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Conserved domains on  [gi|578837832|ref|XP_006724532|]
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dystrophin isoform X2 [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 ...
3117-3278 2.15e-113

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: 357.03  E-value: 2.15e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3117 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 3196
Cdd:cd16246     1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3197 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3276
Cdd:cd16246    81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                  ..
gi 578837832 3277 MR 3278
Cdd:cd16246   161 MR 162
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
128-238 6.91e-69

second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.


:

Pssm-ID: 409082  Cd Length: 111  Bit Score: 227.50  E-value: 6.91e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  128 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDP 207
Cdd:cd21233     1 SEKILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSATERLDHAFNIARQHLGIEKLLDP 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832  208 EDVDTTYPDKKSILMYITSLFQVLPQQVSIE 238
Cdd:cd21233    81 EDVATAHPDKKSILMYVTSLFQVLPQQVSIE 111
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
3-113 1.31e-66

first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.


:

Pssm-ID: 409080  Cd Length: 111  Bit Score: 220.95  E-value: 1.31e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    3 DEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 82
Cdd:cd21231     1 YEREDVQKKTFTKWINAQFAKFGKPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832   83 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21231    81 LVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
3303-3351 6.48e-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: 6.48e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578837832 3303 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 3351
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
333-550 8.27e-27

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: 111.00  E-value: 8.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  333 LDRYQTALEEVLSWLLSAEDTLQAQgEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEV 412
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI---EEGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  413 QEQMNLLNSRWECLRVASMEKQSNLHRVLMDLQ-NQKLKELNDWLTKTEERtrkMEEEPLGPDLEDLKRQVQQHKVLQED 491
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQfFRDADDLEQWLEEKEAA---LASEDLGKDLESVEELLKKHKELEEE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837832  492 LEQEQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDIL 550
Cdd:cd00176   155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2097-2312 1.96e-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: 101.37  E-value: 1.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2097 KWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAK-YKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtDASILQE 2175
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEaLLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2176 KLGSLNLRWQEVCKQLSDRKKRLEEQKNiLSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLR 2255
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837832 2256 QGILKQLNETGGPVLVSAPisPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQI 2312
Cdd:cd00176   159 EPRLKSLNELAEELLEEGH--PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2682-2925 1.24e-20

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: 93.28  E-value: 1.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2682 LLQQFPLDLEKFLAWLTEAETTANVLQDAtrkerllEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGS 2761
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-------DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGH 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2762 DDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELLVWLQLKDDELSRQaPIGGDFPAVQKQNDVHR 2841
Cdd:cd00176    72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2842 AFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKI 2921
Cdd:cd00176   150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------------IEEKLEELNERWEELLELAEERQKKL 209

                  ....
gi 578837832 2922 DETL 2925
Cdd:cd00176   210 EEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2464-2680 2.49e-20

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: 92.12  E-value: 2.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2464 LADFNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIIT 2543
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2544 DRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAkEEAEQVLGQARAKLESwKEGPYTVDAIQKKITETKQLAKDLR 2623
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837832 2624 QWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETH 2680
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1041-1255 3.54e-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: 80.18  E-value: 3.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1041 KLRKIQNHIQTLKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEfASRLE 1120
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1121 TELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQkDLSEMHEWMTQAEEEyLERDFEYKTPDELQKAVEEMKRAKEEAQ 1200
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAA-LASEDLGKDLESVEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578837832 1201 QKEAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNGKCKTLEE 1255
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
235kDa-fam super family cl31124
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
755-1930 9.24e-15

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


The actual alignment was detected with superfamily member TIGR01612:

Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 82.02  E-value: 9.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   755 VNAIEREKAEKFRKLQDASRSAQALVE-QMVNEGVNA-------DSIKQASEQLNSRWIEFCQLLSErLNWLeYQNNIIA 826
Cdd:TIGR01612  598 INKLKLELKEKIKNISDKNEYIKKAIDlKKIIENNNAyidelakISPYQVPEHLKNKDKIYSTIKSE-LSKI-YEDDIDA 675
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   827 FYNQLQ---------------QLEQMTTTAEN-WLKIQPTtpsEPTAIKSQLKICKDEVNRLSDLQPQIERL-------- 882
Cdd:TIGR01612  676 LYNELSsivkenaidntedkaKLDDLKSKIDKeYDKIQNM---ETATVELHLSNIENKKNELLDIIVEIKKHihgeinkd 752
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   883 ---KIQSIALKEKGQGPMFLD-ADFVAFTNHFKQVFSDVQAR---EKELQTIFDTLPPMRYQETMSAIRTW-VQQSETKL 954
Cdd:TIGR01612  753 lnkILEDFKNKEKELSNKINDyAKEKDELNKYKSKISEIKNHyndQINIDNIKDEDAKQNYDKSKEYIKTIsIKEDEIFK 832
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   955 SIPQLSVTDYEIMeQRLGELQALQSSLQEQQSGLYylsTTVKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQK 1034
Cdd:TIGR01612  833 IINEMKFMKDDFL-NKVDKFINFENNCKEKIDSEH---EQFAELTNKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEE 908
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1035 LEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEwpalgdsEILKKQLKQcrllvsDIQTIQPSlnsvneggqkikNEAEPE 1114
Cdd:TIGR01612  909 EYQNINTLKKVDEYIKICENTKESIEKFHNKQ-------NILKEILNK------NIDTIKES------------NLIEKS 963
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1115 FASRLETELKELNTQWDHMCQQVyarkeALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFeyktpDELQKAVEEMKR 1194
Cdd:TIGR01612  964 YKDKFDNTLIDKINELDKAFKDA-----SLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQF-----DEKEKATNDIEQ 1033
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1195 AKEEAQQKEAKVKL--------LTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNgkcktleevwacWHELLSY 1266
Cdd:TIGR01612 1034 KIEDANKNIPNIEIaihtsiynIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLK------------HYNFDDF 1101
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1267 LEKAN-KWLNEVEfklKTTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDggVMDELINEEletfnsrwre 1345
Cdd:TIGR01612 1102 GKEENiKYADEIN---KIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLED--VADKAISND---------- 1166
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1346 lheeavrrqklleqsiqSAQETEKSlhlIQESLTFIDKQlaAYIADKVDaaQMPQEAQKIQSDLTSheisLEEMKKHNQ- 1424
Cdd:TIGR01612 1167 -----------------DPEEIEKK---IENIVTKIDKK--KNIYDEIK--KLLNEIAEIEKDKTS----LEEVKGINLs 1218
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1425 -GKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPanfeqrlqeskmiLDEVKMHLPALETKSVEQEVVQSQLNhcvNLYKS 1503
Cdd:TIGR01612 1219 yGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIED-------------LDEIKEKSPEIENEMGIEMDIKAEME---TFNIS 1282
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1504 LSEVKSevemviktgRQIVQKKQTENPKELDERvtALKL-HYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAat 1582
Cdd:TIGR01612 1283 HDDDKD---------HHIISKKHDENISDIREK--SLKIiEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIA-- 1349
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1583 dmeltkrsavegmpsNLDSEVAWGKaTQKEIEKQKVHLKSITEVGEALKTVLGKKETLVedKLSLLNSNWIAVTSRAEEW 1662
Cdd:TIGR01612 1350 ---------------NIYNILKLNK-IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLI--KKIKDDINLEECKSKIEST 1411
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1663 LNllleyQKHMETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKaelndirpKVDSTRDQAANLMANRGDHCR 1742
Cdd:TIGR01612 1412 LD-----DKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFK--------NIEMADNKSQHILKIKKDNAT 1478
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1743 KLVEPQISELNHRFAAiSHRIKT-----GKASIPLKEL-EQFNSDIQKLLEPL-EAEIQQGVNLKEEDFNKDMNEDNEGT 1815
Cdd:TIGR01612 1479 NDHDFNINELKEHIDK-SKGCKDeadknAKAIEKNKELfEQYKKDVTELLNKYsALAIKNKFAKTKKDSEIIIKEIKDAH 1557
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1816 VKELLQRGDNLQQriTDERKREEIKIKQQLLQT-KHN-ALKDLRSQRR---KKALEISHqwyqYKRQADDLLKCLDDIEK 1890
Cdd:TIGR01612 1558 KKFILEAEKSEQK--IKEIKKEKFRIEDDAAKNdKSNkAAIDIQLSLEnfeNKFLKISD----IKKKINDCLKETESIEK 1631
                         1210      1220      1230      1240
                   ....*....|....*....|....*....|....*....|
gi 578837832  1891 KLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSE 1930
Cdd:TIGR01612 1632 KISSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIED 1671
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2926-3032 1.41e-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: 63.49  E-value: 1.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2926 ERLRELQEATDELDLKLRQAEVIKgSWQPVGDLLiDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYN 3005
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 578837832  3006 LSTLEDLNTRWKLLQVAVEDRVRQLHE 3032
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
3051-3080 7.94e-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: 53.30  E-value: 7.94e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 578837832 3051 GPWERAISPNKVPYYINHETQTTCWDHPKM 3080
Cdd:cd00201     2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2313-2571 4.28e-07

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 53.60  E-value: 4.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2313 KDLGQLEKKLEDLEEQLNHLLL--WLSPIRNQLEiynqpnqegpfDVKETEIAVQAKQPDVEEILSKGQHLYKEKP-ATQ 2389
Cdd:cd00176     7 RDADELEAWLSEKEELLSSTDYgdDLESVEALLK-----------KHEALEAELAAHEERVEALNELGEQLIEEGHpDAE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2390 PVKRKLEDLSSEWKAVNRLLQELRAKqpdlapglttigasptqtvtlvtqpvvtketaisklempsslMLEVPALADFNR 2469
Cdd:cd00176    76 EIQERLEELNQRWEELRELAEERRQR------------------------------------------LEEALDLQQFFR 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2470 AWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKtSNQEARTIITDRIERI 2549
Cdd:cd00176   114 DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEE-GHPDADEEIEEKLEEL 191
                         250       260
                  ....*....|....*....|..
gi 578837832 2550 QNQWDEVQEHLQNRRQQLNEML 2571
Cdd:cd00176   192 NERWEELLELAEERQKKLEEAL 213
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1870-2094 2.22e-05

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 48.60  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1870 QWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQI 1942
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1943 Q--LSKRWREIESKFAQFRRLnfaqihtvreetmmvmtedmpLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCaKDF 2020
Cdd:cd00176    81 LeeLNQRWEELRELAEERRQR---------------------LEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDL 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578837832 2021 EDLFKQEESLKNIKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFDRS 2094
Cdd:cd00176   139 ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
552-819 4.39e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 41.66  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  552 KWQRLTEEQCLFSAWLSEKEDAVNKIHTTgfKDQNEMLSSLQKLAVLKADLEKKKQSMGKLYSLKQDLLSTLKNKSvtQK 631
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA--EE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  632 TEAWLDNFARCWDNLVQKLEKSTAQISQAVTTTQPSLtqttvmetvttvttreqilvkhaqeelpppppqkkrqitvdse 711
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR------------------------------------------- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  712 irkrldvDITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEgvNAD 791
Cdd:cd00176   114 -------DADDLEQWLEEKEAALASEDLG--KDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPD--ADE 182
                         250       260
                  ....*....|....*....|....*...
gi 578837832  792 SIKQASEQLNSRWIEFCQLLSERLNWLE 819
Cdd:cd00176   183 EIEEKLEELNERWEELLELAEERQKKLE 210
 
Name Accession Description Interval E-value
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
3117-3278 2.15e-113

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: 357.03  E-value: 2.15e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3117 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 3196
Cdd:cd16246     1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3197 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3276
Cdd:cd16246    81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                  ..
gi 578837832 3277 MR 3278
Cdd:cd16246   161 MR 162
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
128-238 6.91e-69

second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.


Pssm-ID: 409082  Cd Length: 111  Bit Score: 227.50  E-value: 6.91e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  128 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDP 207
Cdd:cd21233     1 SEKILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSATERLDHAFNIARQHLGIEKLLDP 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832  208 EDVDTTYPDKKSILMYITSLFQVLPQQVSIE 238
Cdd:cd21233    81 EDVATAHPDKKSILMYVTSLFQVLPQQVSIE 111
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
3-113 1.31e-66

first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.


Pssm-ID: 409080  Cd Length: 111  Bit Score: 220.95  E-value: 1.31e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    3 DEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 82
Cdd:cd21231     1 YEREDVQKKTFTKWINAQFAKFGKPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832   83 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21231    81 LVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
3081-3199 1.20e-56

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: 193.14  E-value: 1.20e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  3081 TELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLK--QNDQPMDILQIINCLTTIYDRLEQEHN 3158
Cdd:pfam09068    1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 578837832  3159 N--LVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLC 3199
Cdd:pfam09068   81 TthQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
2-224 3.63e-34

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 142.00  E-value: 3.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    2 EDEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPK--EKGSTRVHALNNVNKALRVLQNN 79
Cdd:COG5069     3 AKKWQKVQKKTFTKWTNEKLISGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   80 NVDLVNIGSTDIVDGNHKLTLGLIWNIILhwqvKNVMKNIMAGLQQTNSEKILLsWVRQSTRNY-PQVNVINFTTSWSDG 158
Cdd:COG5069    83 GVKLFNIGPQDIVDGNPKLILGLIWSLIS----RLTIATINEEGELTKHINLLL-WCDEDTGGYkPEVDTFDFFRSWRDG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578837832  159 LALNALIHSHRPDLFDWNSVVCQQSATQ-RLEHAFNIARYQLGIEKLLDPEDV-DTTYPDKKSILMYI 224
Cdd:COG5069   158 LAFSALIHDSRPDTLDPNVLDLQKKNKAlNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYV 225
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
3303-3351 6.48e-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: 6.48e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578837832 3303 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 3351
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
333-550 8.27e-27

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: 111.00  E-value: 8.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  333 LDRYQTALEEVLSWLLSAEDTLQAQgEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEV 412
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI---EEGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  413 QEQMNLLNSRWECLRVASMEKQSNLHRVLMDLQ-NQKLKELNDWLTKTEERtrkMEEEPLGPDLEDLKRQVQQHKVLQED 491
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQfFRDADDLEQWLEEKEAA---LASEDLGKDLESVEELLKKHKELEEE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837832  492 LEQEQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDIL 550
Cdd:cd00176   155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2097-2312 1.96e-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: 101.37  E-value: 1.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2097 KWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAK-YKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtDASILQE 2175
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEaLLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2176 KLGSLNLRWQEVCKQLSDRKKRLEEQKNiLSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLR 2255
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837832 2256 QGILKQLNETGGPVLVSAPisPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQI 2312
Cdd:cd00176   159 EPRLKSLNELAEELLEEGH--PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
11-109 3.22e-21

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 90.84  E-value: 3.22e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832     11 KTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEK---GSTRVHALNNVNKALRVLQNNNVDLVNIG 87
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 578837832     88 STDIVDGNhKLTLGLIWNIILH 109
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
130-227 3.80e-21

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 90.84  E-value: 3.80e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    130 KILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQ---QSATQRLEHAFNIARYQLGIEKLLD 206
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 578837832    207 PEDVDTTYPDKKSILMYITSL 227
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2682-2925 1.24e-20

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: 93.28  E-value: 1.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2682 LLQQFPLDLEKFLAWLTEAETTANVLQDAtrkerllEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGS 2761
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-------DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGH 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2762 DDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELLVWLQLKDDELSRQaPIGGDFPAVQKQNDVHR 2841
Cdd:cd00176    72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2842 AFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKI 2921
Cdd:cd00176   150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------------IEEKLEELNERWEELLELAEERQKKL 209

                  ....
gi 578837832 2922 DETL 2925
Cdd:cd00176   210 EEAL 213
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
128-232 2.42e-20

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 88.88  E-value: 2.42e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   128 SEKILLSWVRQSTRNY-PQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQS-ATQRLEHAFNIARYQLGIEK-L 204
Cdd:pfam00307    3 LEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFdKLENINLALDVAEKKLGVPKvL 82
                           90       100
                   ....*....|....*....|....*...
gi 578837832   205 LDPEDVDTtyPDKKSILMYITSLFQVLP 232
Cdd:pfam00307   83 IEPEDLVE--GDNKSVLTYLASLFRRFQ 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2464-2680 2.49e-20

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: 92.12  E-value: 2.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2464 LADFNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIIT 2543
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2544 DRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAkEEAEQVLGQARAKLESwKEGPYTVDAIQKKITETKQLAKDLR 2623
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837832 2624 QWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETH 2680
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
7-111 4.42e-20

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 88.11  E-value: 4.42e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832     7 DVQKKTFTKWVNAQFSK-FGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEK-GSTRVHALNNVNKALRVLQNN-NVDL 83
Cdd:pfam00307    1 LELEKELLRWINSHLAEyGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKlGVPK 80
                           90       100
                   ....*....|....*....|....*...
gi 578837832    84 VNIGSTDIVDGNHKLTLGLIWNIILHWQ 111
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
3299-3344 9.74e-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: 9.74e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 578837832  3299 AKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSgRVAKGHKM 3344
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQM 45
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1041-1255 3.54e-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: 80.18  E-value: 3.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1041 KLRKIQNHIQTLKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEfASRLE 1120
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1121 TELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQkDLSEMHEWMTQAEEEyLERDFEYKTPDELQKAVEEMKRAKEEAQ 1200
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAA-LASEDLGKDLESVEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578837832 1201 QKEAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNGKCKTLEE 1255
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
755-1930 9.24e-15

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 82.02  E-value: 9.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   755 VNAIEREKAEKFRKLQDASRSAQALVE-QMVNEGVNA-------DSIKQASEQLNSRWIEFCQLLSErLNWLeYQNNIIA 826
Cdd:TIGR01612  598 INKLKLELKEKIKNISDKNEYIKKAIDlKKIIENNNAyidelakISPYQVPEHLKNKDKIYSTIKSE-LSKI-YEDDIDA 675
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   827 FYNQLQ---------------QLEQMTTTAEN-WLKIQPTtpsEPTAIKSQLKICKDEVNRLSDLQPQIERL-------- 882
Cdd:TIGR01612  676 LYNELSsivkenaidntedkaKLDDLKSKIDKeYDKIQNM---ETATVELHLSNIENKKNELLDIIVEIKKHihgeinkd 752
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   883 ---KIQSIALKEKGQGPMFLD-ADFVAFTNHFKQVFSDVQAR---EKELQTIFDTLPPMRYQETMSAIRTW-VQQSETKL 954
Cdd:TIGR01612  753 lnkILEDFKNKEKELSNKINDyAKEKDELNKYKSKISEIKNHyndQINIDNIKDEDAKQNYDKSKEYIKTIsIKEDEIFK 832
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   955 SIPQLSVTDYEIMeQRLGELQALQSSLQEQQSGLYylsTTVKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQK 1034
Cdd:TIGR01612  833 IINEMKFMKDDFL-NKVDKFINFENNCKEKIDSEH---EQFAELTNKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEE 908
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1035 LEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEwpalgdsEILKKQLKQcrllvsDIQTIQPSlnsvneggqkikNEAEPE 1114
Cdd:TIGR01612  909 EYQNINTLKKVDEYIKICENTKESIEKFHNKQ-------NILKEILNK------NIDTIKES------------NLIEKS 963
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1115 FASRLETELKELNTQWDHMCQQVyarkeALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFeyktpDELQKAVEEMKR 1194
Cdd:TIGR01612  964 YKDKFDNTLIDKINELDKAFKDA-----SLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQF-----DEKEKATNDIEQ 1033
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1195 AKEEAQQKEAKVKL--------LTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNgkcktleevwacWHELLSY 1266
Cdd:TIGR01612 1034 KIEDANKNIPNIEIaihtsiynIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLK------------HYNFDDF 1101
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1267 LEKAN-KWLNEVEfklKTTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDggVMDELINEEletfnsrwre 1345
Cdd:TIGR01612 1102 GKEENiKYADEIN---KIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLED--VADKAISND---------- 1166
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1346 lheeavrrqklleqsiqSAQETEKSlhlIQESLTFIDKQlaAYIADKVDaaQMPQEAQKIQSDLTSheisLEEMKKHNQ- 1424
Cdd:TIGR01612 1167 -----------------DPEEIEKK---IENIVTKIDKK--KNIYDEIK--KLLNEIAEIEKDKTS----LEEVKGINLs 1218
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1425 -GKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPanfeqrlqeskmiLDEVKMHLPALETKSVEQEVVQSQLNhcvNLYKS 1503
Cdd:TIGR01612 1219 yGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIED-------------LDEIKEKSPEIENEMGIEMDIKAEME---TFNIS 1282
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1504 LSEVKSevemviktgRQIVQKKQTENPKELDERvtALKL-HYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAat 1582
Cdd:TIGR01612 1283 HDDDKD---------HHIISKKHDENISDIREK--SLKIiEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIA-- 1349
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1583 dmeltkrsavegmpsNLDSEVAWGKaTQKEIEKQKVHLKSITEVGEALKTVLGKKETLVedKLSLLNSNWIAVTSRAEEW 1662
Cdd:TIGR01612 1350 ---------------NIYNILKLNK-IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLI--KKIKDDINLEECKSKIEST 1411
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1663 LNllleyQKHMETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKaelndirpKVDSTRDQAANLMANRGDHCR 1742
Cdd:TIGR01612 1412 LD-----DKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFK--------NIEMADNKSQHILKIKKDNAT 1478
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1743 KLVEPQISELNHRFAAiSHRIKT-----GKASIPLKEL-EQFNSDIQKLLEPL-EAEIQQGVNLKEEDFNKDMNEDNEGT 1815
Cdd:TIGR01612 1479 NDHDFNINELKEHIDK-SKGCKDeadknAKAIEKNKELfEQYKKDVTELLNKYsALAIKNKFAKTKKDSEIIIKEIKDAH 1557
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1816 VKELLQRGDNLQQriTDERKREEIKIKQQLLQT-KHN-ALKDLRSQRR---KKALEISHqwyqYKRQADDLLKCLDDIEK 1890
Cdd:TIGR01612 1558 KKFILEAEKSEQK--IKEIKKEKFRIEDDAAKNdKSNkAAIDIQLSLEnfeNKFLKISD----IKKKINDCLKETESIEK 1631
                         1210      1220      1230      1240
                   ....*....|....*....|....*....|....*....|
gi 578837832  1891 KLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSE 1930
Cdd:TIGR01612 1632 KISSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIED 1671
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
3300-3343 2.36e-14

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: 2.36e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 578837832   3300 KHQAKCNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHK 3343
Cdd:smart00291    2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2115-2810 4.15e-14

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: 79.33  E-value: 4.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2115 AEQFLRKTQIPENWEHAKYKWYLKELQDGIGQRQtvvRTLNATGEEIiqQSSKTDASILQEKLGSLNLRWQEVCKQLSDR 2194
Cdd:TIGR02168  212 AERYKELKAELRELELALLVLRLEELREELEELQ---EELKEAEEEL--EELTAELQELEEKLEELRLEVSELEEEIEEL 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2195 KKRLEEQKNILSEFQRDLNEFVLWLEEADNI-----ASIPLEPGKEQQLKEKLEQVKLLVEEL-PLRQGILKQLNEtggp 2268
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLERQleeleAQLEELESKLDELAEELAELEEKLEELkEELESLEAELEE---- 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2269 vlvsapiSPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ 2348
Cdd:TIGR02168  363 -------LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2349 PNQEGPFDVKETEIA-VQAKQPDVEEILSKGQHLYKEKP-ATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLApGLTTI 2426
Cdd:TIGR02168  436 KELQAELEELEEELEeLQEELERLEEALEELREELEEAEqALDAAERELAQLQARLDSLERLQENLEGFSEGVK-ALLKN 514
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2427 GASPTQTVTLVTQPVVTK---ETAISKLEMPSSLMLEVPALADFNRA-----WTELTDWLSLLDQVIKSQRVMVGDLEDI 2498
Cdd:TIGR02168  515 QSGLSGILGVLSELISVDegyEAAIEAALGGRLQAVVVENLNAAKKAiaflkQNELGRVTFLPLDSIKGTEIQGNDREIL 594
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2499 NEmIIKQKATMQDLEQRRPQLEELI-------------TAAQNLKNKTsNQEARTIITD--------------------- 2544
Cdd:TIGR02168  595 KN-IEGFLGVAKDLVKFDPKLRKALsyllggvlvvddlDNALELAKKL-RPGYRIVTLDgdlvrpggvitggsaktnssi 672
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2545 -----RIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLA 2619
Cdd:TIGR02168  673 lerrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2620 KDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENINA---SWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAW 2696
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERR 832
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2697 LTEAETTANVLQDatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDvyHNLDENSQKILRSLEGSDDAVLLQRRLDNMNF 2776
Cdd:TIGR02168  833 IAATERRLEDLEE--QIEELSEDIESLAAEIEELEELIEELESELE--ALLNERASLEEALALLRSELEELSEELRELES 908
                          730       740       750
                   ....*....|....*....|....*....|....
gi 578837832  2777 KWSELRKKSLNIRSHLEASSDQWKRLHLSLQELL 2810
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
719-925 1.22e-12

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 69.78  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  719 DITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQmvnEGVNADSIKQASE 798
Cdd:cd00176     8 DADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE---GHPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  799 QLNSRWIEFCQLLSERLNWLEYQNNIIAFYNQLQQLEQMTTTAENWLKIQPTTPSePTAIKSQLKICKDEVNRLSDLQPQ 878
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578837832  879 IERLKIQSIALKEKGQ--GPMFLDADFVAFTNHFKQVFSDVQAREKELQ 925
Cdd:cd00176   162 LKSLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELAEERQKKLE 210
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1040-1144 5.03e-12

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: 65.03  E-value: 5.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1040 NKLRKIQNHIQTLKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEaEPEFASRL 1119
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYG-KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEI 78
                           90       100
                   ....*....|....*....|....*
gi 578837832  1120 ETELKELNTQWDHMCQQVYARKEAL 1144
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKL 103
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2926-3032 1.41e-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: 63.49  E-value: 1.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2926 ERLRELQEATDELDLKLRQAEVIKgSWQPVGDLLiDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYN 3005
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 578837832  3006 LSTLEDLNTRWKLLQVAVEDRVRQLHE 3032
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
441-548 2.04e-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: 63.11  E-value: 2.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   441 LMDLQNQKLKELNDWLTKTEErtrKMEEEPLGPDLEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVdESSGDHATAA 520
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEA---LLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKL-IDEGHYASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 578837832   521 LEEQLKVLGDRWANICRWTEDRWVLLQD 548
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
2099-2199 4.15e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 62.35  E-value: 4.15e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   2099 RRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKW-YLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtDASILQEKL 2177
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLkKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 578837832   2178 GSLNLRWQEVCKQLSDRKKRLE 2199
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2927-3037 1.34e-10

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 64.00  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2927 RLRELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNL 3006
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832 3007 STLEDLNTRWKLLQVAVEDRVRQLHEAHRDF 3037
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQ 109
SPEC smart00150
Spectrin repeats;
335-437 2.49e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.04  E-value: 2.49e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    335 RYQTALEEVLSWLLSAEDTLQAQgEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEVQE 414
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI---EEGHPDAEEIEE 77
                            90       100
                    ....*....|....*....|...
gi 578837832    415 QMNLLNSRWECLRVASMEKQSNL 437
Cdd:smart00150   78 RLEELNERWEELKELAEERRQKL 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2096-2200 2.88e-10

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: 60.02  E-value: 2.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2096 EKWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEH--AKYKWYlKELQDGIGQRQTVVRTLNATGEEIIQqSSKTDASIL 2173
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESvqALLKKH-KALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 578837832  2174 QEKLGSLNLRWQEVCKQLSDRKKRLEE 2200
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
2467-2568 2.94e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.65  E-value: 2.94e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   2467 FNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIITDRI 2546
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 578837832   2547 ERIQNQWDEVQEHLQNRRQQLN 2568
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2562-2678 2.57e-09

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: 57.33  E-value: 2.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2562 NRRQQLNEMLKDSTQWLEakeEAEQVLgqarakleSWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLr 2641
Cdd:pfam00435    1 LLLQQFFRDADDLESWIE---EKEALL--------SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI- 68
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 578837832  2642 DYSADDTRKVHMITENINASWRSIHKRVSEREAALEE 2678
Cdd:pfam00435   69 DEGHYASEEIQERLEELNERWEQLLELAAERKQKLEE 105
PTZ00121 PTZ00121
MAEBL; Provisional
1349-1956 5.35e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.85  E-value: 5.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1349 EAVRRQKLLEQSIQSAQETEKsLHLIQESLTFIDKQLAAYI----ADKVDAAQMPQEAQKIQSDLTSHEI-SLEEMKKHN 1423
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEE-ERNNEEIRKFEEARMAHFArrqaAIKAEEARKADELKKAEEKKKADEAkKAEEKKKAD 1305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1424 QGKEAAQRVlSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKM-HLPALETKSVEQEVVQSQLNhcvnlyK 1502
Cdd:PTZ00121 1306 EAKKKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAdEAEAAEEKAEAAEKKKEEAK------K 1378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1503 SLSEVKSEVEMVIKTGRqiVQKKQTENPKELDE--RVTALKLHYNELGAKvTERKQQLEKCLKLSRKMRKEMNVLTEWLA 1580
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADE--AKKKAEEDKKKADElkKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1581 ATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEvgEALKTVLGKKETLVEDKlsllnsnwiAVTSRAE 1660
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD--EAKKAAEAKKKADEAKK---------AEEAKKA 1524
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1661 EWLNLLLEYQKHMETfdQNVDHITKwiiqADTLLDESEKKKPQQKEDVLKRLKAElnDIRPKVDSTRDQAANLMANRGDH 1740
Cdd:PTZ00121 1525 DEAKKAEEAKKADEA--KKAEEKKK----ADELKKAEELKKAEEKKKAEEAKKAE--EDKNMALRKAEEAKKAEEARIEE 1596
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1741 CRKLVEPQISELNHRF-AAISHRIKTGKasipLKELEQFNSDIQKLLEPLEAEIQQGVNL-KEEDFNKDMNEDNEGTVKE 1818
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAkKAEEAKIKAEE----LKKAEEEKKKVEQLKKKEAEEKKKAEELkKAEEENKIKAAEEAKKAEE 1672
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1819 LLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEP 1898
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837832 1899 RDER-KIKEIDRELQKKKEElnaVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFA 1956
Cdd:PTZ00121 1753 EEEKkKIAHLKKEEEKKAEE---IRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFA 1808
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
3051-3080 7.94e-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: 53.30  E-value: 7.94e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 578837832 3051 GPWERAISPNKVPYYINHETQTTCWDHPKM 3080
Cdd:cd00201     2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
SPEC smart00150
Spectrin repeats;
2684-2793 1.43e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 55.03  E-value: 1.43e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   2684 QQFPLDLEKFLAWLTEAETTAnvlqdatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGSDD 2763
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL-------ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPD 71
                            90       100       110
                    ....*....|....*....|....*....|
gi 578837832   2764 AVLLQRRLDNMNFKWSELRKKSLNIRSHLE 2793
Cdd:smart00150   72 AEEIEERLEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1869-1971 2.76e-08

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: 54.25  E-value: 2.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1869 HQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVE--PTQIQLSK 1946
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEghYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 578837832  1947 RWREIESKFAQFRRLNFAQIHTVRE 1971
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
3048-3080 2.99e-08

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: 51.83  E-value: 2.99e-08
                            10        20        30
                    ....*....|....*....|....*....|...
gi 578837832   3048 SVQGPWERAISPNKVPYYINHETQTTCWDHPKM 3080
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
SPEC smart00150
Spectrin repeats;
2929-3030 3.47e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.87  E-value: 3.47e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   2929 RELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNLST 3008
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEER 78
                            90       100
                    ....*....|....*....|..
gi 578837832   3009 LEDLNTRWKLLQVAVEDRVRQL 3030
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
3052-3078 9.44e-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: 9.44e-08
                           10        20
                   ....*....|....*....|....*..
gi 578837832  3052 PWERAISPNKVPYYINHETQTTCWDHP 3078
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2313-2571 4.28e-07

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 53.60  E-value: 4.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2313 KDLGQLEKKLEDLEEQLNHLLL--WLSPIRNQLEiynqpnqegpfDVKETEIAVQAKQPDVEEILSKGQHLYKEKP-ATQ 2389
Cdd:cd00176     7 RDADELEAWLSEKEELLSSTDYgdDLESVEALLK-----------KHEALEAELAAHEERVEALNELGEQLIEEGHpDAE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2390 PVKRKLEDLSSEWKAVNRLLQELRAKqpdlapglttigasptqtvtlvtqpvvtketaisklempsslMLEVPALADFNR 2469
Cdd:cd00176    76 EIQERLEELNQRWEELRELAEERRQR------------------------------------------LEEALDLQQFFR 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2470 AWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKtSNQEARTIITDRIERI 2549
Cdd:cd00176   114 DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEE-GHPDADEEIEEKLEEL 191
                         250       260
                  ....*....|....*....|..
gi 578837832 2550 QNQWDEVQEHLQNRRQQLNEML 2571
Cdd:cd00176   192 NERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
1052-1145 3.06e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.48  E-value: 3.06e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   1052 LKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEfASRLETELKELNTQWD 1131
Cdd:smart00150   10 LEAWLEEKEQLLASEDLG-KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERLEELNERWE 87
                            90
                    ....*....|....
gi 578837832   1132 HMCQQVYARKEALK 1145
Cdd:smart00150   88 ELKELAEERRQKLE 101
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1689-1963 8.01e-06

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 50.68  E-value: 8.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1689 QADTLLDESEKKKPQQKE--DVLKRLKAELNDIRPKVDSTRDQAANLMANRGDHCRKLVE--PQISELNHRFAAISHRIK 1764
Cdd:COG1340    16 KIEELREEIEELKEKRDElnEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKElkEERDELNEKLNELREELD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1765 TGKASIPLKELEQFNSD-IQKLLEPLEAEIQqgvnlkeedfNKDMNEDNEgtvKELLQRGDNLQQRITDERKREEIKIKQ 1843
Cdd:COG1340    96 ELRKELAELNKAGGSIDkLRKEIERLEWRQQ----------TEVLSPEEE---KELVEKIKELEKELEKAKKALEKNEKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1844 QLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDER--KIKEIDRELQKKKEELNAV 1921
Cdd:COG1340   163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAqeKADELHEEIIELQKELREL 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578837832 1922 RRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNF 1963
Cdd:COG1340   243 RKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTT 284
SPEC smart00150
Spectrin repeats;
719-819 9.28e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.94  E-value: 9.28e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    719 DITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQmvnEGVNADSIKQASE 798
Cdd:smart00150    6 DADELEAWLEEKEQLLASEDLG--KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE---GHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 578837832    799 QLNSRWIEFCQLLSERLNWLE 819
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2469-2773 1.40e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2469 RAWTELTDWLSLLDQVIKSQRVmvgDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTI------- 2541
Cdd:COG1196   232 LKLRELEAELEELEAELEELEA---ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiarle 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2542 -----ITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESwkegpyTVDAIQKKITETK 2616
Cdd:COG1196   309 errreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------AEAELAEAEEELE 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2617 QLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKvhmitENINASWRSIHKRVSEREAALEETHRLLQQfplDLEKFLAW 2696
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERL-----ERLEEELEELEEALAELEEEEEEEEEALEE---AAEEEAEL 454
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578837832 2697 LTEAETTANVLQDATRKERLLEdskgvkelmKQWQDLQGEIEAHTDVYHNLdensQKILRSLEGSDDAVLLQRRLDN 2773
Cdd:COG1196   455 EEEEEALLELLAELLEEAALLE---------AALAELLEELAEAAARLLLL----LEAEADYEGFLEGVKAALLLAG 518
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2152-2620 1.45e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2152 RTLNATGEEIIQQSSKTD--ASILQEKLGSLnlrwQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASI- 2228
Cdd:PRK03918  296 IKLSEFYEEYLDELREIEkrLSRLEEEINGI----EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKk 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2229 -----------PLEPGKEQQLKEKLEQVKLLVEE----LPLRQGILKQ--------LNETGG-----PVlVSAPISPEEQ 2280
Cdd:PRK03918  372 eelerlkkrltGLTPEKLEKELEELEKAKEEIEEeiskITARIGELKKeikelkkaIEELKKakgkcPV-CGRELTEEHR 450
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2281 DKLENKLKqtnlqwikvsralpEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ----PNQEGPFD 2356
Cdd:PRK03918  451 KELLEEYT--------------AELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQlkelEEKLKKYN 516
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2357 VKETEiavqAKQPDVEEILSKGQHLYKEKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVtl 2436
Cdd:PRK03918  517 LEELE----KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL-- 590
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2437 vtqpvvtkETAISKLEmpsslmlevpalaDFNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQKAtmqDLEQRR 2516
Cdd:PRK03918  591 --------EERLKELE-------------PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK---RLEELR 646
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2517 PQLEELITA--------AQNLKNKTSNQEARtiITDRIERIQNQWDEVQEHLQNRRQQLNEMLKdstqwleAKEEAEqVL 2588
Cdd:PRK03918  647 KELEELEKKyseeeyeeLREEYLELSRELAG--LRAELEELEKRREEIKKTLEKLKEELEEREK-------AKKELE-KL 716
                         490       500       510
                  ....*....|....*....|....*....|..
gi 578837832 2589 GQARAKLEswkegpytvdAIQKKITETKQLAK 2620
Cdd:PRK03918  717 EKALERVE----------ELREKVKKYKALLK 738
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1870-2094 2.22e-05

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 48.60  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1870 QWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQI 1942
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1943 Q--LSKRWREIESKFAQFRRLnfaqihtvreetmmvmtedmpLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCaKDF 2020
Cdd:cd00176    81 LeeLNQRWEELRELAEERRQR---------------------LEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDL 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578837832 2021 EDLFKQEESLKNIKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFDRS 2094
Cdd:cd00176   139 ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2681-2783 5.09e-05

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: 45.00  E-value: 5.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2681 RLLQQFPLDLEKFLAWLTEAETTANvlqdatrKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILrsLEG 2760
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLS-------SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI--DEG 71
                           90       100
                   ....*....|....*....|...
gi 578837832  2761 SDDAVLLQRRLDNMNFKWSELRK 2783
Cdd:pfam00435   72 HYASEEIQERLEELNERWEQLLE 94
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
2478-2617 9.31e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.20  E-value: 9.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2478 LSLLDQVIKSQRVMVG-DLEDINEMIikqkatmQDLEQRRPQLEELITAAQNLKNKTsnqeartiitdriERIQNQWDEV 2556
Cdd:PRK00409  497 LGLPENIIEEAKKLIGeDKEKLNELI-------ASLEELERELEQKAEEAEALLKEA-------------EKLKEELEEK 556
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578837832 2557 QEHLQNRRQQLNEMLKDSTQWL--EAKEEAEQVLGQARaklESWKEGPYTVDAiqKKITETKQ 2617
Cdd:PRK00409  557 KEKLQEEEDKLLEEAEKEAQQAikEAKKEADEIIKELR---QLQKGGYASVKA--HELIEARK 614
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
2152-2348 2.25e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2152 RTLNATGEEIIQQSSKTDASILQEKLGSLNlrwqevcKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIple 2231
Cdd:COG3206   152 AVANALAEAYLEQNLELRREEARKALEFLE-------EQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQL--- 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2232 pgkeQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSAPISPEEQDkLENKLKQTNLQWIKVS----------RAL 2301
Cdd:COG3206   222 ----SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-LRAQLAELEAELAELSarytpnhpdvIAL 296
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578837832 2302 PEKQGEIEAQIKDlgQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ 2348
Cdd:COG3206   297 RAQIAALRAQLQQ--EAQRILASLEAELEALQAREASLQAQLAQLEA 341
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1109-1379 3.81e-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: 43.51  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1109 NEAEPEFaSRLETELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDfeyktpDELQKA 1188
Cdd:TIGR02168  701 AELRKEL-EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE------ERLEEA 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1189 VEEMKRAKEEAQQKEAKVKLLTESVNSVIAQappvaQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLE 1268
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREA-----LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1269 KANKWLNEVEFKLKTTENipgGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDG-----GVMDEL------------ 1331
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEE---LIEELESELEALLNERASLEEALALLRSELEELSEElreleSKRSELrreleelrekla 925
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1332 ------------INEELETFNSRWRELHEEAVRRQKLLEQSIQSAQEtekSLHLIQESLT 1379
Cdd:TIGR02168  926 qlelrleglevrIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR---RLKRLENKIK 982
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
552-819 4.39e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 41.66  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  552 KWQRLTEEQCLFSAWLSEKEDAVNKIHTTgfKDQNEMLSSLQKLAVLKADLEKKKQSMGKLYSLKQDLLSTLKNKSvtQK 631
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA--EE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  632 TEAWLDNFARCWDNLVQKLEKSTAQISQAVTTTQPSLtqttvmetvttvttreqilvkhaqeelpppppqkkrqitvdse 711
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR------------------------------------------- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  712 irkrldvDITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEgvNAD 791
Cdd:cd00176   114 -------DADDLEQWLEEKEAALASEDLG--KDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPD--ADE 182
                         250       260
                  ....*....|....*....|....*...
gi 578837832  792 SIKQASEQLNSRWIEFCQLLSERLNWLE 819
Cdd:cd00176   183 EIEEKLEELNERWEELLELAEERQKKLE 210
 
Name Accession Description Interval E-value
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
3117-3278 2.15e-113

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: 357.03  E-value: 2.15e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3117 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 3196
Cdd:cd16246     1 SLSAACEALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3197 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3276
Cdd:cd16246    81 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 160

                  ..
gi 578837832 3277 MR 3278
Cdd:cd16246   161 MR 162
EFh_DMD_like cd16242
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ...
3117-3278 1.10e-103

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: 329.20  E-value: 1.10e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3117 SLSAACDALDQHNLK-QNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGI 3195
Cdd:cd16242     1 SLSTAIEAFDQHGLRaQNDKLIDVPDMITCLTTIYEALEEEHPTLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSFKVGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3196 ISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLD 3275
Cdd:cd16242    81 VLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSNIEPSVRSCFEKAGEKPEISAAHFLD 160

                  ...
gi 578837832 3276 WMR 3278
Cdd:cd16242   161 WLK 163
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
3118-3278 5.88e-84

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: 272.93  E-value: 5.88e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3118 LSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIIS 3197
Cdd:cd16247     2 LNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLMS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3198 LCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWM 3277
Cdd:cd16247    82 LSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDWM 161

                  .
gi 578837832 3278 R 3278
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 ...
3117-3277 4.65e-80

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: 261.65  E-value: 4.65e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3117 SLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 3196
Cdd:cd16248     1 TLSSATEIFTEHELQMSERVMDVVEVIHCLTALYERLEEERGILVNVPLCVDMCLNWLLNVYDSGRNGKIRVLSFKTGIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3197 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3276
Cdd:cd16248    81 CLCNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAFGGSNVEPSVRSCFRFAPGKPVIELSQFLEW 160

                  .
gi 578837832 3277 M 3277
Cdd:cd16248   161 M 161
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
128-238 6.91e-69

second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.


Pssm-ID: 409082  Cd Length: 111  Bit Score: 227.50  E-value: 6.91e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  128 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDP 207
Cdd:cd21233     1 SEKILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSATERLDHAFNIARQHLGIEKLLDP 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832  208 EDVDTTYPDKKSILMYITSLFQVLPQQVSIE 238
Cdd:cd21233    81 EDVATAHPDKKSILMYVTSLFQVLPQQVSIE 111
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
3118-3277 9.27e-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: 226.38  E-value: 9.27e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3118 LSAACDALDQHNLKQ-NDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGII 3196
Cdd:cd15901     2 LSTVLSVFDRHGLSGsQDSVLDCEELETILTELYIKLNKRRPDLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVKIALI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3197 SLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDW 3276
Cdd:cd15901    82 TLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVEAAVESCFQLARSRVGVSEDTFLSW 161

                  .
gi 578837832 3277 M 3277
Cdd:cd15901   162 L 162
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
3-113 1.31e-66

first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.


Pssm-ID: 409080  Cd Length: 111  Bit Score: 220.95  E-value: 1.31e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    3 DEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 82
Cdd:cd21231     1 YEREDVQKKTFTKWINAQFAKFGKPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832   83 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21231    81 LVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
7-113 1.82e-64

first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409035  Cd Length: 107  Bit Score: 214.55  E-value: 1.82e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    7 DVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNI 86
Cdd:cd21186     1 DVQKKTFTKWINSQLSKANKPPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNI 80
                          90       100
                  ....*....|....*....|....*..
gi 578837832   87 GSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21186    81 SSNDIVDGNPKLTLGLVWSIILHWQVK 107
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
128-232 2.17e-59

second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409036  Cd Length: 104  Bit Score: 199.96  E-value: 2.17e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  128 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDP 207
Cdd:cd21187     1 LEKTLLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLV-KDSPESRLEHAFTVAHEHLGIEKLLDP 79
                          90       100
                  ....*....|....*....|....*
gi 578837832  208 EDVDTTYPDKKSILMYITSLFQVLP 232
Cdd:cd21187    80 EDVNVEQPDKKSILMYVTSLFQVLP 104
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
3081-3199 1.20e-56

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: 193.14  E-value: 1.20e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  3081 TELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLK--QNDQPMDILQIINCLTTIYDRLEQEHN 3158
Cdd:pfam09068    1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 578837832  3159 N--LVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLC 3199
Cdd:pfam09068   81 TthQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
7-113 1.20e-55

first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.


Pssm-ID: 409081  Cd Length: 107  Bit Score: 189.45  E-value: 1.20e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    7 DVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNI 86
Cdd:cd21232     1 DVQKKTFTKWINARFSKSGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNI 80
                          90       100
                  ....*....|....*....|....*..
gi 578837832   87 GSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21232    81 GGTDIVDGNHKLTLGLLWSIILHWQVK 107
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
128-232 1.38e-51

second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.


Pssm-ID: 409083 [Multi-domain]  Cd Length: 104  Bit Score: 177.84  E-value: 1.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  128 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDP 207
Cdd:cd21234     1 SEKILLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVV-KMSPVERLEHAFSKAKNHLGIEKLLDP 79
                          90       100
                  ....*....|....*....|....*
gi 578837832  208 EDVDTTYPDKKSILMYITSLFQVLP 232
Cdd:cd21234    80 EDVAVQLPDKKSIIMYLTSLFEVLP 104
EF-hand_3 pfam09069
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
3203-3294 1.73e-49

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: 171.33  E-value: 1.73e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  3203 LEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGsnIEPSVRSCFQFANNKPEIEAALFLDWMRLEPQ 3282
Cdd:pfam09069    1 LVDKYRYLFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGG--IEPSVRSCFEQVGGKPKITLNHFLDWLMSEPQ 78
                           90
                   ....*....|..
gi 578837832  3283 SMVWLPVLHRVA 3294
Cdd:pfam09069   79 SLVWLPVLHRLA 90
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
127-232 9.76e-43

second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409038  Cd Length: 105  Bit Score: 152.55  E-value: 9.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  127 NSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLD 206
Cdd:cd21189     1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVR-NQSNRENLENAFNVAEKEFGVTRLLD 79
                          90       100
                  ....*....|....*....|....*.
gi 578837832  207 PEDVDTTYPDKKSILMYITSLFQVLP 232
Cdd:cd21189    80 PEDVDVPEPDEKSIITYVSSLYDVFP 105
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
3-108 9.39e-42

first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409095  Cd Length: 117  Bit Score: 150.21  E-value: 9.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    3 DEREDVQKKTFTKWVNAQFSKFGkQHIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNNNV 81
Cdd:cd21246    11 DEREAVQKKTFTKWVNSHLARVG-CRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQRV 89
                          90       100
                  ....*....|....*....|....*..
gi 578837832   82 DLVNIGSTDIVDGNHKLTLGLIWNIIL 108
Cdd:cd21246    90 HLENMGSHDIVDGNHRLTLGLIWTIIL 116
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
8-111 1.16e-41

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409037  Cd Length: 105  Bit Score: 149.47  E-value: 1.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    8 VQKKTFTKWVNAQFSKFGKqHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNIG 87
Cdd:cd21188     3 VQKKTFTKWVNKHLIKARR-RVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNIR 81
                          90       100
                  ....*....|....*....|....
gi 578837832   88 STDIVDGNHKLTLGLIWNIILHWQ 111
Cdd:cd21188    82 AEDIVDGNPKLTLGLIWTIILHFQ 105
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
132-228 1.01e-37

second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409043  Cd Length: 105  Bit Score: 138.31  E-value: 1.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDPEDVD 211
Cdd:cd21194     7 LLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLD-PNDHLGNLNNAFDVAEQELGIAKLLDAEDVD 85
                          90
                  ....*....|....*..
gi 578837832  212 TTYPDKKSILMYITSLF 228
Cdd:cd21194    86 VARPDEKSIMTYVASYY 102
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
1-108 1.17e-37

first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409042  Cd Length: 116  Bit Score: 138.58  E-value: 1.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    1 MEDEREDVQKKTFTKWVNAQFSKFGkQHIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNN 79
Cdd:cd21193     9 LQEERINIQKKTFTKWINSFLEKAN-LEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFLKTK 87
                          90       100
                  ....*....|....*....|....*....
gi 578837832   80 nVDLVNIGSTDIVDGNHKLTLGLIWNIIL 108
Cdd:cd21193    88 -VRLENIGAEDIVDGNPRLILGLIWTIIL 115
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
132-228 1.59e-37

second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409097  Cd Length: 105  Bit Score: 137.53  E-value: 1.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDPEDVD 211
Cdd:cd21248     7 LLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLS-KSNALYNLQNAFNVAEQKLGLTKLLDPEDVN 85
                          90
                  ....*....|....*..
gi 578837832  212 TTYPDKKSILMYITSLF 228
Cdd:cd21248    86 VEQPDEKSIITYVVTYY 102
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
1-108 5.82e-36

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409166  Cd Length: 132  Bit Score: 134.41  E-value: 5.82e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    1 MEDEREDVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNN 79
Cdd:cd21317    24 LADEREAVQKKTFTKWVNSHLARVTCR-IGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLKEQ 102
                          90       100
                  ....*....|....*....|....*....
gi 578837832   80 NVDLVNIGSTDIVDGNHKLTLGLIWNIIL 108
Cdd:cd21317   103 KVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
1-108 6.59e-36

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409167  Cd Length: 139  Bit Score: 134.38  E-value: 6.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    1 MEDEREDVQKKTFTKWVNAQFSKFGkQHIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNN 79
Cdd:cd21318    31 LADEREAVQKKTFTKWVNSHLARVP-CRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQ 109
                          90       100
                  ....*....|....*....|....*....
gi 578837832   80 NVDLVNIGSTDIVDGNHKLTLGLIWNIIL 108
Cdd:cd21318   110 RVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
124-229 7.29e-36

second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409168  Cd Length: 112  Bit Score: 133.21  E-value: 7.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  124 QQTNSEK-ILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIE 202
Cdd:cd21319     1 RETRSAKdALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLK-KSNARHNLEHAFNVAERQLGIT 79
                          90       100
                  ....*....|....*....|....*..
gi 578837832  203 KLLDPEDVDTTYPDKKSILMYITSLFQ 229
Cdd:cd21319    80 KLLDPEDVFTENPDEKSIITYVVAFYH 106
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
4-113 2.25e-35

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409090  Cd Length: 113  Bit Score: 131.73  E-value: 2.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    4 EREDVQKKTFTKWVNAQFSKFGK-QHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGST--RVHALNNVNKALRVLQNNN 80
Cdd:cd21241     1 EQERVQKKTFTNWINSYLAKRKPpMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578837832   81 VDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21241    81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
3-115 2.64e-35

first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409085  Cd Length: 128  Bit Score: 132.42  E-value: 2.64e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    3 DEREDVQKKTFTKWVNAQFSKFgKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 82
Cdd:cd21236    12 DERDKVQKKTFTKWINQHLMKV-RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVK 90
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578837832   83 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVKNV 115
Cdd:cd21236    91 LVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 123
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
4-113 1.13e-34

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409091  Cd Length: 111  Bit Score: 129.95  E-value: 1.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    4 EREDVQKKTFTKWVNAQFSKFGKQH-IENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 82
Cdd:cd21242     1 EQEQTQKRTFTNWINSQLAKHSPPSvVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832   83 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21242    81 LINIHVPDIIEGKPSIILGLIWTIILHFHIE 111
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
2-224 3.63e-34

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 142.00  E-value: 3.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    2 EDEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPK--EKGSTRVHALNNVNKALRVLQNN 79
Cdd:COG5069     3 AKKWQKVQKKTFTKWTNEKLISGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   80 NVDLVNIGSTDIVDGNHKLTLGLIWNIILhwqvKNVMKNIMAGLQQTNSEKILLsWVRQSTRNY-PQVNVINFTTSWSDG 158
Cdd:COG5069    83 GVKLFNIGPQDIVDGNPKLILGLIWSLIS----RLTIATINEEGELTKHINLLL-WCDEDTGGYkPEVDTFDFFRSWRDG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578837832  159 LALNALIHSHRPDLFDWNSVVCQQSATQ-RLEHAFNIARYQLGIEKLLDPEDV-DTTYPDKKSILMYI 224
Cdd:COG5069   158 LAFSALIHDSRPDTLDPNVLDLQKKNKAlNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYV 225
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
3-118 1.03e-33

first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409084  Cd Length: 119  Bit Score: 127.45  E-value: 1.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    3 DEREDVQKKTFTKWVNAQFSKfGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 82
Cdd:cd21235     1 DERDRVQKKTFTKWVNKHLIK-AQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 578837832   83 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVKNVMKN 118
Cdd:cd21235    80 LVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 115
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
4-113 1.14e-32

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409039  Cd Length: 113  Bit Score: 124.22  E-value: 1.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    4 EREDVQKKTFTKWVNAQFSKFGKQH-IENLFSDLQDGRRLLDLLEGLTGQKLPKEKG--STRVHALNNVNKALRVLQNNN 80
Cdd:cd21190     1 EQERVQKKTFTNWINSHLAKLSQPIvINDLFVDIKDGTALLRLLEVLSGQKLPIESGrvLQRAHKLSNIRNALDFLTKRC 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578837832   81 VDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21190    81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
6-108 3.21e-32

first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409063  Cd Length: 105  Bit Score: 122.50  E-value: 3.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    6 EDVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNNNVDLV 84
Cdd:cd21214     3 EKQQRKTFTAWCNSHLRKAGTQ-IENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLV 81
                          90       100
                  ....*....|....*....|....
gi 578837832   85 NIGSTDIVDGNHKLTLGLIWNIIL 108
Cdd:cd21214    82 SIGAEEIVDGNLKMTLGMIWTIIL 105
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
3-115 4.32e-31

first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409086  Cd Length: 118  Bit Score: 119.75  E-value: 4.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    3 DEREDVQKKTFTKWVNAQFSKFgKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVD 82
Cdd:cd21237     1 DERDRVQKKTFTKWVNKHLMKV-RKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVK 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578837832   83 LVNIGSTDIVDGNHKLTLGLIWNIILHWQVKNV 115
Cdd:cd21237    80 LVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 112
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
126-232 4.51e-31

second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409088  Cd Length: 104  Bit Score: 119.32  E-value: 4.51e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  126 TNSEKILLsWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQrLEHAFNIARyQLGIEKLL 205
Cdd:cd21239     1 SAKERLLL-WSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLAN-LEHAFYVAE-KLGVTRLL 77
                          90       100
                  ....*....|....*....|....*..
gi 578837832  206 DPEDVDTTYPDKKSILMYITSLFQVLP 232
Cdd:cd21239    78 DPEDVDVSSPDEKSVITYVSSLYDVFP 104
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
6-108 2.23e-30

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409064  Cd Length: 107  Bit Score: 117.50  E-value: 2.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    6 EDVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK--EKGSTRVHALNNVNKALRVLQNNNVDL 83
Cdd:cd21215     2 VDVQKKTFTKWLNTKLSSRGLS-ITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKL 80
                          90       100
                  ....*....|....*....|....*
gi 578837832   84 VNIGSTDIVDGNHKLTLGLIWNIIL 108
Cdd:cd21215    81 TNIGAEDIVDGNLKLILGLLWTLIL 105
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
125-228 2.44e-30

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409098  Cd Length: 109  Bit Score: 117.27  E-value: 2.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  125 QTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKL 204
Cdd:cd21249     2 LRSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLR-PDRPLYNLANAFLVAEQELGISQL 80
                          90       100
                  ....*....|....*....|....
gi 578837832  205 LDPEDVDTTYPDKKSILMYItSLF 228
Cdd:cd21249    81 LDPEDVAVPHPDERSIMTYV-SLY 103
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
124-229 3.43e-30

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409170  Cd Length: 119  Bit Score: 117.47  E-value: 3.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  124 QQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEK 203
Cdd:cd21321     2 EKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLK-KSNAHYNLQNAFNVAEKELGLTK 80
                          90       100
                  ....*....|....*....|....*.
gi 578837832  204 LLDPEDVDTTYPDKKSILMYITSLFQ 229
Cdd:cd21321    81 LLDPEDVNVDQPDEKSIITYVATYYH 106
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
124-229 3.57e-30

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409171  Cd Length: 130  Bit Score: 117.85  E-value: 3.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  124 QQTNSEK-ILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIE 202
Cdd:cd21322    13 RETRSAKdALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLT-KSNATYNLQQAFNTAEQHLGLT 91
                          90       100
                  ....*....|....*....|....*..
gi 578837832  203 KLLDPEDVDTTYPDKKSILMYITSLFQ 229
Cdd:cd21322    92 KLLDPEDVNMEAPDEKSIITYVVSFYH 118
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
3303-3351 6.48e-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: 6.48e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578837832 3303 AKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEY 3351
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
125-232 7.44e-30

second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409092  Cd Length: 109  Bit Score: 115.88  E-value: 7.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  125 QTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKL 204
Cdd:cd21243     3 KGGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLK-RRSNRENLETAFTVAEKELGIPRL 81
                          90       100
                  ....*....|....*....|....*...
gi 578837832  205 LDPEDVDTTYPDKKSILMYITSLFQVLP 232
Cdd:cd21243    82 LDPEDVDVDKPDEKSIMTYVAQFLKKYP 109
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
4-113 1.74e-29

first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409040  Cd Length: 114  Bit Score: 114.98  E-value: 1.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    4 EREDVQKKTFTKWVNAQFSKFGKQ-HIENLFSDLQDGRRLLDLLEGLTGQKLPKE--KGSTRVHALNNVNKALRVLQNNN 80
Cdd:cd21191     1 ERENVQKRTFTRWINLHLEKCNPPlEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578837832   81 VDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVK 113
Cdd:cd21191    81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIK 113
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
1-108 1.83e-29

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409165  Cd Length: 154  Bit Score: 116.68  E-value: 1.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    1 MEDEREDVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQNN 79
Cdd:cd21316    46 LADEREAVQKKTFTKWVNSHLARVSCR-ITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQ 124
                          90       100
                  ....*....|....*....|....*....
gi 578837832   80 NVDLVNIGSTDIVDGNHKLTLGLIWNIIL 108
Cdd:cd21316   125 RVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
7-112 2.79e-28

first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409076  Cd Length: 109  Bit Score: 111.23  E-value: 2.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    7 DVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK--EKGSTRVHALNNVNKALRVLQNNNVDLV 84
Cdd:cd21227     3 EIQKNTFTNWVNEQLKPTGMS-VEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLV 81
                          90       100
                  ....*....|....*....|....*...
gi 578837832   85 NIGSTDIVDGNHKLTLGLIWNIILHWQV 112
Cdd:cd21227    82 NIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
126-232 8.36e-28

second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409087  Cd Length: 106  Bit Score: 110.11  E-value: 8.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  126 TNSEKILLsWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLL 205
Cdd:cd21238     2 TAKEKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLL 79
                          90       100
                  ....*....|....*....|....*..
gi 578837832  206 DPEDVDTTYPDKKSILMYITSLFQVLP 232
Cdd:cd21238    80 DPEDVDVPQPDEKSIITYVSSLYDAMP 106
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
124-230 2.44e-27

second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409065  Cd Length: 115  Bit Score: 108.99  E-value: 2.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  124 QQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEK 203
Cdd:cd21216     7 EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLR-KDDPRENLNLAFDVAEKHLDIPK 85
                          90       100
                  ....*....|....*....|....*...
gi 578837832  204 LLDPED-VDTTYPDKKSILMYITSLFQV 230
Cdd:cd21216    86 MLDAEDiVNTPRPDERSVMTYVSCYYHA 113
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
127-229 3.54e-27

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409169  Cd Length: 108  Bit Score: 108.26  E-value: 3.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  127 NSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLD 206
Cdd:cd21320     2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLK-KSNAHYNLQNAFNLAEQHLGLTKLLD 80
                          90       100
                  ....*....|....*....|...
gi 578837832  207 PEDVDTTYPDKKSILMYITSLFQ 229
Cdd:cd21320    81 PEDISVDHPDEKSIITYVVTYYH 103
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
333-550 8.27e-27

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: 111.00  E-value: 8.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  333 LDRYQTALEEVLSWLLSAEDTLQAQgEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEV 412
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI---EEGHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  413 QEQMNLLNSRWECLRVASMEKQSNLHRVLMDLQ-NQKLKELNDWLTKTEERtrkMEEEPLGPDLEDLKRQVQQHKVLQED 491
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQQfFRDADDLEQWLEEKEAA---LASEDLGKDLESVEELLKKHKELEEE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837832  492 LEQEQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDIL 550
Cdd:cd00176   155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
129-232 1.15e-25

second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409089  Cd Length: 107  Bit Score: 103.97  E-value: 1.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  129 EKILLsWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARyQLGIEKLLDPE 208
Cdd:cd21240     7 EKLLL-WTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQ-IQSNRENLEQAFEVAE-RLGVTRLLDAE 83
                          90       100
                  ....*....|....*....|....
gi 578837832  209 DVDTTYPDKKSILMYITSLFQVLP 232
Cdd:cd21240    84 DVDVPSPDEKSVITYVSSIYDAFP 107
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
125-232 1.66e-25

second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409041  Cd Length: 107  Bit Score: 103.27  E-value: 1.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  125 QTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKL 204
Cdd:cd21192     1 QGSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVK-NRSPRDNLELAFRIAEQHLNIPRL 79
                          90       100
                  ....*....|....*....|....*...
gi 578837832  205 LDPEDVDTTYPDKKSILMYITSLFQVLP 232
Cdd:cd21192    80 LEVEDVLVDKPDERSIMTYVSQFLRMFP 107
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
8-112 1.89e-25

first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409160  Cd Length: 124  Bit Score: 104.07  E-value: 1.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    8 VQKKTFTKWVNAQFSKFGKqHIENLFSDLQDGRRLLDLLEGLTGQKLPK--EKGSTRVHALNNVNKALRVLQNN-NVDLV 84
Cdd:cd21311    15 IQQNTFTRWANEHLKTANK-HIADLETDLSDGLRLIALVEVLSGKKFPKfnKRPTFRSQKLENVSVALKFLEEDeGIKIV 93
                          90       100
                  ....*....|....*....|....*...
gi 578837832   85 NIGSTDIVDGNHKLTLGLIWNIILHWQV 112
Cdd:cd21311    94 NIDSSDIVDGKLKLILGLIWTLILHYSI 121
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
128-228 2.32e-25

second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409075  Cd Length: 103  Bit Score: 102.93  E-value: 2.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  128 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDwNSVVCQQSATQRLEHAFNIARYQLGIEKLLDP 207
Cdd:cd21226     1 SEDGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFK-QAAIEQMDAEARLNLAFDFAEKKLGIPKLLEA 79
                          90       100
                  ....*....|....*....|.
gi 578837832  208 EDVDTTYPDKKSILMYiTSLF 228
Cdd:cd21226    80 EDVMTGNPDERSIVLY-TSLF 99
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
130-231 1.28e-24

calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409102  Cd Length: 106  Bit Score: 100.88  E-value: 1.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  130 KILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVvcqqSATQRLEH---AFNIARYQLGIEKLLD 206
Cdd:cd21253     4 KALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSL----SKENVYENnklAFTVAEKELGIPALLD 79
                          90       100
                  ....*....|....*....|....*.
gi 578837832  207 PED-VDTTYPDKKSILMYITSLFQVL 231
Cdd:cd21253    80 AEDmVALKVPDKLSILTYVSQYYNYF 105
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
132-228 4.62e-24

second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409140  Cd Length: 115  Bit Score: 99.52  E-value: 4.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDPEDV- 210
Cdd:cd21291    15 LLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLD-KKDHRGNMQLAFDIASKEIGIPQLLDVEDVc 93
                          90
                  ....*....|....*...
gi 578837832  211 DTTYPDKKSILMYITSLF 228
Cdd:cd21291    94 DVAKPDERSIMTYVAYYF 111
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
1-112 1.08e-23

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409096  Cd Length: 125  Bit Score: 99.06  E-value: 1.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    1 MEDEREDVQKKTFTKWVNAQFSKFGKQ-HIENLFSDLQDGRRLLDLLEGLTGQKLPK-EKGSTRVHALNNVNKALRVLQN 78
Cdd:cd21247    13 LQEQRMTMQKKTFTKWMNNVFSKNGAKiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLKT 92
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 578837832   79 N-NVDLvnIGSTDIVDGNHKLTLGLIWNIILHWQV 112
Cdd:cd21247    93 KvPVKL--IGPENIVDGDRTLILGLIWIIILRFQI 125
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2097-2312 1.96e-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: 101.37  E-value: 1.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2097 KWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAK-YKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtDASILQE 2175
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEaLLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2176 KLGSLNLRWQEVCKQLSDRKKRLEEQKNiLSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLR 2255
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837832 2256 QGILKQLNETGGPVLVSAPisPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQI 2312
Cdd:cd00176   159 EPRLKSLNELAEELLEEGH--PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
132-231 8.97e-23

calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409188  Cd Length: 105  Bit Score: 95.43  E-value: 8.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSA--TQRlehAFNIARYQLGIEKLLDPED 209
Cdd:cd22198     5 LLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAenNQL---AFDVAEQELGIPPVMTGQE 81
                          90       100
                  ....*....|....*....|...
gi 578837832  210 -VDTTYPDKKSILMYITSLFQVL 231
Cdd:cd22198    82 mASLAVPDKLSMVSYLSQFYEAF 104
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
8-110 9.35e-23

first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409032  Cd Length: 108  Bit Score: 95.63  E-value: 9.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    8 VQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK---EKGSTRVHALNNVNKALRVLQNNNVDLV 84
Cdd:cd21183     4 IQANTFTRWCNEHLKERGMQ-IHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
                          90       100
                  ....*....|....*....|....*.
gi 578837832   85 NIGSTDIVDGNHKLTLGLIWNIILHW 110
Cdd:cd21183    83 NIGSGDIVNGNIKLILGLIWTLILHY 108
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
127-227 4.33e-22

calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409047  Cd Length: 105  Bit Score: 93.64  E-value: 4.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  127 NSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSvVCQQSATQRLEHAFNIARyQLGIEKLLD 206
Cdd:cd21198     1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSS-LSPHDIKENCKLAFDAAA-KLGIPRLLD 78
                          90       100
                  ....*....|....*....|..
gi 578837832  207 PED-VDTTYPDKKSILMYITSL 227
Cdd:cd21198    79 PADmVLLSVPDKLSVMTYLHQI 100
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
125-229 4.68e-22

second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409093  Cd Length: 109  Bit Score: 93.75  E-value: 4.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  125 QTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKL 204
Cdd:cd21244     3 KMSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLK-GRSNRENLEEAFRIAEQELKIPRL 81
                          90       100
                  ....*....|....*....|....*
gi 578837832  205 LDPEDVDTTYPDKKSILMYITSLFQ 229
Cdd:cd21244    82 LEPEDVDVVNPDEKSIMTYVAQFLQ 106
EFh_DAH cd16245
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ...
3117-3277 2.55e-21

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: 93.51  E-value: 2.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3117 SLSAACDALDQHNLKQND-----QPMDILQIINcltTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSF 3191
Cdd:cd16245     1 PLKLIMGVFDRHQLSNSEnnlclPPDELEAVLH---DIYFAAEKLGNFNIDVDLATELLANLFLNVFDPERKKSISVLEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3192 KTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAA 3271
Cdd:cd16245    78 KVFLTLLCGSSLQEKYLYLFQLLADHNNCVSRKRLEALLKSLAKLLSYLGEDVAFGSHLIELAVEQCFENSPGLVGLTEY 157

                  ....*.
gi 578837832 3272 LFLDWM 3277
Cdd:cd16245   158 QFIGWW 163
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
11-109 3.22e-21

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 90.84  E-value: 3.22e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832     11 KTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEK---GSTRVHALNNVNKALRVLQNNNVDLVNIG 87
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 578837832     88 STDIVDGNhKLTLGLIWNIILH 109
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLISL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
130-227 3.80e-21

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 90.84  E-value: 3.80e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    130 KILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQ---QSATQRLEHAFNIARYQLGIEKLLD 206
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 578837832    207 PEDVDTTYPDKKSILMYITSL 227
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
131-231 9.99e-21

calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409049  Cd Length: 107  Bit Score: 89.71  E-value: 9.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  131 ILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVvcqqSATQR---LEHAFNIARYQLGIEKLLDP 207
Cdd:cd21200     5 MLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSL----DPKNRrknFELAFSTAEELADIAPLLEV 80
                          90       100
                  ....*....|....*....|....*.
gi 578837832  208 ED--VDTTYPDKKSILMYITSLFQVL 231
Cdd:cd21200    81 EDmvRMGNRPDWKCVFTYVQSLYRHL 106
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2682-2925 1.24e-20

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: 93.28  E-value: 1.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2682 LLQQFPLDLEKFLAWLTEAETTANVLQDAtrkerllEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGS 2761
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-------DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGH 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2762 DDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHlSLQELLVWLQLKDDELSRQaPIGGDFPAVQKQNDVHR 2841
Cdd:cd00176    72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2842 AFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKlyqeprelppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKI 2921
Cdd:cd00176   150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE--------------------IEEKLEELNERWEELLELAEERQKKL 209

                  ....
gi 578837832 2922 DETL 2925
Cdd:cd00176   210 EEAL 213
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
8-110 1.86e-20

first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409077  Cd Length: 108  Bit Score: 89.08  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    8 VQKKTFTKWVNAQFSKFGKqHIENLFSDLQDGRRLLDLLEGLTGQKLPK---EKGSTRVHALNNVNKALRVLQNNNVDLV 84
Cdd:cd21228     4 IQQNTFTRWCNEHLKCVNK-RIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
                          90       100
                  ....*....|....*....|....*.
gi 578837832   85 NIGSTDIVDGNHKLTLGLIWNIILHW 110
Cdd:cd21228    83 SIDSSAIVDGNLKLILGLIWTLILHY 108
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
130-228 1.97e-20

calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409046  Cd Length: 105  Bit Score: 88.75  E-value: 1.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  130 KILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVvcqqSATQRLEH---AFNIARYQLGIEKLLD 206
Cdd:cd21197     3 QALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSL----KKDNWLENnrlAFRVAETSLGIPALLD 78
                          90       100
                  ....*....|....*....|...
gi 578837832  207 PED-VDTTYPDKKSILMYITSLF 228
Cdd:cd21197    79 AEDmVTMHVPDRLSIITYVSQYY 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
128-232 2.42e-20

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 88.88  E-value: 2.42e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   128 SEKILLSWVRQSTRNY-PQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQS-ATQRLEHAFNIARYQLGIEK-L 204
Cdd:pfam00307    3 LEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFdKLENINLALDVAEKKLGVPKvL 82
                           90       100
                   ....*....|....*....|....*...
gi 578837832   205 LDPEDVDTtyPDKKSILMYITSLFQVLP 232
Cdd:pfam00307   83 IEPEDLVE--GDNKSVLTYLASLFRRFQ 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2464-2680 2.49e-20

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: 92.12  E-value: 2.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2464 LADFNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIIT 2543
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2544 DRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAkEEAEQVLGQARAKLESwKEGPYTVDAIQKKITETKQLAKDLR 2623
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837832 2624 QWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETH 2680
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
123-231 2.90e-20

second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409139  Cd Length: 125  Bit Score: 89.37  E-value: 2.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  123 LQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQrLEHAFNIARYQLGIE 202
Cdd:cd21290     9 VEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTN-LNNAFEVAEKYLDIP 87
                          90       100       110
                  ....*....|....*....|....*....|
gi 578837832  203 KLLDPED-VDTTYPDKKSILMYITSLFQVL 231
Cdd:cd21290    88 KMLDAEDiVNTARPDEKAIMTYVSSFYHAF 117
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
7-111 4.42e-20

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 88.11  E-value: 4.42e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832     7 DVQKKTFTKWVNAQFSK-FGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEK-GSTRVHALNNVNKALRVLQNN-NVDL 83
Cdd:pfam00307    1 LELEKELLRWINSHLAEyGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKlGVPK 80
                           90       100
                   ....*....|....*....|....*...
gi 578837832    84 VNIGSTDIVDGNHKLTLGLIWNIILHWQ 111
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
130-232 1.24e-19

second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409094  Cd Length: 106  Bit Score: 86.77  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  130 KILLSWVRQSTRNYpQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDPED 209
Cdd:cd21245     6 KALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQAL-EKSPRENLEDAFRIAQESLGIPPLLEPED 83
                          90       100
                  ....*....|....*....|...
gi 578837832  210 VDTTYPDKKSILMYITSLFQVLP 232
Cdd:cd21245    84 VMVDSPDEQSIMTYVAQFLEHFP 106
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
123-231 2.12e-19

second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409138  Cd Length: 124  Bit Score: 86.70  E-value: 2.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  123 LQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWnSVVCQQSATQRLEHAFNIARYQLGIE 202
Cdd:cd21289     6 VEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDY-AKLRKDDPIGNLNTAFEVAEKYLDIP 84
                          90       100       110
                  ....*....|....*....|....*....|
gi 578837832  203 KLLDPED-VDTTYPDKKSILMYITSLFQVL 231
Cdd:cd21289    85 KMLDAEDiVNTPKPDEKAIMTYVSCFYHAF 114
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
123-231 4.25e-19

second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409136  Cd Length: 124  Bit Score: 85.91  E-value: 4.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  123 LQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQrLEHAFNIARYQLGIE 202
Cdd:cd21287     6 VEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTN-LNTAFDVAEKYLDIP 84
                          90       100       110
                  ....*....|....*....|....*....|
gi 578837832  203 KLLDPED-VDTTYPDKKSILMYITSLFQVL 231
Cdd:cd21287    85 KMLDAEDiVGTARPDEKAIMTYVSSFYHAF 114
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
132-231 4.88e-19

calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409044 [Multi-domain]  Cd Length: 110  Bit Score: 85.09  E-value: 4.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDPEDVD 211
Cdd:cd21195     9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLN-EDDAVENNQLAFDVAEREFGIPPVTTGKEMA 87
                          90       100
                  ....*....|....*....|.
gi 578837832  212 TT-YPDKKSILMYITSLFQVL 231
Cdd:cd21195    88 SAqEPDKLSMVMYLSKFYELF 108
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
128-226 6.49e-19

second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409033  Cd Length: 103  Bit Score: 84.60  E-value: 6.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  128 SEKILLSWVRQSTrnyPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDP 207
Cdd:cd21184     2 GKSLLLEWVNSKI---PEYKVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPLENATKAMDIAEEELGIPKIITP 78
                          90
                  ....*....|....*....
gi 578837832  208 EDVDTTYPDKKSILMYITS 226
Cdd:cd21184    79 EDMVSPNVDELSVMTYLSY 97
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
3136-3277 1.03e-18

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: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3136 PMDILQIINCLTTIY----DRLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLF 3211
Cdd:cd16244    22 ELSVSRLETLLSSIYyqlnKRLPTTHQ--IDVDQSISLLLNWLLAAYDPEATGRLTVFSVKVALSTLCAGKLVDKLRYIF 99
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578837832 3212 KQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSniEPSVRSCFQfANNKPEIEAalFLDWM 3277
Cdd:cd16244   100 SQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYN--ESAARSCFP-GQSKVTVND--FLDVM 160
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
132-231 1.06e-18

calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409100 [Multi-domain]  Cd Length: 111  Bit Score: 84.23  E-value: 1.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARYQLGIEKLLDPEDVD 211
Cdd:cd21251    10 LLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLD-EQDVEKNNQLAFDIAEKEFGISPIMTGKEMA 88
                          90       100
                  ....*....|....*....|.
gi 578837832  212 TT-YPDKKSILMYITSLFQVL 231
Cdd:cd21251    89 SVgEPDKLSMVMYLTQFYEMF 109
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
129-234 1.38e-18

calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409108  Cd Length: 112  Bit Score: 83.89  E-value: 1.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  129 EKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSvVCQQSATQRLEHAFNIARYQLGIEKLLDPE 208
Cdd:cd21259     3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQ-LSPQNRRHNFEVAFSSAEKHADCPQLLDVE 81
                          90       100
                  ....*....|....*....|....*..
gi 578837832  209 D-VDTTYPDKKSILMYITSLFQVLPQQ 234
Cdd:cd21259    82 DmVRMREPDWKCVYTYIQEFYRCLVQK 108
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
127-230 4.04e-18

calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409103  Cd Length: 107  Bit Score: 82.21  E-value: 4.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  127 NSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSvVCQQSATQRLEHAFNIARyQLGIEKLLD 206
Cdd:cd21254     1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKS-LNPHDIKENNKKAYDGFA-SLGISRLLE 78
                          90       100
                  ....*....|....*....|....*
gi 578837832  207 PED-VDTTYPDKKSILMYitsLFQV 230
Cdd:cd21254    79 PSDmVLLAVPDKLTVMTY---LYQI 100
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
132-228 4.44e-18

calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409101  Cd Length: 107  Bit Score: 82.22  E-value: 4.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSvVCQQSATQRLEHAFNIARYQLGIEKLLDPED-V 210
Cdd:cd21252     5 LQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDS-LSKDNVYENNRLAFEVAERELGIPALLDPEDmV 83
                          90
                  ....*....|....*...
gi 578837832  211 DTTYPDKKSILMYITSLF 228
Cdd:cd21252    84 SMKVPDCLSIMTYVSQYY 101
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
128-234 7.12e-18

calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409109  Cd Length: 116  Bit Score: 82.05  E-value: 7.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  128 SEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVvcqQSATQR--LEHAFNIARYQLGIEKLL 205
Cdd:cd21260     2 VKNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAEL---DPANRRhnFTLAFSTAEKHADCAPLL 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 578837832  206 DPED-VDTTYPDKKSILMYITSLFQVLPQQ 234
Cdd:cd21260    79 EVEDmVRMSVPDSKCVYTYIQELYRSLVQK 108
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
123-231 8.86e-18

second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409137  Cd Length: 124  Bit Score: 82.04  E-value: 8.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  123 LQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWnSVVCQQSATQRLEHAFNIARYQLGIE 202
Cdd:cd21288     6 VEETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDY-SKLNKDDPIGNINLAMEIAEKHLDIP 84
                          90       100       110
                  ....*....|....*....|....*....|
gi 578837832  203 KLLDPED-VDTTYPDKKSILMYITSLFQVL 231
Cdd:cd21288    85 KMLDAEDiVNTPKPDERAIMTYVSCFYHAF 114
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
9-109 9.49e-18

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.


Pssm-ID: 409061  Cd Length: 105  Bit Score: 81.09  E-value: 9.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    9 QKKTFTKWVNAQFSKFG-KQHIENLFSDLQDGRRLLDLLEGLTGQKLPK--EKGSTRVHALNNVNKALRVLQNNNVDLVN 85
Cdd:cd21212     1 EIEIYTDWANHYLEKGGhKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGihSRPKTRAQKLENIQACLQFLAALGVDVQG 80
                          90       100
                  ....*....|....*....|....
gi 578837832   86 IGSTDIVDGNHKLTLGLIWNIILH 109
Cdd:cd21212    81 ITAEDIVDGNLKAILGLFFSLSRY 104
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
129-231 8.29e-17

calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409107  Cd Length: 111  Bit Score: 78.94  E-value: 8.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  129 EKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSvVCQQSATQRLEHAFNIARYQLGIEKLLDPE 208
Cdd:cd21258     3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQ-LSPQNRRQNFEVAFSAAEMLADCVPLVEVE 81
                          90       100
                  ....*....|....*....|....*
gi 578837832  209 D--VDTTYPDKKSILMYITSLFQVL 231
Cdd:cd21258    82 DmmIMGKKPDSKCVFTYVQSLYNHL 106
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
8-112 9.17e-17

first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409159  Cd Length: 125  Bit Score: 79.30  E-value: 9.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    8 VQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPKE---KGSTRVHALNNVNKALRVLQNNNVDLV 84
Cdd:cd21310    16 IQQNTFTRWCNEHLKCVQKR-LNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
                          90       100
                  ....*....|....*....|....*...
gi 578837832   85 NIGSTDIVDGNHKLTLGLIWNIILHWQV 112
Cdd:cd21310    95 SIDSKAIVDGNLKLILGLIWTLILHYSI 122
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
3299-3344 9.74e-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: 9.74e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 578837832  3299 AKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSgRVAKGHKM 3344
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQM 45
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
132-230 3.05e-16

calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409099 [Multi-domain]  Cd Length: 110  Bit Score: 77.23  E-value: 3.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSvVCQQSATQRLEHAFNIARYQLGIEKLLDPEDVD 211
Cdd:cd21250     9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDS-LNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMA 87
                          90       100
                  ....*....|....*....|
gi 578837832  212 TTY-PDKKSILMYITSLFQV 230
Cdd:cd21250    88 SAEePDKLSMVMYLSKFYEL 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1041-1255 3.54e-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: 80.18  E-value: 3.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1041 KLRKIQNHIQTLKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEfASRLE 1120
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1121 TELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQkDLSEMHEWMTQAEEEyLERDFEYKTPDELQKAVEEMKRAKEEAQ 1200
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAA-LASEDLGKDLESVEELLKKHKELEEELE 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578837832 1201 QKEAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNGKCKTLEE 1255
Cdd:cd00176   157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
132-227 3.66e-16

calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409104  Cd Length: 105  Bit Score: 76.75  E-value: 3.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNiARYQLGIEKLLDPED-V 210
Cdd:cd21255     6 LLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLD-PLDIKENNKKAFE-AFASLGVPRLLEPADmV 83
                          90
                  ....*....|....*..
gi 578837832  211 DTTYPDKKSILMYITSL 227
Cdd:cd21255    84 LLPIPDKLIVMTYLCQL 100
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
129-231 3.97e-16

calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409110  Cd Length: 107  Bit Score: 76.54  E-value: 3.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  129 EKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVvcqqSATQR---LEHAFNIARYQLGIEKLL 205
Cdd:cd21261     3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSL----SPSNRkhnFELAFSMAEKLANCDRLI 78
                          90       100
                  ....*....|....*....|....*...
gi 578837832  206 DPED--VDTTYPDKKSILMYITSLFQVL 231
Cdd:cd21261    79 EVEDmmVMGRKPDPMCVFTYVQSLYNHL 106
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
6-112 1.68e-15

first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409157  Cd Length: 129  Bit Score: 75.89  E-value: 1.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    6 EDVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK---EKGSTRVHALNNVNKALRVLQNNNVD 82
Cdd:cd21308    18 KKIQQNTFTRWCNEHLKCVSKR-IANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIK 96
                          90       100       110
                  ....*....|....*....|....*....|
gi 578837832   83 LVNIGSTDIVDGNHKLTLGLIWNIILHWQV 112
Cdd:cd21308    97 LVSIDSKAIVDGNLKLILGLIWTLILHYSI 126
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
6-112 3.24e-15

first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409158  Cd Length: 131  Bit Score: 75.12  E-value: 3.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    6 EDVQKKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLPK---EKGSTRVHALNNVNKALRVLQNNNVD 82
Cdd:cd21309    15 KKIQQNTFTRWCNEHLKCVNKR-IGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIK 93
                          90       100       110
                  ....*....|....*....|....*....|
gi 578837832   83 LVNIGSTDIVDGNHKLTLGLIWNIILHWQV 112
Cdd:cd21309    94 LVSIDSKAIVDGNLKLILGLVWTLILHYSI 123
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
6-104 6.03e-15

first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409074  Cd Length: 111  Bit Score: 73.33  E-value: 6.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    6 EDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKE---KGSTRVHALNNVNKALRVLQNN-NV 81
Cdd:cd21225     2 EKVQIKAFTAWVNSVLEKRGIPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
                          90       100
                  ....*....|....*....|...
gi 578837832   82 DLVNIGSTDIVDGNHKLTLGLIW 104
Cdd:cd21225    82 RVQGIGAEDFVDNNKKLILGLLW 104
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
132-229 6.39e-15

calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409048  Cd Length: 112  Bit Score: 73.55  E-value: 6.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSAtQRLEHAFNIARYQlGIEKLLDPED-V 210
Cdd:cd21199    13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKR-RNFTLAFKAAESV-GIPTTLTIDEmV 90
                          90
                  ....*....|....*....
gi 578837832  211 DTTYPDKKSILMYITSLFQ 229
Cdd:cd21199    91 SMERPDWQSVMSYVTAIYK 109
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
10-108 6.79e-15

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 73.14  E-value: 6.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   10 KKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKE--KGSTRVHALNNVNKALRVLQNNNV-DLVNI 86
Cdd:cd00014     1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
                          90       100
                  ....*....|....*....|...
gi 578837832   87 GSTDIV-DGNHKLTLGLIWNIIL 108
Cdd:cd00014    81 EPEDLYeKGNLKKVLGTLWALAL 103
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
755-1930 9.24e-15

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 82.02  E-value: 9.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   755 VNAIEREKAEKFRKLQDASRSAQALVE-QMVNEGVNA-------DSIKQASEQLNSRWIEFCQLLSErLNWLeYQNNIIA 826
Cdd:TIGR01612  598 INKLKLELKEKIKNISDKNEYIKKAIDlKKIIENNNAyidelakISPYQVPEHLKNKDKIYSTIKSE-LSKI-YEDDIDA 675
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   827 FYNQLQ---------------QLEQMTTTAEN-WLKIQPTtpsEPTAIKSQLKICKDEVNRLSDLQPQIERL-------- 882
Cdd:TIGR01612  676 LYNELSsivkenaidntedkaKLDDLKSKIDKeYDKIQNM---ETATVELHLSNIENKKNELLDIIVEIKKHihgeinkd 752
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   883 ---KIQSIALKEKGQGPMFLD-ADFVAFTNHFKQVFSDVQAR---EKELQTIFDTLPPMRYQETMSAIRTW-VQQSETKL 954
Cdd:TIGR01612  753 lnkILEDFKNKEKELSNKINDyAKEKDELNKYKSKISEIKNHyndQINIDNIKDEDAKQNYDKSKEYIKTIsIKEDEIFK 832
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   955 SIPQLSVTDYEIMeQRLGELQALQSSLQEQQSGLYylsTTVKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQK 1034
Cdd:TIGR01612  833 IINEMKFMKDDFL-NKVDKFINFENNCKEKIDSEH---EQFAELTNKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEE 908
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1035 LEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEwpalgdsEILKKQLKQcrllvsDIQTIQPSlnsvneggqkikNEAEPE 1114
Cdd:TIGR01612  909 EYQNINTLKKVDEYIKICENTKESIEKFHNKQ-------NILKEILNK------NIDTIKES------------NLIEKS 963
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1115 FASRLETELKELNTQWDHMCQQVyarkeALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFeyktpDELQKAVEEMKR 1194
Cdd:TIGR01612  964 YKDKFDNTLIDKINELDKAFKDA-----SLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQF-----DEKEKATNDIEQ 1033
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1195 AKEEAQQKEAKVKL--------LTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNgkcktleevwacWHELLSY 1266
Cdd:TIGR01612 1034 KIEDANKNIPNIEIaihtsiynIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLK------------HYNFDDF 1101
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1267 LEKAN-KWLNEVEfklKTTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDggVMDELINEEletfnsrwre 1345
Cdd:TIGR01612 1102 GKEENiKYADEIN---KIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLED--VADKAISND---------- 1166
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1346 lheeavrrqklleqsiqSAQETEKSlhlIQESLTFIDKQlaAYIADKVDaaQMPQEAQKIQSDLTSheisLEEMKKHNQ- 1424
Cdd:TIGR01612 1167 -----------------DPEEIEKK---IENIVTKIDKK--KNIYDEIK--KLLNEIAEIEKDKTS----LEEVKGINLs 1218
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1425 -GKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPanfeqrlqeskmiLDEVKMHLPALETKSVEQEVVQSQLNhcvNLYKS 1503
Cdd:TIGR01612 1219 yGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIED-------------LDEIKEKSPEIENEMGIEMDIKAEME---TFNIS 1282
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1504 LSEVKSevemviktgRQIVQKKQTENPKELDERvtALKL-HYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAat 1582
Cdd:TIGR01612 1283 HDDDKD---------HHIISKKHDENISDIREK--SLKIiEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIA-- 1349
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1583 dmeltkrsavegmpsNLDSEVAWGKaTQKEIEKQKVHLKSITEVGEALKTVLGKKETLVedKLSLLNSNWIAVTSRAEEW 1662
Cdd:TIGR01612 1350 ---------------NIYNILKLNK-IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLI--KKIKDDINLEECKSKIEST 1411
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1663 LNllleyQKHMETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKaelndirpKVDSTRDQAANLMANRGDHCR 1742
Cdd:TIGR01612 1412 LD-----DKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFK--------NIEMADNKSQHILKIKKDNAT 1478
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1743 KLVEPQISELNHRFAAiSHRIKT-----GKASIPLKEL-EQFNSDIQKLLEPL-EAEIQQGVNLKEEDFNKDMNEDNEGT 1815
Cdd:TIGR01612 1479 NDHDFNINELKEHIDK-SKGCKDeadknAKAIEKNKELfEQYKKDVTELLNKYsALAIKNKFAKTKKDSEIIIKEIKDAH 1557
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1816 VKELLQRGDNLQQriTDERKREEIKIKQQLLQT-KHN-ALKDLRSQRR---KKALEISHqwyqYKRQADDLLKCLDDIEK 1890
Cdd:TIGR01612 1558 KKFILEAEKSEQK--IKEIKKEKFRIEDDAAKNdKSNkAAIDIQLSLEnfeNKFLKISD----IKKKINDCLKETESIEK 1631
                         1210      1220      1230      1240
                   ....*....|....*....|....*....|....*....|
gi 578837832  1891 KLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSE 1930
Cdd:TIGR01612 1632 KISSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIED 1671
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
3300-3343 2.36e-14

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: 2.36e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 578837832   3300 KHQAKCNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHK 3343
Cdd:smart00291    2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
446-652 3.01e-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: 74.79  E-value: 3.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  446 NQKLKELNDWLTKTEErtrKMEEEPLGPDLEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVDESsGDHATAALEEQL 525
Cdd:cd00176     6 LRDADELEAWLSEKEE---LLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  526 KVLGDRWANICRWTEDRWVLLQDiLLKWQRLTEEQCLFSAWLSEKEDAVNKIHTTgfKDQNEMLSSLQKLAVLKADLEKK 605
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEE-ALDLQQFFRDADDLEQWLEEKEAALASEDLG--KDLESVEELLKKHKELEEELEAH 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578837832  606 KQSMGKLYSLKQDLLStLKNKSVTQKTEAWLDNFARCWDNLVQKLEK 652
Cdd:cd00176   159 EPRLKSLNELAEELLE-EGHPDADEEIEEKLEELNERWEELLELAEE 204
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2115-2810 4.15e-14

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: 79.33  E-value: 4.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2115 AEQFLRKTQIPENWEHAKYKWYLKELQDGIGQRQtvvRTLNATGEEIiqQSSKTDASILQEKLGSLNLRWQEVCKQLSDR 2194
Cdd:TIGR02168  212 AERYKELKAELRELELALLVLRLEELREELEELQ---EELKEAEEEL--EELTAELQELEEKLEELRLEVSELEEEIEEL 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2195 KKRLEEQKNILSEFQRDLNEFVLWLEEADNI-----ASIPLEPGKEQQLKEKLEQVKLLVEEL-PLRQGILKQLNEtggp 2268
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLERQleeleAQLEELESKLDELAEELAELEEKLEELkEELESLEAELEE---- 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2269 vlvsapiSPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ 2348
Cdd:TIGR02168  363 -------LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2349 PNQEGPFDVKETEIA-VQAKQPDVEEILSKGQHLYKEKP-ATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLApGLTTI 2426
Cdd:TIGR02168  436 KELQAELEELEEELEeLQEELERLEEALEELREELEEAEqALDAAERELAQLQARLDSLERLQENLEGFSEGVK-ALLKN 514
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2427 GASPTQTVTLVTQPVVTK---ETAISKLEMPSSLMLEVPALADFNRA-----WTELTDWLSLLDQVIKSQRVMVGDLEDI 2498
Cdd:TIGR02168  515 QSGLSGILGVLSELISVDegyEAAIEAALGGRLQAVVVENLNAAKKAiaflkQNELGRVTFLPLDSIKGTEIQGNDREIL 594
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2499 NEmIIKQKATMQDLEQRRPQLEELI-------------TAAQNLKNKTsNQEARTIITD--------------------- 2544
Cdd:TIGR02168  595 KN-IEGFLGVAKDLVKFDPKLRKALsyllggvlvvddlDNALELAKKL-RPGYRIVTLDgdlvrpggvitggsaktnssi 672
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2545 -----RIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLA 2619
Cdd:TIGR02168  673 lerrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2620 KDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENINA---SWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAW 2696
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERR 832
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2697 LTEAETTANVLQDatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDvyHNLDENSQKILRSLEGSDDAVLLQRRLDNMNF 2776
Cdd:TIGR02168  833 IAATERRLEDLEE--QIEELSEDIESLAAEIEELEELIEELESELE--ALLNERASLEEALALLRSELEELSEELRELES 908
                          730       740       750
                   ....*....|....*....|....*....|....
gi 578837832  2777 KWSELRKKSLNIRSHLEASSDQWKRLHLSLQELL 2810
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1118-1928 1.22e-13

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: 77.79  E-value: 1.22e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1118 RLETELKELNTQWDHMCQQVYARKE--ALKGGLEktvSLQKDLSEMHewMTQAEEEYLERDFEYKtpdelqKAVEEMKRA 1195
Cdd:TIGR02168  190 RLEDILNELERQLKSLERQAEKAERykELKAELR---ELELALLVLR--LEELREELEELQEELK------EAEEELEEL 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1196 KEEAQQKEAKVKLLTESVNSV-----IAQAppvAQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKA 1270
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELeeeieELQK---ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1271 NKWLNEVEFKLkttenipggaEEISEVLDSLENLMRHSEDnpnqirilaqtltdggvmdelINEELETFNSRWRELHEEA 1350
Cdd:TIGR02168  336 AEELAELEEKL----------EELKEELESLEAELEELEA---------------------ELEELESRLEELEEQLETL 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1351 VRRQKLLEQSIQSAQETeksLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQK--IQSDLTSHEISLEEMKKHNQGKEA 1428
Cdd:TIGR02168  385 RSKVAQLELQIASLNNE---IERLEARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEE 461
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1429 AQRVLS-QIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEvkmhlpalETKSVEQEvvQSQLNHCVNLYKSLSEV 1507
Cdd:TIGR02168  462 ALEELReELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE--------GVKALLKN--QSGLSGILGVLSELISV 531
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1508 KSEVEMVIktgrqivqkkqtenpkelderVTALKLHyneLGAKVTERKQQLEKC---LKLSRKMRKEMNVLTEW----LA 1580
Cdd:TIGR02168  532 DEGYEAAI---------------------EAALGGR---LQAVVVENLNAAKKAiafLKQNELGRVTFLPLDSIkgteIQ 587
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1581 ATDMELTKRsaVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGEAL--KTVLGKKETLVEDKLSLLNSNWIaVTSR 1658
Cdd:TIGR02168  588 GNDREILKN--IEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALelAKKLRPGYRIVTLDGDLVRPGGV-ITGG 664
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1659 AEEWLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDESEKKKpQQKEDVLKRLKAELNDIRPKVDSTRDQAANL----- 1733
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL-EELEEELEQLRKELEELSRQISALRKDLARLeaeve 743
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1734 ----MANRGDHCRKLVEPQISELNHRFAAISHRIKTGKAsiplkELEQFNSDIQKLLEPLEAEIQQGVNLKEEdfnkdmn 1809
Cdd:TIGR02168  744 qleeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEA-----EIEELEAQIEQLKEELKALREALDELRAE------- 811
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1810 ednegtVKELLQRGDNLQQRITDERKReeIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQY---KRQADDLLKCLD 1886
Cdd:TIGR02168  812 ------LTLLNEEAANLRERLESLERR--IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeelESELEALLNERA 883
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|.
gi 578837832  1887 DIEKKLASLPEPRD---------ERKIKEIDRELQKKKEELNAVRRQAEGL 1928
Cdd:TIGR02168  884 SLEEALALLRSELEelseelrelESKRSELRRELEELREKLAQLELRLEGL 934
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2576-2795 1.92e-13

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: 72.09  E-value: 1.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2576 QWLEAKEEAEQVLGQARAKLESWkEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDYSaDDTRKVHMIT 2655
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2656 ENINASWRSIHKRVSEREAALEETHRLLQQFpLDLEKFLAWLTEAETTANvlqdatrKERLLEDSKGVKELMKQWQDLQG 2735
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALA-------SEDLGKDLESVEELLKKHKELEE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2736 EIEAHTDVYHNLDENSQKiLRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEAS 2795
Cdd:cd00176   154 ELEAHEPRLKSLNELAEE-LLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
132-229 4.02e-13

calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409106  Cd Length: 112  Bit Score: 68.52  E-value: 4.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSAtQRLEHAFNIARyQLGIEKLLDPED-V 210
Cdd:cd21257    13 LLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKK-RNLLLAFQAAE-SVGIKPSLELSEmM 90
                          90
                  ....*....|....*....
gi 578837832  211 DTTYPDKKSILMYITSLFQ 229
Cdd:cd21257    91 YTDRPDWQSVMQYVAQIYK 109
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
2-109 1.09e-12

third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409068  Cd Length: 113  Bit Score: 66.92  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    2 EDEREdvqKKTFTKWVNaqfSKFGKQHIENLFSDLQDGRRLLDLLEGL-----TGQKLPKEKGSTRVHALNNVNKALRVL 76
Cdd:cd21219     1 EGSRE---ERAFRMWLN---SLGLDPLINNLYEDLRDGLVLLQVLDKIqpgcvNWKKVNKPKPLNKFKKVENCNYAVDLA 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 578837832   77 QNNNVDLVNIGSTDIVDGNHKLTLGLIWNIILH 109
Cdd:cd21219    75 KKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
719-925 1.22e-12

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 69.78  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  719 DITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQmvnEGVNADSIKQASE 798
Cdd:cd00176     8 DADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE---GHPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  799 QLNSRWIEFCQLLSERLNWLEYQNNIIAFYNQLQQLEQMTTTAENWLKIQPTTPSePTAIKSQLKICKDEVNRLSDLQPQ 878
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPR 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578837832  879 IERLKIQSIALKEKGQ--GPMFLDADFVAFTNHFKQVFSDVQAREKELQ 925
Cdd:cd00176   162 LKSLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2003-2200 3.66e-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: 68.63  E-value: 3.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2003 LLEVEQLLNAPDLcAKDFEDLFKQEESLKNIKDSLQQSSGRIDIIHsKKTAALQSATPVERVKLQEALSQLDFQWEKVNK 2082
Cdd:cd00176    16 LSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALN-ELGEQLIEEGHPDAEEIQERLEELNQRWEELRE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2083 MYKDRQGRFDRSVEKWRRFHyDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKW-YLKELQDGIGQRQTVVRTLNATGEEI 2161
Cdd:cd00176    94 LAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLESVEELLkKHKELEEELEAHEPRLKSLNELAEEL 172
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 578837832 2162 IQQSSKTDASILQEKLGSLNLRWQEVCKQLSDRKKRLEE 2200
Cdd:cd00176   173 LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
128-225 4.80e-12

second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409078  Cd Length: 105  Bit Score: 65.10  E-value: 4.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  128 SEKILLSWVRQSTrnyPQVNVINFTTSWSDGLALNALIHSHRPDLF-DWNSVvcqqSATQRLEH---AFNIARYQLGIEK 203
Cdd:cd21229     4 PKKLMLAWLQAVL---PELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKL----DPSNSLENcrrAMDLAKREFNIPM 76
                          90       100
                  ....*....|....*....|..
gi 578837832  204 LLDPEDVDTTYPDKKSILMYIT 225
Cdd:cd21229    77 VLSPEDLSSPHLDELSGMTYLS 98
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1040-1144 5.03e-12

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: 65.03  E-value: 5.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1040 NKLRKIQNHIQTLKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEaEPEFASRL 1119
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYG-KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEI 78
                           90       100
                   ....*....|....*....|....*
gi 578837832  1120 ETELKELNTQWDHMCQQVYARKEAL 1144
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKL 103
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
132-229 8.19e-12

calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409105  Cd Length: 119  Bit Score: 64.71  E-value: 8.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVcQQSATQRLEHAFNIARyQLGIEKLLDPED-V 210
Cdd:cd21256    19 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELN-SQDKRRNFTLAFQAAE-SVGIKSTLDINEmV 96
                          90
                  ....*....|....*....
gi 578837832  211 DTTYPDKKSILMYITSLFQ 229
Cdd:cd21256    97 RTERPDWQSVMTYVTAIYK 115
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2798-3034 8.91e-12

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 67.47  E-value: 8.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2798 QWKRLHLSLQELLVWLQLKDDELSRQAPiGGDFPAVQKQNDVHRAFKRELKTKEPVImstletvriflteqplEGLEKLY 2877
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERV----------------EALNELG 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2878 QEPRELPPEERAQnvtrlLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEAtDELDLKLRQAEVIKGSWQPVGD 2957
Cdd:cd00176    64 EQLIEEGHPDAEE-----IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGKD 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578837832 2958 LliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNL-STLEDLNTRWKLLQVAVEDRVRQLHEAH 3034
Cdd:cd00176   138 L--ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIeEKLEELNERWEELLELAEERQKKLEEAL 213
EFh_DYTN cd16243
EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate ...
3146-3278 1.23e-11

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: 65.49  E-value: 1.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3146 LTTIYDRLEQEHNNLVNVPLCvDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFK----QVASSTGFC 3221
Cdd:cd16243    31 LERLFQSASQEVPGQVSAEAT-EQTCRLLFRLYDREQTGFVSLRSVEAALIALSGDTLSAKYRALFQlyesGQGGSSGSI 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837832 3222 DQRRLGLLLHDSIQIPRQLGEVASFGgsNIEPSVRSCFQFANNkPEIEAALFLDWMR 3278
Cdd:cd16243   110 TRSGLRVLLQDLSQIPAVVQESHVFG--NVETAVRSCFSGVLT-ASISEEHFLSWLQ 163
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2926-3032 1.41e-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: 63.49  E-value: 1.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2926 ERLRELQEATDELDLKLRQAEVIKgSWQPVGDLLiDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYN 3005
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALL-SSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 578837832  3006 LSTLEDLNTRWKLLQVAVEDRVRQLHE 3032
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
441-548 2.04e-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: 63.11  E-value: 2.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   441 LMDLQNQKLKELNDWLTKTEErtrKMEEEPLGPDLEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVdESSGDHATAA 520
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEA---LLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKL-IDEGHYASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 578837832   521 LEEQLKVLGDRWANICRWTEDRWVLLQD 548
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
935-1144 2.59e-11

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 65.93  E-value: 2.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  935 RYQETMSAIRTWVQQSETKLSIPQLSVTDYEIMEQRLgELQALQSSLQEQQSGLYYLSTTVKEMSKKAPSEiSRKYQSEF 1014
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLK-KHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1015 EEIEGRWKKLSSQLVEHCQKLEEQMNKLRKIQNHIQtLKKWMAEVDVFLKEEWPaLGDSEILKKQLKQCRLLVSDIQTIQ 1094
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578837832 1095 PSLNSVNEGGQKIKNEAEPEFASRLETELKELNTQWDHMCQQVYARKEAL 1144
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
332-439 2.79e-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: 62.72  E-value: 2.79e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   332 NLDRYQTALEEVLSWLLSAEDTLQAQgEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIGTGKlseDEETE 411
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH---YASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 578837832   412 VQEQMNLLNSRWECLRVASMEKQSNLHR 439
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
2099-2199 4.15e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 62.35  E-value: 4.15e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   2099 RRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKW-YLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtDASILQEKL 2177
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLkKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 578837832   2178 GSLNLRWQEVCKQLSDRKKRLE 2199
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1154-1361 5.58e-11

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 65.16  E-value: 5.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1154 LQKDLSEMHEWMTQAEEEYLERDFEyKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPVAQEaLKKELE 1233
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE-IQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1234 TLTTNYQWLCTRLNGKCKTLEEVWAcWHELLSYLEKANKWLNEVEFKLKTTEnIPGGAEEISEVLDSLENLMRH---SED 1310
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAALASED-LGKDLESVEELLKKHKELEEEleaHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578837832 1311 NPNQIRILAQTLTDGGV--MDELINEELETFNSRWRELHEEAVRRQKLLEQSI 1361
Cdd:cd00176   161 RLKSLNELAEELLEEGHpdADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
132-225 6.00e-11

second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409079  Cd Length: 103  Bit Score: 61.63  E-value: 6.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTrnyPQVNVINFTTSWSDGLALNALIHSHRPDLF----DWNSVVCQQSATQrlehAFNIARYQLGIEKLLDP 207
Cdd:cd21230     6 LLGWIQNKI---PQLPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDALENATE----AMQLAEDWLGVPQLITP 78
                          90
                  ....*....|....*...
gi 578837832  208 EDVDTTYPDKKSILMYIT 225
Cdd:cd21230    79 EEIINPNVDEMSVMTYLS 96
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
129-227 7.37e-11

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 61.59  E-value: 7.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  129 EKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDW--NSVVCQQSATQRLEHAFNIAR-YQLGIEKLL 205
Cdd:cd00014     1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKinKKPKSPFKKRENINLFLNACKkLGLPELDLF 80
                          90       100
                  ....*....|....*....|..
gi 578837832  206 DPEDVDTTyPDKKSILMYITSL 227
Cdd:cd00014    81 EPEDLYEK-GNLKKVLGTLWAL 101
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
2-104 1.04e-10

third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409149  Cd Length: 119  Bit Score: 61.67  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    2 EDEREdvqKKTFTKWVNaqfSKFGKQHIENLFSDLQDGRRLLDLLEGLTG--------QKLPKEKGSTRVHALNNVNKAL 73
Cdd:cd21300     4 EGERE---ARVFTLWLN---SLDVEPAVNDLFEDLRDGLILLQAYDKVIPgsvnwkkvNKAPASAEISRFKAVENTNYAV 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832   74 RVLQNNNVDLVNIGSTDIVDGNHKLTLGLIW 104
Cdd:cd21300    78 ELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2927-3037 1.34e-10

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 64.00  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2927 RLRELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNL 3006
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832 3007 STLEDLNTRWKLLQVAVEDRVRQLHEAHRDF 3037
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQ 109
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
28-107 1.64e-10

first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409072  Cd Length: 113  Bit Score: 60.68  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   28 HIENLFSDLQDGRRLLDLLEGLTGQKLPKEKgsTRVHALN------NVNKALRVLQNNNV----DLVNIGSTDIVDGNHK 97
Cdd:cd21223    25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSK--LRVPAISrlqklhNVEVALKALKEAGVlrggDGGGITAKDIVDGHRE 102
                          90
                  ....*....|
gi 578837832   98 LTLGLIWNII 107
Cdd:cd21223   103 KTLALLWRII 112
SPEC smart00150
Spectrin repeats;
335-437 2.49e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.04  E-value: 2.49e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    335 RYQTALEEVLSWLLSAEDTLQAQgEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEVQE 414
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI---EEGHPDAEEIEE 77
                            90       100
                    ....*....|....*....|...
gi 578837832    415 QMNLLNSRWECLRVASMEKQSNL 437
Cdd:smart00150   78 RLEELNERWEELKELAEERRQKL 100
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2096-2200 2.88e-10

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: 60.02  E-value: 2.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2096 EKWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEH--AKYKWYlKELQDGIGQRQTVVRTLNATGEEIIQqSSKTDASIL 2173
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESvqALLKKH-KALEAELAAHQDRVEALNELAEKLID-EGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 578837832  2174 QEKLGSLNLRWQEVCKQLSDRKKRLEE 2200
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
2467-2568 2.94e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 59.65  E-value: 2.94e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   2467 FNRAWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIITDRI 2546
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 578837832   2547 ERIQNQWDEVQEHLQNRRQQLN 2568
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
9-103 3.78e-10

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409062  Cd Length: 107  Bit Score: 59.62  E-value: 3.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    9 QKKTFTKWVNAQFSKF-GKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHAL--NNVNKALRVLQNNNVDLVN 85
Cdd:cd21213     1 QLQAYVAWVNSQLKKRpGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAErkENVEKVLQFMASKRIRMHQ 80
                          90
                  ....*....|....*...
gi 578837832   86 IGSTDIVDGNHKLTLGLI 103
Cdd:cd21213    81 TSAKDIVDGNLKAIMRLI 98
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
2-104 4.80e-10

third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409147  Cd Length: 117  Bit Score: 59.56  E-value: 4.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    2 EDEREDvqkKTFTKWVNaqfSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQ--------KLPKEKGSTrVHALNNVNKAL 73
Cdd:cd21298     3 EETREE---KTYRNWMN---SLGVNPFVNHLYSDLRDGLVLLQLYDKIKPGvvdwsrvnKPFKKLGAN-MKKIENCNYAV 75
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832   74 RVLQNNNVDLVNIGSTDIVDGNHKLTLGLIW 104
Cdd:cd21298    76 ELGKKLKFSLVGIGGKDIYDGNRTLTLALVW 106
EFh_DTNB cd16250
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ...
3152-3277 7.52e-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: 60.42  E-value: 7.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3152 RLEQEHNnlVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLH 3231
Cdd:cd16250    42 RLPSTHQ--ISVEQSISLLLNFMIAAYDSEGHGKLTVFSVKAMLATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLR 119
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 578837832 3232 DSIQIPRQLGEVASFGGSniEPSVRSCFQfanNKPEIEAALFLDWM 3277
Cdd:cd16250   120 EVLKLPTAVFEGPSFGYT--EHSVRTCFP---QQKKIMLNMFLDTM 160
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
3146-3259 8.87e-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: 60.30  E-value: 8.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 3146 LTTIYDRLEQE--HNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQ 3223
Cdd:cd16249    32 LSTIFYQLNKRmpTTHQINVEQSISLLLNFLLAAFDPEGHGKISVFAVKMALATLCGGKIMDKLRYIFSMISDSNGVMVY 111
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 578837832 3224 RRLGLLLHDSIQIPRQLGEVASFGGSniEPSVRSCF 3259
Cdd:cd16249   112 GRYDQFLREVLKLPTAVFEGPSFGYT--EQSARSCF 145
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1772-1960 1.09e-09

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 61.31  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1772 LKELEQFNSDIQKLLEPLEAEIQQgvnLKEEDFNKDMNEdNEGTVKELLQRGDNLQQRitDERKREEIKIKQQLLQTKHN 1851
Cdd:cd00176    16 LSEKEELLSSTDYGDDLESVEALL---KKHEALEAELAA-HEERVEALNELGEQLIEE--GHPDAEEIQERLEELNQRWE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1852 ALKDLrSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQ 1924
Cdd:cd00176    90 ELREL-AEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLesveellKKHKELEEELEAHEPRLKSLNEL 168
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 578837832 1925 AEGLSEDG---AAMAVEPTQIQLSKRWREIESKFAQFRR 1960
Cdd:cd00176   169 AEELLEEGhpdADEEIEEKLEELNERWEELLELAEERQK 207
SPEC smart00150
Spectrin repeats;
446-547 1.55e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 57.72  E-value: 1.55e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    446 NQKLKELNDWLTKTEertRKMEEEPLGPDLEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVDEsSGDHATAALEEQL 525
Cdd:smart00150    4 LRDADELEAWLEEKE---QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE-EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 578837832    526 KVLGDRWANICRWTEDRWVLLQ 547
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
132-210 1.59e-09

calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409045  Cd Length: 106  Bit Score: 57.75  E-value: 1.59e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578837832  132 LLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDwNSVVCQQSATQRLEHAFNIARYQLGIEKLLDPEDV 210
Cdd:cd21196     8 LLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLE-PSELQGLGALEATAWALKVAENELGITPVVSAQAV 85
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2562-2678 2.57e-09

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: 57.33  E-value: 2.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2562 NRRQQLNEMLKDSTQWLEakeEAEQVLgqarakleSWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLr 2641
Cdd:pfam00435    1 LLLQQFFRDADDLESWIE---EKEALL--------SSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI- 68
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 578837832  2642 DYSADDTRKVHMITENINASWRSIHKRVSEREAALEE 2678
Cdd:pfam00435   69 DEGHYASEEIQERLEELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1260-1466 4.09e-09

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 59.38  E-value: 4.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1260 WHELLSYLEKANKWLNEVEFKLKTTENI--PGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDGGVMD-ELINEEL 1336
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGddLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDaEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1337 ETFNSRWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQK-IQSDLTSHEIS 1415
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKeLEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578837832 1416 LEEMKKhnQGKE-AAQRVLSQIDVAQKKLQDVSMKFRLFQKPA-NFEQRLQES 1466
Cdd:cd00176   162 LKSLNE--LAEElLEEGHPDADEEIEEKLEELNERWEELLELAeERQKKLEEA 212
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2205-2310 4.14e-09

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: 56.56  E-value: 4.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2205 LSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSapiSPEEQDKLE 2284
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE---GHYASEEIQ 79
                           90       100
                   ....*....|....*....|....*.
gi 578837832  2285 NKLKQTNLQWIKVSRALPEKQGEIEA 2310
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1154-1255 5.03e-09

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: 56.17  E-value: 5.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1154 LQKDLSEMHEWMTQAEEEYLERDFEyKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIaQAPPVAQEALKKELE 1233
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSEDYG-KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI-DEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|..
gi 578837832  1234 TLTTNYQWLCTRLNGKCKTLEE 1255
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLEE 105
PTZ00121 PTZ00121
MAEBL; Provisional
1349-1956 5.35e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.85  E-value: 5.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1349 EAVRRQKLLEQSIQSAQETEKsLHLIQESLTFIDKQLAAYI----ADKVDAAQMPQEAQKIQSDLTSHEI-SLEEMKKHN 1423
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEE-ERNNEEIRKFEEARMAHFArrqaAIKAEEARKADELKKAEEKKKADEAkKAEEKKKAD 1305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1424 QGKEAAQRVlSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKM-HLPALETKSVEQEVVQSQLNhcvnlyK 1502
Cdd:PTZ00121 1306 EAKKKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAdEAEAAEEKAEAAEKKKEEAK------K 1378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1503 SLSEVKSEVEMVIKTGRqiVQKKQTENPKELDE--RVTALKLHYNELGAKvTERKQQLEKCLKLSRKMRKEMNVLTEWLA 1580
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADE--AKKKAEEDKKKADElkKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1581 ATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEvgEALKTVLGKKETLVEDKlsllnsnwiAVTSRAE 1660
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD--EAKKAAEAKKKADEAKK---------AEEAKKA 1524
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1661 EWLNLLLEYQKHMETfdQNVDHITKwiiqADTLLDESEKKKPQQKEDVLKRLKAElnDIRPKVDSTRDQAANLMANRGDH 1740
Cdd:PTZ00121 1525 DEAKKAEEAKKADEA--KKAEEKKK----ADELKKAEELKKAEEKKKAEEAKKAE--EDKNMALRKAEEAKKAEEARIEE 1596
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1741 CRKLVEPQISELNHRF-AAISHRIKTGKasipLKELEQFNSDIQKLLEPLEAEIQQGVNL-KEEDFNKDMNEDNEGTVKE 1818
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAkKAEEAKIKAEE----LKKAEEEKKKVEQLKKKEAEEKKKAEELkKAEEENKIKAAEEAKKAEE 1672
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1819 LLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEP 1898
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837832 1899 RDER-KIKEIDRELQKKKEElnaVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFA 1956
Cdd:PTZ00121 1753 EEEKkKIAHLKKEEEKKAEE---IRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFA 1808
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
3051-3080 7.94e-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: 53.30  E-value: 7.94e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 578837832 3051 GPWERAISPNKVPYYINHETQTTCWDHPKM 3080
Cdd:cd00201     2 PGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
4-107 8.29e-09

third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409180  Cd Length: 134  Bit Score: 56.55  E-value: 8.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    4 EREDVQKKTFTKWVNAQFSKfgkQHIENLFSDLQDGRRLLDLLEGL-------TGQKLPKEKGSTRVHALNNVNKALRVL 76
Cdd:cd21331    18 EGETREERTFRNWMNSLGVN---PHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVELG 94
                          90       100       110
                  ....*....|....*....|....*....|..
gi 578837832   77 QNN-NVDLVNIGSTDIVDGNHKLTLGLIWNII 107
Cdd:cd21331    95 KHPaKFSLVGIGGQDLNDGNPTLTLALVWQLM 126
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1013-1625 1.02e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.62  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1013 EFEEIEGRWKKLSS---QLVEHCQKLEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEWPALGDSEI----LKKQLKQCRL 1085
Cdd:PRK03918  201 ELEEVLREINEISSelpELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEErieeLKKEIEELEE 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1086 LVSDIQTIQPS------LNSVNEGGQKIKNEAEPEfASRLETELKELNTQWDHMCQQVyARKEALKGGLEKtvsLQKDLS 1159
Cdd:PRK03918  281 KVKELKELKEKaeeyikLSEFYEEYLDELREIEKR-LSRLEEEINGIEERIKELEEKE-ERLEELKKKLKE---LEKRLE 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1160 EMHEWMTQAEE--------EYLERDFEYKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQappvaqeaLKKE 1231
Cdd:PRK03918  356 ELEERHELYEEakakkeelERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE--------LKKA 427
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1232 LETLttnyqwlcTRLNGKCKT----LEEvwacwHELLSYLEKANKWLNEVEFKLKTTENIpggAEEISEVLDSLENLMRH 1307
Cdd:PRK03918  428 IEEL--------KKAKGKCPVcgreLTE-----EHRKELLEEYTAELKRIEKELKEIEEK---ERKLRKELRELEKVLKK 491
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1308 SEDNPNQIRILAQTLTDGGVMDELINEELETFNSRWRELHEEAVR---RQKLLEQSIQSAQETEKSLHLIQESLTFIDKQ 1384
Cdd:PRK03918  492 ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKlkgEIKSLKKELEKLEELKKKLAELEKKLDELEEE 571
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1385 LAAYIadkvdaAQMPQEAQKIQSDLTSHEISLEEM-KKHNQGKEAAQRVLSQIDVAQKKLQDVSMKFrlfqkpanfeQRL 1463
Cdd:PRK03918  572 LAELL------KELEELGFESVEELEERLKELEPFyNEYLELKDAEKELEREEKELKKLEEELDKAF----------EEL 635
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1464 QESKMILDEVKMHLPALETKSVEQEvvqsqlnhcvnlYKSLSEVKSEVEMVIKTGRqivqkkqtENPKELDERVTALKLH 1543
Cdd:PRK03918  636 AETEKRLEELRKELEELEKKYSEEE------------YEELREEYLELSRELAGLR--------AELEELEKRREEIKKT 695
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1544 YNELGAKVTERKQQLEKcLKLSRKMRKEMNVLTEWLAATDMELTKR--SAVEGMPSNLDSEVAWGKATQKEI--EKQKVH 1619
Cdd:PRK03918  696 LEKLKEELEEREKAKKE-LEKLEKALERVEELREKVKKYKALLKERalSKVGEIASEIFEELTEGKYSGVRVkaEENKVK 774

                  ....*.
gi 578837832 1620 LKSITE 1625
Cdd:PRK03918  775 LFVVYQ 780
SPEC smart00150
Spectrin repeats;
2684-2793 1.43e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 55.03  E-value: 1.43e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   2684 QQFPLDLEKFLAWLTEAETTAnvlqdatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRslEGSDD 2763
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL-------ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPD 71
                            90       100       110
                    ....*....|....*....|....*....|
gi 578837832   2764 AVLLQRRLDNMNFKWSELRKKSLNIRSHLE 2793
Cdd:smart00150   72 AEEIEERLEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1869-1971 2.76e-08

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: 54.25  E-value: 2.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1869 HQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVE--PTQIQLSK 1946
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEghYASEEIQE 80
                           90       100
                   ....*....|....*....|....*
gi 578837832  1947 RWREIESKFAQFRRLNFAQIHTVRE 1971
Cdd:pfam00435   81 RLEELNERWEQLLELAAERKQKLEE 105
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
3048-3080 2.99e-08

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: 51.83  E-value: 2.99e-08
                            10        20        30
                    ....*....|....*....|....*....|...
gi 578837832   3048 SVQGPWERAISPNKVPYYINHETQTTCWDHPKM 3080
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1342-1972 3.01e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 3.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1342 RWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKK 1421
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1422 HNQGKEAA-----QRVLSQIDVAQKKLQDVSMKFRLFQKP-ANFEQRLQESKMILDEVKMHLPALETK--SVEQEVVQSQ 1493
Cdd:TIGR02168  313 NLERQLEEleaqlEELESKLDELAEELAELEEKLEELKEElESLEAELEELEAELEELESRLEELEEQleTLRSKVAQLE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1494 L------NHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRK 1567
Cdd:TIGR02168  393 LqiaslnNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1568 MRKEMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGE----ALKTVLGKK------ 1637
Cdd:TIGR02168  473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEgyeaAIEAALGGRlqavvv 552
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1638 ----------ETLVEDKL-------------SLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVDHITKWIIQADTLL 1694
Cdd:TIGR02168  553 enlnaakkaiAFLKQNELgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLD 632
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1695 DESEKKKPQQKEDVLKRLKAELndIRPKVDST--RDQAANLMANRG---DHCRKLVEPQISELNhrfaaishriktgKAS 1769
Cdd:TIGR02168  633 NALELAKKLRPGYRIVTLDGDL--VRPGGVITggSAKTNSSILERRreiEELEEKIEELEEKIA-------------ELE 697
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1770 IPLKELEQFNSDIQKLLEPLEA---EIQQGVNLKEEDFnkdmnEDNEGTVKELLQRGDNLQQRITD-ERKREEIKIKQQL 1845
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKeleELSRQISALRKDL-----ARLEAEVEQLEERIAQLSKELTElEAEIEELEERLEE 772
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1846 LQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLpeprdERKIKEIDRELQKKKEELNAVRRQA 1925
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL-----RERLESLERRIAATERRLEDLEEQI 847
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|
gi 578837832  1926 EGLSEDGAAMAVEPTQIQLSKrwREIESKFAQF---RRLNFAQIHTVREE 1972
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELI--EELESELEALlneRASLEEALALLRSE 895
SPEC smart00150
Spectrin repeats;
2929-3030 3.47e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.87  E-value: 3.47e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   2929 RELQEATDELDLKLRQAEVIKGSWQPVGDLliDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNLST 3008
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEER 78
                            90       100
                    ....*....|....*....|..
gi 578837832   3009 LEDLNTRWKLLQVAVEDRVRQL 3030
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
10-107 5.95e-08

first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 53.73  E-value: 5.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   10 KKTFTKWVNAQFSK--FGKQHI------ENLFSDLQDGRRLLDLLE----GLTG-QKLPKEKGSTRVHALNNVNKALRVL 76
Cdd:cd21217     3 KEAFVEHINSLLADdpDLKHLLpidpdgDDLFEALRDGVLLCKLINkivpGTIDeRKLNKKKPKNIFEATENLNLALNAA 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832   77 QNNNVDLVNIGSTDIVDGNHKLTLGLIWNII 107
Cdd:cd21217    83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
3052-3078 9.44e-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: 9.44e-08
                           10        20
                   ....*....|....*....|....*..
gi 578837832  3052 PWERAISPNKVPYYINHETQTTCWDHP 3078
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
2-109 1.11e-07

third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409148  Cd Length: 114  Bit Score: 52.89  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    2 EDEREDvqkKTFTKWVNaqfSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQ------------KLPKEKgstrvhaLNNV 69
Cdd:cd21299     1 ETSREE---RCFRLWIN---SLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGsvnwkhankppiKMPFKK-------VENC 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 578837832   70 NKALRVLQNNNVDLVNIGSTDIVDGNHKLTLGLIWNIILH 109
Cdd:cd21299    68 NQVVKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1139-1971 1.13e-07

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 58.44  E-value: 1.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1139 ARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQKAVEEMKRAKEEAQQK-EAKVKLLTESVNSVI 1217
Cdd:pfam02463  170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKlNEERIDLLQELLRDE 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1218 AQAPPVAQEALKKELETLTTNYQWLctRLNGKCKTLEEVWACWHELLsyLEKANKWLNEVEFKLKTTENIPGGAEEISEV 1297
Cdd:pfam02463  250 QEEIESSKQEIEKEEEKLAQVLKEN--KEEEKEKKLQEEELKLLAKE--EEELKSELLKLERRKVDDEEKLKESEKEKKK 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1298 LDSLENLMRHSEDNPNQIRILAQTLTdggvmdelINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQ-ETEKSLHLIQE 1376
Cdd:pfam02463  326 AEKELKKEKEEIEELEKELKELEIKR--------EAEEEEEEELEKLQEKLEQLEEELLAKKKLESERlSSAAKLKEEEL 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1377 SLTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKKHNQGKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKP 1456
Cdd:pfam02463  398 ELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET 477
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1457 ANFEQRLQESKMILDEVKMHLPALETKSVE---------QEVVQSQLNHCVNLYKSLSEVK--------------SEVEM 1513
Cdd:pfam02463  478 QLVKLQEQLELLLSRQKLEERSQKESKARSglkvllaliKDGVGGRIISAHGRLGDLGVAVenykvaistaviveVSATA 557
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1514 VIKTGRQIVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAVE 1593
Cdd:pfam02463  558 DEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKL 637
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1594 GMPSNLDSEVAWGKATQKEIEKQKVHLKSITEvgealktvLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHM 1673
Cdd:pfam02463  638 KESAKAKESGLRKGVSLEEGLAEKSEVKASLS--------ELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREK 709
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1674 ETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAA------NLMANRGDHCRKLVEP 1747
Cdd:pfam02463  710 EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSelslkeKELAEEREKTEKLKVE 789
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1748 QISELNHRFAAISHRIKTGKASIPLKELEQFNSDIQKLLEPLEAEIQQ-------GVNLKEEDFNKDMNEDNEGTVKELL 1820
Cdd:pfam02463  790 EEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEElalelkeEQKLEKLAEEELERLEEEITKEELL 869
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1821 QRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKklaSLPEPRD 1900
Cdd:pfam02463  870 QELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEE---LLLEEAD 946
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578837832  1901 ERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNFAQIHTVRE 1971
Cdd:pfam02463  947 EKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1671-1768 1.21e-07

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: 52.32  E-value: 1.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1671 KHMETFDQNVDHITKWIIQADTLLDESEKKK----PQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANrGDHCRKLVE 1746
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKdlesVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQ 79
                           90       100
                   ....*....|....*....|..
gi 578837832  1747 PQISELNHRFAAISHRIKTGKA 1768
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQ 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1563-1668 1.57e-07

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: 51.94  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1563 KLSRKMRKEMNVLTEWLAATDMELTKRSaVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGEALKTVLGKKETLVE 1642
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSED-YGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79
                           90       100
                   ....*....|....*....|....*.
gi 578837832  1643 DKLSLLNSNWIAVTSRAEEWLNLLLE 1668
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKLEE 105
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
914-1558 1.84e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.37  E-value: 1.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   914 FSDVQAREKELQTIFDTLPPMRYQETMSAIRTWVQQSETKLSI--PQLSVTDYEIMEQRLgELQALQSSLQEQQSGLYYL 991
Cdd:TIGR02168  215 YKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEEltAELQELEEKLEELRL-EVSELEEEIEELQKELYAL 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   992 STTVKEMSKKApseisRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEWPALG 1071
Cdd:TIGR02168  294 ANEISRLEQQK-----QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1072 DSEILKKQL---------------KQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEFASRLETELKELNTQWDhmcqq 1136
Cdd:TIGR02168  369 ELESRLEELeeqletlrskvaqleLQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE----- 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1137 vyARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQKAVEEMKRAKEEAQQKEAKVKL-------- 1208
Cdd:TIGR02168  444 --ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKnqsglsgi 521
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1209 ---------------------LTESVNSVI---AQAPPVAQEALKKELETLTTNY---QWLCTRLNGK----CKTLEEVW 1257
Cdd:TIGR02168  522 lgvlselisvdegyeaaieaaLGGRLQAVVvenLNAAKKAIAFLKQNELGRVTFLpldSIKGTEIQGNdreiLKNIEGFL 601
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1258 ACWHELLSYLEKANKWLN----------------EVEFKLKTTENI---------------PGGAEEISEVLD---SLEN 1303
Cdd:TIGR02168  602 GVAKDLVKFDPKLRKALSyllggvlvvddldnalELAKKLRPGYRIvtldgdlvrpggvitGGSAKTNSSILErrrEIEE 681
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1304 LMRHSEDNPNQIRILAQTLTDGGVMDELINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDK 1383
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1384 QLAAYIADKVDAAQMPQEA-QKIQSDLTSHEISLEEMKKHNQGKEAAQRVLS--QIDVAQKKLQDVSMKFRLFQKPANFE 1460
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAeAEIEELEAQIEQLKEELKALREALDELRAELTllNEEAANLRERLESLERRIAATERRLE 841
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1461 QRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHCVNLYKSLSE----VKSEVEMVIKTGRQIVQKKQ--TENPKELD 1534
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalalLRSELEELSEELRELESKRSelRRELEELR 921
                          730       740
                   ....*....|....*....|....
gi 578837832  1535 ERVTALKLHYNELGAKVTERKQQL 1558
Cdd:TIGR02168  922 EKLAQLELRLEGLEVRIDNLQERL 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
743-1488 2.41e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 2.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   743 RKEGNFSDLKEKVNAIER--EKAEKFRKLQDASRSAQ---------ALVEQM----VNEGVNADSIKQASEQLNSRWIEF 807
Cdd:TIGR02168  190 RLEDILNELERQLKSLERqaEKAERYKELKAELRELElallvlrleELREELeelqEELKEAEEELEELTAELQELEEKL 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   808 CQL------LSERLNwlEYQNNIIAFYNQLQQLEQMTTTAENWLKIQPTTPSEPTAIKSQLKICKDEVN-RLSDLQPQIE 880
Cdd:TIGR02168  270 EELrlevseLEEEIE--ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAeELAELEEKLE 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   881 RLKIQSIALKEKGQGpmfLDADFVAFTNHFKQVF-------SDVQAREKELQTIFDTLPPMRYQETMSAIRTWVQQSETK 953
Cdd:TIGR02168  348 ELKEELESLEAELEE---LEAELEELESRLEELEeqletlrSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   954 LSIPQLSVTDYEIMEQRLGELQALQSSLQEQQSGLYYLSTTVKEMSKKAPSEIsRKYQSEFEEIEGRWKKLSSQLVEH-- 1031
Cdd:TIGR02168  425 ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQENLeg 503
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1032 -CQKLEEQMNKLRKIQNHIQTL-------KKWMAEVDVFLKE---------EWPALGDSEILKKQLKQcRLLVSDIQTIQ 1094
Cdd:TIGR02168  504 fSEGVKALLKNQSGLSGILGVLselisvdEGYEAAIEAALGGrlqavvvenLNAAKKAIAFLKQNELG-RVTFLPLDSIK 582
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1095 PSLNSVNEGGQKIKNEAEPEFASRLETELKELNTQWDHMCQQVY--------ARKEALKGGLEKTVSLQKDLSEMHEWMT 1166
Cdd:TIGR02168  583 GTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvddldnaLELAKKLRPGYRIVTLDGDLVRPGGVIT 662
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1167 QAEEEY----LERDFEYKtpdELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPVAQE------ALKKELETLT 1236
Cdd:TIGR02168  663 GGSAKTnssiLERRREIE---ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqisALRKDLARLE 739
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1237 TNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKANKWLNEVEfklkttenipggaEEISEVLDSLENLMRHSEDNPNQIR 1316
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-------------AEIEELEAQIEQLKEELKALREALD 806
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1317 ILAQTLTDggvMDELINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAA 1396
Cdd:TIGR02168  807 ELRAELTL---LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1397 QMPQEAQKIQSDLTSHEISLEEMKKHNQGKEAaqrvlsQIDVAQKKLQDVSMKF-RLFQKPANFEQRLQES-KMILDEVK 1474
Cdd:TIGR02168  884 SLEEALALLRSELEELSEELRELESKRSELRR------ELEELREKLAQLELRLeGLEVRIDNLQERLSEEySLTLEEAE 957
                          810
                   ....*....|....
gi 578837832  1475 MHLPALETKSVEQE 1488
Cdd:TIGR02168  958 ALENKIEDDEEEAR 971
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
128-229 2.48e-07

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409067  Cd Length: 114  Bit Score: 51.92  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  128 SEKILLSWVrqstrNY-------PQVNVINFTTSWSDGLALNALIHSHRP---DLFDWNSVVCQQSATQRLEHAFNIARy 197
Cdd:cd21218    11 PEEILLRWV-----NYhlkkagpTKKRVTNFSSDLKDGEVYALLLHSLAPelcDKELVLEVLSEEDLEKRAEKVLQAAE- 84
                          90       100       110
                  ....*....|....*....|....*....|..
gi 578837832  198 QLGIEKLLDPEDVDTtyPDKKSILMYITSLFQ 229
Cdd:cd21218    85 KLGCKYFLTPEDIVS--GNPRLNLAFVATLFN 114
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
124-227 2.49e-07

second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409163  Cd Length: 115  Bit Score: 52.00  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  124 QQTNSEKiLLSWVRQSTrnyPQVNVINFTTSWSDGLALNALIHSHRPDLF-DWNSVVCQQsATQRLEHAFNIARYQLGIE 202
Cdd:cd21314     9 KQTPKQR-LLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQ-PVQNAREAMQQADDWLGVP 83
                          90       100
                  ....*....|....*....|....*
gi 578837832  203 KLLDPEDVDTTYPDKKSILMYITSL 227
Cdd:cd21314    84 QVIAPEEIVDPNVDEHSVMTYLSQF 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1459-1668 3.03e-07

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 53.99  E-value: 3.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1459 FEQRLQESKMILDEVKMHLPALETKSVEQEVvQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPkELDERVT 1538
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSSTDYGDDLESV-EALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1539 ALKLHYNELGAKVTERKQQLEKCLKLSRKMRkEMNVLTEWLAATDMELTKRSAVEGMPSnLDSEVAWGKATQKEIEKQKV 1618
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578837832 1619 HLKSITEVGEALKTVLGKKETL-VEDKLSLLNSNWIAVTSRAEEWLNLLLE 1668
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDADEeIEEKLEELNERWEELLELAEERQKKLEE 211
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2057-2898 3.31e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 56.61  E-value: 3.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2057 SATPVERVKLQEALSQLDFQWEKVNKMYKDrqgrFDRSVEKWRRFHYDIKIFNQWL----TEAEQFLRKTQIPENWEHAK 2132
Cdd:TIGR02169  149 SMSPVERRKIIDEIAGVAEFDRKKEKALEE----LEEVEENIERLDLIIDEKRQQLerlrREREKAERYQALLKEKREYE 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2133 YKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKTDAsiLQEKLGSLNLRWQEVCKQLSDR--------KKRLEEQKNI 2204
Cdd:TIGR02169  225 GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE--LEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAE 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2205 LSEFQRDLNEFVLWLEEADNiasiplepgKEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSapiSPEEQDKLE 2284
Cdd:TIGR02169  303 IASLERSIAEKERELEDAEE---------RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE---LKEELEDLR 370
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2285 NKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQPNQEGPFDVKETEIAV 2364
Cdd:TIGR02169  371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2365 QAKQPDVEEI---LSK-GQHLYKEKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVTLVTQP 2440
Cdd:TIGR02169  451 KKQEWKLEQLaadLSKyEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2441 VVTKETAISKLEMPSSLMLEVPALADFNRA-------------------WTELTDWLSLLDqvIKSQRVMVGDLEDINEM 2501
Cdd:TIGR02169  531 GSVGERYATAIEVAAGNRLNNVVVEDDAVAkeaiellkrrkagratflpLNKMRDERRDLS--ILSEDGVIGFAVDLVEF 608
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2502 ----------IIKQKATMQDLEQRRPQLEE--LITAAQNL------------------KNKTSNQEARTIITDRIERIQN 2551
Cdd:TIGR02169  609 dpkyepafkyVFGDTLVVEDIEAARRLMGKyrMVTLEGELfeksgamtggsraprggiLFSRSEPAELQRLRERLEGLKR 688
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2552 QWDEVQE---HLQNRRQQLNEMLKDSTQWLEAKE-EAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLAKDLR---Q 2624
Cdd:TIGR02169  689 ELSSLQSelrRIENRLDELSQELSDASRKIGEIEkEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEariE 768
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2625 WQTNVDVANDLALKLLRDysaddtRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQfpLDLEKFLAwltEAEtta 2704
Cdd:TIGR02169  769 ELEEDLHKLEEALNDLEA------RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR--LTLEKEYL---EKE--- 834
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2705 nvLQDATRKERLLEDSKgvKELMKQWQDLQGEIEAHTDVYhnldENSQKILRSLEGSddAVLLQRRLDNMNFKWSELRKK 2784
Cdd:TIGR02169  835 --IQELQEQRIDLKEQI--KSIEKEIENLNGKKEELEEEL----EELEAALRDLESR--LGDLKKERDELEAQLRELERK 904
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2785 SLNIRSHLEASSDQWKRLHLSLQELLVWLQLKDDELSRQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTL----ET 2860
Cdd:TIGR02169  905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIqeyeEV 984
                          890       900       910
                   ....*....|....*....|....*....|....*...
gi 578837832  2861 VRIFLTEQplEGLEKLYQEPRELppEERAQNVTRLLRK 2898
Cdd:TIGR02169  985 LKRLDELK--EKRAKLEEERKAI--LERIEEYEKKKRE 1018
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
3305-3351 3.87e-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: 3.87e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578837832 3305 CNICKEcPIIGFRYRSLKHFNYDICQSCFFSGRvaKGHKMHYPMVEY 3351
Cdd:cd02249     3 CDGCLK-PIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2313-2571 4.28e-07

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 53.60  E-value: 4.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2313 KDLGQLEKKLEDLEEQLNHLLL--WLSPIRNQLEiynqpnqegpfDVKETEIAVQAKQPDVEEILSKGQHLYKEKP-ATQ 2389
Cdd:cd00176     7 RDADELEAWLSEKEELLSSTDYgdDLESVEALLK-----------KHEALEAELAAHEERVEALNELGEQLIEEGHpDAE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2390 PVKRKLEDLSSEWKAVNRLLQELRAKqpdlapglttigasptqtvtlvtqpvvtketaisklempsslMLEVPALADFNR 2469
Cdd:cd00176    76 EIQERLEELNQRWEELRELAEERRQR------------------------------------------LEEALDLQQFFR 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2470 AWTELTDWLSLLDQVIKSQrVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKtSNQEARTIITDRIERI 2549
Cdd:cd00176   114 DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEE-GHPDADEEIEEKLEEL 191
                         250       260
                  ....*....|....*....|..
gi 578837832 2550 QNQWDEVQEHLQNRRQQLNEML 2571
Cdd:cd00176   192 NERWEELLELAEERQKKLEEAL 213
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1352-1930 5.65e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.82  E-value: 5.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1352 RRQKLLEQSIQSAQETEKSLH-----LIQEsLTFIDKQLAAYIADKVDAAQMPQEAQKIqsdLTSHEISLEEmkkhnqgk 1426
Cdd:PRK02224  185 QRGSLDQLKAQIEEKEEKDLHerlngLESE-LAELDEEIERYEEQREQARETRDEADEV---LEEHEERREE-------- 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1427 eaaqrvlsqIDVAQKKLQDVSMKFR-LFQKPANFEQRLQESKMILDEVKMHLPAL----ETKSVEQEVVQSQLNhcvnly 1501
Cdd:PRK02224  253 ---------LETLEAEIEDLRETIAeTEREREELAEEVRDLRERLEELEEERDDLlaeaGLDDADAEAVEARRE------ 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1502 kSLSEVKSEVEMVIKTGRQIVQKKQ------TENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVL 1575
Cdd:PRK02224  318 -ELEDRDEELRDRLEECRVAAQAHNeeaeslREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1576 TEWLAATDMEL----TKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVG---------------EALKTVLGK 1636
Cdd:PRK02224  397 RERFGDAPVDLgnaeDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGkcpecgqpvegsphvETIEEDRER 476
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1637 KETLvEDKLSLLNSNWIAVTSRAEEwLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDEsekkkpqqKEDVLKRLKAEL 1716
Cdd:PRK02224  477 VEEL-EAELEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEE--------KRERAEELRERA 546
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1717 NDIRPKVDSTRDQAANLMaNRGDHCRKlvepQISELNHRFAAISHRIKTgkasipLKELEqfnsDIQKLLEPLEAEIQQg 1796
Cdd:PRK02224  547 AELEAEAEEKREAAAEAE-EEAEEARE----EVAELNSKLAELKERIES------LERIR----TLLAAIADAEDEIER- 610
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1797 VNLKEEDFNkDMNEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKaleishqwyqykr 1876
Cdd:PRK02224  611 LREKREALA-ELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREER------------- 676
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578837832 1877 qaDDLLKCLDDIEKKLASLPEPRDERKikeidrELQKKKEELNAVRRQAEGLSE 1930
Cdd:PRK02224  677 --DDLQAEIGAVENELEELEELRERRE------ALENRVEALEALYDEAEELES 722
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
10-109 5.85e-07

second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409071  Cd Length: 121  Bit Score: 51.05  E-value: 5.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   10 KKTFTKWVNAQFSKFGKQhIENLFSDLQDGRRLLDLLEGLTGQKLP----KEKGSTRVHALNNVNKALRVLQNNNVDLVN 85
Cdd:cd21222    18 KELLLQFVNKHLAKLNIE-VTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELMEDAGISTPK 96
                          90       100
                  ....*....|....*....|....
gi 578837832   86 IGSTDIVDGNHKLTLGLIWNIILH 109
Cdd:cd21222    97 IRPEDIVNGDLKSILRVLYSLFSK 120
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
124-227 6.13e-07

second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409161  Cd Length: 114  Bit Score: 50.96  E-value: 6.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  124 QQTNSEKiLLSWVRQstrNYPQVNVINFTTSWSDGLALNALIHSHRPDLF-DWNSVVCQQSATQRLEhAFNIARYQLGIE 202
Cdd:cd21312    10 KQTPKQR-LLGWIQN---KLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNARE-AMQQADDWLGIP 84
                          90       100
                  ....*....|....*....|....*
gi 578837832  203 KLLDPEDVDTTYPDKKSILMYITSL 227
Cdd:cd21312    85 QVITPEEIVDPNVDEHSVMTYLSQF 109
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2278-3012 7.14e-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: 55.45  E-value: 7.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2278 EEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ--PNQEGPF 2355
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRErlANLERQL 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2356 DVKETEIAVQAKQPD--------VEEILSKGQHLYKEKPATQPVKR-KLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTI 2426
Cdd:TIGR02168  319 EELEAQLEELESKLDelaeelaeLEEKLEELKEELESLEAELEELEaELEELESRLEELEEQLETLRSKVAQLELQIASL 398
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2427 GASPTQTVTLVTQPVVTKETAISKLEmpssLMLEVPALADFNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQK 2506
Cdd:TIGR02168  399 NNEIERLEARLERLEDRRERLQQEIE----ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2507 ATMQDLEQRRPQLEELITAAQNLKNKTS-----------NQEARTIITDRIE---RIQNQWD-EVQEHLQNRRQQLneML 2571
Cdd:TIGR02168  475 QALDAAERELAQLQARLDSLERLQENLEgfsegvkallkNQSGLSGILGVLSeliSVDEGYEaAIEAALGGRLQAV--VV 552
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2572 KDSTQWLEAKEEAEQ---------VLGQARA------KLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDL- 2635
Cdd:TIGR02168  553 ENLNAAKKAIAFLKQnelgrvtflPLDSIKGteiqgnDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLd 632
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2636 -ALKLLRDYSAdDTRKVHMITENINASWRSIHKRVS------EREAALEETHRLLQQFPLDLEKFLAWLTEAETTANVLQ 2708
Cdd:TIGR02168  633 nALELAKKLRP-GYRIVTLDGDLVRPGGVITGGSAKtnssilERRREIEELEEKIEELEEKIAELEKALAELRKELEELE 711
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2709 DATRK--ERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRSLEGsddavlLQRRLDNMNFKWSELRKKSL 2786
Cdd:TIGR02168  712 EELEQlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE------LEERLEEAEEELAEAEAEIE 785
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2787 NIRSHLEASSDQWKRLHLSLQELLVWLQLKDDELSRQApiggdFPAVQKQNDVHRAfKRELKTKEPVIMSTLETVrIFLT 2866
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR-----ERLESLERRIAAT-ERRLEDLEEQIEELSEDI-ESLA 858
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2867 EQplegLEKLYQEPRELPPE-ERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQA 2945
Cdd:TIGR02168  859 AE----IEELEELIEELESElEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578837832  2946 EV-IKGSWQPVGDLLIDSLQDHLEKVKALRGEIAPLKEnvsHVNDLARQLTTLGiqlsPYNLSTLEDL 3012
Cdd:TIGR02168  935 EVrIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR---RLKRLENKIKELG----PVNLAAIEEY 995
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
647-1256 2.82e-06

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 53.43  E-value: 2.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   647 VQKLEKSTAQISQAVTTTQPSLTQTTVMETVTTVTTREQILVKHAQEELPPPPPQKKRQITVDSEIRKRLDVDITELHSw 726
Cdd:TIGR00618  221 KQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI- 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   727 itrsEAVLQSPefaiFRKEGNFSDLKEKvnaiEREKAEKFRKLQDASRSAQALVEQMVNEGV---NADSIKQASEQLNSR 803
Cdd:TIGR00618  300 ----KAVTQIE----QQAQRIHTELQSK----MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsQEIHIRDAHEVATSI 367
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   804 WIEFCQLLSERLNWLEYQNNIIAFYNQLQQLEQMTTTAENWLKIQPTTPSEPTAIKSQLKICKDEVnrlsdlQPQIERLK 883
Cdd:TIGR00618  368 REISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ------ELQQRYAE 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   884 IQSIALKEKGQGPMFLDAdfvaftnHFKQVFSDVQAREKELQTIFDTLPPMRYQETMSAIRTWVQQSETKLSIPQLSvtD 963
Cdd:TIGR00618  442 LCAAAITCTAQCEKLEKI-------HLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCI--H 512
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   964 YEIMEQRLGELQALQSSLQEQQSGLYYLSTTVKEMSKKAPSEisRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQMNKLR 1043
Cdd:TIGR00618  513 PNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSE--RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ 590
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1044 KIQNHIQTLKKWMAEVDVFLKEEW--------PALGDSEI-LKKQLKQCRL-------------LVSDIQTIQPSLNSVN 1101
Cdd:TIGR00618  591 NITVRLQDLTEKLSEAEDMLACEQhallrklqPEQDLQDVrLHLQQCSQELalkltalhalqltLTQERVREHALSIRVL 670
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1102 EGGQKIKNEAEPEFASR---------------------LETELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQKDLSE 1160
Cdd:TIGR00618  671 PKELLASRQLALQKMQSekeqltywkemlaqcqtllreLETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH 750
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1161 MHEWMTQAEEEYLERDFE-----YKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESvnsvIAQAPPVAQEALKKELETL 1235
Cdd:TIGR00618  751 QARTVLKARTEAHFNNNEevtaaLQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAE----IGQEIPSDEDILNLQCETL 826
                          650       660
                   ....*....|....*....|.
gi 578837832  1236 TTNYQWLCTRLNGKCKTLEEV 1256
Cdd:TIGR00618  827 VQEEEQFLSRLEEKSATLGEI 847
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1607-1764 2.92e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 51.29  E-value: 2.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1607 KATQKEIEKQKVHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQnVDHITKW 1686
Cdd:cd00176    43 EALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQW 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1687 IIQADTLLDESEK-KKPQQKEDVLKRLKA---ELNDIRPKVDSTRDQAANLMANRGDHCRKLVEPQISELNHRFAAISHR 1762
Cdd:cd00176   122 LEEKEAALASEDLgKDLESVEELLKKHKEleeELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLEL 201

                  ..
gi 578837832 1763 IK 1764
Cdd:cd00176   202 AE 203
SPEC smart00150
Spectrin repeats;
1052-1145 3.06e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.48  E-value: 3.06e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   1052 LKKWMAEVDVFLKEEWPAlGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEfASRLETELKELNTQWD 1131
Cdd:smart00150   10 LEAWLEEKEQLLASEDLG-KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERLEELNERWE 87
                            90
                    ....*....|....
gi 578837832   1132 HMCQQVYARKEALK 1145
Cdd:smart00150   88 ELKELAEERRQKLE 101
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
133-228 3.15e-06

third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409034  Cd Length: 98  Bit Score: 48.07  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  133 LSWVRQSTrnyPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSaTQRLEHAFNIARyQLGIEKLLDPEDVDT 212
Cdd:cd21185     7 LRWVRQLL---PDVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEES-ENNIQRGLEAGK-SLGVEPVLTAEEMAD 81
                          90
                  ....*....|....*.
gi 578837832  213 TYPDKKSILMYITSLF 228
Cdd:cd21185    82 PEVEHLGIMAYAAQLQ 97
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
3305-3348 5.68e-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: 5.68e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 578837832 3305 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPM 3348
Cdd:cd02338     3 CDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPM 46
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1689-1963 8.01e-06

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 50.68  E-value: 8.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1689 QADTLLDESEKKKPQQKE--DVLKRLKAELNDIRPKVDSTRDQAANLMANRGDHCRKLVE--PQISELNHRFAAISHRIK 1764
Cdd:COG1340    16 KIEELREEIEELKEKRDElnEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKElkEERDELNEKLNELREELD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1765 TGKASIPLKELEQFNSD-IQKLLEPLEAEIQqgvnlkeedfNKDMNEDNEgtvKELLQRGDNLQQRITDERKREEIKIKQ 1843
Cdd:COG1340    96 ELRKELAELNKAGGSIDkLRKEIERLEWRQQ----------TEVLSPEEE---KELVEKIKELEKELEKAKKALEKNEKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1844 QLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDER--KIKEIDRELQKKKEELNAV 1921
Cdd:COG1340   163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAqeKADELHEEIIELQKELREL 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 578837832 1922 RRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNF 1963
Cdd:COG1340   243 RKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTT 284
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
132-231 9.20e-06

second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409073 [Multi-domain]  Cd Length: 138  Bit Score: 48.07  E-value: 9.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTRNYpQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHA-------------------- 191
Cdd:cd21224     5 LLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQTVDRAQDeaedfwvaefspstgdsgls 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578837832  192 ----------FNIAR---YQLG-IEKLLDPEDVDTTYPDKKSILMYITSLFQVL 231
Cdd:cd21224    84 sellanekrnFKLVQqavAELGgVPALLRASDMSNTIPDEKVVILFLSYLCARL 137
SPEC smart00150
Spectrin repeats;
719-819 9.28e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.94  E-value: 9.28e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    719 DITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQmvnEGVNADSIKQASE 798
Cdd:smart00150    6 DADELEAWLEEKEQLLASEDLG--KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE---GHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 578837832    799 QLNSRWIEFCQLLSERLNWLE 819
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
1412-2058 1.23e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 51.66  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1412 HEISLEEMKKHNQ--GKEAAQRVLS----QIDVAQKKLQDVS-----MKFRLFQKPANFEQRLQESKMILDEVkMHLPAL 1480
Cdd:pfam15921   57 YEVELDSPRKIIAypGKEHIERVLEeyshQVKDLQRRLNESNelhekQKFYLRQSVIDLQTKLQEMQMERDAM-ADIRRR 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1481 ETKSveQEVVQSQLNHCVNLYKSLSEVKSEveMVIKTGRQIVQKKQTENPKE--LDERVTALKLHYNELGAKVTERKQql 1558
Cdd:pfam15921  136 ESQS--QEDLRNQLQNTVHELEAAKCLKED--MLEDSNTQIEQLRKMMLSHEgvLQEIRSILVDFEEASGKKIYEHDS-- 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1559 ekclkLSRKMRKEMNvltewlaatdmeltkrSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSitEVGEALKTVLGKKE 1638
Cdd:pfam15921  210 -----MSTMHFRSLG----------------SAISKILRELDTEISYLKGRIFPVEDQLEALKS--ESQNKIELLLQQHQ 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1639 TLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETF-----DQN------VDHITKWIIQADTLLDESEKKKPQQKED 1707
Cdd:pfam15921  267 DRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIqeqarNQNsmymrqLSDLESTVSQLRSELREAKRMYEDKIEE 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1708 VLKRL---KAELNDIRpkvdSTRDQAANLMANRGDHCRKLvepqISELNHRFAAISHRIKTGKA--------SIPL---- 1772
Cdd:pfam15921  347 LEKQLvlaNSELTEAR----TERDQFSQESGNLDDQLQKL----LADLHKREKELSLEKEQNKRlwdrdtgnSITIdhlr 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1773 KELEQFNSDIQK---LLEPLEAEIqQGVNLKEEDFNKDMNEDNEgTVKELLQRGDNLQQRItdERKREEIKIKQQLLQTK 1849
Cdd:pfam15921  419 RELDDRNMEVQRleaLLKAMKSEC-QGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEML--RKVVEELTAKKMTLESS 494
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1850 HNALKDLRS--QRRKKALEISHQWYQYKRQADDL-LKCLDDIEKKLASLPEPRDErkIKEIDRELQKKKEELNAVRRQAE 1926
Cdd:pfam15921  495 ERTVSDLTAslQEKERAIEATNAEITKLRSRVDLkLQELQHLKNEGDHLRNVQTE--CEALKLQMAEKDKVIEILRQQIE 572
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1927 GLSE-------DGAAMAVEPTQIQLSKRWREIESKfaQFRRLNFAQIHTVREetMMVMTEDMPLEISYVPSTYLTEITHV 1999
Cdd:pfam15921  573 NMTQlvgqhgrTAGAMQVEKAQLEKEINDRRLELQ--EFKILKDKKDAKIRE--LEARVSDLELEKVKLVNAGSERLRAV 648
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837832  2000 SQALLEVEQLLNAPDLCAKDFEDLFKQEESLKNikdSLQQSSGRIDIIHSKKTAALQSA 2058
Cdd:pfam15921  649 KDIKQERDQLLNEVKTSRNELNSLSEDYEVLKR---NFRNKSEEMETTTNKLKMQLKSA 704
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2469-2773 1.40e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2469 RAWTELTDWLSLLDQVIKSQRVmvgDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTI------- 2541
Cdd:COG1196   232 LKLRELEAELEELEAELEELEA---ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiarle 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2542 -----ITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESwkegpyTVDAIQKKITETK 2616
Cdd:COG1196   309 errreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------AEAELAEAEEELE 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2617 QLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKvhmitENINASWRSIHKRVSEREAALEETHRLLQQfplDLEKFLAW 2696
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERL-----ERLEEELEELEEALAELEEEEEEEEEALEE---AAEEEAEL 454
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578837832 2697 LTEAETTANVLQDATRKERLLEdskgvkelmKQWQDLQGEIEAHTDVYHNLdensQKILRSLEGSDDAVLLQRRLDN 2773
Cdd:COG1196   455 EEEEEALLELLAELLEEAALLE---------AALAELLEELAEAAARLLLL----LEAEADYEGFLEGVKAALLLAG 518
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2152-2620 1.45e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2152 RTLNATGEEIIQQSSKTD--ASILQEKLGSLnlrwQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASI- 2228
Cdd:PRK03918  296 IKLSEFYEEYLDELREIEkrLSRLEEEINGI----EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKk 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2229 -----------PLEPGKEQQLKEKLEQVKLLVEE----LPLRQGILKQ--------LNETGG-----PVlVSAPISPEEQ 2280
Cdd:PRK03918  372 eelerlkkrltGLTPEKLEKELEELEKAKEEIEEeiskITARIGELKKeikelkkaIEELKKakgkcPV-CGRELTEEHR 450
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2281 DKLENKLKqtnlqwikvsralpEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ----PNQEGPFD 2356
Cdd:PRK03918  451 KELLEEYT--------------AELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQlkelEEKLKKYN 516
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2357 VKETEiavqAKQPDVEEILSKGQHLYKEKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVtl 2436
Cdd:PRK03918  517 LEELE----KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL-- 590
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2437 vtqpvvtkETAISKLEmpsslmlevpalaDFNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQKAtmqDLEQRR 2516
Cdd:PRK03918  591 --------EERLKELE-------------PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK---RLEELR 646
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2517 PQLEELITA--------AQNLKNKTSNQEARtiITDRIERIQNQWDEVQEHLQNRRQQLNEMLKdstqwleAKEEAEqVL 2588
Cdd:PRK03918  647 KELEELEKKyseeeyeeLREEYLELSRELAG--LRAELEELEKRREEIKKTLEKLKEELEEREK-------AKKELE-KL 716
                         490       500       510
                  ....*....|....*....|....*....|..
gi 578837832 2589 GQARAKLEswkegpytvdAIQKKITETKQLAK 2620
Cdd:PRK03918  717 EKALERVE----------ELREKVKKYKALLK 738
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2481-3013 1.69e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2481 LDQVIKSQRVMVGDLEDINEMIIKQKATMQDLEQRrpqLEELITAAQNLKNKTSNQEARTI-ITDRIERIQNQWDEVQEH 2559
Cdd:COG1196   283 LEEAQAEEYELLAELARLEQDIARLEERRRELEER---LEELEEELAELEEELEELEEELEeLEEELEEAEEELEEAEAE 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2560 LQNRRQQLNEMLKDSTQWLEA-KEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALK 2638
Cdd:COG1196   360 LAEAEEALLEAEAELAEAEEElEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2639 LLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQfpLDLEKFLAWLTEAETTANVLQDATRKERLLE 2718
Cdd:COG1196   440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL--AEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2719 DSKGVKELMKQWQDLQGEIEAHTDVYhnLDENSQKILRSLEGSDDAV---LLQRRLDNMNFKwselrkkSLNIRSHLEAS 2795
Cdd:COG1196   518 GLRGLAGAVAVLIGVEAAYEAALEAA--LAAALQNIVVEDDEVAAAAieyLKAAKAGRATFL-------PLDKIRARAAL 588
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2796 SDQWKRLHLSLQELLVWLQLKDDELSRQAPIGGDFPAVQKQNDVHRAFKRELKTKEpvimsTLETVRIFLTEQPLEGLEK 2875
Cdd:COG1196   589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG-----RLREVTLEGEGGSAGGSLT 663
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2876 LYQEPRELPPEERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQAEVIkgswqpV 2955
Cdd:COG1196   664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE------L 737
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578837832 2956 GDLLIDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGiqlsPYNLSTLEDLN 3013
Cdd:COG1196   738 LEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG----PVNLLAIEEYE 791
SPEC smart00150
Spectrin repeats;
1872-1954 1.89e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.17  E-value: 1.89e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   1872 YQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDG--AAMAVEPTQI 1942
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLesveallKKHEAFEAELEAHEERVEALNELGEQLIEEGhpDAEEIEERLE 80
                            90
                    ....*....|..
gi 578837832   1943 QLSKRWREIESK 1954
Cdd:smart00150   81 ELNERWEELKEL 92
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1870-2094 2.22e-05

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 48.60  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1870 QWYQYKRQADDLLKCLDDIEKKLASLPEPRDE-------RKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQI 1942
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLesveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1943 Q--LSKRWREIESKFAQFRRLnfaqihtvreetmmvmtedmpLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCaKDF 2020
Cdd:cd00176    81 LeeLNQRWEELRELAEERRQR---------------------LEEALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDL 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578837832 2021 EDLFKQEESLKNIKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFDRS 2094
Cdd:cd00176   139 ESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC smart00150
Spectrin repeats;
2207-2309 2.41e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.78  E-value: 2.41e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   2207 EFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSapiSPEEQDKLENK 2286
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE---GHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 578837832   2287 LKQTNLQWIKVSRALPEKQGEIE 2309
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1610-1918 2.62e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.40  E-value: 2.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1610 QKEIEKQKVHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVDHITKwiiQ 1689
Cdd:TIGR04523  213 NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK---Q 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1690 ADTLLDESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANlmanrgdhcrklVEPQISELNHRFAAISHRiktgkas 1769
Cdd:TIGR04523  290 LNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQ------------NNKIISQLNEQISQLKKE------- 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1770 ipLKELEQFNSDIQKLLEPLEAEIQQgvNLKEEDFNKDMNEDNEGTVKELLQRGDNLQQriTDERKREEIKIKQQLLQTK 1849
Cdd:TIGR04523  351 --LTNSESENSEKQRELEEKQNEIEK--LKKENQSYKQEIKNLESQINDLESKIQNQEK--LNQQKDEQIKKLQQEKELL 424
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578837832  1850 HNALKDLRSQRRKKALEIS---HQWYQYKRQADDLLKCLDDIEKKLASLpeprdERKIKEIDRELQKKKEEL 1918
Cdd:TIGR04523  425 EKEIERLKETIIKNNSEIKdltNQDSVKELIIKNLDNTRESLETQLKVL-----SRSINKIKQNLEQKQKEL 491
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
914-1860 2.87e-05

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 50.43  E-value: 2.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   914 FSDVQAREKELQTIFDTLPPMRYQETMSAIRtwvQQSETKLSIPQLSVTDYEIMEQRLGELQAlqsslqeqqsglyylST 993
Cdd:TIGR00606  165 LSEGKALKQKFDEIFSATRYIKALETLRQVR---QTQGQKVQEHQMELKYLKQYKEKACEIRD---------------QI 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   994 TVKEMSKKAPSEISRKYQSEFEEIEGRWKKLssqlvehcqklEEQMNKLRKIQNHIQTLKKWMAEVdvflkeewpalgds 1073
Cdd:TIGR00606  227 TSKEAQLESSREIVKSYENELDPLKNRLKEI-----------EHNLSKIMKLDNEIKALKSRKKQM-------------- 281
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1074 EILKKQLKQCRllVSDIQTIQPSLNSVNEGGQKIKNEAEPEFAsRLETELKELNTQWDHMCQQ-----VYARKEALKGGL 1148
Cdd:TIGR00606  282 EKDNSELELKM--EKVFQGTDEQLNDLYHNHQRTVREKERELV-DCQRELEKLNKERRLLNQEktellVEQGRLQLQADR 358
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1149 EKTVSLQKDlSEMHEWMTQAEEEYLERDfeyktPDeLQKAVEEMKRAKEEAQQKEAKV--KLLTEsvnsvIAQAPPVAQE 1226
Cdd:TIGR00606  359 HQEHIRARD-SLIQSLATRLELDGFERG-----PF-SERQIKNFHTLVIERQEDEAKTaaQLCAD-----LQSKERLKQE 426
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1227 ALKKeletlttnyqwLCTRLNGKCKTLEevwacwhellSYLEKANKWLNEVEFKLKTTENIPGGAEEISEvldsLENLMR 1306
Cdd:TIGR00606  427 QADE-----------IRDEKKGLGRTIE----------LKKEILEKKQEELKFVIKELQQLEGSSDRILE----LDQELR 481
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1307 HSEDNPNQIRILAQTLTDGGVMDELINEELETFNSRwRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDKQLA 1386
Cdd:TIGR00606  482 KAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKL-RKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSD 560
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1387 AYIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKKHNQGKEAAQRVLSQIDVAQKKL--QDVSMKFRLFQ--KPANFEQR 1462
Cdd:TIGR00606  561 ELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKeeQLSSYEDKLFDvcGSQDEESD 640
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1463 LQESKMILDEVKMHLPALETKS------VEQEVVQSQlnHCVNLYKSLSEVKSEVEMVIK----------TGRQIVQKKQ 1526
Cdd:TIGR00606  641 LERLKEEIEKSSKQRAMLAGATavysqfITQLTDENQ--SCCPVCQRVFQTEAELQEFISdlqsklrlapDKLKSTESEL 718
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1527 TENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEW---------------LAATDMELTKR-- 1589
Cdd:TIGR00606  719 KKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQetllgtimpeeesakVCLTDVTIMERfq 798
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1590 -------SAVEGMPSNLDSEVAWGKATQ--KEIEKQKVHLKSITEVGEALKTVL---GKKETLVEDKLSLLNSNWIAVTS 1657
Cdd:TIGR00606  799 melkdveRKIAQQAAKLQGSDLDRTVQQvnQEKQEKQHELDTVVSKIELNRKLIqdqQEQIQHLKSKTNELKSEKLQIGT 878
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1658 RAEEwlnlLLEYQKHMETFDQNVDHITKWIIQA--DTLLDESEKKKPQQKEDVL--------KRLKAELNDIRPKVDSTR 1727
Cdd:TIGR00606  879 NLQR----RQQFEEQLVELSTEVQSLIREIKDAkeQDSPLETFLEKDQQEKEELissketsnKKAQDKVNDIKEKVKNIH 954
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1728 DQAANLMANRGDHCRKLVEPQISELNHRFAAISHRiktgkasipLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNKD 1807
Cdd:TIGR00606  955 GYMKDIENKIQDGKDDYLKQKETELNTVNAQLEEC---------EKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRK 1025
                          970       980       990      1000      1010
                   ....*....|....*....|....*....|....*....|....*....|...
gi 578837832  1808 MNEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQR 1860
Cdd:TIGR00606 1026 RENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQK 1078
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1183-1926 4.10e-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: 49.68  E-value: 4.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1183 DELQKAVEEMKRAKEEAQQKEAKVKLLTEsvnsviaqappVAQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHE 1262
Cdd:TIGR02169  194 DEKRQQLERLRREREKAERYQALLKEKRE-----------YEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1263 LLSYLEKANKWLNEVEFKLK--TTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDGgvmDELINEELETFN 1340
Cdd:TIGR02169  263 LEKRLEEIEQLLEELNKKIKdlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL---EAEIDKLLAEIE 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1341 SRWRELHEEAVRRQKLLEQSIQSAQETEKSLhliqesltfidkqlaayiadkvdaaqmpqeaQKIQSDLTSHEISLEEMK 1420
Cdd:TIGR02169  340 ELEREIEEERKRRDKLTEEYAELKEELEDLR-------------------------------AELEEVDKEFAETRDELK 388
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1421 KHNQGKEAAQRVLSQIDVAQKKLQDvsmkfrlfqkpanfeqRLQESKMILDEVKMHLPALETKsveqevvqsqlnhcvnl 1500
Cdd:TIGR02169  389 DYREKLEKLKREINELKRELDRLQE----------------ELQRLSEELADLNAAIAGIEAK----------------- 435
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1501 yksLSEVKSEVEMVIKTGRQIVQKKQT--ENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMnvlTEW 1578
Cdd:TIGR02169  436 ---INELEEEKEDKALEIKKQEWKLEQlaADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV---RGG 509
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1579 LAATDMELTKRSAVEGMPSNLDSevaWGKATQKEIEkqkvhlksiTEVGEALKTVLGKKETLVEDKLSLLNS-------- 1650
Cdd:TIGR02169  510 RAVEEVLKASIQGVHGTVAQLGS---VGERYATAIE---------VAAGNRLNNVVVEDDAVAKEAIELLKRrkagratf 577
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1651 ---NWIAVTSRAEEWLNL--LLEYQKHMETFDQNVDHITKWIIQaDTLLDES---------------------------- 1697
Cdd:TIGR02169  578 lplNKMRDERRDLSILSEdgVIGFAVDLVEFDPKYEPAFKYVFG-DTLVVEDieaarrlmgkyrmvtlegelfeksgamt 656
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1698 ---------------EKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANRGDHCRKLVEPQ--ISELNHRFAAIS 1760
Cdd:TIGR02169  657 ggsraprggilfsrsEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeIEQLEQEEEKLK 736
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1761 HRIKTGKASIplKELEQFNSDIQKLLEPLEAEIQQ------GVNLKEEDFNKDMN-----------EDNEGTVKELLQRG 1823
Cdd:TIGR02169  737 ERLEELEEDL--SSLEQEIENVKSELKELEARIEEleedlhKLEEALNDLEARLShsripeiqaelSKLEEEVSRIEARL 814
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1824 DNLQQRITDERKREEI-KIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDER 1902
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYlEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
                          810       820
                   ....*....|....*....|....
gi 578837832  1903 KIKEidRELQKKKEELNAVRRQAE 1926
Cdd:TIGR02169  895 EAQL--RELERKIEELEAQIEKKR 916
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
122-227 4.31e-05

second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409162  Cd Length: 110  Bit Score: 45.47  E-value: 4.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  122 GLQQTNSEKiLLSWVRQSTrnyPQVNVINFTTSWSDGLALNALIHSHRPDLF-DWNSVVCQQSATQRLEhAFNIARYQLG 200
Cdd:cd21313     4 AKKQTPKQR-LLGWIQNKI---PYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNARE-AMQQADDWLG 78
                          90       100
                  ....*....|....*....|....*..
gi 578837832  201 IEKLLDPEDVDTTYPDKKSILMYITSL 227
Cdd:cd21313    79 VPQVITPEEIIHPDVDEHSVMTYLSQF 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2467-2569 4.36e-05

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: 45.00  E-value: 4.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2467 FNRAWTELTDWLSLLDQVIKSQRvMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNktSNQEARTIITDRI 2546
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSED-YGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID--EGHYASEEIQERL 82
                           90       100
                   ....*....|....*....|...
gi 578837832  2547 ERIQNQWDEVQEHLQNRRQQLNE 2569
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2681-2783 5.09e-05

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: 45.00  E-value: 5.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2681 RLLQQFPLDLEKFLAWLTEAETTANvlqdatrKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILrsLEG 2760
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLS-------SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI--DEG 71
                           90       100
                   ....*....|....*....|...
gi 578837832  2761 SDDAVLLQRRLDNMNFKWSELRK 2783
Cdd:pfam00435   72 HYASEEIQERLEELNERWEQLLE 94
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1657-2419 5.83e-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: 49.30  E-value: 5.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1657 SRAEEWLNLLLEYQKHMETFDQNVDHITKwiiQADTLLDESEKKKPQQkeDVLKRL-KAELNDIRPKVDSTRDQAANLMA 1735
Cdd:TIGR02169  170 RKKEKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKAERYQ--ALLKEKrEYEGYELLKEKEALERQKEAIER 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1736 NRGDHCRKL--VEPQISELNHRFAAISHRIKTGKASI-PLKELEQFNsdIQKLLEPLEAEIQQGVnlKEEDFNKDMNEDN 1812
Cdd:TIGR02169  245 QLASLEEELekLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLR--VKEKIGELEAEIASLE--RSIAEKERELEDA 320
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1813 EGTVKELLQRGDNLQQRITD--------------------ERKREEIKIKQQL--LQTKHNALKDLRSQRRKKALEISHQ 1870
Cdd:TIGR02169  321 EERLAKLEAEIDKLLAEIEElereieeerkrrdklteeyaELKEELEDLRAELeeVDKEFAETRDELKDYREKLEKLKRE 400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1871 WYQYKRQADDLLKCLDDIEKKLASLPE--PRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQIQ----- 1943
Cdd:TIGR02169  401 INELKRELDRLQEELQRLSEELADLNAaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKeeydr 480
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1944 ----LSKRWREIESKFAQFRRLNFAQIHTVREEtmMVMTEDMPLEISYVPStyLTEITHVSQALLEVEQLLNAPDLCAKD 2019
Cdd:TIGR02169  481 vekeLSKLQRELAEAEAQARASEERVRGGRAVE--EVLKASIQGVHGTVAQ--LGSVGERYATAIEVAAGNRLNNVVVED 556
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2020 FEDLFKQEESLKNIKdslqqsSGRIDIIHSKKTAALQSatPVERVKLQEALsqlDFQWEKVnkmykdrqgRFDRSVEKWR 2099
Cdd:TIGR02169  557 DAVAKEAIELLKRRK------AGRATFLPLNKMRDERR--DLSILSEDGVI---GFAVDLV---------EFDPKYEPAF 616
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2100 RFhydikifnqwlteaeqFLRKTQIPENWEHAKY---KWYLKELQDGIGQRQTVVrtlnaTGEEIIQQSSKTDASILQEK 2176
Cdd:TIGR02169  617 KY----------------VFGDTLVVEDIEAARRlmgKYRMVTLEGELFEKSGAM-----TGGSRAPRGGILFSRSEPAE 675
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2177 LGSLNLRWQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIPLEpgKEQQLKEKLEQVKLLVEELplrq 2256
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ--EEEKLKERLEELEEDLSSL---- 749
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2257 gilkqlnetggpvlvsapispeEQDKLENKLKQTNLQwikvsralpekqGEIEAQIKDLGQLEKKLEDLEEQLNHLLlwL 2336
Cdd:TIGR02169  750 ----------------------EQEIENVKSELKELE------------ARIEELEEDLHKLEEALNDLEARLSHSR--I 793
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2337 SPIRNQLEIYNQPNQEGPFDVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQ----PVKRKLEDLSSEWKAVNRLLQEL 2412
Cdd:TIGR02169  794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKeqikSIEKEIENLNGKKEELEEELEEL 873

                   ....*..
gi 578837832  2413 RAKQPDL 2419
Cdd:TIGR02169  874 EAALRDL 880
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
11-106 6.44e-05

calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409135  Cd Length: 105  Bit Score: 44.64  E-value: 6.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   11 KTFTKWVNAQFSKFG-KQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHA--LNNVNKALRVLQNNNVDLVNIG 87
Cdd:cd21286     3 KIYTDWANHYLAKSGhKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSqmIENVDVCLSFLAARGVNVQGLS 82
                          90
                  ....*....|....*....
gi 578837832   88 STDIVDGNHKLTLGLIWNI 106
Cdd:cd21286    83 AEEIRNGNLKAILGLFFSL 101
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
1684-2570 6.49e-05

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 49.27  E-value: 6.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1684 TKWIIQADTL----LDESEKKKPQQKE-DVLKRLKAELNDIRPKVDSTRDQAANlmanrGDHCRKLVEPQISELNHRFAA 1758
Cdd:TIGR00606  182 TRYIKALETLrqvrQTQGQKVQEHQMElKYLKQYKEKACEIRDQITSKEAQLES-----SREIVKSYENELDPLKNRLKE 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1759 ISH-RIKTGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNkDMNEDNEGTVKELLQRgdnlqqRITDERKRE 1837
Cdd:TIGR00606  257 IEHnLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLN-DLYHNHQRTVREKERE------LVDCQRELE 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1838 EIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQY--KRQADDLLKCLDDIE---------KKLASLPEPRDERKIKE 1906
Cdd:TIGR00606  330 KLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARdsLIQSLATRLELDGFErgpfserqiKNFHTLVIERQEDEAKT 409
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1907 IDRELQKKKEELNAVRRQAEGLSED--GAAMAVEPTQIQLSKRWREIESKFAQFRRLNFAQIHTVREETMMVMTEDmplE 1984
Cdd:TIGR00606  410 AAQLCADLQSKERLKQEQADEIRDEkkGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAER---E 486
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1985 ISYVPSTYLTEITHVSQALLEVEQLLNAPDLCAKDfedlfKQEESLKNIKDSLQQssgrIDIIHSKKTAALQSATPVERV 2064
Cdd:TIGR00606  487 LSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLD-----QEMEQLNHHTTTRTQ----MEMLTKDKMDKDEQIRKIKSR 557
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2065 KLQEALSQL-DFQWEKVnkmykdrqgrfdrsVEKWrrFHYDIKIFNQwlteAEQFLRKTQIPENWEHAKYKWYLKELQDG 2143
Cdd:TIGR00606  558 HSDELTSLLgYFPNKKQ--------------LEDW--LHSKSKEINQ----TRDRLAKLNKELASLEQNKNHINNELESK 617
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2144 IGQrqtvvrtLNATGEEIIQQSSKTDasiLQEKLGSLNLRWQEVCKQLSdrkkRLEEQKNILSEFQRDLNEfvlwleeaD 2223
Cdd:TIGR00606  618 EEQ-------LSSYEDKLFDVCGSQD---EESDLERLKEEIEKSSKQRA----MLAGATAVYSQFITQLTD--------E 675
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2224 NIASIPL-----EPGKE-QQLKEKLEQVKLLV-EELPLRQGILKQLNETGGPVLVSAPISPEEQDKLENKLKQTNLQWIK 2296
Cdd:TIGR00606  676 NQSCCPVcqrvfQTEAElQEFISDLQSKLRLApDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK 755
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2297 VSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLL----LWLSPIRNQLEIYNQPNQ----EGPFDVKETEIAVQAKQ 2368
Cdd:TIGR00606  756 VNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTimerFQMELKDVERKIAQQAAKlqgsDLDRTVQQVNQEKQEKQ 835
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2369 PDVEEILSKGQHLYK----EKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIgASPTQTVTLVTQPVVTK 2444
Cdd:TIGR00606  836 HELDTVVSKIELNRKliqdQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV-QSLIREIKDAKEQDSPL 914
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2445 ETAISKLEMPSSLMLEVPALADfNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQK--------ATMQDLEQRR 2516
Cdd:TIGR00606  915 ETFLEKDQQEKEELISSKETSN-KKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKetelntvnAQLEECEKHQ 993
                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 578837832  2517 PQLEELITAAQNLKNKTSNQEarTIITDRIER--IQNQWDEVQEHLQNRRQQLNEM 2570
Cdd:TIGR00606  994 EKINEDMRLMRQDIDTQKIQE--RWLQDNLTLrkRENELKEVEEELKQHLKEMGQM 1047
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
4-107 6.81e-05

third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409179  Cd Length: 125  Bit Score: 45.37  E-value: 6.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    4 EREDVQKKTFTKWVNaqfSKFGKQHIENLFSDLQDGRRLLDLLEGLTG-------QKLPKEKGSTRVHALNNVNKALRVL 76
Cdd:cd21330     9 EGETREERTFRNWMN---SLGVNPRVNHLYSDLSDALVIFQLYEKIKVpvdwnrvNKPPYPKLGENMKKLENCNYAVELG 85
                          90       100       110
                  ....*....|....*....|....*....|..
gi 578837832   77 QNN-NVDLVNIGSTDIVDGNHKLTLGLIWNII 107
Cdd:cd21330    86 KNKaKFSLVGIAGQDLNEGNRTLTLALIWQLM 117
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1696-2344 7.27e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.90  E-value: 7.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1696 ESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMAnrgdhcrkLVEPQISELNHRFAAISHRIKTGKASipLKEL 1775
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA--------ELEEKLEELKEELESLEAELEELEAE--LEEL 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1776 EQFNSDIQKLLEPLEAEiqqgVNLKEEDFNKDMNEdnegtvkelLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKD 1855
Cdd:TIGR02168  371 ESRLEELEEQLETLRSK----VAQLELQIASLNNE---------IERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1856 LRSQRRKKaleishqwyqyKRQADDLLKCLDDIEKKLASLPEPRDE-----RKIKEIDRELQKKKEELNAVRRQAEGLSE 1930
Cdd:TIGR02168  438 LQAELEEL-----------EEELEELQEELERLEEALEELREELEEaeqalDAAERELAQLQARLDSLERLQENLEGFSE 506
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1931 DGAAMAVEPTQI-----QLSKRWrEIESKFAqfrrlnfAQIHTVREETM-MVMTEDMpleisyvpSTYLTEITHVSQALL 2004
Cdd:TIGR02168  507 GVKALLKNQSGLsgilgVLSELI-SVDEGYE-------AAIEAALGGRLqAVVVENL--------NAAKKAIAFLKQNEL 570
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2005 EVEQLLNAPDLcaKDFEDLFKQEESLKNIKDSLQQSSGRIDI---IHSKKTAALQSATPVERvkLQEAL---SQLDFQW- 2077
Cdd:TIGR02168  571 GRVTFLPLDSI--KGTEIQGNDREILKNIEGFLGVAKDLVKFdpkLRKALSYLLGGVLVVDD--LDNALelaKKLRPGYr 646
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2078 ------EKVNKMY-------KDRQGRFDRSVEkwrrfhydIKIFNQWLTEAEQFLRKTQIPenwehakykwyLKELQDGI 2144
Cdd:TIGR02168  647 ivtldgDLVRPGGvitggsaKTNSSILERRRE--------IEELEEKIEELEEKIAELEKA-----------LAELRKEL 707
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2145 GQRQTVVRTLNATGEEIIQQSSKtdasiLQEKLGSLNLRWQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEA-D 2223
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISA-----LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAeA 782
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2224 NIASIplepgkEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSAPISPEEQDKLENKLKQTNLQWIKVSRALPE 2303
Cdd:TIGR02168  783 EIEEL------EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 578837832  2304 KQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLE 2344
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
1106-1874 7.49e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 48.81  E-value: 7.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1106 KIKNEAEPEfASRLETELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDfeyktpdEL 1185
Cdd:TIGR00618  187 AKKKSLHGK-AELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL-------KK 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1186 QKAVEEMKRAKEEAQQKEAKVKLLTESVNsviaQAPPVAQEALKKEletlttnyqwlctrlngkcktleevwacwhells 1265
Cdd:TIGR00618  259 QQLLKQLRARIEELRAQEAVLEETQERIN----RARKAAPLAAHIK---------------------------------- 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1266 YLEKANKWLNEVEFKLKTTENipggaeEISEVLDSLENLMRHSEDNPNQIRILAQTLTDggvmdelineelETFNSRWRE 1345
Cdd:TIGR00618  301 AVTQIEQQAQRIHTELQSKMR------SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ------------EIHIRDAHE 362
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1346 lhEEAVRRqkllEQSIQSAQETEKSLHLIQESLTFIDK-QLAAYIADKVDAAQMPQEAQKI-QSDLTSHEISLEEMKKHN 1423
Cdd:TIGR00618  363 --VATSIR----EISCQQHTLTQHIHTLQQQKTTLTQKlQSLCKELDILQREQATIDTRTSaFRDLQGQLAHAKKQQELQ 436
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1424 QGKEAAQRVLSQiDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKmhlpalETKSVEQEVVQSQLNHCVNLYKS 1503
Cdd:TIGR00618  437 QRYAELCAAAIT-CTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQET------RKKAVVLARLLELQEEPCPLCGS 509
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1504 LSEVKSEVEMVIKTG------RQIVQ--KKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVL 1575
Cdd:TIGR00618  510 CIHPNPARQDIDNPGpltrrmQRGEQtyAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL 589
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1576 TEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGEALKTVL-GKKETLVEDKLSllnSNWIA 1654
Cdd:TIGR00618  590 QNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALhALQLTLTQERVR---EHALS 666
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1655 VTSRAEEWLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDESEK------KKPQQKEDVLKRLKAELNdirpkvdsTRD 1728
Cdd:TIGR00618  667 IRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELEThieeydREFNEIENASSSLGSDLA--------ARE 738
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1729 QAANLMANRGDHCRKLV-EPQISELNHRFAAISHRIKTGkasiplKELEQFNSDIQKLLEPLEAEIQQGVNLKEE--DFN 1805
Cdd:TIGR00618  739 DALNQSLKELMHQARTVlKARTEAHFNNNEEVTAALQTG------AELSHLAAEIQFFNRLREEDTHLLKTLEAEigQEI 812
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1806 KDMNEDNEGTVKELLQRGDNLQQRItDERKREEIKIKQQLLQTKHNA-LKDLRSQRRKKALEISHQWYQY 1874
Cdd:TIGR00618  813 PSDEDILNLQCETLVQEEEQFLSRL-EEKSATLGEITHQLLKYEECSkQLAQLTQEQAKIIQLSDKLNGI 881
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
137-210 7.84e-05

CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.


Pssm-ID: 432229  Cd Length: 85  Bit Score: 43.83  E-value: 7.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   137 RQSTRNYPQVNviNFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQR-----LEHAFNIARYQLGIEKL-LDPEDV 210
Cdd:pfam11971    4 QRSLPLSPPVE--DLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLAdslynIQLLQEFCQRHLGNRCChLTLEDL 81
SPEC smart00150
Spectrin repeats;
1261-1358 8.47e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 44.24  E-value: 8.47e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   1261 HELLSYLEKANKWLNEVEFKLKTTE--NIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDGGVMD-ELINEELE 1337
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDlgKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDaEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 578837832   1338 TFNSRWRELHEEAVRRQKLLE 1358
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1816-2597 8.98e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.90  E-value: 8.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1816 VKELLQRGDNLQQRITD-ERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLAS 1894
Cdd:TIGR02168  234 LEELREELEELQEELKEaEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1895 LPEPRD--ERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAM-----AVEPTQIQLSKRWREIESKFAQFRR------- 1960
Cdd:TIGR02168  314 LERQLEelEAQLEELESKLDELAEELAELEEKLEELKEELESLeaeleELEAELEELESRLEELEEQLETLRSkvaqlel 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1961 -LNFAQIHTVREETMMVMTEDMpleisyvpstylTEITHVSQALLEVEQLLNAPDLCAKDFEDLFKQEESLKNIKDSLQQ 2039
Cdd:TIGR02168  394 qIASLNNEIERLEARLERLEDR------------RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEE 461
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2040 SSGRIDIIHSKKTAALQSAtpveRVKLQEALSQLDfqwekvnkMYKDRQGRFdrsvekwRRFHYDIKifnQWLTEAEQF- 2118
Cdd:TIGR02168  462 ALEELREELEEAEQALDAA----ERELAQLQARLD--------SLERLQENL-------EGFSEGVK---ALLKNQSGLs 519
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2119 ------LRKTQIPENWEHAKykwyLKELQDGIGQrqTVVRTLNATGEEI--IQQSSKTDASILQEKLgslnLRWQEVCKQ 2190
Cdd:TIGR02168  520 gilgvlSELISVDEGYEAAI----EAALGGRLQA--VVVENLNAAKKAIafLKQNELGRVTFLPLDS----IKGTEIQGN 589
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2191 LSDRKKRLEEQKNILSEFQRDLNEFVLWLEE-------ADNIASiplepgKEQQLKEKLEQVKLLVE--ELPLRQGILkq 2261
Cdd:TIGR02168  590 DREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDN------ALELAKKLRPGYRIVTLdgDLVRPGGVI-- 661
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2262 lneTGGPVlvsapispeeqdklenklkQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRN 2341
Cdd:TIGR02168  662 ---TGGSA-------------------KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK 719
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2342 QLEIYNQPNQEGPFDVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQpvkRKLEDLSSEWKAVNRLLQELRAKQPDLAP 2421
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE---ERLEEAEEELAEAEAEIEELEAQIEQLKE 796
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2422 GLTTIgasptqtvtlvtqpvvtkETAISKLEMpsslmlevpALADFNRAWTELTDwlslldqviksqrvmvgDLEDINEM 2501
Cdd:TIGR02168  797 ELKAL------------------REALDELRA---------ELTLLNEEAANLRE-----------------RLESLERR 832
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2502 IIKQKATMQDLEQRRPQLEELITAAQnlKNKTSNQEARTIITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAK 2581
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLA--AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
                          810
                   ....*....|....*.
gi 578837832  2582 EEAEQVLGQARAKLES 2597
Cdd:TIGR02168  911 SELRRELEELREKLAQ 926
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1824-2624 1.16e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1824 DNLQqRITDERKreEIKIKQQLLQT---KHNALKDLRSQRRKKALEIshqwyqYKRQADDLLKCLDDIEKKLASLpeprd 1900
Cdd:TIGR02168  186 ENLD-RLEDILN--ELERQLKSLERqaeKAERYKELKAELRELELAL------LVLRLEELREELEELQEELKEA----- 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1901 ERKIKEIDRELQKKKEELNAVRRQaeglsedgaamaveptQIQLSKRWREIESKFAQFRrlnfAQIHTVREETMMVMTED 1980
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLE----------------VSELEEEIEELQKELYALA----NEISRLEQQKQILRERL 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1981 MPLEISYVpstylteithvsQALLEVEQLLNAPDLCAKDFEDLFKQEESLKNIKDSLQQssgRIDIIHSKKTAALQSATP 2060
Cdd:TIGR02168  312 ANLERQLE------------ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA---ELEELEAELEELESRLEE 376
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2061 VERV--KLQEALSQLDFQWEKVNK---MYKDRQGRFDRSVEKWRrfhydikifnqwlTEAEQFLRKTQIPEnwehakykw 2135
Cdd:TIGR02168  377 LEEQleTLRSKVAQLELQIASLNNeieRLEARLERLEDRRERLQ-------------QEIEELLKKLEEAE--------- 434
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2136 yLKELQDGIGQRQTVVRTLNATGEEIIQQSSKTDASILQEKLGSLNLRWQEvcKQLSDRKKRLEEQKNILSEFQRDLNEF 2215
Cdd:TIGR02168  435 -LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL--AQLQARLDSLERLQENLEGFSEGVKAL 511
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2216 VLWLEEADNIA-----SIPLEPGKEQQLKEKLEQV--KLLVEEL-PLRQGILKQLNETGGPVLVSAPISPEEQDKLENKl 2287
Cdd:TIGR02168  512 LKNQSGLSGILgvlseLISVDEGYEAAIEAALGGRlqAVVVENLnAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGND- 590
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2288 kqtnlqwikvsRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQPNQEGPFDVKETEIA---- 2363
Cdd:TIGR02168  591 -----------REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVrpgg 659
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2364 VQAKQPDVEE--ILSKGQHLykeKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVTLVTQPV 2441
Cdd:TIGR02168  660 VITGGSAKTNssILERRREI---EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2442 VTKETAISKLEMPSSLMLEvpaLADFNRAWTELTDWLSLLDQVIKSQRVMVGDLE-DINEMIIKQKATMQDLEQRRPQLE 2520
Cdd:TIGR02168  737 RLEAEVEQLEERIAQLSKE---LTELEAEIEELEERLEEAEEELAEAEAEIEELEaQIEQLKEELKALREALDELRAELT 813
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2521 ELITAAQNLKNKTSNQEARTI-ITDRIERIQNQWDEVQEHLQ-------NRRQQLNEMLKDSTQWLEAKEEAEQVLGQAR 2592
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAaTERRLEDLEEQIEELSEDIEslaaeieELEELIEELESELEALLNERASLEEALALLR 893
                          810       820       830
                   ....*....|....*....|....*....|..
gi 578837832  2593 AKLESWKEgpyTVDAIQKKITETKQLAKDLRQ 2624
Cdd:TIGR02168  894 SELEELSE---ELRELESKRSELRRELEELRE 922
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
827-1039 1.23e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 46.28  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  827 FYNQLQQLEQMTTTAENWLKiQPTTPSEPTAIKSQLKICKDEVNRLSDLQPQIERLKIQSIALKEKGQGpmflDADFV-- 904
Cdd:cd00176     5 FLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP----DAEEIqe 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  905 ---AFTNHFKQVFSDVQAREKELQtifDTLPPMRYQETMSAIRTWVQQSETKLSiPQLSVTDYEIMEQRLGELQALQSSL 981
Cdd:cd00176    80 rleELNQRWEELRELAEERRQRLE---EALDLQQFFRDADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578837832  982 QEQQSGLYYLSTTVKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQM 1039
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1332-2352 1.45e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 1.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1332 INEELETfnsRWRELHEEAVRRQKLLEQSiqsAQETEKSLHLIQESLTFIDKQLAAYiadKVDAAQMPQEAQKIQSDLTS 1411
Cdd:TIGR02168  194 ILNELER---QLKSLERQAEKAERYKELK---AELRELELALLVLRLEELREELEEL---QEELKEAEEELEELTAELQE 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1412 HEISLEEMKKHNQGKEaaqrvlSQIDVAQKKLQDVSMKFrlfqkpanfeQRLQESKMILDEVKMHLPA-LETKSVEQEVV 1490
Cdd:TIGR02168  265 LEEKLEELRLEVSELE------EEIEELQKELYALANEI----------SRLEQQKQILRERLANLERqLEELEAQLEEL 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1491 QSQLNHcvnLYKSLSEVKSEVEMViktgrqivqkkqTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRK 1570
Cdd:TIGR02168  329 ESKLDE---LAEELAELEEKLEEL------------KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1571 EMNVLTEWLAATDMELTkrsAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKsITEVGEALKTVLGKKETLVEDKLSL--- 1647
Cdd:TIGR02168  394 QIASLNNEIERLEARLE---RLEDRRERLQQEIEELLKKLEEAELKELQAE-LEELEEELEELQEELERLEEALEELree 469
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1648 LNSNWIAVTSRAEEW------LNLLLEYQKHMETFDQNVDHITKWIIQADTLLD------ESEKKKPQQKEDVLKrlkAE 1715
Cdd:TIGR02168  470 LEEAEQALDAAERELaqlqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlseliSVDEGYEAAIEAALG---GR 546
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1716 LNDIRPKVDSTRDQAANLMA-NRGDHCRKLVEPQIS----ELNHRFAAISHRIKTGkasiPLKELEQFNSDIQKLLEPLE 1790
Cdd:TIGR02168  547 LQAVVVENLNAAKKAIAFLKqNELGRVTFLPLDSIKgteiQGNDREILKNIEGFLG----VAKDLVKFDPKLRKALSYLL 622
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1791 AEIqqgvnlkeedfnkdmnednegTVKELLQRGDNLQQRItdeRKREEIKIKQQLLQTKHNALKDLRSQRRKKALEishq 1870
Cdd:TIGR02168  623 GGV---------------------LVVDDLDNALELAKKL---RPGYRIVTLDGDLVRPGGVITGGSAKTNSSILE---- 674
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1871 wyqYKRQADDLlkclddiekklaslpeprdERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAamaveptqiQLSKRWRE 1950
Cdd:TIGR02168  675 ---RRREIEEL-------------------EEKIEELEEKIAELEKALAELRKELEELEEELE---------QLRKELEE 723
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1951 IESKFAQFR-RLNFAQIHTVREETMMVMTEDMPLEISYVPSTYLTEITHVSQALLEVEQLLNapdlcakdfedlfKQEES 2029
Cdd:TIGR02168  724 LSRQISALRkDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE-------------ELEAQ 790
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2030 LKNIKDSLQQSSGRIDIIHSKKTAalqsatpvervkLQEALSQLDFQWEKVNKMYKDRQGRFDRSVEKWRRFHYDIKIFN 2109
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTL------------LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2110 QWLTEAEQFLRKTQIP-ENW--EHAKYKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKtdasiLQEKLGSLNLRWQE 2186
Cdd:TIGR02168  859 AEIEELEELIEELESElEALlnERASLEEALALLRSELEELSEELRELESKRSELRRELEE-----LREKLAQLELRLEG 933
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2187 VckqlsdrKKRLEEQKNILSEFQRDLNEFVLWLEEADniasiplePGKEQQLKEKLEQVKLLVEELplrqgilkqlnetg 2266
Cdd:TIGR02168  934 L-------EVRIDNLQERLSEEYSLTLEEAEALENKI--------EDDEEEARRRLKRLENKIKEL-------------- 984
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2267 GPVlvsapispeeqdklenklkqtNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNhlllwlSPIRNQ-LEI 2345
Cdd:TIGR02168  985 GPV---------------------NLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID------REARERfKDT 1037

                   ....*..
gi 578837832  2346 YNQPNQE 2352
Cdd:TIGR02168 1038 FDQVNEN 1044
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2189-2624 1.57e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2189 KQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASiplepgKEQQLKEKLEQVKLLVEELPLRQgilkqlnetggp 2268
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA------ELEELREELEKLEKLLQLLPLYQ------------ 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2269 vlvsapispeEQDKLENKLKQTNLQWikvsRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSP-IRNQLEIYN 2347
Cdd:COG4717   133 ----------ELEALEAELAELPERL----EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLaTEEELQDLA 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2348 QPNQEGPFDVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQPvKRKLEDLSSEWKAVNRLLqELRAKQPDLAPGLTTIG 2427
Cdd:COG4717   199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL-EERLKEARLLLLIAAALL-ALLGLGGSLLSLILTIA 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2428 ASPTQTVTLVTQPVVTKETAISKLEMPSSLMLEVPALADF-NRAWTEL------------TDWLSLLDQVIKSQRVM--- 2491
Cdd:COG4717   277 GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELeEEELEELlaalglppdlspEELLELLDRIEELQELLrea 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2492 ------------------------VGDLEDINEmIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTIITDRIE 2547
Cdd:COG4717   357 eeleeelqleeleqeiaallaeagVEDEEELRA-ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELE 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2548 RIQNQWDEVQEHLQNRRQQLNE------MLKDSTQWLEAKEEAEQVLGQARAKLESWKegpyTVDAIQKKITETKQLAKD 2621
Cdd:COG4717   436 ELEEELEELEEELEELREELAEleaeleQLEEDGELAELLQELEELKAELRELAEEWA----ALKLALELLEEAREEYRE 511

                  ...
gi 578837832 2622 LRQ 2624
Cdd:COG4717   512 ERL 514
PRK01156 PRK01156
chromosome segregation protein; Provisional
1274-1842 1.66e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 47.59  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1274 LNEVEFKLKTTENipgGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDGGVM-DELINE---ELETFNSRWRELHEE 1349
Cdd:PRK01156  185 IDYLEEKLKSSNL---ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNlKSALNElssLEDMKNRYESEIKTA 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1350 AVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEIS---LEEMKKHNQGK 1426
Cdd:PRK01156  262 ESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIikkLSVLQKDYNDY 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1427 EAAQRVLSQIDVAQKKLQDVSMKFRLFQKpaNFEQ----RLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHcvnLYK 1502
Cdd:PRK01156  342 IKKKSRYDDLNNQILELEGYEMDYNSYLK--SIESlkkkIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNE---INV 416
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1503 SLSEVKSEVEMVIKTGRQIVQKKQ--TENPKEL--------------DERVTALKLHYNELGAKVTERKQQLEKCLKLSR 1566
Cdd:PRK01156  417 KLQDISSKVSSLNQRIRALRENLDelSRNMEMLngqsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREIEIEVKDID 496
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1567 KMRKEMNVLTEWLAATDMEltkrsavegmpsNLDSEVAWGKATQKEIEKQKVHLKSITEvgealktvlgkKETLVEDKLS 1646
Cdd:PRK01156  497 EKIVDLKKRKEYLESEEIN------------KSINEYNKIESARADLEDIKIKINELKD-----------KHDKYEEIKN 553
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1647 LLNSNWIA-VTSRAEEWLNLLLEYQK-HMETFDQNVDHITKWIIQADTLLDESEKKKPQQK---EDVLKRLKAELNDIRP 1721
Cdd:PRK01156  554 RYKSLKLEdLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyiDKSIREIENEANNLNN 633
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1722 KVDSTRDQAANLMANRGdhcrklvepQISELNHRFAAISHRIKTgkasipLKELEQFNSDIQKLLEPLEAEIQqgvnlke 1801
Cdd:PRK01156  634 KYNEIQENKILIEKLRG---------KIDNYKKQIAEIDSIIPD------LKEITSRINDIEDNLKKSRKALD------- 691
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 578837832 1802 eDFNKDMNEdNEGTVKELLQRGDNLQQRITDERKREEIKIK 1842
Cdd:PRK01156  692 -DAKANRAR-LESTIEILRTRINELSDRINDINETLESMKK 730
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
132-225 1.74e-04

second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409164  Cd Length: 118  Bit Score: 44.00  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  132 LLSWVRQSTrnyPQVNVINFTTSWSDGLALNALIHSHR----PDLFDWNSvvcqQSATQRLEHAFNIARYQLGIEKLLDP 207
Cdd:cd21315    21 LLGWIQSKV---PDLPITNFTNDWNDGKAIGALVDALApglcPDWEDWDP----KDAVKNAKEAMDLAEDWLDVPQLIKP 93
                          90
                  ....*....|....*...
gi 578837832  208 EDVDTTYPDKKSILMYIT 225
Cdd:cd21315    94 EEMVNPKVDELSMMTYLS 111
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
822-925 2.17e-04

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 43.08  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   822 NNIIAFYNQLQQLEQMTTTAENWLKIQPTtPSEPTAIKSQLKICKDEVNRLSDLQPQIERLKIQSIAL-KEKGQGPMFLD 900
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDY-GKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLiDEGHYASEEIQ 79
                           90       100
                   ....*....|....*....|....*
gi 578837832   901 ADFVAFTNHFKQVFSDVQAREKELQ 925
Cdd:pfam00435   80 ERLEELNERWEQLLELAAERKQKLE 104
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
4-116 2.43e-04

third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409178  Cd Length: 118  Bit Score: 43.44  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    4 EREDVQKKTFTKWVNAqfskFG-KQHIENLFSDLQDGRRLLDLLEGLT-------GQKLPKEKGSTRVHALNNVNKALRV 75
Cdd:cd21329     2 EGESSEERTFRNWMNS----LGvNPYVNHLYSDLCDALVIFQLYEMTRvpvdwghVNKPPYPALGGNMKKIENCNYAVEL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 578837832   76 LQNN-NVDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVkNVM 116
Cdd:cd21329    78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTL-NVL 118
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
61-107 2.68e-04

first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409143  Cd Length: 125  Bit Score: 43.59  E-value: 2.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837832   61 TRVHALNNvnkaLRVLQNNNV----------DLVNIGSTDIVDGNHKLTLGLIWNII 107
Cdd:cd21294    70 RKNKPLNN----FQMIENNNIvinsakaigcSVVNIGAGDIIEGREHLILGLIWQII 122
SPEC smart00150
Spectrin repeats;
1488-1559 3.00e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 42.70  E-value: 3.00e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578837832   1488 EVVQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKkQTENPKELDERVTALKLHYNELGAKVTERKQQLE 1559
Cdd:smart00150   31 ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEERLEELNERWEELKELAEERRQKLE 101
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
968-1740 3.63e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.89  E-value: 3.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   968 EQRLGELQALQSSLQEQQSGLYYLSTT-----VKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQMNKL 1042
Cdd:pfam02463  244 ELLRDEQEEIESSKQEIEKEEEKLAQVlkenkEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1043 RKIQNHIQTLKKWMAEVDVFLKEEWPALGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEFASRLETE 1122
Cdd:pfam02463  324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1123 LKELNTQWDHMCQQVYARKEALKGGLEKTVSLQK--DLSEMHEWMTQAEEEYLERDFEYKTPDELQKAVEEMKRAKEEAQ 1200
Cdd:pfam02463  404 EKEAQLLLELARQLEDLLKEEKKEELEILEEEEEsiELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQ 483
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1201 QKEAK----VKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKANKWLNE 1276
Cdd:pfam02463  484 EQLELllsrQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEER 563
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1277 VEFKLKTTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQtlTDGGVMDELINEELETFNSRWRELHEEAVRRQKL 1356
Cdd:pfam02463  564 QKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQ--LDKATLEADEDDKRAKVVEGILKDTELTKLKESA 641
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1357 LEQSIQSaQETEKSLHLIQESLTFIDKQLAayIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKKHNQGKEaaqrvLSQI 1436
Cdd:pfam02463  642 KAKESGL-RKGVSLEEGLAEKSEVKASLSE--LTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREK-----EELK 713
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1437 DVAQKKLQDVSMKFRLFQKPANFEQRLQESKmiLDEVKMHLPALETKSVEQEVVQSQLnhcvnlyksLSEVKSEVEMVIK 1516
Cdd:pfam02463  714 KLKLEAEELLADRVQEAQDKINEELKLLKQK--IDEEEEEEEKSRLKKEEKEEEKSEL---------SLKEKELAEEREK 782
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1517 TGRQIVQKKQTENPKELDERVTALKlhynelgAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAvegmp 1596
Cdd:pfam02463  783 TEKLKVEEEKEEKLKAQEEELRALE-------EELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEK----- 850
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1597 SNLDSEVAWGKATQKEIEKQKVHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETF 1676
Cdd:pfam02463  851 LAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEIL 930
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578837832  1677 DQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANRGDH 1740
Cdd:pfam02463  931 LKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDE 994
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
3305-3351 4.04e-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: 4.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578837832 3305 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRvakgHKMHYPMVEY 3351
Cdd:cd02339     3 CDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDK----HDLEHRFYRY 45
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
15-106 4.22e-04

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409067  Cd Length: 114  Bit Score: 42.67  E-value: 4.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   15 KWVNAQFSKFGKQH--IENLFSDLQDGRRLLDLLEGLTGQKLPKEKGStrvHALNNVNKALR---VLQnnNVDLVN---- 85
Cdd:cd21218    17 RWVNYHLKKAGPTKkrVTNFSSDLKDGEVYALLLHSLAPELCDKELVL---EVLSEEDLEKRaekVLQ--AAEKLGckyf 91
                          90       100
                  ....*....|....*....|.
gi 578837832   86 IGSTDIVDGNHKLTLGLIWNI 106
Cdd:cd21218    92 LTPEDIVSGNPRLNLAFVATL 112
SPEC smart00150
Spectrin repeats;
2565-2677 4.79e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 41.93  E-value: 4.79e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   2565 QQLNEMLKDSTQWLEAKEeaeqvlgqaraKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDyS 2644
Cdd:smart00150    1 QQFLRDADELEAWLEEKE-----------QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-G 68
                            90       100       110
                    ....*....|....*....|....*....|...
gi 578837832   2645 ADDTRKVHMITENINASWRSIHKRVSEREAALE 2677
Cdd:smart00150   69 HPDAEEIEERLEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
1154-1254 5.94e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 41.93  E-value: 5.94e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   1154 LQKDLSEMHEWMTQAEEeYLERDFEYKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPVAQEaLKKELE 1233
Cdd:smart00150    3 FLRDADELEAWLEEKEQ-LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE-IEERLE 80
                            90       100
                    ....*....|....*....|.
gi 578837832   1234 TLTTNYQWLCTRLNGKCKTLE 1254
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
9-107 6.45e-04

first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409172  Cd Length: 145  Bit Score: 42.72  E-value: 6.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    9 QKKTFTKWVNAQFSKFGK-QHI-------ENLFSDLQDGR---RLLDLLEGLT-GQKLPKEKGSTRVHALNNVNKALRVL 76
Cdd:cd21323    25 EKVAFVNWINKALEGDPDcKHVvpmnptdESLFKSLADGIllcKMINLSQPDTiDERAINKKKLTPFTISENLNLALNSA 104
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578837832   77 QNNNVDLVNIGSTDIVDGNHKLTLGLIWNII 107
Cdd:cd21323   105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQII 135
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
3305-3350 6.46e-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: 6.46e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578837832 3305 CNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVE 3350
Cdd:cd02345     3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
921-1465 6.55e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 6.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  921 EKELQTIFDTLPPMRyqETMSAIRTWVQQ-SETKLSIPQLSVTdyeiMEQRLGELQALQSSLQEQQSGLYYLSTTVKEMS 999
Cdd:PRK03918  206 LREINEISSELPELR--EELEKLEKEVKElEELKEEIEELEKE----LESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1000 KKAP---------------SEISRKYQSEFEEIEGRWKKLSSQ---LVEHCQKLEEQMNKLRKIQNHIQTLKKWMAEvdv 1061
Cdd:PRK03918  280 EKVKelkelkekaeeyiklSEFYEEYLDELREIEKRLSRLEEEingIEERIKELEEKEERLEELKKKLKELEKRLEE--- 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1062 fLKEEWPALGDSEILKKQLKQCRLLVSDIqtiqpSLNSVNEGGQKIKNEAEpefasRLETELKELNTQWDHMCQQVYARK 1141
Cdd:PRK03918  357 -LEERHELYEEAKAKKEELERLKKRLTGL-----TPEKLEKELEELEKAKE-----EIEEEISKITARIGELKKEIKELK 425
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1142 EA---LKGGLEKTVSLQKDLSEMH--EWMTQAEEEYLERDFEYKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSV 1216
Cdd:PRK03918  426 KAieeLKKAKGKCPVCGRELTEEHrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQL 505
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1217 IAqappvAQEALKK----ELETLTTNYQWLCTRLN---GKCKTLEEVwacwhelLSYLEKANKWLNEVEFKLKTTEnipg 1289
Cdd:PRK03918  506 KE-----LEEKLKKynleELEKKAEEYEKLKEKLIklkGEIKSLKKE-------LEKLEELKKKLAELEKKLDELE---- 569
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1290 gaEEISEVLDSLENLMRHSEDNpnqirilaqtltdggvmDELINEELETFNSRWREL---HEEAVRRQKLLEQSIQSAQE 1366
Cdd:PRK03918  570 --EELAELLKELEELGFESVEE-----------------LEERLKELEPFYNEYLELkdaEKELEREEKELKKLEEELDK 630
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1367 TEKSLHLIQESLTFIDKQLAA--YIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKKHnqgKEAAQRVLSQIDVAQKKLQ 1444
Cdd:PRK03918  631 AFEELAETEKRLEELRKELEEleKKYSEEEYEELREEYLELSRELAGLRAELEELEKR---REEIKKTLEKLKEELEERE 707
                         570       580
                  ....*....|....*....|.
gi 578837832 1445 DVSMKFRLFQKPANFEQRLQE 1465
Cdd:PRK03918  708 KAKKELEKLEKALERVEELRE 728
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
1660-1926 8.88e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 45.33  E-value: 8.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1660 EEWLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDEsekkKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANRGD 1739
Cdd:COG5185   232 EEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLE----KLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDI 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1740 hcrKLVEPQISELNHRFAAISHRIK-----TGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKE-EDFNKDMNEDN- 1812
Cdd:COG5185   308 ---KKATESLEEQLAAAEAEQELEEskretETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSEELDSFKd 384
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1813 --EGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQtkhnaLKDLRSQRRKKALEIShqwyQYKRQADDLLKCLDDIEK 1890
Cdd:COG5185   385 tiESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQ-----IEELQRQIEQATSSNE----EVSKLLNELISELNKVMR 455
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 578837832 1891 KLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAE 1926
Cdd:COG5185   456 EADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIE 491
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
2478-2617 9.31e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.20  E-value: 9.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2478 LSLLDQVIKSQRVMVG-DLEDINEMIikqkatmQDLEQRRPQLEELITAAQNLKNKTsnqeartiitdriERIQNQWDEV 2556
Cdd:PRK00409  497 LGLPENIIEEAKKLIGeDKEKLNELI-------ASLEELERELEQKAEEAEALLKEA-------------EKLKEELEEK 556
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578837832 2557 QEHLQNRRQQLNEMLKDSTQWL--EAKEEAEQVLGQARaklESWKEGPYTVDAiqKKITETKQ 2617
Cdd:PRK00409  557 KEKLQEEEDKLLEEAEKEAQQAikEAKKEADEIIKELR---QLQKGGYASVKA--HELIEARK 614
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
897-1806 1.11e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 45.04  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   897 MFLDADFVAFTNHFKQVFSDVQAREKELQTIFDTLPpmRYQETMSAIRTWVQQSETKLSIPQLSVTDYEI----MEQRLG 972
Cdd:TIGR00606  178 IFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLK--QYKEKACEIRDQITSKEAQLESSREIVKSYENeldpLKNRLK 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   973 ELQALQSSLQEQQSGLYYLSTTVKEMsKKAPSEISRK----YQSEFEEIEGRWKKLSSQLVEHCQKLEEQMNKLRKIQNH 1048
Cdd:TIGR00606  256 EIEHNLSKIMKLDNEIKALKSRKKQM-EKDNSELELKmekvFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKE 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1049 IQTLKKWMAEvdvFLKEEWPALGDSEILKKQLKQCRLLVSDIQTiQPSLNSVNEGG---QKIKN---------EAEPEFA 1116
Cdd:TIGR00606  335 RRLLNQEKTE---LLVEQGRLQLQADRHQEHIRARDSLIQSLAT-RLELDGFERGPfseRQIKNfhtlvierqEDEAKTA 410
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1117 SRLETELKELNTQWDHMCQQVYARKEALKGGLE-KTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQKAVEEMKRA 1195
Cdd:TIGR00606  411 AQLCADLQSKERLKQEQADEIRDEKKGLGRTIElKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKA 490
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1196 KEEA--QQKEAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTR--LNGKCKTLEEVWACWHELLSYL---- 1267
Cdd:TIGR00606  491 EKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKdkMDKDEQIRKIKSRHSDELTSLLgyfp 570
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1268 --EKANKWLNEVEFKLKTTEnipggaeeisEVLDSLENLMRHSEDNPNQIRILAQTLT------DGGVMDELINEELETF 1339
Cdd:TIGR00606  571 nkKQLEDWLHSKSKEINQTR----------DRLAKLNKELASLEQNKNHINNELESKEeqlssyEDKLFDVCGSQDEESD 640
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1340 NSRWRELHEEAVRRQKLL-------EQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAAQM-PQEAQKIQSDLTS 1411
Cdd:TIGR00606  641 LERLKEEIEKSSKQRAMLagatavySQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLaPDKLKSTESELKK 720
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1412 HEISLEEMKKHNQGKEAA-QRVLSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKM--------------ILDEVKMH 1476
Cdd:TIGR00606  721 KEKRRDEMLGLAPGRQSIiDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMpeeesakvcltdvtIMERFQME 800
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1477 LPALEtKSVEQEVVQSQlnhCVNLYKSLSEVKSEVEMVIKTGRQIVQK---------KQTENPKELDERVTALKLHYNEL 1547
Cdd:TIGR00606  801 LKDVE-RKIAQQAAKLQ---GSDLDRTVQQVNQEKQEKQHELDTVVSKielnrkliqDQQEQIQHLKSKTNELKSEKLQI 876
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1548 GAKVTERKQQLEKCLKLSRKMRKemnVLTEWLAATDMELTKRSAVEGMPSNlDSEVAWGKATQKEIEKQKVHL--KSITE 1625
Cdd:TIGR00606  877 GTNLQRRQQFEEQLVELSTEVQS---LIREIKDAKEQDSPLETFLEKDQQE-KEELISSKETSNKKAQDKVNDikEKVKN 952
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1626 VGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVD--HITKWIIQAD-TLLDESEKKKP 1702
Cdd:TIGR00606  953 IHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqKIQERWLQDNlTLRKRENELKE 1032
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1703 ----------QQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANRGDHCR--KLVEPQISELNHRFAAISHRiktgKASI 1770
Cdd:TIGR00606 1033 veeelkqhlkEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKeiKHFKKELREPQFRDAEEKYR----EMMI 1108
                          970       980       990
                   ....*....|....*....|....*....|....*.
gi 578837832  1771 PLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNK 1806
Cdd:TIGR00606 1109 VMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINK 1144
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2284-3039 1.15e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2284 ENKLKQTNLQWIKVSRALpekqGEIEAQIKDLG-QLEK--KLEDLEEQLNHLLLWLSPIR-----NQLEIYNQPNQEGPF 2355
Cdd:TIGR02168  178 ERKLERTRENLDRLEDIL----NELERQLKSLErQAEKaeRYKELKAELRELELALLVLRleelrEELEELQEELKEAEE 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2356 DVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQpvkRKLEDLSSEWKAVNRLLQELRAKQPDLapglttigasptqtvt 2435
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQ---KELYALANEISRLEQQKQILRERLANL---------------- 314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2436 lvtqpvvtkETAISKLEMpsslmlevpALADFNRAWTELTDWLSLLDQVIKSQRVmvgDLEDINEMIIKQKATMQDLEQR 2515
Cdd:TIGR02168  315 ---------ERQLEELEA---------QLEELESKLDELAEELAELEEKLEELKE---ELESLEAELEELEAELEELESR 373
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2516 RPQLEELITAAQNLKNKTSNQEARtiITDRIERIQNQWDEVQEHLQNRRQQLNEMLK--DSTQWLEAK---EEAEQVLGQ 2590
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLELQIAS--LNNEIERLEARLERLEDRRERLQQEIEELLKklEEAELKELQaelEELEEELEE 451
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2591 ARAKLESWKEGPYTVDA-IQKKITETKQLAKDLRQWQTNVDVANDLaLKLLRDYSADdtrkvhmITENINASWR--SIHK 2667
Cdd:TIGR02168  452 LQEELERLEEALEELREeLEEAEQALDAAERELAQLQARLDSLERL-QENLEGFSEG-------VKALLKNQSGlsGILG 523
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2668 RVSER-------EAALE---------------ETHRLLQQF------------PLDL-----------------EKFLAW 2696
Cdd:TIGR02168  524 VLSELisvdegyEAAIEaalggrlqavvvenlNAAKKAIAFlkqnelgrvtflPLDSikgteiqgndreilkniEGFLGV 603
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2697 LTEAETT-----------------ANVLQDATRKERLL-------------------------EDSKGVKELMKQWQDLQ 2734
Cdd:TIGR02168  604 AKDLVKFdpklrkalsyllggvlvVDDLDNALELAKKLrpgyrivtldgdlvrpggvitggsaKTNSSILERRREIEELE 683
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2735 GEIEAHTDVYHNLDENSQKILRSL-EGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELLVWL 2813
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELeELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2814 QLKDDELsrqapiggdfpavQKQNDVHRAFKRELKTKEPVIMSTLEtvRIFLTEQPLEGLEKLYQEPRE-----LPPEER 2888
Cdd:TIGR02168  764 EELEERL-------------EEAEEELAEAEAEIEELEAQIEQLKE--ELKALREALDELRAELTLLNEeaanlRERLES 828
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2889 AQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLRELQEATDELDLKLRQAEVIKGSWQPVGDLLIDSLQDHLE 2968
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2969 KVKALRGEIAPLKEnvsHVNDLARQLTTLGIQLspynLSTLEDLNTRWKL-LQVAV-------------EDRVRQLHEAH 3034
Cdd:TIGR02168  909 KRSELRRELEELRE---KLAQLELRLEGLEVRI----DNLQERLSEEYSLtLEEAEalenkieddeeeaRRRLKRLENKI 981

                   ....*
gi 578837832  3035 RDFGP 3039
Cdd:TIGR02168  982 KELGP 986
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2512-3037 2.03e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2512 LEQRRPQLEELITAAQNLKNKTSNQEAR-TIITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQ 2590
Cdd:PRK03918  174 IKRRIERLEKFIKRTENIEELIKEKEKElEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2591 ARAKLESWKEgpytvdaIQKKITETKQLAKDLRQwqtnvdvaNDLALKLLRDYsADDTRKVHMITENINASWRSIHKRVS 2670
Cdd:PRK03918  254 KRKLEEKIRE-------LEERIEELKKEIEELEE--------KVKELKELKEK-AEEYIKLSEFYEEYLDELREIEKRLS 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2671 EREAALEETHRLLQqfplDLEKflawlteaettanvlqdatRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDEN 2750
Cdd:PRK03918  318 RLEEEINGIEERIK----ELEE-------------------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2751 SQkiLRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELlvwlqlkdDELSRQAPIGGDF 2830
Cdd:PRK03918  375 ER--LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL--------KKAKGKCPVCGRE 444
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2831 PAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEqpLEGLEKLYQEPRELPPEERaqnvtrlLRKQAEEVNTEWEKL 2910
Cdd:PRK03918  445 LTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKE--LRELEKVLKKESELIKLKE-------LAEQLKELEEKLKKY 515
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2911 NLhsadwqrkidETLERLRELQEATDELDLKLRQAevikgswqpvgdllIDSLQDHLEKVKALRGEIAPLKENvshVNDL 2990
Cdd:PRK03918  516 NL----------EELEKKAEEYEKLKEKLIKLKGE--------------IKSLKKELEKLEELKKKLAELEKK---LDEL 568
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 578837832 2991 ARQLTTLGIQLSPYNLSTLEDLntrwkllqvavEDRVRQLHEAHRDF 3037
Cdd:PRK03918  569 EEELAELLKELEELGFESVEEL-----------EERLKELEPFYNEY 604
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2544-2759 2.11e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2544 DRIERIQNQWD---EVQEHLQNRRQQ---LNEMLKDSTQWLEAKEEAEQvLGQARAKLESWKEGpYTVDAIQKKIT---- 2613
Cdd:COG4913   225 EAADALVEHFDdleRAHEALEDAREQielLEPIRELAERYAAARERLAE-LEYLRAALRLWFAQ-RRLELLEAELEelra 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2614 ETKQLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENInASWRSIHKRVSEREAALEE-THRLLQQFPLDLEK 2692
Cdd:COG4913   303 ELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREI-ERLERELEERERRRARLEAlLAALGLPLPASAEE 381
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578837832 2693 FLAWLTEAETTANVLQDATRK--ERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRSLE 2759
Cdd:COG4913   382 FAALRAEAAALLEALEEELEAleEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
2152-2348 2.25e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2152 RTLNATGEEIIQQSSKTDASILQEKLGSLNlrwqevcKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIple 2231
Cdd:COG3206   152 AVANALAEAYLEQNLELRREEARKALEFLE-------EQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQL--- 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 2232 pgkeQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSAPISPEEQDkLENKLKQTNLQWIKVS----------RAL 2301
Cdd:COG3206   222 ----SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-LRAQLAELEAELAELSarytpnhpdvIAL 296
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578837832 2302 PEKQGEIEAQIKDlgQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQ 2348
Cdd:COG3206   297 RAQIAALRAQLQQ--EAQRILASLEAELEALQAREASLQAQLAQLEA 341
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
710-1388 2.26e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.94  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   710 SEIRKRLDVDITELHSWITRSEAVLQSPEfaifrkegnfSDLKEKVNAIEREKaEKFRKLQDASRSAQALVEQMVNEgvN 789
Cdd:pfam05483   77 SRLYSKLYKEAEKIKKWKVSIEAELKQKE----------NKLQENRKIIEAQR-KAIQELQFENEKVSLKLEEEIQE--N 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   790 ADSIKQ--ASEQLNSRWIEFCQLLSERLNWLEYQNN-----IIAFYNQLQQL----EQMTTTAENW-LKIQPTTPSEPTA 857
Cdd:pfam05483  144 KDLIKEnnATRHLCNLLKETCARSAEKTKKYEYEREetrqvYMDLNNNIEKMilafEELRVQAENArLEMHFKLKEDHEK 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   858 IKSQLKICKDEVNrlsDLQPQIERLKIQSIALKEKGQGPMFLDADFVAFTNHFKQVFSDVQAREKELQTIFDTLPPMRYQ 937
Cdd:pfam05483  224 IQHLEEEYKKEIN---DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED 300
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   938 ETMSAIRTWVQQSETKLSIPQLSVTDYEIMEQRLGELQALQSSLQEQQSGLYYLSTTVKEMSkkapsEISRKYQSEFEEI 1017
Cdd:pfam05483  301 IKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE-----ELLRTEQQRLEKN 375
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1018 EGRWKKLSSQLVEHCQKLEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEWPALGDSEILKKQLKQCRLLVS----DIQTI 1093
Cdd:pfam05483  376 EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQarekEIHDL 455
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1094 QPSLNSVNEGGQKIKNEAEpEFASRLETElKELNTQWDHMCQQV-YARKEALKGGLEKTVSLQKDLSEMHEwmTQAEEEY 1172
Cdd:pfam05483  456 EIQLTAIKTSEEHYLKEVE-DLKTELEKE-KLKNIELTAHCDKLlLENKELTQEASDMTLELKKHQEDIIN--CKKQEER 531
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1173 LERDFEYKTPDELQKAvEEMKRAKEEAQQK--EAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNyqwLCTRLNGKC 1250
Cdd:pfam05483  532 MLKQIENLEEKEMNLR-DELESVREEFIQKgdEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN---LKKQIENKN 607
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1251 KTLEEVWACWHELLSYLEKANKWLNEVEFKLKTTE-NIPGGAEEISEVLDSLEnlmrhsednpnqirilaQTLTDGGVMD 1329
Cdd:pfam05483  608 KNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElELASAKQKFEEIIDNYQ-----------------KEIEDKKISE 670
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 578837832  1330 ELINEELEtfnsRWRELHEEAVRRQKLLEQSIQsaqetekslHLIQESLTFIDKQLAAY 1388
Cdd:pfam05483  671 EKLLEEVE----KAKAIADEAVKLQKEIDKRCQ---------HKIAEMVALMEKHKHQY 716
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
1260-1926 2.56e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.94  E-value: 2.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1260 WHELLSYLEKANKWLNEVEFKLKTTENipgGAEEISEVLDSLENLMRHSEDNPNQIRI-LAQTLTDGgvmDELINEELET 1338
Cdd:pfam05483   80 YSKLYKEAEKIKKWKVSIEAELKQKEN---KLQENRKIIEAQRKAIQELQFENEKVSLkLEEEIQEN---KDLIKENNAT 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1339 fnSRWRELHEEAVRRQKllEQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQ-KIQSDLTSHEISLE 1417
Cdd:pfam05483  154 --RHLCNLLKETCARSA--EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEE 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1418 EMKKHNQGKE-AAQRVLSQIDVAQKKLQDVSmkFRLFQKPANFEQRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNH 1496
Cdd:pfam05483  230 EYKKEINDKEkQVSLLLIQITEKENKMKDLT--FLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQR 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1497 CVNLYKSLSEvksEVEMVIKTGRQIVQKKQTENpKELDERVTALKLHYNELGAKVTerkqQLEKCLKlSRKMRKEMNvlT 1576
Cdd:pfam05483  308 SMSTQKALEE---DLQIATKTICQLTEEKEAQM-EELNKAKAAHSFVVTEFEATTC----SLEELLR-TEQQRLEKN--E 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1577 EWLAATDMELTKRSavegmpSNLDSEVAWGKATQKEIEKqkvhlksitevgeaLKTVLGKKETLVEDKlSLLNSNWIAVT 1656
Cdd:pfam05483  377 DQLKIITMELQKKS------SELEEMTKFKNNKEVELEE--------------LKKILAEDEKLLDEK-KQFEKIAEELK 435
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1657 SRAEEWLNLLLEYQKHMETFDQNVdhitkwiiqadTLLDESEKKKPQQKEDVLKRLKAElndirpKVDSTRDQAanlman 1736
Cdd:pfam05483  436 GKEQELIFLLQAREKEIHDLEIQL-----------TAIKTSEEHYLKEVEDLKTELEKE------KLKNIELTA------ 492
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1737 rgdHCRKLvepqiselnhrfaAISHRIKTGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNkdMNEDNEGTV 1816
Cdd:pfam05483  493 ---HCDKL-------------LLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN--LRDELESVR 554
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1817 KELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLP 1896
Cdd:pfam05483  555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
                          650       660       670
                   ....*....|....*....|....*....|
gi 578837832  1897 EPRDERKIKEIDRELQKKKEELNAVRRQAE 1926
Cdd:pfam05483  635 EIKVNKLELELASAKQKFEEIIDNYQKEIE 664
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
9-106 2.62e-03

calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409134  Cd Length: 121  Bit Score: 40.72  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832    9 QKKTFTKWVNAQFSKFG-KQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKG--STRVHALNNVNKALRVLQNNNVDLVN 85
Cdd:cd21285    11 DKQIYTDWANHYLAKSGhKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGINIQG 90
                          90       100
                  ....*....|....*....|.
gi 578837832   86 IGSTDIVDGNHKLTLGLIWNI 106
Cdd:cd21285    91 LSAEEIRNGNLKAILGLFFSL 111
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
3307-3349 2.72e-03

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: 2.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578837832 3307 ICKEC--PIIGFRYRSLKHFNYDICQSCffsgrVAKG-HKMHyPMV 3349
Cdd:cd02340     2 ICDGCqgPIVGVRYKCLVCPDYDLCESC-----EAKGvHPEH-AML 41
PTZ00121 PTZ00121
MAEBL; Provisional
1390-1926 3.54e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1390 ADKVDAAQMPQEAQKIQSDLTSHEI-SLEEMKKHNQGK--EAAQRVLSQIDVAQ-------KKLQDVSmKFRLFQKPANF 1459
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEVrKAEELRKAEDARkaEAARKAEEERKAEEarkaedaKKAEAVK-KAEEAKKDAEE 1241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1460 EQRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQ--KKQTENPKELDE-- 1535
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADeaKKKAEEAKKADEak 1321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1536 -RVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIE 1614
Cdd:PTZ00121 1322 kKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1615 KQKVHLKSITEVGEALKTVLGKKETlVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVDHITKwiiqADTLL 1694
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK----ADEAK 1476
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1695 DESEKKKpqqKEDVLKRlKAElnDIRPKVDSTRDQAANLM----ANRGDHCRKLVEPQISElNHRFAAISHRIKTGKASI 1770
Cdd:PTZ00121 1477 KKAEEAK---KADEAKK-KAE--EAKKKADEAKKAAEAKKkadeAKKAEEAKKADEAKKAE-EAKKADEAKKAEEKKKAD 1549
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1771 PLKELEQFN--SDIQKLLEPLEAEIQQGVNLKEEDFNKDMNEDNEGTVKELLQRGDNLQQRitDERKREEIKIKQQLLQT 1848
Cdd:PTZ00121 1550 ELKKAEELKkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE--EAKKAEEAKIKAEELKK 1627
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1849 KHNALKDLRSQRRKKALEishqwyqyKRQADDLLKCLDDIEKKLASLP--EPRDERKIKEIDRELQKKKEELNAVRRQAE 1926
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEE--------KKKAEELKKAEEENKIKAAEEAkkAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
SPEC smart00150
Spectrin repeats;
2801-2922 3.63e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 39.62  E-value: 3.63e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   2801 RLHLSLQELLVWLQLKDDELSrQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEklyqep 2880
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE------ 74
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 578837832   2881 relppeeraqnvtrlLRKQAEEVNTEWEKLNLHSADWQRKID 2922
Cdd:smart00150   75 ---------------IEERLEELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1109-1379 3.81e-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: 43.51  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1109 NEAEPEFaSRLETELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDfeyktpDELQKA 1188
Cdd:TIGR02168  701 AELRKEL-EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE------ERLEEA 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1189 VEEMKRAKEEAQQKEAKVKLLTESVNSVIAQappvaQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLE 1268
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREA-----LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1269 KANKWLNEVEFKLKTTENipgGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDG-----GVMDEL------------ 1331
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEE---LIEELESELEALLNERASLEEALALLRSELEELSEElreleSKRSELrreleelrekla 925
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1332 ------------INEELETFNSRWRELHEEAVRRQKLLEQSIQSAQEtekSLHLIQESLT 1379
Cdd:TIGR02168  926 qlelrleglevrIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR---RLKRLENKIK 982
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
953-1539 3.87e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.42  E-value: 3.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   953 KLSIPQLSVTDYEIMEQRLGELQALQSSLQEQQSGLYYLSTtvkemskkapseisrkyQSEFEEIEGRWKKLSSQLVEHC 1032
Cdd:TIGR00618  207 TLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQ-----------------KREAQEEQLKKQQLLKQLRARI 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1033 QKLEEQMNKLRKIQNHIQTLKKWMAEVDVflkeewpalgdseilKKQLKQCRllvSDIQTIQPSLnsvneggQKIKNEAE 1112
Cdd:TIGR00618  270 EELRAQEAVLEETQERINRARKAAPLAAH---------------IKAVTQIE---QQAQRIHTEL-------QSKMRSRA 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1113 PEFASRLETELKELNTQwdhmcqqvyarkealkgglEKTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQKaVEEM 1192
Cdd:TIGR00618  325 KLLMKRAAHVKQQSSIE-------------------EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQH-IHTL 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1193 KRAKEEAQQKEAKVKLLTESVNSVIAQAPP--VAQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKA 1270
Cdd:TIGR00618  385 QQQKTTLTQKLQSLCKELDILQREQATIDTrtSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES 464
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1271 NKWLNEVEFKLKTTENIPGGAEEISEV-------LDSLENLMRHSEDNPNQIRILAQTL-TDGGVMDELINEEL---ETF 1339
Cdd:TIGR00618  465 AQSLKEREQQLQTKEQIHLQETRKKAVvlarlleLQEEPCPLCGSCIHPNPARQDIDNPgPLTRRMQRGEQTYAqleTSE 544
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1340 NSRWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQES------LTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHE 1413
Cdd:TIGR00618  545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSkedipnLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1414 ISLEEMKKHNQ-----------GKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKMHLPALET 1482
Cdd:TIGR00618  625 QDLQDVRLHLQqcsqelalkltALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQT 704
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578837832  1483 KSVEQEVVQSQLNHCVN-LYKSLSEVKSEVEMVIKTGRQIVQKKQTENPKELDERVTA 1539
Cdd:TIGR00618  705 LLRELETHIEEYDREFNeIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEA 762
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1033-1474 4.09e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1033 QKLEEQMNKLRKIQ--------NHIQTLKKWMAEVDVFLKEEWPALGDSEILKKQLKQCRLLVSDIQTIQPSLNsvnegg 1104
Cdd:COG4717    49 ERLEKEADELFKPQgrkpelnlKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE------ 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1105 QKIKNEAEPEFASRLETELKELNTQWDhmcqQVYARKEALKGGLEKTVSLQKDLSEmhewmTQAEEEYLERDFEYKTPDE 1184
Cdd:COG4717   123 KLLQLLPLYQELEALEAELAELPERLE----ELEERLEELRELEEELEELEAELAE-----LQEELEELLEQLSLATEEE 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1185 LQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPVAQEAL-KKELETLTTNYQWLCTR-----LNGKCKTLEEVWA 1258
Cdd:COG4717   194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEaAALEERLKEARLLLLIAaallaLLGLGGSLLSLIL 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1259 CWHELLSYLEKANKWLNEVEFKLKTTENIPGGAEEISEVLDSLENlmrhsednpnqiRILAQTLTDGGVMDELINEELET 1338
Cdd:COG4717   274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEE------------EELEELLAALGLPPDLSPEELLE 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832 1339 FNSRWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDkQLAAYIADKVDAAQMPQEAQKIQSDLTSHEISLEE 1418
Cdd:COG4717   342 LLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE-ELRAALEQAEEYQELKEELEELEEQLEELLGELEE 420
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578837832 1419 ----------MKKHNQGKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVK 1474
Cdd:COG4717   421 llealdeeelEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELR 486
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
552-819 4.39e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 41.66  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  552 KWQRLTEEQCLFSAWLSEKEDAVNKIHTTgfKDQNEMLSSLQKLAVLKADLEKKKQSMGKLYSLKQDLLSTLKNKSvtQK 631
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA--EE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  632 TEAWLDNFARCWDNLVQKLEKSTAQISQAVTTTQPSLtqttvmetvttvttreqilvkhaqeelpppppqkkrqitvdse 711
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR------------------------------------------- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  712 irkrldvDITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEgvNAD 791
Cdd:cd00176   114 -------DADDLEQWLEEKEAALASEDLG--KDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPD--ADE 182
                         250       260
                  ....*....|....*....|....*...
gi 578837832  792 SIKQASEQLNSRWIEFCQLLSERLNWLE 819
Cdd:cd00176   183 EIEEKLEELNERWEELLELAEERQKKLE 210
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
432-1133 4.58e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.18  E-value: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   432 EKQS-NLHRVLMDLQNqKLKELN---DWLTKTEERTRKMEEEpLGPDLEDLKRQVQQHKVLQEDL------EQEQVRVNS 501
Cdd:pfam15921  102 EKQKfYLRQSVIDLQT-KLQEMQmerDAMADIRRRESQSQED-LRNQLQNTVHELEAAKCLKEDMledsntQIEQLRKMM 179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   502 LTH---------MVVVVDESSGD--HATAALEE-QLKVLGDRWANICR-------WTEDRWVLLQDILLKWQrlTEEQCL 562
Cdd:pfam15921  180 LSHegvlqeirsILVDFEEASGKkiYEHDSMSTmHFRSLGSAISKILReldteisYLKGRIFPVEDQLEALK--SESQNK 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   563 FSAWLSEKEDAVNKI---HTTGFKDQNEMLSSLQKLA-VLKADLEKKKQSMGKLYSLKQDLLSTLKNKSVTQKTEawLDN 638
Cdd:pfam15921  258 IELLLQQHQDRIEQLiseHEVEITGLTEKASSARSQAnSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSE--LRE 335
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   639 FARCWDNLVQKLEKSTAQISQAVTTTQPSLTQTTVMETVTTVTTREQILVKHAQE-ELPPPPPQKKR--------QITVD 709
Cdd:pfam15921  336 AKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREkELSLEKEQNKRlwdrdtgnSITID 415
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   710 sEIRKRLDVDITElhswITRSEAVLQSpefaifRKEGNFSDLKEKVNAIE--REKAEKFRKLQDASRSAQALVEQMVNEG 787
Cdd:pfam15921  416 -HLRRELDDRNME----VQRLEALLKA------MKSECQGQMERQMAAIQgkNESLEKVSSLTAQLESTKEMLRKVVEEL 484
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   788 VNADSIKQASEQLNSrwiEFCQLLSERLNWLEYQNNIIAFYN-----QLQQLEQMTTTAENWLKIQpttpSEPTAIKSQL 862
Cdd:pfam15921  485 TAKKMTLESSERTVS---DLTASLQEKERAIEATNAEITKLRsrvdlKLQELQHLKNEGDHLRNVQ----TECEALKLQM 557
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   863 KiCKDEVnrLSDLQPQIERLkIQSIALKEKGQGPMFLDAdfvaftnhfKQVFSDVQAREKELQTIfdtlppmryqetmsa 942
Cdd:pfam15921  558 A-EKDKV--IEILRQQIENM-TQLVGQHGRTAGAMQVEK---------AQLEKEINDRRLELQEF--------------- 609
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   943 iRTWVQQSETKLSIPQLSVTDYEIMEQRL-----GELQALQSSLQEQQSGLYYLSTTVKEMSKKAPSE--ISRKYQSEFE 1015
Cdd:pfam15921  610 -KILKDKKDAKIRELEARVSDLELEKVKLvnagsERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYevLKRNFRNKSE 688
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1016 EIEGRWKKLSSQLVEHCQKLEEQMNKLRKIQNHIQTLKKwmaevdvflkeewPALGDSEILKKQLKQCRLLVSDIQTIQP 1095
Cdd:pfam15921  689 EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMK-------------VAMGMQKQITAKRGQIDALQSKIQFLEE 755
                          730       740       750
                   ....*....|....*....|....*....|....*...
gi 578837832  1096 SLNSVNEGGQKIKNEaepefASRLETELKELNTQWDHM 1133
Cdd:pfam15921  756 AMTNANKEKHFLKEE-----KNKLSQELSTVATEKNKM 788
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
719-819 5.25e-03

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 39.22  E-value: 5.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832   719 DITELHSWITRSEAVLQSPEFAifRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEqmvNEGVNADSIKQASE 798
Cdd:pfam00435    9 DADDLESWIEEKEALLSSEDYG--KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID---EGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|.
gi 578837832   799 QLNSRWIEFCQLLSERLNWLE 819
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLE 104
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
2156-2764 6.25e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.65  E-value: 6.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2156 ATGEEIIQQSSKTDASILQEKLGSLNLRWQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIPLEpgKE 2235
Cdd:TIGR00618  182 ALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK--KQ 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2236 QQLKEKLEQVKLLVEELPlrqgILKQLNETGGPVLVSAPISPEEQdklenKLKQTNLQWIKVSRALPEKQGEIEAQIKDL 2315
Cdd:TIGR00618  260 QLLKQLRARIEELRAQEA----VLEETQERINRARKAAPLAAHIK-----AVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2316 GQLEKKLEDLEEQLNHLLLWLspiRNQLEIYNQPNQEGPFdvkeTEIAVQAKQpDVEEILSKGQHLYKEKPATQPVKRKL 2395
Cdd:TIGR00618  331 AAHVKQQSSIEEQRRLLQTLH---SQEIHIRDAHEVATSI----REISCQQHT-LTQHIHTLQQQKTTLTQKLQSLCKEL 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2396 EDLSSEWKAVNRLLQELRAKQPDLAPGLTTIgaSPTQTVTLVTQPVVTKETAISKlempsslmLEVPALADFNRAWTELT 2475
Cdd:TIGR00618  403 DILQREQATIDTRTSAFRDLQGQLAHAKKQQ--ELQQRYAELCAAAITCTAQCEK--------LEKIHLQESAQSLKERE 472
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2476 DWLSLLDQVIKSQrvmvgdlEDINEMIIKQKATMQdlEQRRP---QLEELITAAQNLKNKTSNqeartiiTDRIERIQNQ 2552
Cdd:TIGR00618  473 QQLQTKEQIHLQE-------TRKKAVVLARLLELQ--EEPCPlcgSCIHPNPARQDIDNPGPL-------TRRMQRGEQT 536
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2553 WDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEgpytvdaiqkKITETKQLAKDLRQWQTNVDVA 2632
Cdd:TIGR00618  537 YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE----------DIPNLQNITVRLQDLTEKLSEA 606
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  2633 NDLALKLLRDYSADDTRKVHMitENINASWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAWLTEAETTANVLQDATR 2712
Cdd:TIGR00618  607 EDMLACEQHALLRKLQPEQDL--QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQK 684
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 578837832  2713 KERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRS----LEGSDDA 2764
Cdd:TIGR00618  685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSlgsdLAAREDA 740
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
1533-1926 9.61e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.88  E-value: 9.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1533 LDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKE 1612
Cdd:TIGR00618  199 LTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAV 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1613 IEKQK-------------VHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEewlnlLLEYQKHMETFDQN 1679
Cdd:TIGR00618  279 LEETQerinrarkaaplaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSS-----IEEQRRLLQTLHSQ 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1680 VDHITKWIIQADTLLDESEKKKP---------------QQKEDVLKRLKAELNDIRPKVDsTRDQAANLMANRGDHCRKL 1744
Cdd:TIGR00618  354 EIHIRDAHEVATSIREISCQQHTltqhihtlqqqkttlTQKLQSLCKELDILQREQATID-TRTSAFRDLQGQLAHAKKQ 432
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1745 VEPQISELNHRFAAISHRIKTGKASIP--------LKELEQFNSDIQKLLE------PLEAEIQQGVNLKEEDFNKDMNE 1810
Cdd:TIGR00618  433 QELQQRYAELCAAAITCTAQCEKLEKIhlqesaqsLKEREQQLQTKEQIHLqetrkkAVVLARLLELQEEPCPLCGSCIH 512
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837832  1811 DNEGTVKELLQRGDN-LQQRITDERKR--EEIKIKQQLLQTKHNALKDLRSQR---RKKALEISHQWYQYKRQADDLLKC 1884
Cdd:TIGR00618  513 PNPARQDIDNPGPLTrRMQRGEQTYAQleTSEEDVYHQLTSERKQRASLKEQMqeiQQSFSILTQCDNRSKEDIPNLQNI 592
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 578837832  1885 LDDIEKKLASLPEPRDeRKIKEIDRELQKKKEELNAVRRQAE 1926
Cdd:TIGR00618  593 TVRLQDLTEKLSEAED-MLACEQHALLRKLQPEQDLQDVRLH 633
 
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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