QVLLSEKEQAESLFAALNAAGEKaLPETSTQGREKIRKD 3787
Cdd:cd00176 3 QQFLRD-ADELEAWLSEKEELLSSTDYGDDLESVEALlkkhEALEAELAAHEERVEALNELGEQ-LIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3788 LRDIRDRWDKLDEGIRNLEKRQEAQGVQLSSYQDILnQTVNWLDQVEKLIHNENPASwtSAQEIRSKLYKYKATNQDINS 3867
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK--DLESVEELLKKHKELEEELEA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442626147 3868 HKRIVEAVNEKAAALLGSAAPANADEISKAVAEVNKRYDQVGQ 3910
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLE 200
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6063-6876 |
3.31e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6063 YNAYHQSLQDVEKWLLQISFQlmahnslfisnreqtqEQIKQHEALLVEIQKYQTNLDDLnakgQAQIKRYESSTPAIRP 6142
Cdd:TIGR02168 215 YKELKAELRELELALLVLRLE----------------ELREELEELQEELKEAEEELEEL----TAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6143 TVeSQLKNIQDSYNSLLQTSVQIKNRLLESLAKFQEYEDTLdsimrnletyepiiQTELDAPATSLELAQNQLRCAQEMQ 6222
Cdd:TIGR02168 275 EV-SELEEEIEELQKELYALANEISRLEQQKQILRERLANL--------------ERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6223 NKLNNEKSRLAAAVQACEAATASISRPSSPLETAMQAIPERELIVRAKLEDLLDQVQSHLGGLTASVSELEQQQKQRAEL 6302
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6303 QDWVKKQQSSVSDWMMRPCKLRPEAAQQELvsmNDLLNSIGDKRSQLMLemtgslgdedtdLDDNIDKLESELMDAIAKK 6382
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEELEEEL---EELQEELERLEEALEE------------LREELEEAEQALDAAEREL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6383 QAGQNVIDGYRQGMADVQNWFDTLIKRMDVLDRGSGLncAQKMAAINEIKNEYELQghpkIQELKGKAAQVAEVISN--- 6459
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGI--LGVLSELISVDEGYEAA----IEAALGGRLQAVVVENLnaa 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6460 LDGQQVEEQMKSLDRRFADLGKRIDRKSQLLDV-TNKGVEGAKGEID-------QLQNWVK------------QQIEELQ 6519
Cdd:TIGR02168 559 KKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDReILKNIEGFLGVAKdlvkfdpKLRKALSyllggvlvvddlDNALELA 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6520 APKPLGY----------------TPKDAEA------RQQKIKSLMKDAEAKQSLADVLEKRVANMQQELEPVEySQLESA 6577
Cdd:TIGR02168 639 KKLRPGYrivtldgdlvrpggviTGGSAKTnssileRRREIEELEEKIEELEEKIAELEKALAELRKELEELE-EELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6578 LRNLNTENRNLSGvLKAELDRALEASKARKSLENDLDKARQWLKTKISEVRKLPVYHPLTSAEIEKKIQE-NRKYDDDAK 6656
Cdd:TIGR02168 718 RKELEELSRQISA-LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEElEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6657 QF--NDSVLTDVQRQAANIMKDCDDAdKAALQQILDEIAADYQTLKDESskrgKSLDDLLQGRKAFEDSMKNMGDWLNEM 6734
Cdd:TIGR02168 797 ELkaLREALDELRAELTLLNEEAANL-RERLESLERRIAATERRLEDLE----EQIEELSEDIESLAAEIEELEELIEEL 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6735 ETATEGELRttslpVLEEQLAHYKKLLSDAENKGGLINDVSEQGKSIlptlsNADKLKLNDDIKNMKDRYGRIKNTID-- 6812
Cdd:TIGR02168 872 ESELEALLN-----ERASLEEALALLRSELEELSEELRELESKRSEL-----RRELEELREKLAQLELRLEGLEVRIDnl 941
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6813 -DRVNA-----LGDHIKKYKDAKSRLAECSQFLGNIQQKLRELNRPIGSRIEDVQDLLGAYEGILKELKD 6876
Cdd:TIGR02168 942 qERLSEeysltLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKED 1011
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
268-374 |
5.49e-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: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 268 EQERVQkktFTNWINSYLL------KRVP-PLRIDDLINDLRDGTKLIALL----------EVLSgerLPVEKGRVLRRP 330
Cdd:cd21294 5 EDERRE---FTKHINAVLAgdpdvgSRLPfPTDTFQLFDECKDGLVLSKLIndsvpdtideRVLN---KPPRKNKPLNNF 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 442626147 331 HFLSNANTALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21294 79 QMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5195-5684 |
5.75e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5195 DKYENLTKQAKDLYEKQKNTIESYQSLIDAGNEFATWLRNAKERlskcseptgdkqaLAEKTHQLKILQGELPEGAQKLK 5274
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKE-------------LEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5275 NAleqgeiacrSAEPEDCEIIEQEVALLQEEfdayREALNKAKDYLEVGIVKWSDYQDQYTEALEWLSKTEALVQSYNKL 5354
Cdd:PRK03918 225 KL---------EKEVKELEELKEEIEELEKE----LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5355 QDSLIQKKVVLEQFqghLQTLFDWQKTLDDLNMKAQVLLETCSDtrisnaIMQLTTKYNALLTLAKEVMRRLEmhyqEHQ 5434
Cdd:PRK03918 292 AEEYIKLSEFYEEY---LDELREIEKRLSRLEEEINGIEERIKE------LEEKEERLEELKKKLKELEKRLE----ELE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5435 QHHSLYEECQSW---------------IEKTREKLSECE----QIPGTLNEVQIKLNTVKNLRQGFETGQNKL------- 5488
Cdd:PRK03918 359 ERHELYEEAKAKkeelerlkkrltgltPEKLEKELEELEkakeEIEEEISKITARIGELKKEIKELKKAIEELkkakgkc 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5489 ----RYLLELKEKVIMNTEQNGAAKIQEDtealKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILiEWLEDVEPSVK 5564
Cdd:PRK03918 439 pvcgRELTEEHRKELLEEYTAELKRIEKE----LKEIEEKERKLRKELRELEKVLKKESELIKLKELA-EQLKELEEKLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5565 TSDefLNDLSEK----RAALEKFRVIQRDINGHNDIVEKINQRLKEDNSLD--LKDFQPGLTKF-DDLQTQVNKIIESLE 5637
Cdd:PRK03918 514 KYN--LEELEKKaeeyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEkkLDELEEELAELlKELEELGFESVEELE 591
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 442626147 5638 NQVNSHEKYKQAYNELQDWLRRTRIEVEQCADCHGEKDQVESRLNRL 5684
Cdd:PRK03918 592 ERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAET 638
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
268-374 |
6.63e-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: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 268 EQERVQKKTFTNWINSyllKRVPPlRIDDLINDLRDGTKLIALLEVLsgeRLPVEKGRVLRRPH--------FLSNANTA 339
Cdd:cd21331 18 EGETREERTFRNWMNS---LGVNP-HVNHLYGDLQDALVILQLYEKI---KVPVDWNKVNKPPYpklganmkKLENCNYA 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 442626147 340 LQFLASK-RIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21331 91 VELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLM 126
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
6996-7611 |
7.80e-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: 53.82 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6996 EQLQSLKNQLQNLRKAVESQRQKHQLQLES------HKKMAAELSEILDWLHSHEGAAKSRPLLDRDpesvERELQKHQS 7069
Cdd:TIGR00618 270 EELRAQEAVLEETQERINRARKAAPLAAHIkavtqiEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ----QSSIEEQRR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7070 LSQDIESYLNKFNKINDgvkteigMPSSLLEMLSEgrslvaslPHELEEREKYLKNNRDSRLEYMQLVAKFNDwvheael 7149
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAHE-------VATSIREISCQ--------QHTLTQHIHTLQQQKTTLTQKLQSLCKELD------- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7150 RLQNSQHGIDYEHLVQ-DLDEHKIFFGNEAPIRNLVHKQIQEAADKIWSSLN------NYEQSELSAELAQFQTKLTNTL 7222
Cdd:TIGR00618 404 ILQREQATIDTRTSAFrDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKlekihlQESAQSLKEREQQLQTKEQIHL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7223 ANAKTQQSE---LEKEAERWREYQQSIDRVKATIERTKFVDEPVQNLAGLHFNIQKLSHAIGNVQSQnsdLTLVNQQAQS 7299
Cdd:TIGR00618 484 QETRKKAVVlarLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQ---LTSERKQRAS 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7300 LIRQAdarnrQLIEQDNAGLNRSWQDLVRSLeqrrDNLQQLAEhwdgfenSLHAWEKALGRLEDKFRnvdptVRSRRHLE 7379
Cdd:TIGR00618 561 LKEQM-----QEIQQSFSILTQCDNRSKEDI----PNLQNITV-------RLQDLTEKLSEAEDMLA-----CEQHALLR 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7380 DTKNAIQELR---EESNQLKSSHKEIEALSKSILTFLGEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEI 7456
Cdd:TIGR00618 620 KLQPEQDLQDvrlHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7457 EQvfrrisqlqdKLNALHEQLQSVHVYDEHIAQTEQLLITLNSQVQQ------------AAEESKLLVAQTTAHYQAKQn 7524
Cdd:TIGR00618 700 AQ----------CQTLLRELETHIEEYDREFNEIENASSSLGSDLAAredalnqslkelMHQARTVLKARTEAHFNNNE- 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7525 QLPSDIaQEFTALELLAERVQVTMETKEKDFKRAKTVRTEYVDGVDE-VQRWLLQAEVQVQERSLTPTQMKELLQRInHE 7603
Cdd:TIGR00618 769 EVTAAL-QTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdEDILNLQCETLVQEEEQFLSRLEEKSATL-GE 846
|
....*...
gi 442626147 7604 ITAIYERF 7611
Cdd:TIGR00618 847 ITHQLLKY 854
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
10363-10928 |
8.92e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 8.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10363 LIRVHGQVDYERLRKATERLEGLAGDLHNREQLIDEL----------KGAAKPLIESCD--VQIVEQIESAV---QEAVV 10427
Cdd:PRK02224 189 LDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYeeqreqaretRDEADEVLEEHEerREELETLEAEIedlRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10428 AWNDTSENL-QQLRTRYQRAVELWDKYRNASA------AVKNSIDQQMDAV-KSLEQPLDALQHAKVCQDNLTTQNDRIL 10499
Cdd:PRK02224 269 ETEREREELaEEVRDLRERLEELEEERDDLLAeaglddADAEAVEARREELeDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10500 ELRDIVAKIAADvgldasalMQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQqDISREAPQ 10579
Cdd:PRK02224 349 EDADDLEERAEE--------LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE-DFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10580 NPKESEEQLAALRAHLQTLARTEEQLRQLKER------HQNSEVAPSVASSDDDGilEVLALWQKIFQDTFQEYHRLSTR 10653
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEALLEAgkcpecGQPVEGSPHVETIEEDR--ERVEELEAELEDLEEEVEEVEER 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10654 LARSQNSSEALRlwrqylqhvqsflscaipeDYSSLREQ----QQLCAIHQNLLISQQSVLSE-----TPLESELSEQYK 10724
Cdd:PRK02224 498 LERAEDLVEAED-------------------RIERLEERredlEELIAERRETIEEKRERAEElreraAELEAEAEEKRE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10725 ALTNLHNETlSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQlryihlkrvpHLKHRLDAMIQQLDQGEQ 10804
Cdd:PRK02224 559 AAAEAEEEA-EEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIE----------RLREKREALAELNDERRE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10805 QSKALQEQQQELARHCDDAlatamrmeqasigqRISNLRAALKTWQGFLQRVT-QLSESYEQRvNQLQQEFGAAQKLLDA 10883
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEA--------------RIEEAREDKERAEEYLEQVEeKLDELREER-DDLQAEIGAVENELEE 692
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 442626147 10884 nseslptqpaaieqlLGSLRAQRVQLGAQVSALESLTVTQEELKE 10928
Cdd:PRK02224 693 ---------------LEELRERREALENRVEALEALYDEAEELES 722
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7238-7448 |
1.09e-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: 50.91 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7238 RWREYQQSIDRVKATIERTKFV---DEPVQNLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIrQADARNRQLIEQ 7314
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELlssTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7315 DNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFeNSLHAWEKALGRLEDKFRNVDPTvrsrRHLEDTKNAIQELREESNQ 7394
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALASEDLG----KDLESVEELLKKHKELEEE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442626147 7395 LKSSHKEIEALSKSILTFLGEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQ 7448
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKK 208
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
10715-11390 |
1.25e-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: 53.05 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10715 LESELSEQYKALTNLHnETLSRIMQRNGELERRVSgWNAYRQQLAALLDWLRQREAE----RNALQLRYIHLKRVPHLKH 10790
Cdd:TIGR00618 224 LEKELKHLREALQQTQ-QSHAYLTQKREAQEEQLK-KQQLLKQLRARIEELRAQEAVleetQERINRARKAAPLAAHIKA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10791 rldamIQQLDQGEQQSKA-LQEQQQELARhcddalATAMRMEQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQ 10869
Cdd:TIGR00618 302 -----VTQIEQQAQRIHTeLQSKMRSRAK------LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10870 LQQEFGAAQKLLdanseSLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELK-ECISPHDMKTIRQRNWLLWQQ 10948
Cdd:TIGR00618 371 SCQQHTLTQHIH-----TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQgQLAHAKKQQELQQRYAELCAA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10949 HADLDYQLANLINSIEERLSllsnyqirydrisqwlQRLEQRVEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWL 11028
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESA----------------QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGS 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11029 LSTSRELLTLYSEPEVRSQVQQQsdsLIDRWQRLKYLAKQKATKIGELKMTLLRLEERIALIRAWLF-------EVESQL 11101
Cdd:TIGR00618 510 CIHPNPARQDIDNPGPLTRRMQR---GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSiltqcdnRSKEDI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11102 DKPLNFESYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDAD-SWRTQVNTSGLAASAQNLEQ-----RWKN 11175
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQcSQELALKLTALHALQLTLTQervreHALS 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11176 VCSQSAERKARILTIWNLLQQLIKLTAEHKNWLGKQESQIAGFERDQKSHSKHkLEERQMELRAKLEELESQSVNLRQLE 11255
Cdd:TIGR00618 667 IRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE-FNEIENASSSLGSDLAAREDALNQSL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11256 QIYAKLAMSAGVEPENIQKLTLPTKVMVSMwrqltprchalLDAIDKDAKLMREFNNAQLEATNSLNAIQKAL--EQLPS 11333
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFNNNEEVTAALQ-----------TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEigQEIPS 814
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442626147 11334 AE-----NQQTSKAEPKAVLQRLESLEKKLQDAQQHVQQADNLAQEAKTRTKQQPQLKQLLE 11390
Cdd:TIGR00618 815 DEdilnlQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4874-5580 |
1.27e-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: 53.14 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4874 FREINQQKENLE--VTMVQWRAYKEEYERLMEWLQQIDILVKNHKlnlcPNLPEKEKQVADMKEVMSRLEKGKDDIDKFN 4951
Cdd:TIGR02168 215 YKELKAELRELElaLLVLRLEELREELEELQEELKEAEEELEELT----AELQELEEKLEELRLEVSELEEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4952 ASAASL---LKSHLDTYVNNQLRHLSSVYQVQVNLAKDVLKKVETNRDQHR------EYDANMKSAKDWIANAKATIQSA 5022
Cdd:TIGR02168 291 YALANEisrLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEleekleELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5023 GEGAGSKEA-----------LQRRLEQIQ-DLIRNRELGQNLVHtainNGEKIIRNTRSDGRDAINTEMKELQTEWDRLV 5090
Cdd:TIGR02168 371 ESRLEELEEqletlrskvaqLELQIASLNnEIERLEARLERLED----RRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5091 KKMSTAKVQLETNLLQWADYSSSYSQLQQWITDREAKLQQA-CEQKIVKSKRGQ-PGLSSGLSERKANLRQTNNI---VQ 5165
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLqARLDSLERLQENlEGFSEGVKALLKNQSGLSGIlgvLS 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5166 DIVSFEP------------MIQSVTSK--------ASVLQQGAPGT----EISDKYENlTKQAKDLyeKQKNTIESYQSL 5221
Cdd:TIGR02168 527 ELISVDEgyeaaieaalggRLQAVVVEnlnaakkaIAFLKQNELGRvtflPLDSIKGT-EIQGNDR--EILKNIEGFLGV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5222 IDAGNEFATWLRNAKERLSKCSEPTGDKQALAEKTHQLK------ILQGEL--PEGAQKLKNALEQGEIACRSAEPEDCE 5293
Cdd:TIGR02168 604 AKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRpgyrivTLDGDLvrPGGVITGGSAKTNSSILERRREIEELE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5294 iieQEVALLQEEFDAYREALNKAK-------DYLEVGIVKWSDYQDQYTEALEWLSKTEALVQSYNKLQDSL-------- 5358
Cdd:TIGR02168 684 ---EKIEELEEKIAELEKALAELRkeleeleEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLskeltele 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5359 IQKKVVLEQFQGHLQTLFDWQKTLDDLNMKAQVLLETCSDTRisNAIMQLTTKYNALLTLAKEVMRRLEMHYQEHQQHHS 5438
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR--EALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5439 LYEECQSWIEKTREKLS----ECEQIPGTLNEVQIKLNTVKNLRQGFETGQNKLRYLLELKEKVIMNTEQNgAAKIQEDT 5514
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIEslaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK-RSELRREL 917
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626147 5515 EALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKL-YKILIEWLEDVEPSVKTSDEFLNDLSEKRAAL 5580
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
10973-11186 |
1.45e-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: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10973 YQIRYDRISQWLQRLEQRVEKDADVTAMTNPEQAAKQLeQQVNSELQLRDKEREWLLSTSRELLTLYSEPEvrSQVQQQS 11052
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKH-EALEAELAAHEERVEALNELGEQLIEEGHPDA--EEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11053 DSLIDRWQRLKYLAKQKATKIGELKMTLLRLEErIALIRAWLFEVESQLDKPLNFESYTPnvIEAKLKEHEQIQRSIEHH 11132
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLES--VEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442626147 11133 SSNVGEVLNLVEMLLNDAdswrTQVNTSGLAASAQNLEQRWKNVCSQSAERKAR 11186
Cdd:cd00176 159 EPRLKSLNELAEELLEEG----HPDADEEIEEKLEELNERWEELLELAEERQKK 208
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
11080-11289 |
1.70e-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: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11080 LLRLEERIALIRAWLFEVESQLDKPLNfeSYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDAdswrtQVNT 11159
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDY--GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-----HPDA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11160 SGLAASAQNLEQRWKNVCSQSAERKARILTIWNLLQQLIKLTAEhKNWLGKQESQIAgfeRDQKSHSKHKLEERQMELRA 11239
Cdd:cd00176 75 EEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-EQWLEEKEAALA---SEDLGKDLESVEELLKKHKE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442626147 11240 KLEELESQSVNLRQLEQIYAKLAMSAgvEPENIQKLTLPTKVMVSMWRQL 11289
Cdd:cd00176 151 LEEELEAHEPRLKSLNELAEELLEEG--HPDADEEIEEKLEELNERWEEL 198
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3360-4146 |
1.92e-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: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3360 IRQQLRALRtlWDNYTDDLNSATQKIDQCLLQFNEfsiaqdqltkwlkdvdkAMQSHTEPKTTLQEKRAQLQNHKLLHQE 3439
Cdd:TIGR02168 218 LKAELRELE--LALLVLRLEELREELEELQEELKE-----------------AEEELEELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3440 I-TTHNVLVDNVCDKAQILvdQIKDNSLNVYLTSIKQLFQSIVQKSDEILHNLddcvQKHNELNNALSSAKTWISNEKAK 3518
Cdd:TIGR02168 279 LeEEIEELQKELYALANEI--SRLEQQKQILRERLANLERQLEELEAQLEELE----SKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3519 LLECDDAYGEKADIKRKIETLGQLAQNKPQAMKiiSDIRDLFEKVkattsekgnEVLDKEIEELETTmkshfddIEGIEG 3598
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLR--SKVAQLELQI---------ASLNNEIERLEAR-------LERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3599 KQKDVLAQWDKFEKALEELTKWCRSAEAVFREQQLQSTLHEKVEQLEKYKIQRELILQKEKEIDAFGDAAHALLNncgad 3678
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA----- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3679 RLKTLTTqITNRYQLLQVLSKEVVNRWSNLVDDHQFYQDKYnEVDlwlQPIESQMAKVLldeptqSSNILQVLLSEKEQA 3758
Cdd:TIGR02168 490 RLDSLER-LQENLEGFSEGVKALLKNQSGLSGILGVLSELI-SVD---EGYEAAIEAAL------GGRLQAVVVENLNAA 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3759 ESLFAAL--NAAGEKALPETSTQGREKIRKDLRDIRDRWDKLDEGIRNLEKRQEAqgvqlssYQDILNqtvNWLDQVekL 3836
Cdd:TIGR02168 559 KKAIAFLkqNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK-------LRKALS---YLLGGV--L 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3837 IHNenpaSWTSAQEIRSKL-YKYKATNQD---INSHKRIVEAVNEKAAALLG------------SAAPANADEISKAVAE 3900
Cdd:TIGR02168 627 VVD----DLDNALELAKKLrPGYRIVTLDgdlVRPGGVITGGSAKTNSSILErrreieeleekiEELEEKIAELEKALAE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3901 VNKRYDQVGQDCAKLVADLDgafDVYQQFSELQKaqqDYQKNLWDRLTGYSDYSGNKAALQARLQKINEIQDALPEGVAK 3980
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELE---ELSRQISALRK---DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3981 LKSLEDHIEQQASNIparskEVMARDLANLHADFEKFGASLSDVKSGLENRLQQWNDYEINLDRLITWLGEAENSLknyn 4060
Cdd:TIGR02168 777 LAEAEAEIEELEAQI-----EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI---- 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4061 lkssfEEKEEQLngfQSLAQNLRQNEADFDKVKDDTSELVQSSGEtrIAVNVQQVSSRFQSIQATAKEILKKCEQAVQDH 4140
Cdd:TIGR02168 848 -----EELSEDI---ESLAAEIEELEELIEELESELEALLNERAS--LEEALALLRSELEELSEELRELESKRSELRREL 917
|
....*.
gi 442626147 4141 GHFNDK 4146
Cdd:TIGR02168 918 EELREK 923
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
273-380 |
2.02e-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: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 273 QKKTFTNWINSYL-----LKRVPPLR--IDDLINDLRDGTKLIALLEVLS----GERLPVEKGRVLRRPHflSNANTALQ 341
Cdd:cd21292 25 EKVAFVNWINKNLgddpdCKHLLPMDpnTDDLFEKVKDGILLCKMINLSVpdtiDERAINKKKLTVFTIH--ENLTLALN 102
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 442626147 342 FLASKRIKLVNINPADLVDGRPPVVLGLIWTII---LYFQIE 380
Cdd:cd21292 103 SASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIrigLFADIE 144
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5752-5959 |
2.06e-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: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5752 WQTFLQKFNKINLWIETMNKRVTKSQegenkTPEDLVNAKKLLE-------EVLAEKDNVEDLNDNCELLMEQS--ACTR 5822
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTD-----YGDDLESVEALLKkhealeaELAAHEERVEALNELGEQLIEEGhpDAEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5823 IRDQTIETQANYTKLLTSAQGLVAKIEKNLSDHtEFLNYKKEMDAWIEKAQQVLDDCSTDGDAAIIAQKLDTVNSLASRL 5902
Cdd:cd00176 77 IQERLEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442626147 5903 PEGQHLLALVQDAYSKASNITPEDKQEKLRELMTKVREDWDALGLAVKQKLSDLKQA 5959
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
10464-10928 |
2.26e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10464 IDQQMDAVKSLEQPLDALQHAkvcQDNLTTQNDRILELRDIVAKIAADVGLDASALMQGELDALGQRLAECKDAITTLAN 10543
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAEL---QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10544 VAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVAS 10623
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10624 SDDDGILEVLALWQKIfQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLCAihqnll 10703
Cdd:COG4717 230 EQLENELEAAALEERL-KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK------ 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10704 isqqsvlsetplESELSEQYKALTNLHNETLSRIMQRNG-ELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHL 10782
Cdd:COG4717 303 ------------EAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10783 KRVPHLKH-------RLDAMIQQLDQGEQQSKALQEQQQELARHCDDALATAMRMEQASIGQRISNLRAALktwqgflqr 10855
Cdd:COG4717 371 EIAALLAEagvedeeELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEEL--------- 441
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626147 10856 vtqlsESYEQRVNQLQQEFGAAQKLLDA--NSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELKE 10928
Cdd:COG4717 442 -----EELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7564-7767 |
2.60e-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: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7564 EYVDGVDEVQRWLLQAEVQVQERSL--TPTQMKELLQR---INHEITAIYERFTLVKTNGQLIIEncRNSEEKTLVQTTI 7638
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYgdDLESVEALLKKheaLEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7639 DQLAASLAQVRGWLDEKKQAVGDSLDAWtRFMNLYQIVMSWASEKRNFIDQTIELRTLPEARNKLN---DYVTSVKSIKP 7715
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKkhkELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442626147 7716 IVKHLSEMDKELEHIGQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEA 7767
Cdd:cd00176 161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7355-8093 |
2.85e-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: 51.99 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7355 EKALGRLEDKFRNVDptvRSRRHLEDTKNAIQELREESNQ------LKSSHKEIEA--LSKSIltflgEVHKPSAEAIQA 7426
Cdd:TIGR02169 173 EKALEELEEVEENIE---RLDLIIDEKRQQLERLRREREKaeryqaLLKEKREYEGyeLLKEK-----EALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7427 KVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQL-QDKLNALHEQLQSVHVydeHIAQTEQLLITLNSQVQQAA 7505
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEA---EIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7506 EESKLLVAQTTAhYQAKQNQLPSDIAQEFTALELLAERVQVTMETKEKDFKRAKTVRTEY---VDGVDEVQRWLLQAEVQ 7582
Cdd:TIGR02169 322 ERLAKLEAEIDK-LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFaetRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7583 VQERSLTPTQMKELLQRINHEITAIYERFTLVKtngqliiencrnsEEKTLVQTTIDQLAASLAQVRGWLDEKKQAVGDS 7662
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIE-------------AKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7663 LDAWTRFMNLYQIVMSWASEKRnfidqtielRTLPEARNKLNDYVTSVKSIKPIVKHLSEMDKELehIGQVTTVGDLKDK 7742
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQ---------RELAEAEAQARASEERVRGGRAVEEVLKASIQGV--HGTVAQLGSVGER 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7743 LQEAEDAKIS--VEAVLLERNSLLQEACEEWDQCE---------RKIKDIRSWHEKTKQG--------LDSSQQQKKP-- 7801
Cdd:TIGR02169 537 YATAIEVAAGnrLNNVVVEDDAVAKEAIELLKRRKagratflplNKMRDERRDLSILSEDgvigfavdLVEFDPKYEPaf 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7802 ---LRDQLGFCEKTLA-DINVQKTKLRLSIEKLEVH------FRNGMGGDPRLSENVDDLVRVLDGLGELVKAKSqSLEQ 7871
Cdd:TIGR02169 617 kyvFGDTLVVEDIEAArRLMGKYRMVTLEGELFEKSgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELS-SLQS 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7872 TLAQIdvyQQQMQSLRQRIIQEEQQLRLVMAPTYLPHDRERALAEQQDLITQELDELLQSLSSVEDGIANMNQ--SSLDG 7949
Cdd:TIGR02169 696 ELRRI---ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAriEELEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7950 MLHGLKLIQSNLEVHERDAI--ELKNQAKKLPTD--------PATERLLNDtVDRIDLLLRRTQQGITMIANAMHGQKK- 8018
Cdd:TIGR02169 773 DLHKLEEALNDLEARLSHSRipEIQAELSKLEEEvsriearlREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKs 851
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626147 8019 RQQEIDEYQQHLLELEQWIIEVSAELASFEptsDSSTDeqvLKSQVERSQQLLRTLKDRQQSMEDLVEQTRQLQS 8093
Cdd:TIGR02169 852 IEKEIENLNGKKEELEEELEELEAALRDLE---SRLGD---LKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7032-7235 |
2.96e-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: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7032 ELSEILDWLHSHEGAAKSrPLLDRDPESVERELQKHQSLSQDIESYLNKFNKINDG----VKTEIGMPSSLLEMLSEGRS 7107
Cdd:cd00176 8 DADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELgeqlIEEGHPDAEEIQERLEELNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7108 LVASLPHELEEREKYLKNNRDsRLEYMQLVAKFNDWVHEAELRLQNSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLVhKQ 7187
Cdd:cd00176 87 RWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRL-KS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 442626147 7188 IQEAADKIWSSLNNYEQSELSAELAQFQTKLTNTLANAKTQQSELEKE 7235
Cdd:cd00176 165 LNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1785-1996 |
3.07e-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: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 1785 WQQFQAGLQQIKPAVEQSEVKVNNVVSkPISLEEAVAMQQNAQQFETQCQEQLDKLHGISNISHKmLCKTNAPD------ 1858
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQ-LIEEGHPDaeeiqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 1859 ELDAMHSRWTAVHENAKQASAKLEKLVANWKsFDADAAKLEDWVGQGEQQMSRRPavlNTPHIDKLEKELVKLKSFNNEI 1938
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASED---LGKDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442626147 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 |
3.53e-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: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 1921 IDKLEKELVK-LKSFNNEISQQQAKLVTlgqNADQISLHL--------APEGAAALKDRVNQMKGKLQKLSEATRGHINE 1991
Cdd:TIGR01612 1057 IDEIEKEIGKnIELLNKEILEEAEINIT---NFNEIKEKLkhynfddfGKEENIKYADEINKIKDDIKNLDQKIDHHIKA 1133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 1992 VSDaiISRQDfnaklvnfSNWMEQLRNQVTQVEEI--------NPERVETSLHVIHALLqehaDKKPSfnaIYDEVKQL- 2062
Cdd:TIGR01612 1134 LEE--IKKKS--------ENYIDEIKAQINDLEDVadkaisndDPEEIEKKIENIVTKI----DKKKN---IYDEIKKLl 1196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2063 -ALGATPEESNALNDAYTALVVNYQNLETNMLQ------KKA-----ALEKWTELL--------------GWKNDTESHL 2116
Cdd:TIGR01612 1197 nEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEkideekKKSehmikAMEAYIEDLdeikekspeienemGIEMDIKAEM 1276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2117 NYLK--HQLDKPEGPAAEELSKVIDEIDN----LGQGIgYWKGQAKEIDENPAIQLRDALSRRPLIaTQIVNDVENKLEN 2190
Cdd:TIGR01612 1277 ETFNisHDDDKDHHIISKKHDENISDIREkslkIIEDF-SEESDINDIKKELQKNLLDAQKHNSDI-NLYLNEIANIYNI 1354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2191 LKLRSQSQQQQIQqmtvrKDKFHALEHNFGQALQE--NRAKLDEILRQHPTLNNIDQIIADLV---ALNDALKYQADLKN 2265
Cdd:TIGR01612 1355 LKLNKIKKIIDEV-----KEYTKEIEENNKNIKDEldKSEKLIKKIKDDINLEECKSKIESTLddkDIDECIKKIKELKN 1429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2266 RI----------------HDEGSLLMREDIASMPAIQESLLIMDKN-----YDSLQNEIADRIQKYNlisqalrEYADSK 2324
Cdd:TIGR01612 1430 HIlseesnidtyfknadeNNENVLLLFKNIEMADNKSQHILKIKKDnatndHDFNINELKEHIDKSK-------GCKDEA 1502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2325 DKFSKELKKAEDLY--------------------NAIPQQPRDET-------ELHQA----SEKTRKTMEQLRKSKLSLD 2373
Cdd:TIGR01612 1503 DKNAKAIEKNKELFeqykkdvtellnkysalaikNKFAKTKKDSEiiikeikDAHKKfileAEKSEQKIKEIKKEKFRIE 1582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2374 ELERRGNNVGKlfSAIGEPIPQEvPQEVTAAKqhwqdLHD-KTAKNAHVYETEAV--------IWSQIEDAKK--DLLPW 2442
Cdd:TIGR01612 1583 DDAAKNDKSNK--AAIDIQLSLE-NFENKFLK-----ISDiKKKINDCLKETESIekkissfsIDSQDTELKEngDNLNS 1654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2443 LSETNQGLCDAADNsieIEFGPMRLSKYRTELPSYQALKDS--------IVEKTNDLVKINKGaEIPALSALNKLLSEQF 2514
Cdd:TIGR01612 1655 LQEFLESLKDQKKN---IEDKKKELDELDSEIEKIEIDVDQhkknyeigIIEKIKEIAIANKE-EIESIKELIEPTIENL 1730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2515 AEVNNNAD--------RLSAITTSFNDQEQELRRRSKEAGERVSKLREQLIKCDDMSGD----NNKIMERLQQCRALRGE 2582
Cdd:TIGR01612 1731 ISSFNTNDlegidpneKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITYDEIKNTrinaQNEFLKIIEIEKKSKSY 1810
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2583 LDN-SGNEIDNI----KQKVDELRNLYpTFSESIIPKELNNVQKRYENVDLYAKkiESSLLQFLKKFHADKVGMLKRIIA 2657
Cdd:TIGR01612 1811 LDDiEAKEFDRIinhfKKKLDHVNDKF-TKEYSKINEGFDDISKSIENVKNSTD--ENLLFDILNKTKDAYAGIIGKKYY 1887
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2658 TQREKVAWCQPESSSDKYNLDVKKSSlqevSKSIDDCKARHAETLKSL-----EMLKAVESPQNLAEL-----TSDAELL 2727
Cdd:TIGR01612 1888 SYKDEAEKIFINISKLANSINIQIQN----NSGIDLFDNINIAILSSLdsekeDTLKFIPSPEKEPEIytkirDSYDTLL 1963
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2728 R--KDMQALQDSFDQIKGILDENVDLWSQYEQSNEqisnwLRDVEGRVKAETSSQVN-LSEVPQKLQELSILQQDVLAHE 2804
Cdd:TIGR01612 1964 DifKKSQDLHKKEQDTLNIIFENQQLYEKIQASNE-----LKDTLSDLKYKKEKILNdVKLLLHKFDELNKLSCDSQNYD 2038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2805 PIinnLEQTSQQLI-------EKNPEARIGQF-VTHLVQRYQAVSKALTSYIDKIRGAQLSNANFAKaAKDFNEWFGDAK 2876
Cdd:TIGR01612 2039 TI---LELSKQDKIkekidnyEKEKEKFGIDFdVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDFSE-EKDNIIQSKKKL 2114
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2877 IEFQELARMGSPGSSSATAQQLQTVKNYIKTfdNGQILLNNAVDIGEALYPVVSpDNRERIRADLRQMREKFDYLRDEAN 2956
Cdd:TIGR01612 2115 KELTEAFNTEIKIIEDKIIEKNDLIDKLIEM--RKECLLFSYATLVETLKSKVI-NHSEFITSAAKFSKDFFEFIEDISD 2191
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2957 AFMQQVEGVliqktsieesytQVSHYLNESKAKVPT-----TDELYPTLATKKAALQ--NYKTQLQEITLHKNALKQLHD 3029
Cdd:TIGR01612 2192 SLNDDIDAL------------QIKYNLNQTKKHMISiladaTKDHNNLIEKEKEATKiiNNLTELFTIDFNNADADILHN 2259
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3030 KAVTLCDDESE-RKTDESIQE-------------------YNTLSKKIsDRITTVGNHVVKHEAYDqvLEKAQDWLNTIK 3089
Cdd:TIGR01612 2260 NKIQIIYFNSElHKSIESIKKlykkinafkllnishinekYFDISKEF-DNIIQLQKHKLTENLND--LKEIDQYISDKK 2336
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3090 SEAIDILNETT-FEKEGAEEkllVVENLLQHKPEGDSIFDTCHKLLETVLTQTHPsghpalLKGFEEPKQSWEDFMTLCQ 3168
Cdd:TIGR01612 2337 NIFLHALNENTnFNFNALKE---IYDDIINRENKADEIENINNKENENIMQYIDT------ITKLTEKIQDILIFVTTYE 2407
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3169 DSLVKLKQLCSKWDEFDtIIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINELMDQGREIEGE 3248
Cdd:TIGR01612 2408 NDNNIIKQHIQDNDEND-VSKIKDNLKKTIQSFQEILNKIDEIKAQFYGGNNINNIIITISQNANDVKNHFSKDLTIENE 2486
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3249 tdlnlkLSRLNTRYQTLKNLC----KESIAKYVNYVKDHesFDKDFDSFKQNlqSSVDELAKTNEIvgdQSVLQDQQNKL 3324
Cdd:TIGR01612 2487 ------LIQIQKRLEDIKNAAheirSEQITKYTNAIHNH--IEEQFKKIENN--SNKDEVYKINEI---DNIIEKIINYN 2553
|
..
gi 442626147 3325 RE 3326
Cdd:TIGR01612 2554 KE 2555
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6973-7943 |
3.96e-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: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6973 ASANDKGQKIASEGNAADKNSITEQLQSLKNQLQNLRKAV-ESQRQKHQLQLESHKKmAAELSEILDWLHShegaaksrp 7051
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALLVLRLEELREELEELQEELkEAEEELEELTAELQEL-EEKLEELRLEVSE--------- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7052 lLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEIGMPSSLLEMLSEGRSLVASLPHELEEREKYLKNNRDSRL 7131
Cdd:TIGR02168 279 -LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7132 EymqLVAKFNDWVHEAELRLQNSQhgidyehlvqdldehkiffgneapirnlvhKQIQEAADKIwsslnnyeqselsAEL 7211
Cdd:TIGR02168 358 A---ELEELEAELEELESRLEELE------------------------------EQLETLRSKV-------------AQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7212 AQFQTKLTNTLANAKTQQSELEKEAERWREYQQSIDRVKATiertkfvdepvQNLAGLHFNIQKLSHAIGNVQSQNSDLt 7291
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE-----------AELKELQAELEELEEELEELQEELERL- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7292 lvnQQAQSLIRQADARNRQLIEQDNAGLNRSwQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFrNVDpt 7371
Cdd:TIGR02168 460 ---EEALEELREELEEAEQALDAAERELAQL-QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI-SVD-- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7372 vrsrrhlEDTKNAIQELREESNQ------LKSSHKEIEALSKSIL---TFLgEVHKPSAEAIQAKVDKLVEQQaklndtl 7442
Cdd:TIGR02168 533 -------EGYEAAIEAALGGRLQavvvenLNAAKKAIAFLKQNELgrvTFL-PLDSIKGTEIQGNDREILKNI------- 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7443 rDKEQQVSKDLEEIEqvfrriSQLQDKLNALheqLQSVHVYDEhIAQTEQLLITLNSQVQQAAEESKLL---------VA 7513
Cdd:TIGR02168 598 -EGFLGVAKDLVKFD------PKLRKALSYL---LGGVLVVDD-LDNALELAKKLRPGYRIVTLDGDLVrpggvitggSA 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7514 QTTAHYQAKQNQLpSDIAQEFTALELLAERVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQM 7593
Cdd:TIGR02168 667 KTNSSILERRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7594 KELLQRINHEITAIYERFTLVKTN-GQLIIENCRNSEEKTLVQTTIDQLAASLAQVRGWLDEKKQAVGDSLDAWTRFMNL 7672
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7673 YQivmswaSEKRNFIDQTIELRTLpearnklndyvtsVKSIKPIVKHLSEMDKELEHigQVTTVGDLKDKLQEAEDAKIS 7752
Cdd:TIGR02168 826 LE------SLERRIAATERRLEDL-------------EEQIEELSEDIESLAAEIEE--LEELIEELESELEALLNERAS 884
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7753 VEAVLLERNSLLQEACEEWDQCERKIKDirswhektkqgldssqqqkkpLRDQLGFCEKTLADINVQKTKLRLSIEKLEv 7832
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSE---------------------LRRELEELREKLAQLELRLEGLEVRIDNLQ- 942
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7833 hfrngmggdPRLSENVDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRlvmaptylphdrer 7912
Cdd:TIGR02168 943 ---------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELK-------------- 999
|
970 980 990
....*....|....*....|....*....|.
gi 442626147 7913 alaEQQDLITQELDELLQSLSSVEDGIANMN 7943
Cdd:TIGR02168 1000 ---ERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
7384-7610 |
4.01e-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: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7384 AIQELREESNQLKSSHKEIEALSKSIltflgEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRI 7463
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKEL-----AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7464 SQLQDKLNALHEQLQSVHVYDEHIAQTEQLLITLNSQ-VQQAAEESKLLvaqttAHYQAKQNQLPSDIAQEFTALELLAE 7542
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEdFLDAVRRLQYL-----KYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442626147 7543 RVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELLQRINHEITAIYER 7610
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1047-1245 |
4.17e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 49.37 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 1047 KEIHQWLSEAEQLLGTHNLSGGRDAINEQLHKHKTYfsrtvyYRSMLESKNKV--FQNLLKAVSSDDKIDTAPASQQMQQ 1124
Cdd:cd00176 10 DELEAWLSEKEELLSSTDYGDDLESVEALLKKHEAL------EAELAAHEERVeaLNELGEQLIEEGHPDAEEIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 1125 LNERFNYVIQNAQQWEQRLDSAAGGWSNFKDnERVVSEWLTQAESMLV-EKHIESKTTIETQKYFFEQV------NDRWM 1197
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALAsEDLGKDLESVEELLKKHKELeeeleaHEPRL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 442626147 1198 NDLVQSAQQLLTTLPAQEQPAVVHSVEQLQSRWKNVLSQAPLHLLKLE 1245
Cdd:cd00176 163 KSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
6787-7838 |
5.41e-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: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6787 NADKLKLNDDIKNMKDRYGRIKNTID-----DRVNALGDHIKK----------------YKDAKSRLAECSQ-------- 6837
Cdd:TIGR01612 599 NKLKLELKEKIKNISDKNEYIKKAIDlkkiiENNNAYIDELAKispyqvpehlknkdkiYSTIKSELSKIYEddidalyn 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6838 FLGNIQQ-----------KLRELNRPIGSRIEDVQDLLGA-YEGILKELKDSKSKMGDMQMDDLPELQSILAQqdDMIKL 6905
Cdd:TIGR01612 679 ELSSIVKenaidntedkaKLDDLKSKIDKEYDKIQNMETAtVELHLSNIENKKNELLDIIVEIKKHIHGEINK--DLNKI 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6906 IEDQLAHLRQLLLLREQFIALINEIIAFIMKYTDV------IIDIENSPDslEDKINKYDdvivKIQECEGVLASANDKG 6979
Cdd:TIGR01612 757 LEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIknhyndQINIDNIKD--EDAKQNYD----KSKEYIKTISIKEDEI 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6980 QKIASEGNAAdKNSITEQLQSLKNQLQNLRKAVESQrqkHQLQLESHKKMAAELSEilDWLHSHEGAAK-SRPLLDRDPE 7058
Cdd:TIGR01612 831 FKIINEMKFM-KDDFLNKVDKFINFENNCKEKIDSE---HEQFAELTNKIKAEISD--DKLNDYEKKFNdSKSLINEINK 904
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7059 SVERELQKHQSL-------------SQDIESYLNKFNKINDGVKTEIGM--PSSLLEMlSEGRSLVASLPHELEEREKYL 7123
Cdd:TIGR01612 905 SIEEEYQNINTLkkvdeyikicentKESIEKFHNKQNILKEILNKNIDTikESNLIEK-SYKDKFDNTLIDKINELDKAF 983
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7124 KNNRDSRLEYM--QLVAKFNDWVHEAELRLQNSqhgidyehLVQDLDEHKIFFGN-EAPIRNlVHKQIQEAADKIWSSLN 7200
Cdd:TIGR01612 984 KDASLNDYEAKnnELIKYFNDLKANLGKNKENM--------LYHQFDEKEKATNDiEQKIED-ANKNIPNIEIAIHTSIY 1054
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7201 NYEQsELSAELAQFQTKL-TNTLANAKTQQSELEKEAERWREYQQSiDRVKAtiERTKFVDEPVQNLAGLHFNIQKLSHA 7279
Cdd:TIGR01612 1055 NIID-EIEKEIGKNIELLnKEILEEAEINITNFNEIKEKLKHYNFD-DFGKE--ENIKYADEINKIKDDIKNLDQKIDHH 1130
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7280 IGNVQS-QNSDLTLVNQQAQSLIRQADARNRQLIEQDNAGLNRSWQDLVRSLEQRR---DNLQQLAEHWDGFENSLHAWE 7355
Cdd:TIGR01612 1131 IKALEEiKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKniyDEIKKLLNEIAEIEKDKTSLE 1210
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7356 KA---------------LGRLEDKFRNVDPTVRSR----RHLEDTKNAIQELREESNQLKSSHKEIEALSKSILTF---- 7412
Cdd:TIGR01612 1211 EVkginlsygknlgklfLEKIDEEKKKSEHMIKAMeayiEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDkdhh 1290
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7413 -LGEVHKPSAEAIQAKVDKLVE---QQAKLNDTLRDKEQQVS---KDLEEIEQVFRRISQLQD--KLNALHEQLQSVHVY 7483
Cdd:TIGR01612 1291 iISKKHDENISDIREKSLKIIEdfsEESDINDIKKELQKNLLdaqKHNSDINLYLNEIANIYNilKLNKIKKIIDEVKEY 1370
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7484 DEHIAQTeqllitlNSQVQQAAEESKLLVAQTtahyqakqnqlpsdiaQEFTALELLAERVQVTMETKEKDfkraktvrt 7563
Cdd:TIGR01612 1371 TKEIEEN-------NKNIKDELDKSEKLIKKI----------------KDDINLEECKSKIESTLDDKDID--------- 1418
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7564 EYVDGVDEVQRWLLQAEVQVQersltpTQMKElLQRINHEITAIYERFTLVKTNGQLIIENCRNSEEKTLvQTTIDQLAA 7643
Cdd:TIGR01612 1419 ECIKKIKELKNHILSEESNID------TYFKN-ADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDH-DFNINELKE 1490
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7644 SLAQVRGWLDE---KKQAVGDSLDAWTRFMNLYQIVMS--WASEKRNFIDQT-----IELRTLPEARNKLN-DYVTSVKS 7712
Cdd:TIGR01612 1491 HIDKSKGCKDEadkNAKAIEKNKELFEQYKKDVTELLNkySALAIKNKFAKTkkdseIIIKEIKDAHKKFIlEAEKSEQK 1570
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7713 IKPIVKHLSEMDKELEH--------IGQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEACE-EWDQCERKIKDIRS 7783
Cdd:TIGR01612 1571 IKEIKKEKFRIEDDAAKndksnkaaIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSfSIDSQDTELKENGD 1650
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*
gi 442626147 7784 WHEKTKQGLDSSQQQKKPLRDQlgfcEKTLADINVQKTKLRLSIEKLEVHFRNGM 7838
Cdd:TIGR01612 1651 NLNSLQEFLESLKDQKKNIEDK----KKELDELDSEIEKIEIDVDQHKKNYEIGI 1701
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3183-3271 |
6.21e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 46.17 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3183 EFDTIIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINELMDQGREI-----EGETDLNLKLSR 3257
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeghPDAEEIEERLEE 81
|
90
....*....|....
gi 442626147 3258 LNTRYQTLKNLCKE 3271
Cdd:smart00150 82 LNERWEELKELAEE 95
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4034-4226 |
6.44e-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: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4034 QWNDYEINLDRLITWLGEAENSLKNYNLKSSFEEKEEQLNGFQSLAQNLRQNEADFDKVKDDTSELVQSSGE--TRIAVN 4111
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPdaEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4112 VQQVSSRFQSIQATAKEILKKCEQAVQDHGHFNDkYKQCADWLANAQARYDDCCDLSTVASRDDLLKKQvviQELLAQQP 4191
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLESVEELLKKH---KELEEELE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 442626147 4192 TATQLLNSTVELGEKCYGSTATEGREAIRSQLDDL 4226
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEEL 191
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
9080-9207 |
6.97e-05 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 49.94 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 9080 QQTTPRIPSPTEKSEVEQDIKSVQTSPQHQPKLDETAVQTSLEVQP------DNQENESQTLIVEITETEA--------- 9144
Cdd:PRK10905 82 QGQTPVATDGQQRVEVQGDLNNALTQPQNQQQLNNVAVNSTLPTEPatvapvRNGNASRQTAKTQTAERPAttrparkqa 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 9145 -------QTTPRSEEQSVAVEISTTEIQTDVSGQPAETVEISSQTTVTTTIEKELQTTPKDSPRAPEAGS 9207
Cdd:PRK10905 162 viepkkpQATAKTEPKPVAQTPKRTEPAAPVASTKAPAATSTPAPKETATTAPVQTASPAQTTATPAAGG 231
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2067-3607 |
7.26e-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: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2067 TPEESNALNDAYTalvvnyQNLETNMLQKKAALEKW-------------TELLGWKNDTESHL-----NYLKHQLDKPEg 2128
Cdd:TIGR01612 953 TIKESNLIEKSYK------DKFDNTLIDKINELDKAfkdaslndyeaknNELIKYFNDLKANLgknkeNMLYHQFDEKE- 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2129 paaEELSKVIDEIDNLGQGIgywkgqakeidenPAIQLrdalsrrpLIATQIVNDVEnKLENL------KLRSQSQQQQI 2202
Cdd:TIGR01612 1026 ---KATNDIEQKIEDANKNI-------------PNIEI--------AIHTSIYNIID-EIEKEigknieLLNKEILEEAE 1080
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2203 QQMTVRKDKFHALEH-NFGQALQENRAKL-DEILRQHPTLNNIDQII-ADLVAL----NDALKYQADLKNRIHD----EG 2271
Cdd:TIGR01612 1081 INITNFNEIKEKLKHyNFDDFGKEENIKYaDEINKIKDDIKNLDQKIdHHIKALeeikKKSENYIDEIKAQINDledvAD 1160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2272 SLLMREDIASMPAIQESLLI-MDK------NYDSLQNEIA---------DRIQKYNL-----ISQALREYADSKDKFSKE 2330
Cdd:TIGR01612 1161 KAISNDDPEEIEKKIENIVTkIDKkkniydEIKKLLNEIAeiekdktslEEVKGINLsygknLGKLFLEKIDEEKKKSEH 1240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2331 LKKA-----EDLYNAIPQQPRDETEL-----------------------HQASEKTRKTMEQLRKSKLSLDELERRGNNV 2382
Cdd:TIGR01612 1241 MIKAmeayiEDLDEIKEKSPEIENEMgiemdikaemetfnishdddkdhHIISKKHDENISDIREKSLKIIEDFSEESDI 1320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2383 GKlfsaigepIPQEVPQEVTAAKQHWQDLHDKTAKNAHVYETEAV-IWSQIEDAKKDLLPWLSETNQGLCDAADNSieie 2461
Cdd:TIGR01612 1321 ND--------IKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLnKIKKIIDEVKEYTKEIEENNKNIKDELDKS---- 1388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2462 fgpMRLSKYRTELPSYQALKdSIVEKTNDLVKINKGAEIPALSAlNKLLSEqfaEVNN-----NADRLSA-ITTSFNDQE 2535
Cdd:TIGR01612 1389 ---EKLIKKIKDDINLEECK-SKIESTLDDKDIDECIKKIKELK-NHILSE---ESNIdtyfkNADENNEnVLLLFKNIE 1460
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2536 ------QELRRRSKEAGE-----RVSKLREQLIK---CDDMSGDNNKIMER----LQQCRALRGELDNSGNEIDnIKQKV 2597
Cdd:TIGR01612 1461 madnksQHILKIKKDNATndhdfNINELKEHIDKskgCKDEADKNAKAIEKnkelFEQYKKDVTELLNKYSALA-IKNKF 1539
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2598 DELRNlyptfSESIIPKELNNVQKRYEnvdLYAKKIEssllQFLKKFHADKVGMLKRIIATQREKVAWCQPESSSDkyNL 2677
Cdd:TIGR01612 1540 AKTKK-----DSEIIIKEIKDAHKKFI---LEAEKSE----QKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLE--NF 1605
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2678 DVKKSSLQEVSKSIDDCKARHAETLKSLEMLKAVESPQNLAELTSDAELLRKDMQALQDsfdQIKGILDENVDLwsqyEQ 2757
Cdd:TIGR01612 1606 ENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKENGDNLNSLQEFLESLKD---QKKNIEDKKKEL----DE 1678
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2758 SNEQISNWLRDVEGRVKaetSSQVNLSEvpqKLQELSILQQdvlahepiiNNLEQTsQQLIEKNPEARIGQFVTHlvqry 2837
Cdd:TIGR01612 1679 LDSEIEKIEIDVDQHKK---NYEIGIIE---KIKEIAIANK---------EEIESI-KELIEPTIENLISSFNTN----- 1737
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2838 qavskaltsyidkirgaQLSNANFAKAAKDFNEWFGDAKIEFQELARMgspgsssaTAQQLQTVKNYIKTFDNgqiLLNN 2917
Cdd:TIGR01612 1738 -----------------DLEGIDPNEKLEEYNTEIGDIYEEFIELYNI--------IAGCLETVSKEPITYDE---IKNT 1789
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2918 AVDIGEALYPVVSPDNRERIRADLRQMREkFDYLRDEANAFMQQVEGVLIQKTS-IEESYTQVSHYLNESKAkvpTTDE- 2995
Cdd:TIGR01612 1790 RINAQNEFLKIIEIEKKSKSYLDDIEAKE-FDRIINHFKKKLDHVNDKFTKEYSkINEGFDDISKSIENVKN---STDEn 1865
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2996 -LYPTLATKKAALQN--------YKTQLQEITLHK-----------------NALKQLHDKAVTLCDDESER--KTDESI 3047
Cdd:TIGR01612 1866 lLFDILNKTKDAYAGiigkkyysYKDEAEKIFINIsklansiniqiqnnsgiDLFDNINIAILSSLDSEKEDtlKFIPSP 1945
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3048 QEYNTLSKKISDRITTVGNhVVKHEAYDQvlEKAQDWLNTI------------KSEAIDILNETTFEKEgaeeKLLVVEN 3115
Cdd:TIGR01612 1946 EKEPEIYTKIRDSYDTLLD-IFKKSQDLH--KKEQDTLNIIfenqqlyekiqaSNELKDTLSDLKYKKE----KILNDVK 2018
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3116 LLQHKpegdsiFDTCHKL------LETVLTQTHPSGHPALLKGFEEPKQSwedfmtLCQDSLVKLKQlcSKWDEFDTIIE 3189
Cdd:TIGR01612 2019 LLLHK------FDELNKLscdsqnYDTILELSKQDKIKEKIDNYEKEKEK------FGIDFDVKAME--EKFDNDIKDIE 2084
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3190 ELDNWMKNVEA------------VVKNQNLKSTAEAKNAHLKQLQDisKDIERrgaaiNELMDQGREIEGETdlnlklsr 3257
Cdd:TIGR01612 2085 KFENNYKHSEKdnhdfseekdniIQSKKKLKELTEAFNTEIKIIED--KIIEK-----NDLIDKLIEMRKEC-------- 2149
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3258 LNTRYQTLKNLCKESIAKYVNYVKDHESFDKDFDSFKQNLQSSVDElaktneivgDQSVLQDQQNkLREMsdKRILDSTL 3337
Cdd:TIGR01612 2150 LLFSYATLVETLKSKVINHSEFITSAAKFSKDFFEFIEDISDSLND---------DIDALQIKYN-LNQT--KKHMISIL 2217
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3338 FEGLIDRGEklyghtspegreIIRQQLRALRTLwDNYTDDLNSATQKIDQCLLQFNEFsiaqdQLTKWLKDVDKAMQSht 3417
Cdd:TIGR01612 2218 ADATKDHNN------------LIEKEKEATKII-NNLTELFTIDFNNADADILHNNKI-----QIIYFNSELHKSIES-- 2277
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3418 ePKTTLQEKRA-QLQNHKLLHQEITTHNVLVDNVCdkaqilvdQIKDNSLNVYLTSIKQLFQSIVQKSDEILHNLDDCVq 3496
Cdd:TIGR01612 2278 -IKKLYKKINAfKLLNISHINEKYFDISKEFDNII--------QLQKHKLTENLNDLKEIDQYISDKKNIFLHALNENT- 2347
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3497 khNELNNALSSAKTWISNEKAKLLECDDAYG-EKADIKRKIETLGQLAQNkpqamkiisdIRDLFEKVkaTTSEKGNEVL 3575
Cdd:TIGR01612 2348 --NFNFNALKEIYDDIINRENKADEIENINNkENENIMQYIDTITKLTEK----------IQDILIFV--TTYENDNNII 2413
|
1690 1700 1710 1720
....*....|....*....|....*....|....*....|
gi 442626147 3576 DKEIEE--------LETTMKSHFDDIEGIEGKQKDVLAQW 3607
Cdd:TIGR01612 2414 KQHIQDndendvskIKDNLKKTIQSFQEILNKIDEIKAQF 2453
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
10755-11124 |
1.06e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.30 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10755 RQQLAALLDwLRQREAERNALQ------LRYihLKRVPHLKHRLDAMIQQLDQGEQQskaLQEQQQELARHCDDALATAm 10828
Cdd:PRK11281 42 QAQLDALNK-QKLLEAEDKLVQqdleqtLAL--LDKIDRQKEETEQLKQQLAQAPAK---LRQAQAELEALKDDNDEET- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10829 rmeqasiGQRISNLRaalktwqgflqrVTQLsesyEQRVNQLQQEFGAAQK-LLDANSE--SLPTQPAaieqllgslRAQ 10905
Cdd:PRK11281 115 -------RETLSTLS------------LRQL----ESRLAQTLDQLQNAQNdLAEYNSQlvSLQTQPE---------RAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10906 RVQLGAQVSALE--SLTVTQEELKECISPhdmktiRQRNWLLWQQHAdLDYQLANLINSIEERLSLLSNYQIRYDRISQW 10983
Cdd:PRK11281 163 AALYANSQRLQQirNLLKGGKVGGKALRP------SQRVLLQAEQAL-LNAQNDLQRKSLEGNTQLQDLLQKQRDYLTAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10984 LQRLEQRVEKDADVTAMTNPEQAAKQLEQQVNS--------------ELQLRDKEREWLLSTSRELLTLySEPEVRsqVQ 11049
Cdd:PRK11281 236 IQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQdeaariqanplvaqELEINLQLSQRLLKATEKLNTL-TQQNLR--VK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11050 QQSDSLIDRWQRLKylakqkaTKIGELKMTLL-------------------RLEERIALIRAWLFEVESQLDKPLNFESY 11110
Cdd:PRK11281 313 NWLDRLTQSERNIK-------EQISVLKGSLLlsrilyqqqqalpsadlieGLADRIADLRLEQFEINQQRDALFQPDAY 385
|
410
....*....|....
gi 442626147 11111 tpnvIEAKLKEHEQ 11124
Cdd:PRK11281 386 ----IDKLEAGHKS 395
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5070-5802 |
1.07e-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: 50.06 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5070 DGRDAINTEMKELQTEWDRLVKKMSTAKVQLETNLLQWADYSSSYSQLQQWITDREAKLQQACEQKIVKSKRGQPGLSS- 5148
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQl 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5149 -GLSERKANLRQTNNIVQDIV-SFEPMIQSVtsKASVLQQGAPGTEISDKYENLTKQAKDLYEK----QKNTIESYQSLI 5222
Cdd:TIGR02168 319 eELEAQLEELESKLDELAEELaELEEKLEEL--KEELESLEAELEELEAELEELESRLEELEEQletlRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5223 DAGNEFATwLRNAKERLSKCSEPTGDKQALAEK---THQLKILQGELPEGAQKLKNALEQGEiacrsAEPEDCEIIEQEV 5299
Cdd:TIGR02168 397 SLNNEIER-LEARLERLEDRRERLQQEIEELLKkleEAELKELQAELEELEEELEELQEELE-----RLEEALEELREEL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5300 ALLQEEFDAYREALNKAK---DYLEVGIVKWSDYQDQYTEALEWLSKTEALV---------------------------- 5348
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQarlDSLERLQENLEGFSEGVKALLKNQSGLSGILgvlselisvdegyeaaieaalggrlqav 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5349 -----QSYNKLQDSLIQKKV----------------------VLEQFQGHLQTLFDWQKTLDDLNMKAQVLLETC---SD 5398
Cdd:TIGR02168 551 vvenlNAAKKAIAFLKQNELgrvtflpldsikgteiqgndreILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvDD 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5399 TRISNAIMQLTTKYNALLTLAKEVMRRLEMHYQEHQQHHSLYEECQSWIEKTREKLsecEQIPGTLNEVQIKLNTVKNLR 5478
Cdd:TIGR02168 631 LDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKI---EELEEKIAELEKALAELRKEL 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5479 QGFETGQNKLRYLLELKEKVIMNTEQNgAAKIQEDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILIEWLED 5558
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKD-LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5559 VEPSVKTSDEFLND----LSEKRAAL----EKFRVIQRDINGHNDIVEKINQRL------KEDNSLDLKDFQPGLTKFDD 5624
Cdd:TIGR02168 787 LEAQIEQLKEELKAlreaLDELRAELtllnEEAANLRERLESLERRIAATERRLedleeqIEELSEDIESLAAEIEELEE 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5625 LQTQVNKIIESLENQVNSHEKYKQAYNELQDWLRRTRIEVEQcadchgEKDQVESRLNRLGDIQSSSLEGKALLEACEEL 5704
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELES------KRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5705 SQAVIAtsgSEGQDNvAQEIKHLTSEWETLQTISRDARSSLESCLAAwqtflqkFNKINLWIETMNKRVTKSQEGENKTP 5784
Cdd:TIGR02168 941 LQERLS---EEYSLT-LEEAEALENKIEDDEEEARRRLKRLENKIKE-------LGPVNLAAIEEYEELKERYDFLTAQK 1009
|
810
....*....|....*...
gi 442626147 5785 EDLVNAKKLLEEVLAEKD 5802
Cdd:TIGR02168 1010 EDLTEAKETLEEAIEEID 1027
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7200-7470 |
1.07e-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: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7200 NNYEQSE-LSAELAQfqtkLTNTLANAKTQQSELEKEAERWREYQQSIDRVKAtiertkfVDEPVQNLAGLHFNIQKLSH 7278
Cdd:COG4913 607 DNRAKLAaLEAELAE----LEEELAEAEERLEALEAELDALQERREALQRLAE-------YSWDEIDVASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7279 AIGNVQSQNSDLTLVNQQAQSLIRQADArnrqlIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKAl 7358
Cdd:COG4913 676 ELERLDASSDDLAALEEQLEELEAELEE-----LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA- 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7359 gRLEDKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKsshkeiEALSKSILTFLGEVHKPSAE------------AIQA 7426
Cdd:COG4913 750 -LLEERFAAALGDAVERELRENLEERIDALRARLNRAE------EELERAMRAFNREWPAETADldadleslpeylALLD 822
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 442626147 7427 KV--DKLVEQQAKLNDTLRDKEQQVSKDL-----EEIEQVFRRISQLQDKL 7470
Cdd:COG4913 823 RLeeDGLPEYEERFKELLNENSIEFVADLlsklrRAIREIKERIDPLNDSL 873
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4890-5101 |
1.19e-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: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4890 QWRAYKEEYERLMEWLQQIDILVKNhkLNLCPNLPEKEKQVADMKEVMSRLEKGKDDIDKFNASAASLLKSHLD--TYVN 4967
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPdaEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4968 NQLRHLSSVYQVQVNLAKDVLKKVETNRDQHREYDaNMKSAKDWIANAKATIQSAGEGaGSKEALQRRLEQIQDLIRNRE 5047
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLG-KDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442626147 5048 LGQNLVHTAINNGEKIIRNTRSDGRDAINTEMKELQTEWDRLVKKMSTAKVQLE 5101
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
2754-2844 |
1.28e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 45.01 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2754 QYEQSNEQISNWLRDVEgRVKAETSSQVNLSEVPQKLQELSILQQDVLAHEPIINNLEQTSQQLIEKNPEAR--IGQFVT 2831
Cdd:smart00150 2 QFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAeeIEERLE 80
|
90
....*....|...
gi 442626147 2832 HLVQRYQAVSKAL 2844
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5644-5842 |
1.36e-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: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5644 EKYKQAYNELQDWLRRTRIEVEQcADCHGEKDQVESRLNRLGDIQSSSLEGKALLEACEELSQAVIAtSGSEGQDNVAQE 5723
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5724 IKHLTSEWETLQTISRDARSSLESCLAAWQtFLQKFNKINLWIETMNKRVTKSQEGENKTP-EDLVNA-KKLLEEVLAEK 5801
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDLGKDLESvEELLKKhKELEEELEAHE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 442626147 5802 DNVEDLNDNCELLMEQS---ACTRIRDQTIETQANYTKLLTSAQ 5842
Cdd:cd00176 160 PRLKSLNELAEELLEEGhpdADEEIEEKLEELNERWEELLELAE 203
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
7409-7610 |
1.42e-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: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7409 ILTFLGEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVhvyDEHIA 7488
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---EAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7489 QTEQLLITLNSQV-QQAAEESKLLVAQTTAHYQAKQNQL-----PSDIAQEFTALELLAERVQVTMETKEKDFKRAKTVR 7562
Cdd:COG4942 87 ELEKEIAELRAELeAQKEELAELLRALYRLGRQPPLALLlspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 442626147 7563 TEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELLQRINHEITAIYER 7610
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10373-11026 |
1.53e-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: 49.67 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10373 ERLRKATERLEGLAGDLHNREQLIDELKG---AAKPLIESCDVQIVEQIES--AVQEAVVAWNDTSENLQQLRTRYQRAV 10447
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERlaNLERQLEELEAQLEELESKLDELAEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10448 ELWDKYRNASAAVKNSIDQQMDAVKSLEQplDALQHAKVCQDNLTTQNDRILELRDIVAKIAADVgldasALMQGELDAL 10527
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELE--ELESRLEELEEQLETLRSKVAQLELQIASLNNEI-----ERLEARLERL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10528 GQRLAECKDAITTLANVAETQDKER-----KELDKEVTLAKAYFNNVQ------QDISREAPQNPKESEEQLAALRAHLQ 10596
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLEealeelREELEEAEQALDAAERELAQLQARLD 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10597 TLARTEEQLRQ--------LKERHQNSEVAPSVAS--------------------------SDDDGILEVLAL-WQKIFQ 10641
Cdd:TIGR02168 493 SLERLQENLEGfsegvkalLKNQSGLSGILGVLSElisvdegyeaaieaalggrlqavvveNLNAAKKAIAFLkQNELGR 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10642 DTFQEYHRLSTRLARSQNssealrlwRQYLQHVQSFLSCAIPEDYSSLREQQQLCAIHQNLLISQqSVLSETPLESELSE 10721
Cdd:TIGR02168 573 VTFLPLDSIKGTEIQGND--------REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVD-DLDNALELAKKLRP 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10722 QYK-------------ALTNLHNETLSRIMQRNGELERrvsgwnaYRQQLAALLDWLRQREAERNAL-QLRYIHLKRVPH 10787
Cdd:TIGR02168 644 GYRivtldgdlvrpggVITGGSAKTNSSILERRREIEE-------LEEKIEELEEKIAELEKALAELrKELEELEEELEQ 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10788 LKHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALAtamrmEQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRV 10867
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK-----ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10868 NQLQQEFGAAQKLLDANS-----------------ESLPTQPAAIEQLLGSLRAQRVQLGAQVSAL----ESLTVTQEEL 10926
Cdd:TIGR02168 792 EQLKEELKALREALDELRaeltllneeaanlrerlESLERRIAATERRLEDLEEQIEELSEDIESLaaeiEELEELIEEL 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10927 KECISPH---------DMKTIRQRNWLLWQQHADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQRLEQRVEKDADV 10997
Cdd:TIGR02168 872 ESELEALlnerasleeALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
730 740
....*....|....*....|....*....
gi 442626147 10998 TAMTNPEQAAKQLEQQVNSELQLRDKERE 11026
Cdd:TIGR02168 952 TLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3158-3271 |
1.59e-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: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3158 QSWEDFMTLCQDSLVKLKQLCSKWDEFDTiIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINE 3237
Cdd:cd00176 86 QRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKS 164
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 442626147 3238 LMDQGREIE------GETDLNLKLSRLNTRYQTLKNLCKE 3271
Cdd:cd00176 165 LNELAEELLeeghpdADEEIEEKLEELNERWEELLELAEE 204
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7298-8091 |
1.62e-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: 49.68 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7298 QSLIRQADARNRQL--IEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGF-ENSLHAWEKALGRLEDKFRNVDPTVR- 7373
Cdd:TIGR02169 233 EALERQKEAIERQLasLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAe 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7374 SRRHLEDTKNAIQELREESNQLKSshkEIEALSKSILTFLGEVHKPSAE--AIQAKVDKLV---EQQAKLNDTLRDKEQQ 7448
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLA---EIEELEREIEEERKRRDKLTEEyaELKEELEDLRaelEEVDKEFAETRDELKD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7449 VSKDLE----EIEQVFRRISQLQDKLNALHEQLQSVH----VYDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAhYQ 7520
Cdd:TIGR02169 390 YREKLEklkrEINELKRELDRLQEELQRLSEELADLNaaiaGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK-YE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7521 AKQNQLPSDIAQ---EFTALELLAERVQVT---METKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQ------------ 7582
Cdd:TIGR02169 469 QELYDLKEEYDRvekELSKLQRELAEAEAQaraSEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERyataievaagnr 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7583 ----VQERSLTPTQMKELLQRINheitaiYERFTLVKTNG-QLIIENCRNSEEKTLVQTTID------QLAASLAQVRGw 7651
Cdd:TIGR02169 549 lnnvVVEDDAVAKEAIELLKRRK------AGRATFLPLNKmRDERRDLSILSEDGVIGFAVDlvefdpKYEPAFKYVFG- 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7652 ldekKQAVGDSLDAWTRFMNLYQIVM--------SWA------SEKRNFIDQTIELRTLPEARNKLNDyvtsvksikpIV 7717
Cdd:TIGR02169 622 ----DTLVVEDIEAARRLMGKYRMVTlegelfekSGAmtggsrAPRGGILFSRSEPAELQRLRERLEG----------LK 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7718 KHLSEMDKELEHIGQvttvgDLKDKLQEAEDAKISVEAVLLERNSLLQEAceewDQCERKIKDIRSWHEKTKQGLDSSQQ 7797
Cdd:TIGR02169 688 RELSSLQSELRRIEN-----RLDELSQELSDASRKIGEIEKEIEQLEQEE----EKLKERLEELEEDLSSLEQEIENVKS 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7798 QKKPLRDQLGFCEKTLAdinvqktKLRLSIEKLEVHFRNgmggdprlsENVDDLVRVLDGLGELVKAKSQSLEQTLAQID 7877
Cdd:TIGR02169 759 ELKELEARIEELEEDLH-------KLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSRIEARLREIEQKLN 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7878 VYQQQMQSLRQRIIQEEQQLRLVmaptylpHDRERALAEQQDLITQELDELLQSLSSVEDGIANmnqssLDGMLHGLKLI 7957
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDL-------KEQIKSIEKEIENLNGKKEELEEELEELEAALRD-----LESRLGDLKKE 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7958 QSNLEVHERDAIELKNQAKklptdpATERLLNDTVDRIDLLLRRTQQGITMIANAmhgqKKRQQEIDEYQQHLLELEQWI 8037
Cdd:TIGR02169 891 RDELEAQLRELERKIEELE------AQIEKKRKRLSELKAKLEALEEELSEIEDP----KGEDEEIPEEELSLEDVQAEL 960
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 442626147 8038 IEVSAELASFEPTSDSSTD--EQVLKSQVERSQQlLRTLKDRQQSMEDLVEQTRQL 8091
Cdd:TIGR02169 961 QRVEEEIRALEPVNMLAIQeyEEVLKRLDELKEK-RAKLEEERKAILERIEEYEKK 1015
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7773-8121 |
1.75e-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: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7773 QCERKIKDIRSWHEKtkqgLDSSQQQKKPLRDQLGFCEKTLADINVQKTKLRLSIEKLEvhfrngmggdprlsENVDDLV 7852
Cdd:COG1196 219 KEELKELEAELLLLK----LRELEAELEELEAELEELEAELEELEAELAELEAELEELR--------------LELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7853 RVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRLVMAptylphdRERALAEQQDLITQELDELLQSL 7932
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE-------ELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7933 SSVEDGIANMNQSSLDgMLHGLKLIQSNLEVHERDAIELKNQAKKLptdpatERLLNDTVDRIDLLLRRTQQGITMIANA 8012
Cdd:COG1196 354 EEAEAELAEAEEALLE-AEAELAEAEEELEELAEELLEALRAAAEL------AAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 8013 MHGQKKRQQEIDEYQQHLLELEQWIIEVSAELASFEptsDSSTDEQVLKSQVERSQQLLRTLKDRQQSMEDLVEQTRQLQ 8092
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL---ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
330 340
....*....|....*....|....*....
gi 442626147 8093 SHPDVSPLADTLMEQLQSIITILREQVTV 8121
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
9045-9204 |
1.83e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 49.27 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 9045 EDAVVSSP--SESPRTPMVELVIPTEVVELA--LVEDEEQQTTPRIPSPTEKSEVEQDIKSVQTSPQHQPKLDETAV--- 9117
Cdd:PRK10811 861 AEEVQVQPvvAEVPVAAAVEPVVSAPVVEAVaeVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDVAvaq 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 9118 QTSLEVQPDNQENESQTLIVEITETEAQTTPRSEEQSVAVEISTTEIQTDVSGQPAETVEISSQTTVTTTIEKELQTTPK 9197
Cdd:PRK10811 941 EVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVEHNHATAPM 1020
|
....*..
gi 442626147 9198 DSPRAPE 9204
Cdd:PRK10811 1021 TRAPAPE 1027
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
10438-11037 |
1.85e-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: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10438 QLRTRYQRAVELWDKYRNASAAVKNsIDQQMDAVKSLEQPLDALQHAKvcqdnlttqnDRILELRDIVAKIAADVGLDAS 10517
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALED-AREQIELLEPIRELAERYAAAR----------ERLAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10518 ALMQGELDALGQRLAECKDAITTLANVAETQDKERKELdkevtlAKAYFNNVQQDIsreapqnpKESEEQLAALRAHL-- 10595
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDEL------EAQIRGNGGDRL--------EQLEREIERLERELee 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10596 --QTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQdtfQEYHRLSTRLARSQNSSEALRLWRQYLQH 10673
Cdd:COG4913 357 reRRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAEIASLER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10674 VQSflscAIPEDYSSLREQqqlcaihqnllISQQSVLSETPL--------------------ESEL----------SEQY 10723
Cdd:COG4913 434 RKS----NIPARLLALRDA-----------LAEALGLDEAELpfvgelievrpeeerwrgaiERVLggfaltllvpPEHY 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10724 KALT----NLHNET---LSRIMQRNGELERRvsgwNAYRQQLAALLD--------WLRQREAERNAL-------QLRY-- 10779
Cdd:COG4913 499 AAALrwvnRLHLRGrlvYERVRTGLPDPERP----RLDPDSLAGKLDfkphpfraWLEAELGRRFDYvcvdspeELRRhp 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10780 --------IHLKRVPHLKHRLDAMIQQLDQG---EQQSKALQEQQQELARHCDDALATAMRMEQASigQRISNLRAALKT 10848
Cdd:COG4913 575 raitragqVKGNGTRHEKDDRRRIRSRYVLGfdnRAKLAALEAELAELEEELAEAEERLEALEAEL--DALQERREALQR 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10849 WQGFLQRVTQLsESYEQRVNQLQQEfgaAQKLLDANSE--SLPTQPAAIEQLLGSLRAQRVQLGAQVSALES-LTVTQEE 10925
Cdd:COG4913 653 LAEYSWDEIDV-ASAEREIAELEAE---LERLDASSDDlaALEEQLEELEAELEELEEELDELKGEIGRLEKeLEQAEEE 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10926 LKECISPHDMKTIRQRNWLlwqqHADLDYQLANLINSiEERLSLLSNYQIRYDRISQWLQRLEQRVEK------------ 10993
Cdd:COG4913 729 LDELQDRLEAAEDLARLEL----RALLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERamrafnrewpae 803
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 442626147 10994 --DADVTAMTNPEqAAKQLEQQVNSEL-QLRDKEREWLLSTSRELLT 11037
Cdd:COG4913 804 taDLDADLESLPE-YLALLDRLEEDGLpEYEERFKELLNENSIEFVA 849
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5857-6051 |
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 442626147 5857 EFLNYKKEMDAWIEKAQQVLDDCSTDGDAAIIAQKLDTVNSLASRLPEGQHLLALVQDAYSKASNITPEDKqEKLRELMT 5936
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA-EEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5937 KVREDWDALGLAVKQKLSDLKQAQNRWNDFaANKDKLEKWLNETETTLKvAPETKGELSEMKTLLERYKTLSNELKLKGN 6016
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 442626147 6017 ELEQLQSEARDLGTEV--DAVNRLQSRCDKLKNDCSA 6051
Cdd:cd00176 161 RLKSLNELAEELLEEGhpDADEEIEEKLEELNERWEE 197
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
11113-11448 |
1.96e-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: 48.98 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11113 NVIEAKLKEHEQIQRSiehHSSNVGEVLNLVEMLLNDADSwrtqvNTSGLAASAQNLEQRWKNVCSQ--SAERKARIL-- 11188
Cdd:pfam07111 133 NLEEGSQRELEEIQRL---HQEQLSSLTQAHEEALSSLTS-----KAEGLEKSLNSLETKRAGEAKQlaEAQKEAELLrk 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11189 ---TIWNLLQQLIKLTAEHKNWLGKQ-----ESQIAGFERDQKSHSKHKLEERQMELRAKLEELESQSVNLR-----QLE 11255
Cdd:pfam07111 205 qlsKTQEELEAQVTLVESLRKYVGEQvppevHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLThmlalQEE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11256 QIYAKLAMSAGVEPENIQKltlpTKVMVSMWRQltprchalldaidKDAKLMREFNNAQLEATNSLNAIQkalEQLPSAE 11335
Cdd:pfam07111 285 ELTRKIQPSDSLEPEFPKK----CRSLLNRWRE-------------KVFALMVQLKAQDLEHRDSVKQLR---GQVAELQ 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11336 NQQTSKAEPKAVLQRleSLEKKLQDAQ------QHVQQADNLAQEAKTRTKQQPQL--KQLLELVSAYTTLWQTVQTRiv 11407
Cdd:pfam07111 345 EQVTSQSQEQAILQR--ALQDKAAEVEvermsaKGLQMELSRAQEARRRQQQQTASaeEQLKFVVNAMSSTQIWLETT-- 420
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 442626147 11408 tlkttwLTRAAQAAASLP-----VSEAANAAVQVNTLSQRKLRQAQ 11448
Cdd:pfam07111 421 ------MTRVEQAVARIPslsnrLSYAVRKVHTIKGLMARKVALAQ 460
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7132-7339 |
1.97e-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: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7132 EYMQLVAKFNDWVHEAELRLQNSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLVhKQIQEAADKIwSSLNNYEQSELSAEL 7211
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERV-EALNELGEQL-IEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7212 AQFQTKLTNTLANAKTQQSELEKEAERWREYQQSIDRVKATIERTKFV--DEPVQNLAGLHFNIQKLSHAIGNVQSQNSD 7289
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALasEDLGKDLESVEELLKKHKELEEELEAHEPR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442626147 7290 LTLVNQQAQSLIRQADARNRQLIEQDNAGLNRSWQDLVRSLEQRRDNLQQ 7339
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6720-6885 |
2.22e-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: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6720 FEDSMKNMGDWLNEMETATEGELRTTSLPVLEEQLAHYKKLLSDAENKGGLINDVSEQGKSILpTLSNADKLKLNDDIKN 6799
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6800 MKDRYGRIKNTIDDRVNALGDHIKKYKdaksRLAECSQFLGNIQQKLRELNR-PIGSRIEDVQDLLGAYEGILKELKDSK 6878
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQ----FFRDADDLEQWLEEKEAALASeDLGKDLESVEELLKKHKELEEELEAHE 159
|
....*..
gi 442626147 6879 SKMGDMQ 6885
Cdd:cd00176 160 PRLKSLN 166
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6442-6802 |
2.50e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6442 KIQELKgKAAQV--AEVISNLDGQQVEEQMKSLDRRFADLGKRIDRKsQLLDVTNKGVEGAKGEIDQLQnwvKQQIEELQ 6519
Cdd:PTZ00121 1547 KADELK-KAEELkkAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA-RIEEVMKLYEEEKKMKAEEAK---KAEEAKIK 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6520 APKPlgytpKDAEARQQKIKSLMKDAEAKQSLADVLEK-----RVANMQQELEPVEYSQLESALRNLNTENRNLSGVLKA 6594
Cdd:PTZ00121 1622 AEEL-----KKAEEEKKKVEQLKKKEAEEKKKAEELKKaeeenKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6595 ELDRALEASKARKSLENDLDKARQWLKTKisEVRKLPVYHPLTSAEIEKKIQENRKYDDDAKQFNDSVLTDVQRQAANIM 6674
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAE--EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6675 KDcddaDKAALQQILDEIAADYQTLKDESSKRGKSLDDLLQgrkafEDSMKN--MGDWLNEMETATEGELRTTSLPVLEE 6752
Cdd:PTZ00121 1775 KE----KEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANII-----EGGKEGnlVINDSKEMEDSAIKEVADSKNMQLEE 1845
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 442626147 6753 QLAHYKkllsdaeNKGGLINDVSEQGKSilPTLSNADKLKLNDDIKNMKD 6802
Cdd:PTZ00121 1846 ADAFEK-------HKFNKNNENGEDGNK--EADFNKEKDLKEDDEEEIEE 1886
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7327-7770 |
2.62e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7327 VRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKSSHKEIEALS 7406
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7407 KSILTFlgevhKPSAEAIQAKVDKLVEQQAKLNDTLRD----KEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVhv 7482
Cdd:COG4717 153 ERLEEL-----RELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEEL-- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7483 yDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAHYQAKQNQLPSDIAQEFTALELLAE--RVQVTMETKEKDFKRAKT 7560
Cdd:COG4717 226 -EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGllALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7561 VRTEYVDGVDEVQRWLLQAEVQVQ--ERSLTPTQMKELLQRINHEITAIYERFTLVKtngQLIIENCRNSEEKTLVQ--- 7635
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALglPPDLSPEELLELLDRIEELQELLREAEELEE---ELQLEELEQEIAALLAEagv 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7636 TTIDQLAASLAQVRGWLDEKKQavgdsLDAWTRFMNLYQIVMSWASEKRNFIDQTIEL----RTLPEARNKLNDYVTSVK 7711
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEE-----LEELEEQLEELLGELEELLEALDEEELEEELeeleEELEELEEELEELREELA 456
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 442626147 7712 SIKPIVKHLSEmDKELEHIGQVttVGDLKDKLQEAEDAKISVEAVLlernSLLQEACEE 7770
Cdd:COG4717 457 ELEAELEQLEE-DGELAELLQE--LEELKAELRELAEEWAALKLAL----ELLEEAREE 508
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1888-2100 |
2.62e-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: 46.67 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 1888 WKSFDADAAKLEDWVGQGEQQMSRRPAVlntPHIDKLEKELVKLKSFNNEISQQQAKLVTLGQNADQIsLHLAPEGAAAL 1967
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYG---DDLESVEALLKKHEALEAELAAHEERVEALNELGEQL-IEEGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 1968 KDRVNQMKGKLQKLSEATRGHINEVSDAIiSRQDFNAKLVNFSNWMEQLRNQVTQVEeinperVETSLHVIHALLQEHAD 2047
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASED------LGKDLESVEELLKKHKE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2048 -------KKPSFNAIYDEVKQLALGATPEESNALNDAYTALVVNYQNLETNMLQKKAALE 2100
Cdd:cd00176 151 leeeleaHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
6991-7657 |
2.63e-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: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6991 KNSITEQLQSLKNQLQNLRKAVESQRQKHQ-LQLESHK---KMAAELSEILDWLHSH-----------EGAAKSRPLLDR 7055
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKAIQeLQFENEKvslKLEEEIQENKDLIKENnatrhlcnllkETCARSAEKTKK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7056 DPESVERELQKHQSLSQDIESYLNKFNKIN-DGVKTEIGMPSSLLEMLSEGRSLVASLPHELEEREKYL---------KN 7125
Cdd:pfam05483 174 YEYEREETRQVYMDLNNNIEKMILAFEELRvQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVsllliqiteKE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7126 NRDSRLEYM--QLVAKFNDWVHEAELRLQNSQHGIDYE-HLVQDLDEHKIFFGNEAPIRNLVHKQIQEAADKIWsSLNNY 7202
Cdd:pfam05483 254 NKMKDLTFLleESRDKANQLEEKTKLQDENLKELIEKKdHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIC-QLTEE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7203 EQSELSaELAQFQTKLTNTLANAKTQQSELEkeaERWREYQQsidRVKATIERTKFVDEPVQNLAGlhfNIQKLSHAIGN 7282
Cdd:pfam05483 333 KEAQME-ELNKAKAAHSFVVTEFEATTCSLE---ELLRTEQQ---RLEKNEDQLKIITMELQKKSS---ELEEMTKFKNN 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7283 VQSQNSDLTLVNQQAQSLIRQadarNRQlIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLE 7362
Cdd:pfam05483 403 KEVELEELKKILAEDEKLLDE----KKQ-FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7363 -----DKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKSSHKEI-------EALSKSILTfLGEVHKPSAEAIQAKVDK 7430
Cdd:pfam05483 478 telekEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIinckkqeERMLKQIEN-LEEKEMNLRDELESVREE 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7431 LVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVHVYDEHIAQTEQLLitlnsqVQQAAEESKL 7510
Cdd:pfam05483 557 FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL------KKKGSAENKQ 630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7511 LVAqttahYQAKQNQLPSDIAQEFTALELLAERVQVTMETKE-------KDFKRAKTVrteyvdgVDEVQRWLLQAEVQV 7583
Cdd:pfam05483 631 LNA-----YEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKiseekllEEVEKAKAI-------ADEAVKLQKEIDKRC 698
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442626147 7584 QERSltpTQMKELLQRINHEITAIYErftlvKTNGQLIIENCRNSEEKTL---VQTTIDQLAASLAQVRGWLDEKKQ 7657
Cdd:pfam05483 699 QHKI---AEMVALMEKHKHQYDKIIE-----ERDSELGLYKNKEQEQSSAkaaLEIELSNIKAELLSLKKQLEIEKE 767
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4566-4777 |
2.75e-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: 46.67 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4566 EDFDNAISDCSSWINEIKEKL---DYCSDMSSMspKELDKKLATIQDVILLKDEgsaRVLKILEQAQHvLANTAPGGHEA 4642
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLsstDYGDDLESV--EALLKKHEALEAELAAHEE---RVEALNELGEQ-LIEEGHPDAEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4643 INKELTDLQDLWSGIALRIMDVKSNLDDSITQWSGFLDqvqnVRKFNEWLDGQVKELS--EHQTTMTEKRAQLDRVKSTE 4720
Cdd:cd00176 77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD----ADDLEQWLEEKEAALAseDLGKDLESVEELLKKHKELE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442626147 4721 EKVRVEKIDVDALKIQAKEMIASGQQSQAAFQAQKvLDTFDELFAKTQKLLSHRQDQ 4777
Cdd:cd00176 153 EELEAHEPRLKSLNELAEELLEEGHPDADEEIEEK-LEELNERWEELLELAEERQKK 208
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
10787-11388 |
3.01e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10787 HLKHRLDAMIQQLDQGEQQSKALQEQQQELARhcddalatamrmeqasIGQRISNLRAALKTWQGFLQRVTQLSESYEQr 10866
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEE----------------VLREINEISSELPELREELEKLEKEVKELEE- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10867 vnqLQQEFGAAQKLLdansESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELKECISPHdMKTIRQRNWLLw 10946
Cdd:PRK03918 236 ---LKEEIEELEKEL----ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY-IKLSEFYEEYL- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10947 QQHADLDYQLANL---INSIEERLSLLSNYQIRYDRISQWLQRLEQRVEKdadvtamtnPEQAAKQLEQQVNSELQLRDK 11023
Cdd:PRK03918 307 DELREIEKRLSRLeeeINGIEERIKELEEKEERLEELKKKLKELEKRLEE---------LEERHELYEEAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11024 EREWLLSTSRELLTLYSEPEVR-SQVQQQSDSLIDRWQRLKYLAKQKATKIGELKMT---------LLRLEERIALIRAW 11093
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAkEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrELTEEHRKELLEEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11094 LFEVESqldkplnfesytpnvIEAKLKEHEQIQRSIEhhssnvgEVLNLVEMLLNDADSWRTQVNtsgLAASAQNLEQRW 11173
Cdd:PRK03918 458 TAELKR---------------IEKELKEIEEKERKLR-------KELRELEKVLKKESELIKLKE---LAEQLKELEEKL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11174 KNVCSQSAERKARILTiwNLLQQLIKLTAEHKNwLGKQESQIAGFERDQKS--HSKHKLEERQMELRAKLEELESQSVN- 11250
Cdd:PRK03918 513 KKYNLEELEKKAEEYE--KLKEKLIKLKGEIKS-LKKELEKLEELKKKLAEleKKLDELEEELAELLKELEELGFESVEe 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11251 ----LRQLEQIYAKLAMSAGVEPEniqkltlptkvmvsmWRQLTPRCHALLDAIDKDAKLMREFNNAQLEATNSLNAIQK 11326
Cdd:PRK03918 590 leerLKELEPFYNEYLELKDAEKE---------------LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626147 11327 AL--EQLPSAENQQTSKA-EPKAVLQRLESLEKKLQDAQqhvQQADNLAQEAKTRTKQQPQLKQL 11388
Cdd:PRK03918 655 KYseEEYEELREEYLELSrELAGLRAELEELEKRREEIK---KTLEKLKEELEEREKAKKELEKL 716
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
10358-10918 |
3.32e-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: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10358 DFMMELIRVHGQVdyERLRKATERLEGLAGD------LHNREQLIDELKGAAKPLIescDVQIVEQIESAVQEAVVAWND 10431
Cdd:COG4913 232 EHFDDLERAHEAL--EDAREQIELLEPIRELaeryaaARERLAELEYLRAALRLWF---AQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10432 TSENLQQLRTRYQRAVELWDKYRNASAAVKNsidqqmDAVKSLEQPLDALQHAkvcqdnLTTQNDRILELRDIVAKIAAD 10511
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERE------LEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10512 VGLDASAL------MQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVT-LAK------AYFNNVQQDISREAP 10578
Cdd:COG4913 375 LPASAEEFaalraeAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAsLERrksnipARLLALRDALAEALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10579 Q--------------NPKESEEQLAALRAhLQTLART----EEQLRQ---------LKERHQNSEVAPSVASS-----DD 10626
Cdd:COG4913 455 LdeaelpfvgelievRPEEERWRGAIERV-LGGFALTllvpPEHYAAalrwvnrlhLRGRLVYERVRTGLPDPerprlDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10627 DGILEVLAlwqkiFQDT-FQEYhrLSTRLARSQNssealrlwrqylqhvqsFLSCAIPEDyssLREQQQlcAIHQNLLIS 10705
Cdd:COG4913 534 DSLAGKLD-----FKPHpFRAW--LEAELGRRFD-----------------YVCVDSPEE---LRRHPR--AITRAGQVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10706 QQSVLSETPLESELSEQY-------KALtnlhnETLSRIMQrngELERRVSGWNAYRQQLAALLDWLRQREAERNALQLR 10778
Cdd:COG4913 585 GNGTRHEKDDRRRIRSRYvlgfdnrAKL-----AALEAELA---ELEEELAEAEERLEALEAELDALQERREALQRLAEY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10779 YIHLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHcdDALATAMRMEQASIGQRISNLRAALKTWQGFLQRVTQ 10858
Cdd:COG4913 657 SWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEEL--EAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10859 LSESYEQRVnQLQQEFGAAQKLLDANseslptQPAAIEQLLGSLRAQRVQLGAQVSALES 10918
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 |
3.54e-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: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 266 QEEQERVQKKTFTNWINSYL-----LKRVPPLR--IDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFL--SNA 336
Cdd:cd21325 18 QHSYSEEEKYAFVNWINKALendpdCRHVIPMNpnTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFIiqENL 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 442626147 337 NTALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTII---LYFQIEEnSRN 385
Cdd:cd21325 98 NLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIkigLFADIEL-SRN 148
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
268-374 |
3.64e-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: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 268 EQERVQKKTFTNWINSYllkRVPPlRIDDLINDLRDGTKLIALLEVLsgeRLPVEKGRVLRRPH--------FLSNANTA 339
Cdd:cd21330 9 EGETREERTFRNWMNSL---GVNP-RVNHLYSDLSDALVIFQLYEKI---KVPVDWNRVNKPPYpklgenmkKLENCNYA 81
|
90 100 110
....*....|....*....|....*....|....*.
gi 442626147 340 LQFLASK-RIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21330 82 VELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLM 117
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7330-7614 |
3.73e-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: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7330 LEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKSSHKEIEALSKSI 7409
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7410 ltflgevhkpsaEAIQAKVDKLVEQQAKLNdtlrdkeqqvskdleeieqvfRRISQLQDKLNALHEQLQSVHvydehiAQ 7489
Cdd:COG4913 695 ------------EELEAELEELEEELDELK---------------------GEIGRLEKELEQAEEELDELQ------DR 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7490 TEQLLITLNSQVQQAAEEsKLLVAQTTAHYQAKQNQLPSDIAQEFTALELLAERVQVTMETKEKDFK-RAKTVRTEyVDG 7568
Cdd:COG4913 736 LEAAEDLARLELRALLEE-RFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPaETADLDAD-LES 813
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 442626147 7569 VDEVQRWL--LQAE--VQVQER------SLTPTQMKELLQRINHEITAIYERFTLV 7614
Cdd:COG4913 814 LPEYLALLdrLEEDglPEYEERfkellnENSIEFVADLLSKLRRAIREIKERIDPL 869
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
8588-8813 |
4.06e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 48.16 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 8588 APVE-------LPAPQVDVEQPVVVATTSP-VHVPTADVV-EPKDSSPTSTTAAVVDVEavvediNEIWPLEHHLKPTNI 8658
Cdd:PRK10263 335 APVEpvtqtppVASVDVPPAQPTVAWQPVPgPQTGEPVIApAPEGYPQQSQYAQPAVQY------NEPLQQPVQPQQPYY 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 8659 DFSQHVEELAAPAAVTAETEASMPVEEIWPTSPETGNSLTLEQYE--------FEPQSPHEESTKSD--LVKPQETEPQV 8728
Cdd:PRK10263 409 APAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQstfapqstYQTEQTYQQPAAQEplYQQPQPVEQQP 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 8729 VAETKPEGITTGSITITKTTTTITSSTEVPE-ETLV---QNVPADEQQPPANKIKTDIQSfleaeqtlAAALKEQSSTPT 8804
Cdd:PRK10263 489 VVEPEPVVEETKPARPPLYYFEEVEEKRARErEQLAawyQPIPEPVKEPEPIKSSLKAPS--------VAAVPPVEAAAA 560
|
....*....
gi 442626147 8805 GASVAEDVQ 8813
Cdd:PRK10263 561 VSPLASGVK 569
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
7005-7806 |
4.11e-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: 48.12 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7005 LQNLRKAVESQRQK---HQLQLESHKKMAAELSEILDWLHSHEGAAKSRPLLDRdpeSVERELQKHQSLSQDIESYLNKF 7081
Cdd:TIGR00606 188 LETLRQVRQTQGQKvqeHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVK---SYENELDPLKNRLKEIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7082 NKINDG----------------------VKTEIGMPSSLLEMLSEGRSLVASLPHELEEREKYLKNNRDSRLEYMQLVAK 7139
Cdd:TIGR00606 265 MKLDNEikalksrkkqmekdnselelkmEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7140 FNDWVHEAELRLQNSQ-HGIDYEHLVQDLDEHKIFFGNEapirnlvHKQIQEAADKIWSSLNNYEQSELSAELAQFQTKL 7218
Cdd:TIGR00606 345 LLVEQGRLQLQADRHQeHIRARDSLIQSLATRLELDGFE-------RGPFSERQIKNFHTLVIERQEDEAKTAAQLCADL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7219 TNTLANAKTQQSELE-KEAERWREYQQSIDRVKATIERTKFVDEPVQNLAGLHFNIQKLSHAIGNVQS------QNSDLT 7291
Cdd:TIGR00606 418 QSKERLKQEQADEIRdEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERelskaeKNSLTE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7292 LVNQQAQSL-IRQADA-RNRQLIEQDNAGLNRSWQDLVRSL----------EQRRDNLQQLAEHWDG----------FEN 7349
Cdd:TIGR00606 498 TLKKEVKSLqNEKADLdRKLRKLDQEMEQLNHHTTTRTQMEmltkdkmdkdEQIRKIKSRHSDELTSllgyfpnkkqLED 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7350 SLHAWEKALGRLEDKFRNVDPTVRSrrhLEDTKNAIQelreesNQLKSSHKEIEALSKSILTFLG-EVHKPSAEAIQAKV 7428
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELAS---LEQNKNHIN------NELESKEEQLSSYEDKLFDVCGsQDEESDLERLKEEI 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7429 DKLVEQQAKLNDTLRDKEQQVSKDLEEIEQ---VFRRISQLQDKLNALHEQLQS-VHVYDEHIAQTEQLLitlnSQVQQA 7504
Cdd:TIGR00606 649 EKSSKQRAMLAGATAVYSQFITQLTDENQSccpVCQRVFQTEAELQEFISDLQSkLRLAPDKLKSTESEL----KKKEKR 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7505 AEESKLLVAQTTAHYQAKQNQLP----------SDIAQEFTALELLAERVQVTMETKE--KDFKRAKTVRTEYVDGVDEV 7572
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPelrnklqkvnRDIQRLKNDIEEQETLLGTIMPEEEsaKVCLTDVTIMERFQMELKDV 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7573 QRWLLQ--AEVQVQERSLTPTQMKELLQRINHEITAIYERFTLvktNGQLIIENcrnSEEKTLVQTTIDQLAASLAQVRG 7650
Cdd:TIGR00606 805 ERKIAQqaAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIEL---NRKLIQDQ---QEQIQHLKSKTNELKSEKLQIGT 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7651 WLDEKKQAVGDSLDAWTRFMNLYQIVmswaSEKRNfidQTIELRTLPEARNKLNDYVTSVK--SIKPIVKHLSEMDKELE 7728
Cdd:TIGR00606 879 NLQRRQQFEEQLVELSTEVQSLIREI----KDAKE---QDSPLETFLEKDQQEKEELISSKetSNKKAQDKVNDIKEKVK 951
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626147 7729 HIgqVTTVGDLKDKLQEA-EDAKISVEAVLLERNSLLQEaceewdqCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQL 7806
Cdd:TIGR00606 952 NI--HGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEE-------CEKHQEKINEDMRLMRQDIDTQKIQERWLQDNL 1021
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4256-4347 |
4.13e-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: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4256 ADSLKSWLDETENALpADIELKTTLDEKRNKLQTYRDILNDINNHQVELGNLQEIAANL----PEKTELVDQIIKDISDR 4331
Cdd:pfam00435 10 ADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLidegHYASEEIQERLEELNER 88
|
90
....*....|....*.
gi 442626147 4332 FGKLQKRAQNYVERYE 4347
Cdd:pfam00435 89 WEQLLELAAERKQKLE 104
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
5507-6318 |
4.15e-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: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5507 AAKIQEDTEALKQDFDKLL---VDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDvepSVKTS-DEFLNDLSEKRAALEK 5582
Cdd:pfam12128 243 FTKLQQEFNTLESAELRLShlhFGYKSDETLIASRQEERQETSAELNQLLRTLDD---QWKEKrDELNGELSAADAAVAK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5583 FRviqrdinghnDIVEKINQRLKEDNSLDLKDFQPGLTKFDDLQTQVNKIIESLENQVNSHEKYKQAYNelqdwlRRTRI 5662
Cdd:pfam12128 320 DR----------SELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYN------RRRSK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5663 EVEQCADchgekdqvesRLNRLGDIQSSSLEGKALLEACEElsqAVIATSGSEGQDNVAQEIKHLTSEWETLQTISRDAR 5742
Cdd:pfam12128 384 IKEQNNR----------DIAGIKDKLAKIREARDRQLAVAE---DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5743 SSLESCLAAWQTFLQKFNKINLwIETMNKRVTKSQEGENKTPEDLVNAKKLLEEVLaekdnvEDLND-NCELLMEQSACT 5821
Cdd:pfam12128 451 LRLNQATATPELLLQLENFDER-IERAREEQEAANAEVERLQSELRQARKRRDQAS------EALRQaSRRLEERQSALD 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5822 RIRDQTIETQANYTKLL-TSAQGLVAKIEKNLSdhTEFLnYKKEMDAwiekaqqVLDDCSTDGDAAIIAQKLDT----VN 5896
Cdd:pfam12128 524 ELELQLFPQAGTLLHFLrKEAPDWEQSIGKVIS--PELL-HRTDLDP-------EVWDGSVGGELNLYGVKLDLkridVP 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5897 SLASRLPEGQHLLALVQDAYSKASnitpeDKQEKLRELMTKVREDWDALGLAVKQKLSDLKQA---QNRWNDFAAN-KDK 5972
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAR-----EKQAAAEEQLVQANGELEKASREETFARTALKNArldLRRLFDEKQSeKDK 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5973 LEKWLNE-----TETTLKVAPETKGELSEMKTLLERYKTLSNELKLKGNELEQLQSEARDlgtevDAVNRLQSRCDKLKN 6047
Cdd:pfam12128 669 KNKALAErkdsaNERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALD-----AQLALLKAAIAARRS 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6048 DCSAHITALEQEmfdynaYHQSLQDvekwlLQISFQLMAHNSLFISNREQTQEQIKQ--HEAL----------LVEIQKY 6115
Cdd:pfam12128 744 GAKAELKALETW------YKRDLAS-----LGVDPDVIAKLKREIRTLERKIERIAVrrQEVLryfdwyqetwLQRRPRL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6116 QTNLDDLNAKG---QAQIKRYESSTPAIRPTVESQLKNIQDSynsllqtsvqiKNRLLESLAKfqeyedtLDSIMRNLET 6192
Cdd:pfam12128 813 ATQLSNIERAIselQQQLARLIADTKLRRAKLEMERKASEKQ-----------QVRLSENLRG-------LRCEMSKLAT 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6193 YepiiqtELDAPATSLEL-AQNQLRCAQEMQNKLNNEKSRLAAAVQACEAATASISRpSSPLETaMQAIPERELIVRAKL 6271
Cdd:pfam12128 875 L------KEDANSEQAQGsIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADHSG-SGLAET-WESLREEDHYQNDKG 946
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 442626147 6272 EDLLDQVQshlggltaSVSELEQQQKQRAELQDWVKKQQSSVSDWMM 6318
Cdd:pfam12128 947 IRLLDYRK--------LVPYLEQWFDVRVPQSIMVLREQVSILGVDL 985
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3819-3914 |
4.40e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 43.47 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3819 YQDILNQTVNWLDQVEKLIHNENPASwtSAQEIRSKLYKYKATNQDINSHKRIVEAVNEKAAALLgSAAPANADEISKAV 3898
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASEDLGK--DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI-EEGHPDAEEIEERL 79
|
90
....*....|....*.
gi 442626147 3899 AEVNKRYDQVGQDCAK 3914
Cdd:smart00150 80 EELNERWEELKELAEE 95
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
6442-6639 |
4.55e-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: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6442 KIQELKGKAAQVAEVISNLDGQQ--VEEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEEL- 6518
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELa 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6519 -------------------------QAPKPLGYTPKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELEpvEYSQ 6573
Cdd:COG4942 108 ellralyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA--ELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442626147 6574 LESALRNLNTENRNLSGVLKAELDRALEASKARKSLENDLDKARQWLKTKISEVRKLPVYHPLTSA 6639
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
7354-7516 |
4.57e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.00 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7354 WEKALGRLEDKFRNVDPTVRSRRH-LEDTKNAIQELREESNQLKSSHK---EIEAL--SKSILTFLGEVHKPSAEAIQAK 7427
Cdd:PRK05771 84 LEELIKDVEEELEKIEKEIKELEEeISELENEIKELEQEIERLEPWGNfdlDLSLLlgFKYVSVFVGTVPEDKLEELKLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7428 VDKLVEQ---QAKLND-----TLRDKEQQVSKDL-----------------EEIEQVFRRISQLQDKLNALHEQLQSV-- 7480
Cdd:PRK05771 164 SDVENVEyisTDKGYVyvvvvVLKELSDEVEEELkklgferleleeegtpsELIREIKEELEEIEKERESLLEELKELak 243
|
170 180 190
....*....|....*....|....*....|....*.
gi 442626147 7481 HVYDEHIAQTEQLLItlnsQVQQAAEESKLLVAQTT 7516
Cdd:PRK05771 244 KYLEELLALYEYLEI----ELERAEALSKFLKTDKT 275
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
10521-10772 |
4.96e-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: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10521 QGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVtlakayfNNVQQDIsreapqnpKESEEQLAALRAHLQTLAR 10600
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------AALARRI--------RALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10601 TEEQLRQLKERHQNsEVAPSVASSDDDGILEVLALwqkifqdtfqeyhrlstrLARSQNSSEALRLwRQYLQHVQSFLSC 10680
Cdd:COG4942 91 EIAELRAELEAQKE-ELAELLRALYRLGRQPPLAL------------------LLSPEDFLDAVRR-LQYLKYLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10681 AIpedySSLREQQQLCAIHQNLLISQQSVLSEtpLESELSEQYKALTNL---HNETLSRIMQRNGELERRVSGWNAYRQQ 10757
Cdd:COG4942 151 QA----EELRADLAELAALRAELEAERAELEA--LLAELEEERAALEALkaeRQKLLARLEKELAELAAELAELQQEAEE 224
|
250
....*....|....*
gi 442626147 10758 LAALLDWLRQREAER 10772
Cdd:COG4942 225 LEALIARLEAEAAAA 239
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3173-3839 |
5.19e-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: 47.74 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3173 KLKQLCSKWDEFDTIIEELDnwMKNVEAVVKNQNLKSTAEAKNAHLK----QLQDISKDIERRGAAINELmdQGREIEGE 3248
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELE--EEIEELQKELYALANEISRLEQQKQilreRLANLERQLEELEAQLEEL--ESKLDELA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3249 TDLNL---KLSRLNTRYQTLKNLCKESIAKYVNYV-------KDHESFDKDFDSFKQN-----------------LQSSV 3301
Cdd:TIGR02168 337 EELAEleeKLEELKEELESLEAELEELEAELEELEsrleeleEQLETLRSKVAQLELQiaslnneierlearlerLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3302 DELAKTNEIVGDQSVLQDQQNKLREMSDKRILDSTLFEGLIDRGEKLyghtspegrEIIRQQLRALRTLWDNYTDDLNSA 3381
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL---------EELREELEEAEQALDAAERELAQL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3382 TQKIDQCLLQFNEFSIAQDQLtKWLKDVDKAMQSHTEPKTTLQEKRAQLQNHKLLHQEITTHNVLVDNVcDKAQILVDQI 3461
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEGV-KALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENL-NAAKKAIAFL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3462 KDNSLN----VYLTSIKQlfQSIVQKSDEILHNLDDCVQKHNELNNALSSAKTWISNEKAKLLECDDaygekadikrkIE 3537
Cdd:TIGR02168 566 KQNELGrvtfLPLDSIKG--TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDD-----------LD 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3538 TLGQLAQNKPQAMKIISDIRDLFEKVKATT--SEKGNEVL---DKEIEELETTMKSHFDDIEGIEGKQKDVLAQWDKFEK 3612
Cdd:TIGR02168 633 NALELAKKLRPGYRIVTLDGDLVRPGGVITggSAKTNSSIlerRREIEELEEKIEELEEKIAELEKALAELRKELEELEE 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3613 ALEELTKWCRSAEAVFREQQLQ-STLHEKVEQLEKYKIQR-----ELILQKEKEIDAFGDAAHALLNncGADRLKTLTTQ 3686
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDlARLEAEVEQLEERIAQLskeltELEAEIEELEERLEEAEEELAE--AEAEIEELEAQ 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3687 ITNRYQLLQVLSKEVVNRWSNLVDDHQFYQDKYNEVDLWLQPIES--QMAKVLLDEPTQSSNILQVLLSEKEQAESLFAA 3764
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAteRRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626147 3765 LNAAGEKALPEtstqgREKIRKDLRDIRDRWDKLDEGIRNLEKRQEAQGVQLSSYQDILNQTVNWLDQVEKLIHN 3839
Cdd:TIGR02168 871 LESELEALLNE-----RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7293-7932 |
5.24e-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: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7293 VNQQAQSLIRQADArnrqlieqdnAglnRSWQDLVRSLEQRRDNLQQLaeHWDGFENSLHAWEKALGRLEDKFRnvdptv 7372
Cdd:COG1196 198 LERQLEPLERQAEK----------A---ERYRELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELE------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7373 RSRRHLEDTKNAIQELREESNQLKsshKEIEALSKSIltflgevhkpsaEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKD 7452
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELE---LELEEAQAEE------------YELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7453 LEEIEQVFRRISQLQDKLNALHEQLQSVhvyDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAHYQAKQNQLpsdiaQ 7532
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEA---EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-----R 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7533 EFTALELLAERVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELLQRINHEITAIYERFT 7612
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7613 LVKTNGQLIIEncRNSEEKTLVQTTIDQLAASLAQVRGWLDEKKQA----VGDSLDAWTRFMNLYQIVMSWASEKRNFID 7688
Cdd:COG1196 474 LLEAALAELLE--ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrgLAGAVAVLIGVEAAYEAALEAALAAALQNI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7689 QTIELRTLPEARNKLNDYVTSVKSIKPIVK-HLSEMDKELEHIGQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEA 7767
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7768 CEEWDqcERKIKDIRSWHEKTKQGLDSSQQQkkplrDQLGFCEKTLADINVQKTKLRLSIEKLEVHfrngmggdpRLSEN 7847
Cdd:COG1196 632 LEAAL--RRAVTLAGRLREVTLEGEGGSAGG-----SLTGGSRRELLAALLEAEAELEELAERLAE---------EELEL 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7848 VDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRLVMAPTYLPHDRERALAEQQdlitQELDE 7927
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE----RELER 771
|
....*
gi 442626147 7928 LLQSL 7932
Cdd:COG1196 772 LEREI 776
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
10372-11041 |
6.88e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.53 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10372 YERLRKATERLEGLAGDLHNREQLIDELKGAAKPLIEScDVQIVEQIEsAVQEAVVAWNdtsenlQQLRTryqraveLWD 10451
Cdd:pfam12128 233 IAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSD-ETLIASRQE-ERQETSAELN------QLLRT-------LDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10452 KYRNASAAVKNSIDQQMDAVKSLEQPLDAL--QHAKVCQDNLTTqndrilelrdivakIAADvgLDASALMQGELDALGQ 10529
Cdd:pfam12128 298 QWKEKRDELNGELSAADAAVAKDRSELEALedQHGAFLDADIET--------------AAAD--QEQLPSWQSELENLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10530 RLaeckDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREApqnpkeSEEQLAALRAHLQTL-----ARTEEQ 10604
Cdd:pfam12128 362 RL----KALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREA------RDRQLAVAEDDLQALeselrEQLEAG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10605 LRQLKERHQNSEVAPSVASS--DDDGILEVLALWQKIFQD-----------TFQEYHRLSTRLA----RSQNSSEALRLW 10667
Cdd:pfam12128 432 KLEFNEEEYRLKSRLGELKLrlNQATATPELLLQLENFDErierareeqeaANAEVERLQSELRqarkRRDQASEALRQA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10668 RQYLQHVQSFLSCA----IPEDYS---SLREQQQLCAIHQNLLISQQsVLSETPLESELSE-QYKALTNLHNETLsrimq 10739
Cdd:pfam12128 512 SRRLEERQSALDELelqlFPQAGTllhFLRKEAPDWEQSIGKVISPE-LLHRTDLDPEVWDgSVGGELNLYGVKL----- 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10740 rngELER-RVSGWNAYRQQLAALLDWL---------RQREAERNALQLRyihlKRVPHLKHRLDAMIQQLDQGEQQSKAL 10809
Cdd:pfam12128 586 ---DLKRiDVPEWAASEEELRERLDKAeealqsareKQAAAEEQLVQAN----GELEKASREETFARTALKNARLDLRRL 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10810 QEQQQELARHCDDALATAMRMEQASIGQRISNLRAALKTWQGFLQRVT-QLSESYEQRVNQLQQEFGAAQklldansesl 10888
Cdd:pfam12128 659 FDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKeQKREARTEKQAYWQVVEGALD---------- 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10889 ptqpAAIEQLLGSLRAQRVQLGAQVSALEsltvtqEELKECISPHDMKTIRQrnwllwqqhADLDYQLANLINSIEerls 10968
Cdd:pfam12128 729 ----AQLALLKAAIAARRSGAKAELKALE------TWYKRDLASLGVDPDVI---------AKLKREIRTLERKIE---- 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10969 llsnyQIRYDR--ISQWLQRLEQR--VEKDADVTAMTNPEQAAKQLEQQV---NSELQLRDKEREWLLSTSRELLTLYSE 11041
Cdd:pfam12128 786 -----RIAVRRqeVLRYFDWYQETwlQRRPRLATQLSNIERAISELQQQLarlIADTKLRRAKLEMERKASEKQQVRLSE 860
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6066-6169 |
7.22e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 43.09 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6066 YHQSLQDVEKWLLQISFQLMAHNslFISNREQTQEQIKQHEALLVEIQKYQTNLDDLNAKGQAQIKRYESSTPAIrptvE 6145
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASED--LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEI----E 76
|
90 100
....*....|....*....|....
gi 442626147 6146 SQLKNIQDSYNSLLQTSVQIKNRL 6169
Cdd:smart00150 77 ERLEELNERWEELKELAEERRQKL 100
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5226-5427 |
7.64e-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: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5226 NEFATWLRNAKERLSKcSEPTGDKQALAEKTHQLKILQGELPEGAQKLKNALEQGEiACRSAEPEDCEIIEQEVALLQEE 5305
Cdd:cd00176 10 DELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGE-QLIEEGHPDAEEIQERLEELNQR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5306 FDAYREALNKAKDYLEVGIVKWSDYQDQyTEALEWLSKTEALVQSYNKLQDsLIQKKVVLEQFQGHLQTLFDWQKTLDDL 5385
Cdd:cd00176 88 WEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442626147 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 |
8.64e-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: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 424 LLNWVTNALPKDSG--VEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQ----RLETAFDVAEsKLGIAKLLD 497
Cdd:cd21218 15 LLRWVNYHLKKAGPtkKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEdlekRAEKVLQAAE-KLGCKYFLT 93
|
90 100
....*....|....*....|
gi 442626147 498 AEdvDVPKPDEKSIMTYVAQ 517
Cdd:cd21218 94 PE--DIVSGNPRLNLAFVAT 111
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7718-8161 |
9.25e-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: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7718 KHLSEMDKELEHIG-QVTTVGDLKDKLQEAEDAKISVEAVLLERNSL-LQEACEEWDQCERKIKDIRSWHEKTKQGLDSS 7795
Cdd:COG4913 235 DDLERAHEALEDAReQIELLEPIRELAERYAAARERLAELEYLRAALrLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7796 QQQKKPLRDQLGFCEKTLADINVQ-KTKLRLSIEKLEVHFRngmggdpRLSENVDDLVRVLDGLGELVKAKSQSLEQTLA 7874
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELE-------ERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7875 QIDVYQQQMQSLRQRIIQEEQQLRlvmaptylphDRERALAEQQDLITQELDELLQSLSSVEDGIANMN----------- 7943
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAE----------AALRDLRRELRELEAEIASLERRKSNIPARLLALRdalaealglde 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7944 -------------------QSSLDGMLHGLKLiqsNLEV---HERDAIELKNQ-----------AKKLPTDPATERLLND 7990
Cdd:COG4913 458 aelpfvgelievrpeeerwRGAIERVLGGFAL---TLLVppeHYAAALRWVNRlhlrgrlvyerVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7991 TV--------------------DRIDLL-------LRRTQQGIT---MI-ANAMHGQKKRQQEIDEY-------QQHLLE 8032
Cdd:COG4913 535 SLagkldfkphpfrawleaelgRRFDYVcvdspeeLRRHPRAITragQVkGNGTRHEKDDRRRIRSRyvlgfdnRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 8033 LEQWIIEVSAELASFEPTSDSSTDEQvlkSQVERSQQLLRTLKDRQQSMEDLVEQTRQLQ-----------SHPDVSPLA 8101
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAEL---DALQERREALQRLAEYSWDEIDVASAEREIAeleaelerldaSSDDLAALE 691
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 8102 DTLmEQLQSIITILREQVTVATKRIFTIEKRIVDLRKAKsEEAQRQRVLADSLIKPPTEA 8161
Cdd:COG4913 692 EQL-EELEAELEELEEELDELKGEIGRLEKELEQAEEEL-DELQDRLEAAEDLARLELRA 749
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
10541-10985 |
1.01e-03 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 46.89 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10541 LANVAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPS 10620
Cdd:COG4995 8 ALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10621 VASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLCAIHQ 10700
Cdd:COG4995 88 ALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10701 NLLISQQSVLSETPLESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYI 10780
Cdd:COG4995 168 LALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10781 HLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALATAMRMEQASIGQRISNLRAALKTWQGFLQRVTQLS 10860
Cdd:COG4995 248 AALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10861 ESYEQRVNQLQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELKECISPHDMKTIRQ 10940
Cdd:COG4995 328 AALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQ 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 442626147 10941 RNWLLWQQHADLDYQLANLInsIEERLSLLSNYQIRYDRISQWLQ 10985
Cdd:COG4995 408 LLRLLLAALALLLALAAYAA--ARLALLALIEYIILPDRLYAFVQ 450
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
7264-7480 |
1.03e-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: 46.30 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7264 QNLAGLHFNIQKLSHAIGNVQSQ----NSDLTLVNQQAQSLIRQADARNRQL--IEQDNAGLNRSWQDLVRSLEQRRDNL 7337
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEekalLKQLAALERRIAALARRIRALEQELaaLEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7338 QQLAEHWdgFENSLHAWEKALGRLEDKFRNVdptvrsrRHLEDTKNAIQELREESNQLKSSHKEIEALSKSILTflgevh 7417
Cdd:COG4942 107 AELLRAL--YRLGRQPPLALLLSPEDFLDAV-------RRLQYLKYLAPARREQAEELRADLAELAALRAELEA------ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626147 7418 kpSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSV 7480
Cdd:COG4942 172 --ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
847-1034 |
1.16e-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: 44.74 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 847 EEWLQLAEQKVNQSEDERL------------DFFQDIPVWKDKFDALASSANYLIASCEEPiAQQLRQRHGALSERFERL 914
Cdd:cd00176 13 EAWLSEKEELLSSTDYGDDlesveallkkheALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQERLEELNQRWEEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 915 FANTKQYMHAGDIIRSRQEYKSGIEQLSRWLRGAESVLDQRQVLGNSEQVKEYGQQLQQLASEIDDNEELFKTISRNFQS 994
Cdd:cd00176 92 RELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442626147 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 442626147 273 QKKTFTNWINSYL-----LKRVPPL--RIDDLINDLRDGTKLIALLEV-LSG---ERlPVEKGRVLRRphFLSNANTALQ 341
Cdd:cd21293 2 EKGSYVDHINRYLgddpfLKQFLPIdpSTNDLFDLVKDGVLLCKLINVaVPGtidER-AINTKKVLNP--WERNENHTLC 78
|
90 100 110
....*....|....*....|....*....|....*
gi 442626147 342 FLASKRI--KLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21293 79 LNSAKAIgcSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5626-6308 |
1.40e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5626 QTQVNKIIESLE------NQVNSHEKYKQAYNELQDWLRRTRIeveqcadchgEKDQVESRLNRLGDIQssslegKALLE 5699
Cdd:PRK03918 134 QGEIDAILESDEsrekvvRQILGLDDYENAYKNLGEVIKEIKR----------RIERLEKFIKRTENIE------ELIKE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5700 ACEELSQaviatsgsegqdnVAQEIKHLTSEwetlqtisrdaRSSLESCLAAWQTFLQKFNKINLWIETMNKRVTKSQEG 5779
Cdd:PRK03918 198 KEKELEE-------------VLREINEISSE-----------LPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5780 ENKTPEDLVNAKKLLEEVLAE----KDNVEDLNDNCELLMEQSACTRIRDQTIETQANYTKLLTSAQGLVAKIEKNLSDH 5855
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEieelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5856 TEFLNYKKEMDAWIEKAQQVLDDCSTDgdaaiiAQKLDTVNSLASRLpegqhllalvQDAYSKASNITPEDKQEKLRELM 5935
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEER------HELYEEAKAKKEEL----------ERLKKRLTGLTPEKLEKELEELE 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5936 TKVREDWDALgLAVKQKLSDLKQAQNRwndfaankdkLEKWLNETETTLKVAPETKGELSE--MKTLLERY----KTLSN 6009
Cdd:PRK03918 398 KAKEEIEEEI-SKITARIGELKKEIKE----------LKKAIEELKKAKGKCPVCGRELTEehRKELLEEYtaelKRIEK 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6010 ELKLKGNELEQLQSEARdlgtEVDAVNRLQSRCDKLKnDCSAHITALEQEMFDYNayhqsLQDVEKwllqisfqlmahns 6089
Cdd:PRK03918 467 ELKEIEEKERKLRKELR----ELEKVLKKESELIKLK-ELAEQLKELEEKLKKYN-----LEELEK-------------- 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6090 lfisnreqTQEQIKQHEALLVEIQKYQTNLDDLNAKGQAQIKRYESSTPAIRpTVESQLKNIQDSYNSLLQTSVQIKNRL 6169
Cdd:PRK03918 523 --------KAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD-ELEEELAELLKELEELGFESVEELEER 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6170 LESLAKFQEYEDTLDSIMRNLETYE---PIIQTELDAPATSLELAQNQLRcaqEMQNKLNNEKSRLAAAV-QACEAATAS 6245
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEkelKKLEEELDKAFEELAETEKRLE---ELRKELEELEKKYSEEEyEELREEYLE 670
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626147 6246 ISRPSSPLETAMQAIPERELIVRAKLEDLLDQvqshLGGLTASVSELEQQQKQRAELQDWVKK 6308
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEKLKEE----LEEREKAKKELEKLEKALERVEELREK 729
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3180-3271 |
1.52e-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: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3180 KWDEFDTIIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINELMDQGREI-----EGETDLNLK 3254
Cdd:pfam00435 2 LLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLideghYASEEIQER 81
|
90
....*....|....*..
gi 442626147 3255 LSRLNTRYQTLKNLCKE 3271
Cdd:pfam00435 82 LEELNERWEQLLELAAE 98
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
273-374 |
1.69e-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: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 273 QKKTFTNWINSYL-----LKRVPPL--RIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFL--SNANTALQFL 343
Cdd:cd21324 25 EKYAFVNWINKALendpdCKHVIPMnpNTDDLFKAVGDGIVLCKMINFSVPDTIDERTINKKKLTPFTiqENLNLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 442626147 344 ASKRIKLVNINPADLVDGRPPVVLGLIWTII 374
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 135
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
5492-6212 |
1.94e-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: 46.12 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5492 LELKEKVIMNTEQNGAAKIQEDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDVEPSVKTSDEFLN 5571
Cdd:TIGR00618 181 LALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5572 DLSEKRAALEKFrviQRDINGHNDIVEKINQRLKEDNSLDL--------KDFQPGLTKFDDLQTQVNKIIESLENQVNSH 5643
Cdd:TIGR00618 261 LLKQLRARIEEL---RAQEAVLEETQERINRARKAAPLAAHikavtqieQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5644 EKYKQAYNELQDWLR---RTRIEVEQCADCHGEKDQVESRLNRLGDIQSSslegkalLEACEELSQavIATSGSEGQDNV 5720
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSqeiHIRDAHEVATSIREISCQQHTLTQHIHTLQQQ-------KTTLTQKLQ--SLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5721 AQEIKHLTSEWETLQTISRDARSSLESCLaAWQTFLQKFNKINLWIETMNKRVTKSQEGENKTPEDLVNAKKLLEEVLAE 5800
Cdd:TIGR00618 409 QATIDTRTSAFRDLQGQLAHAKKQQELQQ-RYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETR 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5801 KDNVEDLNDNCELLMEQSACTRIRDQTIETQANY-----TKLLTSAQGLVAKIEKNLSD----HTEFLNYKKEMDAWIEK 5871
Cdd:TIGR00618 488 KKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDnpgplTRRMQRGEQTYAQLETSEEDvyhqLTSERKQRASLKEQMQE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5872 AQQvlddcstdgDAAIIAQKldtVNSLASRLPEGQHLLALVQ---DAYSKASNITPEDKQEKLRELMTKVREDWDALGLA 5948
Cdd:TIGR00618 568 IQQ---------SFSILTQC---DNRSKEDIPNLQNITVRLQdltEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5949 VKQK-LSDLKQAQNRWNDFAANKDKLEKWLNETETTLKVAPETKGELSEMKTLLEryktlsnELKLKGNELEQLQSEARD 6027
Cdd:TIGR00618 636 QCSQeLALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKE-------QLTYWKEMLAQCQTLLRE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6028 LGTEVDAVNRLQsrcDKLKNDCSAHITALEQEMFDYNAYHQSLQDVEKWLLQisfqlmahnslfisnrEQTQEQIKQHEA 6107
Cdd:TIGR00618 709 LETHIEEYDREF---NEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK----------------ARTEAHFNNNEE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6108 LLVEIQKyQTNLDDLNAKGQAQIKRYESSTPAIRPTVESQLKNIQDSYNSLLQTSVQIKNRLLESLAKFQEYEDTLDSIM 6187
Cdd:TIGR00618 770 VTAALQT-GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEIT 848
|
730 740
....*....|....*....|....*
gi 442626147 6188 RNLETYEPIIQTELDAPATSLELAQ 6212
Cdd:TIGR00618 849 HQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2712-2844 |
1.97e-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: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2712 ESPQNLAELTSDAELLRKDMQALQDSFDQIKGILDENVDLWSQYEQSnEQISNWLRDVEGRVKAETSSQvNLSEVPQKLQ 2791
Cdd:cd00176 69 EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGK-DLESVEELLK 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 442626147 2792 ELSILQQDVLAHEPIINNLEQTSQQLIEKNPEAR---IGQFVTHLVQRYQAVSKAL 2844
Cdd:cd00176 147 KHKELEEELEAHEPRLKSLNELAEELLEEGHPDAdeeIEEKLEELNERWEELLELA 202
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6442-6741 |
2.06e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6442 KIQELKGKAAQVAEVisnldgqqVEEQMKSLDRRFAD-LGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEELQa 6520
Cdd:PTZ00121 1419 KADEAKKKAEEKKKA--------DEAKKKAEEAKKADeAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK- 1489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6521 pkplgytpKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELEPVEYSQLESALRNLNtENRNLSGVLKAE-LDRA 6599
Cdd:PTZ00121 1490 --------KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE-EKKKADELKKAEeLKKA 1560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6600 LEASKARKSLENDLDK---------ARQWLKTKISEVRKLPVYHPLTSAEIEKKIQENRKYDDDAKQfNDSVLTDVQRQA 6670
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKnmalrkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLK 1639
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626147 6671 ANIMKDCDDADKAALQQILDEIAADYQTLKDESSKRGKSlddllQGRKAFEDSMKNMGDWLNEMETATEGE 6741
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE-----EAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
7130-7943 |
2.18e-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: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7130 RLEYMQLVAKFNDwVHEAELRLQnSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLV---HKQIQEAADKIwsslnNYEQSE 7206
Cdd:pfam12128 240 RPEFTKLQQEFNT-LESAELRLS-HLHFGYKSDETLIASRQEERQETSAELNQLLrtlDDQWKEKRDEL-----NGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7207 LSAELAQFQtkltntlanaktqqSELEKEAERWREYQQS-IDRVKATIERTKFVDEPVQNLAGLHfniQKLSHAIGNVQs 7285
Cdd:pfam12128 313 ADAAVAKDR--------------SELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERL---KALTGKHQDVT- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7286 qnsdltlvnQQAQSLIRQADARNRQLIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHW----DGFENSLHAWEKAL-GR 7360
Cdd:pfam12128 375 ---------AKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELreqlEAGKLEFNEEEYRLkSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7361 LED-KFRNVDPTVRSrrhledtknaiqelrEESNQLKSSHKEIEALSKSIltflgevhkpsaEAIQAKVDKLVEQQAKLn 7439
Cdd:pfam12128 446 LGElKLRLNQATATP---------------ELLLQLENFDERIERAREEQ------------EAANAEVERLQSELRQA- 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7440 DTLRDKEqqvskdLEEIEQVFRRISQLQDKLNALHEQLqsvhvydehIAQTEQLLITLNSQVQQAAEE-----SKLLVAQ 7514
Cdd:pfam12128 498 RKRRDQA------SEALRQASRRLEERQSALDELELQL---------FPQAGTLLHFLRKEAPDWEQSigkviSPELLHR 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7515 TTAHYQAKQNQlPSDiAQEFTALELLAERVQV------TMETKEKDFKRAKTVRTEYvDGVDEVQRWLLQAEVQVQERSL 7588
Cdd:pfam12128 563 TDLDPEVWDGS-VGG-ELNLYGVKLDLKRIDVpewaasEEELRERLDKAEEALQSAR-EKQAAAEEQLVQANGELEKASR 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7589 TPTQMKELLQriNHEITAIyeRFTLVKTNGQLIIENCRnSEEKTLVQTTIDQLAASLAQV----RGWLDEKKqavGDSLD 7664
Cdd:pfam12128 640 EETFARTALK--NARLDLR--RLFDEKQSEKDKKNKAL-AERKDSANERLNSLEAQLKQLdkkhQAWLEEQK---EQKRE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7665 AWTRFMNLYQIVMSWASEKRNFIDQTIE-LRTLPEARNKL--NDYVTSVKSIKPIVKHLSEMDKELEHIgqVTTVGDLKD 7741
Cdd:pfam12128 712 ARTEKQAYWQVVEGALDAQLALLKAAIAaRRSGAKAELKAleTWYKRDLASLGVDPDVIAKLKREIRTL--ERKIERIAV 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7742 KLQEAEDAKISVEAVLLERNSLLQEACEEwdqCERKIKDIRSwhEKTKQGLDSSQQQKKpLRDQLGFCEKTLADINVQKT 7821
Cdd:pfam12128 790 RRQEVLRYFDWYQETWLQRRPRLATQLSN---IERAISELQQ--QLARLIADTKLRRAK-LEMERKASEKQQVRLSENLR 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7822 KLRLSIEKL--------------EVHFRNGMGGD-----PRLSENVDDLVRVLDGlgeLVKAKS--------QSLEQTLA 7874
Cdd:pfam12128 864 GLRCEMSKLatlkedanseqaqgSIGERLAQLEDlklkrDYLSESVKKYVEHFKN---VIADHSgsglaetwESLREEDH 940
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626147 7875 QIDVYQQQMQSLRQrIIQEEQQLRLVMAPtylphDRERALAEQQDLITQELDELLQSLSSVEDGIANMN 7943
Cdd:pfam12128 941 YQNDKGIRLLDYRK-LVPYLEQWFDVRVP-----QSIMVLREQVSILGVDLTEFYDVLADFDRRIASFS 1003
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
7419-7532 |
2.25e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7419 PSAEAIQAKVDKLVEQ----------QAKLNDTLR--DKEQQVSKDLEE----IEQVFRRISQLQDKLNALHEQLQSVHV 7482
Cdd:PRK11281 36 PTEADVQAQLDALNKQklleaedklvQQDLEQTLAllDKIDRQKEETEQlkqqLAQAPAKLRQAQAELEALKDDNDEETR 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 442626147 7483 YD---EHIAQTEQLLITLNSQVQQA----AEESKLLVAQTTAHYQAkQNQLPSDIAQ 7532
Cdd:PRK11281 116 ETlstLSLRQLESRLAQTLDQLQNAqndlAEYNSQLVSLQTQPERA-QAALYANSQR 171
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
10792-11018 |
2.32e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.82 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10792 LDAMIQQLDQGEQQSKALQEQQQELarhcDD--ALATAMRMEQASIGQRISNLRAALKTwQGFLQRVTQLSESYEQRVNQ 10869
Cdd:PRK10929 50 LQSALNWLEERKGSLERAKQYQQVI----DNfpKLSAELRQQLNNERDEPRSVPPNMST-DALEQEILQVSSQLLEKSRQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10870 LQQEFGAAQKLLDANSEsLPTQPAA-------IEQLLGSL--------RAQRVQLGAQVSALESLtVTQEELKECISPHD 10934
Cdd:PRK10929 125 AQQEQDRAREISDSLSQ-LPQQQTEarrqlneIERRLQTLgtpntplaQAQLTALQAESAALKAL-VDELELAQLSANNR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10935 MKTIRQRNWLLWQQHADLDYQLANLINSIeerlsllsNYQiRYDRISQWLQRLEQRVEKDADVtamtnPEQAAKQLeqQV 11014
Cdd:PRK10929 203 QELARLRSELAKKRSQQLDAYLQALRNQL--------NSQ-RQREAERALESTELLAEQSGDL-----PKSIVAQF--KI 266
|
....
gi 442626147 11015 NSEL 11018
Cdd:PRK10929 267 NREL 270
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4460-4560 |
2.38e-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: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4460 QHWSEYEQLRDQCLAWIRDTDNNLHAIDLKEDLPKKRAQLDALKALQGDVRAKELEVDNVTEKAQTLLkgpsSNRASGPE 4539
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI----DEGHYASE 76
|
90 100
....*....|....*....|.
gi 442626147 4540 LVTKyqqifhKVKELNNRWQQ 4560
Cdd:pfam00435 77 EIQE------RLEELNERWEQ 91
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5418-6024 |
2.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5418 LAKEVMRRLEMHYQEHQQHHSLYEECQSWIEKTREKLSECEQIPGTLNEVQIKLNTVKNLRQGFETGQNKLRYLLELKEK 5497
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5498 VIMNTEQNGA--AKIQEDTEALKQdFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDVEPSVKTSDEFLNDLSE 5575
Cdd:PRK03918 274 EIEELEEKVKelKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5576 KRAALEKFRVIQRDINGHNDIVEKINQRLKEDNSLDLKDfqpgltKFDDLQTQVNKIIESLENQVNSHEKYKQAYNELQD 5655
Cdd:PRK03918 353 RLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK------ELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5656 WLRRTRIEVEQCADC------HGEKDQVESRLNRLGDIQSSSLEGKALLEAC----EELSQAVIATSGSEGQDNVAQEIK 5725
Cdd:PRK03918 427 AIEELKKAKGKCPVCgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLrkelRELEKVLKKESELIKLKELAEQLK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5726 HLTSEWE--TLQTISRDARSslesclaaWQTFLQKFNKINLWIETMNKRVTKSQEGENKTpEDLVNAKKLLEEVLAE-KD 5802
Cdd:PRK03918 507 ELEEKLKkyNLEELEKKAEE--------YEKLKEKLIKLKGEIKSLKKELEKLEELKKKL-AELEKKLDELEEELAElLK 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5803 NVEDLNDNCELLMEQsactRIRDqtietqanytklltsaqglvakIEKNLSDHTEFLNYKKEmdawIEKAQQVLDDCSTD 5882
Cdd:PRK03918 578 ELEELGFESVEELEE----RLKE----------------------LEPFYNEYLELKDAEKE----LEREEKELKKLEEE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5883 GDAAI--IAQKLDTVNSLASRLPEgqhllalVQDAYSkasnitpEDKQEKLRELMTKVREdwdalglAVKQKLSDLKQAQ 5960
Cdd:PRK03918 628 LDKAFeeLAETEKRLEELRKELEE-------LEKKYS-------EEEYEELREEYLELSR-------ELAGLRAELEELE 686
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626147 5961 NRWNDFAANKDKLEKWLNETETTLKVAPETKGELSEMKTLLERYKTLSNELKLKG-NELEQLQSE 6024
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERAlSKVGEIASE 751
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3952-4136 |
2.52e-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: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3952 DYSGNKAALQARLQKINEIQDALPEGVAKLKSLEDHIEQQASNIPARSKEVMARdLANLHADFEKFGASLSDVKSGLENR 4031
Cdd:cd00176 27 DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER-LEELNQRWEELRELAEERRQRLEEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4032 LQQWNDYEiNLDRLITWLGEAENSLKNYNLKSSFEEKEEQLNGFQSLAQNLRQNEADFDKVKDDTSELVQSS---GETRI 4108
Cdd:cd00176 106 LDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGhpdADEEI 184
|
170 180
....*....|....*....|....*...
gi 442626147 4109 AVNVQQVSSRFQSIQATAKEILKKCEQA 4136
Cdd:cd00176 185 EEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
10501-11262 |
2.66e-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: 45.60 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10501 LRDIVAKIAAD--VGLDASALMQGELDA------LGQRLAECKDAITTLANVAETQDKERKELDkevTLAKAYFNnvqqD 10572
Cdd:pfam12128 198 VKSMIVAILEDdgVVPPKSRLNRQQVEHwirdiqAIAGIMKIRPEFTKLQQEFNTLESAELRLS---HLHFGYKS----D 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10573 ISREAPQNpKESEEQLAALRAHLQTLartEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTfqeyhRLST 10652
Cdd:pfam12128 271 ETLIASRQ-EERQETSAELNQLLRTL---DDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDA-----DIET 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10653 RLARSQNsseaLRLWRQYLQHVQsflscaipedysslreqqqlcAIHQNLLISQQSVLSET-PLESELSEQYKALTNLHN 10731
Cdd:pfam12128 342 AAADQEQ----LPSWQSELENLE---------------------ERLKALTGKHQDVTAKYnRRRSKIKEQNNRDIAGIK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10732 ETLSRImqRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIhlKRVPHLKHRLDAMIQQLDQGEQQskalqE 10811
Cdd:pfam12128 397 DKLAKI--REARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLK--SRLGELKLRLNQATATPELLLQL-----E 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10812 QQQELARHCDDALaTAMRMEQASIGQRISNLRAALKTWQGFLQRVtqlsesyEQRVNQLQQEFGAAQKLLDANSES---- 10887
Cdd:pfam12128 468 NFDERIERAREEQ-EAANAEVERLQSELRQARKRRDQASEALRQA-------SRRLEERQSALDELELQLFPQAGTllhf 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10888 LPTQPAAIEQLLGSLRAQ----RVQL-----GAQVSALESLTVTQEELKECISP--HDM-KTIRQRNWLL-------WQQ 10948
Cdd:pfam12128 540 LRKEAPDWEQSIGKVISPellhRTDLdpevwDGSVGGELNLYGVKLDLKRIDVPewAASeEELRERLDKAeealqsaREK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10949 HADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQRL--EQRVEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKE-R 11025
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLfdEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKhQ 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11026 EWLLSTSRELLTLYSEpevrsqvqqqsdslidRWQRLKYLAKQKATKIGELKMTLLRLEERIAlirAWLFEVESQLDKPL 11105
Cdd:pfam12128 700 AWLEEQKEQKREARTE----------------KQAYWQVVEGALDAQLALLKAAIAARRSGAK---AELKALETWYKRDL 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11106 NFESYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLnlvemllndadSWRtqvntsglaasaQNLEQRWKNVCSQSAERKA 11185
Cdd:pfam12128 761 ASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVL-----------RYF------------DWYQETWLQRRPRLATQLS 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11186 RILT-IWNLLQQLIKLTAEHKNWLGKQESQIAGFERDQ----KSHSKHKLEERQM---ELRAKLEELE-SQSVNLRQLEQ 11256
Cdd:pfam12128 818 NIERaISELQQQLARLIADTKLRRAKLEMERKASEKQQvrlsENLRGLRCEMSKLatlKEDANSEQAQgSIGERLAQLED 897
|
....*.
gi 442626147 11257 IYAKLA 11262
Cdd:pfam12128 898 LKLKRD 903
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
6684-7509 |
2.79e-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: 45.42 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6684 ALQQILDEIAadyqtlkdESSKRGKSLDDLLQGRKAFEDSMKNMGDWLNEMETATEGELRT-TSLPVLEEQLAHYKKLLS 6762
Cdd:TIGR00606 170 ALKQKFDEIF--------SATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIrDQITSKEAQLESSREIVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6763 DAENKgglINDVSEQGKSILPTLSNAdkLKLNDDIKNMKDRYGRIKNT--------------IDDRVNAL-GDHIKKYKD 6827
Cdd:TIGR00606 242 SYENE---LDPLKNRLKEIEHNLSKI--MKLDNEIKALKSRKKQMEKDnselelkmekvfqgTDEQLNDLyHNHQRTVRE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6828 AKSRLAECSQFLGNIQQKLRELNRPiGSRIEDVQDLLGA-----YEGILKELKDSKSKMGDMQMDDLPELQSILAQQDDM 6902
Cdd:TIGR00606 317 KERELVDCQRELEKLNKERRLLNQE-KTELLVEQGRLQLqadrhQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNF 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6903 IKLI----EDQLAHLRQLLLLREQFIALINEIIAFI-MKYTDVIIDIENSPDSLEDKINKYDDVIVKIQECEGVLASAND 6977
Cdd:TIGR00606 396 HTLVierqEDEAKTAAQLCADLQSKERLKQEQADEIrDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6978 KGQ---KIASEGNAADKNSITEQLQSLKNQLQNlrkavesqrqkHQLQLESHKKMAAELSEILDwlhSHEGAAKSRPLLD 7054
Cdd:TIGR00606 476 LDQelrKAERELSKAEKNSLTETLKKEVKSLQN-----------EKADLDRKLRKLDQEMEQLN---HHTTTRTQMEMLT 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7055 RDPESVERELQKHQSL-SQDIESYLNKFNKINDGVKTEigmpSSLLEMLSEGRSLVASLPHELE--EREKYLKNNRDSRL 7131
Cdd:TIGR00606 542 KDKMDKDEQIRKIKSRhSDELTSLLGYFPNKKQLEDWL----HSKSKEINQTRDRLAKLNKELAslEQNKNHINNELESK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7132 EYMQLvaKFNDWVHEAelrLQNSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLVHKQIQEAADKIWSSLNNYEQS-ELSAE 7210
Cdd:TIGR00606 618 EEQLS--SYEDKLFDV---CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVfQTEAE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7211 LAQFQTKLTNTLANAKTQQSELEKEAERwREYQQSIDRVKATIeRTKFVDEPVQNLAGLHFNIQKLSHAIgnvQSQNSDL 7290
Cdd:TIGR00606 693 LQEFISDLQSKLRLAPDKLKSTESELKK-KEKRRDEMLGLAPG-RQSIIDLKEKEIPELRNKLQKVNRDI---QRLKNDI 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7291 TLVNQQAQSLIRQADARNrqlIEQDNAGLNRSWQDLVRSLEQRrdnLQQLAEHWDGFENSLhAWEKALGRLEDKFRNVDP 7370
Cdd:TIGR00606 768 EEQETLLGTIMPEEESAK---VCLTDVTIMERFQMELKDVERK---IAQQAAKLQGSDLDR-TVQQVNQEKQEKQHELDT 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7371 TVRS----RRHLEDTKNAIQELREESNQLKSSHKEI-------EALSKSILTFLGEVHKPSAEAIQAKVDKLVEQQAKlN 7439
Cdd:TIGR00606 841 VVSKielnRKLIQDQQEQIQHLKSKTNELKSEKLQIgtnlqrrQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFL-E 919
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442626147 7440 DTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVHVY-----DEHIAQTEQLLITLNSQVQQAAEESK 7509
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgkDDYLKQKETELNTVNAQLEECEKHQE 994
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
7356-7507 |
2.88e-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: 43.76 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7356 KALGRLEDKFRNVdptvrsRRHLEDTKNAIQELREESNQLKSSHKEIEALSKSILTFLGEVHKP-SAEAIQAKVDKLVEQ 7434
Cdd:COG1579 31 AELAELEDELAAL------EARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkEYEALQKEIESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626147 7435 QAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLqsvhvyDEHIAQTEQLLITLNSQVQQAAEE 7507
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL------DEELAELEAELEELEAEREELAAK 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7729-8148 |
2.96e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7729 HIGQVTTVGDLKDKLQEAEDAKISVEAVLLErnslLQEACEEWDQCERKIKDIRSWHEKTKQgldssQQQKKPLRDQLGF 7808
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEE----LEELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7809 CEKTLADINVQKTKLRLSIEKLEVHFRNGmggdPRLSENVDDLVRVLDGLGELVK-AKSQSLEQTLAQIDVYQQQMQSLR 7887
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEEL----EELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7888 QRIIQEEQQLRLVMAPTYLPHDRERALAEQQDLitQELDELLQSLSSVEdGIANMNQSSLDGMLHGLKLIQSNLEV---- 7963
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERL--KEARLLLLIAAALL-ALLGLGGSLLSLILTIAGVLFLVLGLlall 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7964 ---HERDAIELKNQAKKLPTDPATERL----LNDTVDRIDLLLRRTQQGITMIANAMHGQKKRQQEIDEYQQHLLeleqw 8036
Cdd:COG4717 290 fllLAREKASLGKEAEELQALPALEELeeeeLEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ----- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 8037 IIEVSAELASFEPTSDSSTDEQVLK--SQVERSQQLLRTLKDRQQSMEDLVEQTRQLQSHPDVSPLADTLmEQLQSIITI 8114
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEEL-EELEEELEE 443
|
410 420 430
....*....|....*....|....*....|....
gi 442626147 8115 LREQVTVATKRIFTIEKRIVDLRKAKSEEAQRQR 8148
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELLQE 477
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3828-3913 |
3.09e-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: 41.15 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3828 NWLDQVEKLIHNENPASwtSAQEIRSKLYKYKATNQDINSHKRIVEAVNEKAAALLGSAAPAnADEISKAVAEVNKRYDQ 3907
Cdd:pfam00435 15 SWIEEKEALLSSEDYGK--DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYA-SEEIQERLEELNERWEQ 91
|
....*.
gi 442626147 3908 VGQDCA 3913
Cdd:pfam00435 92 LLELAA 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
11053-11774 |
3.30e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11053 DSLIDRWQRLKYLAKQKATKIGELKMTLLRLEERIALIRAWLFEVESQLDKpLNFESYTPNVIEAKLKEHEQIQRSIEHH 11132
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE-LQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11133 SSNVGEVLNLVemlLNDADSWRTQVNTSgLAASAQNLEQRWKNVCSQSAERKARILTIWNLLQQLIKLTAEhknwLGKQE 11212
Cdd:TIGR02168 314 LERQLEELEAQ---LEELESKLDELAEE-LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ----LETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11213 SQIAGFERDQKSHSKhkleeRQMELRAKLEELESqsvNLRQLEQIYAKLAMsagvEPENIQKLTLPTKVmvsmwrqltpr 11292
Cdd:TIGR02168 386 SKVAQLELQIASLNN-----EIERLEARLERLED---RRERLQQEIEELLK----KLEEAELKELQAEL----------- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11293 chALLDAIDKDAKLMREFNNAQLEatnslnAIQKALEQLPSAenQQTSKAEPKAVLQRLESLEKKLQDAQQHVQQADNLA 11372
Cdd:TIGR02168 443 --EELEEELEELQEELERLEEALE------ELREELEEAEQA--LDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11373 QEAKTRTKQQPQLKQLLELVSAYTTLWQTV-QTRIVTLKTTWLTRAAQAAASLPVSEAANAAVQVNTLSQRKLRQAQQMQ 11451
Cdd:TIGR02168 513 KNQSGLSGILGVLSELISVDEGYEAAIEAAlGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDRE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11452 RETSITAKDAYIMELQTAITECQNNLDE-LQRTVV--------DKTRKPGP-----------------------QKIAKL 11499
Cdd:TIGR02168 593 ILKNIEGFLGVAKDLVKFDPKLRKALSYlLGGVLVvddldnalELAKKLRPgyrivtldgdlvrpggvitggsaKTNSSI 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11500 LGNAQSSTELVKHLSHLLLTECKADDQAAEVDT-VAELTLRFDTLQSQW--KARQQHDQNAS-EVGRLTCPLCTQRNWQQ 11575
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKeLEELEEELEQLRKELeeLSRQISALRKDlARLEAEVEQLEERIAQL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11576 IDNDLWRLEQWLQFAESTQKAQSAPPSNIELLEDVTQDHREFLLDLESHKSIISSLNvvgdhlATHTLDTEKARQLRSRL 11655
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR------AELTLLNEEAANLRERL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11656 EADNERwnnvcINATKwqgllqtalmgnsefhQTIGELVEWLQRTEQNIKASEPV--DLTEERSVLETKFKKFKDLRAEL 11733
Cdd:TIGR02168 827 ESLERR-----IAATE----------------RRLEDLEEQIEELSEDIESLAAEieELEELIEELESELEALLNERASL 885
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 442626147 11734 ERCEPRVVSLQDAADQLLRSVEGSEQQSQHTYERTLSRLTD 11774
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
10373-10618 |
3.50e-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: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10373 ERLRKATERLEGLAGDLHNREQLIDELKGAAKPLIESCDV-QIVEQIEsAVQEAVVAWNDTSENLQQLRTRYQRAVELWD 10451
Cdd:COG4913 624 EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVaSAEREIA-ELEAELERLDASSDDLAALEEQLEELEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10452 KYRNAsaavknsIDQQMDAVKSLEQPLDALQhakvcqdnlttqnDRILELRDIVAKIAADVGLDASALMQGELDALGQRL 10531
Cdd:COG4913 703 ELEEE-------LDELKGEIGRLEKELEQAE-------------EELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10532 AEcKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPkESEEQLAALRAHLQT--LARTEEQLRQLK 10609
Cdd:COG4913 763 VE-RELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADL-ESLPEYLALLDRLEEdgLPEYEERFKELL 840
|
....*....
gi 442626147 10610 ERHQNSEVA 10618
Cdd:COG4913 841 NENSIEFVA 849
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10225-10847 |
3.52e-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: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10225 LRDQLQAIQEGISNQRKHQAKISVILDECEAAERQGADVLEKAVADCQAAGEELVISWQEIMRirqmlhtlpmrlkmsvs 10304
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR----------------- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10305 pvkLERDISQLQDDHAFLESKctniMAILRSRLAVWlryERQLELVHGSVQETDfmmelirvhgqvdyERLRKATERLEG 10384
Cdd:COG1196 300 ---LEQDIARLEERRRELEER----LEELEEELAEL---EEELEELEEELEELE--------------EELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10385 LAGDLHNREQLIDELKGAAKPLIEScdvqiVEQIESAVQEAVVAWNDTSENLQQLRTRYQRAVELWDKYRNASAAVKNSI 10464
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEE-----LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10465 DQQMDAVKSLEQPLDALQHAKVCQDNLTTQNDRIL-----ELRDIVAKIAADVGLDASALMQGELDALGQRLAECKDAIT 10539
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLaelleEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10540 TLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPKESEEQLAALRAHLQTL---ARTEEQLRQLKERHQNSE 10616
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagRATFLPLDKIRARAALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10617 VAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEALRlwrqylqhvqsflscaipedysslreqqqlc 10696
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA------------------------------- 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10697 aihQNLLISQQSVLSETPLESELSEQYKALTNLHNETLSRIMQRNGELERRVSgwnayRQQLAALLDWLRQREAERNALQ 10776
Cdd:COG1196 640 ---VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA-----EEELELEEALLAEEEEERELAE 711
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442626147 10777 LRyihlKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHcDDALATAMRMEQASIGQRISNLRAALK 10847
Cdd:COG1196 712 AE----EERLEEELEEEALEEQLEAEREELLEELLEEEELLEE-EALEELPEPPDLEELERELERLEREIE 777
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
5441-6230 |
3.65e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.43 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5441 EECQSWIEKTREKLSECEQipgtlnevqiklNTVKNLRQGFETGQNKLRYLLELKEKVIMNTEQNGAAKIQEDTEALKQD 5520
Cdd:TIGR01612 699 DDLKSKIDKEYDKIQNMET------------ATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILEDFKNKEKE 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5521 FDKLLVDLNDVRQKLANRLAQLEEIFKLY--KILIEWL--EDVEPSVKTSDEFLNDLSEKRAalEKFRVI---------- 5586
Cdd:TIGR01612 767 LSNKINDYAKEKDELNKYKSKISEIKNHYndQINIDNIkdEDAKQNYDKSKEYIKTISIKED--EIFKIInemkfmkddf 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5587 --------------QRDIN-GHNDIVEKINQRLKEDNSLDLKDFQpglTKFDDLQTQVNKIIESLENQVNSHEKYKQayn 5651
Cdd:TIGR01612 845 lnkvdkfinfenncKEKIDsEHEQFAELTNKIKAEISDDKLNDYE---KKFNDSKSLINEINKSIEEEYQNINTLKK--- 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5652 eLQDWLRRTRIEVEQCADCHGEKDQVESRLNR-LGDIQSSSLEGKA--------LLEACEELSQAVIATSGSEGQDNVAQ 5722
Cdd:TIGR01612 919 -VDEYIKICENTKESIEKFHNKQNILKEILNKnIDTIKESNLIEKSykdkfdntLIDKINELDKAFKDASLNDYEAKNNE 997
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5723 EIKHLTSEWETLQTISRDarsslesclAAWQTFLQK---FNKINLWIETMNKRVTK------------SQEGENKTPEdl 5787
Cdd:TIGR01612 998 LIKYFNDLKANLGKNKEN---------MLYHQFDEKekaTNDIEQKIEDANKNIPNieiaihtsiyniIDEIEKEIGK-- 1066
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5788 vNAKKLLEEVLAEKD-NVEDLNDNCELLMEQSACTRIRDQTIETQANYTKLLTSAQGLVAKIEKNLSDHTEFL----NYK 5862
Cdd:TIGR01612 1067 -NIELLNKEILEEAEiNITNFNEIKEKLKHYNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKkkseNYI 1145
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5863 KEMDAWIEKAQQVLDDCSTDGDAAIIAQKLDTVnslasrlpegqhllalvqdayskasnITPEDKQEKLRELMTKVREDW 5942
Cdd:TIGR01612 1146 DEIKAQINDLEDVADKAISNDDPEEIEKKIENI--------------------------VTKIDKKKNIYDEIKKLLNEI 1199
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5943 DalglAVKQKLSDLKQAQNRWNDFAANKDKLekwlnetetTLKVAPETKGELSEMKTLLERYKTLSNELKLKGNELEQLQ 6022
Cdd:TIGR01612 1200 A----EIEKDKTSLEEVKGINLSYGKNLGKL---------FLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEM 1266
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6023 SEARDLGTEVDAVNRLQSRCDKL-----KNDCS-AHITALEQEMFDYNAYHQSLQDVEKWLLQISFQLMAHNS------- 6089
Cdd:TIGR01612 1267 GIEMDIKAEMETFNISHDDDKDHhiiskKHDENiSDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSdinlyln 1346
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 6090 --------LFISNREQTQEQIKQHEAllvEIQKYQTNLDDLNAKGQAQIK--RYESSTPAIRPTVESQL--KNIqdsyNS 6157
Cdd:TIGR01612 1347 eianiyniLKLNKIKKIIDEVKEYTK---EIEENNKNIKDELDKSEKLIKkiKDDINLEECKSKIESTLddKDI----DE 1419
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626147 6158 LLQTSVQIKNRLLESlakfqeyEDTLDSIMRNLETYEPIIQTELDapatSLELAQNQLRcaQEMQNKLNNEKS 6230
Cdd:TIGR01612 1420 CIKKIKELKNHILSE-------ESNIDTYFKNADENNENVLLLFK----NIEMADNKSQ--HILKIKKDNATN 1479
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
11531-11680 |
3.95e-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: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11531 DTVAELTLRFDTLQSQWKARQQHDQNASEVgrltcplctqrnwQQIDNDLWRLEQWLQFAESTQKAQSaPPSNIELLEDV 11610
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDL-------------QQFFRDADDLEQWLEEKEAALASED-LGKDLESVEEL 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11611 TQDHREFLLDLESHKSIISSLNVVGDHLATHtLDTEKARQLRSRLEADNERWNNVCINATKWQGLLQTAL 11680
Cdd:cd00176 145 LKKHKELEEELEAHEPRLKSLNELAEELLEE-GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1253-1444 |
3.99e-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: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 1253 FYQSLKDVEKELQLEQQALNRNEDVDSILQRNQQF----LLQQDVVPRLERcLQNMQRLAQAHRQQQPGDIS-LDQAYDN 1327
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLkkheALEAELAAHEER-VEALNELGEQLIEEGHPDAEeIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 1328 AKSQWQLLSNKLGDMRQTLQQIPAQWQgYHLKFNDMVDWMNGVDQSLKNIVNeVNTMEEFEKEKVVFQKICQDADNKRED 1407
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEAHEPR 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 442626147 1408 MKWLVKTLDSLLSYATEDEANLEQKKLEDLIARYKNL 1444
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEEL 198
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
10732-11031 |
4.06e-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: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10732 ETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALqLRYIHLKRVPHLKHRLDAMIQQLDQgeqqskaLQE 10811
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKL-LPQANLLADETLADRLEELREELDA-------AQE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10812 QQQELARHcddalatamrmeqasiGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQefgaAQKLLDANSEslptq 10891
Cdd:COG3096 908 AQAFIQQH----------------GKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRR----LKQQIFALSE----- 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10892 paaieqllgsLRAQRVQLGAQVSAlESLTVTQ---EELKECISphDMKTIRQRNWLLWQQHADlDYQLANlinsiEERLS 10968
Cdd:COG3096 963 ----------VVQRRPHFSYEDAV-GLLGENSdlnEKLRARLE--QAEEARREAREQLRQAQA-QYSQYN-----QVLAS 1023
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626147 10969 LLSNYQIRYdrisQWLQRLEQRVEkDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWLLST 11031
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 |
4.14e-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: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2209 KDKFHALEHNFGQALQE------NRAKLDEILRQHPTLNNIDQIIADLVALNDALK-YQAD---------------LKNR 2266
Cdd:TIGR01612 458 KSKLKALEKRFFEIFEEewgsydIKKDIDENSKQDNTVKLILMRMKDFKDIIDFMElYKPDevpskniigfdidqnIKAK 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2267 IHDEGSLLMREDIASMPAIQESLLIMDK-----NYDS--LQNEIADRIQKY----------NLISQALREYADSKDKFSK 2329
Cdd:TIGR01612 538 LYKEIEAGLKESYELAKNWKKLIHEIKKeleeeNEDSihLEKEIKDLFDKYleiddeiiyiNKLKLELKEKIKNISDKNE 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2330 ELKKAEDLYNAIPQQPRDETEL-----HQASE--KTRKTMEQLRKSKLSldelERRGNNVGKLFSAIGEpIPQEVPQEVT 2402
Cdd:TIGR01612 618 YIKKAIDLKKIIENNNAYIDELakispYQVPEhlKNKDKIYSTIKSELS----KIYEDDIDALYNELSS-IVKENAIDNT 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2403 AAKQHWQDLH---DKTAKNAHVYETEAVI--WSQIEDAKKDLLPWLSETNQGLCDAADNSIEiefgpmrlskyrTELPSY 2477
Cdd:TIGR01612 693 EDKAKLDDLKskiDKEYDKIQNMETATVElhLSNIENKKNELLDIIVEIKKHIHGEINKDLN------------KILEDF 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2478 QALKDSIVEKTNDLVKINkgaeipalSALNKLLSeQFAEVNNNADRLSAITTSFNDQEQELRRRSKEAGERVSKLREQLI 2557
Cdd:TIGR01612 761 KNKEKELSNKINDYAKEK--------DELNKYKS-KISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIF 831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2558 KC--------DDMSGDNNKIMERLQQCRalrgELDNSGNE-----IDNIKQKV-DELRNLYPTF---SESIIPKELNNVQ 2620
Cdd:TIGR01612 832 KIinemkfmkDDFLNKVDKFINFENNCK----EKIDSEHEqfaelTNKIKAEIsDDKLNDYEKKfndSKSLINEINKSIE 907
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2621 KRYENVDLYAK-----KIESSLLQFLKKFHaDKVGMLKRIIATQREKVAWCQ--PESSSDKYN--LDVKKSSLQEVSK-- 2689
Cdd:TIGR01612 908 EEYQNINTLKKvdeyiKICENTKESIEKFH-NKQNILKEILNKNIDTIKESNliEKSYKDKFDntLIDKINELDKAFKda 986
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2690 SIDDCKARHAETLKSLEMLKA---VESPQNLAELTSDAELLRKDMQalQDSFDQIKGILDENVDLWSQYEQSNEQISNWL 2766
Cdd:TIGR01612 987 SLNDYEAKNNELIKYFNDLKAnlgKNKENMLYHQFDEKEKATNDIE--QKIEDANKNIPNIEIAIHTSIYNIIDEIEKEI 1064
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2767 -RDVEGR----VKAETSSQVNLSEVPQKLQELSIlqQDVLAHEpiinNLEQTSQQLIEKNPEARIGQFVTHLVQRYQAVS 2841
Cdd:TIGR01612 1065 gKNIELLnkeiLEEAEINITNFNEIKEKLKHYNF--DDFGKEE----NIKYADEINKIKDDIKNLDQKIDHHIKALEEIK 1138
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2842 KALTSYIDKIRgAQLSNANFAKAAKDFNEwfgdakiefqelarmgSPGSSSATAQQLQT---VKNYIktFDNGQILLNNA 2918
Cdd:TIGR01612 1139 KKSENYIDEIK-AQINDLEDVADKAISND----------------DPEEIEKKIENIVTkidKKKNI--YDEIKKLLNEI 1199
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2919 VDIgealypvvspdnrERIRADLRQMRE-KFDYLRDEANAFMQQVEGvliQKTSIEESYTQVSHY---LNESKAKVPTTD 2994
Cdd:TIGR01612 1200 AEI-------------EKDKTSLEEVKGiNLSYGKNLGKLFLEKIDE---EKKKSEHMIKAMEAYiedLDEIKEKSPEIE 1263
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2995 ELYPTLATKKAALQ-------NYKTQLQEITLHKNALKQLHDKAVTLCDDESERKTDESIQEynTLSKKISDrittvgnh 3067
Cdd:TIGR01612 1264 NEMGIEMDIKAEMEtfnishdDDKDHHIISKKHDENISDIREKSLKIIEDFSEESDINDIKK--ELQKNLLD-------- 1333
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3068 VVKHEA-YDQVLEKAQDWLNTIK----SEAIDILNETTFEKE----GAEEKLLVVENLLQhKPEGDSIFDTCHKLLETVL 3138
Cdd:TIGR01612 1334 AQKHNSdINLYLNEIANIYNILKlnkiKKIIDEVKEYTKEIEennkNIKDELDKSEKLIK-KIKDDINLEECKSKIESTL 1412
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3139 TQTHPSGhpallkgfeepkqswedfmtlCQDSLVKLKQ-LCSKWDEFDTIIEELDNWMKNVEAVVKNQNLkstAEAKNAH 3217
Cdd:TIGR01612 1413 DDKDIDE---------------------CIKKIKELKNhILSEESNIDTYFKNADENNENVLLLFKNIEM---ADNKSQH 1468
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3218 LKQLQ--DISKDIERRGAAINELMDQGREIEGETDLNLKLSRLNTR-YQTLKNLCKESIAKYVNYV---------KDHES 3285
Cdd:TIGR01612 1469 ILKIKkdNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKElFEQYKKDVTELLNKYSALAiknkfaktkKDSEI 1548
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3286 FDKDFDSFKQN--LQSSVDElAKTNEIVGDQSVLQDQQNKlREMSDKRILDStlfeglidrgeklygHTSPEGREIIRQQ 3363
Cdd:TIGR01612 1549 IIKEIKDAHKKfiLEAEKSE-QKIKEIKKEKFRIEDDAAK-NDKSNKAAIDI---------------QLSLENFENKFLK 1611
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3364 LRALRTlwdnYTDDLNSATQKIDQcllQFNEFSI-AQDQLTKWLKDVDKAMQSHTEP----KTTLQEKRAQLQNhkllhq 3438
Cdd:TIGR01612 1612 ISDIKK----KINDCLKETESIEK---KISSFSIdSQDTELKENGDNLNSLQEFLESlkdqKKNIEDKKKELDE------ 1678
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3439 eitthnvlVDNVCDKAQILVDQIKDNslnvYLTSIKQLFQSIVQKSDEILHNLDDCVQkhNELNNALSSAKT-----WIS 3513
Cdd:TIGR01612 1679 --------LDSEIEKIEIDVDQHKKN----YEIGIIEKIKEIAIANKEEIESIKELIE--PTIENLISSFNTndlegIDP 1744
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 3514 NEKaklleCDDAYGEKADIKRKIETLGQLAQNkpqAMKIISDIRDLFEKVKATTSEKGNEVLdkEIEELETTMKSHFDDI 3593
Cdd:TIGR01612 1745 NEK-----LEEYNTEIGDIYEEFIELYNIIAG---CLETVSKEPITYDEIKNTRINAQNEFL--KIIEIEKKSKSYLDDI 1814
|
....
gi 442626147 3594 EGIE 3597
Cdd:TIGR01612 1815 EAKE 1818
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4252-4347 |
4.21e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.78 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4252 FDEIADSLKSWLDETENALpADIELKTTLDEKRNKLQTYRDILNDINNHQVELGNLQEIAANL----PEKTELVDQIIKD 4327
Cdd:smart00150 3 FLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieegHPDAEEIEERLEE 81
|
90 100
....*....|....*....|
gi 442626147 4328 ISDRFGKLQKRAQNYVERYE 4347
Cdd:smart00150 82 LNERWEELKELAEERRQKLE 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2538-2873 |
4.62e-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: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2538 LRRRSKEAGERVSKLREQLIKCDDMSGDNNKIMERLQ-------QCRALRGELDN-----SGNEIDNIKQKVDELRNLYP 2605
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLErqaekaeRYKELKAELRElelalLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2606 TFSESI--IPKELNNVQKRYENVDLYAKKIESSLLQFLKKFHA--DKVGMLKRIIATQREKVAWCQPESSSDKYNLDVKK 2681
Cdd:TIGR02168 250 EAEEELeeLTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaNEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2682 SSLQEVSKSIDDCKARHAETLKSLEMLKA--VESPQNLAELTSDAELLRKDMQALQDSFDQIKGILDEN----VDLWSQY 2755
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLnneiERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2756 EQSNEQISNWLRDVEGRVKAETSSQvnLSEVPQKLQELSILQQDVLAHEPIINNLEQTSQQLIEKNPEARigQFVTHLVQ 2835
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL--DAAERELA 485
|
330 340 350
....*....|....*....|....*....|....*...
gi 442626147 2836 RYQAVSKALTSYIDKIRGAQLSNANFAKAAKDFNEWFG 2873
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILG 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10766-11488 |
4.74e-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: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10766 RQREAERNaLQLRYIHLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELaRHCDDALAT-----------AMRMEQAS 10834
Cdd:TIGR02168 173 RRKETERK-LERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAEL-RELELALLVlrleelreeleELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10835 IGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKLLDAnsesLPTQPAAIEQLLGSLRAQRVQLGAQVS 10914
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR----LEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10915 ALESltvTQEELKEcisphDMKTIRQRNWLLWQQHADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQRLEQRVekd 10994
Cdd:TIGR02168 327 ELES---KLDELAE-----ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI--- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10995 advtamtnpEQAAKQLEQQVnSELQLRDKEREWLLSTSRELLTLYSEPEVRsQVQQQSDSLIdrwQRLKYLAKQKATKIG 11074
Cdd:TIGR02168 396 ---------ASLNNEIERLE-ARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELE---EELEELQEELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11075 ELKmtllRLEERIALIRAWLFEVESQLDKpLNFESYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDADSWR 11154
Cdd:TIGR02168 462 ALE----ELREELEEAEQALDAAERELAQ-LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11155 TQVNTSgLAASAQ-----NLEQRWKNVCSQSAERKARILTIWNLLQQLIKLTAEHKNWLGKQEsqiaGFERDQKSHSKHK 11229
Cdd:TIGR02168 537 AAIEAA-LGGRLQavvveNLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIE----GFLGVAKDLVKFD 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11230 LEERQ------------------MELRAKLEELESqSVNLrQLEQIYAKLAMSAGVEPENIQKLTLPTKVmvsmwRQLTP 11291
Cdd:TIGR02168 612 PKLRKalsyllggvlvvddldnaLELAKKLRPGYR-IVTL-DGDLVRPGGVITGGSAKTNSSILERRREI-----EELEE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11292 RCHALLDAIdkdaklmREFNNAQLEATNSLNAIQKALEQLPSAENQQTSK-AEPKAVLQRLESLEKKLQDAQQhvQQADN 11370
Cdd:TIGR02168 685 KIEELEEKI-------AELEKALAELRKELEELEEELEQLRKELEELSRQiSALRKDLARLEAEVEQLEERIA--QLSKE 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 11371 LAQEAKTRTKQQPQLKQLLELVSAYTTLWQTVQTRIVTLKTTWLT-----RAAQAAASLPVSEAANAAVQVNTLSQRKLR 11445
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealDELRAELTLLNEEAANLRERLESLERRIAA 835
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 442626147 11446 QAQQMQRETSITAKDAYIME-LQTAITECQNNLDELQRTVVDKT 11488
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIEsLAAEIEELEELIEELESELEALL 879
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
10371-10803 |
4.88e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10371 DYERLRKATERLEGLAGDLHNREQLIDELKGAAKpLIESCDVQIVEQIESAVQEAVVAWNDTSENLQQLRTRYQRAVELW 10450
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEE-ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10451 DKYRNASAAVKNSIDQQMDAVKSLEQPLDALQHAKVCQDNLTTqndrILELRDIVAKIAADVGLDASALMQGELDALGQR 10530
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL----LLIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10531 LAECKDAITTLANVAETQDKER-KELDKEVTLAKAYFNNVQQDISREAPQNPKESEE---QLAALRAHLQTLARTEEQLR 10606
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEElQALPALEELEEEELEELLAALGLPPDLSPEELLElldRIEELQELLREAEELEEELQ 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10607 QLKERHQNSEVAPSVASSDDDGILEVLALWQKiFQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQhvqsflscaIPEDY 10686
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEE---------LEEEL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10687 SSLREQQQLcaihqnllisqqsvlsetpLESELSEQYKALTNLHNETlsRIMQRNGELERRvsgwnayRQQLAALLDWLR 10766
Cdd:COG4717 435 EELEEELEE-------------------LEEELEELREELAELEAEL--EQLEEDGELAEL-------LQELEELKAELR 486
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 442626147 10767 QREAERNALQL---------RYIHLKRVPHLKHRLDAMIQQLDQGE 10803
Cdd:COG4717 487 ELAEEWAALKLalelleearEEYREERLPPVLERASEYFSRLTDGR 532
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2512-2810 |
5.23e-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: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2512 EQFAEVNNNADRLSAITTSFNDQEQELRRRSKEAGERVSKLREqlikCDDMSGDNNKIMERL-QQCRALRGELDNSGNEI 2590
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD----ASRKIGEIEKEIEQLeQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2591 DNIKQKVDELRNLYPTFSESIIPKELNNVQKRYENVDLYAKKIESSL------LQFLKKFHADKVGMLKRIIA-----TQ 2659
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpeiqaeLSKLEEEVSRIEARLREIEQklnrlTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 2660 REKVAwcQPESSSDKYNLDVKKSSLQEVSKSIDDCKARHAETLKSLEMLKAVESP--QNLAELTSDAELLRKDMQALQDS 2737
Cdd:TIGR02169 827 EKEYL--EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDleSRLGDLKKERDELEAQLRELERK 904
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626147 2738 FDQIKGILDENVDLWSQYEQSNEQISNWLRDVEGRVKAETSSQVNLSEVPQKLQELSILQQDVLAHEPiINNL 2810
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEP-VNML 976
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
10692-10989 |
5.64e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10692 QQQLCAIHQNLLISQQSVLSETPLESELseqykaltnlhnETLSRIMQRNGELErrvsgwnAYRQQLAALLDWLRQREAE 10771
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQTL------------ALLDKIDRQKEETE-------QLKQQLAQAPAKLRQAQAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10772 RNALQLryihlKRVPHLKHRLDAM-IQQL-DQGEQQSKALQEQQQELARHCDDALATAMRME--QASIG---QRISNLRA 10844
Cdd:PRK11281 103 LEALKD-----DNDEETRETLSTLsLRQLeSRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPEraQAALYansQRLQQIRN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10845 ALKTwqgflQRVTQLSESYEQRvNQLQQEfgaaQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALES------ 10918
Cdd:PRK11281 178 LLKG-----GKVGGKALRPSQR-VLLQAE----QALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHqlqllq 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626147 10919 -------LTVTQEELKECISPHDMKTIrQRNWLLwQQHADLDYQLAN-LINSIeERLSLLSNYQIrydRISQWLQRLEQ 10989
Cdd:PRK11281 248 eainskrLTLSEKTVQEAQSQDEAARI-QANPLV-AQELEINLQLSQrLLKAT-EKLNTLTQQNL---RVKNWLDRLTQ 320
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4780-4992 |
5.64e-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: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4780 DHRLFKEAYDDLVSWIGRAREKFPSlkQSSLSDKLAIENAVQATEALLNKQAQGELLVEHLVHTGEvVLASTSAQGQEII 4859
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGE-QLIEEGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 4860 RNDIRALRDSFEGLFREINQQKENLEVTMVQWRAYKEEYErLMEWLQQIDILVKNHklNLCPNLPEKEKQVADMKEVMSR 4939
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEEE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442626147 4940 LEKGKDDIDKFNASAASLLKSH---LDTYVNNQLRHLSSVYQVQVNLAKDVLKKVE 4992
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGhpdADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7319-7538 |
5.70e-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: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7319 LNRSWQDLVRsLEQRRDNLQQLAEHWDgfenslhAWEKALGRLE--DKFRNVDPTVRSRRHLEDTKNAIQELREESNQLK 7396
Cdd:COG4913 237 LERAHEALED-AREQIELLEPIRELAE-------RYAAARERLAelEYLRAALRLWFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7397 sshKEIEALSKSIltflgevhkpsaEAIQAKVDKLVEQQAKL-NDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHE 7475
Cdd:COG4913 309 ---AELERLEARL------------DALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442626147 7476 QL-QSVHVYDEHIAQTEQLLITLNSQVQQAAEEsklLVAQTTAHYQAKQNQlpSDIAQEFTALE 7538
Cdd:COG4913 374 PLpASAEEFAALRAEAAALLEALEEELEALEEA---LAEAEAALRDLRREL--RELEAEIASLE 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
10702-10966 |
5.78e-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: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10702 LLISQQSVLSETPLESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLryih 10781
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10782 lkrvphlkhRLDAMIQQLDQGEQQskaLQEQQQELARHcddaLATAMRMEQASIGQRISNLRAALKtwqgfLQRVTQLSE 10861
Cdd:COG4942 84 ---------ELAELEKEIAELRAE---LEAQKEELAEL----LRALYRLGRQPPLALLLSPEDFLD-----AVRRLQYLK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10862 SYEQRVNQLQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLtvtQEELKEcisphDMKTIRQR 10941
Cdd:COG4942 143 YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEK-----ELAELAAE 214
|
250 260
....*....|....*....|....*
gi 442626147 10942 NWLLWQQHADLDYQLANLINSIEER 10966
Cdd:COG4942 215 LAELQQEAEELEALIARLEAEAAAA 239
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
5088-5870 |
5.80e-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: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5088 RLVKKMSTAKVQLETNLLQwaDYSSSYSQLQQWITDREAklQQACEQKIVKSKRGQpglssgLSERKANLRQTNNIVQDI 5167
Cdd:TIGR00606 195 RQTQGQKVQEHQMELKYLK--QYKEKACEIRDQITSKEA--QLESSREIVKSYENE------LDPLKNRLKEIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5168 VSFEPMIQSVTSKAsvLQQGAPGTEISDK----YENLTKQAKDLYEKQKNTIESY-QSLIDAGNEFATWLRNAKERLSKC 5242
Cdd:TIGR00606 265 MKLDNEIKALKSRK--KQMEKDNSELELKmekvFQGTDEQLNDLYHNHQRTVREKeRELVDCQRELEKLNKERRLLNQEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5243 SE---PTGDKQALAEKTH----------QLKILQGEL------PEGAQKLKNALE---QGEIACRSAEPEDCEIIEQEVA 5300
Cdd:TIGR00606 343 TEllvEQGRLQLQADRHQehirardsliQSLATRLELdgfergPFSERQIKNFHTlviERQEDEAKTAAQLCADLQSKER 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5301 LLQEEFDAYREALNKAKDYLEVGIVKWSDYQDQYTEALEWLSKTEALVQSYNKLQDSLIQKKVVLEQFQGHLQTLFDWQK 5380
Cdd:TIGR00606 423 LKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5381 TLDDLNMKAQVLLETCSDTRISNAIMQLTTKYNALLTLAKEVMRRLEMHYQEHQQHHSLYEECQSWIEKTREKLSECEQI 5460
Cdd:TIGR00606 503 VKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5461 PGTLNEVQIKLNTVKNLRQGFETGQNKLRYLLELKEKVIMNTEQN-----GAAKIQEDTEALKQDFDKLLVDLNDVRQKL 5535
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcGSQDEESDLERLKEEIEKSSKQRAMLAGAT 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5536 ANRLAQLEE--------------IFKLYKILIEWLEDVEPSVKTSDEFLNDLSEKRAALEKFR------------VIQRD 5589
Cdd:TIGR00606 663 AVYSQFITQltdenqsccpvcqrVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRdemlglapgrqsIIDLK 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5590 INGHNDIVEKIN------QRLK---EDNSLDLKDFQPGLTKFDDLQTQVNkIIESLENQVNSHE-KYKQAYNELQDW-LR 5658
Cdd:TIGR00606 743 EKEIPELRNKLQkvnrdiQRLKndiEEQETLLGTIMPEEESAKVCLTDVT-IMERFQMELKDVErKIAQQAAKLQGSdLD 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5659 RTRIEVEQcadchgekdQVESRLNRLGDIQSSSLEGKALLEACEELSQAVIATSGSEGQDNV------------AQEIKH 5726
Cdd:TIGR00606 822 RTVQQVNQ---------EKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLqigtnlqrrqqfEEQLVE 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5727 LTSEWETLQTISRDARSSlescLAAWQTFLQKFnkinlwiETMNKRVTKSQEGENKTPEDLVN--AKKLLEEVLAEKDNV 5804
Cdd:TIGR00606 893 LSTEVQSLIREIKDAKEQ----DSPLETFLEKD-------QQEKEELISSKETSNKKAQDKVNdiKEKVKNIHGYMKDIE 961
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442626147 5805 EDLNDNCEllmeqsactrirDQTIETQANYTKL---LTSAQGLVAKIEKNLSDHTEFLNYKKEMDAWIE 5870
Cdd:TIGR00606 962 NKIQDGKD------------DYLKQKETELNTVnaqLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQ 1018
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
10751-10941 |
6.72e-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: 42.43 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10751 WNAYRQQLAALLDWLRQREAERNALQLRyIHLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDAlATAMRM 10830
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10831 EQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQrVNQLQQEFGAAQKLLdaNSESLPTQPAAIEQLLGSLRAQRVQLG 10910
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAAL--ASEDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190
....*....|....*....|....*....|.
gi 442626147 10911 AQVSALESLTVTQEELKECISPHDMKTIRQR 10941
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEK 187
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
10510-10916 |
6.95e-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: 44.17 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10510 ADVGLDASALMQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDIsreapqnpkESEEQLA 10589
Cdd:COG3096 280 RRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTAL---------RQQEKIE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10590 ALRAHLQTLA-RTEEQLRQLKERHqnsevapsvassdddgilEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEAL-RLW 10667
Cdd:COG3096 351 RYQEDLEELTeRLEEQEEVVEEAA------------------EQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqTRA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10668 RQYLQHVQSflscaipedyssLREQQQLCAI----------HQNLLISQQSVLSETPLESE--LSEQyKALTNLHNETLS 10735
Cdd:COG3096 413 IQYQQAVQA------------LEKARALCGLpdltpenaedYLAAFRAKEQQATEEVLELEqkLSVA-DAARRQFEKAYE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10736 RIMQRNGELERRvSGWNAYRQQLAallDWLRQR-EAER-NALQLRYIHLKRVPHLKHRLDAMIQQLDQGEQQS------- 10806
Cdd:COG3096 480 LVCKIAGEVERS-QAWQTARELLR---RYRSQQaLAQRlQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQldaaeel 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10807 KALQEQQQELARHCDDALATA------MRMEQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKL 10880
Cdd:COG3096 556 EELLAELEAQLEELEEQAAEAveqrseLRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQL 635
|
410 420 430
....*....|....*....|....*....|....*.
gi 442626147 10881 LDANSEslptqpaaIEQLLGSLRAQRVQLGAQVSAL 10916
Cdd:COG3096 636 LERERE--------ATVERDELAARKQALESQIERL 663
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
7731-7944 |
8.37e-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: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7731 GQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEACEEWDQCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQLgfcE 7810
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI---A 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7811 KTLADINVQKTKLRlsiEKLEVHFRNGMGGDPRL---SENVDDLVRVLDGLGELV----------KAKSQSLEQTLAQID 7877
Cdd:COG4942 94 ELRAELEAQKEELA---ELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAparreqaeelRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 7878 VYQQQMQSLRQRIIQEEQQLRLVMAptylphDRERALAE---QQDLITQELDELLQSLSSVEDGIANMNQ 7944
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA------ERQKLLARlekELAELAAELAELQQEAEELEALIARLEA 234
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
10416-10822 |
9.59e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.64 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10416 EQIESAVQEAVVAWNDTSENLQQLRTRYqravelwdKYRNASAAVKNSIDQQMDAVKSLEQPLDALQHAKVCQDNLTTQN 10495
Cdd:PRK10246 443 AQLQVAIQNVTQEQTQRNAALNEMRQRY--------KEKTQQLADVKTICEQEARIKDLEAQRAQLQAGQPCPLCGSTSH 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10496 DRI-----LEL------RDIVAKIAADVGlDASALMQGELDALGQRLAECKDAITTLANVAETQDKERKEL--DKEVTLa 10562
Cdd:PRK10246 515 PAVeayqaLEPgvnqsrLDALEKEVKKLG-EEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVcaSLNITL- 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10563 kayfnNVQQDISrEAPQNPKESEEQL----------AALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGilev 10632
Cdd:PRK10246 593 -----QPQDDIQ-PWLDAQEEHERQLrllsqrhelqGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDE---- 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10633 LALWQKIFQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLC-AIHQNLLISQQSVLS 10711
Cdd:PRK10246 663 EASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQClSLHSQLQTLQQQDVL 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 10712 ETPLESELSEQYK-ALTN-------------LHNETLSRIMQRNGELERRvsgwnayRQQLAALLDWLRQREAERNALQL 10777
Cdd:PRK10246 743 EAQRLQKAQAQFDtALQAsvfddqqaflaalLDEETLTQLEQLKQNLENQ-------RQQAQTLVTQTAQALAQHQQHRP 815
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442626147 10778 RYIHLK-RVPHLKHRLDAMIQQL-----DQGE------------QQSKALQEQQQELARHCDD 10822
Cdd:PRK10246 816 DGLDLTvTVEQIQQELAQLAQQLrenttRQGEirqqlkqdadnrQQQQALMQQIAQATQQVED 878
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5488-6047 |
9.80e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5488 LRYLLELKEKVIMNTEQngaakIQEDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDVEPSVKtsd 5567
Cdd:PRK03918 174 IKRRIERLEKFIKRTEN-----IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEK--- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5568 EFLNDLSEKRAALEKFRVIQRDINGHNDIVEKINQRLKEDNSLD------------LKDFQPGLTKFDDLQTQVNKIIES 5635
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekaeeyiklsefYEEYLDELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5636 LENQVNSHEKYKQAYNELQDWLRRTRIEVEQCADCHGEKDQVESRLNRLGDIqSSSLEGKALLEACEELSQAviatsgSE 5715
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERL-KKRLTGLTPEKLEKELEEL------EK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5716 GQDNVAQEIKHLTSEWETLQTISRDARSSLESCLAAWQ---------TFLQKFNKINLWIETMNKRVTKSQEGENKTpED 5786
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKE-RK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5787 LVNAKKLLEEVLAEKDNVEDLNDNCELLME-QSACTRIRDQTIETQAN-YTKLLTSAQGLVAKIEKNLSDHTEFLNYKKE 5864
Cdd:PRK03918 478 LRKELRELEKVLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKAEeYEKLKEKLIKLKGEIKSLKKELEKLEELKKK 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5865 MDAwIEKAQQVLDDCSTDGDAAIIAQKLDTVNSLASRLPEgqhlLALVQDAYSKASNITPE-----DKQEKLRELMTKVR 5939
Cdd:PRK03918 558 LAE-LEKKLDELEEELAELLKELEELGFESVEELEERLKE----LEPFYNEYLELKDAEKElereeKELKKLEEELDKAF 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442626147 5940 EDWDALGLAVKQKLSDLKQAQNRWNDfaankdklEKWLNETETTLKVAPETKGELSEMKTLLERYKTLSNELKLKGNELE 6019
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYSE--------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
570 580 590
....*....|....*....|....*....|.
gi 442626147 6020 QLQS---EARDLGTEVDAVNRLQSRCDKLKN 6047
Cdd:PRK03918 705 EREKakkELEKLEKALERVEELREKVKKYKA 735
|
|
| |
