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Conserved domains on  [gi|1677537836|ref|NP_004014|]
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dystrophin isoform Dp140bc [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
665-826 3.68e-116

EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. 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 involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). 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. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.


:

Pssm-ID: 320004  Cd Length: 162  Bit Score: 356.26  E-value: 3.68e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  665 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 744
Cdd:cd16246      1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  745 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 824
Cdd:cd16246     81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                   ..
gi 1677537836  825 MR 826
Cdd:cd16246    161 MR 162
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
851-899 1.99e-30

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


:

Pssm-ID: 239074  Cd Length: 49  Bit Score: 113.99  E-value: 1.99e-30
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1677537836  851 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 899
Cdd:cd02334      1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
230-473 1.22e-23

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: 100.21  E-value: 1.22e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  230 LLQQFPLDLEKFLAWLTEAETTANVLQDAtrkerllEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGS 309
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG-------DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGH 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  310 DDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELLVWLQLKDDELSRQaPIGGDFPAVQKQNDVHR 389
Cdd:cd00176     72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHK 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  390 AFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKI 469
Cdd:cd00176    150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------------IEEKLEELNERWEELLELAEERQKKL 209

                   ....
gi 1677537836  470 DETL 473
Cdd:cd00176    210 EEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
12-228 5.44e-23

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: 98.29  E-value: 5.44e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   12 LADFNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIIT 91
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   92 DRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAkEEAEQVLGQARAKLESwKEGPYTVDAIQKKITETKQLAKDLR 171
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1677537836  172 QWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETH 228
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
474-580 1.77e-13

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: 67.73  E-value: 1.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  474 ERLRELQEATDELDLKLRQAEVIKgSWQPVGDLLiDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYN 553
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 1677537836  554 LSTLEDLNTRWKLLQVAVEDRVRQLHE 580
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
599-628 2.25e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


:

Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 53.69  E-value: 2.25e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 1677537836  599 GPWERAISPNKVPYYINHETQTTCWDHPKM 628
Cdd:cd00201      2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
 
Name Accession Description Interval E-value
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
665-826 3.68e-116

EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. 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 involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). 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. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.


Pssm-ID: 320004  Cd Length: 162  Bit Score: 356.26  E-value: 3.68e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  665 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 744
Cdd:cd16246      1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  745 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 824
Cdd:cd16246     81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                   ..
gi 1677537836  825 MR 826
Cdd:cd16246    161 MR 162
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
629-747 4.46e-57

EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 462668  Cd Length: 123  Bit Score: 192.75  E-value: 4.46e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  629 TELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLK--QNDQPMDILQIINCLTTIYDRLEQEHN 706
Cdd:pfam09068    1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1677537836  707 N--LVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLC 747
Cdd:pfam09068   81 TthQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
851-899 1.99e-30

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 113.99  E-value: 1.99e-30
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1677537836  851 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 899
Cdd:cd02334      1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
230-473 1.22e-23

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: 100.21  E-value: 1.22e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  230 LLQQFPLDLEKFLAWLTEAETTANVLQDAtrkerllEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGS 309
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG-------DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGH 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  310 DDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELLVWLQLKDDELSRQaPIGGDFPAVQKQNDVHR 389
Cdd:cd00176     72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHK 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  390 AFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKI 469
Cdd:cd00176    150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------------IEEKLEELNERWEELLELAEERQKKL 209

                   ....
gi 1677537836  470 DETL 473
Cdd:cd00176    210 EEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
12-228 5.44e-23

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: 98.29  E-value: 5.44e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   12 LADFNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIIT 91
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   92 DRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAkEEAEQVLGQARAKLESwKEGPYTVDAIQKKITETKQLAKDLR 171
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1677537836  172 QWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETH 228
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
847-892 2.99e-17

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 76.37  E-value: 2.99e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1677537836  847 AKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSgRVAKGHKM 892
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQM 45
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
848-891 7.25e-15

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 69.39  E-value: 7.25e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1677537836   848 KHQAKCNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHK 891
Cdd:smart00291    2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
474-580 1.77e-13

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: 67.73  E-value: 1.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  474 ERLRELQEATDELDLKLRQAEVIKgSWQPVGDLLiDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYN 553
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 1677537836  554 LSTLEDLNTRWKLLQVAVEDRVRQLHE 580
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
475-585 2.01e-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: 67.86  E-value: 2.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  475 RLRELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNL 554
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1677537836  555 STLEDLNTRWKLLQVAVEDRVRQLHEAHRDF 585
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQ 109
SPEC smart00150
Spectrin repeats;
15-116 3.95e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 63.50  E-value: 3.95e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836    15 FNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIITDRI 94
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 1677537836    95 ERIQNQWDEVQEHLQNRRQQLN 116
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
110-226 2.99e-11

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: 61.18  E-value: 2.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  110 NRRQQLNEMLKDSTQWLEakeEAEQVLgqarakleSWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLr 189
Cdd:pfam00435    1 LLLQQFFRDADDLESWIE---EKEALL--------SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI- 68
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1677537836  190 DYSADDTRKVHMITENINASWRSIHKRVSEREAALEE 226
Cdd:pfam00435   69 DEGHYASEEIQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
232-341 2.34e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 58.50  E-value: 2.34e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   232 QQFPLDLEKFLAWLTEAETTANvlqdatrKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGSDD 311
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLA-------SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPD 71
                            90       100       110
                    ....*....|....*....|....*....|
gi 1677537836   312 AVLLQRRLDNMNFKWSELRKKSLNIRSHLE 341
Cdd:smart00150   72 AEEIEERLEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
477-578 7.59e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 56.95  E-value: 7.59e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   477 RELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNLST 556
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEER 78
                            90       100
                    ....*....|....*....|..
gi 1677537836   557 LEDLNTRWKLLQVAVEDRVRQL 578
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
599-628 2.25e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 53.69  E-value: 2.25e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 1677537836  599 GPWERAISPNKVPYYINHETQTTCWDHPKM 628
Cdd:cd00201      2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
596-628 7.81e-09

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 52.22  E-value: 7.81e-09
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1677537836   596 SVQGPWERAISPNKVPYYINHETQTTCWDHPKM 628
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
600-626 2.92e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 50.20  E-value: 2.92e-08
                           10        20
                   ....*....|....*....|....*..
gi 1677537836  600 PWERAISPNKVPYYINHETQTTCWDHP 626
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
25-358 3.36e-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: 54.68  E-value: 3.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   25 WLSLLDQVIKSQRVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNlknktsnqeARTIITDRIERIQNQWDEV 104
Cdd:TIGR02168  647 IVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEK---------ALAELRKELEELEEELEQL 717
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  105 QEHLQNRRQQLNEMLKDstqwLEAKEEAEQVLGQARAKLESWKEgpytvDAIQKKITETKQLAKdlrqwqtnvdvaNDLA 184
Cdd:TIGR02168  718 RKELEELSRQISALRKD----LARLEAEVEQLEERIAQLSKELT-----ELEAEIEELEERLEE------------AEEE 776
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  185 LKLLRDYSADDTRKVhmitENINASWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAWLTEAETTANVLQDatRKERL 264
Cdd:TIGR02168  777 LAEAEAEIEELEAQI----EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE--QIEEL 850
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  265 LEDSKGVKELMKQWQDLQGEIEAHTDvyHNLDENSQKILRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASS 344
Cdd:TIGR02168  851 SEDIESLAAEIEELEELIEELESELE--ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
                          330
                   ....*....|....
gi 1677537836  345 DQWKRLHLSLQELL 358
Cdd:TIGR02168  929 LRLEGLEVRIDNLQ 942
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
60-585 4.11e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.30  E-value: 4.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   60 LEQRRPQLEELITAAQNLKNKTSNQEAR-TIITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQ 138
Cdd:PRK03918   174 IKRRIERLEKFIKRTENIEELIKEKEKElEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  139 ARAKLESWKEgpytvdaIQKKITETKQLAKDLRQwqtnvdvaNDLALKLLRDYsADDTRKVHMITENINASWRSIHKRVS 218
Cdd:PRK03918   254 KRKLEEKIRE-------LEERIEELKKEIEELEE--------KVKELKELKEK-AEEYIKLSEFYEEYLDELREIEKRLS 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  219 EREAALEETHRLLQqfplDLEKflawlteaettanvlqdatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDEN 298
Cdd:PRK03918   318 RLEEEINGIEERIK----ELEE-------------------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  299 SQkiLRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELlvwlqlkdDELSRQAPIGGDF 378
Cdd:PRK03918   375 ER--LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL--------KKAKGKCPVCGRE 444
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  379 PAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEqpLEGLEKLYQEPRELPPEERaqnvtrlLRKQAEEVNTEWEKL 458
Cdd:PRK03918   445 LTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKE--LRELEKVLKKESELIKLKE-------LAEQLKELEEKLKKY 515
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  459 NLhsadwqrkidETLERLRELQEATDELDLKLRQAevikgswqpvgdllIDSLQDHLEKVKALRGEIAPLKENvshVNDL 538
Cdd:PRK03918   516 NL----------EELEKKAEEYEKLKEKLIKLKGE--------------IKSLKKELEKLEELKKKLAELEKK---LDEL 568
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1677537836  539 ARQLTTLGIQLSPYNLSTLEDLntrwkllqvavEDRVRQLHEAHRDF 585
Cdd:PRK03918   569 EEELAELLKELEELGFESVEEL-----------EERLKELEPFYNEY 604
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
29-561 5.41e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 5.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   29 LDQVIKSQRVMVGDLEDINEMIIKQKATMQDLEQRrpqLEELITAAQNLKNKTSNQEARTI-ITDRIERIQNQWDEVQEH 107
Cdd:COG1196    283 LEEAQAEEYELLAELARLEQDIARLEERRRELEER---LEELEEELAELEEELEELEEELEeLEEELEEAEEELEEAEAE 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  108 LQNRRQQLNEMLKDSTQWLEA-KEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALK 186
Cdd:COG1196    360 LAEAEEALLEAEAELAEAEEElEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  187 LLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQfpLDLEKFLAWLTEAETTANVLQDATRKERLLE 266
Cdd:COG1196    440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL--AEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  267 DSKGVKELMKQWQDLQGEIEAHTDVYhnLDENSQKILRSLEGSDDAV---LLQRRLDNMNFKwselrkkSLNIRSHLEAS 343
Cdd:COG1196    518 GLRGLAGAVAVLIGVEAAYEAALEAA--LAAALQNIVVEDDEVAAAAieyLKAAKAGRATFL-------PLDKIRARAAL 588
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  344 SDQWKRLHLSLQELLVWLQLKDDELSRQAPIGGDFPAVQKQNDVHRAFKRELKTKEpvimsTLETVRIFLTEQPLEGLEK 423
Cdd:COG1196    589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG-----RLREVTLEGEGGSAGGSLT 663
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  424 LYQEPRELPPEERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQAEVIkgswqpV 503
Cdd:COG1196    664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE------L 737
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1677537836  504 GDLLIDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGiqlsPYNLSTLEDLN 561
Cdd:COG1196    738 LEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG----PVNLLAIEEYE 791
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
17-321 5.60e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 5.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   17 RAWTELTDWLSLLDQVIKSQRVmvgDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTI------- 89
Cdd:COG1196    232 LKLRELEAELEELEAELEELEA---ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiarle 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   90 -----ITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESwkegpyTVDAIQKKITETK 164
Cdd:COG1196    309 errreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------AEAELAEAEEELE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  165 QLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKvhmitENINASWRSIHKRVSEREAALEETHRLLQQfplDLEKFLAW 244
Cdd:COG1196    383 ELAEELLEALRAAAELAAQLEELEEAEEALLERL-----ERLEEELEELEEALAELEEEEEEEEEALEE---AAEEEAEL 454
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677537836  245 LTEAETTANVLQDATRKERLLEdskgvkelmKQWQDLQGEIEAHTDVYHNLdensQKILRSLEGSDDAVLLQRRLDN 321
Cdd:COG1196    455 EEEEEALLELLAELLEEAALLE---------AALAELLEELAEAAARLLLL----LEAEADYEGFLEGVKAALLLAG 518
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
229-331 1.40e-06

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: 48.08  E-value: 1.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  229 RLLQQFPLDLEKFLAWLTEAETTANvlqdatrKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILrsLEG 308
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLS-------SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI--DEG 71
                           90       100
                   ....*....|....*....|...
gi 1677537836  309 SDDAVLLQRRLDNMNFKWSELRK 331
Cdd:pfam00435   72 HYASEEIQERLEELNERWEQLLE 94
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
41-587 9.93e-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: 50.06  E-value: 9.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   41 GDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARtiITDRIERIQNQWDEVQEHLQNRRQQLNEMLK 120
Cdd:TIGR02168  351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS--LNNEIERLEARLERLEDRRERLQQEIEELLK 428
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  121 --DSTQWLEAK---EEAEQVLGQARAKLESWKEGPYTVDA-IQKKITETKQLAKDLRQWQTNVDVANDLaLKLLRDYSAD 194
Cdd:TIGR02168  429 klEEAELKELQaelEELEEELEELQEELERLEEALEELREeLEEAEQALDAAERELAQLQARLDSLERL-QENLEGFSEG 507
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  195 dtrkvhmITENINASWR--SIHKRVSER-------EAALE---------------ETHRLLQQF------------PLDL 238
Cdd:TIGR02168  508 -------VKALLKNQSGlsGILGVLSELisvdegyEAAIEaalggrlqavvvenlNAAKKAIAFlkqnelgrvtflPLDS 580
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  239 -----------------EKFLAWLTEAETT-----------------ANVLQDATRKERLL------------------- 265
Cdd:TIGR02168  581 ikgteiqgndreilkniEGFLGVAKDLVKFdpklrkalsyllggvlvVDDLDNALELAKKLrpgyrivtldgdlvrpggv 660
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  266 ------EDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRSL-EGSDDAVLLQRRLDNMNFKWSELRKKSLNIRS 338
Cdd:TIGR02168  661 itggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELeELEEELEQLRKELEELSRQISALRKDLARLEA 740
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  339 HLEASSDQWKRLHLSLQELLVWLQLKDDELsrqapiggdfpavQKQNDVHRAFKRELKTKEPVIMSTLEtvRIFLTEQPL 418
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIEELEERL-------------EEAEEELAEAEAEIEELEAQIEQLKE--ELKALREAL 805
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  419 EGLEKLYQEPRE-----LPPEERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQA 493
Cdd:TIGR02168  806 DELRAELTLLNEeaanlRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  494 EVIKGSWQPVGDLLIDSLQDHLEKVKALRGEIAPLKEnvsHVNDLARQLTTLGIQLspynLSTLEDLNTRWKL-LQVAV- 571
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRRELEELRE---KLAQLELRLEGLEVRI----DNLQERLSEEYSLtLEEAEa 958
                          650       660
                   ....*....|....*....|....*...
gi 1677537836  572 ------------EDRVRQLHEAHRDFGP 587
Cdd:TIGR02168  959 lenkieddeeeaRRRLKRLENKIKELGP 986
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
202-587 4.67e-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: 47.76  E-value: 4.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  202 ITENINASWRSIHKRVSEREAALEETHRLlQQFPLDLEKFLAWLTEAETTANVLQDATRkerllEDSKGVKELMKQWQDL 281
Cdd:TIGR02169  655 MTGGSRAPRGGILFSRSEPAELQRLRERL-EGLKRELSSLQSELRRIENRLDELSQELS-----DASRKIGEIEKEIEQL 728
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  282 QGEIEAHTDVYHNLDENSQKILRSLEGSDDAVL-LQRRLDNMNFKWSELRKKSLNIRSHLEASsdQWKRLHLSLQELlvw 360
Cdd:TIGR02169  729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKeLEARIEELEEDLHKLEEALNDLEARLSHS--RIPEIQAELSKL--- 803
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  361 lqlkDDELSRQAPIGGDfpAVQKQNDVHraFKRELKTKEpviMSTLETVRIFLTEQPLEgleklyqeprelppeeraqnv 440
Cdd:TIGR02169  804 ----EEEVSRIEARLRE--IEQKLNRLT--LEKEYLEKE---IQELQEQRIDLKEQIKS--------------------- 851
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  441 trlLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQAEVIKG--SWQpvgdllIDSLQDHLEKV 518
Cdd:TIGR02169  852 ---IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEelEAQ------IEKKRKRLSEL 922
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1677537836  519 KALRGEiapLKENVSHVNDLARQlttlgIQLSPYNLSTLEDlntrwkllqvaVEDRVRQLHEAHRDFGP 587
Cdd:TIGR02169  923 KAKLEA---LEEELSEIEDPKGE-----DEEIPEEELSLED-----------VQAELQRVEEEIRALEP 972
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
26-165 5.18e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 47.51  E-value: 5.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   26 LSLLDQVIKSQRVMVG-DLEDINEMIikqkatmQDLEQRRPQLEELITAAQNLKNKTsnqeartiitdriERIQNQWDEV 104
Cdd:PRK00409   497 LGLPENIIEEAKKLIGeDKEKLNELI-------ASLEELERELEQKAEEAEALLKEA-------------EKLKEELEEK 556
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677537836  105 QEHLQNRRQQLNEMLKDSTQWL--EAKEEAEQVLGQARaklESWKEGPYTVDAiqKKITETKQ 165
Cdd:PRK00409   557 KEKLQEEEDKLLEEAEKEAQQAikEAKKEADEIIKELR---QLQKGGYASVKA--HELIEARK 614
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
60-526 5.19e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 5.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   60 LEQRRPQLEELITAAQNLKNKTSNQEARTIITDRIERIQNQwdevQEHLQNRRQQLNEMLKDSTQWLEAKeeaeqvlgQA 139
Cdd:COG4717     70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE----LEELREELEKLEKLLQLLPLYQELE--------AL 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  140 RAKLEswkEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENINaswrsihkRVSE 219
Cdd:COG4717    138 EAELA---ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE--------ELQQ 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  220 REAALEEthrllqqfpldlekflawltEAETTANVLQDATRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVyHNLDENS 299
Cdd:COG4717    207 RLAELEE--------------------ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAL-LALLGLG 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  300 QKILRSLEGSDDAVLLQRRLdnMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELLVWlqLKDDELSRQAPIGGDFP 379
Cdd:COG4717    266 GSLLSLILTIAGVLFLVLGL--LALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL--LAALGLPPDLSPEELLE 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  380 AVQKQNDVHRAFKRELKTKEPV-IMSTLETVRIFLTEQPLEGLEKLY------QEPRELppEERAQNVTRLLRKQAEEVN 452
Cdd:COG4717    342 LLDRIEELQELLREAEELEEELqLEELEQEIAALLAEAGVEDEEELRaaleqaEEYQEL--KEELEELEEQLEELLGELE 419
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677537836  453 TEWEKLNLhsADWQRKIDETLERLRELQEATDELDLKLRQAEVIKGSWQpvGDLLIDSLQDHLEKVKALRGEIA 526
Cdd:COG4717    420 ELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLE--EDGELAELLQELEELKAELRELA 489
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
435-584 6.12e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 6.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  435 ERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDlkLRQAEVIKGswqpvgdlLIDSLQDH 514
Cdd:COG4913    284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG--GDRLEQLER--------EIERLERE 353
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  515 LEKVKALRGEiaplkenvshvndLARQLTTLGIQLsPYNLSTLEDLNTRWKLLQVAVEDRVRQLHEAHRD 584
Cdd:COG4913    354 LEERERRRAR-------------LEALLAALGLPL-PASAEEFAALRAEAAALLEALEEELEALEEALAE 409
 
Name Accession Description Interval E-value
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
665-826 3.68e-116

EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. 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 involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). 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. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.


Pssm-ID: 320004  Cd Length: 162  Bit Score: 356.26  E-value: 3.68e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  665 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 744
Cdd:cd16246      1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  745 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 824
Cdd:cd16246     81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                   ..
gi 1677537836  825 MR 826
Cdd:cd16246    161 MR 162
EFh_DMD_like cd16242
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ...
665-826 2.04e-105

EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes dystrophin and its two paralogs, utrophin and DRP-2. Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. 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 also involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. 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. DRP-2 is mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. The dystrophins subfamily has been characterized by a compact cluster of domains comprising a WW domain, four EF-hand-like motifs and a ZZ-domain, followed by two syntrophin binding sites (SBSs) and a looser region with two coiled-coils.


Pssm-ID: 320000  Cd Length: 163  Bit Score: 327.66  E-value: 2.04e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  665 SLSAACDALDQHNLK-QNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGI 743
Cdd:cd16242      1 SLSTAIEAFDQHGLRaQNDKLIDVPDMITCLTTIYEALEEEHPTLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSFKVGL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  744 ISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLD 823
Cdd:cd16242     81 VLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSNIEPSVRSCFEKAGEKPEISAAHFLD 160

                   ...
gi 1677537836  824 WMR 826
Cdd:cd16242    161 WLK 163
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
666-826 4.44e-86

EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. 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.


Pssm-ID: 320005  Cd Length: 162  Bit Score: 275.24  E-value: 4.44e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  666 LSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIIS 745
Cdd:cd16247      2 LNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLMS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  746 LCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWM 825
Cdd:cd16247     82 LSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDWM 161

                   .
gi 1677537836  826 R 826
Cdd:cd16247    162 R 162
EFh_DRP-2 cd16248
EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin ...
665-825 3.53e-81

EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin homologue mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. Like dystrophin, DRP-2 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 only two spectrin repeats (SRs) and a WW domain.


Pssm-ID: 320006  Cd Length: 162  Bit Score: 262.04  E-value: 3.53e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  665 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 744
Cdd:cd16248      1 TLSSATEIFTEHELQMSERVMDVVEVIHCLTALYERLEEERGILVNVPLCVDMCLNWLLNVYDSGRNGKIRVLSFKTGIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  745 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 824
Cdd:cd16248     81 CLCNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAFGGSNVEPSVRSCFRFAPGKPVIELSQFLEW 160

                   .
gi 1677537836  825 M 825
Cdd:cd16248    161 M 161
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
666-825 4.39e-68

EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family 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. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 319999  Cd Length: 163  Bit Score: 225.61  E-value: 4.39e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  666 LSAACDALDQHNLKQ-NDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 744
Cdd:cd15901      2 LSTVLSVFDRHGLSGsQDSVLDCEELETILTELYIKLNKRRPDLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVKIALI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  745 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 824
Cdd:cd15901     82 TLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVEAAVESCFQLARSRVGVSEDTFLSW 161

                   .
gi 1677537836  825 M 825
Cdd:cd15901    162 L 162
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
629-747 4.46e-57

EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 462668  Cd Length: 123  Bit Score: 192.75  E-value: 4.46e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  629 TELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLK--QNDQPMDILQIINCLTTIYDRLEQEHN 706
Cdd:pfam09068    1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1677537836  707 N--LVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLC 747
Cdd:pfam09068   81 TthQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
EF-hand_3 pfam09069
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
751-842 6.30e-50

EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 462669  Cd Length: 90  Bit Score: 170.95  E-value: 6.30e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  751 LEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGsnIEPSVRSCFQFANNKPEIEAALFLDWMRLEPQ 830
Cdd:pfam09069    1 LVDKYRYLFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGG--IEPSVRSCFEQVGGKPKITLNHFLDWLMSEPQ 78
                           90
                   ....*....|..
gi 1677537836  831 SMVWLPVLHRVA 842
Cdd:pfam09069   79 SLVWLPVLHRLA 90
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
851-899 1.99e-30

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 113.99  E-value: 1.99e-30
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1677537836  851 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 899
Cdd:cd02334      1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
230-473 1.22e-23

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: 100.21  E-value: 1.22e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  230 LLQQFPLDLEKFLAWLTEAETTANVLQDAtrkerllEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGS 309
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG-------DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGH 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  310 DDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELLVWLQLKDDELSRQaPIGGDFPAVQKQNDVHR 389
Cdd:cd00176     72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHK 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  390 AFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKI 469
Cdd:cd00176    150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------------IEEKLEELNERWEELLELAEERQKKL 209

                   ....
gi 1677537836  470 DETL 473
Cdd:cd00176    210 EEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
12-228 5.44e-23

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: 98.29  E-value: 5.44e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   12 LADFNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIIT 91
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   92 DRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAkEEAEQVLGQARAKLESwKEGPYTVDAIQKKITETKQLAKDLR 171
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1677537836  172 QWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETH 228
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
EFh_DAH cd16245
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ...
665-825 5.98e-22

EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and similar proteins; DAH, the product of the dah (discontinuous actin hexagon) gene, is a Drosophila homolog to vertebrate dystrotelin. It is tightly membrane-associated and highly phosphorylated in a time-dependent fashion. DAH plays an essential role in the process of cellularization, and is associated with vesicles that convene at the cleavage furrow. The absence of DAH leads the severe disruption of the cleavage furrows around the nuclei and development stalls. DAH contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils.


Pssm-ID: 320003 [Multi-domain]  Cd Length: 164  Bit Score: 93.90  E-value: 5.98e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  665 SLSAACDALDQHNLKQND-----QPMDILQIINcltTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSF 739
Cdd:cd16245      1 PLKLIMGVFDRHQLSNSEnnlclPPDELEAVLH---DIYFAAEKLGNFNIDVDLATELLANLFLNVFDPERKKSISVLEL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  740 KTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAA 819
Cdd:cd16245     78 KVFLTLLCGSSLQEKYLYLFQLLADHNNCVSRKRLEALLKSLAKLLSYLGEDVAFGSHLIELAVEQCFENSPGLVGLTEY 157

                   ....*.
gi 1677537836  820 LFLDWM 825
Cdd:cd16245    158 QFIGWW 163
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
684-825 3.15e-19

EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the dystrophin-glycoprotein complex (DGC). They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. The family includes two paralogs dystrobrevins, alpha- and beta-dystrobrevin, both of which are cytoplasmic components of the dystrophin-associated protein complex that function as scaffold proteins in signal transduction and intracellular transport. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. The dystrobrevins 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, dystrobrevins contain one or two syntrophin binding sites (SBSs).


Pssm-ID: 320002 [Multi-domain]  Cd Length: 161  Bit Score: 85.75  E-value: 3.15e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  684 PMDILQIINCLTTIY----DRLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLF 759
Cdd:cd16244     22 ELSVSRLETLLSSIYyqlnKRLPTTHQ--IDVDQSISLLLNWLLAAYDPEATGRLTVFSVKVALSTLCAGKLVDKLRYIF 99
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677537836  760 KQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSniEPSVRSCFQfANNKPEIEAalFLDWM 825
Cdd:cd16244    100 SQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYN--ESAARSCFP-GQSKVTVND--FLDVM 160
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
847-892 2.99e-17

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 76.37  E-value: 2.99e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1677537836  847 AKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSgRVAKGHKM 892
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQM 45
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
124-343 7.51e-16

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: 77.49  E-value: 7.51e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  124 QWLEAKEEAEQVLGQARAKLESWkEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDYSaDDTRKVHMIT 203
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  204 ENINASWRSIHKRVSEREAALEETHRLLQQFpLDLEKFLAWLTEAETTANvlqdatrKERLLEDSKGVKELMKQWQDLQG 283
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALA-------SEDLGKDLESVEELLKKHKELEE 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  284 EIEAHTDVYHNLDENSQKiLRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEAS 343
Cdd:cd00176    154 ELEAHEPRLKSLNELAEE-LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
848-891 7.25e-15

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 69.39  E-value: 7.25e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1677537836   848 KHQAKCNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHK 891
Cdd:smart00291    2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
346-582 2.92e-14

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: 72.86  E-value: 2.92e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  346 QWKRLHLSLQELLVWLQLKDDELSRQAPiGGDFPAVQKQNDVHRAFKRELKTKEPVImstletvriflteqplEGLEKLY 425
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERV----------------EALNELG 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  426 QEPRELPPEERAQnvtrlLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEAtDELDLKLRQAEVIKGSWQPVGD 505
Cdd:cd00176     64 EQLIEEGHPDAEE-----IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGKD 137
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677537836  506 LliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNL-STLEDLNTRWKLLQVAVEDRVRQLHEAH 582
Cdd:cd00176    138 L--ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIeEKLEELNERWEELLELAEERQKKLEEAL 213
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
474-580 1.77e-13

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: 67.73  E-value: 1.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  474 ERLRELQEATDELDLKLRQAEVIKgSWQPVGDLLiDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYN 553
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 1677537836  554 LSTLEDLNTRWKLLQVAVEDRVRQLHE 580
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
475-585 2.01e-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: 67.86  E-value: 2.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  475 RLRELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNL 554
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1677537836  555 STLEDLNTRWKLLQVAVEDRVRQLHEAHRDF 585
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQ 109
EFh_DYTN cd16243
EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate ...
694-826 2.98e-12

EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate orthologue of Drosophila DAH, which is involved in the synchronised cellularization of thousands of nuclei in the syncytial early fly embryo (a specialised form of cytokinesis). Dystrotelin is mainly expressed in the developing central nervous system (CNS) and adult nervous and muscular tissues. Heterologously expressed dystrotelin protein localizes spontaneously to the cytoplasmic membrane, and possibly to the endoplasmic reticulum (ER). Dystrotelin is not critical for mammalian development. It may be involved in other forms of cytokinesis. Its N-terminal region contains 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. The C-terminal region is extremely divergent. Unlike other superfamily members, dystrophin or dystrobrevin, the residues directly involved in beta-dystroglycan binding are not conserved in dystrotelin, which makes it unlikely that dystrotelin interacts with this ligand. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 320001  Cd Length: 163  Bit Score: 65.87  E-value: 2.98e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  694 LTTIYDRLEQEHNNLVNVPLCvDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFK----QVASSTGFC 769
Cdd:cd16243     31 LERLFQSASQEVPGQVSAEAT-EQTCRLLFRLYDREQTGFVSLRSVEAALIALSGDTLSAKYRALFQlyesGQGGSSGSI 109
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1677537836  770 DQRRLGLLLHDSIQIPRQLGEVASFGgsNIEPSVRSCFQFANNkPEIEAALFLDWMR 826
Cdd:cd16243    110 TRSGLRVLLQDLSQIPAVVQESHVFG--NVETAVRSCFSGVLT-ASISEEHFLSWLQ 163
SPEC smart00150
Spectrin repeats;
15-116 3.95e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 63.50  E-value: 3.95e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836    15 FNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIITDRI 94
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 1677537836    95 ERIQNQWDEVQEHLQNRRQQLN 116
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
110-226 2.99e-11

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: 61.18  E-value: 2.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  110 NRRQQLNEMLKDSTQWLEakeEAEQVLgqarakleSWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLr 189
Cdd:pfam00435    1 LLLQQFFRDADDLESWIE---EKEALL--------SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI- 68
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1677537836  190 DYSADDTRKVHMITENINASWRSIHKRVSEREAALEE 226
Cdd:pfam00435   69 DEGHYASEEIQERLEELNERWEQLLELAAERKQKLEE 105
EFh_DTNB cd16250
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ...
700-825 1.48e-10

EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin beta (DTN-B), is a dystrophin-related protein that is restricted to non-muscle tissues and is abundantly expressed in brain, lung, kidney, and liver. It may be involved in regulating chromatin dynamics, possibly playing a role in neuronal differentiation, through the interactions with the high mobility group HMG20 proteins iBRAF/HMG20a and BRAF35 /HMG20b. It also binds to and represses the promoter of synapsin I, a neuronal differentiation gene. Moreover, beta-dystrobrevin functions as a kinesin-binding receptor involved in brain development via the association with the extracellular matrix components pancortins. Furthermore, beta-dystrobrevin binds directly to dystrophin and is a cytoplasmic component of the dystrophin-associated glycoprotein complex, a multimeric protein complex that links the extracellular matrix to the cortical actin cytoskeleton and acts as a scaffold for signaling proteins such as protein kinase A. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. Beta-dystrobrevin 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, beta-dystrobrevin contain two syntrophin binding sites (SBSs).


Pssm-ID: 320008  Cd Length: 161  Bit Score: 60.81  E-value: 1.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  700 RLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLH 779
Cdd:cd16250     42 RLPSTHQ--ISVEQSISLLLNFMIAAYDSEGHGKLTVFSVKAMLATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLR 119
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1677537836  780 DSIQIPRQLGEVASFGGSniEPSVRSCFQfanNKPEIEAALFLDWM 825
Cdd:cd16250    120 EVLKLPTAVFEGPSFGYT--EHSVRTCFP---QQKKIMLNMFLDTM 160
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
694-807 1.66e-10

EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin alpha (DTN-A), or dystrophin-related protein 3 (DRP-3), is the mammalian ortholog of the Torpedo 87 kDa postsynaptic protein that tightly associates with dystrophin. It is a cytoplasmic protein expressed predominantly in skeletal muscle, heart, lung, and brain. Alpha-dystrobrevin has been implicated in the regulation of acetylcholine receptor (AChR) aggregate density and patterning. It is also essential in the pathogenesis of dystrophin-dependent muscular dystrophies. It plays a critical role in the full functionality of dystrophin through increasing dystrophin's binding to the dystrophin-glycoprotein complex (DGC), and provides protection during cardiac stress. Alpha-dystrobrevin binds to the intermediate filament proteins syncoilin and beta-synemin, thereby linking the dystrophin-associated protein complex (DAPC) to the intermediate filament network. Moreover, alpha-dystrobrevin involves in cell signaling via interaction with other proteins such as syntrophin, a modular adaptor protein that coordinates the assembly of the signaling proteins nitric oxide synthase, stress-activated protein kinase-3, and Grb2 to the DAPC. Furthermore, alpha-dystrobrevin plays an important role in muscle function, as well as in nuclear morphology maintenance through specific interaction with the nuclear lamina component lamin B1. In addition, alpha-dystrobrevin is required in dystrophin-associated protein scaffolding in brain. Absence of glial alpha-dystrobrevin causes abnormalities of the blood-brain barrier and progressive brain edema. Alpha-dystrobrevin 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, alpha-dystrobrevin contain two syntrophin binding sites (SBSs).


Pssm-ID: 320007  Cd Length: 161  Bit Score: 60.68  E-value: 1.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  694 LTTIY----DRLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFC 769
Cdd:cd16249     32 LSTIFyqlnKRMPTTHQ--INVEQSISLLLNFLLAAFDPEGHGKISVFAVKMALATLCGGKIMDKLRYIFSMISDSNGVM 109
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1677537836  770 DQRRLGLLLHDSIQIPRQLGEVASFGGSniEPSVRSCF 807
Cdd:cd16249    110 VYGRYDQFLREVLKLPTAVFEGPSFGYT--EQSARSCF 145
SPEC smart00150
Spectrin repeats;
232-341 2.34e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 58.50  E-value: 2.34e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   232 QQFPLDLEKFLAWLTEAETTANvlqdatrKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGSDD 311
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLA-------SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPD 71
                            90       100       110
                    ....*....|....*....|....*....|
gi 1677537836   312 AVLLQRRLDNMNFKWSELRKKSLNIRSHLE 341
Cdd:smart00150   72 AEEIEERLEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
477-578 7.59e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 56.95  E-value: 7.59e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   477 RELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNLST 556
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEER 78
                            90       100
                    ....*....|....*....|..
gi 1677537836   557 LEDLNTRWKLLQVAVEDRVRQL 578
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
599-628 2.25e-09

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 53.69  E-value: 2.25e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 1677537836  599 GPWERAISPNKVPYYINHETQTTCWDHPKM 628
Cdd:cd00201      2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
596-628 7.81e-09

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 52.22  E-value: 7.81e-09
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1677537836   596 SVQGPWERAISPNKVPYYINHETQTTCWDHPKM 628
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
600-626 2.92e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 50.20  E-value: 2.92e-08
                           10        20
                   ....*....|....*....|....*..
gi 1677537836  600 PWERAISPNKVPYYINHETQTTCWDHP 626
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
853-899 1.19e-07

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 48.97  E-value: 1.19e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1677537836  853 CNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRvaKGHKMHYPMVEY 899
Cdd:cd02249      3 CDGCLK-PIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
25-358 3.36e-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: 54.68  E-value: 3.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   25 WLSLLDQVIKSQRVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNlknktsnqeARTIITDRIERIQNQWDEV 104
Cdd:TIGR02168  647 IVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEK---------ALAELRKELEELEEELEQL 717
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  105 QEHLQNRRQQLNEMLKDstqwLEAKEEAEQVLGQARAKLESWKEgpytvDAIQKKITETKQLAKdlrqwqtnvdvaNDLA 184
Cdd:TIGR02168  718 RKELEELSRQISALRKD----LARLEAEVEQLEERIAQLSKELT-----ELEAEIEELEERLEE------------AEEE 776
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  185 LKLLRDYSADDTRKVhmitENINASWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAWLTEAETTANVLQDatRKERL 264
Cdd:TIGR02168  777 LAEAEAEIEELEAQI----EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE--QIEEL 850
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  265 LEDSKGVKELMKQWQDLQGEIEAHTDvyHNLDENSQKILRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASS 344
Cdd:TIGR02168  851 SEDIESLAAEIEELEELIEELESELE--ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
                          330
                   ....*....|....
gi 1677537836  345 DQWKRLHLSLQELL 358
Cdd:TIGR02168  929 LRLEGLEVRIDNLQ 942
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
60-585 4.11e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.30  E-value: 4.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   60 LEQRRPQLEELITAAQNLKNKTSNQEAR-TIITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQ 138
Cdd:PRK03918   174 IKRRIERLEKFIKRTENIEELIKEKEKElEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  139 ARAKLESWKEgpytvdaIQKKITETKQLAKDLRQwqtnvdvaNDLALKLLRDYsADDTRKVHMITENINASWRSIHKRVS 218
Cdd:PRK03918   254 KRKLEEKIRE-------LEERIEELKKEIEELEE--------KVKELKELKEK-AEEYIKLSEFYEEYLDELREIEKRLS 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  219 EREAALEETHRLLQqfplDLEKflawlteaettanvlqdatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDEN 298
Cdd:PRK03918   318 RLEEEINGIEERIK----ELEE-------------------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  299 SQkiLRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELlvwlqlkdDELSRQAPIGGDF 378
Cdd:PRK03918   375 ER--LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL--------KKAKGKCPVCGRE 444
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  379 PAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEqpLEGLEKLYQEPRELPPEERaqnvtrlLRKQAEEVNTEWEKL 458
Cdd:PRK03918   445 LTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKE--LRELEKVLKKESELIKLKE-------LAEQLKELEEKLKKY 515
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  459 NLhsadwqrkidETLERLRELQEATDELDLKLRQAevikgswqpvgdllIDSLQDHLEKVKALRGEIAPLKENvshVNDL 538
Cdd:PRK03918   516 NL----------EELEKKAEEYEKLKEKLIKLKGE--------------IKSLKKELEKLEELKKKLAELEKK---LDEL 568
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1677537836  539 ARQLTTLGIQLSPYNLSTLEDLntrwkllqvavEDRVRQLHEAHRDF 585
Cdd:PRK03918   569 EEELAELLKELEELGFESVEEL-----------EERLKELEPFYNEY 604
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
29-561 5.41e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 5.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   29 LDQVIKSQRVMVGDLEDINEMIIKQKATMQDLEQRrpqLEELITAAQNLKNKTSNQEARTI-ITDRIERIQNQWDEVQEH 107
Cdd:COG1196    283 LEEAQAEEYELLAELARLEQDIARLEERRRELEER---LEELEEELAELEEELEELEEELEeLEEELEEAEEELEEAEAE 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  108 LQNRRQQLNEMLKDSTQWLEA-KEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALK 186
Cdd:COG1196    360 LAEAEEALLEAEAELAEAEEElEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  187 LLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQfpLDLEKFLAWLTEAETTANVLQDATRKERLLE 266
Cdd:COG1196    440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL--AEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  267 DSKGVKELMKQWQDLQGEIEAHTDVYhnLDENSQKILRSLEGSDDAV---LLQRRLDNMNFKwselrkkSLNIRSHLEAS 343
Cdd:COG1196    518 GLRGLAGAVAVLIGVEAAYEAALEAA--LAAALQNIVVEDDEVAAAAieyLKAAKAGRATFL-------PLDKIRARAAL 588
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  344 SDQWKRLHLSLQELLVWLQLKDDELSRQAPIGGDFPAVQKQNDVHRAFKRELKTKEpvimsTLETVRIFLTEQPLEGLEK 423
Cdd:COG1196    589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG-----RLREVTLEGEGGSAGGSLT 663
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  424 LYQEPRELPPEERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQAEVIkgswqpV 503
Cdd:COG1196    664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE------L 737
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1677537836  504 GDLLIDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGiqlsPYNLSTLEDLN 561
Cdd:COG1196    738 LEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG----PVNLLAIEEYE 791
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
17-321 5.60e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 5.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   17 RAWTELTDWLSLLDQVIKSQRVmvgDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTI------- 89
Cdd:COG1196    232 LKLRELEAELEELEAELEELEA---ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiarle 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   90 -----ITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESwkegpyTVDAIQKKITETK 164
Cdd:COG1196    309 errreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------AEAELAEAEEELE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  165 QLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKvhmitENINASWRSIHKRVSEREAALEETHRLLQQfplDLEKFLAW 244
Cdd:COG1196    383 ELAEELLEALRAAAELAAQLEELEEAEEALLERL-----ERLEEELEELEEALAELEEEEEEEEEALEE---AAEEEAEL 454
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677537836  245 LTEAETTANVLQDATRKERLLEdskgvkelmKQWQDLQGEIEAHTDVYHNLdensQKILRSLEGSDDAVLLQRRLDN 321
Cdd:COG1196    455 EEEEEALLELLAELLEEAALLE---------AALAELLEELAEAAARLLLL----LEAEADYEGFLEGVKAALLLAG 518
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
15-117 1.33e-06

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: 48.08  E-value: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   15 FNRAWTELTDWLSLLDQVIKSQRvMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIITDRI 94
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSED-YGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID--EGHYASEEIQERL 82
                           90       100
                   ....*....|....*....|...
gi 1677537836   95 ERIQNQWDEVQEHLQNRRQQLNE 117
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
229-331 1.40e-06

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: 48.08  E-value: 1.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  229 RLLQQFPLDLEKFLAWLTEAETTANvlqdatrKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILrsLEG 308
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLS-------SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI--DEG 71
                           90       100
                   ....*....|....*....|...
gi 1677537836  309 SDDAVLLQRRLDNMNFKWSELRK 331
Cdd:pfam00435   72 HYASEEIQERLEELNERWEQLLE 94
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
853-896 1.74e-06

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 45.80  E-value: 1.74e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1677537836  853 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPM 896
Cdd:cd02338      3 CDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPM 46
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
41-587 9.93e-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: 50.06  E-value: 9.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   41 GDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARtiITDRIERIQNQWDEVQEHLQNRRQQLNEMLK 120
Cdd:TIGR02168  351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS--LNNEIERLEARLERLEDRRERLQQEIEELLK 428
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  121 --DSTQWLEAK---EEAEQVLGQARAKLESWKEGPYTVDA-IQKKITETKQLAKDLRQWQTNVDVANDLaLKLLRDYSAD 194
Cdd:TIGR02168  429 klEEAELKELQaelEELEEELEELQEELERLEEALEELREeLEEAEQALDAAERELAQLQARLDSLERL-QENLEGFSEG 507
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  195 dtrkvhmITENINASWR--SIHKRVSER-------EAALE---------------ETHRLLQQF------------PLDL 238
Cdd:TIGR02168  508 -------VKALLKNQSGlsGILGVLSELisvdegyEAAIEaalggrlqavvvenlNAAKKAIAFlkqnelgrvtflPLDS 580
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  239 -----------------EKFLAWLTEAETT-----------------ANVLQDATRKERLL------------------- 265
Cdd:TIGR02168  581 ikgteiqgndreilkniEGFLGVAKDLVKFdpklrkalsyllggvlvVDDLDNALELAKKLrpgyrivtldgdlvrpggv 660
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  266 ------EDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRSL-EGSDDAVLLQRRLDNMNFKWSELRKKSLNIRS 338
Cdd:TIGR02168  661 itggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELeELEEELEQLRKELEELSRQISALRKDLARLEA 740
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  339 HLEASSDQWKRLHLSLQELLVWLQLKDDELsrqapiggdfpavQKQNDVHRAFKRELKTKEPVIMSTLEtvRIFLTEQPL 418
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIEELEERL-------------EEAEEELAEAEAEIEELEAQIEQLKE--ELKALREAL 805
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  419 EGLEKLYQEPRE-----LPPEERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQA 493
Cdd:TIGR02168  806 DELRAELTLLNEeaanlRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  494 EVIKGSWQPVGDLLIDSLQDHLEKVKALRGEIAPLKEnvsHVNDLARQLTTLGIQLspynLSTLEDLNTRWKL-LQVAV- 571
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRRELEELRE---KLAQLELRLEGLEVRI----DNLQERLSEEYSLtLEEAEa 958
                          650       660
                   ....*....|....*....|....*...
gi 1677537836  572 ------------EDRVRQLHEAHRDFGP 587
Cdd:TIGR02168  959 lenkieddeeeaRRRLKRLENKIKELGP 986
SPEC smart00150
Spectrin repeats;
113-225 1.31e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.01  E-value: 1.31e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   113 QQLNEMLKDSTQWLEAKEeaeqvlgqaraKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDyS 192
Cdd:smart00150    1 QQFLRDADELEAWLEEKE-----------QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-G 68
                            90       100       110
                    ....*....|....*....|....*....|...
gi 1677537836   193 ADDTRKVHMITENINASWRSIHKRVSEREAALE 225
Cdd:smart00150   69 HPDAEEIEERLEELNERWEELKELAEERRQKLE 101
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
202-587 4.67e-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: 47.76  E-value: 4.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  202 ITENINASWRSIHKRVSEREAALEETHRLlQQFPLDLEKFLAWLTEAETTANVLQDATRkerllEDSKGVKELMKQWQDL 281
Cdd:TIGR02169  655 MTGGSRAPRGGILFSRSEPAELQRLRERL-EGLKRELSSLQSELRRIENRLDELSQELS-----DASRKIGEIEKEIEQL 728
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  282 QGEIEAHTDVYHNLDENSQKILRSLEGSDDAVL-LQRRLDNMNFKWSELRKKSLNIRSHLEASsdQWKRLHLSLQELlvw 360
Cdd:TIGR02169  729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKeLEARIEELEEDLHKLEEALNDLEARLSHS--RIPEIQAELSKL--- 803
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  361 lqlkDDELSRQAPIGGDfpAVQKQNDVHraFKRELKTKEpviMSTLETVRIFLTEQPLEgleklyqeprelppeeraqnv 440
Cdd:TIGR02169  804 ----EEEVSRIEARLRE--IEQKLNRLT--LEKEYLEKE---IQELQEQRIDLKEQIKS--------------------- 851
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  441 trlLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQAEVIKG--SWQpvgdllIDSLQDHLEKV 518
Cdd:TIGR02169  852 ---IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEelEAQ------IEKKRKRLSEL 922
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1677537836  519 KALRGEiapLKENVSHVNDLARQlttlgIQLSPYNLSTLEDlntrwkllqvaVEDRVRQLHEAHRDFGP 587
Cdd:TIGR02169  923 KAKLEA---LEEELSEIEDPKGE-----DEEIPEEELSLED-----------VQAELQRVEEEIRALEP 972
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
26-165 5.18e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 47.51  E-value: 5.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   26 LSLLDQVIKSQRVMVG-DLEDINEMIikqkatmQDLEQRRPQLEELITAAQNLKNKTsnqeartiitdriERIQNQWDEV 104
Cdd:PRK00409   497 LGLPENIIEEAKKLIGeDKEKLNELI-------ASLEELERELEQKAEEAEALLKEA-------------EKLKEELEEK 556
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677537836  105 QEHLQNRRQQLNEMLKDSTQWL--EAKEEAEQVLGQARaklESWKEGPYTVDAiqKKITETKQ 165
Cdd:PRK00409   557 KEKLQEEEDKLLEEAEKEAQQAikEAKKEADEIIKELR---QLQKGGYASVKA--HELIEARK 614
SPEC smart00150
Spectrin repeats;
349-470 9.02e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 42.70  E-value: 9.02e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   349 RLHLSLQELLVWLQLKDDELSrQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEklyqep 428
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE------ 74
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 1677537836   429 relppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKID 470
Cdd:smart00150   75 ---------------IEERLEELNERWEELKELAEERRQKLE 101
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
853-899 1.24e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 40.52  E-value: 1.24e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1677537836  853 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRvakgHKMHYPMVEY 899
Cdd:cd02339      3 CDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDK----HDLEHRFYRY 45
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
853-898 1.97e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.


Pssm-ID: 239085  Cd Length: 49  Bit Score: 40.27  E-value: 1.97e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1677537836  853 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVE 898
Cdd:cd02345      3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
92-307 4.18e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 4.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   92 DRIERIQNQWD---EVQEHLQNRRQQ---LNEMLKDSTQWLEAKEEAEQvLGQARAKLESWKEGpYTVDAIQKKIT---- 161
Cdd:COG4913    225 EAADALVEHFDdleRAHEALEDAREQielLEPIRELAERYAAARERLAE-LEYLRAALRLWFAQ-RRLELLEAELEelra 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  162 ETKQLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENInASWRSIHKRVSEREAALEE-THRLLQQFPLDLEK 240
Cdd:COG4913    303 ELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREI-ERLERELEERERRRARLEAlLAALGLPLPASAEE 381
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1677537836  241 FLAWLTEAETTANVLQDATRK--ERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRSLE 307
Cdd:COG4913    382 FAALRAEAAALLEALEEELEAleEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
60-526 5.19e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 5.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   60 LEQRRPQLEELITAAQNLKNKTSNQEARTIITDRIERIQNQwdevQEHLQNRRQQLNEMLKDSTQWLEAKeeaeqvlgQA 139
Cdd:COG4717     70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE----LEELREELEKLEKLLQLLPLYQELE--------AL 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  140 RAKLEswkEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENINaswrsihkRVSE 219
Cdd:COG4717    138 EAELA---ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE--------ELQQ 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  220 REAALEEthrllqqfpldlekflawltEAETTANVLQDATRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVyHNLDENS 299
Cdd:COG4717    207 RLAELEE--------------------ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAL-LALLGLG 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  300 QKILRSLEGSDDAVLLQRRLdnMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELLVWlqLKDDELSRQAPIGGDFP 379
Cdd:COG4717    266 GSLLSLILTIAGVLFLVLGL--LALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL--LAALGLPPDLSPEELLE 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  380 AVQKQNDVHRAFKRELKTKEPV-IMSTLETVRIFLTEQPLEGLEKLY------QEPRELppEERAQNVTRLLRKQAEEVN 452
Cdd:COG4717    342 LLDRIEELQELLREAEELEEELqLEELEQEIAALLAEAGVEDEEELRaaleqaEEYQEL--KEELEELEEQLEELLGELE 419
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677537836  453 TEWEKLNLhsADWQRKIDETLERLRELQEATDELDLKLRQAEVIKGSWQpvGDLLIDSLQDHLEKVKALRGEIA 526
Cdd:COG4717    420 ELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLE--EDGELAELLQELEELKAELRELA 489
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
42-542 6.37e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 6.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   42 DLEDINEMIIKQKATMQDLEQRRPQLEELITAAQ----------NLKNKTSNQEAR-TIITDRIERIQNQWDEVQ----- 105
Cdd:PRK03918   260 KIRELEERIEELKKEIEELEEKVKELKELKEKAEeyiklsefyeEYLDELREIEKRlSRLEEEINGIEERIKELEekeer 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  106 -EHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARaKLESwKEGPYTVDAIQKKITETKQLAKDLrqwqtnvdvandla 184
Cdd:PRK03918   340 lEELKKKLKELEKRLEELEERHELYEEAKAKKEELE-RLKK-RLTGLTPEKLEKELEELEKAKEEI-------------- 403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  185 lkllrdysaddTRKVHMITENINaswrSIHKRVSEREAALE-----------------ETHR--LLQQFPLDLEKFLAWL 245
Cdd:PRK03918   404 -----------EEEISKITARIG----ELKKEIKELKKAIEelkkakgkcpvcgreltEEHRkeLLEEYTAELKRIEKEL 468
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  246 TEAETTANVLQDATRK-ERLLEDSKGV---KELMKQWQDLQG--------EIEAHTDVYHNLDENSQKILRSLEGsddav 313
Cdd:PRK03918   469 KEIEEKERKLRKELRElEKVLKKESELiklKELAEQLKELEEklkkynleELEKKAEEYEKLKEKLIKLKGEIKS----- 543
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  314 lLQRRLDNMNfkwsELRKKSLNIRSHLEASSDQWKRLHLSLQEL-LVWLQLKDDELSRQAPIGGDFPAVQKQNDVHRAFK 392
Cdd:PRK03918   544 -LKKELEKLE----ELKKKLAELEKKLDELEEELAELLKELEELgFESVEELEERLKELEPFYNEYLELKDAEKELEREE 618
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  393 RELKTKEPVIMSTLEtvRIFLTEQPLEGLEKLYQEPRELPPEERAQNVTRL---LRKQAEEVNTEWEKLNLHSADWQRKI 469
Cdd:PRK03918   619 KELKKLEEELDKAFE--ELAETEKRLEELRKELEELEKKYSEEEYEELREEyleLSRELAGLRAELEELEKRREEIKKTL 696
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677537836  470 DETLERLRELQEATDELDlKLRQAevikgswqpvgdllIDSLQDHLEKVKALRGEiapLKEN-VSHVNDLARQL 542
Cdd:PRK03918   697 EKLKEELEEREKAKKELE-KLEKA--------------LERVEELREKVKKYKAL---LKERaLSKVGEIASEI 752
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
855-897 8.34e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 38.01  E-value: 8.34e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1677537836  855 ICKEC--PIIGFRYRSLKHFNYDICQSCffsgrVAKG-HKMHyPMV 897
Cdd:cd02340      2 ICDGCqgPIVGVRYKCLVCPDYDLCESC-----EAKGvHPEH-AML 41
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
33-542 9.03e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 9.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   33 IKSQRVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTIITDRIERIQNQWDEVQEHLqnrr 112
Cdd:COG4717     73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERL---- 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  113 QQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKE--GPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRD 190
Cdd:COG4717    149 EELEERLEELRELEEELEELEAELAELQEELEELLEqlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  191 YSADDTRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQFPLDLEkflAWLTEAETTANVLQDATRKERLLEDSKG 270
Cdd:COG4717    229 LEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG---VLFLVLGLLALLFLLLAREKASLGKEAE 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  271 VKELMKQWQDLQG-EIEAHTDVYHNLDENSQKILRslegsdDAVLLQRRLDNMNFKWSELRKKSlnirshleassdQWKR 349
Cdd:COG4717    306 ELQALPALEELEEeELEELLAALGLPPDLSPEELL------ELLDRIEELQELLREAEELEEEL------------QLEE 367
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  350 LHLSLQELLVWLQLKDDElsrqapiggDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGL-EKLYQEP 428
Cdd:COG4717    368 LEQEIAALLAEAGVEDEE---------ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELeEELEELE 438
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  429 RELppEERAQNVTRLLRKQAEevnTEWEKLNLHSadwqrkiDETLERLR-ELQEATDELDLKLRQAEVIKgswqpvgdLL 507
Cdd:COG4717    439 EEL--EELEEELEELREELAE---LEAELEQLEE-------DGELAELLqELEELKAELRELAEEWAALK--------LA 498
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1677537836  508 IDSLQDHLEKVKalrgeiaplKENVSHVNDLARQL 542
Cdd:COG4717    499 LELLEEAREEYR---------EERLPPVLERASEY 524
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
218-599 1.18e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  218 SEREAALEEthrlLQQFPLDLEKFLAWLTEaettanVLQDATRKERLLEDSKGVKELMKQWQDLQGEIEAHTdvYHNLDE 297
Cdd:TIGR02169  170 RKKEKALEE----LEEVEENIERLDLIIDE------KRQQLERLRREREKAERYQALLKEKREYEGYELLKE--KEALER 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  298 NSQKILRSLEGsddavlLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQellvwLQLKDDELSRQAPIGGD 377
Cdd:TIGR02169  238 QKEAIERQLAS------LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-----LRVKEKIGELEAEIASL 306
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  378 FPAVQ-KQNDVHRAFKRELKTKEPV--IMSTLETVRIFLTEQPLEgLEKLYQEPRELppeeraQNVTRLLRKQAEEVNTE 454
Cdd:TIGR02169  307 ERSIAeKERELEDAEERLAKLEAEIdkLLAEIEELEREIEEERKR-RDKLTEEYAEL------KEELEDLRAELEEVDKE 379
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  455 WEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQAEV--------IKGSWQPVGDlLIDSLQDHLEKVKALRGEIA 526
Cdd:TIGR02169  380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEeladlnaaIAGIEAKINE-LEEEKEDKALEIKKQEWKLE 458
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677537836  527 PLKENVSHVNDLARQLTtlgiqlspynlSTLEDLNTRWKLLQ---VAVEDRVRQLHEAHRDFGPASQhFLSTSVQG 599
Cdd:TIGR02169  459 QLAADLSKYEQELYDLK-----------EEYDRVEKELSKLQrelAEAEAQARASEERVRGGRAVEE-VLKASIQG 522
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
42-252 1.58e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   42 DLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARtiITDRIERIQNQWDEVQEHLQNRRQQLNEMLKd 121
Cdd:COG4942     35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA--LEAELAELEKEIAELRAELEAQKEELAELLR- 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  122 sTQWLEAKEEAEQVLGQARAKLESWKEGPY---TVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDYSADDTRK 198
Cdd:COG4942    112 -ALYRLGRQPPLALLLSPEDFLDAVRRLQYlkyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1677537836  199 VHMITENinaswRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAWLTEAETTA 252
Cdd:COG4942    191 EALKAER-----QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
44-194 3.68e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 3.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   44 EDINEMIIKQKATMQDLEQRRPQLEELITaaqNLKNKTSNQEART-IITDRIERIQNQWDEVQEHLQNRRQQLNEM---- 118
Cdd:TIGR04523  429 ERLKETIIKNNSEIKDLTNQDSVKELIIK---NLDNTRESLETQLkVLSRSINKIKQNLEQKQKELKSKEKELKKLneek 505
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  119 ----------------LKDSTQWLEA-KEEAEQVLGQARAKLESWKEGpYTVDAIQKKITETKQLAKDLRQWQTNVDVAN 181
Cdd:TIGR04523  506 keleekvkdltkkissLKEKIEKLESeKKEKESKISDLEDELNKDDFE-LKKENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
                          170
                   ....*....|...
gi 1677537836  182 DLALKLLRDYSAD 194
Cdd:TIGR04523  585 EEKQELIDQKEKE 597
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
853-885 5.25e-03

Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of the RSC complex, which is closely related to the SWI/SNF complex and is involved in remodeling chromatin structure. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239076  Cd Length: 45  Bit Score: 35.76  E-value: 5.25e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1677537836  853 CNIC-KECpiIGFRYRSLKHFNYDICQSCFFSGR 885
Cdd:cd02336      3 CFTCgNDC--TRVRYHNLKAKKYDLCPSCYQEGR 34
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
20-545 5.73e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 5.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   20 TELTDWLSLLDQVIKSQRvmvGDLEDINEMIIKQKATMQDL-------EQRRPQLEELITAAQNLKNKTSNQEA-RTIIT 91
Cdd:PRK02224   202 KDLHERLNGLESELAELD---EEIERYEEQREQARETRDEAdevleehEERREELETLEAEIEDLRETIAETEReREELA 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   92 DRIERIQNQWDEVQEHLQNRRQQLN------EMLKDSTQWLEA-KEEAEQVLGQARAKLESWKEgpyTVDAIQKKITETK 164
Cdd:PRK02224   279 EEVRDLRERLEELEEERDDLLAEAGlddadaEAVEARREELEDrDEELRDRLEECRVAAQAHNE---EAESLREDADDLE 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  165 QLAKDLRqwqtnvDVANDLALKLLRDYSADDTRKVHMitENINASWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAW 244
Cdd:PRK02224   356 ERAEELR------EEAAELESELEEAREAVEDRREEI--EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  245 LTEAETTANVLQDATRK-ERLL------------EDSKGVKELmkqwQDLQGEIEAHTDVYHNLDENSQKILRSLEGSDD 311
Cdd:PRK02224   428 EAELEATLRTARERVEEaEALLeagkcpecgqpvEGSPHVETI----EEDRERVEELEAELEDLEEEVEEVEERLERAED 503
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  312 AVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELLVWLQLKDDELSRQAPiggdfpAVQKQNDVHRAF 391
Cdd:PRK02224   504 LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE------EAEEAREEVAEL 577
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  392 KRELKTKEPVIMStLETVRIFLT-----EQPLEGLEKLYQEPRELPPEERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQ 466
Cdd:PRK02224   578 NSKLAELKERIES-LERIRTLLAaiadaEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKE 656
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  467 RK---IDETLERLRELQEATDELdlklrQAEvikgswqpvgdllIDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLT 543
Cdd:PRK02224   657 RAeeyLEQVEEKLDELREERDDL-----QAE-------------IGAVENELEELEELRERREALENRVEALEALYDEAE 718

                   ..
gi 1677537836  544 TL 545
Cdd:PRK02224   719 EL 720
GvpP COG4980
Gas vesicle protein YhaH [General function prediction only];
82-172 5.97e-03

Gas vesicle protein YhaH [General function prediction only];


Pssm-ID: 444004 [Multi-domain]  Cd Length: 106  Bit Score: 37.64  E-value: 5.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   82 SNQEARTIITDRIERIqnqWDEVQEHLQNRRQQLNEMLKdstqwlEAKEEAEQVLGQARAKLESWKEgpytvdAIQKKIT 161
Cdd:COG4980     28 SGKETRKKLKDKADDL---KDKAEDLKDELKEKASELSE------EAKEKLDELIEEIKEKIEELKE------EVEPKIE 92
                           90
                   ....*....|.
gi 1677537836  162 ETKQLAKDLRQ 172
Cdd:COG4980     93 ELKEEAEKLQK 103
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
435-584 6.12e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 6.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  435 ERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDlkLRQAEVIKGswqpvgdlLIDSLQDH 514
Cdd:COG4913    284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG--GDRLEQLER--------EIERLERE 353
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  515 LEKVKALRGEiaplkenvshvndLARQLTTLGIQLsPYNLSTLEDLNTRWKLLQVAVEDRVRQLHEAHRD 584
Cdd:COG4913    354 LEERERRRAR-------------LEALLAALGLPL-PASAEEFAALRAEAAALLEALEEELEALEEALAE 409
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
40-289 6.54e-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: 40.82  E-value: 6.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   40 VGDLEDINEMIIKQKAT-MQDLEQRRPQLE-------ELITAAQN--LKNKTSNQEARTIITDRIERIQNQWDEVQEHLQ 109
Cdd:TIGR02169  182 VEENIERLDLIIDEKRQqLERLRREREKAEryqallkEKREYEGYelLKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  110 NRRQQLNEM---LKDSTQWLEAKEEAEQVlgQARAKLESWK-EGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLAL 185
Cdd:TIGR02169  262 ELEKRLEEIeqlLEELNKKIKDLGEEEQL--RVKEKIGELEaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  186 KLLRDYSADDTRKVHMITENIN--ASWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAWLTEAETTANVLQDATRK-- 261
Cdd:TIGR02169  340 ELEREIEEERKRRDKLTEEYAElkEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRls 419
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1677537836  262 ---ERLLEDSKGVKELMKQWQ----DLQGEIEAHT 289
Cdd:TIGR02169  420 eelADLNAAIAGIEAKINELEeekeDKALEIKKQE 454
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
29-302 7.12e-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: 40.81  E-value: 7.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   29 LDQVIKSQRVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARtiITDRIERIQNQwdevQEHL 108
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR--LEQQKQILRER----LANL 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  109 QNRRQQLNEMLkdsTQWLEAKEEAEQVLGQARAKLESWKEgpyTVDAIQKKITETKQLAKDL----RQWQTNVD-VANDL 183
Cdd:TIGR02168  315 ERQLEELEAQL---EELESKLDELAEELAELEEKLEELKE---ELESLEAELEELEAELEELesrlEELEEQLEtLRSKV 388
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  184 ALKLLRDYSADDTRKVHMIT-ENINASWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAWLTEAETTANVLQDATRKE 262
Cdd:TIGR02168  389 AQLELQIASLNNEIERLEARlERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1677537836  263 RLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKI 302
Cdd:TIGR02168  469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
11-145 8.02e-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: 40.43  E-value: 8.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   11 ALADFNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQkatMQDLEQRRPQLEELITAAQnlKNKTSNQEARTII 90
Cdd:TIGR02168  797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR---LEDLEEQIEELSEDIESLA--AEIEELEELIEEL 871
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1677537836   91 TDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLES 145
Cdd:TIGR02168  872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
93-358 8.18e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 8.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836   93 RIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEgpyTVDAIQKKITE-TKQLAKDLR 171
Cdd:COG1196    226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL---ELEEAQAEEYElLAELARLEQ 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  172 QWQTNVDVANDLALKLLRDYSADDTRKVHMIT-----ENINASWRSIHKRVSEREAALEETHRLLQQfplDLEKFLAWLT 246
Cdd:COG1196    303 DIARLEERRRELEERLEELEEELAELEEELEEleeelEELEEELEEAEEELEEAEAELAEAEEALLE---AEAELAEAEE 379
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  247 EAETTANVLQDATRkeRLLEDSKGVKELMKQWQDLQGEIEAHTDvyhNLDENSQKILRSLEGSDDAVLLQRRLDNMNFKW 326
Cdd:COG1196    380 ELEELAEELLEALR--AAAELAAQLEELEEAEEALLERLERLEE---ELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1677537836  327 SELRKKSLNIRSHLEASSDQWKRLHLSLQELL 358
Cdd:COG1196    455 EEEEEALLELLAELLEEAALLEAALAELLEEL 486
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
211-586 8.35e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 8.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  211 RSIHKRVSEREAALEETHRLLQQFPLDLEKFLAWLTEAETTANVLQDATRKERLLEDSKGVKELMKQWQDLQGEI-EAHT 289
Cdd:COG4717     98 EELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELaELQE 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  290 DVYHNLDENSQKILRSLEGsddavlLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLhlslqELLVWLQLKDDELS 369
Cdd:COG4717    178 ELEELLEQLSLATEEELQD------LAEELEELQQRLAELEEELEEAQEELEELEEELEQL-----ENELEAAALEERLK 246
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  370 RQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKLYQEPRELPPEERAQNVTRLLRKQAE 449
Cdd:COG4717    247 EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLA 326
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  450 EVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQAEvIKGSWQPVGDLLIDSLQDHLEKVKALRgeiaplk 529
Cdd:COG4717    327 ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE-IAALLAEAGVEDEEELRAALEQAEEYQ------- 398
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1677537836  530 ENVSHVNDLARQLTTL-GIQLSPYNLSTLEDLNTRWKLLQVAVEDRVRQLHEAHRDFG 586
Cdd:COG4717    399 ELKEELEELEEQLEELlGELEELLEALDEEELEEELEELEEELEELEEELEELREELA 456
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
243-562 9.38e-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: 40.21  E-value: 9.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  243 AWLTEAETTANVLQDATRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDE---NSQKILRSLEGSDDAVLLQRRl 319
Cdd:pfam12128  225 HWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEerqETSAELNQLLRTLDDQWKEKR- 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  320 DNMNFKWSELRKKSLNIRSHLEASSDQWKR--------LHLSLQELLVW-LQLKDDELSRQAPIGgdfpavqKQNDVHRA 390
Cdd:pfam12128  304 DELNGELSAADAAVAKDRSELEALEDQHGAfldadietAAADQEQLPSWqSELENLEERLKALTG-------KHQDVTAK 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  391 FKR-------ELKTKEPVIMSTLETVRIFLTEQPLEGLEKLYQEPRELPPEERAQNvtRLLRKQAEEV--NTEWEKLNLH 461
Cdd:pfam12128  377 YNRrrskikeQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGK--LEFNEEEYRLksRLGELKLRLN 454
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677537836  462 SADWQrkiDETLERLRELQEATDELDLKLRQAEviKGswqpvgdllIDSLQDHLEKVKALRGEiAPLKENVSH--VNDLA 539
Cdd:pfam12128  455 QATAT---PELLLQLENFDERIERAREEQEAAN--AE---------VERLQSELRQARKRRDQ-ASEALRQASrrLEERQ 519
                          330       340
                   ....*....|....*....|...
gi 1677537836  540 RQLTTLGIQLSPYNLSTLEDLNT 562
Cdd:pfam12128  520 SALDELELQLFPQAGTLLHFLRK 542
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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