|
Name |
Accession |
Description |
Interval |
E-value |
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
627-739 |
2.15e-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: 2.15e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 627 EQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKR 706
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|...
gi 320544542 707 IKLVNINPADLVDGRPPVVLGLIWTIILYFQIE 739
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
774-882 |
3.85e-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: 3.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 774 KWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAK 853
Cdd:cd21243 1 KFKGGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPR 80
|
90 100
....*....|....*....|....*....
gi 320544542 854 LLDAEDVDVPKPDEKSIMTYVAQFLHKYP 882
Cdd:cd21243 81 LLDPEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
627-739 |
2.91e-48 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 170.06 E-value: 2.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 627 EQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKR 706
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|...
gi 320544542 707 IKLVNINPADLVDGRPPVVLGLIWTIILYFQIE 739
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQIE 113
|
|
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
629-737 |
2.33e-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: 156.02 E-value: 2.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 629 ERVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASKRIK 708
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKA--RRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRM--RFHRLQNVQTALDFLKYRKIK 76
|
90 100
....*....|....*....|....*....
gi 320544542 709 LVNINPADLVDGRPPVVLGLIWTIILYFQ 737
Cdd:cd21188 77 LVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
627-739 |
2.76e-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: 2.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 627 EQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGrvLRRPHFLSNANTALQFLASKR 706
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKG--HNVFQCRSNIETALSFLKNKS 78
|
90 100 110
....*....|....*....|....*....|...
gi 320544542 707 IKLVNINPADLVDGRPPVVLGLIWTIILYFQIE 739
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 ... |
619-734 |
1.06e-37 |
|
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: 140.19 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 619 SHIKEKREEQERVQKKTFTNWINSYLlKRVPpLRIDDLINDLRDGTKLIALLEVLSGERLP-VEKGRVlrRPHFLSNANT 697
Cdd:cd21246 4 SRIKALADEREAVQKKTFTKWVNSHL-ARVG-CRINDLYTDLRDGRMLIKLLEVLSGERLPkPTKGKM--RIHCLENVDK 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 320544542 698 ALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTIIL 734
Cdd:cd21246 80 ALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
619-734 |
1.43e-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: 137.04 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 619 SHIKEKREEQERVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLP-VEKGRVlrRPHFLSNANT 697
Cdd:cd21193 4 GRIRALQEERINIQKKTFTKWINSFLEKA--NLEIGDLFTDLSDGKLLLKLLEIISGEKLGkPNRGRL--RVQKIENVNK 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 320544542 698 ALQFLASKrIKLVNINPADLVDGRPPVVLGLIWTIIL 734
Cdd:cd21193 80 ALAFLKTK-VRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
776-882 |
3.54e-36 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 135.24 E-value: 3.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 776 KQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLL 855
Cdd:cd21192 1 QGSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLL 80
|
90 100
....*....|....*....|....*..
gi 320544542 856 DAEDVDVPKPDEKSIMTYVAQFLHKYP 882
Cdd:cd21192 81 EVEDVLVDKPDERSIMTYVSQFLRMFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
631-738 |
4.01e-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: 4.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 631 VQKKTFTNWINSYLLKRVPPLrIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASKRIKLV 710
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKPP-IKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRM--RVHHLNNVNRALQVLEQNNVKLV 78
|
90 100
....*....|....*....|....*...
gi 320544542 711 NINPADLVDGRPPVVLGLIWTIILYFQI 738
Cdd:cd21186 79 NISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
774-878 |
9.15e-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: 9.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 774 KWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAK 853
Cdd:cd21244 1 RWKMSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPR 80
|
90 100
....*....|....*....|....*
gi 320544542 854 LLDAEDVDVPKPDEKSIMTYVAQFL 878
Cdd:cd21244 81 LLEPEDVDVVNPDEKSIMTYVAQFL 105
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
779-882 |
1.21e-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: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 858
Cdd:cd21189 2 AKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDPE 81
|
90 100
....*....|....*....|....
gi 320544542 859 DVDVPKPDEKSIMTYVAQFLHKYP 882
Cdd:cd21189 82 DVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
617-740 |
1.59e-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: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 617 YDSHIKEKREEQERVQKKTFTNWINSYLLKRVPplRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNAN 696
Cdd:cd21236 3 YENVLERYKDERDKVQKKTFTKWINQHLMKVRK--HVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRM--RFHRLQNVQ 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 320544542 697 TALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTIILYFQIEE 740
Cdd:cd21236 79 IALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISD 122
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
779-881 |
2.04e-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: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 858
Cdd:cd21194 3 AKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDAE 82
|
90 100
....*....|....*....|...
gi 320544542 859 DVDVPKPDEKSIMTYVAQFLHKY 881
Cdd:cd21194 83 DVDVARPDEKSIMTYVASYYHYF 105
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
627-905 |
2.81e-32 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 138.15 E-value: 2.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 627 EQERVQKKTFTNWINSYLLKRVPPlRIDDLINDLRDGTKLIALLEVLSGERLpVEKGRVLR-RPHFLSNANTALQFLASK 705
Cdd:COG5069 5 KWQKVQKKTFTKWTNEKLISGGQK-EFGDLDTDLKDGVKLAQLLEALQKDNA-GEYNETPEtRIHVMENVSGRLEFIKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 706 RIKLVNINPADLVDGRPPVVLGLIWTIILYFQIEENSRNLEYLGHgiggsvSSLDSVGNQKHGDLKAEkwkqgarktlln 785
Cdd:COG5069 83 GVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGELTKH------INLLLWCDEDTGGYKPE------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 786 wvtnalpkdsgVEVKDFGASWRDGVAFLALI-----DAIKANLVNLAELKKTSNRQRletAFDVAESKLGIAKLLDAEDV 860
Cdd:COG5069 145 -----------VDTFDFFRSWRDGLAFSALIhdsrpDTLDPNVLDLQKKNKALNNFQ---AFENANKVIGIARLIGVEDI 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 320544542 861 -DVPKPDEKSIMTYVAQFLHKYpepkgasRDQSHVQQEADELRRFL 905
Cdd:COG5069 211 vNVSIPDERSIMTYVSWYIIRF-------GLLEKIDIALHRVYRLL 249
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
629-734 |
3.34e-32 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 124.04 E-value: 3.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 629 ERVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLP-VEKGRVlrRPHFLSNANTALQFLASKRI 707
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKA--GTQIENIEEDFRDGLKLMLLLEVISGERLPkPERGKM--RFHKIANVNKALDFIASKGV 78
|
90 100
....*....|....*....|....*..
gi 320544542 708 KLVNINPADLVDGRPPVVLGLIWTIIL 734
Cdd:cd21214 79 KLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
619-734 |
1.31e-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: 123.60 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 619 SHIKEKREEQERVQKKTFTNWINSYLLKrvPPLRIDDLINDLRDGTKLIALLEVLSGERLPV-EKGRVlrRPHFLSNANT 697
Cdd:cd21318 26 SRIKALADEREAVQKKTFTKWVNSHLAR--VPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRM--RIHSLENVDK 101
|
90 100 110
....*....|....*....|....*....|....*..
gi 320544542 698 ALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTIIL 734
Cdd:cd21318 102 ALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
779-882 |
3.04e-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: 3.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKdSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 858
Cdd:cd21245 4 AIKALLNWVQRRTRK-YGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPE 82
|
90 100
....*....|....*....|....
gi 320544542 859 DVDVPKPDEKSIMTYVAQFLHKYP 882
Cdd:cd21245 83 DVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
626-738 |
3.05e-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: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 626 EEQERVQKKTFTNWINSYLLKrvPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASK 705
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLRHR 76
|
90 100 110
....*....|....*....|....*....|...
gi 320544542 706 RIKLVNINPADLVDGRPPVVLGLIWTIILYFQI 738
Cdd:cd21235 77 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 109
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
627-740 |
3.22e-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: 118.84 E-value: 3.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 627 EQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKR 706
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 320544542 707 IKLVNINPADLVDGRPPVVLGLIWTIILYFQIEE 740
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
619-734 |
6.34e-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: 118.62 E-value: 6.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 619 SHIKEKREEQERVQKKTFTNWINSYLlKRVPpLRIDDLINDLRDGTKLIALLEVLSGERLPV-EKGRVlrRPHFLSNANT 697
Cdd:cd21317 19 SRIKALADEREAVQKKTFTKWVNSHL-ARVT-CRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRM--RIHCLENVDK 94
|
90 100 110
....*....|....*....|....*....|....*..
gi 320544542 698 ALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTIIL 734
Cdd:cd21317 95 ALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
626-740 |
4.99e-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: 4.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 626 EEQERVQKKTFTNWINSYLLKRVPplRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASK 705
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRK--HINDLYEDLRDGHNLISLLEVLSGVKLPREKGRM--RFHRLQNVQIALDFLKQR 76
|
90 100 110
....*....|....*....|....*....|....*
gi 320544542 706 RIKLVNINPADLVDGRPPVVLGLIWTIILYFQIEE 740
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 ... |
779-879 |
1.46e-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: 113.64 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNalpKDSG---VEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLL 855
Cdd:cd21248 3 AKDALLLWCQM---KTAGypnVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLL 79
|
90 100
....*....|....*....|....
gi 320544542 856 DAEDVDVPKPDEKSIMTYVAQFLH 879
Cdd:cd21248 80 DPEDVNVEQPDEKSIITYVVTYYH 103
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
627-739 |
1.80e-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: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 627 EQERVQKKTFTNWINSYLLK-RVPPlrIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASK 705
Cdd:cd21231 2 EREDVQKKTFTKWINAQFAKfGKPP--IEDLFTDLQDGRRLLELLEGLTGQKLVKEKGST--RVHALNNVNKALQVLQKN 77
|
90 100 110
....*....|....*....|....*....|....
gi 320544542 706 RIKLVNINPADLVDGRPPVVLGLIWTIILYFQIE 739
Cdd:cd21231 78 NVDLVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
618-738 |
1.01e-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: 111.77 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 618 DSHIKEKREEQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPV-EKGRVlrRPHFLSNAN 696
Cdd:cd21247 7 KGHIRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKM--RVHFLENNS 84
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 320544542 697 TALQFLASK-RIKLvnINPADLVDGRPPVVLGLIWTIILYFQI 738
Cdd:cd21247 85 KAITFLKTKvPVKL--IGPENIVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
629-736 |
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 320544542 629 ERVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLpvekGRVLRRP----HFLSNANTALQFLAS 704
Cdd:cd21215 2 VDVQKKTFTKWLNTKLSSR--GLSITDLVTDLSDGVRLIQLLEIIGDESL----GRYNKNPkmrvQKLENVNKALEFIKS 75
|
90 100 110
....*....|....*....|....*....|..
gi 320544542 705 KRIKLVNINPADLVDGRPPVVLGLIWTIILYF 736
Cdd:cd21215 76 RGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
776-879 |
2.63e-27 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 110.34 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 776 KQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLL 855
Cdd:cd21249 2 LRSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLL 81
|
90 100
....*....|....*....|....
gi 320544542 856 DAEDVDVPKPDEKSIMTYVAQFLH 879
Cdd:cd21249 82 DPEDVAVPHPDERSIMTYVSLYYH 105
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
781-882 |
3.81e-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: 3.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 781 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDV 860
Cdd:cd21187 3 KTLLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDV 82
|
90 100
....*....|....*....|..
gi 320544542 861 DVPKPDEKSIMTYVAQFLHKYP 882
Cdd:cd21187 83 NVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
779-881 |
5.99e-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: 5.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 858
Cdd:cd21216 11 AKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKMLDAE 90
|
90 100
....*....|....*....|....
gi 320544542 859 D-VDVPKPDEKSIMTYVAQFLHKY 881
Cdd:cd21216 91 DiVNTPRPDERSVMTYVSCYYHAF 114
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
779-881 |
1.42e-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: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 858
Cdd:cd21291 11 AKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGIPQLLDVE 90
|
90 100
....*....|....*....|....
gi 320544542 859 DV-DVPKPDEKSIMTYVAQFLHKY 881
Cdd:cd21291 91 DVcDVAKPDERSIMTYVAYYFHAF 114
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
777-885 |
1.43e-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: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 777 QGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLD 856
Cdd:cd21319 4 RSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLD 83
|
90 100
....*....|....*....|....*....
gi 320544542 857 AEDVDVPKPDEKSIMTYVAQFLHKYPEPK 885
Cdd:cd21319 84 PEDVFTENPDEKSIITYVVAFYHYFSKMK 112
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
631-738 |
1.54e-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: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 631 VQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKRIKLV 710
Cdd:cd21227 4 IQKNTFTNWVNEQL--KPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIKLV 81
|
90 100
....*....|....*....|....*...
gi 320544542 711 NINPADLVDGRPPVVLGLIWTIILYFQI 738
Cdd:cd21227 82 NIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| KASH |
pfam10541 |
Nuclear envelope localization domain; The KASH (for Klarsicht/ANC-1/Syne-1 homology) or KLS ... |
12289-12345 |
2.97e-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: 2.97e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 320544542 12289 FLGRVARASLPIQALMLLLLGVATLVPHG-EDYTCMFSNTFARSLEPMLSYPHGPPPT 12345
Cdd:pfam10541 1 FLGRVLRAALPLQLLLLLLLLLACLLPAGeEDYSCTLANNFARSFHPMLRYVNGPPPT 58
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
596-734 |
7.00e-25 |
|
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: 105.13 E-value: 7.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 596 QEYQEFQSTMASINYARSNSQYD----SHIKEKREEQERVQKKTFTNWINSYLLKrvPPLRIDDLINDLRDGTKLIALLE 671
Cdd:cd21316 14 QQYSDVNNRWDVDEWDNENSSARlferSRIKALADEREAVQKKTFTKWVNSHLAR--VSCRITDLYMDLRDGRMLIKLLE 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320544542 672 VLSGERLPV-EKGRVlrRPHFLSNANTALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTIIL 734
Cdd:cd21316 92 VLSGERLPKpTKGRM--RIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
630-736 |
1.42e-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: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 630 RVQKKTFTNWINSYLLKRvpPLRIDDLINDLRDGTKLIALLEVLSGERLpveKGRVLRRP----HFLSNANTALQFLASK 705
Cdd:cd21183 3 RIQANTFTRWCNEHLKER--GMQIHDLATDFSDGLCLIALLENLSTRPL---KRSYNRRPafqqHYLENVSTALKFIEAD 77
|
90 100 110
....*....|....*....|....*....|.
gi 320544542 706 RIKLVNINPADLVDGRPPVVLGLIWTIILYF 736
Cdd:cd21183 78 HIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
631-739 |
1.60e-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: 102.01 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 631 VQKKTFTNWINSYLLKRVPPlRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVlrRPHFLSNANTALQFLASKRIKLV 710
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKP-PIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGST--RVHALNNVNRVLQVLHQNNVELV 78
|
90 100
....*....|....*....|....*....
gi 320544542 711 NINPADLVDGRPPVVLGLIWTIILYFQIE 739
Cdd:cd21232 79 NIGGTDIVDGNHKLTLGLLWSIILHWQVK 107
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
774-886 |
2.82e-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: 102.06 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 774 KWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAK 853
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100 110
....*....|....*....|....*....|...
gi 320544542 854 LLDAEDVDVPKPDEKSIMTYVAQFLHKYPEPKG 886
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKMKA 113
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
629-738 |
8.04e-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: 8.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 629 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLAS-KRI 707
Cdd:cd21311 13 KRIQQNTFTRWANEHL--KTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEEdEGI 90
|
90 100 110
....*....|....*....|....*....|.
gi 320544542 708 KLVNINPADLVDGRPPVVLGLIWTIILYFQI 738
Cdd:cd21311 91 KIVNIDSSDIVDGKLKLILGLIWTLILHYSI 121
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
779-882 |
2.71e-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: 2.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAEsKLGIAKLLDAE 858
Cdd:cd21239 2 AKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAE-KLGVTRLLDPE 80
|
90 100
....*....|....*....|....
gi 320544542 859 DVDVPKPDEKSIMTYVAQFLHKYP 882
Cdd:cd21239 81 DVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
779-882 |
4.47e-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: 4.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGIAKLLDAE 858
Cdd:cd21240 5 AKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAE 83
|
90 100
....*....|....*....|....
gi 320544542 859 DVDVPKPDEKSIMTYVAQFLHKYP 882
Cdd:cd21240 84 DVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
778-879 |
1.38e-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: 96.54 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 778 GARKTLLNWVTNALPKDSgveVKDFGASWRDGVAFLALIDAIKANL-VNLAELKKTSNRQRLETAFDVAESKLGIAKLLD 856
Cdd:cd21184 1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLiPDNESLDKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|...
gi 320544542 857 AEDVDVPKPDEKSIMTYVAQFLH 879
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSYFRN 100
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
781-881 |
3.14e-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: 95.61 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 781 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDV 860
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 320544542 861 DVPKPDEKSIMTYVAQFLHKY 881
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
779-882 |
7.73e-22 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 94.32 E-value: 7.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 858
Cdd:cd21238 3 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 82
|
90 100
....*....|....*....|....
gi 320544542 859 DVDVPKPDEKSIMTYVAQFLHKYP 882
Cdd:cd21238 83 DVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
629-736 |
6.20e-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: 6.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 629 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVE-KGRVLRRPHFLSNANTALQFLASKRI 707
Cdd:cd21228 2 KKIQQNTFTRWCNEHL--KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKyNKRPTFRQMKLENVSVALEFLERESI 79
|
90 100
....*....|....*....|....*....
gi 320544542 708 KLVNINPADLVDGRPPVVLGLIWTIILYF 736
Cdd:cd21228 80 KLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
779-882 |
6.79e-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: 91.96 E-value: 6.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKD-SGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKT--SNRQRLETAFDVAESKLGIAK-L 854
Cdd:pfam00307 3 LEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVPKvL 82
|
90 100
....*....|....*....|....*...
gi 320544542 855 LDAEDVDvpKPDEKSIMTYVAQFLHKYP 882
Cdd:pfam00307 83 IEPEDLV--EGDNKSVLTYLASLFRRFQ 108
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
631-738 |
8.09e-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: 8.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 631 VQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKgRVLRRPHFLSNANTALQFLASK-RIKL 709
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK-LNKSEFDKLENINLALDVAEKKlGVPK 80
|
90 100
....*....|....*....|....*....
gi 320544542 710 VNINPADLVDGRPPVVLGLIWTIILYFQI 738
Cdd:pfam00307 81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
796-881 |
2.09e-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: 90.48 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 796 GVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAED-VDVPKPDEKSIMTYV 874
Cdd:cd21253 19 DVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVALKVPDKLSILTYV 98
|
....*..
gi 320544542 875 AQFlHKY 881
Cdd:cd21253 99 SQY-YNY 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
777-886 |
3.07e-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: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 777 QGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLD 856
Cdd:cd21322 16 RSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHLGLTKLLD 95
|
90 100 110
....*....|....*....|....*....|
gi 320544542 857 AEDVDVPKPDEKSIMTYVAQFLHKYPEPKG 886
Cdd:cd21322 96 PEDVNMEAPDEKSIITYVVSFYHYFSKMKA 125
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
777-881 |
1.04e-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: 88.62 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 777 QGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLD 856
Cdd:cd21320 1 KSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD 80
|
90 100
....*....|....*....|....*
gi 320544542 857 AEDVDVPKPDEKSIMTYVAQFLHKY 881
Cdd:cd21320 81 PEDISVDHPDEKSIITYVVTYYHYF 105
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
779-881 |
8.46e-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: 8.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 858
Cdd:cd21289 11 AKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAE 90
|
90 100
....*....|....*....|....
gi 320544542 859 D-VDVPKPDEKSIMTYVAQFLHKY 881
Cdd:cd21289 91 DiVNTPKPDEKAIMTYVSCFYHAF 114
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
779-881 |
1.01e-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: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 858
Cdd:cd21287 11 AKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDAE 90
|
90 100
....*....|....*....|....
gi 320544542 859 D-VDVPKPDEKSIMTYVAQFLHKY 881
Cdd:cd21287 91 DiVGTARPDEKAIMTYVSSFYHAF 114
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
779-881 |
1.52e-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: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 858
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAE 80
|
90 100
....*....|....*....|....
gi 320544542 859 D-VDVPKPDEKSIMTYVAQFLHKY 881
Cdd:cd21197 81 DmVTMHVPDRLSIITYVSQYYNHF 104
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
779-882 |
1.54e-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: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 858
Cdd:cd21234 1 SEKILLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPE 80
|
90 100
....*....|....*....|....
gi 320544542 859 DVDVPKPDEKSIMTYVAQFLHKYP 882
Cdd:cd21234 81 DVAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
629-738 |
1.91e-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: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 629 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLpveKGRVLRRPHF----LSNANTALQFLAS 704
Cdd:cd21310 14 KKIQQNTFTRWCNEHL--KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKM---YRKYHPRPNFrqmkLENVSVALEFLDR 88
|
90 100 110
....*....|....*....|....*....|....
gi 320544542 705 KRIKLVNINPADLVDGRPPVVLGLIWTIILYFQI 738
Cdd:cd21310 89 EHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 122
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
632-736 |
2.48e-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: 84.56 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 632 QKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPvekgRVLRRP----HFLSNANTALQFLASKRI 707
Cdd:cd21212 1 EIEIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVP----GIHSRPktraQKLENIQACLQFLAALGV 76
|
90 100
....*....|....*....|....*....
gi 320544542 708 KLVNINPADLVDGRPPVVLGLIWTIILYF 736
Cdd:cd21212 77 DVQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
779-883 |
1.78e-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: 82.28 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNL-AELKKTSNRQRLETAFDVAESKLGIAKLLDA 857
Cdd:cd21233 1 SEKILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWnSVVSQQSATERLDHAFNIARQHLGIEKLLDP 80
|
90 100
....*....|....*....|....*.
gi 320544542 858 EDVDVPKPDEKSIMTYVAQFLHKYPE 883
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 ... |
781-877 |
5.83e-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: 5.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 781 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTS---NRQRletAFDVAESKLGIAKLLDA 857
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENiaeNNQL---AFDVAEQELGIPPVMTG 79
|
90 100
....*....|....*....|.
gi 320544542 858 ED-VDVPKPDEKSIMTYVAQF 877
Cdd:cd22198 80 QEmASLAVPDKLSMVSYLSQF 100
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
779-884 |
1.08e-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: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 858
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|....*..
gi 320544542 859 D-VDVPKPDEKSIMTYVAQFLHKYPEP 884
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYYNHFSNP 107
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
779-881 |
1.34e-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: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 858
Cdd:cd21290 14 AKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAE 93
|
90 100
....*....|....*....|....
gi 320544542 859 D-VDVPKPDEKSIMTYVAQFLHKY 881
Cdd:cd21290 94 DiVNTARPDEKAIMTYVSSFYHAF 117
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
783-877 |
2.08e-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: 78.96 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 783 LLNWVTNALPKDSgveVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQR-LETAFDVAESKLGIAKLLDAEDVD 861
Cdd:cd21230 6 LLGWIQNKIPQLP---ITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDALEnATEAMQLAEDWLGVPQLITPEEII 82
|
90
....*....|....*.
gi 320544542 862 VPKPDEKSIMTYVAQF 877
Cdd:cd21230 83 NPNVDEMSVMTYLSQF 98
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
779-881 |
4.49e-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: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAE 858
Cdd:cd21288 11 AKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAE 90
|
90 100
....*....|....*....|....
gi 320544542 859 D-VDVPKPDEKSIMTYVAQFLHKY 881
Cdd:cd21288 91 DiVNTPKPDERAIMTYVSCFYHAF 114
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
781-877 |
8.95e-16 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 76.97 E-value: 8.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 781 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNR----QRLETAFDVAESKLGIAKLLD 856
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 320544542 857 AEDVDVPKPDEKSIMTYVAQF 877
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 ... |
629-738 |
1.17e-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: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 629 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLpveKGRVLRRPHF----LSNANTALQFLAS 704
Cdd:cd21309 15 KKIQQNTFTRWCNEHL--KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRM---YRKYHQRPTFrqmqLENVSVALEFLDR 89
|
90 100 110
....*....|....*....|....*....|....
gi 320544542 705 KRIKLVNINPADLVDGRPPVVLGLIWTIILYFQI 738
Cdd:cd21309 90 ESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSI 123
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
633-734 |
2.64e-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: 75.84 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 633 KKTFTNWINSyLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLAS-KRIKLVN 711
Cdd:cd00014 1 EEELLKWINE-VLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKlGLPELDL 79
|
90 100
....*....|....*....|....
gi 320544542 712 INPADLV-DGRPPVVLGLIWTIIL 734
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 ... |
629-738 |
4.58e-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: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 629 ERVQKKTFTNWINSYLlkRVPPLRIDDLINDLRDGTKLIALLEVLSGERLpveKGRVLRRPHF----LSNANTALQFLAS 704
Cdd:cd21308 18 KKIQQNTFTRWCNEHL--KCVSKRIANLQTDLSDGLRLIALLEVLSQKKM---HRKHNQRPTFrqmqLENVSVALEFLDR 92
|
90 100 110
....*....|....*....|....*....|....
gi 320544542 705 KRIKLVNINPADLVDGRPPVVLGLIWTIILYFQI 738
Cdd:cd21308 93 ESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 126
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
629-732 |
4.74e-15 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 75.26 E-value: 4.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 629 ERVQKKTFTNWINSYLLKRVPPlRIDDLINDLRDGTKLIALLEVLSGERLPVE-----KGRVLRrphfLSNANTALQFLA 703
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGIP-KISDLATDLSDGVRLIFFLELVSGKKFPKKfdlepKNRIQM----IQNLHLAMLFIE 76
|
90 100 110
....*....|....*....|....*....|
gi 320544542 704 SK-RIKLVNINPADLVDGRPPVVLGLIWTI 732
Cdd:cd21225 77 EDlKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
778-880 |
6.31e-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: 6.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 778 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDA 857
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|....*
gi 320544542 858 EDVDV--PKPDEKSIMTYVAQFLHK 880
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLYRH 105
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
634-735 |
1.40e-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: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 634 KTFTNWINSYLLKRVPPlRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRP-HFLSNANTALQFLASKRIKLVNI 712
Cdd:smart00033 1 KTLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfKKIENINLALSFAEKLGGKVVLF 79
|
90 100
....*....|....*....|...
gi 320544542 713 NPADLVDGrPPVVLGLIWTIILY 735
Cdd:smart00033 80 EPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
632-736 |
1.79e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 73.49 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 632 QKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLP----VEKGRVLRRphflSNANTALQFLASKRI 707
Cdd:cd21213 1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPgidwNPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 320544542 708 KLVNINPADLVDGRPPVVLGLIWTIILYF 736
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
781-876 |
1.80e-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: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 781 KTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAEsKLGIAKLLDAED- 859
Cdd:cd21198 4 QDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAA-KLGIPRLLDPADm 82
|
90
....*....|....*..
gi 320544542 860 VDVPKPDEKSIMTYVAQ 876
Cdd:cd21198 83 VLLSVPDKLSVMTYLHQ 99
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
778-876 |
3.91e-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: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 778 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGIAKLLDA 857
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|
gi 320544542 858 ED-VDVPKPDEKSIMTYVAQ 876
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQ 99
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
780-883 |
8.92e-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: 8.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 780 RKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGIAKLLDAED 859
Cdd:cd21199 10 RNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAES-VGIPTTLTIDE 88
|
90 100
....*....|....*....|....*
gi 320544542 860 -VDVPKPDEKSIMTYVAQfLHKYPE 883
Cdd:cd21199 89 mVSMERPDWQSVMSYVTA-IYKHFE 112
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
780-880 |
9.64e-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: 9.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 780 RKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLvnLAELKKTSNRQRLET---AFDVAESKLGIAKLLD 856
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGL--CPNWRKLDPSNSLENcrrAMDLAKREFNIPMVLS 79
|
90 100
....*....|....*....|....
gi 320544542 857 AEDVDVPKPDEKSIMTYVAQFLHK 880
Cdd:cd21229 80 PEDLSSPHLDELSGMTYLSYFMKE 103
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
778-877 |
9.74e-13 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 68.86 E-value: 9.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 778 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDA 857
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80
|
90 100
....*....|....*....|.
gi 320544542 858 ED-VDVPKPDEKSIMTYVAQF 877
Cdd:cd21259 81 EDmVRMREPDWKCVYTYIQEF 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6321-6532 |
4.19e-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: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6321 RWNDFAANKDKLEKWLNETETTLKvAPETKGELSEMKTLLERYKTLSNELKLKGNELEQLQSEARDLGTE--------VD 6392
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEghpdaeeiQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6393 AVNRLQSRCDKLKNDCSAHITALEQEMfDYNAYHQSLQDVEKWLLQISFQLMAHNslFISNREQTQEQIKQHEALLVEIQ 6472
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6473 KYQTNLDDLNAKGQAQIkryESSTPAIRPTVESQLKNIQDSYNSLLQTSVQIKNRLLESL 6532
Cdd:cd00176 157 AHEPRLKSLNELAEELL---EEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
780-879 |
1.49e-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: 65.05 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 780 RKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSN---RQRLETAFDVAES-KLGIAKLL 855
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 320544542 856 DAEDVdVPKPDEKSIMTYVAQFLH 879
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
779-876 |
1.81e-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: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 779 ARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAeSKLGIAKLLDAE 858
Cdd:cd21254 2 ASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGF-ASLGISRLLEPS 80
|
90
....*....|....*....
gi 320544542 859 D-VDVPKPDEKSIMTYVAQ 876
Cdd:cd21254 81 DmVLLAVPDKLTVMTYLYQ 99
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5685-5898 |
5.93e-11 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 66.70 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5685 KWSDYQDQYTEALEWLSKTEALVQSYNKLQDsLIQKKVVLEQFQGHLQTLFDWQKTLDDLNMKAQVLLETCSD--TRISN 5762
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPdaEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5763 AIMQLTTKYNALLTLAKEVMRRLEMHYQEHQQHHSLYEECQsWIEKTREKLSEcEQIPGTLNEVQIKLNTVKNLRQGFET 5842
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQ-WLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 320544542 5843 GQNKLRYLLELKEKVIMNTEQNGAAKIQEDTEALKQDFDKLLVDLNDVRQKLANRL 5898
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
778-886 |
7.82e-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: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 778 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDA 857
Cdd:cd21260 1 GVKNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEV 80
|
90 100 110
....*....|....*....|....*....|
gi 320544542 858 ED-VDVPKPDEKSIMTYVaQFLHKYPEPKG 886
Cdd:cd21260 81 EDmVRMSVPDSKCVYTYI-QELYRSLVQKG 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7643-8356 |
1.11e-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: 70.09 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7643 QTKLTNTLANAKTQQSELEKE--AERWREYQQSIDRVKATIERT-KFVDEPVQNLAGLHFNIQKLSHAIGNVQSQNSDLT 7719
Cdd:TIGR02168 208 QAEKAERYKELKAELRELELAllVLRLEELREELEELQEELKEAeEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7720 LVNQQAQSLI-------RQADARNRQLiEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDK 7792
Cdd:TIGR02168 288 KELYALANEIsrleqqkQILRERLANL-ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7793 FRNvdptvrSRRHLEDTKNAIQELREESNQLKsshKEIEALSKSIltflgEVHKPSAEAIQAKVDKLVEQQAKLNDTLrd 7872
Cdd:TIGR02168 367 LEE------LESRLEELEEQLETLRSKVAQLE---LQIASLNNEI-----ERLEARLERLEDRRERLQQEIEELLKKL-- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7873 KEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVhvyDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAHYQ---- 7948
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEEL---REELEEAEQALDAAERELAQLQARLDSLERLQENLEGfseg 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7949 -----AKQNQLPSDIAQ-----EF-----TALEL-LAERVQ-VTMETKEkdfkraktvrtEYVDGVD-----EVQRWLLQ 8006
Cdd:TIGR02168 508 vkallKNQSGLSGILGVlseliSVdegyeAAIEAaLGGRLQaVVVENLN-----------AAKKAIAflkqnELGRVTFL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8007 AEVQVQERSLTPTQMKEL------------------------------------LQRINHEITAIYERFTLVKTNGQLI- 8049
Cdd:TIGR02168 577 PLDSIKGTEIQGNDREILkniegflgvakdlvkfdpklrkalsyllggvlvvddLDNALELAKKLRPGYRIVTLDGDLVr 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8050 ----------------------IENCRnsEEKTLVQTTIDQLAASLAQVRGWLDEKKQAVGDSLDAWTRFmnlyQIVMSW 8107
Cdd:TIGR02168 657 pggvitggsaktnssilerrreIEELE--EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL----SRQISA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8108 ASEKRNFIDQTIELRTLPEARNKLndyvTSVKSIKPIVKHLSEMDKELEHIGQV-TTVGDLKDKLQEAEDAKISVEAVLL 8186
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSK----ELTELEAEIEELEERLEEAEEELAEAeAEIEELEAQIEQLKEELKALREALD 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8187 ERNSLLQEACEEWDQCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQLGFCEKTLADINVQKTKLRLSIEKLEVHFRNGM 8266
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8267 GGDPRLSENVDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRL-------VMAPTYLPHDRE 8339
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeysltleEAEALENKIEDD 966
|
810
....*....|....*...
gi 320544542 8340 RALAEQQ-DLITQELDEL 8356
Cdd:TIGR02168 967 EEEARRRlKRLENKIKEL 984
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
783-877 |
1.17e-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: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 783 LLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDV-D 861
Cdd:cd21195 9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEMaS 88
|
90
....*....|....*.
gi 320544542 862 VPKPDEKSIMTYVAQF 877
Cdd:cd21195 89 AQEPDKLSMVMYLSKF 104
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
784-879 |
1.30e-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: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 784 LNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGIAKLLDAEDVDVP 863
Cdd:cd21185 7 LRWVRQLLPD---VDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADP 82
|
90
....*....|....*.
gi 320544542 864 KPDEKSIMTYVAQFLH 879
Cdd:cd21185 83 EVEHLGIMAYAAQLQK 98
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
772-883 |
1.75e-10 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 62.35 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 772 AEKWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGI 851
Cdd:cd21257 2 AREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VGI 80
|
90 100 110
....*....|....*....|....*....|...
gi 320544542 852 AKLLDAED-VDVPKPDEKSIMTYVAQfLHKYPE 883
Cdd:cd21257 81 KPSLELSEmMYTDRPDWQSVMQYVAQ-IYKYFE 112
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
12001-12179 |
1.97e-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: 65.16 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 12001 WQQIDNDLWRLEQWLQfaESTQKAQSA-PPSNIELLEDVTQDHREFLLDLESHKSIISSLNVVGDHLAThtLDTEKARQL 12079
Cdd:cd00176 2 LQQFLRDADELEAWLS--EKEELLSSTdYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 12080 RSRLEADNERWNNVCINATKWQGLLQTALMGNSEFHQTIgELVEWLQRTEQNIKASEPVDLTEErsvLETKFKKFKDLRA 12159
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLES---VEELLKKHKELEE 153
|
170 180
....*....|....*....|
gi 320544542 12160 ELERCEPRVVSLQDAADQLL 12179
Cdd:cd00176 154 ELEAHEPRLKSLNELAEELL 173
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2947-4106 |
1.99e-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: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2947 NEIDNI--KQKVDELRNLYPTFSESIIPKELNNVQKRYENVDLYAKKIESSLLQFLKKFHADKVGMLKRIIATQREKvaw 3024
Cdd:TIGR01612 687 NAIDNTedKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILEDFKNK--- 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3025 cQPESSSD-----KYN--LDVKKSSLQEVSK------SIDDCKARHAET--LKSLEMLKAVESPQN-LAELTSDAELLRK 3088
Cdd:TIGR01612 764 -EKELSNKindyaKEKdeLNKYKSKISEIKNhyndqiNIDNIKDEDAKQnyDKSKEYIKTISIKEDeIFKIINEMKFMKD 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3089 DMQALQDSFDQIKGILDENVDlwSQYEQSNEQISnwlrdvegRVKAETSSQvnlsevpqklqELSILQQDVLAHEPIINN 3168
Cdd:TIGR01612 843 DFLNKVDKFINFENNCKEKID--SEHEQFAELTN--------KIKAEISDD-----------KLNDYEKKFNDSKSLINE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3169 LEQTsqqlIEKNPearigQFVTHL--VQRYQAVSKALTSYIDKIRGAQ-------------LSNAN-FAKAAKD-FNEWF 3231
Cdd:TIGR01612 902 INKS----IEEEY-----QNINTLkkVDEYIKICENTKESIEKFHNKQnilkeilnknidtIKESNlIEKSYKDkFDNTL 972
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3232 GDAKIEFQELARMGSPGSSSATAQQLqtvknyIKTFDNgqILLNNAVDIGEALYpvvspdnreriradlrqmrEKFDYLR 3311
Cdd:TIGR01612 973 IDKINELDKAFKDASLNDYEAKNNEL------IKYFND--LKANLGKNKENMLY-------------------HQFDEKE 1025
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3312 DEANAFMQQVEGVLIQKTSIEES-YTQVSHYLNESKAKVPTTDELYPTLATKKAALQnyKTQLQEItlhKNALKqlHDKA 3390
Cdd:TIGR01612 1026 KATNDIEQKIEDANKNIPNIEIAiHTSIYNIIDEIEKEIGKNIELLNKEILEEAEIN--ITNFNEI---KEKLK--HYNF 1098
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3391 VTLCDDESERKTDESiqeyntlsKKISDRITTVGNHVVKH-EAYDQVLEKAQDWLNTIKSEAIDI--LNETTFEKEGAEE 3467
Cdd:TIGR01612 1099 DDFGKEENIKYADEI--------NKIKDDIKNLDQKIDHHiKALEEIKKKSENYIDEIKAQINDLedVADKAISNDDPEE 1170
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3468 KLLVVENLLQHKPEGDSIFDTCHKLL---------ETVLTQTH-------PSGHPALLKGFEEPKQSWEDFMTLCQDSLV 3531
Cdd:TIGR01612 1171 IEKKIENIVTKIDKKKNIYDEIKKLLneiaeiekdKTSLEEVKginlsygKNLGKLFLEKIDEEKKKSEHMIKAMEAYIE 1250
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3532 KLKQLCSKWDEFDTIIEELDNWMKNVEA------------VVKNQNLKSTAEAKNAHLKQLQDISkdierRGAAINELMD 3599
Cdd:TIGR01612 1251 DLDEIKEKSPEIENEMGIEMDIKAEMETfnishdddkdhhIISKKHDENISDIREKSLKIIEDFS-----EESDINDIKK 1325
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3600 --QGREIEGE---TDLNLKLSRLNTRYQTLKnlcKESIAKYVNYVKDhesFDKDFDSFKQNLQSSVDELAKTNEIVGDQS 3674
Cdd:TIGR01612 1326 elQKNLLDAQkhnSDINLYLNEIANIYNILK---LNKIKKIIDEVKE---YTKEIEENNKNIKDELDKSEKLIKKIKDDI 1399
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3675 VLQDQQNKLREMSDKRILDstlfeGLIDRGEKLYGHTSPEGREIirqqlralrtlwDNYtddLNSATQKIDQCLLQFNEF 3754
Cdd:TIGR01612 1400 NLEECKSKIESTLDDKDID-----ECIKKIKELKNHILSEESNI------------DTY---FKNADENNENVLLLFKNI 1459
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3755 SIAQDQLTKWLK-------------------DVDKAMQSHTEPKttlQEKRAQLQNHKLLHQEITTHNVLVDNVCDKA-Q 3814
Cdd:TIGR01612 1460 EMADNKSQHILKikkdnatndhdfninelkeHIDKSKGCKDEAD---KNAKAIEKNKELFEQYKKDVTELLNKYSALAiK 1536
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3815 ILVDQIKDNSlNVYLTSIKQLFQSIV-------QKSDEILH---NLDDCVQKHNELNNALSSAKTWISNEKAKLL----- 3879
Cdd:TIGR01612 1537 NKFAKTKKDS-EIIIKEIKDAHKKFIleaekseQKIKEIKKekfRIEDDAAKNDKSNKAAIDIQLSLENFENKFLkisdi 1615
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3880 --ECDDAYGEKADIKRKIETLG------QLAQNKPQAMKIISDIRDLFEKVKATTSEKGN-EVLDKEIEELETTMKSHFD 3950
Cdd:TIGR01612 1616 kkKINDCLKETESIEKKISSFSidsqdtELKENGDNLNSLQEFLESLKDQKKNIEDKKKElDELDSEIEKIEIDVDQHKK 1695
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3951 DIE-GIEGKQKDV-LAQWDKFEKALEELTKWCRSAEAVFREQQLQSTlhEKVEQLEKYKIQRELILQKEKEIdafgdaaH 4028
Cdd:TIGR01612 1696 NYEiGIIEKIKEIaIANKEEIESIKELIEPTIENLISSFNTNDLEGI--DPNEKLEEYNTEIGDIYEEFIEL-------Y 1766
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4029 ALLNNCgadrLKTLT-----------TQITNRYQLLQVLskEVVNRWSNLVDDhqfyqDKYNEVDLWLQPIESQMAKVLL 4097
Cdd:TIGR01612 1767 NIIAGC----LETVSkepitydeiknTRINAQNEFLKII--EIEKKSKSYLDD-----IEAKEFDRIINHFKKKLDHVND 1835
|
....*....
gi 320544542 4098 DEPTQSSNI 4106
Cdd:TIGR01612 1836 KFTKEYSKI 1844
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
783-877 |
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 320544542 783 LLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDV-D 861
Cdd:cd21251 10 LLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPIMTGKEMaS 89
|
90
....*....|....*.
gi 320544542 862 VPKPDEKSIMTYVAQF 877
Cdd:cd21251 90 VGEPDKLSMVMYLTQF 105
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
780-874 |
2.50e-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: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 780 RKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAED 859
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90
....*....|....*..
gi 320544542 860 VDV--PKPDEKSIMTYV 874
Cdd:cd21258 83 MMImgKKPDSKCVFTYV 99
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
6855-7456 |
2.58e-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: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6855 AINEIKNEYELQGHPKIQELKGKAAQVAEV-ISNLDgqQVEEQMKSLDrrFADLGKR---------------IDRKSQLL 6918
Cdd:TIGR01612 1052 SIYNIIDEIEKEIGKNIELLNKEILEEAEInITNFN--EIKEKLKHYN--FDDFGKEenikyadeinkikddIKNLDQKI 1127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6919 DVTNKGVEGAKGEIDQLQNWVKQQIEELQAPKPLGYTPKDAEARQQKIKSLMKDAEAKQSLADVLEKrvanMQQELEPVE 6998
Cdd:TIGR01612 1128 DHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKK----LLNEIAEIE 1203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6999 YSQ--LESaLRNLN-TENRNLSGVLKAELDRALEAS----KARKSLENDLDKarqwLKTKISEVRKLPVYHPLTSAEIEK 7071
Cdd:TIGR01612 1204 KDKtsLEE-VKGINlSYGKNLGKLFLEKIDEEKKKSehmiKAMEAYIEDLDE----IKEKSPEIENEMGIEMDIKAEMET 1278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7072 KIQENRKYDD--DAKQFNDSVLTDVQRQAANIMKD-----------------CDDADK--AALQQILDEIAADYQTLKDE 7130
Cdd:TIGR01612 1279 FNISHDDDKDhhIISKKHDENISDIREKSLKIIEDfseesdindikkelqknLLDAQKhnSDINLYLNEIANIYNILKLN 1358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7131 SSKrgKSLDDLLQGRKAFEDSMKNMGDWLNEMETATEGELRTTSLPVLEEQLahykKLLSDAENKGGLINDVSEQGKSIL 7210
Cdd:TIGR01612 1359 KIK--KIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKI----ESTLDDKDIDECIKKIKELKNHIL 1432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7211 PTLSNADKLKLNDDIKN--------------------MKDRYGRIKNTIDDRVNALGDHIKKYKDAKSRlaecsqflGNI 7270
Cdd:TIGR01612 1433 SEESNIDTYFKNADENNenvlllfkniemadnksqhiLKIKKDNATNDHDFNINELKEHIDKSKGCKDE--------ADK 1504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7271 QQKLRELNRPIGSRI-EDVQDLLGAYEGI-LKELKDSKSKMGDMQMDDLPELQSILaqqddmikLIEDQLAHLRQLLLLR 7348
Cdd:TIGR01612 1505 NAKAIEKNKELFEQYkKDVTELLNKYSALaIKNKFAKTKKDSEIIIKEIKDAHKKF--------ILEAEKSEQKIKEIKK 1576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7349 EQFIalINEIIAFIMKYTDVIIDIENSPDSLEDKINKYDDVIVKIQEC-------EGVLASANDKGQKIASEGNAADKNS 7421
Cdd:TIGR01612 1577 EKFR--IEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDClketesiEKKISSFSIDSQDTELKENGDNLNS 1654
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 320544542 7422 ITEQLQSLKNQLQNLRKA------VESQRQKHQLQLESHKK 7456
Cdd:TIGR01612 1655 LQEFLESLKDQKKNIEDKkkeldeLDSEIEKIEIDVDQHKK 1695
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7721-8521 |
3.37e-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: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7721 VNQQAQSLIRQADARNR------QLIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFR 7794
Cdd:TIGR02168 198 LERQLKSLERQAEKAERykelkaELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7795 NVDPTVRSRRH-LEDTKNAI----QELREESNQLKSSHKEIEALSKSILTF----------LGEVHKPSAEaIQAKVDKL 7859
Cdd:TIGR02168 278 ELEEEIEELQKeLYALANEIsrleQQKQILRERLANLERQLEELEAQLEELeskldelaeeLAELEEKLEE-LKEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7860 VEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSvhvYDEHIAQTEQllitlnSQVQQAAEESKLL 7939
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER---LEARLERLED------RRERLQQEIEELL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7940 VAQTTAHYQAKQNQLPSDIAQEFTALELLaERVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPT 8019
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEEL-ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8020 QMKELLQRiNHEITAIYERFtlvktnGQLIieNCRNSEEKTLVQTtidqLAASLAQVrgwLDEKKQAVGD--SLDAWTRF 8097
Cdd:TIGR02168 507 GVKALLKN-QSGLSGILGVL------SELI--SVDEGYEAAIEAA----LGGRLQAV---VVENLNAAKKaiAFLKQNEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8098 MNLYQIVMSWASEKRNFIDQTIELRTLPEARNKLNDYVTSVKSIKPIVKHLS-------------EMDKELEHIGQ-VTT 8163
Cdd:TIGR02168 571 GRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLggvlvvddldnalELAKKLRPGYRiVTL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8164 VGDL--KDKLQEAEDAKisVEAVLLERNSLLQEACEEWDQCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQLGFCEKTL 8241
Cdd:TIGR02168 651 DGDLvrPGGVITGGSAK--TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8242 ADINVQKTKLRLSIEKLEVHFRNGMGGDPRLSENVDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQE 8321
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8322 EQQLRLVMAPTYLPHDRERALAEQQDLITQELDELLQSLSSVEDGIANMNQSSLDgmlhglklIQSNLEVHERDAIELKN 8401
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE--------LEELIEELESELEALLN 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8402 QAKKLPTDPATERL--------LNDTVDRIDLLLRRTQQGITMIANAMHGQKKRQQEIDEYQQHLLELEQWIIEVSAELA 8473
Cdd:TIGR02168 881 ERASLEEALALLRSeleelseeLRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE 960
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320544542 8474 SFEPTSDSSTDEQV--LKSQVER-------SQQLLRTLKDRQQSM----EDLVEQTRQLQS 8521
Cdd:TIGR02168 961 NKIEDDEEEARRRLkrLENKIKElgpvnlaAIEEYEELKERYDFLtaqkEDLTEAKETLEE 1021
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
652-733 |
4.51e-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: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 652 RIDDLINDLRDGTKLIALLEVLSGERLPVEKGRV--LRRPHFLSNANTALQFLASK----RIKLVNINPADLVDGRPPVV 725
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaISRLQKLHNVEVALKALKEAgvlrGGDGGGITAKDIVDGHREKT 104
|
....*...
gi 320544542 726 LGLIWTII 733
Cdd:cd21223 105 LALLWRII 112
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
11146-11346 |
5.37e-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: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11146 ELSEQYKALTNLHN---------ETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERnalqlryihlkrvphL 11216
Cdd:COG4913 229 ALVEHFDDLERAHEaledareqiELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL---------------L 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11217 KHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALAtamRMEQASiGQRISNLRAALKTWQGFLQRVTQLSESYEQRVN 11296
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEA---QIRGNG-GDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 320544542 11297 QL-------QQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALES 11346
Cdd:COG4913 370 ALglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
768-877 |
5.90e-10 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 60.95 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 768 GDLKAEKWKQGARKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLV-NLAELKKTSNRQRLETAFDVAE 846
Cdd:cd21315 6 DDGPDDGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAE 82
|
90 100 110
....*....|....*....|....*....|.
gi 320544542 847 SKLGIAKLLDAEDVDVPKPDEKSIMTYVAQF 877
Cdd:cd21315 83 DWLDVPQLIKPEEMVNPKVDELSMMTYLSQF 113
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
633-733 |
6.53e-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: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 633 KKTFTNWINSYL-----LKRVPPLRI--DDLINDLRDGTKLIALLEVLSGERLPVekgRVLRRPHFLS------NANTAL 699
Cdd:cd21217 3 KEAFVEHINSLLaddpdLKHLLPIDPdgDDLFEALRDGVLLCKLINKIVPGTIDE---RKLNKKKPKNifeateNLNLAL 79
|
90 100 110
....*....|....*....|....*....|....
gi 320544542 700 QFLASKRIKLVNINPADLVDGRPPVVLGLIWTII 733
Cdd:cd21217 80 NAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
11013-11759 |
1.03e-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: 66.62 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11013 EEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSseal 11092
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER---- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11093 rlwRQYLQHVQSFLSCAIPEDYSSLREQQQLCAihqnllisqqsvlsetplesELSEQYKALTNLHNETLSRIMQRNGEL 11172
Cdd:TIGR02168 311 ---LANLERQLEELEAQLEELESKLDELAEELA--------------------ELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11173 ERRVSGWNAYRQQL----AALLDWLRQREAERNALQLRYIHLKRVPHLKHRLDAMIQQLDQG--EQQSKALQEQQQELAR 11246
Cdd:TIGR02168 368 EELESRLEELEEQLetlrSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKleEAELKELQAELEELEE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11247 HCDDALATAMRMEQA--SIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKLLDAN----------SE 11314
Cdd:TIGR02168 448 ELEELQEELERLEEAleELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQsglsgilgvlSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11315 SLPTQP---AAIEQLLGSlRAQRV---QLGAQVSALESLT------VTQEELKecISPHDMKTIRQRNWLLWQQ------ 11376
Cdd:TIGR02168 528 LISVDEgyeAAIEAALGG-RLQAVvveNLNAAKKAIAFLKqnelgrVTFLPLD--SIKGTEIQGNDREILKNIEgflgva 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11377 ----------HADLDYQLANLI--NSIEERLSLLSNYQIRY-------DRIS-----------QWLQRLEQRVEKDADVT 11426
Cdd:TIGR02168 605 kdlvkfdpklRKALSYLLGGVLvvDDLDNALELAKKLRPGYrivtldgDLVRpggvitggsakTNSSILERRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11427 AMTNPEQAAKQLEQQVN---SELQLRDKEREWLLSTSRELLTLYSEPEVR-SQVQQQSDSLIDRWQRLKYLAKQKATKIG 11502
Cdd:TIGR02168 685 KIEELEEKIAELEKALAelrKELEELEEELEQLRKELEELSRQISALRKDlARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11503 ELKMTLLRLEERIALIRAWLFEVESQLDkplNFESYTPNVIEAKLKEHEQIQRsiehHSSNVGEVLNLVEMLLNDADSWR 11582
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIE---QLKEELKALREALDELRAELTL----LNEEAANLRERLESLERRIAATE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11583 TQvntsglaasAQNLEQRWKNVCSQSAERKARILTIWNLLQQLIKLTAEHKNWLGKQESQI--AGFERDQKSHSKHKLEE 11660
Cdd:TIGR02168 838 RR---------LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALalLRSELEELSEELRELES 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11661 RQMELRAKLEELESQ--SVNLR------QLEQIYAKLAMSAGVEPENIQKLTLPTKVMVSMWR----QLTPRCHAL---- 11724
Cdd:TIGR02168 909 KRSELRRELEELREKlaQLELRleglevRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARrrlkRLENKIKELgpvn 988
|
810 820 830
....*....|....*....|....*....|....*...
gi 320544542 11725 LDAID--KDAKLMREFNNAQLE-ATNSLNAIQKALEQL 11759
Cdd:TIGR02168 989 LAAIEeyEELKERYDFLTAQKEdLTEAKETLEEAIEEI 1026
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
623-735 |
1.30e-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: 59.99 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 623 EKREEqervqkKTFTNWINSYLLkrvpPLRIDDLINDLRDGtklIALLEVLsgERL---PVEKGRVLR-----RPHFLSN 694
Cdd:cd21219 2 GSREE------RAFRMWLNSLGL----DPLINNLYEDLRDG---LVLLQVL--DKIqpgCVNWKKVNKpkplnKFKKVEN 66
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 320544542 695 ANTALQfLASKR-IKLVNINPADLVDGRPPVVLGLIWTIILY 735
Cdd:cd21219 67 CNYAVD-LAKKLgFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
772-883 |
2.48e-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: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 772 AEKWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESkLGI 851
Cdd:cd21256 8 AREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGI 86
|
90 100 110
....*....|....*....|....*....|...
gi 320544542 852 AKLLDAED-VDVPKPDEKSIMTYVAQfLHKYPE 883
Cdd:cd21256 87 KSTLDINEmVRTERPDWQSVMTYVTA-IYKYFE 118
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
621-732 |
4.20e-09 |
|
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: 58.40 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 621 IKEKREEqervqkKTFTNWINSYllkRVPPlRIDDLINDLRDGTKLIALLEVLSgerlP--VEKGRVLRRPH-------F 691
Cdd:cd21298 2 IEETREE------KTYRNWMNSL---GVNP-FVNHLYSDLRDGLVLLQLYDKIK----PgvVDWSRVNKPFKklganmkK 67
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 320544542 692 LSNANTALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTI 732
Cdd:cd21298 68 IENCNYAVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQL 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3110-3322 |
4.54e-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: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3110 LWSQYEQSNEQISNWLRDVEGRVKAETSSQvNLSEVPQKLQELSILQQDVLAHEPIINNLEQTSQQLIEKNPEA--RIGQ 3187
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDaeEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3188 FVTHLVQRYQAVSKALTSYIDKIRGAQLSnANFAKAAKDFNEWFGDAKiefQELARMGSPGSSSATAQQLQTVKNYIKTF 3267
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLEEKE---AALASEDLGKDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 320544542 3268 DNGQILLNNAVDIGEALYPVVSPDNRERIRADLRQMREKFDYLRDEANAFMQQVE 3322
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6316-7127 |
4.69e-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: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6316 KQAQNRWNDFAANKDKLEKWLNETETTLKvapetkgELSEMKTLLERYKTLSNELK------------LKGNELEQLQSE 6383
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLK-------SLERQAEKAERYKELKAELRelelallvlrleELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6384 ARDLGTEVDAVNRLQSRCDKLKNDCSAHITALEQEMFD----YNAYHQSLQDVEKWLLQISFQLMAHNslfiSNREQTQE 6459
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkeLYALANEISRLEQQKQILRERLANLE----RQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6460 QIKQHE-----------ALLVEIQKYQTNLDDLNAKGQAQIKRYESSTPAIRpTVESQLKNIQDSYNSLLQTSVQIKNRL 6528
Cdd:TIGR02168 324 QLEELEskldelaeelaELEEKLEELKEELESLEAELEELEAELEELESRLE-ELEEQLETLRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6529 ------LESLAKFQEYEDT-------------LDSIMRNLETYEPII---QTELDAPATSLELAQNQLRCAQEMQNKLNN 6586
Cdd:TIGR02168 403 erlearLERLEDRRERLQQeieellkkleeaeLKELQAELEELEEELeelQEELERLEEALEELREELEEAEQALDAAER 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6587 EKSRLAAAVQACEAATASISRPSSPLETAMQAIPERELIVrAKLEDLLdqKPPPKTRSST----GG-----VSTDDDKDE 6657
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGIL-GVLSELI--SVDEGYEAAIeaalGGrlqavVVENLNAAK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6658 ADVEIQVE----------LSDVNEALLDPIAHERVKNYRRIVRLNSAHVGKLNELVAKVQSHLGGLtASVSELEQQQKQR 6727
Cdd:TIGR02168 560 KAIAFLKQnelgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV-LVVDDLDNALELA 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6728 AELqdwvKKQQSSVSdwmmrpcklrpeaAQQELVSMNDLLNSIGDKRSQLMLEmtgslgdedtdLDDNIDKLESELMDAI 6807
Cdd:TIGR02168 639 KKL----RPGYRIVT-------------LDGDLVRPGGVITGGSAKTNSSILE-----------RRREIEELEEKIEELE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6808 AKKQAGQNVIDGYRQGMADVQNWFDTLIKRMDVLDRGSGLNCAQKMAAINEIKNEYEL--QGHPKIQELKGKAAQVAEVI 6885
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaQLSKELTELEAEIEELEERL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6886 SNLDG---------QQVEEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEELQApkpLGYTP 6956
Cdd:TIGR02168 771 EEAEEelaeaeaeiEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED---LEEQI 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6957 KDAEARQQKIKSLMKDAEAK----QSLADVLEKRVANMQQELEpveysQLESALRNLNTENRNLSGVLKAELDRALEASK 7032
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELieelESELEALLNERASLEEALA-----LLRSELEELSEELRELESKRSELRRELEELRE 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7033 ARKSLENDLDKARQWLKTKISEVR-----------KLPVYHPLTSAEIEKKI----------------------QENRKY 7079
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDNLQERLSeeysltleeaeALENKIEDDEEEARRRLkrlenkikelgpvnlaaieeyeELKERY 1002
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 320544542 7080 DDDAKQFNDsvLTDVQRQAANIMKDCDDADKAALQQILDEIAADYQTL 7127
Cdd:TIGR02168 1003 DFLTAQKED--LTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRV 1048
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4750-4919 |
5.79e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.54 E-value: 5.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4750 LDRLKNLKASLADEFPRVDQVRALGEKVIPGTVDVGQvNIKSQIDTTQQEWESLLTTISSTIEAIEARLQHWSEYEQLrD 4829
Cdd:cd00176 39 LKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-D 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4830 QCLAWIRDTDNNLHAIDLKEDLPKKRAQLDALKALQGDVRAKELEVDNVTEKAQTLLKGPSSNRAsgpelvtkyQQIFHK 4909
Cdd:cd00176 117 DLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDAD---------EEIEEK 187
|
170
....*....|
gi 320544542 4910 VKELNNRWQQ 4919
Cdd:cd00176 188 LEELNERWEE 197
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
778-877 |
5.81e-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: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 778 GARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDA 857
Cdd:cd21196 3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSA 82
|
90 100
....*....|....*....|
gi 320544542 858 EDVdVPKPDEKSIMTYVAQF 877
Cdd:cd21196 83 QAV-VAGSDPLGLIAYLSHF 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7241-7929 |
5.94e-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: 64.31 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7241 DRVNALGDHI----KKYKDAKSRLAECSQFLGNIQQKLRELNRPIGSRIEDVQDLLGAYEGILKELKDSKSkmgdmqmdD 7316
Cdd:TIGR02168 232 LRLEELREELeelqEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ--------Q 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7317 LPELQSILAQQDDMIKLIEDQLAHLRQLLLLREQFIALINEIIAFIMK-YTDVIIDIENSPDSLEDKINKYDDVIVKIQE 7395
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEeLESLEAELEELEAELEELESRLEELEEQLET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7396 CEGVLASANDKGQKIASE--GNAADKNSITEQLQSLKNQL-QNLRKAVESQRQKHQLQLESHKKMAAELSEILDWLHSH- 7471
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEieRLEARLERLEDRRERLQQEIeELLKKLEEAELKELQAELEELEEELEELQEELERLEEAl 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7472 EGAAKSRPLLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEIgMPSSLLemlSEGRSLVASLPHELEEREKYL 7551
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL-KNQSGL---SGILGVLSELISVDEGYEAAI 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7552 KNNRDSRLEYMqLVAKFNDWVHEAELRLQNSQHGIDYehLVQDLDEHKIFFGNEAPIRNLVHKQIQEAAD--KIWSSLNN 7629
Cdd:TIGR02168 540 EAALGGRLQAV-VVENLNAAKKAIAFLKQNELGRVTF--LPLDSIKGTEIQGNDREILKNIEGFLGVAKDlvKFDPKLRK 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7630 YEQSELSaelaqfQTKLTNTLANAKTQQSELEKEA-------ERWR-----------------EYQQSIDRVKATIERT- 7684
Cdd:TIGR02168 617 ALSYLLG------GVLVVDDLDNALELAKKLRPGYrivtldgDLVRpggvitggsaktnssilERRREIEELEEKIEELe 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7685 --------------KFVDEPVQNLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIRQADARNRQLIEQDnAGLNRS 7750
Cdd:TIGR02168 691 ekiaelekalaelrKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI-EELEER 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7751 WQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFRNV-----DPTVRSRRHLEDTKNAIQELREESNQLKS 7825
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeaaNLRERLESLERRIAATERRLEDLEEQIEE 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7826 SHKEIEALSKSILTFlgevhKPSAEAIQAKVDKLVEQQAKLN---DTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALH 7902
Cdd:TIGR02168 850 LSEDIESLAAEIEEL-----EELIEELESELEALLNERASLEealALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
730 740
....*....|....*....|....*..
gi 320544542 7903 EQLQsvhvydEHIAQTEQLLITLNSQV 7929
Cdd:TIGR02168 925 AQLE------LRLEGLEVRIDNLQERL 945
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4174-4391 |
6.67e-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: 6.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4174 QLSSYQDILNQTVNWLDQVEKLIHNENPASwtSAQEIRSKLYKYKATNQDINSHKRIVEAVNEKAAALLgSAAPANADEI 4253
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGD--DLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4254 SKAVAEVNKRYDQVGQDCAKLVADLDGAFDVYQQFSELQKAQQDYQKNlwDRLTGYSDYSGNKAALQARLQKINEIQDAL 4333
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEK--EAALASEDLGKDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 320544542 4334 PEGVAKLKSLEDHIEQQASNIPARSKEVMARDLANLHADFEKFGASLSDVKSGLENRL 4391
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
780-874 |
8.61e-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: 8.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 780 RKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAED 859
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90
....*....|....*..
gi 320544542 860 VDV--PKPDEKSIMTYV 874
Cdd:cd21261 83 MMVmgRKPDPMCVFTYV 99
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3965-4170 |
9.72e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.15 E-value: 9.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3965 QWDKFEKALEELTKWCRSAEAVFREQQLQSTLHEKVEQLEKYKIQRELILQKEKEIDAFGDAAHALLNNCG--ADRLKTL 4042
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHpdAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4043 TTQITNRYQLLQVLSKEVVNRWSNLVDDHQFYQDKYnEVDLWLQPIESQMAKVLLDEPTQSSNIL----QVLLSEKEQAE 4118
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLESVEELlkkhKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 320544542 4119 SLFAALNAAGEKALPETSTQGREKIRKDLRDIRDRWDKLDEGIRNLEKRQEA 4170
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
776-877 |
1.97e-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: 56.62 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 776 KQGARKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLV-NLAELKKTSNRQRLETAFDVAESKLGIAKL 854
Cdd:cd21314 9 KQTPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQV 85
|
90 100
....*....|....*....|...
gi 320544542 855 LDAEDVDVPKPDEKSIMTYVAQF 877
Cdd:cd21314 86 IAPEEIVDPNVDEHSVMTYLSQF 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7037-7248 |
2.73e-08 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 58.61 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7037 LENDLDKARQWLKTKISEVRKLpvYHPLTSAEIEKKIQENRKYDDDAKQFNDSVlTDVQRQAANIMKDCDDaDKAALQQI 7116
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSST--DYGDDLESVEALLKKHEALEAELAAHEERV-EALNELGEQLIEEGHP-DAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7117 LDEIAADYQTLKDESSKRGKSLDDLLQGRKAFEDSMKnMGDWLNEMETATEGELRTTSLPVLEEQLAHYKKLLSDAENKG 7196
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 320544542 7197 GLINDVSEQGKSILPTLSNADKLKLNDDIKNMKDRYGRIKNTIDDRVNALGD 7248
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7752-8570 |
3.56e-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: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7752 QDLVRSLEQRRDNLQ---QLAEHWDGFENSLHAWEKAL--GRLEDKFRNVDPTvrsrrhLEDTKNAIQELREESNQLKSS 7826
Cdd:TIGR02168 192 EDILNELERQLKSLErqaEKAERYKELKAELRELELALlvLRLEELREELEEL------QEELKEAEEELEELTAELQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7827 HKEIEALSKsiltFLGEVHKpSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQ 7906
Cdd:TIGR02168 266 EEKLEELRL----EVSELEE-EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7907 SVHvydehiAQTEQLLITLNSQVQQAAEESKLLVAQTTA--HYQAKQNQLPSDIAQEFTALELLAERVQVTMETKEkdfk 7984
Cdd:TIGR02168 341 ELE------EKLEELKEELESLEAELEELEAELEELESRleELEEQLETLRSKVAQLELQIASLNNEIERLEARLE---- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7985 raktvrteyvDGVDEVQRWllQAEVQVQERSLTPTQMKELLQRINHEITaiyERFTLVKTNGQLIIENCRNSEEKTLVQT 8064
Cdd:TIGR02168 411 ----------RLEDRRERL--QQEIEELLKKLEEAELKELQAELEELEE---ELEELQEELERLEEALEELREELEEAEQ 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8065 TIDQLAASLAQVRGWLDEKKQAVGdsldawtRFMNLYQ---IVMSWASEKRNFIDQTIELRTLPE---------ARNKLN 8132
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQE-------NLEGFSEgvkALLKNQSGLSGILGVLSELISVDEgyeaaieaaLGGRLQ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8133 DYVT-SVKSIKPIVKHLSEMDKELEHIGQVTTVGDlkDKLQEAEDAKISVEAVLLERNSLLQEACEEWdqceRKIKDIRS 8211
Cdd:TIGR02168 549 AVVVeNLNAAKKAIAFLKQNELGRVTFLPLDSIKG--TEIQGNDREILKNIEGFLGVAKDLVKFDPKL----RKALSYLL 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8212 WHEKTKQGLDSSQQQKKPLRDQLGFCekTLADINVQKtklRLSIEKLEVHFRNGMGGdprLSENVDDLVRVLDGLGELVK 8291
Cdd:TIGR02168 623 GGVLVVDDLDNALELAKKLRPGYRIV--TLDGDLVRP---GGVITGGSAKTNSSILE---RRREIEELEEKIEELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8292 AKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRLVMAPTYLPHDRERALAEQQDLITQELDELLQSLSSVEDGIANMN 8371
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8372 QSsldgmlhgLKLIQSNLEVHERDAIELKNQAKKLptdpatERLLNDTVDRIDLLLRRtqqgitmIANAMHGQKKRQQEI 8451
Cdd:TIGR02168 775 EE--------LAEAEAEIEELEAQIEQLKEELKAL------REALDELRAELTLLNEE-------AANLRERLESLERRI 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8452 DEYQQHLLELEQWIIEVSAELASfeptsdsstdeqvLKSQVERSQQLLRTLKDRQQSMEDLVEQTRQLqshpdvspladt 8531
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEA------------ 888
|
810 820 830
....*....|....*....|....*....|....*....
gi 320544542 8532 lmeqlqsiITILREQVTVATKRIFTIEKRIVDLRKAKSE 8570
Cdd:TIGR02168 889 --------LALLRSELEELSEELRELESKRSELRRELEE 919
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5900-6108 |
4.36e-08 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 58.23 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5900 QLEEIFKLYKILIEWLEDVEPSVkTSDEFLNDLSEKRAALEKFRVIQRDINGHNDIVEKIN---QRLKEDNSLDLKDFQP 5976
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNelgEQLIEEGHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5977 GL----TKFDDLQTQVNKIIESLENQVNSHEKYKQAYnELQDWLRRTRIEVEQCADCHgEKDQVESRLNRLGDIQSSSLE 6052
Cdd:cd00176 80 RLeelnQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 320544542 6053 GKALLEACEELSQAVIATSGSEGQDNVAQEIKHLTSEWETLQTISRDARSSLESCL 6108
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
776-877 |
4.45e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 55.48 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 776 KQGARKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLVNLAEL---KKTSNRQRleTAFDVAESKLGIA 852
Cdd:cd21313 6 KQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCPDWESwdpQKPVDNAR--EAMQQADDWLGVP 80
|
90 100
....*....|....*....|....*
gi 320544542 853 KLLDAEDVDVPKPDEKSIMTYVAQF 877
Cdd:cd21313 81 QVITPEEIIHPDVDEHSVMTYLSQF 105
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
10968-11918 |
5.70e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.13 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10968 TLANVAETQdKERKELDKEVTLAKAYFNNvqqDISREAPQNPKESEEQLAALRAhlqtLARTEEQLRQLKERHQN--SEV 11045
Cdd:PRK04863 245 TLEAIRVTQ-SDRDLFKHLITESTNYVAA---DYMRHANERRVHLEEALELRRE----LYTSRRQLAAEQYRLVEmaREL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11046 ApsvASSDDDGILEvlalwqkifqdtfQEYHRLSTRLARSQNsseALRLWRQYLQHVQSFLscaipEDYSSLREQQQLCA 11125
Cdd:PRK04863 317 A---ELNEAESDLE-------------QDYQAASDHLNLVQT---ALRQQEKIERYQADLE-----ELEERLEEQNEVVE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11126 IHQNLLISQQSVLSETPLE-SELSEQykaltnlhnetLSRIMQRNGELERRVSgwnAYRQQLAAL--------------- 11189
Cdd:PRK04863 373 EADEQQEENEARAEAAEEEvDELKSQ-----------LADYQQALDVQQTRAI---QYQQAVQALerakqlcglpdltad 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11190 --LDWLRQREAERNALQLRyihlkrVPHLKHRL---DAMIQQLDQGEQQSKAL-----QEQQQELARhcdDALATAMrmE 11259
Cdd:PRK04863 439 naEDWLEEFQAKEQEATEE------LLSLEQKLsvaQAAHSQFEQAYQLVRKIagevsRSEAWDVAR---ELLRRLR--E 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11260 QASIGQRISNLRAALKTWQGFL---QRVTQLSESYEQRVNQ---LQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQ 11333
Cdd:PRK04863 508 QRHLAEQLQQLRMRLSELEQRLrqqQRAERLLAEFCKRLGKnldDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11334 RVQLGAQVSALESLT----VTQ---EELKECiSPHDMKTiRQRNWLLWQQHADLDYQLANLINSIEERLSLLsnyQIRYD 11406
Cdd:PRK04863 588 LEQLQARIQRLAARApawlAAQdalARLREQ-SGEEFED-SQDVTEYMQQLLERERELTVERDELAARKQAL---DEEIE 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11407 RISQ-------WLQRLEQRV------EKDADVTAMTNPEQAAkqLEQQVNSELQLRDkerewLLSTSRELLTLYSEPEVR 11473
Cdd:PRK04863 663 RLSQpggsedpRLNALAERFggvllsEIYDDVSLEDAPYFSA--LYGPARHAIVVPD-----LSDAAEQLAGLEDCPEDL 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11474 SQVQQQSDSLIDRWQRLKYLAKQKATKIGELKMTLLRL-----------EERIALIRAWLFEVESQLDKpLNFESytpnv 11542
Cdd:PRK04863 736 YLIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFpevplfgraarEKRIEQLRAEREELAERYAT-LSFDV----- 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11543 ieaklkehEQIQRSIEHHSSNVGEVLNLV-----EMLLNDADSWRTQVNTSGLAASAQNLEQRwknvcsqSAERKARilt 11617
Cdd:PRK04863 810 --------QKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVELERALADHESQEQQQR-------SQLEQAK--- 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11618 iwNLLQQLIKLtaehknwlgkqESQIAGFERDQkshskhkLEERQMELRAKLEELE-------SQSVNLRQLEQIYAKLA 11690
Cdd:PRK04863 872 --EGLSALNRL-----------LPRLNLLADET-------LADRVEEIREQLDEAEeakrfvqQHGNALAQLEPIVSVLQ 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11691 msagVEPENIQKLTLPTKVMVSMWRQLTPRCHALLDAIDKDAKLMREFNNAQLEATNSLNaiqkalEQLPsaenqqtska 11770
Cdd:PRK04863 932 ----SDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKNSDLN------EKLR---------- 991
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11771 epkavlQRLESLEKKLQDAQQHVQQADNLAQEAKTRtkqqpqlkqLLELVSAYTTLWQTVQtrivtlkttwltRAAQAAA 11850
Cdd:PRK04863 992 ------QRLEQAEQERTRAREQLRQAQAQLAQYNQV---------LASLKSSYDAKRQMLQ------------ELKQELQ 1044
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 320544542 11851 SLPV----SEAANAAVQVNTLSQRkLRQAQQmQREtsitakdayimELQTAITECQNNLDELQRTVVDKTRK 11918
Cdd:PRK04863 1045 DLGVpadsGAEERARARRDELHAR-LSANRS-RRN-----------QLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6802-7151 |
5.79e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6802 ELMDAIA-------KKQAGQNVIDGYRQGMADVQNWFDTLIKRMDVLDRGSglNCAQKMAAINEIKNEYElqGHPKIQEL 6874
Cdd:TIGR02169 157 KIIDEIAgvaefdrKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER--EKAERYQALLKEKREYE--GYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6875 KGKAAQVAEVISNLDGQqvEEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEgAKGEIDQLQnwVKQQIEELQAP----- 6949
Cdd:TIGR02169 233 EALERQKEAIERQLASL--EEELEKLTEEISELEKRLEEIEQLLEELNKKIK-DLGEEEQLR--VKEKIGELEAEiasle 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6950 ---KPLGYTPKDAEARQQKIKSLMkdaEAKQSLADVLEKRVANMQQELEPV---------EYSQLESALRNLNTENRNLS 7017
Cdd:TIGR02169 308 rsiAEKERELEDAEERLAKLEAEI---DKLLAEIEELEREIEEERKRRDKLteeyaelkeELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7018 GVLKAELDRALEASKARKSLENDLDKARQWLKTKISEVRKLpvyhpltSAEIEKKIQENRKYDDDAKQFNDSVLTDVQRQ 7097
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL-------NAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 320544542 7098 AANImkdcddADKAALQQILDEIAADYQTLKDESSKRGKSLDDLLQGRKAFEDS 7151
Cdd:TIGR02169 458 EQLA------ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7371-7514 |
5.94e-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: 5.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7371 DIENSPDSLEDKINKYDDVIVKIQECEGVLASANDKGQKIASEGnAADKNSITEQLQSLKNQLQNLRKAVESQRQKHQLQ 7450
Cdd:cd00176 27 DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQERLEELNQRWEELRELAEERRQRLEEA 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320544542 7451 LESHKKMaAELSEILDWLHSHEGAAKSRPlLDRDPESVERELQKHQSLSQDIESYLNKFNKIND 7514
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 ... |
783-877 |
7.68e-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: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 783 LLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDVD- 861
Cdd:cd21250 9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMAs 88
|
90
....*....|....*.
gi 320544542 862 VPKPDEKSIMTYVAQF 877
Cdd:cd21250 89 AEEPDKLSMVMYLSKF 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1291-1505 |
1.11e-07 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 57.07 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 1291 QEYKSGIEQLSRWLRGAESVLDQRQVLGNSEQVKEYGQQLQQLASEIDDNEELFKTISRNFQSLIQDLSRD--EVDKMMK 1368
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDaeEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 1369 LLKQEKESLVRIRAQLpaKLHLFHQLQIQQESLEAgqKEIHQWLSEAEQLLGTHNLSGGRDAINEQLHKHKTYFSRTVYY 1448
Cdd:cd00176 83 ELNQRWEELRELAEER--RQRLEEALDLQQFFRDA--DDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 320544542 1449 RSMLESKNKVFQNLLKAVSSDDKIDTApasQQMQQLNERFNYVIQNAQQWEQRLDSA 1505
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIE---EKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5791-6004 |
1.21e-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: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5791 EHQQHHSLYEECQSWIEKTREKLSEcEQIPGTLNEVQIKLNTVKNLRQGFETGQNKLRYLLELKEKVImNTEQNGAAKIQ 5870
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5871 EDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILiEWLEDVEPSVKtSDEFLNDLSEKRAALEKFRVIQRDIN 5950
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 320544542 5951 GHNDIVEKINQRLKEdnsLDLKDFQPGLTKFDDLQTQVNKIIESLENQVNSHEK 6004
Cdd:cd00176 157 AHEPRLKSLNELAEE---LLEEGHPDADEEIEEKLEELNERWEELLELAEERQK 207
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6931-7142 |
1.38e-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: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6931 EIDQLQNWVKQQIEELQAPKPlGYTPKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELePVEYSQLESALRNLN 7010
Cdd:cd00176 8 DADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7011 TENRNLSGvLKAELDRALEASKARKSLENDLDKARQWLKTKISEVRKLPVYHPLTsaEIEKKIQENRKYDDDAKQfNDSV 7090
Cdd:cd00176 86 QRWEELRE-LAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLE--SVEELLKKHKELEEELEA-HEPR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 320544542 7091 LTDVQRQAANIMKDCDDADKAALQQILDEIAADYQTLKDESSKRGKSLDDLL 7142
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
627-730 |
1.52e-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: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 627 EQERvQKKTFTNWINSYllkRVPPlRIDDLINDLRDGTKLI-ALLEVLSGErlpVEKGRV--------LRRPHFLSNANT 697
Cdd:cd21300 4 EGER-EARVFTLWLNSL---DVEP-AVNDLFEDLRDGLILLqAYDKVIPGS---VNWKKVnkapasaeISRFKAVENTNY 75
|
90 100 110
....*....|....*....|....*....|...
gi 320544542 698 ALQFLASKRIKLVNINPADLVDGRPPVVLGLIW 730
Cdd:cd21300 76 AVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
11143-11530 |
1.59e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11143 LESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHLK----------- 11211
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELReeleklekllq 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11212 ------RVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELAR------HCDDALATAMRMEQASIGQRISNLRAALKTWQG 11279
Cdd:COG4717 127 llplyqELEALEAELAELPERLEELEERLEELRELEEELEEleaelaELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11280 FLQRVTQLSESYEQRVNQLQQEFGAAQKllDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESL------------ 11347
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLEN--ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIltiagvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11348 -------------TVTQEELKECISPHDMKTIRQRNWLLWqqHADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQR 11414
Cdd:COG4717 285 llallflllarekASLGKEAEELQALPALEELEEEELEEL--LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11415 LEQRVEKD--------ADVTAMTNPEQAAKQLEQQVNSELQLRDKER--EWLLSTSRELLTLYSEPEVRSQVQQQSDSLI 11484
Cdd:COG4717 363 LQLEELEQeiaallaeAGVEDEEELRAALEQAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEELE 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 320544542 11485 DRWQRLKYLAKQKATKIGELKMtlLRLEERIALIRAWLFEVESQLD 11530
Cdd:COG4717 443 ELEEELEELREELAELEAELEQ--LEEDGELAELLQELEELKAELR 486
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3539-3732 |
1.60e-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: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3539 KWDEFDTIIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINELMDQGREI-----EGETDLNLK 3613
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeghPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3614 LSRLNTRYQTLKNLCKESIAKYVNYVKDHEsFDKDFDSFKQNLQsSVDELAKTNEIVGDQSVLQDQQNKLREMSDKRILD 3693
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLE-EKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 320544542 3694 STLFEGLIDRGEKLYGHTSPEGREIIRQQLRALRTLWDN 3732
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEE 197
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7621-7908 |
1.80e-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: 59.31 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7621 DKIWSSLNNYEQSELSAELAQFQTKLTNTLANAKTQQSELEKEAERWREYQQSIDRVKATIE------RTKFVDEPVQ-- 7692
Cdd:TIGR02169 214 QALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEelnkkiKDLGEEEQLRvk 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7693 -NLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIRQADARNRQLIEQ--DNAGLNRSWQDLVRSLEQRRDNLQQLA 7769
Cdd:TIGR02169 294 eKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieEERKRRDKLTEEYAELKEELEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7770 EhwdgfenslhAWEKALGRLEDKFRNVdptvrsRRHLEDTKNAIQELR-------EESNQLKSSHKEIEALSKSILTFLG 7842
Cdd:TIGR02169 374 E----------EVDKEFAETRDELKDY------REKLEKLKREINELKreldrlqEELQRLSEELADLNAAIAGIEAKIN 437
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320544542 7843 EVhKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSV 7908
Cdd:TIGR02169 438 EL-EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
7223-7898 |
2.11e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7223 DDIKNMKDRYGRIKNTIDDRVNALGDHIKKYKDAKSRLAECSQFLGNIQQKLRELNrpigSRIEDVQDLLGAYEGILKEL 7302
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEIS----SELPELREELEKLEKEVKEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7303 KDSKSKMGDMQMDDLPELQSILAQQDDmIKLIEDQLAHLRQLLLLREQFIALINEI----------IAFIMKYTDVIIDI 7372
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEK-IRELEERIEELKKEIEELEEKVKELKELkekaeeyiklSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7373 ENSPDSLEDKINkydDVIVKIQECEgvlasandkgqkiasegnaadknSITEQLQSLKNQLQNLRKAVESQRQKHQLqLE 7452
Cdd:PRK03918 313 EKRLSRLEEEIN---GIEERIKELE-----------------------EKEERLEELKKKLKELEKRLEELEERHEL-YE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7453 SHKKMAAELSEIldwlhshegaaKSRpLLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEIGMPSSLLEMLSE 7532
Cdd:PRK03918 366 EAKAKKEELERL-----------KKR-LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7533 GRSLVASLPHEL-EEREKYLKNnrdsrlEYMQLVAKFNDWVHEAELRLqnsqhgidyEHLVQDLDEHKIFFGNEAPIRNL 7611
Cdd:PRK03918 434 AKGKCPVCGRELtEEHRKELLE------EYTAELKRIEKELKEIEEKE---------RKLRKELRELEKVLKKESELIKL 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7612 vhKQIQEAADKIWSSLNNYEQSELSAELAQFQtKLTNTLANAKTQQSELEKEAERWREYQQSidrvKATIERTKfvDEPV 7691
Cdd:PRK03918 499 --KELAEQLKELEEKLKKYNLEELEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKL--DELE 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7692 QNLAGLHFNIQKLSHaignvqsqnSDLTLVNQQAQSLirqaDARNRQLIEQDNAglNRSWQDLVRSLEQRRDNLQQLAEH 7771
Cdd:PRK03918 570 EELAELLKELEELGF---------ESVEELEERLKEL----EPFYNEYLELKDA--EKELEREEKELKKLEEELDKAFEE 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7772 WDGFENSLhawEKALGRLEDKFRNVDPtvrsrrhlEDTKNAIQELREESNQLKSSHKEIEALSKSIltflgevhkpsaEA 7851
Cdd:PRK03918 635 LAETEKRL---EELRKELEELEKKYSE--------EEYEELREEYLELSRELAGLRAELEELEKRR------------EE 691
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 320544542 7852 IQAKVDKLVEQqaklndtlRDKEQQVSKDLEEIEQVFRRISQLQDKL 7898
Cdd:PRK03918 692 IKKTLEKLKEE--------LEEREKAKKELEKLEKALERVEELREKV 730
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4829-5031 |
2.29e-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: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4829 DQCLAWIRDTDNNLHAIDLKEDLPKKRAQLDALKALQGDVRAKELEVDNVTEKAQTLLkgpSSNRASGPELVTKYQQIFH 4908
Cdd:cd00176 10 DELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI---EEGHPDAEEIQERLEELNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4909 KVKELNNRWQQYVTSHED------FDNAISDCSSWINEIKEKL---DYCSDMSSMspKELDKKLATIQDVILLKDEgsaR 4979
Cdd:cd00176 87 RWEELRELAEERRQRLEEaldlqqFFRDADDLEQWLEEKEAALaseDLGKDLESV--EELLKKHKELEEELEAHEP---R 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 320544542 4980 VLKILEQAQHVLANTAPGGHEAINKELTDLQDLWSGIALRIMDVKSNLDDSI 5031
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
627-739 |
2.42e-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: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 627 EQERVqkkTFTNWINSYL-----LKRVPPLRIDD--LINDLRDGT---KLIALLEVLSGERLPVEKGRVlrRPHFLS-NA 695
Cdd:cd21323 23 EEEKV---AFVNWINKALegdpdCKHVVPMNPTDesLFKSLADGIllcKMINLSQPDTIDERAINKKKL--TPFTISeNL 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 320544542 696 NTALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTII---LYFQIE 739
Cdd:cd21323 98 NLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIkvgLFADIE 144
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
627-733 |
2.89e-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: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 627 EQERVQKKTFTNWINSYllkRVPPLrIDDLINDLRDGTKLIALLEVLsgeRLPVEKGRVLRRPHFL--------SNANTA 698
Cdd:cd21329 2 EGESSEERTFRNWMNSL---GVNPY-VNHLYSDLCDALVIFQLYEMT---RVPVDWGHVNKPPYPAlggnmkkiENCNYA 74
|
90 100 110
....*....|....*....|....*....|....*.
gi 320544542 699 LQFLASK-RIKLVNINPADLVDGRPPVVLGLIWTII 733
Cdd:cd21329 75 VELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLM 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10951-11558 |
3.09e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10951 ELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDIsreapqnpkesEEQLAALRAHLQTLARTE 11030
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-----------EEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11031 EQLRQLKERHQNsevapsvASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEALRLwrqylqhvqsflscai 11110
Cdd:COG1196 302 QDIARLEERRRE-------LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA---------------- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11111 pedysSLREQQQLCAIHQNLLISQQSVLSEtpLESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALL 11190
Cdd:COG1196 359 -----ELAEAEEALLEAEAELAEAEEELEE--LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11191 DWLRQREAERNALQlryihlkrvphlkhRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALATAMRmEQASIGQRISNL 11270
Cdd:COG1196 432 ELEEEEEEEEEALE--------------EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE-ELAEAAARLLLL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11271 RAALKTWQGFLQRVTQLsesyeqrvnQLQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRV--QLGAQVSALESLT 11348
Cdd:COG1196 497 LEAEADYEGFLEGVKAA---------LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVveDDEVAAAAIEYLK 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11349 VTQEELKECISPHDMKTIRQRNWLLWQQHADLDYQL-ANLINSIEERLSLLSNY----QIRYDRISQWLQRLEQRVEKDA 11423
Cdd:COG1196 568 AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLvASDLREADARYYVLGDTllgrTLVAARLEAALRRAVTLAGRLR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11424 DVT-AMTNPEQAAKQLEQQVNSELQLRDKEREWLLSTSRELLtlysepEVRSQVQQQSDSLIDRWQRLKYLAKQKATKIG 11502
Cdd:COG1196 648 EVTlEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA------EEELELEEALLAEEEEERELAEAEEERLEEEL 721
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 320544542 11503 ELKMTLLRLEERIALIRAWLFEVESQLDKPLNFESYTPNVIEAKLKEHEQIQRSIE 11558
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5860-6591 |
3.99e-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: 58.14 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5860 NTEQNGAAKIQEDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDVEPSVKTSDEFLND----LSEK 5935
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERqleeLEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5936 RAALEKFRVIQRDINghNDIVEKINQRLKEDNSLDLKdfqpgLTKFDDLQTQVNKIIESLENQvnsHEKYKQAYNELQDW 6015
Cdd:TIGR02168 325 LEELESKLDELAEEL--AELEEKLEELKEELESLEAE-----LEELEAELEELESRLEELEEQ---LETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6016 LRRTRIEVEQCADchgEKDQVESRLNRLGDIQSSslEGKALLEACEELSQAVIATsgsegqdnVAQEIKHLTSEWETLQT 6095
Cdd:TIGR02168 395 IASLNNEIERLEA---RLERLEDRRERLQQEIEE--LLKKLEEAELKELQAELEE--------LEEELEELQEELERLEE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6096 ISRDARSSLESCLAAWQTFLQKFNKINLWIETMNKRVTKsQEGENKTPEDLVNAKKLLEE---VLAEKDNVEDlndNCEL 6172
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN-LEGFSEGVKALLKNQSGLSGilgVLSELISVDE---GYEA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6173 LMEQSACTRIRDQTIETQANYTK----LLTSAQGLVAKIEKNLSDHTEFLNYKKEMDAWIEKAQQVLDDCSTDGDAA--- 6245
Cdd:TIGR02168 538 AIEAALGGRLQAVVVENLNAAKKaiafLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrka 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6246 --------IIAQKLDTVNSLASRLPEGqhllalvqdayskASNITPEDKQEKLRELMTKVREDWDALGLAVKQKLSDLKQ 6317
Cdd:TIGR02168 618 lsyllggvLVVDDLDNALELAKKLRPG-------------YRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6318 aqnrwndfaankdklekwlnetettlkvapetkgelsEMKTLLERYKTLSNELKLKGNELEQLQSEARDLGTEVDAVNRL 6397
Cdd:TIGR02168 685 -------------------------------------KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6398 QSRCDKLKNDCSAHITALEQEMFDYNAYHQSLQDVEKWLLQISFQLMAHNSLFISNREQTQEQIKQHEALLV----EIQK 6473
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalreALDE 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6474 YQTNLDDLNAKGQAQIKRYESStpairptvESQLKNIQDSYNSLLQTSVQIKNRLLESLAKFQEYEDTLDSIMRNLEtye 6553
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESL--------ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE--- 876
|
730 740 750
....*....|....*....|....*....|....*...
gi 320544542 6554 pIIQTELDAPATSLELAQNQLRCAQEMQNKLNNEKSRL 6591
Cdd:TIGR02168 877 -ALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
6892-7464 |
6.43e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6892 QVEEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNwVKQQIEELQapKPLGYTPKDAEARQQKIKSLMK 6971
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-LKEEIEELE--KELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6972 DAEAKQSLADVLEKRVANMqQELEPV--EYSQLESALRNLNTENRNLSgVLKAELDRALEASKARKSLENDLDKARQWLK 7049
Cdd:PRK03918 267 RIEELKKEIEELEEKVKEL-KELKEKaeEYIKLSEFYEEYLDELREIE-KRLSRLEEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7050 TKISEVRK----LPVYHPLTSaEIEKKIQENRKYDddaKQFNDSVLTDVQRQAANIMKdcddaDKAALQQILDEIAADYQ 7125
Cdd:PRK03918 345 KKLKELEKrleeLEERHELYE-EAKAKKEELERLK---KRLTGLTPEKLEKELEELEK-----AKEEIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7126 TLKDESSKRGKSLDDL--------LQGRKAFEDSMKN--------MGDWLNEMETATEGE--LRtTSLPVLEEQLAHYKK 7187
Cdd:PRK03918 416 ELKKEIKELKKAIEELkkakgkcpVCGRELTEEHRKElleeytaeLKRIEKELKEIEEKErkLR-KELRELEKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7188 LLSdaenkgglINDVSEQGKSILPTLSNADKLKLNDDIKNMKDRYGRIkNTIDDRVNALGDHIKKYKDAKSRLAECSQFL 7267
Cdd:PRK03918 495 LIK--------LKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKL-IKLKGEIKSLKKELEKLEELKKKLAELEKKL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7268 GNIQQKLRELNRPIGSR----IEDVQDLLGAYEGILK---ELKDSKSkmgdmqmddlpELQSILAQQDDMIKLIEDQLAH 7340
Cdd:PRK03918 566 DELEEELAELLKELEELgfesVEELEERLKELEPFYNeylELKDAEK-----------ELEREEKELKKLEEELDKAFEE 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7341 LRQLLLLREQfiaLINEIIAFIMKYTDviidienspdslEDKINKYDDVIVKIQECEGVLASAndkgqkiasEGNAADKN 7420
Cdd:PRK03918 635 LAETEKRLEE---LRKELEELEKKYSE------------EEYEELREEYLELSRELAGLRAEL---------EELEKRRE 690
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 320544542 7421 SITEQLQSLKNQLQNLRKAVEsqrqkhqlQLESHKKMAAELSEI 7464
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKK--------ELEKLEKALERVEEL 726
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
7288-7832 |
7.35e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7288 VQDLLGAYEGILKELKDSKSKMGDMQMDD-LPELQSILAQQDDMIKLIEDQLAHLRQLLLLREQFIAL-------INEII 7359
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDLHErLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEheerreeLETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7360 AFIMKYTDVIIDIENSPDSLEDKINKYDDVIVKI-QECEGVLASAndkgqkiasEGNAADKNSITEQLQSLKNQLQNLRK 7438
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELeEERDDLLAEA---------GLDDADAEAVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7439 AVESQR---QKHQLQLESHKKMAAELSEILDWLHshEGAAKsrplLDRDPESVERELQKHQSLSQDIESYLNKFNKINDG 7515
Cdd:PRK02224 329 RLEECRvaaQAHNEEAESLREDADDLEERAEELR--EEAAE----LESELEEAREAVEDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7516 VKTEIGMPSSLLEMLSEGRSlvaSLPHELEEREKYLKNNRDSRLEYMQLVAKFNdwVHEAELRLQNSQH--GI-DYEHLV 7592
Cdd:PRK02224 403 APVDLGNAEDFLEELREERD---ELREREAELEATLRTARERVEEAEALLEAGK--CPECGQPVEGSPHveTIeEDRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7593 QDLDEHKIFFGNEAPIRNLVH---KQIQEAADKIWSSLNNYEQS-ELSAELAQFQTKLTNTLANAKTQQSELEKEAERWR 7668
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLeraEDLVEAEDRIERLEERREDLeELIAERRETIEEKRERAEELRERAAELEAEAEEKR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7669 E-YQQSIDRVKATIERTKFVD----------EPVQNLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIRQADARNR 7737
Cdd:PRK02224 558 EaAAEAEEEAEEAREEVAELNsklaelkeriESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKR 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7738 QLIEQ-DNAGLNRSWQDLVRS---LEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDkfrnvdptVRSRR-HLEDTKNA 7812
Cdd:PRK02224 638 ELEAEfDEARIEEAREDKERAeeyLEQVEEKLDELREERDDLQAEIGAVENELEELEE--------LRERReALENRVEA 709
|
570 580
....*....|....*....|
gi 320544542 7813 IQELREESNQLKSSHKEIEA 7832
Cdd:PRK02224 710 LEALYDEAEELESMYGDLRA 729
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
626-742 |
7.85e-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: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 626 EEQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASK 705
Cdd:cd21285 5 EAENGFDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSFLAAK 84
|
90 100 110
....*....|....*....|....*....|....*..
gi 320544542 706 RIKLVNINPADLVDGRPPVVLGLIWTIILYFQIEENS 742
Cdd:cd21285 85 GINIQGLSAEEIRNGNLKAILGLFFSLSRYKQQQQQP 121
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6421-6591 |
8.31e-07 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 54.37 E-value: 8.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6421 DYNAYHQSLQDVEKWLLQIsfQLMAHNSLFISNREQTQEQIKQHEALLVEIQKYQTNLDDLNAKGQAQIKRYESSTPAIR 6500
Cdd:cd00176 1 KLQQFLRDADELEAWLSEK--EELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6501 ptveSQLKNIQDSYNSLLQTSVQIKNRLLESLAKFQEYEDTLDsIMRNLETYEPIIQTELdaPATSLELAQNQLRCAQEM 6580
Cdd:cd00176 79 ----ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKEL 151
|
170
....*....|.
gi 320544542 6581 QNKLNNEKSRL 6591
Cdd:cd00176 152 EEELEAHEPRL 162
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
10978-11690 |
8.61e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 57.29 E-value: 8.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10978 KERKELDKEVTLAKAYFNNVQQDisreAPQNPKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSdddgi 11057
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLC----TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK----- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11058 levlalWQKIFQDTFQEYHRLSTRLARSQNSSEAL---RLWRQYLQHVQSFLSC--AIPEDYSSLREQQ----QLCAIHQ 11128
Cdd:TIGR00618 258 ------KQQLLKQLRARIEELRAQEAVLEETQERInraRKAAPLAAHIKAVTQIeqQAQRIHTELQSKMrsraKLLMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11129 NLLISQQSVLSETPLESELSEQYKALTNLHNETLSR--IMQRNGELERRVSGWnayRQQLAALLDWLRQREAERNALQlR 11206
Cdd:TIGR00618 332 AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIreISCQQHTLTQHIHTL---QQQKTTLTQKLQSLCKELDILQ-R 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11207 YIHLKRVPHLKHRldAMIQQLDQGEQQSKALQE--QQQELARHCDDALATAMRMEQASIGQRISNLRAALKTWQGFLQRV 11284
Cdd:TIGR00618 408 EQATIDTRTSAFR--DLQGQLAHAKKQQELQQRyaELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11285 TQLSESYEQRVNQLQQefgaaqklldanseslptQPAAIEQLLGSLRAQRVQLGaqvsalesltvtqeelkecISPHD-- 11362
Cdd:TIGR00618 486 TRKKAVVLARLLELQE------------------EPCPLCGSCIHPNPARQDID-------------------NPGPLtr 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11363 -MKTIRQRNWLLWQQHADLDYQLanliNSIEERLSLLSNYQIRYDRISQWLQRLEQRVEKDADVTamtnpeqaaKQLEQQ 11441
Cdd:TIGR00618 529 rMQRGEQTYAQLETSEEDVYHQL----TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL---------QNITVR 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11442 VNSELQLRDKEREWLLSTSRELLTlysepEVRSQVQQQSDSLIDRwQRLKYLAKQKATKIGELkMTLLRLEERIALIRAW 11521
Cdd:TIGR00618 596 LQDLTEKLSEAEDMLACEQHALLR-----KLQPEQDLQDVRLHLQ-QCSQELALKLTALHALQ-LTLTQERVREHALSIR 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11522 LFEVESqLDKPLNFESYTPNVIEA---KLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDADSWRT--QVNTSGLAASAQN 11596
Cdd:TIGR00618 669 VLPKEL-LASRQLALQKMQSEKEQltyWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSdlAAREDALNQSLKE 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11597 LEQRWKNVCSQSAERKARiltiwNLLQQLIKLT--AEHKNWLGKQESQIAGFERDQKShSKHKLEERQMELRAKLEELES 11674
Cdd:TIGR00618 748 LMHQARTVLKARTEAHFN-----NNEEVTAALQtgAELSHLAAEIQFFNRLREEDTHL-LKTLEAEIGQEIPSDEDILNL 821
|
730
....*....|....*..
gi 320544542 11675 QSVNLRQ-LEQIYAKLA 11690
Cdd:TIGR00618 822 QCETLVQeEEQFLSRLE 838
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
634-735 |
9.64e-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: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 634 KTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKRIKLVNIN 713
Cdd:cd21286 3 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 82
|
90 100
....*....|....*....|..
gi 320544542 714 PADLVDGRPPVVLGLIWTIILY 735
Cdd:cd21286 83 AEEIRNGNLKAILGLFFSLSRY 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
11188-11788 |
9.71e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 9.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11188 ALLDWLRQREAERNALQLRyihlkrvpHLKHRLDAMIQQLDQGEQQSKALQEQQQEL---------ARHCDDALATAMRM 11258
Cdd:COG1196 217 ELKEELKELEAELLLLKLR--------ELEAELEELEAELEELEAELEELEAELAELeaeleelrlELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11259 EQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKLLDANSESLptqpAAIEQLLGSLRAQRVQLG 11338
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL----EEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11339 AQVSALESLTVTQEELKEcisphdmktirqrnwLLWQQHADLDYQLANLINSIEERLSLLSNYQIRYDRisqwlqRLEQR 11418
Cdd:COG1196 365 EALLEAEAELAEAEEELE---------------ELAEELLEALRAAAELAAQLEELEEAEEALLERLER------LEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11419 VEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWLLSTSRELltLYSEPEVRSQVQQQSDSLIDRWQRLK------- 11491
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL--LEEAALLEAALAELLEELAEAAARLLllleaea 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11492 -YLAKQKATKIGELKMTLLRLEERIALIRAWLFEVESQLDKPLNfesytPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNL 11570
Cdd:COG1196 502 dYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA-----AALQNIVVEDDEVAAAAIEYLKAAKAGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11571 VEMLLNDADSWRTQVNTSGLAASAQNL---EQRWKNVCSQSAERKARILTIWNL-----------LQQLIKLTAEHKNWL 11636
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLvasDLREADARYYVLGDTLLGRTLVAArleaalrravtLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11637 GKQESQIAGFERDQKSHSKHKLEERQMELRAKLEELESQSVNLRQLE--QIYAKLAMSAGVEPENIQKLTLPTKVMVSMW 11714
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEeeERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320544542 11715 RQLTPRCHALLDAIDKDAKLMREFNNAQLEAtnSLNAIQKALEQL----PSAENQQtskaepKAVLQRLESLEKKLQD 11788
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELER--ELERLEREIEALgpvnLLAIEEY------EELEERYDFLSEQRED 806
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
773-877 |
1.03e-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: 51.73 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 773 EKWKQGARKTLLNWVTNALPKdsgVEVKDFGASWRDGVAFLALIDAIKANLV-NLAELKKTSNRQRLETAFDVAESKLGI 851
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*.
gi 320544542 852 AKLLDAEDVDVPKPDEKSIMTYVAQF 877
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQF 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7416-8082 |
1.07e-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: 56.99 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7416 AADKNSITEQLQSLKNQLQNLRKAVESQRQKHQlQLESHKKMAAEL-----SEILDWLHSHEGAAKSRPLLDRDPESVER 7490
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELE-ELESRLEELEEQletlrSKVAQLELQIASLNNEIERLEARLERLED 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7491 ELQKhqsLSQDIESYLNKFNKINdgvKTEIGMPSSLLEMLSEgrslvaSLPHELEEREKYLKNNRDSRLEYMQLVAKFND 7570
Cdd:TIGR02168 415 RRER---LQQEIEELLKKLEEAE---LKELQAELEELEEELE------ELQEELERLEEALEELREELEEAEQALDAAER 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7571 WVHEAELRLqnsqhgidyeHLVQDLDEHKIFFGNEapIRNLVHKQIQEAADK--IWSSLNNYEQSELSAELA---QFQTK 7645
Cdd:TIGR02168 483 ELAQLQARL----------DSLERLQENLEGFSEG--VKALLKNQSGLSGILgvLSELISVDEGYEAAIEAAlggRLQAV 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7646 LTNTLANAKTQQSELeKEAERWREYQQSIDRVKAT------IERTKFVDEPVQNLAGLHFNIQKLSHAIGNVQSQnsdLT 7719
Cdd:TIGR02168 551 VVENLNAAKKAIAFL-KQNELGRVTFLPLDSIKGTeiqgndREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGG---VL 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7720 LVN--QQAQSLIRQADARNRqLIEQDNAGLNRSW------QDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLED 7791
Cdd:TIGR02168 627 VVDdlDNALELAKKLRPGYR-IVTLDGDLVRPGGvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRK 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7792 KFRNVDPTVRSRRHLEDTKNaiQELREESNQLKSSHKEIEALSKSILTFLGEVHKPSAE--AIQAKVDKLVEQQAKLNDT 7869
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELS--RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEieELEERLEEAEEELAEAEAE 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7870 LRDKEQQVSKDLEEIEQVFRRISQLQDKLNAL----HEQLQSVHVYDEHIAQTEQLLITLNSQVQQAAEESKLLVAQtta 7945
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELTLLneeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE--- 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7946 hyQAKQNQLPSDIAQEFTALELLAERVQVTMETKEKDfkraktvRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELL 8025
Cdd:TIGR02168 861 --IEELEELIEELESELEALLNERASLEEALALLRSE-------LEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 320544542 8026 QRINHEITAIYERFT-LVKTNGQLIIENCRNSEEKtlvqttIDQLAASLAQVRGWLDE 8082
Cdd:TIGR02168 932 EGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDD------EEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10627-11393 |
1.68e-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: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10627 EKVGELFSLSHKISTqIAEELEGASVLRDQLQAIQEGISNQRKHQAKISVILDECEAAERQGADVLEKAVADCQAAGEEL 10706
Cdd:TIGR02168 285 ELQKELYALANEISR-LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10707 VISWQEIMRIRQMLHTLPMRLKMSVSpvKLERDISQLQDDHAFLESKCTNI---MAILRSRLAVWLR--YERQLELVHGS 10781
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVA--QLELQIASLNNEIERLEARLERLedrRERLQQEIEELLKklEEAELKELQAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10782 VQETDFMMELIRVHGQVDYERLRKATERLEGLAGDLHNREQLIDELKGAAKPLiescdVQIVEQIESAvQEAVVAWNDTS 10861
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL-----ERLQENLEGF-SEGVKALLKNQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10862 ENLQQLRTRYQRAVELWDKYRNASAAVKNSiDQQMDAVKSLEQPLDALQHAKvcQDNLTTQNdrILELRDIVAKIAADVG 10941
Cdd:TIGR02168 516 SGLSGILGVLSELISVDEGYEAAIEAALGG-RLQAVVVENLNAAKKAIAFLK--QNELGRVT--FLPLDSIKGTEIQGND 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10942 LDASALMQGELDALgQRLAECKDAITT-----LANVAETQDkerkeLDKEVTLAKAY---FNNVQQD---ISREAPQNPK 11010
Cdd:TIGR02168 591 REILKNIEGFLGVA-KDLVKFDPKLRKalsylLGGVLVVDD-----LDNALELAKKLrpgYRIVTLDgdlVRPGGVITGG 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11011 ESEEQLAALrAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSE 11090
Cdd:TIGR02168 665 SAKTNSSIL-ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11091 ALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLCAIHQNLLISQQSVLSE-----TPLESELSEQYKALTNLhNETLSRI 11165
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeelKALREALDELRAELTLL-NEEAANL 822
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11166 MQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHLKRVphLKHRLDAMIQQLDQGEQQSKALQEQQQELA 11245
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE--LESELEALLNERASLEEALALLRSELEELS 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11246 RHCDDALATAMRMEQASIGQRISNLRAALKtWQGFLQRVTQLSEsyeqrvnQLQQEFGAAQKLLDANSESLPTQPAAIEQ 11325
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELR-LEGLEVRIDNLQE-------RLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320544542 11326 LLGSLRAQRVQLGA-QVSALESLtvtqEELKEcisphdmktiRQRNwlLWQQHADLDYQLANLINSIEE 11393
Cdd:TIGR02168 973 RLKRLENKIKELGPvNLAAIEEY----EELKE----------RYDF--LTAQKEDLTEAKETLEEAIEE 1025
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10927-11490 |
1.77e-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: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10927 LELRDIVAKIAADVGLDAS-ALMQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREA 11005
Cdd:COG1196 222 LKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11006 pqnpKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARS 11085
Cdd:COG1196 302 ----QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11086 QnsSEALRLWRQYLQHVQsflscaipEDYSSLREQQQLCAIHQNLLISQQSVLSEtplESELSEQYKALTNLHNETLSRI 11165
Cdd:COG1196 378 E--EELEELAEELLEALR--------AAAELAAQLEELEEAEEALLERLERLEEE---LEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11166 MQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHLKRvphLKHRLDAMIQQLDQGEQQSKALQ--EQQQE 11243
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA---RLLLLLEAEADYEGFLEGVKAALllAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11244 LARHCDDALATAMRMEQAsigqrisnLRAALKTWQgfLQRVTQLSESYEQRVNQLQQEFGAAQKLLDANSESLPTQPAAI 11323
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAA--------LEAALAAAL--QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11324 EQLLGSLRAQRVQLGAQVSALESLTVTQEELKEcispHDMKTIRQRNWLLWQQHADLDY--------------QLANLIN 11389
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLG----RTLVAARLEAALRRAVTLAGRLrevtlegeggsaggSLTGGSR 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11390 SIEERLSLLSNYQIRYDRISQWLQRLEQRVEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWLLSTSRELLTLYS- 11468
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEl 747
|
570 580 590
....*....|....*....|....*....|..
gi 320544542 11469 ----------EPEVRSQVQQQSDSLIDRWQRL 11490
Cdd:COG1196 748 leeealeelpEPPDLEELERELERLEREIEAL 779
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4607-4804 |
1.77e-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: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4607 KWSGFDEIADSLKSWLDETENALpADIELKTTLDEKRNKLQTYRDILNDINNHQVELGNLQEIAANL----PEKTELVDQ 4682
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieegHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4683 IIKDISDRFGKLQKRAQNYVERYEGIVSAHQQYSKAvMDAQEFIDATLNTV-HYWGDLDLEQISLHtnLDRLKNLKASLA 4761
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALaSEDLGKDLESVEEL--LKKHKELEEELE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 320544542 4762 DEFPRVDQVRALGEKVIPGTVDVGQVNIKSQIDTTQQEWESLL 4804
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELL 199
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3641-3853 |
1.77e-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: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3641 DHESFDKDFDSFKQNLqSSVDELAKTNEIVGDQSVLQDQQNKLREMSDKRILDSTLFEGLIDRGEKLyGHTSPEGREIIR 3720
Cdd:cd00176 1 KLQQFLRDADELEAWL-SEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQL-IEEGHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3721 QQLRALRTLWDNYTDDLNSATQKIDQCLLQFNEFSIAqDQLTKWLKDVDKAMQSHtEPKTTLQEKRAQLQNHKLLHQEIT 3800
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 320544542 3801 THNVLVDNVCDKAQILVDQIKDNSLNVY---LTSIKQLFQSIVQKSDEILHNLDDC 3853
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIeekLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4071-4269 |
2.74e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 52.83 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4071 HQFYQDkYNEVDLWLQPIESQMAKVLLDEPTQSSNIL----QVLLSEKEQAESLFAALNAAGEKaLPETSTQGREKIRKD 4146
Cdd:cd00176 3 QQFLRD-ADELEAWLSEKEELLSSTDYGDDLESVEALlkkhEALEAELAAHEERVEALNELGEQ-LIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4147 LRDIRDRWDKLDEGIRNLEKRQEAQGVQLSSYQDILnQTVNWLDQVEKLIHNENPASwtSAQEIRSKLYKYKATNQDINS 4226
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK--DLESVEELLKKHKELEEELEA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 320544542 4227 HKRIVEAVNEKAAALLGSAAPANADEISKAVAEVNKRYDQVGQ 4269
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLE 200
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3904-4170 |
2.86e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3904 NKPQAMKIISDIRDLFEkvkattsekgNEVLD-KEIEELETTMKSHFDDIEGIEG------KQKDVL----AQWDKFEKA 3972
Cdd:COG4913 198 HKTQSFKPIGDLDDFVR----------EYMLEePDTFEAADALVEHFDDLERAHEaledarEQIELLepirELAERYAAA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3973 LEELTKW--CRSAEAVFREQQLQSTLHEKVEQLE----KYKIQRELILQKEKEIDAFGDAAHALLNNCGADRLKTLTTQI 4046
Cdd:COG4913 268 RERLAELeyLRAALRLWFAQRRLELLEAELEELRaelaRLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4047 TNryqlLQVLSKEVVNRWSNLvddhqfyqdkynevDLWLQPIEsqmakvlldeptqssniLQVLLSEKEqaeslFAALNA 4126
Cdd:COG4913 348 ER----LERELEERERRRARL--------------EALLAALG-----------------LPLPASAEE-----FAALRA 387
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 320544542 4127 AGeKALPETSTQGREKIRKDLRDIRDRWDKLDEGIRNLEKRQEA 4170
Cdd:COG4913 388 EA-AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
3520-4687 |
2.90e-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: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3520 EDFMTLCQDSLVKLKQLCSKWDEFDTIIEELDNWMKNVEAVVKNQNLKSTAE-AKNAHLKQLQDISKDI--------ERR 3590
Cdd:TIGR01612 751 KDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDnIKDEDAKQNYDKSKEYiktisikeDEI 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3591 GAAINELMDQGREIegetdlnlkLSRLNtRYQTLKNLCKESI-------AKYVNYVKDHESfDKDFDSFKQNLQSSVDEL 3663
Cdd:TIGR01612 831 FKIINEMKFMKDDF---------LNKVD-KFINFENNCKEKIdseheqfAELTNKIKAEIS-DDKLNDYEKKFNDSKSLI 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3664 AKTNeivgdQSVLQDQQN--KLREMSDK-RILDSTL--FEGLIDRGEKLyghtspegREIIRQQLRALR---TLWDNYTD 3735
Cdd:TIGR01612 900 NEIN-----KSIEEEYQNinTLKKVDEYiKICENTKesIEKFHNKQNIL--------KEILNKNIDTIKesnLIEKSYKD 966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3736 DL-NSATQKIDQCLLQFNEFSiaqdqLTKWLKDVDKAMQSHTEPKTTLQEKRAQLQNHKLLHQEITTHNVLvdnvcdkaQ 3814
Cdd:TIGR01612 967 KFdNTLIDKINELDKAFKDAS-----LNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFDEKEKATNDIE--------Q 1033
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3815 ILVDqIKDNSLNVYLTsikqLFQSIVQKSDEILHNLDDCVQKHNElnNALSSAKTWISN-----EKAKLLECDDaYGEKA 3889
Cdd:TIGR01612 1034 KIED-ANKNIPNIEIA----IHTSIYNIIDEIEKEIGKNIELLNK--EILEEAEINITNfneikEKLKHYNFDD-FGKEE 1105
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3890 DIKRKIETLGQLAQNKPQAMKIISDIRDLfEKVKATTSEKGNEvLDKEIEELETTMKSHF--DDIEGIEGKQKDVLAQWD 3967
Cdd:TIGR01612 1106 NIKYADEINKIKDDIKNLDQKIDHHIKAL-EEIKKKSENYIDE-IKAQINDLEDVADKAIsnDDPEEIEKKIENIVTKID 1183
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3968 KFEKALEELTKWCRSAEAVFREQqlqsTLHEKV----------------EQLEKYKIQRELILQKE----KEIDAFGDAA 4027
Cdd:TIGR01612 1184 KKKNIYDEIKKLLNEIAEIEKDK----TSLEEVkginlsygknlgklflEKIDEEKKKSEHMIKAMeayiEDLDEIKEKS 1259
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4028 HALLNNCGADRLKTLTTQITN----RYQLLQVLSKEVVNRWSNLVDDH-QFYQDKYNEVDlwLQPIESQMAKVLLDEPTQ 4102
Cdd:TIGR01612 1260 PEIENEMGIEMDIKAEMETFNishdDDKDHHIISKKHDENISDIREKSlKIIEDFSEESD--INDIKKELQKNLLDAQKH 1337
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4103 SSNILQVLlsekEQAESLFAALNAAGEKALPETSTQGREKIRKDLRDIRDRWDKLDEGIRNLEkrqeaQGVQLSSYQDIL 4182
Cdd:TIGR01612 1338 NSDINLYL----NEIANIYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIK-----DDINLEECKSKI 1408
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4183 NQTVNWLDQVEKLIHNENPASWTSAQEIRSKLY--KYKATNQDINSHKRIVEAVNEKAAALLG-------SAAPANADEI 4253
Cdd:TIGR01612 1409 ESTLDDKDIDECIKKIKELKNHILSEESNIDTYfkNADENNENVLLLFKNIEMADNKSQHILKikkdnatNDHDFNINEL 1488
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4254 SKAVAEVNKRYDQVGQDcAKLVADLDGAFDVYQQ--------FSELQ-KAQQDYQKNLWDRLTGYSDYSGNKAALQARL- 4323
Cdd:TIGR01612 1489 KEHIDKSKGCKDEADKN-AKAIEKNKELFEQYKKdvtellnkYSALAiKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKs 1567
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4324 -QKINEIqdalpegvaklKSLEDHIEQQASNIPARSKEVMarDLANLHADFEKFGASLSDVKSGLENRLQQWNDYEINLD 4402
Cdd:TIGR01612 1568 eQKIKEI-----------KKEKFRIEDDAAKNDKSNKAAI--DIQLSLENFENKFLKISDIKKKINDCLKETESIEKKIS 1634
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4403 RL--------ITWLGEAENSLKNY-----NLKSSFEEKEEQLNGFQSlaqNLRQNEADFDKVKDDTS-ELVQSSGETRIA 4468
Cdd:TIGR01612 1635 SFsidsqdteLKENGDNLNSLQEFleslkDQKKNIEDKKKELDELDS---EIEKIEIDVDQHKKNYEiGIIEKIKEIAIA 1711
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4469 vNVQQVSSRFQSIQATAKEILKKC-----------EQAVQDHGHFNDKYKQCADwLANAQARYddccdLSTVAsrddllK 4537
Cdd:TIGR01612 1712 -NKEEIESIKELIEPTIENLISSFntndlegidpnEKLEEYNTEIGDIYEEFIE-LYNIIAGC-----LETVS------K 1778
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4538 KQVVIQELLAQQPTATQLLNSTVELGEKCygstategreaiRSQLDDLT---FDQL-------FDNIAITARKIQDKIAK 4607
Cdd:TIGR01612 1779 EPITYDEIKNTRINAQNEFLKIIEIEKKS------------KSYLDDIEakeFDRIinhfkkkLDHVNDKFTKEYSKINE 1846
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4608 wsGFDEIADSLKSWLDETENALPADIeLKTTLDEKRN----KLQTYRDILNDINNHQVELGNLQEIAANLPEKTELVDQI 4683
Cdd:TIGR01612 1847 --GFDDISKSIENVKNSTDENLLFDI-LNKTKDAYAGiigkKYYSYKDEAEKIFINISKLANSINIQIQNNSGIDLFDNI 1923
|
....
gi 320544542 4684 IKDI 4687
Cdd:TIGR01612 1924 NIAI 1927
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
627-733 |
5.24e-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: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 627 EQERVQKKTFTNWINSyllKRVPPlRIDDLINDLRDGTKLIALLEVLsgeRLPVEKGRVLRRPH--------FLSNANTA 698
Cdd:cd21331 18 EGETREERTFRNWMNS---LGVNP-HVNHLYGDLQDALVILQLYEKI---KVPVDWNKVNKPPYpklganmkKLENCNYA 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 320544542 699 LQFLASK-RIKLVNINPADLVDGRPPVVLGLIWTII 733
Cdd:cd21331 91 VELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLM 126
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
627-733 |
5.69e-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: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 627 EQERVQkktFTNWINSYLL------KRVP-PLRIDDLINDLRDGTKLIALL----------EVLSgerLPVEKGRVLRRP 689
Cdd:cd21294 5 EDERRE---FTKHINAVLAgdpdvgSRLPfPTDTFQLFDECKDGLVLSKLIndsvpdtideRVLN---KPPRKNKPLNNF 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 320544542 690 HFLSNANTALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTII 733
Cdd:cd21294 79 QMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
7424-8039 |
7.25e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7424 EQLQSLKNQLQNLRKAVESQRQKHQLQLES------HKKMAAELSEILDWLHSHEGAAKSRPLLDRDpesvERELQKHQS 7497
Cdd:TIGR00618 270 EELRAQEAVLEETQERINRARKAAPLAAHIkavtqiEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ----QSSIEEQRR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7498 LSQDIESYLNKFNKINDgvkteigMPSSLLEMLSEgrslvaslPHELEEREKYLKNNRDSRLEYMQLVAKFNDwvheael 7577
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAHE-------VATSIREISCQ--------QHTLTQHIHTLQQQKTTLTQKLQSLCKELD------- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7578 RLQNSQHGIDYEHLVQ-DLDEHKIFFGNEAPIRNLVHKQIQEAADKIWSSLN------NYEQSELSAELAQFQTKLTNTL 7650
Cdd:TIGR00618 404 ILQREQATIDTRTSAFrDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKlekihlQESAQSLKEREQQLQTKEQIHL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7651 ANAKTQQSE---LEKEAERWREYQQSIDRVKATIERTKFVDEPVQNLAGLHFNIQKLSHAIGNVQSQnsdLTLVNQQAQS 7727
Cdd:TIGR00618 484 QETRKKAVVlarLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQ---LTSERKQRAS 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7728 LIRQAdarnrQLIEQDNAGLNRSWQDLVRSLeqrrDNLQQLAEhwdgfenSLHAWEKALGRLEDKFRnvdptVRSRRHLE 7807
Cdd:TIGR00618 561 LKEQM-----QEIQQSFSILTQCDNRSKEDI----PNLQNITV-------RLQDLTEKLSEAEDMLA-----CEQHALLR 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7808 DTKNAIQELR---EESNQLKSSHKEIEALSKSILTFLGEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEI 7884
Cdd:TIGR00618 620 KLQPEQDLQDvrlHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7885 EQvfrrisqlqdKLNALHEQLQSVHVYDEHIAQTEQLLITLNSQVQQ------------AAEESKLLVAQTTAHYQAKQn 7952
Cdd:TIGR00618 700 AQ----------CQTLLRELETHIEEYDREFNEIENASSSLGSDLAAredalnqslkelMHQARTVLKARTEAHFNNNE- 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7953 QLPSDIaQEFTALELLAERVQVTMETKEKDFKRAKTVRTEYVDGVDE-VQRWLLQAEVQVQERSLTPTQMKELLQRInHE 8031
Cdd:TIGR00618 769 EVTAAL-QTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdEDILNLQCETLVQEEEQFLSRLEEKSATL-GE 846
|
....*...
gi 320544542 8032 ITAIYERF 8039
Cdd:TIGR00618 847 ITHQLLKY 854
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5554-6043 |
7.95e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5554 DKYENLTKQAKDLYEKQKNTIESYQSLIDAGNEFATWLRNAKERlskcseptgdkqaLAEKTHQLKILQGELPEGAQKLK 5633
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKE-------------LEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5634 NAleqgeiacrSAEPEDCEIIEQEVALLQEEfdayREALNKAKDYLEVGIVKWSDYQDQYTEALEWLSKTEALVQSYNKL 5713
Cdd:PRK03918 225 KL---------EKEVKELEELKEEIEELEKE----LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5714 QDSLIQKKVVLEQFqghLQTLFDWQKTLDDLNMKAQVLLETCSDtrisnaIMQLTTKYNALLTLAKEVMRRLEmhyqEHQ 5793
Cdd:PRK03918 292 AEEYIKLSEFYEEY---LDELREIEKRLSRLEEEINGIEERIKE------LEEKEERLEELKKKLKELEKRLE----ELE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5794 QHHSLYEECQSW---------------IEKTREKLSECE----QIPGTLNEVQIKLNTVKNLRQGFETGQNKL------- 5847
Cdd:PRK03918 359 ERHELYEEAKAKkeelerlkkrltgltPEKLEKELEELEkakeEIEEEISKITARIGELKKEIKELKKAIEELkkakgkc 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5848 ----RYLLELKEKVIMNTEQNGAAKIQEDtealKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILiEWLEDVEPSVK 5923
Cdd:PRK03918 439 pvcgRELTEEHRKELLEEYTAELKRIEKE----LKEIEEKERKLRKELRELEKVLKKESELIKLKELA-EQLKELEEKLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5924 TSDefLNDLSEK----RAALEKFRVIQRDINGHNDIVEKINQRLKEDNSLD--LKDFQPGLTKF-DDLQTQVNKIIESLE 5996
Cdd:PRK03918 514 KYN--LEELEKKaeeyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEkkLDELEEELAELlKELEELGFESVEELE 591
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 320544542 5997 NQVNSHEKYKQAYNELQDWLRRTRIEVEQCADCHGEKDQVESRLNRL 6043
Cdd:PRK03918 592 ERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAET 638
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7666-7876 |
9.71e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 51.29 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7666 RWREYQQSIDRVKATIERTKFV---DEPVQNLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIrQADARNRQLIEQ 7742
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELlssTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7743 DNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFeNSLHAWEKALGRLEDKFRNVDPTvrsrRHLEDTKNAIQELREESNQ 7822
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALASEDLG----KDLESVEELLKKHKELEEE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 320544542 7823 LKSSHKEIEALSKSILTFLGEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQ 7876
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKK 208
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
11143-11818 |
1.10e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11143 LESELSEQYKALTNLHnETLSRIMQRNGELERRVSgWNAYRQQLAALLDWLRQREAE----RNALQLRYIHLKRVPHLKH 11218
Cdd:TIGR00618 224 LEKELKHLREALQQTQ-QSHAYLTQKREAQEEQLK-KQQLLKQLRARIEELRAQEAVleetQERINRARKAAPLAAHIKA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11219 rldamIQQLDQGEQQSKA-LQEQQQELARhcddalATAMRMEQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQ 11297
Cdd:TIGR00618 302 -----VTQIEQQAQRIHTeLQSKMRSRAK------LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11298 LQQEFGAAQKLLdanseSLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELK-ECISPHDMKTIRQRNWLLWQQ 11376
Cdd:TIGR00618 371 SCQQHTLTQHIH-----TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQgQLAHAKKQQELQQRYAELCAA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11377 HADLDYQLANLINSIEERLSllsnyqirydrisqwlQRLEQRVEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWL 11456
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESA----------------QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGS 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11457 LSTSRELLTLYSEPEVRSQVQQQsdsLIDRWQRLKYLAKQKATKIGELKMTLLRLEERIALIRAWLF-------EVESQL 11529
Cdd:TIGR00618 510 CIHPNPARQDIDNPGPLTRRMQR---GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSiltqcdnRSKEDI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11530 DKPLNFESYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDAD-SWRTQVNTSGLAASAQNLEQ-----RWKN 11603
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQcSQELALKLTALHALQLTLTQervreHALS 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11604 VCSQSAERKARILTIWNLLQQLIKLTAEHKNWLGKQESQIAGFERDQKSHSKHkLEERQMELRAKLEELESQSVNLRQLE 11683
Cdd:TIGR00618 667 IRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE-FNEIENASSSLGSDLAAREDALNQSL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11684 QIYAKLAMSAGVEPENIQKLTLPTKVMVSMwrqltprchalLDAIDKDAKLMREFNNAQLEATNSLNAIQKAL--EQLPS 11761
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFNNNEEVTAALQ-----------TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEigQEIPS 814
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 320544542 11762 AE-----NQQTSKAEPKAVLQRLESLEKKLQDAQQHVQQADNLAQEAKTRTKQQPQLKQLLE 11818
Cdd:TIGR00618 815 DEdilnlQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
10791-11356 |
1.33e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10791 LIRVHGQVDYERLRKATERLEGLAGDLHNREQLIDEL----------KGAAKPLIESCD--VQIVEQIESAV---QEAVV 10855
Cdd:PRK02224 189 LDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYeeqreqaretRDEADEVLEEHEerREELETLEAEIedlRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10856 AWNDTSENL-QQLRTRYQRAVELWDKYRNASA------AVKNSIDQQMDAV-KSLEQPLDALQHAKVCQDNLTTQNDRIL 10927
Cdd:PRK02224 269 ETEREREELaEEVRDLRERLEELEEERDDLLAeaglddADAEAVEARREELeDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10928 ELRDIVAKIAADvgldasalMQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQqDISREAPQ 11007
Cdd:PRK02224 349 EDADDLEERAEE--------LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE-DFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11008 NPKESEEQLAALRAHLQTLARTEEQLRQLKER------HQNSEVAPSVASSDDDGilEVLALWQKIFQDTFQEYHRLSTR 11081
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEALLEAgkcpecGQPVEGSPHVETIEEDR--ERVEELEAELEDLEEEVEEVEER 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11082 LARSQNSSEALRlwrqylqhvqsflscaipeDYSSLREQ----QQLCAIHQNLLISQQSVLSE-----TPLESELSEQYK 11152
Cdd:PRK02224 498 LERAEDLVEAED-------------------RIERLEERredlEELIAERRETIEEKRERAEElreraAELEAEAEEKRE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11153 ALTNLHNETlSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQlryihlkrvpHLKHRLDAMIQQLDQGEQ 11232
Cdd:PRK02224 559 AAAEAEEEA-EEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIE----------RLREKREALAELNDERRE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11233 QSKALQEQQQELARHCDDAlatamrmeqasigqRISNLRAALKTWQGFLQRVT-QLSESYEQRvNQLQQEFGAAQKLLDA 11311
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEA--------------RIEEAREDKERAEEYLEQVEeKLDELREER-DDLQAEIGAVENELEE 692
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 320544542 11312 nseslptqpaaieqlLGSLRAQRVQLGAQVSALESLTVTQEELKE 11356
Cdd:PRK02224 693 ---------------LEELRERREALENRVEALEALYDEAEELES 722
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
11401-11614 |
1.34e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 50.91 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11401 YQIRYDRISQWLQRLEQRVEKDADVTAMTNPEQAAKQLeQQVNSELQLRDKEREWLLSTSRELLTLYSEPEvrSQVQQQS 11480
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKH-EALEAELAAHEERVEALNELGEQLIEEGHPDA--EEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11481 DSLIDRWQRLKYLAKQKATKIGELKMTLLRLEErIALIRAWLFEVESQLDKPLNFESYTPnvIEAKLKEHEQIQRSIEHH 11560
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLES--VEELLKKHKELEEELEAH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 320544542 11561 SSNVGEVLNLVEMLLNDAdswrTQVNTSGLAASAQNLEQRWKNVCSQSAERKAR 11614
Cdd:cd00176 159 EPRLKSLNELAEELLEEG----HPDADEEIEEKLEELNERWEELLELAEERQKK 208
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
11508-11717 |
1.57e-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: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11508 LLRLEERIALIRAWLFEVESQLDKPLNfeSYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDAdswrtQVNT 11587
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDY--GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-----HPDA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11588 SGLAASAQNLEQRWKNVCSQSAERKARILTIWNLLQQLIKLTAEhKNWLGKQESQIAgfeRDQKSHSKHKLEERQMELRA 11667
Cdd:cd00176 75 EEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL-EQWLEEKEAALA---SEDLGKDLESVEELLKKHKE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 320544542 11668 KLEELESQSVNLRQLEQIYAKLAMSAgvEPENIQKLTLPTKVMVSMWRQL 11717
Cdd:cd00176 151 LEEELEAHEPRLKSLNELAEELLEEG--HPDADEEIEEKLEELNERWEEL 198
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
625-739 |
1.82e-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: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 625 REEQERvqkkTFTNWINSYL-----LKRVPPLR--IDDLINDLRDGTKLIALLEVLS----GERLPVEKGRVLRRPHflS 693
Cdd:cd21292 22 SEEEKV----AFVNWINKNLgddpdCKHLLPMDpnTDDLFEKVKDGILLCKMINLSVpdtiDERAINKKKLTVFTIH--E 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 320544542 694 NANTALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTII---LYFQIE 739
Cdd:cd21292 96 NLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIrigLFADIE 144
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6111-6318 |
1.88e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 50.14 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6111 WQTFLQKFNKINLWIETMNKRVTKSQegenkTPEDLVNAKKLLE-------EVLAEKDNVEDLNDNCELLMEQS--ACTR 6181
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTD-----YGDDLESVEALLKkhealeaELAAHEERVEALNELGEQLIEEGhpDAEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6182 IRDQTIETQANYTKLLTSAQGLVAKIEKNLSDHtEFLNYKKEMDAWIEKAQQVLDDCSTDGDAAIIAQKLDTVNSLASRL 6261
Cdd:cd00176 77 IQERLEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 320544542 6262 PEGQHLLALVQDAYSKASNITPEDKQEKLRELMTKVREDWDALGLAVKQKLSDLKQA 6318
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
10892-11356 |
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 320544542 10892 IDQQMDAVKSLEQPLDALQHAkvcQDNLTTQNDRILELRDIVAKIAADVGLDASALMQGELDALGQRLAECKDAITTLAN 10971
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAEL---QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10972 VAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVAS 11051
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11052 SDDDGILEVLALWQKIfQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLCAihqnll 11131
Cdd:COG4717 230 EQLENELEAAALEERL-KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK------ 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11132 isqqsvlsetplESELSEQYKALTNLHNETLSRIMQRNG-ELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHL 11210
Cdd:COG4717 303 ------------EAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11211 KRVPHLKH-------RLDAMIQQLDQGEQQSKALQEQQQELARHCDDALATAMRMEQASIGQRISNLRAALktwqgflqr 11283
Cdd:COG4717 371 EIAALLAEagvedeeELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEEL--------- 441
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320544542 11284 vtqlsESYEQRVNQLQQEFGAAQKLLDA--NSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELKE 11356
Cdd:COG4717 442 -----EELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3719-4505 |
2.46e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3719 IRQQLRALRtlWDNYTDDLNSATQKIDQCLLQFNEfsiaqdqltkwlkdvdkAMQSHTEPKTTLQEKRAQLQNHKLLHQE 3798
Cdd:TIGR02168 218 LKAELRELE--LALLVLRLEELREELEELQEELKE-----------------AEEELEELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3799 I-TTHNVLVDNVCDKAQILvdQIKDNSLNVYLTSIKQLFQSIVQKSDEILHNLddcvQKHNELNNALSSAKTWISNEKAK 3877
Cdd:TIGR02168 279 LeEEIEELQKELYALANEI--SRLEQQKQILRERLANLERQLEELEAQLEELE----SKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3878 LLECDDAYGEKADIKRKIETLGQLAQNKPQAMKiiSDIRDLFEKVkattsekgnEVLDKEIEELETTmkshfddIEGIEG 3957
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLR--SKVAQLELQI---------ASLNNEIERLEAR-------LERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3958 KQKDVLAQWDKFEKALEELTKWCRSAEAVFREQQLQSTLHEKVEQLEKYKIQRELILQKEKEIDAFGDAAHALLNncgad 4037
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA----- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4038 RLKTLTTqITNRYQLLQVLSKEVVNRWSNLVDDHQFYQDKYnEVDlwlQPIESQMAKVLldeptqSSNILQVLLSEKEQA 4117
Cdd:TIGR02168 490 RLDSLER-LQENLEGFSEGVKALLKNQSGLSGILGVLSELI-SVD---EGYEAAIEAAL------GGRLQAVVVENLNAA 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4118 ESLFAAL--NAAGEKALPETSTQGREKIRKDLRDIRDRWDKLDEGIRNLEKRQEAqgvqlssYQDILNqtvNWLDQVekL 4195
Cdd:TIGR02168 559 KKAIAFLkqNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK-------LRKALS---YLLGGV--L 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4196 IHNenpaSWTSAQEIRSKL-YKYKATNQD---INSHKRIVEAVNEKAAALLG------------SAAPANADEISKAVAE 4259
Cdd:TIGR02168 627 VVD----DLDNALELAKKLrPGYRIVTLDgdlVRPGGVITGGSAKTNSSILErrreieeleekiEELEEKIAELEKALAE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4260 VNKRYDQVGQDCAKLVADLDgafDVYQQFSELQKaqqDYQKNLWDRLTGYSDYSGNKAALQARLQKINEIQDALPEGVAK 4339
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELE---ELSRQISALRK---DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4340 LKSLEDHIEQQASNIparskEVMARDLANLHADFEKFGASLSDVKSGLENRLQQWNDYEINLDRLITWLGEAENSLknyn 4419
Cdd:TIGR02168 777 LAEAEAEIEELEAQI-----EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI---- 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4420 lkssfEEKEEQLngfQSLAQNLRQNEADFDKVKDDTSELVQSSGEtrIAVNVQQVSSRFQSIQATAKEILKKCEQAVQDH 4499
Cdd:TIGR02168 848 -----EELSEDI---ESLAAEIEELEELIEELESELEALLNERAS--LEEALALLRSELEELSEELRELESKRSELRREL 917
|
....*.
gi 320544542 4500 GHFNDK 4505
Cdd:TIGR02168 918 EELREK 923
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7460-7663 |
2.53e-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: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7460 ELSEILDWLHSHEGAAKSrPLLDRDPESVERELQKHQSLSQDIESYLNKFNKINDG----VKTEIGMPSSLLEMLSEGRS 7535
Cdd:cd00176 8 DADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELgeqlIEEGHPDAEEIQERLEELNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7536 LVASLPHELEEREKYLKNNRDsRLEYMQLVAKFNDWVHEAELRLQNSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLVhKQ 7615
Cdd:cd00176 87 RWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRL-KS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 320544542 7616 IQEAADKIWSSLNNYEQSELSAELAQFQTKLTNTLANAKTQQSELEKE 7663
Cdd:cd00176 165 LNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7992-8195 |
2.53e-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: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7992 EYVDGVDEVQRWLLQAEVQVQERSL--TPTQMKELLQR---INHEITAIYERFTLVKTNGQLIIEncRNSEEKTLVQTTI 8066
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYgdDLESVEALLKKheaLEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8067 DQLAASLAQVRGWLDEKKQAVGDSLDAWtRFMNLYQIVMSWASEKRNFIDQTIELRTLPEARNKLN---DYVTSVKSIKP 8143
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKkhkELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 320544542 8144 IVKHLSEMDKELEHIGQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEA 8195
Cdd:cd00176 161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2144-2355 |
2.57e-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: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2144 WQQFQAGLQQIKPAVEQSEVKVNNVVSkPISLEEAVAMQQNAQQFETQCQEQLDKLHGISNISHKmLCKTNAPD------ 2217
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQ-LIEEGHPDaeeiqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2218 ELDAMHSRWTAVHENAKQASAKLEKLVANWKsFDADAAKLEDWVGQGEQQMSRRPavlNTPHIDKLEKELVKLKSFNNEI 2297
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASED---LGKDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 320544542 2298 SQQQAKLVTLGQNADQISLHLAPEGAAALKDRVNQMKGKLQKLSEATRGHINEVSDAI 2355
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2280-3685 |
3.54e-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: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2280 IDKLEKELVK-LKSFNNEISQQQAKLVTlgqNADQISLHL--------APEGAAALKDRVNQMKGKLQKLSEATRGHINE 2350
Cdd:TIGR01612 1057 IDEIEKEIGKnIELLNKEILEEAEINIT---NFNEIKEKLkhynfddfGKEENIKYADEINKIKDDIKNLDQKIDHHIKA 1133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2351 VSDaiISRQDfnaklvnfSNWMEQLRNQVTQVEEI--------NPERVETSLHVIHALLqehaDKKPSfnaIYDEVKQL- 2421
Cdd:TIGR01612 1134 LEE--IKKKS--------ENYIDEIKAQINDLEDVadkaisndDPEEIEKKIENIVTKI----DKKKN---IYDEIKKLl 1196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2422 -ALGATPEESNALNDAYTALVVNYQNLETNMLQ------KKA-----ALEKWTELL--------------GWKNDTESHL 2475
Cdd:TIGR01612 1197 nEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEkideekKKSehmikAMEAYIEDLdeikekspeienemGIEMDIKAEM 1276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2476 NYLK--HQLDKPEGPAAEELSKVIDEIDN----LGQGIgYWKGQAKEIDENPAIQLRDALSRRPLIaTQIVNDVENKLEN 2549
Cdd:TIGR01612 1277 ETFNisHDDDKDHHIISKKHDENISDIREkslkIIEDF-SEESDINDIKKELQKNLLDAQKHNSDI-NLYLNEIANIYNI 1354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2550 LKLRSQSQQQQIQqmtvrKDKFHALEHNFGQALQE--NRAKLDEILRQHPTLNNIDQIIADLV---ALNDALKYQADLKN 2624
Cdd:TIGR01612 1355 LKLNKIKKIIDEV-----KEYTKEIEENNKNIKDEldKSEKLIKKIKDDINLEECKSKIESTLddkDIDECIKKIKELKN 1429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2625 RI----------------HDEGSLLMREDIASMPAIQESLLIMDKN-----YDSLQNEIADRIQKYNlisqalrEYADSK 2683
Cdd:TIGR01612 1430 HIlseesnidtyfknadeNNENVLLLFKNIEMADNKSQHILKIKKDnatndHDFNINELKEHIDKSK-------GCKDEA 1502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2684 DKFSKELKKAEDLY--------------------NAIPQQPRDET-------ELHQA----SEKTRKTMEQLRKSKLSLD 2732
Cdd:TIGR01612 1503 DKNAKAIEKNKELFeqykkdvtellnkysalaikNKFAKTKKDSEiiikeikDAHKKfileAEKSEQKIKEIKKEKFRIE 1582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2733 ELERRGNNVGKlfSAIGEPIPQEvPQEVTAAKqhwqdLHD-KTAKNAHVYETEAV--------IWSQIEDAKK--DLLPW 2801
Cdd:TIGR01612 1583 DDAAKNDKSNK--AAIDIQLSLE-NFENKFLK-----ISDiKKKINDCLKETESIekkissfsIDSQDTELKEngDNLNS 1654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2802 LSETNQGLCDAADNsieIEFGPMRLSKYRTELPSYQALKDS--------IVEKTNDLVKINKGaEIPALSALNKLLSEQF 2873
Cdd:TIGR01612 1655 LQEFLESLKDQKKN---IEDKKKELDELDSEIEKIEIDVDQhkknyeigIIEKIKEIAIANKE-EIESIKELIEPTIENL 1730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2874 AEVNNNAD--------RLSAITTSFNDQEQELRRRSKEAGERVSKLREQLIKCDDMSGD----NNKIMERLQQCRALRGE 2941
Cdd:TIGR01612 1731 ISSFNTNDlegidpneKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITYDEIKNTrinaQNEFLKIIEIEKKSKSY 1810
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2942 LDN-SGNEIDNI----KQKVDELRNLYpTFSESIIPKELNNVQKRYENVDLYAKkiESSLLQFLKKFHADKVGMLKRIIA 3016
Cdd:TIGR01612 1811 LDDiEAKEFDRIinhfKKKLDHVNDKF-TKEYSKINEGFDDISKSIENVKNSTD--ENLLFDILNKTKDAYAGIIGKKYY 1887
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3017 TQREKVAWCQPESSSDKYNLDVKKSSlqevSKSIDDCKARHAETLKSL-----EMLKAVESPQNLAEL-----TSDAELL 3086
Cdd:TIGR01612 1888 SYKDEAEKIFINISKLANSINIQIQN----NSGIDLFDNINIAILSSLdsekeDTLKFIPSPEKEPEIytkirDSYDTLL 1963
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3087 R--KDMQALQDSFDQIKGILDENVDLWSQYEQSNEqisnwLRDVEGRVKAETSSQVN-LSEVPQKLQELSILQQDVLAHE 3163
Cdd:TIGR01612 1964 DifKKSQDLHKKEQDTLNIIFENQQLYEKIQASNE-----LKDTLSDLKYKKEKILNdVKLLLHKFDELNKLSCDSQNYD 2038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3164 PIinnLEQTSQQLI-------EKNPEARIGQF-VTHLVQRYQAVSKALTSYIDKIRGAQLSNANFAKaAKDFNEWFGDAK 3235
Cdd:TIGR01612 2039 TI---LELSKQDKIkekidnyEKEKEKFGIDFdVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDFSE-EKDNIIQSKKKL 2114
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3236 IEFQELARMGSPGSSSATAQQLQTVKNYIKTfdNGQILLNNAVDIGEALYPVVSpDNRERIRADLRQMREKFDYLRDEAN 3315
Cdd:TIGR01612 2115 KELTEAFNTEIKIIEDKIIEKNDLIDKLIEM--RKECLLFSYATLVETLKSKVI-NHSEFITSAAKFSKDFFEFIEDISD 2191
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3316 AFMQQVEGVliqktsieesytQVSHYLNESKAKVPT-----TDELYPTLATKKAALQ--NYKTQLQEITLHKNALKQLHD 3388
Cdd:TIGR01612 2192 SLNDDIDAL------------QIKYNLNQTKKHMISiladaTKDHNNLIEKEKEATKiiNNLTELFTIDFNNADADILHN 2259
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3389 KAVTLCDDESE-RKTDESIQE-------------------YNTLSKKIsDRITTVGNHVVKHEAYDqvLEKAQDWLNTIK 3448
Cdd:TIGR01612 2260 NKIQIIYFNSElHKSIESIKKlykkinafkllnishinekYFDISKEF-DNIIQLQKHKLTENLND--LKEIDQYISDKK 2336
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3449 SEAIDILNETT-FEKEGAEEkllVVENLLQHKPEGDSIFDTCHKLLETVLTQTHPsghpalLKGFEEPKQSWEDFMTLCQ 3527
Cdd:TIGR01612 2337 NIFLHALNENTnFNFNALKE---IYDDIINRENKADEIENINNKENENIMQYIDT------ITKLTEKIQDILIFVTTYE 2407
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3528 DSLVKLKQLCSKWDEFDtIIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINELMDQGREIEGE 3607
Cdd:TIGR01612 2408 NDNNIIKQHIQDNDEND-VSKIKDNLKKTIQSFQEILNKIDEIKAQFYGGNNINNIIITISQNANDVKNHFSKDLTIENE 2486
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3608 tdlnlkLSRLNTRYQTLKNLC----KESIAKYVNYVKDHesFDKDFDSFKQNlqSSVDELAKTNEIvgdQSVLQDQQNKL 3683
Cdd:TIGR01612 2487 ------LIQIQKRLEDIKNAAheirSEQITKYTNAIHNH--IEEQFKKIENN--SNKDEVYKINEI---DNIIEKIINYN 2553
|
..
gi 320544542 3684 RE 3685
Cdd:TIGR01612 2554 KE 2555
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1406-1604 |
3.69e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 49.37 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 1406 KEIHQWLSEAEQLLGTHNLSGGRDAINEQLHKHKTYfsrtvyYRSMLESKNKV--FQNLLKAVSSDDKIDTAPASQQMQQ 1483
Cdd:cd00176 10 DELEAWLSEKEELLSSTDYGDDLESVEALLKKHEAL------EAELAAHEERVeaLNELGEQLIEEGHPDAEEIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 1484 LNERFNYVIQNAQQWEQRLDSAAGGWSNFKDnERVVSEWLTQAESMLV-EKHIESKTTIETQKYFFEQV------NDRWM 1556
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALAsEDLGKDLESVEELLKKHKELeeeleaHEPRL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 320544542 1557 NDLVQSAQQLLTTLPAQEQPAVVHSVEQLQSRWKNVLSQAPLHLLKLE 1604
Cdd:cd00176 163 KSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
7812-8038 |
4.12e-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: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7812 AIQELREESNQLKSSHKEIEALSKSIltflgEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRI 7891
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKEL-----AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7892 SQLQDKLNALHEQLQSVHVYDEHIAQTEQLLITLNSQ-VQQAAEESKLLvaqttAHYQAKQNQLPSDIAQEFTALELLAE 7970
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEdFLDAVRRLQYL-----KYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320544542 7971 RVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELLQRINHEITAIYER 8038
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7783-8521 |
4.20e-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: 51.61 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7783 EKALGRLEDKFRNVDptvRSRRHLEDTKNAIQELREESNQ------LKSSHKEIEA--LSKSIltflgEVHKPSAEAIQA 7854
Cdd:TIGR02169 173 EKALEELEEVEENIE---RLDLIIDEKRQQLERLRREREKaeryqaLLKEKREYEGyeLLKEK-----EALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7855 KVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQL-QDKLNALHEQLQSVHVydeHIAQTEQLLITLNSQVQQAA 7933
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEA---EIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7934 EESKLLVAQTTAhYQAKQNQLPSDIAQEFTALELLAERVQVTMETKEKDFKRAKTVRTEY---VDGVDEVQRWLLQAEVQ 8010
Cdd:TIGR02169 322 ERLAKLEAEIDK-LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFaetRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8011 VQERSLTPTQMKELLQRINHEITAIYERFTLVKtngqliiencrnsEEKTLVQTTIDQLAASLAQVRGWLDEKKQAVGDS 8090
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIE-------------AKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8091 LDAWTRFMNLYQIVMSWASEKRnfidqtielRTLPEARNKLNDYVTSVKSIKPIVKHLSEMDKELehIGQVTTVGDLKDK 8170
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQ---------RELAEAEAQARASEERVRGGRAVEEVLKASIQGV--HGTVAQLGSVGER 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8171 LQEAEDAKIS--VEAVLLERNSLLQEACEEWDQCE---------RKIKDIRSWHEKTKQG--------LDSSQQQKKP-- 8229
Cdd:TIGR02169 537 YATAIEVAAGnrLNNVVVEDDAVAKEAIELLKRRKagratflplNKMRDERRDLSILSEDgvigfavdLVEFDPKYEPaf 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8230 ---LRDQLGFCEKTLA-DINVQKTKLRLSIEKLEVH------FRNGMGGDPRLSENVDDLVRVLDGLGELVKAKSqSLEQ 8299
Cdd:TIGR02169 617 kyvFGDTLVVEDIEAArRLMGKYRMVTLEGELFEKSgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELS-SLQS 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8300 TLAQIdvyQQQMQSLRQRIIQEEQQLRLVMAPTYLPHDRERALAEQQDLITQELDELLQSLSSVEDGIANMNQ--SSLDG 8377
Cdd:TIGR02169 696 ELRRI---ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAriEELEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8378 MLHGLKLIQSNLEVHERDAI--ELKNQAKKLPTD--------PATERLLNDtVDRIDLLLRRTQQGITMIANAMHGQKK- 8446
Cdd:TIGR02169 773 DLHKLEEALNDLEARLSHSRipEIQAELSKLEEEvsriearlREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKs 851
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320544542 8447 RQQEIDEYQQHLLELEQWIIEVSAELASFEptsDSSTDeqvLKSQVERSQQLLRTLKDRQQSMEDLVEQTRQLQS 8521
Cdd:TIGR02169 852 IEKEIENLNGKKEELEEELEELEAALRDLE---SRLGD---LKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
6870-7090 |
4.48e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6870 KIQELKGKAAQVAEVISNLDGQ--QVEEQMKSLDRRFADLGKRIDRKSQLLDVtnkgvEGAKGEIDQLQnwvkQQIEELQ 6947
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERleALEAELDALQERREALQRLAEYSWDEIDV-----ASAEREIAELE----AELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6948 ApkplgyTPKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELEpveysQLESALRNLNTENRNLSGVLKAELDRA 7027
Cdd:COG4913 682 A------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELE-----QAEEELDELQDRLEAAEDLARLELRAL 750
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320544542 7028 LEASKARKSLENDLDKARQWLKTKISEVRKLPVYHpltSAEIEKKIQE-NRKYDDDAKQFNDSV 7090
Cdd:COG4913 751 LEERFAAALGDAVERELRENLEERIDALRARLNRA---EEELERAMRAfNREWPAETADLDADL 811
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7401-8371 |
4.81e-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: 51.21 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7401 ASANDKGQKIASEGNAADKNSITEQLQSLKNQLQNLRKAV-ESQRQKHQLQLESHKKmAAELSEILDWLHShegaaksrp 7479
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALLVLRLEELREELEELQEELkEAEEELEELTAELQEL-EEKLEELRLEVSE--------- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7480 lLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEIGMPSSLLEMLSEGRSLVASLPHELEEREKYLKNNRDSRL 7559
Cdd:TIGR02168 279 -LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7560 EymqLVAKFNDWVHEAELRLQNSQhgidyehlvqdldehkiffgneapirnlvhKQIQEAADKIwsslnnyeqselsAEL 7639
Cdd:TIGR02168 358 A---ELEELEAELEELESRLEELE------------------------------EQLETLRSKV-------------AQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7640 AQFQTKLTNTLANAKTQQSELEKEAERWREYQQSIDRVKATiertkfvdepvQNLAGLHFNIQKLSHAIGNVQSQNSDLt 7719
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE-----------AELKELQAELEELEEELEELQEELERL- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7720 lvnQQAQSLIRQADARNRQLIEQDNAGLNRSwQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFrNVDpt 7799
Cdd:TIGR02168 460 ---EEALEELREELEEAEQALDAAERELAQL-QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI-SVD-- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7800 vrsrrhlEDTKNAIQELREESNQ------LKSSHKEIEALSKSIL---TFLgEVHKPSAEAIQAKVDKLVEQQaklndtl 7870
Cdd:TIGR02168 533 -------EGYEAAIEAALGGRLQavvvenLNAAKKAIAFLKQNELgrvTFL-PLDSIKGTEIQGNDREILKNI------- 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7871 rDKEQQVSKDLEEIEqvfrriSQLQDKLNALheqLQSVHVYDEhIAQTEQLLITLNSQVQQAAEESKLL---------VA 7941
Cdd:TIGR02168 598 -EGFLGVAKDLVKFD------PKLRKALSYL---LGGVLVVDD-LDNALELAKKLRPGYRIVTLDGDLVrpggvitggSA 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7942 QTTAHYQAKQNQLpSDIAQEFTALELLAERVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQM 8021
Cdd:TIGR02168 667 KTNSSILERRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8022 KELLQRINHEITAIYERFTLVKTN-GQLIIENCRNSEEKTLVQTTIDQLAASLAQVRGWLDEKKQAVGDSLDAWTRFMNL 8100
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8101 YQivmswaSEKRNFIDQTIELRTLpearnklndyvtsVKSIKPIVKHLSEMDKELEHigQVTTVGDLKDKLQEAEDAKIS 8180
Cdd:TIGR02168 826 LE------SLERRIAATERRLEDL-------------EEQIEELSEDIESLAAEIEE--LEELIEELESELEALLNERAS 884
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8181 VEAVLLERNSLLQEACEEWDQCERKIKDirswhektkqgldssqqqkkpLRDQLGFCEKTLADINVQKTKLRLSIEKLEv 8260
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSE---------------------LRRELEELREKLAQLELRLEGLEVRIDNLQ- 942
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8261 hfrngmggdPRLSENVDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRlvmaptylphdrer 8340
Cdd:TIGR02168 943 ---------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELK-------------- 999
|
970 980 990
....*....|....*....|....*....|.
gi 320544542 8341 alaEQQDLITQELDELLQSLSSVEDGIANMN 8371
Cdd:TIGR02168 1000 ---ERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
7215-8266 |
5.38e-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: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7215 NADKLKLNDDIKNMKDRYGRIKNTID-----DRVNALGDHIKK----------------YKDAKSRLAECSQ-------- 7265
Cdd:TIGR01612 599 NKLKLELKEKIKNISDKNEYIKKAIDlkkiiENNNAYIDELAKispyqvpehlknkdkiYSTIKSELSKIYEddidalyn 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7266 FLGNIQQ-----------KLRELNRPIGSRIEDVQDLLGA-YEGILKELKDSKSKMGDMQMDDLPELQSILAQqdDMIKL 7333
Cdd:TIGR01612 679 ELSSIVKenaidntedkaKLDDLKSKIDKEYDKIQNMETAtVELHLSNIENKKNELLDIIVEIKKHIHGEINK--DLNKI 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7334 IEDQLAHLRQLLLLREQFIALINEIIAFIMKYTDV------IIDIENSPDslEDKINKYDdvivKIQECEGVLASANDKG 7407
Cdd:TIGR01612 757 LEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIknhyndQINIDNIKD--EDAKQNYD----KSKEYIKTISIKEDEI 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7408 QKIASEGNAAdKNSITEQLQSLKNQLQNLRKAVESQrqkHQLQLESHKKMAAELSEilDWLHSHEGAAK-SRPLLDRDPE 7486
Cdd:TIGR01612 831 FKIINEMKFM-KDDFLNKVDKFINFENNCKEKIDSE---HEQFAELTNKIKAEISD--DKLNDYEKKFNdSKSLINEINK 904
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7487 SVERELQKHQSL-------------SQDIESYLNKFNKINDGVKTEIGM--PSSLLEMlSEGRSLVASLPHELEEREKYL 7551
Cdd:TIGR01612 905 SIEEEYQNINTLkkvdeyikicentKESIEKFHNKQNILKEILNKNIDTikESNLIEK-SYKDKFDNTLIDKINELDKAF 983
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7552 KNNRDSRLEYM--QLVAKFNDWVHEAELRLQNSqhgidyehLVQDLDEHKIFFGN-EAPIRNlVHKQIQEAADKIWSSLN 7628
Cdd:TIGR01612 984 KDASLNDYEAKnnELIKYFNDLKANLGKNKENM--------LYHQFDEKEKATNDiEQKIED-ANKNIPNIEIAIHTSIY 1054
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7629 NYEQsELSAELAQFQTKL-TNTLANAKTQQSELEKEAERWREYQQSiDRVKAtiERTKFVDEPVQNLAGLHFNIQKLSHA 7707
Cdd:TIGR01612 1055 NIID-EIEKEIGKNIELLnKEILEEAEINITNFNEIKEKLKHYNFD-DFGKE--ENIKYADEINKIKDDIKNLDQKIDHH 1130
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7708 IGNVQS-QNSDLTLVNQQAQSLIRQADARNRQLIEQDNAGLNRSWQDLVRSLEQRR---DNLQQLAEHWDGFENSLHAWE 7783
Cdd:TIGR01612 1131 IKALEEiKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKniyDEIKKLLNEIAEIEKDKTSLE 1210
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7784 KA---------------LGRLEDKFRNVDPTVRSR----RHLEDTKNAIQELREESNQLKSSHKEIEALSKSILTF---- 7840
Cdd:TIGR01612 1211 EVkginlsygknlgklfLEKIDEEKKKSEHMIKAMeayiEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDkdhh 1290
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7841 -LGEVHKPSAEAIQAKVDKLVE---QQAKLNDTLRDKEQQVS---KDLEEIEQVFRRISQLQD--KLNALHEQLQSVHVY 7911
Cdd:TIGR01612 1291 iISKKHDENISDIREKSLKIIEdfsEESDINDIKKELQKNLLdaqKHNSDINLYLNEIANIYNilKLNKIKKIIDEVKEY 1370
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7912 DEHIAQTeqllitlNSQVQQAAEESKLLVAQTtahyqakqnqlpsdiaQEFTALELLAERVQVTMETKEKDfkraktvrt 7991
Cdd:TIGR01612 1371 TKEIEEN-------NKNIKDELDKSEKLIKKI----------------KDDINLEECKSKIESTLDDKDID--------- 1418
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7992 EYVDGVDEVQRWLLQAEVQVQersltpTQMKElLQRINHEITAIYERFTLVKTNGQLIIENCRNSEEKTLvQTTIDQLAA 8071
Cdd:TIGR01612 1419 ECIKKIKELKNHILSEESNID------TYFKN-ADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDH-DFNINELKE 1490
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8072 SLAQVRGWLDE---KKQAVGDSLDAWTRFMNLYQIVMS--WASEKRNFIDQT-----IELRTLPEARNKLN-DYVTSVKS 8140
Cdd:TIGR01612 1491 HIDKSKGCKDEadkNAKAIEKNKELFEQYKKDVTELLNkySALAIKNKFAKTkkdseIIIKEIKDAHKKFIlEAEKSEQK 1570
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8141 IKPIVKHLSEMDKELEH--------IGQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEACE-EWDQCERKIKDIRS 8211
Cdd:TIGR01612 1571 IKEIKKEKFRIEDDAAKndksnkaaIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSfSIDSQDTELKENGD 1650
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*
gi 320544542 8212 WHEKTKQGLDSSQQQKKPLRDQlgfcEKTLADINVQKTKLRLSIEKLEVHFRNGM 8266
Cdd:TIGR01612 1651 NLNSLQEFLESLKDQKKNIEDK----KKELDELDSEIEKIEIDVDQHKKNYEIGI 1701
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4393-4585 |
5.87e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 48.98 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4393 QWNDYEINLDRLITWLGEAENSLKNYNLKSSFEEKEEQLNGFQSLAQNLRQNEADFDKVKDDTSELVQSSGE--TRIAVN 4470
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPdaEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4471 VQQVSSRFQSIQATAKEILKKCEQAVQDHGHFNDkYKQCADWLANAQARYDDCCDLSTVASRDDLLKKQvviQELLAQQP 4550
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLESVEELLKKH---KELEEELE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 320544542 4551 TATQLLNSTVELGEKCYGSTATEGREAIRSQLDDL 4585
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEEL 191
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3542-3630 |
5.95e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 46.17 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3542 EFDTIIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINELMDQGREI-----EGETDLNLKLSR 3616
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeghPDAEEIEERLEE 81
|
90
....*....|....
gi 320544542 3617 LNTRYQTLKNLCKE 3630
Cdd:smart00150 82 LNERWEELKELAEE 95
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5431-6161 |
6.09e-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: 51.21 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5431 RDAINTEMKELQTEWDRLVKKMStaKVQLETNLLQWADYSssYSQLQQWITDREAKLQQACEQKIVKSKRGQPGLSSGLS 5510
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVS--ELEEEIEELQKELYA--LANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5511 ERKANLRQTNNIVQDIVSFEPMIQSVTSKASVLQQGAPGTE--ISDKYENLTKQAKDLYEKQK------NTIESYQSLI- 5581
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELEsrLEELEEQLETLRSKVAQLELqiaslnNEIERLEARLe 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5582 DAGNEFATWLRNAKERLSKCSEPTGDKQA--LAEKTHQLKILQGELPEGAQKLKNA---LEQGEIACRSAEPE------D 5650
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELKELQaeLEELEEELEELQEELERLEEALEELreeLEEAEQALDAAERElaqlqaR 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5651 CEIIEQEVALLQEEFDAYREALNKAK----------DYLEVG------------------IVKWSDYQDQYTEALEWLSK 5702
Cdd:TIGR02168 491 LDSLERLQENLEGFSEGVKALLKNQSglsgilgvlsELISVDegyeaaieaalggrlqavVVENLNAAKKAIAFLKQNEL 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5703 TEALVQSYNKLQDSLIQKK--VVLEQFQGHLQTLFDWQKTLDDLNMKAQVLLETC---SDTRISNAIMQLTTKYNALLTL 5777
Cdd:TIGR02168 571 GRVTFLPLDSIKGTEIQGNdrEILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvDDLDNALELAKKLRPGYRIVTL 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5778 AKEVMRRLEMHYQEHQQHHSLYEECQSWIEKTREKLsecEQIPGTLNEVQIKLNTVKNLRQGFETGQNKLRYLLELKEKV 5857
Cdd:TIGR02168 651 DGDLVRPGGVITGGSAKTNSSILERRREIEELEEKI---EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5858 IMNTEQNgAAKIQEDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDVEPSVKTSDEFLND----LS 5933
Cdd:TIGR02168 728 ISALRKD-LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlreaLD 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5934 EKRAAL----EKFRVIQRDINGHNDIVEKINQRL------KEDNSLDLKDFQPGLTKFDDLQTQVNKIIESLENQVNSHE 6003
Cdd:TIGR02168 807 ELRAELtllnEEAANLRERLESLERRIAATERRLedleeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6004 KYKQAYNELQDWLRRTRIEVEQcadchgEKDQVESRLNRLGDIQSSSLEGKALLEACEELSQAVIAtsgSEGQDNvAQEI 6083
Cdd:TIGR02168 887 EALALLRSELEELSEELRELES------KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS---EEYSLT-LEEA 956
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320544542 6084 KHLTSEWETLQTISRDARSSLESCLAAwqtflqkFNKINLWIETMNKRVTKSQEGENKTPEDLVNAKKLLEEVLAEKD 6161
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKE-------LGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
9508-9635 |
7.28e-05 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 49.55 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 9508 QQTTPRIPSPTEKSEVEQDIKSVQTSPQHQPKLDETAVQTSLEVQP------DNQENESQTLIVEITETEA--------- 9572
Cdd:PRK10905 82 QGQTPVATDGQQRVEVQGDLNNALTQPQNQQQLNNVAVNSTLPTEPatvapvRNGNASRQTAKTQTAERPAttrparkqa 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 9573 -------QTTPRSEEQSVAVEISTTEIQTDVSGQPAETVEISSQTTVTTTIEKELQTTPKDSPRAPEAGS 9635
Cdd:PRK10905 162 viepkkpQATAKTEPKPVAQTPKRTEPAAPVASTKAPAATSTPAPKETATTAPVQTASPAQTTATPAAGG 231
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2426-3966 |
7.40e-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: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2426 TPEESNALNDAYTalvvnyQNLETNMLQKKAALEKW-------------TELLGWKNDTESHL-----NYLKHQLDKPEg 2487
Cdd:TIGR01612 953 TIKESNLIEKSYK------DKFDNTLIDKINELDKAfkdaslndyeaknNELIKYFNDLKANLgknkeNMLYHQFDEKE- 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2488 paaEELSKVIDEIDNLGQGIgywkgqakeidenPAIQLrdalsrrpLIATQIVNDVEnKLENL------KLRSQSQQQQI 2561
Cdd:TIGR01612 1026 ---KATNDIEQKIEDANKNI-------------PNIEI--------AIHTSIYNIID-EIEKEigknieLLNKEILEEAE 1080
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2562 QQMTVRKDKFHALEH-NFGQALQENRAKL-DEILRQHPTLNNIDQII-ADLVAL----NDALKYQADLKNRIHD----EG 2630
Cdd:TIGR01612 1081 INITNFNEIKEKLKHyNFDDFGKEENIKYaDEINKIKDDIKNLDQKIdHHIKALeeikKKSENYIDEIKAQINDledvAD 1160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2631 SLLMREDIASMPAIQESLLI-MDK------NYDSLQNEIA---------DRIQKYNL-----ISQALREYADSKDKFSKE 2689
Cdd:TIGR01612 1161 KAISNDDPEEIEKKIENIVTkIDKkkniydEIKKLLNEIAeiekdktslEEVKGINLsygknLGKLFLEKIDEEKKKSEH 1240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2690 LKKA-----EDLYNAIPQQPRDETEL-----------------------HQASEKTRKTMEQLRKSKLSLDELERRGNNV 2741
Cdd:TIGR01612 1241 MIKAmeayiEDLDEIKEKSPEIENEMgiemdikaemetfnishdddkdhHIISKKHDENISDIREKSLKIIEDFSEESDI 1320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2742 GKlfsaigepIPQEVPQEVTAAKQHWQDLHDKTAKNAHVYETEAV-IWSQIEDAKKDLLPWLSETNQGLCDAADNSieie 2820
Cdd:TIGR01612 1321 ND--------IKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLnKIKKIIDEVKEYTKEIEENNKNIKDELDKS---- 1388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2821 fgpMRLSKYRTELPSYQALKdSIVEKTNDLVKINKGAEIPALSAlNKLLSEqfaEVNN-----NADRLSA-ITTSFNDQE 2894
Cdd:TIGR01612 1389 ---EKLIKKIKDDINLEECK-SKIESTLDDKDIDECIKKIKELK-NHILSE---ESNIdtyfkNADENNEnVLLLFKNIE 1460
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2895 ------QELRRRSKEAGE-----RVSKLREQLIK---CDDMSGDNNKIMER----LQQCRALRGELDNSGNEIDnIKQKV 2956
Cdd:TIGR01612 1461 madnksQHILKIKKDNATndhdfNINELKEHIDKskgCKDEADKNAKAIEKnkelFEQYKKDVTELLNKYSALA-IKNKF 1539
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2957 DELRNlyptfSESIIPKELNNVQKRYEnvdLYAKKIEssllQFLKKFHADKVGMLKRIIATQREKVAWCQPESSSDkyNL 3036
Cdd:TIGR01612 1540 AKTKK-----DSEIIIKEIKDAHKKFI---LEAEKSE----QKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLE--NF 1605
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3037 DVKKSSLQEVSKSIDDCKARHAETLKSLEMLKAVESPQNLAELTSDAELLRKDMQALQDsfdQIKGILDENVDLwsqyEQ 3116
Cdd:TIGR01612 1606 ENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKENGDNLNSLQEFLESLKD---QKKNIEDKKKEL----DE 1678
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3117 SNEQISNWLRDVEGRVKaetSSQVNLSEvpqKLQELSILQQdvlahepiiNNLEQTsQQLIEKNPEARIGQFVTHlvqry 3196
Cdd:TIGR01612 1679 LDSEIEKIEIDVDQHKK---NYEIGIIE---KIKEIAIANK---------EEIESI-KELIEPTIENLISSFNTN----- 1737
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3197 qavskaltsyidkirgaQLSNANFAKAAKDFNEWFGDAKIEFQELARMgspgsssaTAQQLQTVKNYIKTFDNgqiLLNN 3276
Cdd:TIGR01612 1738 -----------------DLEGIDPNEKLEEYNTEIGDIYEEFIELYNI--------IAGCLETVSKEPITYDE---IKNT 1789
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3277 AVDIGEALYPVVSPDNRERIRADLRQMREkFDYLRDEANAFMQQVEGVLIQKTS-IEESYTQVSHYLNESKAkvpTTDE- 3354
Cdd:TIGR01612 1790 RINAQNEFLKIIEIEKKSKSYLDDIEAKE-FDRIINHFKKKLDHVNDKFTKEYSkINEGFDDISKSIENVKN---STDEn 1865
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3355 -LYPTLATKKAALQN--------YKTQLQEITLHK-----------------NALKQLHDKAVTLCDDESER--KTDESI 3406
Cdd:TIGR01612 1866 lLFDILNKTKDAYAGiigkkyysYKDEAEKIFINIsklansiniqiqnnsgiDLFDNINIAILSSLDSEKEDtlKFIPSP 1945
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3407 QEYNTLSKKISDRITTVGNhVVKHEAYDQvlEKAQDWLNTI------------KSEAIDILNETTFEKEgaeeKLLVVEN 3474
Cdd:TIGR01612 1946 EKEPEIYTKIRDSYDTLLD-IFKKSQDLH--KKEQDTLNIIfenqqlyekiqaSNELKDTLSDLKYKKE----KILNDVK 2018
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3475 LLQHKpegdsiFDTCHKL------LETVLTQTHPSGHPALLKGFEEPKQSwedfmtLCQDSLVKLKQlcSKWDEFDTIIE 3548
Cdd:TIGR01612 2019 LLLHK------FDELNKLscdsqnYDTILELSKQDKIKEKIDNYEKEKEK------FGIDFDVKAME--EKFDNDIKDIE 2084
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3549 ELDNWMKNVEA------------VVKNQNLKSTAEAKNAHLKQLQDisKDIERrgaaiNELMDQGREIEGETdlnlklsr 3616
Cdd:TIGR01612 2085 KFENNYKHSEKdnhdfseekdniIQSKKKLKELTEAFNTEIKIIED--KIIEK-----NDLIDKLIEMRKEC-------- 2149
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3617 LNTRYQTLKNLCKESIAKYVNYVKDHESFDKDFDSFKQNLQSSVDElaktneivgDQSVLQDQQNkLREMsdKRILDSTL 3696
Cdd:TIGR01612 2150 LLFSYATLVETLKSKVINHSEFITSAAKFSKDFFEFIEDISDSLND---------DIDALQIKYN-LNQT--KKHMISIL 2217
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3697 FEGLIDRGEklyghtspegreIIRQQLRALRTLwDNYTDDLNSATQKIDQCLLQFNEFsiaqdQLTKWLKDVDKAMQSht 3776
Cdd:TIGR01612 2218 ADATKDHNN------------LIEKEKEATKII-NNLTELFTIDFNNADADILHNNKI-----QIIYFNSELHKSIES-- 2277
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3777 ePKTTLQEKRA-QLQNHKLLHQEITTHNVLVDNVCdkaqilvdQIKDNSLNVYLTSIKQLFQSIVQKSDEILHNLDDCVq 3855
Cdd:TIGR01612 2278 -IKKLYKKINAfKLLNISHINEKYFDISKEFDNII--------QLQKHKLTENLNDLKEIDQYISDKKNIFLHALNENT- 2347
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3856 khNELNNALSSAKTWISNEKAKLLECDDAYG-EKADIKRKIETLGQLAQNkpqamkiisdIRDLFEKVkaTTSEKGNEVL 3934
Cdd:TIGR01612 2348 --NFNFNALKEIYDDIINRENKADEIENINNkENENIMQYIDTITKLTEK----------IQDILIFV--TTYENDNNII 2413
|
1690 1700 1710 1720
....*....|....*....|....*....|....*....|
gi 320544542 3935 DKEIEE--------LETTMKSHFDDIEGIEGKQKDVLAQW 3966
Cdd:TIGR01612 2414 KQHIQDndendvskIKDNLKKTIQSFQEILNKIDEIKAQF 2453
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
11183-11552 |
8.86e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.68 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11183 RQQLAALLDwLRQREAERNALQ------LRYihLKRVPHLKHRLDAMIQQLDQGEQQskaLQEQQQELARHCDDALATAm 11256
Cdd:PRK11281 42 QAQLDALNK-QKLLEAEDKLVQqdleqtLAL--LDKIDRQKEETEQLKQQLAQAPAK---LRQAQAELEALKDDNDEET- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11257 rmeqasiGQRISNLRaalktwqgflqrVTQLsesyEQRVNQLQQEFGAAQK-LLDANSE--SLPTQPAaieqllgslRAQ 11333
Cdd:PRK11281 115 -------RETLSTLS------------LRQL----ESRLAQTLDQLQNAQNdLAEYNSQlvSLQTQPE---------RAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11334 RVQLGAQVSALE--SLTVTQEELKECISPhdmktiRQRNWLLWQQHAdLDYQLANLINSIEERLSLLSNYQIRYDRISQW 11411
Cdd:PRK11281 163 AALYANSQRLQQirNLLKGGKVGGKALRP------SQRVLLQAEQAL-LNAQNDLQRKSLEGNTQLQDLLQKQRDYLTAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11412 LQRLEQRVEKDADVTAMTNPEQAAKQLEQQVNS--------------ELQLRDKEREWLLSTSRELLTLySEPEVRsqVQ 11477
Cdd:PRK11281 236 IQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQdeaariqanplvaqELEINLQLSQRLLKATEKLNTL-TQQNLR--VK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11478 QQSDSLIDRWQRLKylakqkaTKIGELKMTLL-------------------RLEERIALIRAWLFEVESQLDKPLNFESY 11538
Cdd:PRK11281 313 NWLDRLTQSERNIK-------EQISVLKGSLLlsrilyqqqqalpsadlieGLADRIADLRLEQFEINQQRDALFQPDAY 385
|
410
....*....|....
gi 320544542 11539 tpnvIEAKLKEHEQ 11552
Cdd:PRK11281 386 ----IDKLEAGHKS 395
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5249-5460 |
1.15e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 47.83 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5249 QWRAYKEEYERLMEWLQQIDILVKNhkLNLCPNLPEKEKQVADMKEVMSRLEKGKDDIDKFNASAASLLKSHLD--TYVN 5326
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPdaEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5327 NQLRHLSSVYQVQVNLAKDVLKKVETNRDQHREYDaNMKSAKDWIANAKATIQSAGEGaGSKEALQRRLEQIQDLIRNRE 5406
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLG-KDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 320544542 5407 LGQNLVHTAINNGEKIIRNTRSDGRDAINTEMKELQTEWDRLVKKMSTAKVQLE 5460
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
3113-3203 |
1.20e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 45.40 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3113 QYEQSNEQISNWLRDVEgRVKAETSSQVNLSEVPQKLQELSILQQDVLAHEPIINNLEQTSQQLIEKNPEAR--IGQFVT 3190
Cdd:smart00150 2 QFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAeeIEERLE 80
|
90
....*....|...
gi 320544542 3191 HLVQRYQAVSKAL 3203
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7628-7898 |
1.21e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7628 NNYEQSE-LSAELAQfqtkLTNTLANAKTQQSELEKEAERWREYQQSIDRVKAtiertkfVDEPVQNLAGLHFNIQKLSH 7706
Cdd:COG4913 607 DNRAKLAaLEAELAE----LEEELAEAEERLEALEAELDALQERREALQRLAE-------YSWDEIDVASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7707 AIGNVQSQNSDLTLVNQQAQSLIRQADArnrqlIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKAl 7786
Cdd:COG4913 676 ELERLDASSDDLAALEEQLEELEAELEE-----LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA- 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7787 gRLEDKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKsshkeiEALSKSILTFLGEVHKPSAE------------AIQA 7854
Cdd:COG4913 750 -LLEERFAAALGDAVERELRENLEERIDALRARLNRAE------EELERAMRAFNREWPAETADldadleslpeylALLD 822
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 320544542 7855 KV--DKLVEQQAKLNDTLRDKEQQVSKDL-----EEIEQVFRRISQLQDKL 7898
Cdd:COG4913 823 RLeeDGLPEYEERFKELLNENSIEFVADLlsklrRAIREIKERIDPLNDSL 873
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6003-6201 |
1.26e-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: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6003 EKYKQAYNELQDWLRRTRIEVEQcADCHGEKDQVESRLNRLGDIQSSSLEGKALLEACEELSQAVIAtSGSEGQDNVAQE 6082
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6083 IKHLTSEWETLQTISRDARSSLESCLAAWQtFLQKFNKINLWIETMNKRVTKSQEGENKTP-EDLVNA-KKLLEEVLAEK 6160
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDLGKDLESvEELLKKhKELEEELEAHE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 320544542 6161 DNVEDLNDNCELLMEQS---ACTRIRDQTIETQANYTKLLTSAQ 6201
Cdd:cd00176 160 PRLKSLNELAEELLEEGhpdADEEIEEKLEELNERWEELLELAE 203
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
7837-8038 |
1.47e-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: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7837 ILTFLGEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVhvyDEHIA 7916
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---EAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7917 QTEQLLITLNSQV-QQAAEESKLLVAQTTAHYQAKQNQL-----PSDIAQEFTALELLAERVQVTMETKEKDFKRAKTVR 7990
Cdd:COG4942 87 ELEKEIAELRAELeAQKEELAELLRALYRLGRQPPLALLlspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 320544542 7991 TEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELLQRINHEITAIYER 8038
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3517-3630 |
1.56e-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: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3517 QSWEDFMTLCQDSLVKLKQLCSKWDEFDTiIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINE 3596
Cdd:cd00176 86 QRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKS 164
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 320544542 3597 LMDQGREIE------GETDLNLKLSRLNTRYQTLKNLCKE 3630
Cdd:cd00176 165 LNELAEELLeeghpdADEEIEEKLEELNERWEELLELAEE 204
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6216-6410 |
1.64e-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: 47.44 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6216 EFLNYKKEMDAWIEKAQQVLDDCSTDGDAAIIAQKLDTVNSLASRLPEGQHLLALVQDAYSKASNITPEDKqEKLRELMT 6295
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA-EEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6296 KVREDWDALGLAVKQKLSDLKQAQNRWNDFaANKDKLEKWLNETETTLKvAPETKGELSEMKTLLERYKTLSNELKLKGN 6375
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 320544542 6376 ELEQLQSEARDLGTEV--DAVNRLQSRCDKLKNDCSA 6410
Cdd:cd00176 161 RLKSLNELAEELLEEGhpDADEEIEEKLEELNERWEE 197
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7560-7767 |
1.75e-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: 47.44 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7560 EYMQLVAKFNDWVHEAELRLQNSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLVhKQIQEAADKIwSSLNNYEQSELSAEL 7639
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERV-EALNELGEQL-IEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7640 AQFQTKLTNTLANAKTQQSELEKEAERWREYQQSIDRVKATIERTKFV--DEPVQNLAGLHFNIQKLSHAIGNVQSQNSD 7717
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALasEDLGKDLESVEELLKKHKELEEELEAHEPR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 320544542 7718 LTLVNQQAQSLIRQADARNRQLIEQDNAGLNRSWQDLVRSLEQRRDNLQQ 7767
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10801-11454 |
1.77e-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: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10801 ERLRKATERLEGLAGDLHNREQLIDELKG---AAKPLIESCDVQIVEQIES--AVQEAVVAWNDTSENLQQLRTRYQRAV 10875
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERlaNLERQLEELEAQLEELESKLDELAEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10876 ELWDKYRNASAAVKNSIDQQMDAVKSLEQplDALQHAKVCQDNLTTQNDRILELRDIVAKIAADVgldasALMQGELDAL 10955
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELE--ELESRLEELEEQLETLRSKVAQLELQIASLNNEI-----ERLEARLERL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10956 GQRLAECKDAITTLANVAETQDKER-----KELDKEVTLAKAYFNNVQ------QDISREAPQNPKESEEQLAALRAHLQ 11024
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLEealeelREELEEAEQALDAAERELAQLQARLD 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11025 TLARTEEQLRQ--------LKERHQNSEVAPSVAS--------------------------SDDDGILEVLAL-WQKIFQ 11069
Cdd:TIGR02168 493 SLERLQENLEGfsegvkalLKNQSGLSGILGVLSElisvdegyeaaieaalggrlqavvveNLNAAKKAIAFLkQNELGR 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11070 DTFQEYHRLSTRLARSQNssealrlwRQYLQHVQSFLSCAIPEDYSSLREQQQLCAIHQNLLISQqSVLSETPLESELSE 11149
Cdd:TIGR02168 573 VTFLPLDSIKGTEIQGND--------REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVD-DLDNALELAKKLRP 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11150 QYK-------------ALTNLHNETLSRIMQRNGELERrvsgwnaYRQQLAALLDWLRQREAERNAL-QLRYIHLKRVPH 11215
Cdd:TIGR02168 644 GYRivtldgdlvrpggVITGGSAKTNSSILERRREIEE-------LEEKIEELEEKIAELEKALAELrKELEELEEELEQ 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11216 LKHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALAtamrmEQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRV 11295
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK-----ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11296 NQLQQEFGAAQKLLDANS-----------------ESLPTQPAAIEQLLGSLRAQRVQLGAQVSAL----ESLTVTQEEL 11354
Cdd:TIGR02168 792 EQLKEELKALREALDELRaeltllneeaanlrerlESLERRIAATERRLEDLEEQIEELSEDIESLaaeiEELEELIEEL 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11355 KECISPH---------DMKTIRQRNWLLWQQHADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQRLEQRVEKDADV 11425
Cdd:TIGR02168 872 ESELEALlnerasleeALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
730 740
....*....|....*....|....*....
gi 320544542 11426 TAMTNPEQAAKQLEQQVNSELQLRDKERE 11454
Cdd:TIGR02168 952 TLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7148-7313 |
1.92e-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: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7148 FEDSMKNMGDWLNEMETATEGELRTTSLPVLEEQLAHYKKLLSDAENKGGLINDVSEQGKSILpTLSNADKLKLNDDIKN 7227
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7228 MKDRYGRIKNTIDDRVNALGDHIKKYKdaksRLAECSQFLGNIQQKLRELNR-PIGSRIEDVQDLLGAYEGILKELKDSK 7306
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQ----FFRDADDLEQWLEEKEAALASeDLGKDLESVEELLKKHKELEEELEAHE 159
|
....*..
gi 320544542 7307 SKMGDMQ 7313
Cdd:cd00176 160 PRLKSLN 166
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
5800-6589 |
1.95e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 49.66 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5800 EECQSWIEKTREKLSECEQipgtlnevqiklNTVKNLRQGFETGQNKLRYLLELKEKVIMNTEQNGAAKIQEDTEALKQD 5879
Cdd:TIGR01612 699 DDLKSKIDKEYDKIQNMET------------ATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILEDFKNKEKE 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5880 FDKLLVDLNDVRQKLANRLAQLEEIFKLY--KILIEWL--EDVEPSVKTSDEFLNDLSEKRAalEKFRVIQRDINGHNDI 5955
Cdd:TIGR01612 767 LSNKINDYAKEKDELNKYKSKISEIKNHYndQINIDNIkdEDAKQNYDKSKEYIKTISIKED--EIFKIINEMKFMKDDF 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5956 VEKINQRLKEDNSLDlKDFQPGLTKFDDLQTQVNKII---------------ESLENQVN-SHEKYKQAYNELQ---DWL 6016
Cdd:TIGR01612 845 LNKVDKFINFENNCK-EKIDSEHEQFAELTNKIKAEIsddklndyekkfndsKSLINEINkSIEEEYQNINTLKkvdEYI 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6017 RRTRIEVEQCADCHGEKDQVESRLNR-LGDIQSSSLEGKA--------LLEACEELSQAVIATSGSEGQDNVAQEIKHLT 6087
Cdd:TIGR01612 924 KICENTKESIEKFHNKQNILKEILNKnIDTIKESNLIEKSykdkfdntLIDKINELDKAFKDASLNDYEAKNNELIKYFN 1003
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6088 SEWETLQTISRDArsslesclaAWQTFLQK---FNKINLWIETMNKRVTK------------SQEGENKTPEdlvNAKKL 6152
Cdd:TIGR01612 1004 DLKANLGKNKENM---------LYHQFDEKekaTNDIEQKIEDANKNIPNieiaihtsiyniIDEIEKEIGK---NIELL 1071
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6153 LEEVLAEKD-NVEDLNDNCELLMEQSACTRIRDQTIETQANYTKLLTSAQGLVAKIEKNLSDHTEFL----NYKKEMDAW 6227
Cdd:TIGR01612 1072 NKEILEEAEiNITNFNEIKEKLKHYNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKkkseNYIDEIKAQ 1151
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6228 IEKAQQVLDDCSTDGDAAIIAQKLDTVnslasrlpegqhllalvqdayskasnITPEDKQEKLRELMTKVREDWDalglA 6307
Cdd:TIGR01612 1152 INDLEDVADKAISNDDPEEIEKKIENI--------------------------VTKIDKKKNIYDEIKKLLNEIA----E 1201
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6308 VKQKLSDLKQAQNRWNDFAANKDKLekwlnetetTLKVAPETKGELSEMKTLLERYKTLSNELKLKGNELEQLQSEARDL 6387
Cdd:TIGR01612 1202 IEKDKTSLEEVKGINLSYGKNLGKL---------FLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDI 1272
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6388 GTEVDAVNRLQSRCDKL-----KNDCS-AHITALEQEMFDYNAYHQSLQDVEKWLLQISFQLMAHNS------------- 6448
Cdd:TIGR01612 1273 KAEMETFNISHDDDKDHhiiskKHDENiSDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSdinlylneianiy 1352
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6449 --LFISNREQTQEQIKQHEAllvEIQKYQTNLDDLNAKGQAQIK--RYESSTPAIRPTVESQL--KNIqdsyNSLLQTSV 6522
Cdd:TIGR01612 1353 niLKLNKIKKIIDEVKEYTK---EIEENNKNIKDELDKSEKLIKkiKDDINLEECKSKIESTLddKDI----DECIKKIK 1425
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320544542 6523 QIKNRLLESlakfqeyEDTLDSIMRNLETYEPIIQTELDapatSLELAQNQLRcaQEMQNKLNNEKS 6589
Cdd:TIGR01612 1426 ELKNHILSE-------ESNIDTYFKNADENNENVLLLFK----NIEMADNKSQ--HILKIKKDNATN 1479
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
8201-8549 |
1.98e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8201 QCERKIKDIRSWHEKtkqgLDSSQQQKKPLRDQLGFCEKTLADINVQKTKLRLSIEKLEvhfrngmggdprlsENVDDLV 8280
Cdd:COG1196 219 KEELKELEAELLLLK----LRELEAELEELEAELEELEAELEELEAELAELEAELEELR--------------LELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8281 RVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRLVMAptylphdRERALAEQQDLITQELDELLQSL 8360
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE-------ELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8361 SSVEDGIANMNQSSLDgMLHGLKLIQSNLEVHERDAIELKNQAKKLptdpatERLLNDTVDRIDLLLRRTQQGITMIANA 8440
Cdd:COG1196 354 EEAEAELAEAEEALLE-AEAELAEAEEELEELAEELLEALRAAAEL------AAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8441 MHGQKKRQQEIDEYQQHLLELEQWIIEVSAELASfepTSDSSTDEQVLKSQVERSQQLLRTLKDRQQSMEDLVEQTRQLQ 8520
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEA---LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
330 340
....*....|....*....|....*....
gi 320544542 8521 SHPDVSPLADTLMEQLQSIITILREQVTV 8549
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
9473-9632 |
2.04e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 49.27 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 9473 EDAVVSSP--SESPRTPMVELVIPTEVVELA--LVEDEEQQTTPRIPSPTEKSEVEQDIKSVQTSPQHQPKLDET---AV 9545
Cdd:PRK10811 861 AEEVQVQPvvAEVPVAAAVEPVVSAPVVEAVaeVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDvavAQ 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 9546 QTSLEVQPDNQENESQTLIVEITETEAQTTPRSEEQSVAVEISTTEIQTDVSGQPAETVEISSQTTVTTTIEKELQTTPK 9625
Cdd:PRK10811 941 EVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVEHNHATAPM 1020
|
....*..
gi 320544542 9626 DSPRAPE 9632
Cdd:PRK10811 1021 TRAPAPE 1027
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7726-8519 |
2.11e-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: 49.30 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7726 QSLIRQADARNRQL--IEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGF-ENSLHAWEKALGRLEDKFRNVDPTVR- 7801
Cdd:TIGR02169 233 EALERQKEAIERQLasLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAe 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7802 SRRHLEDTKNAIQELREESNQLKSshkEIEALSKSILTFLGEVHKPSAE--AIQAKVDKLV---EQQAKLNDTLRDKEQQ 7876
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLA---EIEELEREIEEERKRRDKLTEEyaELKEELEDLRaelEEVDKEFAETRDELKD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7877 VSKDLE----EIEQVFRRISQLQDKLNALHEQLQSVH----VYDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAhYQ 7948
Cdd:TIGR02169 390 YREKLEklkrEINELKRELDRLQEELQRLSEELADLNaaiaGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK-YE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7949 AKQNQLPSDIAQ---EFTALELLAERVQVT---METKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQ------------ 8010
Cdd:TIGR02169 469 QELYDLKEEYDRvekELSKLQRELAEAEAQaraSEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERyataievaagnr 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8011 ----VQERSLTPTQMKELLQRINheitaiYERFTLVKTNG-QLIIENCRNSEEKTLVQTTID------QLAASLAQVRGw 8079
Cdd:TIGR02169 549 lnnvVVEDDAVAKEAIELLKRRK------AGRATFLPLNKmRDERRDLSILSEDGVIGFAVDlvefdpKYEPAFKYVFG- 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8080 ldekKQAVGDSLDAWTRFMNLYQIVM--------SWA------SEKRNFIDQTIELRTLPEARNKLNDyvtsvksikpIV 8145
Cdd:TIGR02169 622 ----DTLVVEDIEAARRLMGKYRMVTlegelfekSGAmtggsrAPRGGILFSRSEPAELQRLRERLEG----------LK 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8146 KHLSEMDKELEHIGQvttvgDLKDKLQEAEDAKISVEAVLLERNSLLQEAceewDQCERKIKDIRSWHEKTKQGLDSSQQ 8225
Cdd:TIGR02169 688 RELSSLQSELRRIEN-----RLDELSQELSDASRKIGEIEKEIEQLEQEE----EKLKERLEELEEDLSSLEQEIENVKS 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8226 QKKPLRDQLGFCEKTLAdinvqktKLRLSIEKLEVHFRNgmggdprlsENVDDLVRVLDGLGELVKAKSQSLEQTLAQID 8305
Cdd:TIGR02169 759 ELKELEARIEELEEDLH-------KLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSRIEARLREIEQKLN 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8306 VYQQQMQSLRQRIIQEEQQLRLVmaptylpHDRERALAEQQDLITQELDELLQSLSSVEDGIANmnqssLDGMLHGLKLI 8385
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDL-------KEQIKSIEKEIENLNGKKEELEEELEELEAALRD-----LESRLGDLKKE 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8386 QSNLEVHERDAIELKNQAKklptdpATERLLNDTVDRIDLLLRRTQQGITMIANAmhgqKKRQQEIDEYQQHLLELEQWI 8465
Cdd:TIGR02169 891 RDELEAQLRELERKIEELE------AQIEKKRKRLSELKAKLEALEEELSEIEDP----KGEDEEIPEEELSLEDVQAEL 960
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 320544542 8466 IEVSAELASFEPTSDSSTD--EQVLKSQVERSQQlLRTLKDRQQSMEDLVEQTRQL 8519
Cdd:TIGR02169 961 QRVEEEIRALEPVNMLAIQeyEEVLKRLDELKEK-RAKLEEERKAILERIEEYEKK 1015
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4925-5136 |
2.24e-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: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4925 EDFDNAISDCSSWINEIKEKL---DYCSDMSSMspKELDKKLATIQDVILLKDEgsaRVLKILEQAQHvLANTAPGGHEA 5001
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLsstDYGDDLESV--EALLKKHEALEAELAAHEE---RVEALNELGEQ-LIEEGHPDAEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5002 INKELTDLQDLWSGIALRIMDVKSNLDDSITQWSGFLDqvqnVRKFNEWLDGQVKELS--EHQTTMTEKRAQLDRVKSTE 5079
Cdd:cd00176 77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD----ADDLEQWLEEKEAALAseDLGKDLESVEELLKKHKELE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 320544542 5080 EKVRVEKIDVDALKIQAKEMIASGQQSQAAFQAQKvLDTFDELFAKTQKLLSHRQDQ 5136
Cdd:cd00176 153 EELEAHEPRLKSLNELAEELLEEGHPDADEEIEEK-LEELNERWEELLELAEERQKK 208
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6004-6913 |
2.24e-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: 49.28 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6004 KYKQAYNELQDWLRRTRIEVEQCADCHGEkdqVESRLNRLgDIQSSSLEgkALLEACEELSQAVIATSgsegqdnvAQEI 6083
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNE---LERQLKSL-ERQAEKAE--RYKELKAELRELELALL--------VLRL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6084 KHLTSEWETLQTISRDARSSLESCLAAWQTFLQKFNKINLWIETMNKRVTKSQEGENKTPEDLVNAKKLLEEVLAEKDNV 6163
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6164 EDLNDNCELLMEQSACTRIRDQTIETQANytKLLTSAQGLVAKIEKnlsDHTEFLNYKKEMDAWIEKAQQVLDDCSTDgd 6243
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELE--EKLEELKEELESLEA---ELEELEAELEELESRLEELEEQLETLRSK-- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6244 aaiIAQKLDTVNSLASRLpegQHLLALVQDAyskasnitpEDKQEKLRElmtkvredwdalglavkQKLSDLKQAQNrwn 6323
Cdd:TIGR02168 388 ---VAQLELQIASLNNEI---ERLEARLERL---------EDRRERLQQ-----------------EIEELLKKLEE--- 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6324 dfaANKDKLEKWLNETETTLKvapETKGELSemkTLLERYKTLSNELKLKGNELEQLQSEARDLGTEVDAVNRLQSRCDK 6403
Cdd:TIGR02168 433 ---AELKELQAELEELEEELE---ELQEELE---RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6404 LkndcSAHITALEQEMFDYNAYHQSLQDV----EKWLLQISFQLMAH-NSLFISNRE---QTQEQIKQHEALLVEIQKYQ 6475
Cdd:TIGR02168 504 F----SEGVKALLKNQSGLSGILGVLSELisvdEGYEAAIEAALGGRlQAVVVENLNaakKAIAFLKQNELGRVTFLPLD 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6476 TNLDDLNAKGQAQIKRYESSTPAIRPTVESQLKNIQDSYNSLLQ-----TSVQIKNRLLESLaKFQEYEDTLD------- 6543
Cdd:TIGR02168 580 SIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGgvlvvDDLDNALELAKKL-RPGYRIVTLDgdlvrpg 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6544 ------SIMRNLETYEPiiQTELDAPATSLELAQNQLRCAQEMQNKLNNEKSRLAAAVQACEAATASISRPSSPLETAMQ 6617
Cdd:TIGR02168 659 gvitggSAKTNSSILER--RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6618 AIPERElivrAKLEDLLDQkpppktrsstggvsTDDDKDEADVEIQVELSDVNEALLDPIAHErvknyrrivrlnsAHVG 6697
Cdd:TIGR02168 737 RLEAEV----EQLEERIAQ--------------LSKELTELEAEIEELEERLEEAEEELAEAE-------------AEIE 785
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6698 KLNELVAKVQSHLGGLTASVSELEQQ-QKQRAELQDWVKKQQSSVSDwmMRPCKLRPEAAQQELVSMndllnsigdkrSQ 6776
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAElTLLNEEAANLRERLESLERR--IAATERRLEDLEEQIEEL-----------SE 852
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6777 LMLEMTGSLgdedTDLDDNIDKLESELMDAIAKKQAGQNVIDGYRQGMADVQNWFDTLIKRMDVLDRGSGlNCAQKMAAI 6856
Cdd:TIGR02168 853 DIESLAAEI----EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE-ELREKLAQL 927
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 320544542 6857 NEIKNEYELQGHPKIQELKGKAAQVAEVISNLDgQQVEEQMKSLDRRFADLGKRIDR 6913
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE-NKIEDDEEEARRRLKRLENKIKE 983
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2247-2459 |
2.30e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 47.06 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2247 WKSFDADAAKLEDWVGQGEQQMSRRPAVlntPHIDKLEKELVKLKSFNNEISQQQAKLVTLGQNADQIsLHLAPEGAAAL 2326
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYG---DDLESVEALLKKHEALEAELAAHEERVEALNELGEQL-IEEGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2327 KDRVNQMKGKLQKLSEATRGHINEVSDAIiSRQDFNAKLVNFSNWMEQLRNQVTQVEeinperVETSLHVIHALLQEHAD 2406
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASED------LGKDLESVEELLKKHKE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2407 -------KKPSFNAIYDEVKQLALGATPEESNALNDAYTALVVNYQNLETNMLQKKAALE 2459
Cdd:cd00176 151 leeeleaHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
11541-11876 |
2.33e-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: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11541 NVIEAKLKEHEQIQRSiehHSSNVGEVLNLVEMLLNDADSwrtqvNTSGLAASAQNLEQRWKNVCSQ--SAERKARIL-- 11616
Cdd:pfam07111 133 NLEEGSQRELEEIQRL---HQEQLSSLTQAHEEALSSLTS-----KAEGLEKSLNSLETKRAGEAKQlaEAQKEAELLrk 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11617 ---TIWNLLQQLIKLTAEHKNWLGKQ-----ESQIAGFERDQKSHSKHKLEERQMELRAKLEELESQSVNLR-----QLE 11683
Cdd:pfam07111 205 qlsKTQEELEAQVTLVESLRKYVGEQvppevHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLThmlalQEE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11684 QIYAKLAMSAGVEPENIQKltlpTKVMVSMWRQltprchalldaidKDAKLMREFNNAQLEATNSLNAIQkalEQLPSAE 11763
Cdd:pfam07111 285 ELTRKIQPSDSLEPEFPKK----CRSLLNRWRE-------------KVFALMVQLKAQDLEHRDSVKQLR---GQVAELQ 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11764 NQQTSKAEPKAVLQRleSLEKKLQDAQ------QHVQQADNLAQEAKTRTKQQPQL--KQLLELVSAYTTLWQTVQTRiv 11835
Cdd:pfam07111 345 EQVTSQSQEQAILQR--ALQDKAAEVEvermsaKGLQMELSRAQEARRRQQQQTASaeEQLKFVVNAMSSTQIWLETT-- 420
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 320544542 11836 tlkttwLTRAAQAAASLP-----VSEAANAAVQVNTLSQRKLRQAQ 11876
Cdd:pfam07111 421 ------MTRVEQAVARIPslsnrLSYAVRKVHTIKGLMARKVALAQ 460
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
10866-11465 |
2.47e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10866 QLRTRYQRAVELWDKYRNASAAVKNsIDQQMDAVKSLEQPLDALQHAKvcqdnlttqnDRILELRDIVAKIAADVGLDAS 10945
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALED-AREQIELLEPIRELAERYAAAR----------ERLAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10946 ALMQGELDALGQRLAECKDAITTLANVAETQDKERKELdkevtlAKAYFNNVQQDIsreapqnpKESEEQLAALRAHL-- 11023
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDEL------EAQIRGNGGDRL--------EQLEREIERLERELee 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11024 --QTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQdtfQEYHRLSTRLARSQNSSEALRLWRQYLQH 11101
Cdd:COG4913 357 reRRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAEIASLER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11102 VQSflscAIPEDYSSLREQqqlcaihqnllISQQSVLSETPL--------------------ESEL----------SEQY 11151
Cdd:COG4913 434 RKS----NIPARLLALRDA-----------LAEALGLDEAELpfvgelievrpeeerwrgaiERVLggfaltllvpPEHY 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11152 KALT----NLHNET---LSRIMQRNGELERRvsgwNAYRQQLAALLD--------WLRQREAERNAL-------QLRY-- 11207
Cdd:COG4913 499 AAALrwvnRLHLRGrlvYERVRTGLPDPERP----RLDPDSLAGKLDfkphpfraWLEAELGRRFDYvcvdspeELRRhp 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11208 --------IHLKRVPHLKHRLDAMIQQLDQG---EQQSKALQEQQQELARHCDDALATAMRMEQASigQRISNLRAALKT 11276
Cdd:COG4913 575 raitragqVKGNGTRHEKDDRRRIRSRYVLGfdnRAKLAALEAELAELEEELAEAEERLEALEAEL--DALQERREALQR 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11277 WQGFLQRVTQLsESYEQRVNQLQQEfgaAQKLLDANSE--SLPTQPAAIEQLLGSLRAQRVQLGAQVSALES-LTVTQEE 11353
Cdd:COG4913 653 LAEYSWDEIDV-ASAEREIAELEAE---LERLDASSDDlaALEEQLEELEAELEELEEELDELKGEIGRLEKeLEQAEEE 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11354 LKECISPHDMKTIRQRNWLlwqqHADLDYQLANLINSiEERLSLLSNYQIRYDRISQWLQRLEQRVEK------------ 11421
Cdd:COG4913 729 LDELQDRLEAAEDLARLEL----RALLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERamrafnrewpae 803
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 320544542 11422 --DADVTAMTNPEqAAKQLEQQVNSEL-QLRDKEREWLLSTSRELLT 11465
Cdd:COG4913 804 taDLDADLESLPE-YLALLDRLEEDGLpEYEERFKELLNENSIEFVA 849
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7755-8198 |
2.56e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7755 VRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKSSHKEIEALS 7834
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7835 KSILTFlgevhKPSAEAIQAKVDKLVEQQAKLNDTLRD----KEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVhv 7910
Cdd:COG4717 153 ERLEEL-----RELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEEL-- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7911 yDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAHYQAKQNQLPSDIAQEFTALELLAE--RVQVTMETKEKDFKRAKT 7988
Cdd:COG4717 226 -EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGllALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7989 VRTEYVDGVDEVQRWLLQAEVQVQ--ERSLTPTQMKELLQRINHEITAIYERFTLVKtngQLIIENCRNSEEKTLVQ--- 8063
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALglPPDLSPEELLELLDRIEELQELLREAEELEE---ELQLEELEQEIAALLAEagv 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8064 TTIDQLAASLAQVRGWLDEKKQavgdsLDAWTRFMNLYQIVMSWASEKRNFIDQTIEL----RTLPEARNKLNDYVTSVK 8139
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEE-----LEELEEQLEELLGELEELLEALDEEELEEELeeleEELEELEEELEELREELA 456
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 320544542 8140 SIKPIVKHLSEmDKELEHIGQVttVGDLKDKLQEAEDAKISVEAVLlernSLLQEACEE 8198
Cdd:COG4717 457 ELEAELEQLEE-DGELAELLQE--LEELKAELRELAEEWAALKLAL----ELLEEAREE 508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6870-7230 |
2.84e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6870 KIQELKgKAAQV--AEVISNLDGQQVEEQMKSLDRRFADLGKRIDRKsQLLDVTNKGVEGAKGEIDQLQnwvKQQIEELQ 6947
Cdd:PTZ00121 1547 KADELK-KAEELkkAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA-RIEEVMKLYEEEKKMKAEEAK---KAEEAKIK 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6948 APKPlgytpKDAEARQQKIKSLMKDAEAKQSLADVLEK-----RVANMQQELEPVEYSQLESALRNLNTENRNLSGVLKA 7022
Cdd:PTZ00121 1622 AEEL-----KKAEEEKKKVEQLKKKEAEEKKKAEELKKaeeenKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7023 ELDRALEASKARKSLENDLDKARQWLKTKisEVRKLPVYHPLTSAEIEKKIQENRKYDDDAKQFNDSVLTDVQRQAANIM 7102
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAE--EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7103 KDcddaDKAALQQILDEIAADYQTLKDESSKRGKSLDDLLQgrkafEDSMKN--MGDWLNEMETATEGELRTTSLPVLEE 7180
Cdd:PTZ00121 1775 KE----KEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANII-----EGGKEGnlVINDSKEMEDSAIKEVADSKNMQLEE 1845
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 320544542 7181 QLAHYKkllsdaeNKGGLINDVSEQGKSilPTLSNADKLKLNDDIKNMKD 7230
Cdd:PTZ00121 1846 ADAFEK-------HKFNKNNENGEDGNK--EADFNKEKDLKEDDEEEIEE 1886
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
7419-8085 |
2.96e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.56 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7419 KNSITEQLQSLKNQLQNLRKAVESQRQKHQ-LQLESHK---KMAAELSEILDWLHSH-----------EGAAKSRPLLDR 7483
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKAIQeLQFENEKvslKLEEEIQENKDLIKENnatrhlcnllkETCARSAEKTKK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7484 DPESVERELQKHQSLSQDIESYLNKFNKIN-DGVKTEIGMPSSLLEMLSEGRSLVASLPHELEEREKYL---------KN 7553
Cdd:pfam05483 174 YEYEREETRQVYMDLNNNIEKMILAFEELRvQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVsllliqiteKE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7554 NRDSRLEYM--QLVAKFNDWVHEAELRLQNSQHGIDYE-HLVQDLDEHKIFFGNEAPIRNLVHKQIQEAADKIWsSLNNY 7630
Cdd:pfam05483 254 NKMKDLTFLleESRDKANQLEEKTKLQDENLKELIEKKdHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIC-QLTEE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7631 EQSELSaELAQFQTKLTNTLANAKTQQSELEkeaERWREYQQsidRVKATIERTKFVDEPVQNLAGlhfNIQKLSHAIGN 7710
Cdd:pfam05483 333 KEAQME-ELNKAKAAHSFVVTEFEATTCSLE---ELLRTEQQ---RLEKNEDQLKIITMELQKKSS---ELEEMTKFKNN 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7711 VQSQNSDLTLVNQQAQSLIRQadarNRQlIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLE 7790
Cdd:pfam05483 403 KEVELEELKKILAEDEKLLDE----KKQ-FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7791 -----DKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKSSHKEI-------EALSKSILTfLGEVHKPSAEAIQAKVDK 7858
Cdd:pfam05483 478 telekEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIinckkqeERMLKQIEN-LEEKEMNLRDELESVREE 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7859 LVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVHVYDEHIAQTEQLLitlnsqVQQAAEESKL 7938
Cdd:pfam05483 557 FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL------KKKGSAENKQ 630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7939 LVAqttahYQAKQNQLPSDIAQEFTALELLAERVQVTMETKE-------KDFKRAKTVrteyvdgVDEVQRWLLQAEVQV 8011
Cdd:pfam05483 631 LNA-----YEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKiseekllEEVEKAKAI-------ADEAVKLQKEIDKRC 698
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320544542 8012 QERSltpTQMKELLQRINHEITAIYErftlvKTNGQLIIENCRNSEEKTL---VQTTIDQLAASLAQVRGWLDEKKQ 8085
Cdd:pfam05483 699 QHKI---AEMVALMEKHKHQYDKIIE-----ERDSELGLYKNKEQEQSSAkaaLEIELSNIKAELLSLKKQLEIEKE 767
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
627-733 |
3.70e-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: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 627 EQERVQKKTFTNWINSYllkRVPPlRIDDLINDLRDGTKLIALLEVLsgeRLPVEKGRVLRRPH--------FLSNANTA 698
Cdd:cd21330 9 EGETREERTFRNWMNSL---GVNP-RVNHLYSDLSDALVIFQLYEKI---KVPVDWNRVNKPPYpklgenmkKLENCNYA 81
|
90 100 110
....*....|....*....|....*....|....*.
gi 320544542 699 LQFLASK-RIKLVNINPADLVDGRPPVVLGLIWTII 733
Cdd:cd21330 82 VELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLM 117
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
9016-9241 |
3.90e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 48.54 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 9016 APVE-------LPAPQVDVEQPVVVATTSP-VHVPTADVV-EPKDSSPTSTTAAVVDVEavvediNEIWPLEHHLKPTNI 9086
Cdd:PRK10263 335 APVEpvtqtppVASVDVPPAQPTVAWQPVPgPQTGEPVIApAPEGYPQQSQYAQPAVQY------NEPLQQPVQPQQPYY 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 9087 DFSQHVEELAAPAAVTAETEASMPVEEIWPTSPETGNSLTLEQYE--------FEPQSPHEESTKSD--LVKPQETEPQV 9156
Cdd:PRK10263 409 APAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQstfapqstYQTEQTYQQPAAQEplYQQPQPVEQQP 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 9157 VAETKPEGITTGSITITKTTTTITSSTEVPE-ETLV---QNVPADEQQPPANKIKTDIQSfleaeqtlAAALKEQSSTPT 9232
Cdd:PRK10263 489 VVEPEPVVEETKPARPPLYYFEEVEEKRARErEQLAawyQPIPEPVKEPEPIKSSLKAPS--------VAAVPPVEAAAA 560
|
....*....
gi 320544542 9233 GASVAEDVQ 9241
Cdd:PRK10263 561 VSPLASGVK 569
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4615-4706 |
3.92e-04 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 43.85 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4615 ADSLKSWLDETENALpADIELKTTLDEKRNKLQTYRDILNDINNHQVELGNLQEIAANL----PEKTELVDQIIKDISDR 4690
Cdd:pfam00435 10 ADDLESWIEEKEALL-SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLidegHYASEEIQERLEELNER 88
|
90
....*....|....*.
gi 320544542 4691 FGKLQKRAQNYVERYE 4706
Cdd:pfam00435 89 WEQLLELAAERKQKLE 104
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4178-4273 |
4.05e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 43.86 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4178 YQDILNQTVNWLDQVEKLIHNENPASwtSAQEIRSKLYKYKATNQDINSHKRIVEAVNEKAAALLgSAAPANADEISKAV 4257
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASEDLGK--DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI-EEGHPDAEEIEERL 79
|
90
....*....|....*.
gi 320544542 4258 AEVNKRYDQVGQDCAK 4273
Cdd:smart00150 80 EELNERWEELKELAEE 95
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7758-8042 |
4.24e-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: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7758 LEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKSSHKEIEALSKSI 7837
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7838 ltflgevhkpsaEAIQAKVDKLVEQQAKLNdtlrdkeqqvskdleeieqvfRRISQLQDKLNALHEQLQSVHvydehiAQ 7917
Cdd:COG4913 695 ------------EELEAELEELEEELDELK---------------------GEIGRLEKELEQAEEELDELQ------DR 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7918 TEQLLITLNSQVQQAAEEsKLLVAQTTAHYQAKQNQLPSDIAQEFTALELLAERVQVTMETKEKDFK-RAKTVRTEyVDG 7996
Cdd:COG4913 736 LEAAEDLARLELRALLEE-RFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPaETADLDAD-LES 813
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 320544542 7997 VDEVQRWL--LQAE--VQVQER------SLTPTQMKELLQRINHEITAIYERFTLV 8042
Cdd:COG4913 814 LPEYLALLdrLEEDglPEYEERfkellnENSIEFVADLLSKLRRAIREIKERIDPL 869
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
10786-11346 |
4.31e-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: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10786 DFMMELIRVHGQVdyERLRKATERLEGLAGD------LHNREQLIDELKGAAKPLIescDVQIVEQIESAVQEAVVAWND 10859
Cdd:COG4913 232 EHFDDLERAHEAL--EDAREQIELLEPIRELaeryaaARERLAELEYLRAALRLWF---AQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10860 TSENLQQLRTRYQRAVELWDKYRNASAAVKNsidqqmDAVKSLEQPLDALQHAkvcqdnLTTQNDRILELRDIVAKIAAD 10939
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERE------LEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10940 VGLDASAL------MQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVT-LAK------AYFNNVQQDISREAP 11006
Cdd:COG4913 375 LPASAEEFaalraeAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAsLERrksnipARLLALRDALAEALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11007 Q--------------NPKESEEQLAALRAhLQTLART----EEQLRQ---------LKERHQNSEVAPSVASS-----DD 11054
Cdd:COG4913 455 LdeaelpfvgelievRPEEERWRGAIERV-LGGFALTllvpPEHYAAalrwvnrlhLRGRLVYERVRTGLPDPerprlDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11055 DGILEVLAlwqkiFQDT-FQEYhrLSTRLARSQNssealrlwrqylqhvqsFLSCAIPEDyssLREQQQlcAIHQNLLIS 11133
Cdd:COG4913 534 DSLAGKLD-----FKPHpFRAW--LEAELGRRFD-----------------YVCVDSPEE---LRRHPR--AITRAGQVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11134 QQSVLSETPLESELSEQY-------KALtnlhnETLSRIMQrngELERRVSGWNAYRQQLAALLDWLRQREAERNALQLR 11206
Cdd:COG4913 585 GNGTRHEKDDRRRIRSRYvlgfdnrAKL-----AALEAELA---ELEEELAEAEERLEALEAELDALQERREALQRLAEY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11207 YIHLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHcdDALATAMRMEQASIGQRISNLRAALKTWQGFLQRVTQ 11286
Cdd:COG4913 657 SWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEEL--EAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11287 LSESYEQRVnQLQQEFGAAQKLLDANseslptQPAAIEQLLGSLRAQRVQLGAQVSALES 11346
Cdd:COG4913 735 RLEAAEDLA-RLELRALLEERFAAAL------GDAVERELRENLEERIDALRARLNRAEE 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
11215-11816 |
4.33e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11215 HLKHRLDAMIQQLDQGEQQSKALQEQQQELARhcddalatamrmeqasIGQRISNLRAALKTWQGFLQRVTQLSESYEQr 11294
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEE----------------VLREINEISSELPELREELEKLEKEVKELEE- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11295 vnqLQQEFGAAQKLLdansESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELKECISPHdMKTIRQRNWLLw 11374
Cdd:PRK03918 236 ---LKEEIEELEKEL----ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY-IKLSEFYEEYL- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11375 QQHADLDYQLANL---INSIEERLSLLSNYQIRYDRISQWLQRLEQRVEKdadvtamtnPEQAAKQLEQQVNSELQLRDK 11451
Cdd:PRK03918 307 DELREIEKRLSRLeeeINGIEERIKELEEKEERLEELKKKLKELEKRLEE---------LEERHELYEEAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11452 EREWLLSTSRELLTLYSEPEVR-SQVQQQSDSLIDRWQRLKYLAKQKATKIGELKMT---------LLRLEERIALIRAW 11521
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAkEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrELTEEHRKELLEEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11522 LFEVESqldkplnfesytpnvIEAKLKEHEQIQRSIEhhssnvgEVLNLVEMLLNDADSWRTQVNtsgLAASAQNLEQRW 11601
Cdd:PRK03918 458 TAELKR---------------IEKELKEIEEKERKLR-------KELRELEKVLKKESELIKLKE---LAEQLKELEEKL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11602 KNVCSQSAERKARILTiwNLLQQLIKLTAEHKNwLGKQESQIAGFERDQKS--HSKHKLEERQMELRAKLEELESQSVN- 11678
Cdd:PRK03918 513 KKYNLEELEKKAEEYE--KLKEKLIKLKGEIKS-LKKELEKLEELKKKLAEleKKLDELEEELAELLKELEELGFESVEe 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11679 ----LRQLEQIYAKLAMSAGVEPEniqkltlptkvmvsmWRQLTPRCHALLDAIDKDAKLMREFNNAQLEATNSLNAIQK 11754
Cdd:PRK03918 590 leerLKELEPFYNEYLELKDAEKE---------------LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320544542 11755 AL--EQLPSAENQQTSKA-EPKAVLQRLESLEKKLQDAQqhvQQADNLAQEAKTRTKQQPQLKQL 11816
Cdd:PRK03918 655 KYseEEYEELREEYLELSrELAGLRAELEELEKRREEIK---KTLEKLKEELEEREKAKKELEKL 716
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
6870-7067 |
4.71e-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: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6870 KIQELKGKAAQVAEVISNLDGQQ--VEEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEEL- 6946
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELa 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6947 -------------------------QAPKPLGYTPKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELEpvEYSQ 7001
Cdd:COG4942 108 ellralyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA--ELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320544542 7002 LESALRNLNTENRNLSGVLKAELDRALEASKARKSLENDLDKARQWLKTKISEVRKLPVYHPLTSA 7067
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
7782-7944 |
4.74e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.00 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7782 WEKALGRLEDKFRNVDPTVRSRRH-LEDTKNAIQELREESNQLKSSHK---EIEAL--SKSILTFLGEVHKPSAEAIQAK 7855
Cdd:PRK05771 84 LEELIKDVEEELEKIEKEIKELEEeISELENEIKELEQEIERLEPWGNfdlDLSLLlgFKYVSVFVGTVPEDKLEELKLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7856 VDKLVEQ---QAKLND-----TLRDKEQQVSKDL-----------------EEIEQVFRRISQLQDKLNALHEQLQSV-- 7908
Cdd:PRK05771 164 SDVENVEyisTDKGYVyvvvvVLKELSDEVEEELkklgferleleeegtpsELIREIKEELEEIEKERESLLEELKELak 243
|
170 180 190
....*....|....*....|....*....|....*.
gi 320544542 7909 HVYDEHIAQTEQLLItlnsQVQQAAEESKLLVAQTT 7944
Cdd:PRK05771 244 KYLEELLALYEYLEI----ELERAEALSKFLKTDKT 275
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
632-744 |
5.02e-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: 44.66 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 632 QKKTFTNWINSYL-----LKRVPPLR--IDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFL--SNANTALQFL 702
Cdd:cd21325 25 EKYAFVNWINKALendpdCRHVIPMNpnTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFIiqENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 320544542 703 ASKRIKLVNINPADLVDGRPPVVLGLIWTII---LYFQIEEnSRN 744
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIkigLFADIEL-SRN 148
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
10949-11200 |
5.18e-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: 47.07 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10949 QGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVtlakayfNNVQQDIsreapqnpKESEEQLAALRAHLQTLAR 11028
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------AALARRI--------RALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11029 TEEQLRQLKERHQNsEVAPSVASSDDDGILEVLALwqkifqdtfqeyhrlstrLARSQNSSEALRLwRQYLQHVQSFLSC 11108
Cdd:COG4942 91 EIAELRAELEAQKE-ELAELLRALYRLGRQPPLAL------------------LLSPEDFLDAVRR-LQYLKYLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11109 AIpedySSLREQQQLCAIHQNLLISQQSVLSEtpLESELSEQYKALTNL---HNETLSRIMQRNGELERRVSGWNAYRQQ 11185
Cdd:COG4942 151 QA----EELRADLAELAALRAELEAERAELEA--LLAELEEERAALEALkaeRQKLLARLEKELAELAAELAELQQEAEE 224
|
250
....*....|....*
gi 320544542 11186 LAALLDWLRQREAER 11200
Cdd:COG4942 225 LEALIARLEAEAAAA 239
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
7433-8234 |
5.35e-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: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7433 LQNLRKAVESQRQK---HQLQLESHKKMAAELSEILDWLHSHEGAAKSRPLLDRdpeSVERELQKHQSLSQDIESYLNKF 7509
Cdd:TIGR00606 188 LETLRQVRQTQGQKvqeHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVK---SYENELDPLKNRLKEIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7510 NKINDGVKT----------------------EIGMPSSLLEMLSEGRSLVASLPHELEEREKYLKNNRDSRLEYMQLVAK 7567
Cdd:TIGR00606 265 MKLDNEIKAlksrkkqmekdnselelkmekvFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7568 FNDWVHEAELRLQNSQ-HGIDYEHLVQDLDEHKIFFGNEapirnlvHKQIQEAADKIWSSLNNYEQSELSAELAQFQTKL 7646
Cdd:TIGR00606 345 LLVEQGRLQLQADRHQeHIRARDSLIQSLATRLELDGFE-------RGPFSERQIKNFHTLVIERQEDEAKTAAQLCADL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7647 TNTLANAKTQQSELE-KEAERWREYQQSIDRVKATIERTKFVDEPVQNLAGLHFNIQKLSHAIGNVQS------QNSDLT 7719
Cdd:TIGR00606 418 QSKERLKQEQADEIRdEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERelskaeKNSLTE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7720 LVNQQAQSL-IRQADA-RNRQLIEQDNAGLNRSWQDLVRSL----------EQRRDNLQQLAEHWDG----------FEN 7777
Cdd:TIGR00606 498 TLKKEVKSLqNEKADLdRKLRKLDQEMEQLNHHTTTRTQMEmltkdkmdkdEQIRKIKSRHSDELTSllgyfpnkkqLED 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7778 SLHAWEKALGRLEDKFRNVDPTVRSrrhLEDTKNAIQelreesNQLKSSHKEIEALSKSILTFLG-EVHKPSAEAIQAKV 7856
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELAS---LEQNKNHIN------NELESKEEQLSSYEDKLFDVCGsQDEESDLERLKEEI 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7857 DKLVEQQAKLNDTLRDKEQQVSKDLEEIEQ---VFRRISQLQDKLNALHEQLQS-VHVYDEHIAQTEQLLitlnSQVQQA 7932
Cdd:TIGR00606 649 EKSSKQRAMLAGATAVYSQFITQLTDENQSccpVCQRVFQTEAELQEFISDLQSkLRLAPDKLKSTESEL----KKKEKR 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7933 AEESKLLVAQTTAHYQAKQNQLP----------SDIAQEFTALELLAERVQVTMETKE--KDFKRAKTVRTEYVDGVDEV 8000
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPelrnklqkvnRDIQRLKNDIEEQETLLGTIMPEEEsaKVCLTDVTIMERFQMELKDV 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8001 QRWLLQ--AEVQVQERSLTPTQMKELLQRINHEITAIYERFTLvktNGQLIIENcrnSEEKTLVQTTIDQLAASLAQVRG 8078
Cdd:TIGR00606 805 ERKIAQqaAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIEL---NRKLIQDQ---QEQIQHLKSKTNELKSEKLQIGT 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8079 WLDEKKQAVGDSLDAWTRFMNLYQIVmswaSEKRNfidQTIELRTLPEARNKLNDYVTSVK--SIKPIVKHLSEMDKELE 8156
Cdd:TIGR00606 879 NLQRRQQFEEQLVELSTEVQSLIREI----KDAKE---QDSPLETFLEKDQQEKEELISSKetSNKKAQDKVNDIKEKVK 951
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320544542 8157 HIgqVTTVGDLKDKLQEA-EDAKISVEAVLLERNSLLQEaceewdqCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQL 8234
Cdd:TIGR00606 952 NI--HGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEE-------CEKHQEKINEDMRLMRQDIDTQKIQERWLQDNL 1021
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
5866-6614 |
5.59e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.91 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5866 AAKIQEDTEALKQDFDKLL---VDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDvepSVKTS-DEFLNDLSEKRAALEK 5941
Cdd:pfam12128 243 FTKLQQEFNTLESAELRLShlhFGYKSDETLIASRQEERQETSAELNQLLRTLDD---QWKEKrDELNGELSAADAAVAK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5942 FRviqrdinghnDIVEKINQRLKEDNSLDLKDFQPGLTKFDDLQTQVNKIIESLENQVNSHEKYKQAYNelqdwlRRTRI 6021
Cdd:pfam12128 320 DR----------SELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYN------RRRSK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6022 EVEQCADchgekdqvesRLNRLGDIQSSSLEGKALLEACEElsqAVIATSGSEGQDNVAQEIKHLTSEWETLQTISRDAR 6101
Cdd:pfam12128 384 IKEQNNR----------DIAGIKDKLAKIREARDRQLAVAE---DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6102 SSLESCLAAWQTFLQKFNKINLwIETMNKRVTKSQEGENKTPEDLVNAKKLLEEVLaekdnvEDLND-NCELLMEQSACT 6180
Cdd:pfam12128 451 LRLNQATATPELLLQLENFDER-IERAREEQEAANAEVERLQSELRQARKRRDQAS------EALRQaSRRLEERQSALD 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6181 RIRDQTIETQANYTKLL-TSAQGLVAKIEKNLSdhTEFLnYKKEMDAwiekaqqVLDDCSTDGDAAIIAQKLDT----VN 6255
Cdd:pfam12128 524 ELELQLFPQAGTLLHFLrKEAPDWEQSIGKVIS--PELL-HRTDLDP-------EVWDGSVGGELNLYGVKLDLkridVP 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6256 SLASRLPEGQHLLALVQDAYSKASnitpeDKQEKLRELMTKVREDWDALGLAVKQKLSDLKQA---QNRWNDFAAN-KDK 6331
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAR-----EKQAAAEEQLVQANGELEKASREETFARTALKNArldLRRLFDEKQSeKDK 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6332 LEKWLNE-----TETTLKVAPETKGELSEMKTLLERYKTLSNELKLKGNELEQLQSEARDlgtevDAVNRLQSRCDKLKN 6406
Cdd:pfam12128 669 KNKALAErkdsaNERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALD-----AQLALLKAAIAARRS 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6407 DCSAHITALEQEmfdynaYHQSLQDvekwlLQISFQLMAHNSLFISNREQTQEQIKQ--HEAL----------LVEIQKY 6474
Cdd:pfam12128 744 GAKAELKALETW------YKRDLAS-----LGVDPDVIAKLKREIRTLERKIERIAVrrQEVLryfdwyqetwLQRRPRL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6475 QTNLDDLNAKG---QAQIKRYESSTPAIRPTVESQLKNIQDSynsllqtsvqiKNRLLESLAKfqeyedtLDSIMRNLET 6551
Cdd:pfam12128 813 ATQLSNIERAIselQQQLARLIADTKLRRAKLEMERKASEKQ-----------QVRLSENLRG-------LRCEMSKLAT 874
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320544542 6552 YepiiqtELDAPATSLEL-AQNQLRCAQEMQNKLNNEKSRLAAAVQACEAATASISRpSSPLET 6614
Cdd:pfam12128 875 L------KEDANSEQAQGsIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADHSG-SGLAET 931
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3532-4198 |
6.26e-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: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3532 KLKQLCSKWDEFDTIIEELDnwMKNVEAVVKNQNLKSTAEAKNAHLK----QLQDISKDIERRGAAINELmdQGREIEGE 3607
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELE--EEIEELQKELYALANEISRLEQQKQilreRLANLERQLEELEAQLEEL--ESKLDELA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3608 TDLNL---KLSRLNTRYQTLKNLCKESIAKYVNYV-------KDHESFDKDFDSFKQN-----------------LQSSV 3660
Cdd:TIGR02168 337 EELAEleeKLEELKEELESLEAELEELEAELEELEsrleeleEQLETLRSKVAQLELQiaslnneierlearlerLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3661 DELAKTNEIVGDQSVLQDQQNKLREMSDKRILDSTLFEGLIDRGEKLyghtspegrEIIRQQLRALRTLWDNYTDDLNSA 3740
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL---------EELREELEEAEQALDAAERELAQL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3741 TQKIDQCLLQFNEFSIAQDQLtKWLKDVDKAMQSHTEPKTTLQEKRAQLQNHKLLHQEITTHNVLVDNVcDKAQILVDQI 3820
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEGV-KALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENL-NAAKKAIAFL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3821 KDNSLN----VYLTSIKQlfQSIVQKSDEILHNLDDCVQKHNELNNALSSAKTWISNEKAKLLECDDaygekadikrkIE 3896
Cdd:TIGR02168 566 KQNELGrvtfLPLDSIKG--TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDD-----------LD 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3897 TLGQLAQNKPQAMKIISDIRDLFEKVKATT--SEKGNEVL---DKEIEELETTMKSHFDDIEGIEGKQKDVLAQWDKFEK 3971
Cdd:TIGR02168 633 NALELAKKLRPGYRIVTLDGDLVRPGGVITggSAKTNSSIlerRREIEELEEKIEELEEKIAELEKALAELRKELEELEE 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3972 ALEELTKWCRSAEAVFREQQLQ-STLHEKVEQLEKYKIQR-----ELILQKEKEIDAFGDAAHALLNncGADRLKTLTTQ 4045
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDlARLEAEVEQLEERIAQLskeltELEAEIEELEERLEEAEEELAE--AEAEIEELEAQ 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4046 ITNRYQLLQVLSKEVVNRWSNLVDDHQFYQDKYNEVDLWLQPIES--QMAKVLLDEPTQSSNILQVLLSEKEQAESLFAA 4123
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAteRRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320544542 4124 LNAAGEKALPEtstqgREKIRKDLRDIRDRWDKLDEGIRNLEKRQEAQGVQLSSYQDILNQTVNWLDQVEKLIHN 4198
Cdd:TIGR02168 871 LESELEALLNE-----RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7721-8360 |
6.43e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7721 VNQQAQSLIRQADArnrqlieqdnAglnRSWQDLVRSLEQRRDNLQQLaeHWDGFENSLHAWEKALGRLEDKFRnvdptv 7800
Cdd:COG1196 198 LERQLEPLERQAEK----------A---ERYRELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELE------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7801 RSRRHLEDTKNAIQELREESNQLKsshKEIEALSKSIltflgevhkpsaEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKD 7880
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELE---LELEEAQAEE------------YELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7881 LEEIEQVFRRISQLQDKLNALHEQLQSVhvyDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAHYQAKQNQLpsdiaQ 7960
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEA---EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-----R 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7961 EFTALELLAERVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELLQRINHEITAIYERFT 8040
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8041 LVKTNGQLIIEncRNSEEKTLVQTTIDQLAASLAQVRGWLDEKKQA----VGDSLDAWTRFMNLYQIVMSWASEKRNFID 8116
Cdd:COG1196 474 LLEAALAELLE--ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrgLAGAVAVLIGVEAAYEAALEAALAAALQNI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8117 QTIELRTLPEARNKLNDYVTSVKSIKPIVK-HLSEMDKELEHIGQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEA 8195
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8196 CEEWDqcERKIKDIRSWHEKTKQGLDSSQQQkkplrDQLGFCEKTLADINVQKTKLRLSIEKLEVHfrngmggdpRLSEN 8275
Cdd:COG1196 632 LEAAL--RRAVTLAGRLREVTLEGEGGSAGG-----SLTGGSRRELLAALLEAEAELEELAERLAE---------EELEL 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8276 VDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRLVMAPTYLPHDRERALAEQQdlitQELDE 8355
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE----RELER 771
|
....*
gi 320544542 8356 LLQSL 8360
Cdd:COG1196 772 LEREI 776
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6425-6528 |
6.79e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 43.09 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6425 YHQSLQDVEKWLLQISFQLMAHNslFISNREQTQEQIKQHEALLVEIQKYQTNLDDLNAKGQAQIKRYESSTPAIrptvE 6504
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASED--LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEI----E 76
|
90 100
....*....|....*....|....
gi 320544542 6505 SQLKNIQDSYNSLLQTSVQIKNRL 6528
Cdd:smart00150 77 ERLEELNERWEELKELAEERRQKL 100
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5585-5786 |
7.09e-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: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5585 NEFATWLRNAKERLSKcSEPTGDKQALAEKTHQLKILQGELPEGAQKLKNALEQGEiACRSAEPEDCEIIEQEVALLQEE 5664
Cdd:cd00176 10 DELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGE-QLIEEGHPDAEEIQERLEELNQR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5665 FDAYREALNKAKDYLEVGIVKWSDYQDQyTEALEWLSKTEALVQSYNKLQDsLIQKKVVLEQFQGHLQTLFDWQKTLDDL 5744
Cdd:cd00176 88 WEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 320544542 5745 NMKAQVLLETC---SDTRISNAIMQLTTKYNALLTLAKEVMRRLE 5786
Cdd:cd00176 166 NELAEELLEEGhpdADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
10800-11469 |
8.09e-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: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10800 YERLRKATERLEGLAGDLHNREQLIDELKGAAKPLIEScDVQIVEQIEsAVQEAVVAWNdtsenlQQLRTryqraveLWD 10879
Cdd:pfam12128 233 IAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSD-ETLIASRQE-ERQETSAELN------QLLRT-------LDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10880 KYRNASAAVKNSIDQQMDAVKSLEQPLDAL--QHAKVCQDNLTTqndrilelrdivakIAADvgLDASALMQGELDALGQ 10957
Cdd:pfam12128 298 QWKEKRDELNGELSAADAAVAKDRSELEALedQHGAFLDADIET--------------AAAD--QEQLPSWQSELENLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10958 RLaeckDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREApqnpkeSEEQLAALRAHLQTL-----ARTEEQ 11032
Cdd:pfam12128 362 RL----KALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREA------RDRQLAVAEDDLQALeselrEQLEAG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11033 LRQLKERHQNSEVAPSVASS--DDDGILEVLALWQKIFQD-----------TFQEYHRLSTRLA----RSQNSSEALRLW 11095
Cdd:pfam12128 432 KLEFNEEEYRLKSRLGELKLrlNQATATPELLLQLENFDErierareeqeaANAEVERLQSELRqarkRRDQASEALRQA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11096 RQYLQHVQSFLSCA----IPEDYS---SLREQQQLCAIHQNLLISQQsVLSETPLESELSE-QYKALTNLHNETLsrimq 11167
Cdd:pfam12128 512 SRRLEERQSALDELelqlFPQAGTllhFLRKEAPDWEQSIGKVISPE-LLHRTDLDPEVWDgSVGGELNLYGVKL----- 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11168 rngELER-RVSGWNAYRQQLAALLDWL---------RQREAERNALQLRyihlKRVPHLKHRLDAMIQQLDQGEQQSKAL 11237
Cdd:pfam12128 586 ---DLKRiDVPEWAASEEELRERLDKAeealqsareKQAAAEEQLVQAN----GELEKASREETFARTALKNARLDLRRL 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11238 QEQQQELARHCDDALATAMRMEQASIGQRISNLRAALKTWQGFLQRVT-QLSESYEQRVNQLQQEFGAAQklldansesl 11316
Cdd:pfam12128 659 FDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKeQKREARTEKQAYWQVVEGALD---------- 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11317 ptqpAAIEQLLGSLRAQRVQLGAQVSALEsltvtqEELKECISPHDMKTIRQrnwllwqqhADLDYQLANLINSIEerls 11396
Cdd:pfam12128 729 ----AQLALLKAAIAARRSGAKAELKALE------TWYKRDLASLGVDPDVI---------AKLKREIRTLERKIE---- 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11397 llsnyQIRYDR--ISQWLQRLEQR--VEKDADVTAMTNPEQAAKQLEQQV---NSELQLRDKEREWLLSTSRELLTLYSE 11469
Cdd:pfam12128 786 -----RIAVRRqeVLRYFDWYQETwlQRRPRLATQLSNIERAISELQQQLarlIADTKLRRAKLEMERKASEKQQVRLSE 860
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
783-876 |
8.69e-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: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 783 LLNWVTNALPKDSG--VEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQ----RLETAFDVAEsKLGIAKLLD 856
Cdd:cd21218 15 LLRWVNYHLKKAGPtkKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEdlekRAEKVLQAAE-KLGCKYFLT 93
|
90 100
....*....|....*....|
gi 320544542 857 AEdvDVPKPDEKSIMTYVAQ 876
Cdd:cd21218 94 PE--DIVSGNPRLNLAFVAT 111
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
10969-11413 |
9.10e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 46.89 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10969 LANVAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPS 11048
Cdd:COG4995 8 ALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11049 VASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLCAIHQ 11128
Cdd:COG4995 88 ALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11129 NLLISQQSVLSETPLESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYI 11208
Cdd:COG4995 168 LALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11209 HLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALATAMRMEQASIGQRISNLRAALKTWQGFLQRVTQLS 11288
Cdd:COG4995 248 AALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11289 ESYEQRVNQLQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELKECISPHDMKTIRQ 11368
Cdd:COG4995 328 AALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQ 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 320544542 11369 RNWLLWQQHADLDYQLANLInsIEERLSLLSNYQIRYDRISQWLQ 11413
Cdd:COG4995 408 LLRLLLAALALLLALAAYAA--ARLALLALIEYIILPDRLYAFVQ 450
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1206-1393 |
1.01e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 45.13 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 1206 EEWLQLAEQKVNQSEDERL------------DFFQDIPVWKDKFDALASSANYLIASCEEPiAQQLRQRHGALSERFERL 1273
Cdd:cd00176 13 EAWLSEKEELLSSTDYGDDlesveallkkheALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQERLEELNQRWEEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 1274 FANTKQYMHAGDIIRSRQEYKSGIEQLSRWLRGAESVLDQRQVLGNSEQVKEYGQQLQQLASEIDDNEELFKTISRNFQS 1353
Cdd:cd00176 92 RELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 320544542 1354 LIQDLSRDEVDKMMKLLKQEKESLVRIRAQLPAKLHLFHQ 1393
Cdd:cd00176 172 LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
7692-7908 |
1.06e-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: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7692 QNLAGLHFNIQKLSHAIGNVQSQ----NSDLTLVNQQAQSLIRQADARNRQL--IEQDNAGLNRSWQDLVRSLEQRRDNL 7765
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEekalLKQLAALERRIAALARRIRALEQELaaLEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7766 QQLAEHWdgFENSLHAWEKALGRLEDKFRNVdptvrsrRHLEDTKNAIQELREESNQLKSSHKEIEALSKSILTflgevh 7845
Cdd:COG4942 107 AELLRAL--YRLGRQPPLALLLSPEDFLDAV-------RRLQYLKYLAPARREQAEELRADLAELAALRAELEA------ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320544542 7846 kpSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSV 7908
Cdd:COG4942 172 --ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
8146-8589 |
1.07e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8146 KHLSEMDKELEHIG-QVTTVGDLKDKLQEAEDAKISVEAVLLERNSL-LQEACEEWDQCERKIKDIRSWHEKTKQGLDSS 8223
Cdd:COG4913 235 DDLERAHEALEDAReQIELLEPIRELAERYAAARERLAELEYLRAALrLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8224 QQQKKPLRDQLGFCEKTLADINVQ-KTKLRLSIEKLEVHFRngmggdpRLSENVDDLVRVLDGLGELVKAKSQSLEQTLA 8302
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELE-------ERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8303 QIDVYQQQMQSLRQRIIQEEQQLRlvmaptylphDRERALAEQQDLITQELDELLQSLSSVEDGIANMN----------- 8371
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAE----------AALRDLRRELRELEAEIASLERRKSNIPARLLALRdalaealglde 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8372 -------------------QSSLDGMLHGLKLiqsNLEV---HERDAIELKNQ-----------AKKLPTDPATERLLND 8418
Cdd:COG4913 458 aelpfvgelievrpeeerwRGAIERVLGGFAL---TLLVppeHYAAALRWVNRlhlrgrlvyerVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8419 TV--------------------DRIDLL-------LRRTQQGIT---MI-ANAMHGQKKRQQEIDEY-------QQHLLE 8460
Cdd:COG4913 535 SLagkldfkphpfrawleaelgRRFDYVcvdspeeLRRHPRAITragQVkGNGTRHEKDDRRRIRSRyvlgfdnRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8461 LEQWIIEVSAELASFEPTSDSSTDEQvlkSQVERSQQLLRTLKDRQQSMEDLVEQTRQLQ-----------SHPDVSPLA 8529
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAEL---DALQERREALQRLAEYSWDEIDVASAEREIAeleaelerldaSSDDLAALE 691
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8530 DTLmEQLQSIITILREQVTVATKRIFTIEKRIVDLRKAKsEEAQRQRVLADSLIKPPTEA 8589
Cdd:COG4913 692 EQL-EELEAELEELEEELDELKGEIGRLEKELEQAEEEL-DELQDRLEAAEDLARLELRA 749
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
632-733 |
1.22e-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: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 632 QKKTFTNWINSYL-----LKRVPPL--RIDDLINDLRDGTKLIALLEV-LSG---ERlPVEKGRVLRRphFLSNANTALQ 700
Cdd:cd21293 2 EKGSYVDHINRYLgddpfLKQFLPIdpSTNDLFDLVKDGVLLCKLINVaVPGtidER-AINTKKVLNP--WERNENHTLC 78
|
90 100 110
....*....|....*....|....*....|....*
gi 320544542 701 FLASKRI--KLVNINPADLVDGRPPVVLGLIWTII 733
Cdd:cd21293 79 LNSAKAIgcSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
3539-3630 |
1.47e-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: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3539 KWDEFDTIIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINELMDQGREI-----EGETDLNLK 3613
Cdd:pfam00435 2 LLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLideghYASEEIQER 81
|
90
....*....|....*..
gi 320544542 3614 LSRLNTRYQTLKNLCKE 3630
Cdd:pfam00435 82 LEELNERWEQLLELAAE 98
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6661-7496 |
1.63e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6661 EIQVELSDVNEALLDPIAHERVKNYRRivrLNSahvgKLNELVAKVQSHLGGLTASVSELEQQQKQRAELQDwvkkqqss 6740
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEELREELEE---LQE----ELKEAEEELEELTAELQELEEKLEELRLEVSELEE-------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6741 vsdwmmrpcklRPEAAQQELvsmNDLLNSIGDKRSQLMLemtgsLGDEDTDLDDNIDKLESELMDAIAKKQAgqnvidgY 6820
Cdd:TIGR02168 282 -----------EIEELQKEL---YALANEISRLEQQKQI-----LRERLANLERQLEELEAQLEELESKLDE-------L 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6821 RQGMADVQNWFDTLIKRMDvldrgsglNCAQKMAAINEIKNEYELQGHPKIQELKGKAAQVAEVisNLDGQQVEEQMKSL 6900
Cdd:TIGR02168 336 AEELAELEEKLEELKEELE--------SLEAELEELEAELEELESRLEELEEQLETLRSKVAQL--ELQIASLNNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6901 DRRFADLGKRIDR-KSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEELQApkplgytpkDAEARQQKIKSLMKDAEAKQSL 6979
Cdd:TIGR02168 406 EARLERLEDRRERlQQEIEELLKKLEEAELKELQAELEELEEELEELQE---------ELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6980 ADVLEKRVANMQQELEpveysQLESALRNLNTENRNLSGVLKAELDRALE----------ASKARKSLENDLDKARQWLK 7049
Cdd:TIGR02168 477 LDAAERELAQLQARLD-----SLERLQENLEGFSEGVKALLKNQSGLSGIlgvlselisvDEGYEAAIEAALGGRLQAVV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7050 TKISEVRKLPVYHPLTSAEIEKKIQENRKYDDDAKQFNDSVLTDVQRQAANIMKDCDDADKA---ALQQILDE--IAADY 7124
Cdd:TIGR02168 552 VENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkALSYLLGGvlVVDDL 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7125 QT-LKDESSKRGK----SLDDLL---QGRKAFEDSMKNMGDWLNEMETAtegELRTTsLPVLEEQLAHYKKLLSDAENKG 7196
Cdd:TIGR02168 632 DNaLELAKKLRPGyrivTLDGDLvrpGGVITGGSAKTNSSILERRREIE---ELEEK-IEELEEKIAELEKALAELRKEL 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7197 GLINDVSEQGKSILPTLSnadklklnDDIKNMKDRYGRIKNTIDDRVNALGDHIKKYKDAKSRLAECSQFLGNIQQKLRE 7276
Cdd:TIGR02168 708 EELEEELEQLRKELEELS--------RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7277 LNRPIGS---RIEDVQDLLGAYEGILKELKDSKSKMGDMQMDDLPELQSILAQQDDMIKLIEDqlahlrqllllREQFIA 7353
Cdd:TIGR02168 780 AEAEIEEleaQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED-----------LEEQIE 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7354 LINEIIAfimKYTDVIIDIENSPDSLEDKINKYDDVIVKIQEcegVLASANDKGQKIASEGNAADKnsiteQLQSLKNQL 7433
Cdd:TIGR02168 849 ELSEDIE---SLAAEIEELEELIEELESELEALLNERASLEE---ALALLRSELEELSEELRELES-----KRSELRREL 917
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320544542 7434 QNLRKAVEsqrqKHQLQLESHKKMAAELSEIL--DWLHSHEGAAKSRPLLDRDPESVERELQKHQ 7496
Cdd:TIGR02168 918 EELREKLA----QLELRLEGLEVRIDNLQERLseEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
632-733 |
1.77e-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: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 632 QKKTFTNWINSYL-----LKRVPPL--RIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFL--SNANTALQFL 702
Cdd:cd21324 25 EKYAFVNWINKALendpdCKHVIPMnpNTDDLFKAVGDGIVLCKMINFSVPDTIDERTINKKKLTPFTiqENLNLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 320544542 703 ASKRIKLVNINPADLVDGRPPVVLGLIWTII 733
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 135
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
3071-3203 |
1.81e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 44.36 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3071 ESPQNLAELTSDAELLRKDMQALQDSFDQIKGILDENVDLWSQYEQSnEQISNWLRDVEGRVKAETSSQvNLSEVPQKLQ 3150
Cdd:cd00176 69 EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGK-DLESVEELLK 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 320544542 3151 ELSILQQDVLAHEPIINNLEQTSQQLIEKNPEAR---IGQFVTHLVQRYQAVSKAL 3203
Cdd:cd00176 147 KHKELEEELEAHEPRLKSLNELAEELLEEGHPDAdeeIEEKLEELNERWEELLELA 202
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
5851-6571 |
1.85e-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: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5851 LELKEKVIMNTEQNGAAKIQEDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDVEPSVKTSDEFLN 5930
Cdd:TIGR00618 181 LALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5931 DLSEKRAALEKFrviQRDINGHNDIVEKINQRLKEDNSLDL--------KDFQPGLTKFDDLQTQVNKIIESLENQVNSH 6002
Cdd:TIGR00618 261 LLKQLRARIEEL---RAQEAVLEETQERINRARKAAPLAAHikavtqieQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6003 EKYKQAYNELQDWLR---RTRIEVEQCADCHGEKDQVESRLNRLGDIQSSslegkalLEACEELSQavIATSGSEGQDNV 6079
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSqeiHIRDAHEVATSIREISCQQHTLTQHIHTLQQQ-------KTTLTQKLQ--SLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6080 AQEIKHLTSEWETLQTISRDARSSLESCLaAWQTFLQKFNKINLWIETMNKRVTKSQEGENKTPEDLVNAKKLLEEVLAE 6159
Cdd:TIGR00618 409 QATIDTRTSAFRDLQGQLAHAKKQQELQQ-RYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETR 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6160 KDNVEDLNDNCELLMEQSACTRIRDQTIETQANY-----TKLLTSAQGLVAKIEKNLSD----HTEFLNYKKEMDAWIEK 6230
Cdd:TIGR00618 488 KKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDnpgplTRRMQRGEQTYAQLETSEEDvyhqLTSERKQRASLKEQMQE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6231 AQQvlddcstdgDAAIIAQKldtVNSLASRLPEGQHLLALVQ---DAYSKASNITPEDKQEKLRELMTKVREDWDALGLA 6307
Cdd:TIGR00618 568 IQQ---------SFSILTQC---DNRSKEDIPNLQNITVRLQdltEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6308 VKQK-LSDLKQAQNRWNDFAANKDKLEKWLNETETTLKVAPETKGELSEMKTLLEryktlsnELKLKGNELEQLQSEARD 6386
Cdd:TIGR00618 636 QCSQeLALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKE-------QLTYWKEMLAQCQTLLRE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6387 LGTEVDAVNRLQsrcDKLKNDCSAHITALEQEMFDYNAYHQSLQDVEKWLLQisfqlmahnslfisnrEQTQEQIKQHEA 6466
Cdd:TIGR00618 709 LETHIEEYDREF---NEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK----------------ARTEAHFNNNEE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6467 LLVEIQKyQTNLDDLNAKGQAQIKRYESSTPAIRPTVESQLKNIQDSYNSLLQTSVQIKNRLLESLAKFQEYEDTLDSIM 6546
Cdd:TIGR00618 770 VTAALQT-GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEIT 848
|
730 740
....*....|....*....|....*
gi 320544542 6547 RNLETYEPIIQTELDAPATSLELAQ 6571
Cdd:TIGR00618 849 HQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
7847-7960 |
2.11e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7847 PSAEAIQAKVDKLVEQ----------QAKLNDTLR--DKEQQVSKDLEE----IEQVFRRISQLQDKLNALHEQLQSVHV 7910
Cdd:PRK11281 36 PTEADVQAQLDALNKQklleaedklvQQDLEQTLAllDKIDRQKEETEQlkqqLAQAPAKLRQAQAELEALKDDNDEETR 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 320544542 7911 YD---EHIAQTEQLLITLNSQVQQA----AEESKLLVAQTTAHYQAkQNQLPSDIAQ 7960
Cdd:PRK11281 116 ETlstLSLRQLESRLAQTLDQLQNAqndlAEYNSQLVSLQTQPERA-QAALYANSQR 171
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
11220-11446 |
2.22e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.82 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11220 LDAMIQQLDQGEQQSKALQEQQQELarhcDD--ALATAMRMEQASIGQRISNLRAALKTwQGFLQRVTQLSESYEQRVNQ 11297
Cdd:PRK10929 50 LQSALNWLEERKGSLERAKQYQQVI----DNfpKLSAELRQQLNNERDEPRSVPPNMST-DALEQEILQVSSQLLEKSRQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11298 LQQEFGAAQKLLDANSEsLPTQPAA-------IEQLLGSL--------RAQRVQLGAQVSALESLtVTQEELKECISPHD 11362
Cdd:PRK10929 125 AQQEQDRAREISDSLSQ-LPQQQTEarrqlneIERRLQTLgtpntplaQAQLTALQAESAALKAL-VDELELAQLSANNR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11363 MKTIRQRNWLLWQQHADLDYQLANLINSIeerlsllsNYQiRYDRISQWLQRLEQRVEKDADVtamtnPEQAAKQLeqQV 11442
Cdd:PRK10929 203 QELARLRSELAKKRSQQLDAYLQALRNQL--------NSQ-RQREAERALESTELLAEQSGDL-----PKSIVAQF--KI 266
|
....
gi 320544542 11443 NSEL 11446
Cdd:PRK10929 267 NREL 270
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4819-4919 |
2.33e-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: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4819 QHWSEYEQLRDQCLAWIRDTDNNLHAIDLKEDLPKKRAQLDALKALQGDVRAKELEVDNVTEKAQTLLkgpsSNRASGPE 4898
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI----DEGHYASE 76
|
90 100
....*....|....*....|.
gi 320544542 4899 LVTKyqqifhKVKELNNRWQQ 4919
Cdd:pfam00435 77 EIQE------RLEELNERWEQ 91
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
6870-7169 |
2.37e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6870 KIQELKGKAAQVAEVisnldgqqVEEQMKSLDRRFAD-LGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEELQa 6948
Cdd:PTZ00121 1419 KADEAKKKAEEKKKA--------DEAKKKAEEAKKADeAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK- 1489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6949 pkplgytpKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELEPVEYSQLESALRNLNtENRNLSGVLKAE-LDRA 7027
Cdd:PTZ00121 1490 --------KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE-EKKKADELKKAEeLKKA 1560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7028 LEASKARKSLENDLDK---------ARQWLKTKISEVRKLPVYHPLTSAEIEKKIQENRKYDDDAKQfNDSVLTDVQRQA 7098
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKnmalrkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLK 1639
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320544542 7099 ANIMKDCDDADKAALQQILDEIAADYQTLKDESSKRGKSlddllQGRKAFEDSMKNMGDWLNEMETATEGE 7169
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE-----EAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
4311-4495 |
2.43e-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: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4311 DYSGNKAALQARLQKINEIQDALPEGVAKLKSLEDHIEQQASNIPARSKEVMARdLANLHADFEKFGASLSDVKSGLENR 4390
Cdd:cd00176 27 DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER-LEELNQRWEELRELAEERRQRLEEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4391 LQQWNDYEiNLDRLITWLGEAENSLKNYNLKSSFEEKEEQLNGFQSLAQNLRQNEADFDKVKDDTSELVQSS---GETRI 4467
Cdd:cd00176 106 LDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGhpdADEEI 184
|
170 180
....*....|....*....|....*...
gi 320544542 4468 AVNVQQVSSRFQSIQATAKEILKKCEQA 4495
Cdd:cd00176 185 EEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
7558-8371 |
2.65e-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: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7558 RLEYMQLVAKFNDwVHEAELRLQnSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLV---HKQIQEAADKIwsslnNYEQSE 7634
Cdd:pfam12128 240 RPEFTKLQQEFNT-LESAELRLS-HLHFGYKSDETLIASRQEERQETSAELNQLLrtlDDQWKEKRDEL-----NGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7635 LSAELAQFQtkltntlanaktqqSELEKEAERWREYQQS-IDRVKATIERTKFVDEPVQNLAGLHfniQKLSHAIGNVQs 7713
Cdd:pfam12128 313 ADAAVAKDR--------------SELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERL---KALTGKHQDVT- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7714 qnsdltlvnQQAQSLIRQADARNRQLIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHW----DGFENSLHAWEKAL-GR 7788
Cdd:pfam12128 375 ---------AKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELreqlEAGKLEFNEEEYRLkSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7789 LED-KFRNVDPTVRSrrhledtknaiqelrEESNQLKSSHKEIEALSKSIltflgevhkpsaEAIQAKVDKLVEQQAKLn 7867
Cdd:pfam12128 446 LGElKLRLNQATATP---------------ELLLQLENFDERIERAREEQ------------EAANAEVERLQSELRQA- 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7868 DTLRDKEqqvskdLEEIEQVFRRISQLQDKLNALHEQLqsvhvydehIAQTEQLLITLNSQVQQAAEE-----SKLLVAQ 7942
Cdd:pfam12128 498 RKRRDQA------SEALRQASRRLEERQSALDELELQL---------FPQAGTLLHFLRKEAPDWEQSigkviSPELLHR 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7943 TTAHYQAKQNQlPSDiAQEFTALELLAERVQV------TMETKEKDFKRAKTVRTEYvDGVDEVQRWLLQAEVQVQERSL 8016
Cdd:pfam12128 563 TDLDPEVWDGS-VGG-ELNLYGVKLDLKRIDVpewaasEEELRERLDKAEEALQSAR-EKQAAAEEQLVQANGELEKASR 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8017 TPTQMKELLQriNHEITAIyeRFTLVKTNGQLIIENCRnSEEKTLVQTTIDQLAASLAQV----RGWLDEKKqavGDSLD 8092
Cdd:pfam12128 640 EETFARTALK--NARLDLR--RLFDEKQSEKDKKNKAL-AERKDSANERLNSLEAQLKQLdkkhQAWLEEQK---EQKRE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8093 AWTRFMNLYQIVMSWASEKRNFIDQTIE-LRTLPEARNKL--NDYVTSVKSIKPIVKHLSEMDKELEHIgqVTTVGDLKD 8169
Cdd:pfam12128 712 ARTEKQAYWQVVEGALDAQLALLKAAIAaRRSGAKAELKAleTWYKRDLASLGVDPDVIAKLKREIRTL--ERKIERIAV 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8170 KLQEAEDAKISVEAVLLERNSLLQEACEEwdqCERKIKDIRSwhEKTKQGLDSSQQQKKpLRDQLGFCEKTLADINVQKT 8249
Cdd:pfam12128 790 RRQEVLRYFDWYQETWLQRRPRLATQLSN---IERAISELQQ--QLARLIADTKLRRAK-LEMERKASEKQQVRLSENLR 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8250 KLRLSIEKL--------------EVHFRNGMGGD-----PRLSENVDDLVRVLDGlgeLVKAKS--------QSLEQTLA 8302
Cdd:pfam12128 864 GLRCEMSKLatlkedanseqaqgSIGERLAQLEDlklkrDYLSESVKKYVEHFKN---VIADHSgsglaetwESLREEDH 940
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320544542 8303 QIDVYQQQMQSLRQrIIQEEQQLRLVMAPtylphDRERALAEQQDLITQELDELLQSLSSVEDGIANMN 8371
Cdd:pfam12128 941 YQNDKGIRLLDYRK-LVPYLEQWFDVRVP-----QSIMVLREQVSILGVDLTEFYDVLADFDRRIASFS 1003
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
4187-4272 |
2.99e-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: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4187 NWLDQVEKLIHNENPASwtSAQEIRSKLYKYKATNQDINSHKRIVEAVNEKAAALLGSAAPAnADEISKAVAEVNKRYDQ 4266
Cdd:pfam00435 15 SWIEEKEALLSSEDYGK--DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYA-SEEIQERLEELNERWEQ 91
|
....*.
gi 320544542 4267 VGQDCA 4272
Cdd:pfam00435 92 LLELAA 97
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
8157-8576 |
3.02e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8157 HIGQVTTVGDLKDKLQEAEDAKISVEAVLLErnslLQEACEEWDQCERKIKDIRSWHEKTKQgldssQQQKKPLRDQLGF 8236
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEE----LEELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8237 CEKTLADINVQKTKLRLSIEKLEVHFRNGmggdPRLSENVDDLVRVLDGLGELVK-AKSQSLEQTLAQIDVYQQQMQSLR 8315
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEEL----EELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8316 QRIIQEEQQLRLVMAPTYLPHDRERALAEQQDLitQELDELLQSLSSVEdGIANMNQSSLDGMLHGLKLIQSNLEV---- 8391
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERL--KEARLLLLIAAALL-ALLGLGGSLLSLILTIAGVLFLVLGLlall 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8392 ---HERDAIELKNQAKKLPTDPATERL----LNDTVDRIDLLLRRTQQGITMIANAMHGQKKRQQEIDEYQQHLLeleqw 8464
Cdd:COG4717 290 fllLAREKASLGKEAEELQALPALEELeeeeLEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ----- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8465 IIEVSAELASFEPTSDSSTDEQVLK--SQVERSQQLLRTLKDRQQSMEDLVEQTRQLQSHPDVSPLADTLmEQLQSIITI 8542
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEEL-EELEEELEE 443
|
410 420 430
....*....|....*....|....*....|....
gi 320544542 8543 LREQVTVATKRIFTIEKRIVDLRKAKSEEAQRQR 8576
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELLQE 477
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6962-7754 |
3.07e-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: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6962 RQQKIKSLMKDAEAKQSLADV------LEKRVANMQQELEPVE-YSQLESALRNLNtenRNLSGV----LKAELDRALEA 7030
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLedilneLERQLKSLERQAEKAErYKELKAELRELE---LALLVLrleeLREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7031 SKARKSLENDLDKARQWLKTKISEVRKLpvYHPL-------------TSAEIEKKIQENRKYDDDAKQFNDS-VLTDVQR 7096
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLE--VSELeeeieelqkelyaLANEISRLEQQKQILRERLANLERQlEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7097 QAANIMKDCDDADKAALQQILDEIAADYQTLKDESSKRGKSLDDLLQGRKAFEDSMKNMGDWLNEMEtategelrtTSLP 7176
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE---------LQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7177 VLEEQLAHYKKLLSDAE-NKGGLINDVSEQGKSILPTlsnadklklndDIKNMKDRYGRIKNTIDDRVNALGDHIKKYKD 7255
Cdd:TIGR02168 397 SLNNEIERLEARLERLEdRRERLQQEIEELLKKLEEA-----------ELKELQAELEELEEELEELQEELERLEEALEE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7256 AKSRLAECSQflgNIQQKLRELNRpIGSRIEDVQDLLGAYEGI---LKELKDSKSKMGD--------MQMD--------- 7315
Cdd:TIGR02168 466 LREELEEAEQ---ALDAAERELAQ-LQARLDSLERLQENLEGFsegVKALLKNQSGLSGilgvlselISVDegyeaaiea 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7316 DLPE-LQSILAQQDDMIKLI----------------------EDQLAHLRQLLLLREQFIALINEIIAFIMKYTDVIID- 7371
Cdd:TIGR02168 542 ALGGrLQAVVVENLNAAKKAiaflkqnelgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYl 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7372 -----IENSPDSLEDKINKYD---------------------------------------------DVIVKIQECEGVLA 7401
Cdd:TIGR02168 622 lggvlVVDDLDNALELAKKLRpgyrivtldgdlvrpggvitggsaktnssilerrreieeleekieELEEKIAELEKALA 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7402 SANDKGQKIASEGNAADK--NSITEQLQSLKNQLQNLRKAVESQRQKHQLQLESHKKMAAELSEILDWLHSHEGAAKSrp 7479
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE-- 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7480 lLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEIGMPSSLLEMLsegRSLVASLPHELEEREKYLKNNRDSRL 7559
Cdd:TIGR02168 780 -AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL---ERRIAATERRLEDLEEQIEELSEDIE 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7560 EYMQLVAKFndWVHEAELRLQNSQHGIDYEHLVQDLDEHKIFFGN-EAPIRNLVHK------QIQEAADKIwSSLNNyEQ 7632
Cdd:TIGR02168 856 SLAAEIEEL--EELIEELESELEALLNERASLEEALALLRSELEElSEELRELESKrselrrELEELREKL-AQLEL-RL 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7633 SELSAELAQFQTKLTN----TLANAKTQQSELEKEAERWREyqqSIDRVKATIERTKFVdepvqNLAGLHfNIQKLSHAI 7708
Cdd:TIGR02168 932 EGLEVRIDNLQERLSEeyslTLEEAEALENKIEDDEEEARR---RLKRLENKIKELGPV-----NLAAIE-EYEELKERY 1002
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 320544542 7709 GNVQSQNSDLTLVNQQAQSLIRQADARNRQL----IEQDNAGLNRSWQDL 7754
Cdd:TIGR02168 1003 DFLTAQKEDLTEAKETLEEAIEEIDREARERfkdtFDQVNENFQRVFPKL 1052
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
10929-11690 |
3.13e-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: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10929 LRDIVAKIAAD--VGLDASALMQGELDA------LGQRLAECKDAITTLANVAETQDKERKELDkevTLAKAYFNnvqqD 11000
Cdd:pfam12128 198 VKSMIVAILEDdgVVPPKSRLNRQQVEHwirdiqAIAGIMKIRPEFTKLQQEFNTLESAELRLS---HLHFGYKS----D 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11001 ISREAPQNpKESEEQLAALRAHLQTLartEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTfqeyhRLST 11080
Cdd:pfam12128 271 ETLIASRQ-EERQETSAELNQLLRTL---DDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDA-----DIET 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11081 RLARSQNsseaLRLWRQYLQHVQsflscaipedysslreqqqlcAIHQNLLISQQSVLSET-PLESELSEQYKALTNLHN 11159
Cdd:pfam12128 342 AAADQEQ----LPSWQSELENLE---------------------ERLKALTGKHQDVTAKYnRRRSKIKEQNNRDIAGIK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11160 ETLSRImqRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIhlKRVPHLKHRLDAMIQQLDQGEQQskalqE 11239
Cdd:pfam12128 397 DKLAKI--REARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLK--SRLGELKLRLNQATATPELLLQL-----E 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11240 QQQELARHCDDALaTAMRMEQASIGQRISNLRAALKTWQGFLQRVtqlsesyEQRVNQLQQEFGAAQKLLDANSES---- 11315
Cdd:pfam12128 468 NFDERIERAREEQ-EAANAEVERLQSELRQARKRRDQASEALRQA-------SRRLEERQSALDELELQLFPQAGTllhf 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11316 LPTQPAAIEQLLGSLRAQ----RVQL-----GAQVSALESLTVTQEELKECISP--HDM-KTIRQRNWLL-------WQQ 11376
Cdd:pfam12128 540 LRKEAPDWEQSIGKVISPellhRTDLdpevwDGSVGGELNLYGVKLDLKRIDVPewAASeEELRERLDKAeealqsaREK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11377 HADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQRL--EQRVEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKE-R 11453
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLfdEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKhQ 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11454 EWLLSTSRELLTLYSEpevrsqvqqqsdslidRWQRLKYLAKQKATKIGELKMTLLRLEERIAlirAWLFEVESQLDKPL 11533
Cdd:pfam12128 700 AWLEEQKEQKREARTE----------------KQAYWQVVEGALDAQLALLKAAIAARRSGAK---AELKALETWYKRDL 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11534 NFESYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLnlvemllndadSWRtqvntsglaasaQNLEQRWKNVCSQSAERKA 11613
Cdd:pfam12128 761 ASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVL-----------RYF------------DWYQETWLQRRPRLATQLS 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11614 RILT-IWNLLQQLIKLTAEHKNWLGKQESQIAGFERDQ----KSHSKHKLEERQM---ELRAKLEELE-SQSVNLRQLEQ 11684
Cdd:pfam12128 818 NIERaISELQQQLARLIADTKLRRAKLEMERKASEKQQvrlsENLRGLRCEMSKLatlKEDANSEQAQgSIGERLAQLED 897
|
....*.
gi 320544542 11685 IYAKLA 11690
Cdd:pfam12128 898 LKLKRD 903
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5777-6383 |
3.25e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5777 LAKEVMRRLEMHYQEHQQHHSLYEECQSWIEKTREKLSECEQIPGTLNEVQIKLNTVKNLRQGFETGQNKLRYLLELKEK 5856
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5857 VIMNTEQNGA--AKIQEDTEALKQdFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDVEPSVKTSDEFLNDLSE 5934
Cdd:PRK03918 274 EIEELEEKVKelKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5935 KRAALEKFRVIQRDINGHNDIVEKINQRLKEDNSLDLKDfqpgltKFDDLQTQVNKIIESLENQVNSHEKYKQAYNELQD 6014
Cdd:PRK03918 353 RLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK------ELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6015 WLRRTRIEVEQCADC------HGEKDQVESRLNRLGDIQSSSLEGKALLEAC----EELSQAVIATSGSEGQDNVAQEIK 6084
Cdd:PRK03918 427 AIEELKKAKGKCPVCgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLrkelRELEKVLKKESELIKLKELAEQLK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6085 HLTSEWE--TLQTISRDARSslesclaaWQTFLQKFNKINLWIETMNKRVTKSQEGENKTpEDLVNAKKLLEEVLAE-KD 6161
Cdd:PRK03918 507 ELEEKLKkyNLEELEKKAEE--------YEKLKEKLIKLKGEIKSLKKELEKLEELKKKL-AELEKKLDELEEELAElLK 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6162 NVEDLNDNCELLMEQsactRIRDqtietqanytklltsaqglvakIEKNLSDHTEFLNYKKEmdawIEKAQQVLDDCSTD 6241
Cdd:PRK03918 578 ELEELGFESVEELEE----RLKE----------------------LEPFYNEYLELKDAEKE----LEREEKELKKLEEE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6242 GDAAI--IAQKLDTVNSLASRLPEgqhllalVQDAYSkasnitpEDKQEKLRELMTKVREdwdalglAVKQKLSDLKQAQ 6319
Cdd:PRK03918 628 LDKAFeeLAETEKRLEELRKELEE-------LEKKYS-------EEEYEELREEYLELSR-------ELAGLRAELEELE 686
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320544542 6320 NRWNDFAANKDKLEKWLNETETTLKVAPETKGELSEMKTLLERYKTLSNELKLKG-NELEQLQSE 6383
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERAlSKVGEIASE 751
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
7784-7935 |
3.27e-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: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7784 KALGRLEDKFRNVdptvrsRRHLEDTKNAIQELREESNQLKSSHKEIEALSKSILTFLGEVHKP-SAEAIQAKVDKLVEQ 7862
Cdd:COG1579 31 AELAELEDELAAL------EARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkEYEALQKEIESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320544542 7863 QAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLqsvhvyDEHIAQTEQLLITLNSQVQQAAEE 7935
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL------DEELAELEAELEELEAEREELAAK 171
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
7112-7937 |
3.31e-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: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7112 ALQQILDEIAadyqtlkdESSKRGKSLDDLLQGRKAFEDSMKNMGDWLNEMETATEGELRT-TSLPVLEEQLAHYKKLLS 7190
Cdd:TIGR00606 170 ALKQKFDEIF--------SATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIrDQITSKEAQLESSREIVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7191 DAENKgglINDVSEQGKSILPTLSNAdkLKLNDDIKNMKDRYGRIKNT--------------IDDRVNAL-GDHIKKYKD 7255
Cdd:TIGR00606 242 SYENE---LDPLKNRLKEIEHNLSKI--MKLDNEIKALKSRKKQMEKDnselelkmekvfqgTDEQLNDLyHNHQRTVRE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7256 AKSRLAECSQFLGNIQQKLRELNRPiGSRIEDVQDLLGA-----YEGILKELKDSKSKMGDMQMDDLPELQSILAQQDDM 7330
Cdd:TIGR00606 317 KERELVDCQRELEKLNKERRLLNQE-KTELLVEQGRLQLqadrhQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNF 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7331 IKLI----EDQLAHLRQLLLLREQFIALINEIIAFI-MKYTDVIIDIENSPDSLEDKINKYDDVIVKIQECEGVLASAND 7405
Cdd:TIGR00606 396 HTLVierqEDEAKTAAQLCADLQSKERLKQEQADEIrDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7406 KGQ---KIASEGNAADKNSITEQLQSLKNQLQNlrkavesqrqkHQLQLESHKKMAAELSEILDwlhSHEGAAKSRPLLD 7482
Cdd:TIGR00606 476 LDQelrKAERELSKAEKNSLTETLKKEVKSLQN-----------EKADLDRKLRKLDQEMEQLN---HHTTTRTQMEMLT 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7483 RDPESVERELQKHQSL-SQDIESYLNKFNKINDGVKTEigmpSSLLEMLSEGRSLVASLPHELE--EREKYLKNNRDSRL 7559
Cdd:TIGR00606 542 KDKMDKDEQIRKIKSRhSDELTSLLGYFPNKKQLEDWL----HSKSKEINQTRDRLAKLNKELAslEQNKNHINNELESK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7560 EYMQLvaKFNDWVHEAelrLQNSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLVHKQIQEAADKIWSSLNNYEQS-ELSAE 7638
Cdd:TIGR00606 618 EEQLS--SYEDKLFDV---CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVfQTEAE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7639 LAQFQTKLTNTLANAKTQQSELEKEAERwREYQQSIDRVKATIeRTKFVDEPVQNLAGLHFNIQKLSHAIgnvQSQNSDL 7718
Cdd:TIGR00606 693 LQEFISDLQSKLRLAPDKLKSTESELKK-KEKRRDEMLGLAPG-RQSIIDLKEKEIPELRNKLQKVNRDI---QRLKNDI 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7719 TLVNQQAQSLIRQADARNrqlIEQDNAGLNRSWQDLVRSLEQRrdnLQQLAEHWDGFENSLhAWEKALGRLEDKFRNVDP 7798
Cdd:TIGR00606 768 EEQETLLGTIMPEEESAK---VCLTDVTIMERFQMELKDVERK---IAQQAAKLQGSDLDR-TVQQVNQEKQEKQHELDT 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7799 TVRS----RRHLEDTKNAIQELREESNQLKSSHKEI-------EALSKSILTFLGEVHKPSAEAIQAKVDKLVEQQAKlN 7867
Cdd:TIGR00606 841 VVSKielnRKLIQDQQEQIQHLKSKTNELKSEKLQIgtnlqrrQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFL-E 919
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320544542 7868 DTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVHVY-----DEHIAQTEQLLITLNSQVQQAAEESK 7937
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgkDDYLKQKETELNTVNAQLEECEKHQE 994
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5985-6550 |
3.45e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5985 QTQVNKIIESLE------NQVNSHEKYKQAYNELQDWLRRTRIeveqcadchgEKDQVESRLNRLGDIQssslegKALLE 6058
Cdd:PRK03918 134 QGEIDAILESDEsrekvvRQILGLDDYENAYKNLGEVIKEIKR----------RIERLEKFIKRTENIE------ELIKE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6059 ACEELSQaviatsgsegqdnVAQEIKHLTSEwetlqtisrdaRSSLESCLAAWQTFLQKFNKINLWIETMNKRVTKSQEG 6138
Cdd:PRK03918 198 KEKELEE-------------VLREINEISSE-----------LPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6139 ENKTPEDLVNAKKLLEEVLAE----KDNVEDLNDNCELLMEQSACTRIRDQTIETQANYTKLLTSAQGLVAKIEKNLSDH 6214
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEieelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6215 TEFLNYKKEMDAWIEKAQQVLDDCSTDgdaaiiAQKLDTVNSLASRLpegqhllalvQDAYSKASNITPEDKQEKLRELM 6294
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEER------HELYEEAKAKKEEL----------ERLKKRLTGLTPEKLEKELEELE 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6295 TKVREDWDALgLAVKQKLSDLKQAQNRwndfaankdkLEKWLNETETTLKVAPETKGELSE--MKTLLERY----KTLSN 6368
Cdd:PRK03918 398 KAKEEIEEEI-SKITARIGELKKEIKE----------LKKAIEELKKAKGKCPVCGRELTEehRKELLEEYtaelKRIEK 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6369 ELKLKGNELEQLQSEARdlgtEVDAVNRLQSRCDKLKnDCSAHITALEQEMFDYNA--YHQSLQDVEKwLLQISFQLMAH 6446
Cdd:PRK03918 467 ELKEIEEKERKLRKELR----ELEKVLKKESELIKLK-ELAEQLKELEEKLKKYNLeeLEKKAEEYEK-LKEKLIKLKGE 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6447 NSLFISNREQTQEQIKQHEALLVEIQKYQTNLDDLNakgqaqiKRYESSTPAIRPTVESQLKNIQDSYNSLLqTSVQIKN 6526
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEELAELL-------KELEELGFESVEELEERLKELEPFYNEYL-ELKDAEK 612
|
570 580
....*....|....*....|....
gi 320544542 6527 RLLESLAKFQEYEDTLDSIMRNLE 6550
Cdd:PRK03918 613 ELEREEKELKKLEEELDKAFEELA 636
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
11959-12108 |
3.57e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 43.59 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11959 DTVAELTLRFDTLQSQWKARQQHDQNASEVgrltcplctqrnwQQIDNDLWRLEQWLQFAESTQKAQSaPPSNIELLEDV 12038
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDL-------------QQFFRDADDLEQWLEEKEAALASED-LGKDLESVEEL 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 12039 TQDHREFLLDLESHKSIISSLNVVGDHLATHtLDTEKARQLRSRLEADNERWNNVCINATKWQGLLQTAL 12108
Cdd:cd00176 145 LKKHKELEEELEAHEPRLKSLNELAEELLEE-GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1612-1803 |
3.67e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 43.59 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 1612 FYQSLKDVEKELQLEQQALNRNEDVDSILQRNQQF----LLQQDVVPRLERcLQNMQRLAQAHRQQQPGDIS-LDQAYDN 1686
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLkkheALEAELAAHEER-VEALNELGEQLIEEGHPDAEeIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 1687 AKSQWQLLSNKLGDMRQTLQQIPAQWQgYHLKFNDMVDWMNGVDQSLKNIVNeVNTMEEFEKEKVVFQKICQDADNKRED 1766
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEAHEPR 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 320544542 1767 MKWLVKTLDSLLSYATEDEANLEQKKLEDLIARYKNL 1803
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEEL 198
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
4611-4706 |
3.99e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.78 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 4611 FDEIADSLKSWLDETENALpADIELKTTLDEKRNKLQTYRDILNDINNHQVELGNLQEIAANL----PEKTELVDQIIKD 4686
Cdd:smart00150 3 FLRDADELEAWLEEKEQLL-ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieegHPDAEEIEERLEE 81
|
90 100
....*....|....*....|
gi 320544542 4687 ISDRFGKLQKRAQNYVERYE 4706
Cdd:smart00150 82 LNERWEELKELAEERRQKLE 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
10801-11046 |
4.01e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10801 ERLRKATERLEGLAGDLHNREQLIDELKGAAKPLIESCDV-QIVEQIEsAVQEAVVAWNDTSENLQQLRTRYQRAVELWD 10879
Cdd:COG4913 624 EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVaSAEREIA-ELEAELERLDASSDDLAALEEQLEELEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10880 KYRNAsaavknsIDQQMDAVKSLEQPLDALQhakvcqdnlttqnDRILELRDIVAKIAADVGLDASALMQGELDALGQRL 10959
Cdd:COG4913 703 ELEEE-------LDELKGEIGRLEKELEQAE-------------EELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10960 AEcKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPkESEEQLAALRAHLQT--LARTEEQLRQLK 11037
Cdd:COG4913 763 VE-RELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADL-ESLPEYLALLDRLEEdgLPEYEERFKELL 840
|
....*....
gi 320544542 11038 ERHQNSEVA 11046
Cdd:COG4913 841 NENSIEFVA 849
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10653-11275 |
4.17e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10653 LRDQLQAIQEGISNQRKHQAKISVILDECEAAERQGADVLEKAVADCQAAGEELVISWQEIMRirqmlhtlpmrlkmsvs 10732
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR----------------- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10733 pvkLERDISQLQDDHAFLESKctniMAILRSRLAVWlryERQLELVHGSVQETDfmmelirvhgqvdyERLRKATERLEG 10812
Cdd:COG1196 300 ---LEQDIARLEERRRELEER----LEELEEELAEL---EEELEELEEELEELE--------------EELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10813 LAGDLHNREQLIDELKGAAKPLIEScdvqiVEQIESAVQEAVVAWNDTSENLQQLRTRYQRAVELWDKYRNASAAVKNSI 10892
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEE-----LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10893 DQQMDAVKSLEQPLDALQHAKVCQDNLTTQNDRIL-----ELRDIVAKIAADVGLDASALMQGELDALGQRLAECKDAIT 10967
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLaelleEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10968 TLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPKESEEQLAALRAHLQTL---ARTEEQLRQLKERHQNSE 11044
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagRATFLPLDKIRARAALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11045 VAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEALRlwrqylqhvqsflscaipedysslreqqqlc 11124
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA------------------------------- 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11125 aihQNLLISQQSVLSETPLESELSEQYKALTNLHNETLSRIMQRNGELERRVSgwnayRQQLAALLDWLRQREAERNALQ 11204
Cdd:COG1196 640 ---VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA-----EEELELEEALLAEEEEERELAE 711
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320544542 11205 LRyihlKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHcDDALATAMRMEQASIGQRISNLRAALK 11275
Cdd:COG1196 712 AE----EERLEEELEEEALEEQLEAEREELLEELLEEEELLEE-EALEELPEPPDLEELERELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
11481-12202 |
4.22e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11481 DSLIDRWQRLKYLAKQKATKIGELKMTLLRLEERIALIRAWLFEVESQLDKpLNFESYTPNVIEAKLKEHEQIQRSIEHH 11560
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE-LQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11561 SSNVGEVLNLVemlLNDADSWRTQVNTSgLAASAQNLEQRWKNVCSQSAERKARILTIWNLLQQLIKLTAEhknwLGKQE 11640
Cdd:TIGR02168 314 LERQLEELEAQ---LEELESKLDELAEE-LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ----LETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11641 SQIAGFERDQKSHSKhkleeRQMELRAKLEELESqsvNLRQLEQIYAKLAMsagvEPENIQKLTLPTKVmvsmwrqltpr 11720
Cdd:TIGR02168 386 SKVAQLELQIASLNN-----EIERLEARLERLED---RRERLQQEIEELLK----KLEEAELKELQAEL----------- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11721 chALLDAIDKDAKLMREFNNAQLEatnslnAIQKALEQLPSAenQQTSKAEPKAVLQRLESLEKKLQDAQQHVQQADNLA 11800
Cdd:TIGR02168 443 --EELEEELEELQEELERLEEALE------ELREELEEAEQA--LDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11801 QEAKTRTKQQPQLKQLLELVSAYTTLWQTV-QTRIVTLKTTWLTRAAQAAASLPVSEAANAAVQVNTLSQRKLRQAQQMQ 11879
Cdd:TIGR02168 513 KNQSGLSGILGVLSELISVDEGYEAAIEAAlGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDRE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11880 RETSITAKDAYIMELQTAITECQNNLDE-LQRTVV--------DKTRKPGP-----------------------QKIAKL 11927
Cdd:TIGR02168 593 ILKNIEGFLGVAKDLVKFDPKLRKALSYlLGGVLVvddldnalELAKKLRPgyrivtldgdlvrpggvitggsaKTNSSI 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11928 LGNAQSSTELVKHLSHLLLTECKADDQAAEVDT-VAELTLRFDTLQSQW--KARQQHDQNAS-EVGRLTCPLCTQRNWQQ 12003
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKeLEELEEELEQLRKELeeLSRQISALRKDlARLEAEVEQLEERIAQL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 12004 IDNDLWRLEQWLQFAESTQKAQSAPPSNIELLEDVTQDHREFLLDLESHKSIISSLNvvgdhlATHTLDTEKARQLRSRL 12083
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR------AELTLLNEEAANLRERL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 12084 EADNERwnnvcINATKwqgllqtalmgnsefhQTIGELVEWLQRTEQNIKASEPV--DLTEERSVLETKFKKFKDLRAEL 12161
Cdd:TIGR02168 827 ESLERR-----IAATE----------------RRLEDLEEQIEELSEDIESLAAEieELEELIEELESELEALLNERASL 885
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 320544542 12162 ERCEPRVVSLQDAADQLLRSVEGSEQQSQHTYERTLSRLTD 12202
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2568-3956 |
4.25e-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: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2568 KDKFHALEHNFGQALQE------NRAKLDEILRQHPTLNNIDQIIADLVALNDALK-YQAD---------------LKNR 2625
Cdd:TIGR01612 458 KSKLKALEKRFFEIFEEewgsydIKKDIDENSKQDNTVKLILMRMKDFKDIIDFMElYKPDevpskniigfdidqnIKAK 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2626 IHDEGSLLMREDIASMPAIQESLLIMDK-----NYDS--LQNEIADRIQKY----------NLISQALREYADSKDKFSK 2688
Cdd:TIGR01612 538 LYKEIEAGLKESYELAKNWKKLIHEIKKeleeeNEDSihLEKEIKDLFDKYleiddeiiyiNKLKLELKEKIKNISDKNE 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2689 ELKKAEDLYNAIPQQPRDETEL-----HQASE--KTRKTMEQLRKSKLSldelERRGNNVGKLFSAIGEpIPQEVPQEVT 2761
Cdd:TIGR01612 618 YIKKAIDLKKIIENNNAYIDELakispYQVPEhlKNKDKIYSTIKSELS----KIYEDDIDALYNELSS-IVKENAIDNT 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2762 AAKQHWQDLH---DKTAKNAHVYETEAVI--WSQIEDAKKDLLPWLSETNQGLCDAADNSIEiefgpmrlskyrTELPSY 2836
Cdd:TIGR01612 693 EDKAKLDDLKskiDKEYDKIQNMETATVElhLSNIENKKNELLDIIVEIKKHIHGEINKDLN------------KILEDF 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2837 QALKDSIVEKTNDLVKINkgaeipalSALNKLLSeQFAEVNNNADRLSAITTSFNDQEQELRRRSKEAGERVSKLREQLI 2916
Cdd:TIGR01612 761 KNKEKELSNKINDYAKEK--------DELNKYKS-KISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIF 831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2917 KC--------DDMSGDNNKIMERLQQCRalrgELDNSGNE-----IDNIKQKV-DELRNLYPTF---SESIIPKELNNVQ 2979
Cdd:TIGR01612 832 KIinemkfmkDDFLNKVDKFINFENNCK----EKIDSEHEqfaelTNKIKAEIsDDKLNDYEKKfndSKSLINEINKSIE 907
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2980 KRYENVDLYAK-----KIESSLLQFLKKFHaDKVGMLKRIIATQREKVAWCQ--PESSSDKYN--LDVKKSSLQEVSK-- 3048
Cdd:TIGR01612 908 EEYQNINTLKKvdeyiKICENTKESIEKFH-NKQNILKEILNKNIDTIKESNliEKSYKDKFDntLIDKINELDKAFKda 986
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3049 SIDDCKARHAETLKSLEMLKA---VESPQNLAELTSDAELLRKDMQalQDSFDQIKGILDENVDLWSQYEQSNEQISNWL 3125
Cdd:TIGR01612 987 SLNDYEAKNNELIKYFNDLKAnlgKNKENMLYHQFDEKEKATNDIE--QKIEDANKNIPNIEIAIHTSIYNIIDEIEKEI 1064
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3126 -RDVEGR----VKAETSSQVNLSEVPQKLQELSIlqQDVLAHEpiinNLEQTSQQLIEKNPEARIGQFVTHLVQRYQAVS 3200
Cdd:TIGR01612 1065 gKNIELLnkeiLEEAEINITNFNEIKEKLKHYNF--DDFGKEE----NIKYADEINKIKDDIKNLDQKIDHHIKALEEIK 1138
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3201 KALTSYIDKIRgAQLSNANFAKAAKDFNEwfgdakiefqelarmgSPGSSSATAQQLQT---VKNYIktFDNGQILLNNA 3277
Cdd:TIGR01612 1139 KKSENYIDEIK-AQINDLEDVADKAISND----------------DPEEIEKKIENIVTkidKKKNI--YDEIKKLLNEI 1199
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3278 VDIgealypvvspdnrERIRADLRQMRE-KFDYLRDEANAFMQQVEGvliQKTSIEESYTQVSHY---LNESKAKVPTTD 3353
Cdd:TIGR01612 1200 AEI-------------EKDKTSLEEVKGiNLSYGKNLGKLFLEKIDE---EKKKSEHMIKAMEAYiedLDEIKEKSPEIE 1263
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3354 ELYPTLATKKAALQ-------NYKTQLQEITLHKNALKQLHDKAVTLCDDESERKTDESIQEynTLSKKISDrittvgnh 3426
Cdd:TIGR01612 1264 NEMGIEMDIKAEMEtfnishdDDKDHHIISKKHDENISDIREKSLKIIEDFSEESDINDIKK--ELQKNLLD-------- 1333
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3427 VVKHEA-YDQVLEKAQDWLNTIK----SEAIDILNETTFEKE----GAEEKLLVVENLLQhKPEGDSIFDTCHKLLETVL 3497
Cdd:TIGR01612 1334 AQKHNSdINLYLNEIANIYNILKlnkiKKIIDEVKEYTKEIEennkNIKDELDKSEKLIK-KIKDDINLEECKSKIESTL 1412
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3498 TQTHPSGhpallkgfeepkqswedfmtlCQDSLVKLKQ-LCSKWDEFDTIIEELDNWMKNVEAVVKNQNLkstAEAKNAH 3576
Cdd:TIGR01612 1413 DDKDIDE---------------------CIKKIKELKNhILSEESNIDTYFKNADENNENVLLLFKNIEM---ADNKSQH 1468
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3577 LKQLQ--DISKDIERRGAAINELMDQGREIEGETDLNLKLSRLNTR-YQTLKNLCKESIAKYVNYV---------KDHES 3644
Cdd:TIGR01612 1469 ILKIKkdNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKElFEQYKKDVTELLNKYSALAiknkfaktkKDSEI 1548
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3645 FDKDFDSFKQN--LQSSVDElAKTNEIVGDQSVLQDQQNKlREMSDKRILDStlfeglidrgeklygHTSPEGREIIRQQ 3722
Cdd:TIGR01612 1549 IIKEIKDAHKKfiLEAEKSE-QKIKEIKKEKFRIEDDAAK-NDKSNKAAIDI---------------QLSLENFENKFLK 1611
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3723 LRALRTlwdnYTDDLNSATQKIDQcllQFNEFSI-AQDQLTKWLKDVDKAMQSHTEP----KTTLQEKRAQLQNhkllhq 3797
Cdd:TIGR01612 1612 ISDIKK----KINDCLKETESIEK---KISSFSIdSQDTELKENGDNLNSLQEFLESlkdqKKNIEDKKKELDE------ 1678
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3798 eitthnvlVDNVCDKAQILVDQIKDNslnvYLTSIKQLFQSIVQKSDEILHNLDDCVQkhNELNNALSSAKT-----WIS 3872
Cdd:TIGR01612 1679 --------LDSEIEKIEIDVDQHKKN----YEIGIIEKIKEIAIANKEEIESIKELIE--PTIENLISSFNTndlegIDP 1744
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3873 NEKaklleCDDAYGEKADIKRKIETLGQLAQNkpqAMKIISDIRDLFEKVKATTSEKGNEVLdkEIEELETTMKSHFDDI 3952
Cdd:TIGR01612 1745 NEK-----LEEYNTEIGDIYEEFIELYNIIAG---CLETVSKEPITYDEIKNTRINAQNEFL--KIIEIEKKSKSYLDDI 1814
|
....
gi 320544542 3953 EGIE 3956
Cdd:TIGR01612 1815 EAKE 1818
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
11160-11459 |
4.62e-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: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11160 ETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALqLRYIHLKRVPHLKHRLDAMIQQLDQgeqqskaLQE 11239
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKL-LPQANLLADETLADRLEELREELDA-------AQE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11240 QQQELARHcddalatamrmeqasiGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQefgaAQKLLDANSEslptq 11319
Cdd:COG3096 908 AQAFIQQH----------------GKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRR----LKQQIFALSE----- 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11320 paaieqllgsLRAQRVQLGAQVSAlESLTVTQ---EELKECISphDMKTIRQRNWLLWQQHADlDYQLANlinsiEERLS 11396
Cdd:COG3096 963 ----------VVQRRPHFSYEDAV-GLLGENSdlnEKLRARLE--QAEEARREAREQLRQAQA-QYSQYN-----QVLAS 1023
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320544542 11397 LLSNYQIRYdrisQWLQRLEQRVEkDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWLLST 11459
Cdd:COG3096 1024 LKSSRDAKQ----QTLQELEQELE-ELGVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQ 1081
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
10799-11231 |
4.89e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10799 DYERLRKATERLEGLAGDLHNREQLIDELKGAAKpLIESCDVQIVEQIESAVQEAVVAWNDTSENLQQLRTRYQRAVELW 10878
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEE-ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10879 DKYRNASAAVKNSIDQQMDAVKSLEQPLDALQHAKVCQDNLTTqndrILELRDIVAKIAADVGLDASALMQGELDALGQR 10958
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL----LLIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10959 LAECKDAITTLANVAETQDKER-KELDKEVTLAKAYFNNVQQDISREAPQNPKESEE---QLAALRAHLQTLARTEEQLR 11034
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEElQALPALEELEEEELEELLAALGLPPDLSPEELLElldRIEELQELLREAEELEEELQ 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11035 QLKERHQNSEVAPSVASSDDDGILEVLALWQKiFQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQhvqsflscaIPEDY 11114
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEE---------LEEEL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11115 SSLREQQQLcaihqnllisqqsvlsetpLESELSEQYKALTNLHNETlsRIMQRNGELERRvsgwnayRQQLAALLDWLR 11194
Cdd:COG4717 435 EELEEELEE-------------------LEEELEELREELAELEAEL--EQLEEDGELAEL-------LQELEELKAELR 486
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 320544542 11195 QREAERNALQL---------RYIHLKRVPHLKHRLDAMIQQLDQGE 11231
Cdd:COG4717 487 ELAEEWAALKLalelleearEEYREERLPPVLERASEYFSRLTDGR 532
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5139-5351 |
5.05e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.82 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5139 DHRLFKEAYDDLVSWIGRAREKFPSlkQSSLSDKLAIENAVQATEALLNKQAQGELLVEHLVHTGEvVLASTSAQGQEII 5218
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGE-QLIEEGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5219 RNDIRALRDSFEGLFREINQQKENLEVTMVQWRAYKEEYErLMEWLQQIDILVKNHKlnLCPNLPEKEKQVADMKEVMSR 5298
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 320544542 5299 LEKGKDDIDKFNASAASLLKSH---LDTYVNNQLRHLSSVYQVQVNLAKDVLKKVE 5351
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGhpdADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
11120-11417 |
5.07e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11120 QQQLCAIHQNLLISQQSVLSETPLESELseqykaltnlhnETLSRIMQRNGELErrvsgwnAYRQQLAALLDWLRQREAE 11199
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQTL------------ALLDKIDRQKEETE-------QLKQQLAQAPAKLRQAQAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11200 RNALQLryihlKRVPHLKHRLDAM-IQQL-DQGEQQSKALQEQQQELARHCDDALATAMRME--QASIG---QRISNLRA 11272
Cdd:PRK11281 103 LEALKD-----DNDEETRETLSTLsLRQLeSRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPEraQAALYansQRLQQIRN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11273 ALKTwqgflQRVTQLSESYEQRvNQLQQEfgaaQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALES------ 11346
Cdd:PRK11281 178 LLKG-----GKVGGKALRPSQR-VLLQAE----QALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHqlqllq 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320544542 11347 -------LTVTQEELKECISPHDMKTIrQRNWLLwQQHADLDYQLAN-LINSIeERLSLLSNYQIrydRISQWLQRLEQ 11417
Cdd:PRK11281 248 eainskrLTLSEKTVQEAQSQDEAARI-QANPLV-AQELEINLQLSQrLLKAT-EKLNTLTQQNL---RVKNWLDRLTQ 320
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2897-3232 |
5.34e-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: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2897 LRRRSKEAGERVSKLREQLIKCDDMSGDNNKIMERLQ-------QCRALRGELDN-----SGNEIDNIKQKVDELRNLYP 2964
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLErqaekaeRYKELKAELRElelalLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2965 TFSESI--IPKELNNVQKRYENVDLYAKKIESSLLQFLKKFHA--DKVGMLKRIIATQREKVAWCQPESSSDKYNLDVKK 3040
Cdd:TIGR02168 250 EAEEELeeLTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaNEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3041 SSLQEVSKSIDDCKARHAETLKSLEMLKA--VESPQNLAELTSDAELLRKDMQALQDSFDQIKGILDEN----VDLWSQY 3114
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLnneiERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3115 EQSNEQISNWLRDVEGRVKAETSSQvnLSEVPQKLQELSILQQDVLAHEPIINNLEQTSQQLIEKNPEARigQFVTHLVQ 3194
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL--DAAERELA 485
|
330 340 350
....*....|....*....|....*....|....*...
gi 320544542 3195 RYQAVSKALTSYIDKIRGAQLSNANFAKAAKDFNEWFG 3232
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILG 523
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2871-3169 |
5.61e-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: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2871 EQFAEVNNNADRLSAITTSFNDQEQELRRRSKEAGERVSKLREqlikCDDMSGDNNKIMERL-QQCRALRGELDNSGNEI 2949
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD----ASRKIGEIEKEIEQLeQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 2950 DNIKQKVDELRNLYPTFSESIIPKELNNVQKRYENVDLYAKKIESSL------LQFLKKFHADKVGMLKRIIA-----TQ 3018
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpeiqaeLSKLEEEVSRIEARLREIEQklnrlTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 3019 REKVAwcQPESSSDKYNLDVKKSSLQEVSKSIDDCKARHAETLKSLEMLKAVESP--QNLAELTSDAELLRKDMQALQDS 3096
Cdd:TIGR02169 827 EKEYL--EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDleSRLGDLKKERDELEAQLRELERK 904
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320544542 3097 FDQIKGILDENVDLWSQYEQSNEQISNWLRDVEGRVKAETSSQVNLSEVPQKLQELSILQQDVLAHEPiINNL 3169
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEP-VNML 976
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
11130-11394 |
5.99e-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: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11130 LLISQQSVLSETPLESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLryih 11209
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11210 lkrvphlkhRLDAMIQQLDQGEQQskaLQEQQQELARHcddaLATAMRMEQASIGQRISNLRAALKtwqgfLQRVTQLSE 11289
Cdd:COG4942 84 ---------ELAELEKEIAELRAE---LEAQKEELAEL----LRALYRLGRQPPLALLLSPEDFLD-----AVRRLQYLK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11290 SYEQRVNQLQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLtvtQEELKEcisphDMKTIRQR 11369
Cdd:COG4942 143 YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEK-----ELAELAAE 214
|
250 260
....*....|....*....|....*
gi 320544542 11370 NWLLWQQHADLDYQLANLINSIEER 11394
Cdd:COG4942 215 LAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
11194-11916 |
6.01e-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: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11194 RQREAERNaLQLRYIHLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELaRHCDDALAT-----------AMRMEQAS 11262
Cdd:TIGR02168 173 RRKETERK-LERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAEL-RELELALLVlrleelreeleELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11263 IGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKLLDAnsesLPTQPAAIEQLLGSLRAQRVQLGAQVS 11342
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR----LEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11343 ALESltvTQEELKEcisphDMKTIRQRNWLLWQQHADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQRLEQRVekd 11422
Cdd:TIGR02168 327 ELES---KLDELAE-----ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI--- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11423 advtamtnpEQAAKQLEQQVnSELQLRDKEREWLLSTSRELLTLYSEPEVRsQVQQQSDSLIdrwQRLKYLAKQKATKIG 11502
Cdd:TIGR02168 396 ---------ASLNNEIERLE-ARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELE---EELEELQEELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11503 ELKmtllRLEERIALIRAWLFEVESQLDKpLNFESYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDADSWR 11582
Cdd:TIGR02168 462 ALE----ELREELEEAEQALDAAERELAQ-LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11583 TQVNTSgLAASAQ-----NLEQRWKNVCSQSAERKARILTIWNLLQQLIKLTAEHKNWLGKQEsqiaGFERDQKSHSKHK 11657
Cdd:TIGR02168 537 AAIEAA-LGGRLQavvveNLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIE----GFLGVAKDLVKFD 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11658 LEERQ------------------MELRAKLEELESqSVNLrQLEQIYAKLAMSAGVEPENIQKLTLPTKVmvsmwRQLTP 11719
Cdd:TIGR02168 612 PKLRKalsyllggvlvvddldnaLELAKKLRPGYR-IVTL-DGDLVRPGGVITGGSAKTNSSILERRREI-----EELEE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11720 RCHALLDAIdkdaklmREFNNAQLEATNSLNAIQKALEQLPSAENQQTSK-AEPKAVLQRLESLEKKLqdAQQHVQQADN 11798
Cdd:TIGR02168 685 KIEELEEKI-------AELEKALAELRKELEELEEELEQLRKELEELSRQiSALRKDLARLEAEVEQL--EERIAQLSKE 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11799 LAQEAKTRTKQQPQLKQLLELVSAYTTLWQTVQTRIVTLKTTWLT-----RAAQAAASLPVSEAANAAVQVNTLSQRKLR 11873
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealDELRAELTLLNEEAANLRERLESLERRIAA 835
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 320544542 11874 QAQQMQRETSITAKDAYIME-LQTAITECQNNLDELQRTVVDKT 11916
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIEsLAAEIEELEELIEELESELEALL 879
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
11179-11369 |
6.24e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.82 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11179 WNAYRQQLAALLDWLRQREAERNALQLRyIHLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDAlATAMRM 11258
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11259 EQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQrVNQLQQEFGAAQKLLdaNSESLPTQPAAIEQLLGSLRAQRVQLG 11338
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAAL--ASEDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190
....*....|....*....|....*....|.
gi 320544542 11339 AQVSALESLTVTQEELKECISPHDMKTIRQR 11369
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEK 187
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7747-7966 |
6.93e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7747 LNRSWQDLVRsLEQRRDNLQQLAEHWDgfenslhAWEKALGRLE--DKFRNVDPTVRSRRHLEDTKNAIQELREESNQLK 7824
Cdd:COG4913 237 LERAHEALED-AREQIELLEPIRELAE-------RYAAARERLAelEYLRAALRLWFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 7825 sshKEIEALSKSIltflgevhkpsaEAIQAKVDKLVEQQAKL-NDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHE 7903
Cdd:COG4913 309 ---AELERLEARL------------DALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320544542 7904 QL-QSVHVYDEHIAQTEQLLITLNSQVQQAAEEsklLVAQTTAHYQAKQNQlpSDIAQEFTALE 7966
Cdd:COG4913 374 PLpASAEEFAALRAEAAALLEALEEELEALEEA---LAEAEAALRDLRREL--RELEAEIASLE 432
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
5447-6229 |
7.17e-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: 44.27 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5447 RLVKKMSTAKVQLETNLLQwaDYSSSYSQLQQWITDREAklQQACEQKIVKSKRGQpglssgLSERKANLRQTNNIVQDI 5526
Cdd:TIGR00606 195 RQTQGQKVQEHQMELKYLK--QYKEKACEIRDQITSKEA--QLESSREIVKSYENE------LDPLKNRLKEIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5527 VSFEPMIQSVTSKAsvLQQGAPGTEISDK----YENLTKQAKDLYEKQKNTIESY-QSLIDAGNEFATWLRNAKERLSKC 5601
Cdd:TIGR00606 265 MKLDNEIKALKSRK--KQMEKDNSELELKmekvFQGTDEQLNDLYHNHQRTVREKeRELVDCQRELEKLNKERRLLNQEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5602 SE---PTGDKQALAEKTH----------QLKILQGEL------PEGAQKLKNALE---QGEIACRSAEPEDCEIIEQEVA 5659
Cdd:TIGR00606 343 TEllvEQGRLQLQADRHQehirardsliQSLATRLELdgfergPFSERQIKNFHTlviERQEDEAKTAAQLCADLQSKER 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5660 LLQEEFDAYREALNKAKDYLEVGIVKWSDYQDQYTEALEWLSKTEALVQSYNKLQDSLIQKKVVLEQFQGHLQTLFDWQK 5739
Cdd:TIGR00606 423 LKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5740 TLDDLNMKAQVLLETCSDTRISNAIMQLTTKYNALLTLAKEVMRRLEMHYQEHQQHHSLYEECQSWIEKTREKLSECEQI 5819
Cdd:TIGR00606 503 VKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5820 PGTLNEVQIKLNTVKNLRQGFETGQNKLRYLLELKEKVIMNTEQN-----GAAKIQEDTEALKQDFDKLLVDLNDVRQKL 5894
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcGSQDEESDLERLKEEIEKSSKQRAMLAGAT 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5895 ANRLAQLEE--------------IFKLYKILIEWLEDVEPSVKTSDEFLNDLSEKRAALEKFR------------VIQRD 5948
Cdd:TIGR00606 663 AVYSQFITQltdenqsccpvcqrVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRdemlglapgrqsIIDLK 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 5949 INGHNDIVEKIN------QRLK---EDNSLDLKDFQPGLTKFDDLQTQVNkIIESLENQVNSHE-KYKQAYNELQDW-LR 6017
Cdd:TIGR00606 743 EKEIPELRNKLQkvnrdiQRLKndiEEQETLLGTIMPEEESAKVCLTDVT-IMERFQMELKDVErKIAQQAAKLQGSdLD 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6018 RTRIEVEQcadchgekdQVESRLNRLGDIQSSSLEGKALLEACEELSQAVIATSGSEGQDNV------------AQEIKH 6085
Cdd:TIGR00606 822 RTVQQVNQ---------EKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLqigtnlqrrqqfEEQLVE 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 6086 LTSEWETLQTISRDARSSlescLAAWQTFLQKFnkinlwiETMNKRVTKSQEGENKTPEDLVN--AKKLLEEVLAEKDNV 6163
Cdd:TIGR00606 893 LSTEVQSLIREIKDAKEQ----DSPLETFLEKD-------QQEKEELISSKETSNKKAQDKVNdiKEKVKNIHGYMKDIE 961
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320544542 6164 EDLNDNCEllmeqsactrirDQTIETQANYTKL---LTSAQGLVAKIEKNLSDHTEFLNYKKEMDAWIE 6229
Cdd:TIGR00606 962 NKIQDGKD------------DYLKQKETELNTVnaqLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQ 1018
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
10938-11344 |
7.83e-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: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10938 ADVGLDASALMQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDIsreapqnpkESEEQLA 11017
Cdd:COG3096 280 RRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTAL---------RQQEKIE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11018 ALRAHLQTLA-RTEEQLRQLKERHqnsevapsvassdddgilEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEAL-RLW 11095
Cdd:COG3096 351 RYQEDLEELTeRLEEQEEVVEEAA------------------EQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqTRA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11096 RQYLQHVQSflscaipedyssLREQQQLCAI----------HQNLLISQQSVLSETPLESE--LSEQyKALTNLHNETLS 11163
Cdd:COG3096 413 IQYQQAVQA------------LEKARALCGLpdltpenaedYLAAFRAKEQQATEEVLELEqkLSVA-DAARRQFEKAYE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11164 RIMQRNGELERRvSGWNAYRQQLAallDWLRQR-EAER-NALQLRYIHLKRVPHLKHRLDAMIQQLDQGEQQS------- 11234
Cdd:COG3096 480 LVCKIAGEVERS-QAWQTARELLR---RYRSQQaLAQRlQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQldaaeel 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11235 KALQEQQQELARHCDDALATA------MRMEQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKL 11308
Cdd:COG3096 556 EELLAELEAQLEELEEQAAEAveqrseLRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQL 635
|
410 420 430
....*....|....*....|....*....|....*.
gi 320544542 11309 LDANSEslptqpaaIEQLLGSLRAQRVQLGAQVSAL 11344
Cdd:COG3096 636 LERERE--------ATVERDELAARKQALESQIERL 663
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
8159-8372 |
8.68e-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: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8159 GQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEACEEWDQCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQLgfcE 8238
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI---A 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8239 KTLADINVQKTKLRlsiEKLEVHFRNGMGGDPRL---SENVDDLVRVLDGLGELV----------KAKSQSLEQTLAQID 8305
Cdd:COG4942 94 ELRAELEAQKEELA---ELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAparreqaeelRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 8306 VYQQQMQSLRQRIIQEEQQLRLVMAptylphDRERALAE---QQDLITQELDELLQSLSSVEDGIANMNQ 8372
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA------ERQKLLARlekELAELAAELAELQQEAEELEALIARLEA 234
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
10844-11250 |
9.21e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.02 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10844 EQIESAVQEAVVAWNDTSENLQQLRTRYqravelwdKYRNASAAVKNSIDQQMDAVKSLEQPLDALQHAKVCQDNLTTQN 10923
Cdd:PRK10246 443 AQLQVAIQNVTQEQTQRNAALNEMRQRY--------KEKTQQLADVKTICEQEARIKDLEAQRAQLQAGQPCPLCGSTSH 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10924 DRI-----LEL------RDIVAKIAADVGlDASALMQGELDALGQRLAECKDAITTLANVAETQDKERKEL--DKEVTLa 10990
Cdd:PRK10246 515 PAVeayqaLEPgvnqsrLDALEKEVKKLG-EEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVcaSLNITL- 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 10991 kayfnNVQQDISrEAPQNPKESEEQL----------AALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGilev 11060
Cdd:PRK10246 593 -----QPQDDIQ-PWLDAQEEHERQLrllsqrhelqGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDE---- 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11061 LALWQKIFQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLC-AIHQNLLISQQSVLS 11139
Cdd:PRK10246 663 EASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQClSLHSQLQTLQQQDVL 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320544542 11140 ETPLESELSEQYK-ALTN-------------LHNETLSRIMQRNGELERRvsgwnayRQQLAALLDWLRQREAERNALQL 11205
Cdd:PRK10246 743 EAQRLQKAQAQFDtALQAsvfddqqaflaalLDEETLTQLEQLKQNLENQ-------RQQAQTLVTQTAQALAQHQQHRP 815
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320544542 11206 RYIHLK-RVPHLKHRLDAMIQQL-----DQGE------------QQSKALQEQQQELARHCDD 11250
Cdd:PRK10246 816 DGLDLTvTVEQIQQELAQLAQQLrenttRQGEirqqlkqdadnrQQQQALMQQIAQATQQVED 878
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