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Conserved domains on  [gi|1777507480|ref|XP_031546370|]
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plectin isoform X6 [Vicugna pacos]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
68-184 7.52e-74

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: 241.54  E-value: 7.52e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   68 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprekGRMRFHKLQNVQIALD 147
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRER------------GRMRFHRLQNVQTALD 68
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507480  148 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 184
Cdd:cd21188     69 FLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
197-302 1.02e-72

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: 238.38  E-value: 1.02e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  197 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 276
Cdd:cd21238      1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 1777507480  277 PEDVDVPQPDEKSIITYVSSLYDAMP 302
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
917-994 4.20e-31

Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.


:

Pssm-ID: 465730  Cd Length: 78  Bit Score: 118.09  E-value: 4.20e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777507480  917 LAWQSLSRDVQLIRSWSLVTFRTLKPEEQRQALRSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSRHYQQLLQS 994
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
816-882 2.34e-23

SH3 domain; This entry represents an SH3 domain.


:

Pssm-ID: 407754  Cd Length: 65  Bit Score: 95.79  E-value: 2.34e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1777507480  816 QLKPRSpaHPVRGRVPLLAVCDYKQVEVTVHKGDECQLVGPAQPFHWKVLSSSGSEAAVPSVCFLIP 882
Cdd:pfam17902    1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
641-819 2.32e-17

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: 83.65  E-value: 2.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  641 LHGFVAAATKELMWLSEKEDEEVGFDWSERSTNTAAKKDSYSALMRELELKEKKIKEIQSTGDRLLREDHPARPTVESFQ 720
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  721 AALQTQWSWMLQLCCCVEAHLKENTAYFQFFSDVREAEEQLRKLQETLRRKYTCDrsiTVTRLEDLLQDAQDEKDQLNEY 800
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
                          170
                   ....*....|....*....
gi 1777507480  801 RGHLSGLAKRAKAIVQLKP 819
Cdd:cd00176    159 EPRLKSLNELAEELLEEGH 177
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2938-2976 1.21e-15

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 72.75  E-value: 1.21e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2938 LLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEMNEIL 2976
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2360-2398 2.24e-15

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 71.98  E-value: 2.24e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2360 LLEAQIATGGIIDPVHSHRLPVDVAFQRGYFDEEMSRIL 2398
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1701-1739 3.94e-15

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 71.20  E-value: 3.94e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 1701 LLEAQIATGGIIDPVHSHRVPVDVAFQRGYFDEEMSRVL 1739
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2619-2657 1.93e-14

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 69.28  E-value: 1.93e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2619 LLEAQAATGFLLDPVKGDRLTVDEAVRKGLVGPELHDRL 2657
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1125-1315 1.55e-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: 72.48  E-value: 1.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1125 EDVLKAHEEQLKEAQaVPATLPELEATKAALKKLRAQAEAQQPVFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1204
Cdd:cd00176     13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1205 TQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLDSWLQDAKRRQEQIQAVPLANSqvVREQLRQEKALLEEIERH 1284
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLES--VEELLKKHKELEEELEAH 158
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1777507480 1285 GEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1315
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2029-2067 2.35e-13

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 66.20  E-value: 2.35e-13
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2029 LLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDEETHTAL 2067
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2284-2322 1.24e-12

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 64.27  E-value: 1.24e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2284 LLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPELHEKL 2322
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3207-3245 1.30e-12

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 64.27  E-value: 1.30e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 3207 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 3245
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2862-2900 2.89e-12

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.12  E-value: 2.89e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2862 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 2900
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2695-2733 3.06e-12

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.12  E-value: 3.06e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2695 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTYDQL 2733
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
937-1505 2.59e-11

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 2.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  937 FRTLKPEEQRQALRSLELHYQAFLRDSQDAGgfgpEDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIR 1016
Cdd:COG1196    215 YRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1017 LQLEACETRTVHRLRLplDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALpepspAAPTLRSELELTLGK 1096
Cdd:COG1196    291 YELLAELARLEQDIAR--LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-----AEEELEEAEAELAEA 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1097 LEQVRSLSAIYLEKLKTISlviRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDEL 1176
Cdd:COG1196    364 EEALLEAEAELAEAEEELE---ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1177 RGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQtdvRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQI 1256
Cdd:COG1196    441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE---LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1257 QAVPLAnsQVVREQLRQEKALLEEIE-----RHGEKVEECQRFAKQYINAIKDYELQLVT-YKAQLEPVASPAKKPKVQS 1330
Cdd:COG1196    518 GLRGLA--GAVAVLIGVEAAYEAALEaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARG 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1331 GSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRERFIEQEKA 1410
Cdd:COG1196    596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1411 KLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAEEN--- 1487
Cdd:COG1196    676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAlee 755
                          570       580
                   ....*....|....*....|....*
gi 1777507480 1488 -------QRLRERLQHLEEEhRAAL 1505
Cdd:COG1196    756 lpeppdlEELERELERLERE-IEAL 779
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1625-1663 2.63e-11

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 60.42  E-value: 2.63e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 1625 LLEAQAASGFLLDPVRNRQLTVNEAVKEGVVGPELHHKL 1663
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3283-3321 9.40e-10

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 56.18  E-value: 9.40e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 3283 FLEVQYLTGGLIEPDAPGRVPLEEALQRGTVDARTAQKL 3321
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1957-1991 4.32e-09

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 54.26  E-value: 4.32e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1777507480 1957 QAGTGHIVDPTTSARLTVAEAVRAGLVGPELHEKL 1991
Cdd:pfam00681    5 QAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3039-3067 3.76e-07

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 48.86  E-value: 3.76e-07
                           10        20
                   ....*....|....*....|....*....
gi 1777507480 3039 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 3067
Cdd:pfam00681   11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
2822-2859 2.21e-06

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.71  E-value: 2.21e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507480  2822 QKFLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTA 2859
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2246-2281 1.36e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.36e-05
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1777507480  2246 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTA 2281
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1587-1625 2.13e-05

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 43.86  E-value: 2.13e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 1587 YLQGRSSIAGLLLQPSNEKLSVYAALRRQLLSPGTALIL 1625
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC smart00150
Spectrin repeats;
545-639 2.67e-05

Spectrin repeats;


:

Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.40  E-value: 2.67e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   545 LRYLQDLLAWVGENQRRVDSAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARTDEGQL---SPATRGAYRDCLGRLD 621
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
                            90
                    ....*....|....*...
gi 1777507480   622 LQYAKLLNSSKARLRSLE 639
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
2580-2616 3.35e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.35e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  2580 RYLYGTGCVAGVYLPGSRQTLTVYQALKKGLLSAEVA 2616
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2321-2357 6.21e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 6.21e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  2321 KLLSAEKAVTGYKDPYTGEQISLFQAMKKGLVLREHG 2357
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3171-3204 6.59e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 6.59e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1777507480  3171 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 3204
Cdd:smart00250    5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
1990-2026 1.20e-04

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.70  E-value: 1.20e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  1990 KLLLAERAVTGYKDPYSGQSVSLFQALKKGLIPREQG 2026
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2656-2692 1.89e-04

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.89e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  2656 RLLSAERAVTGYRDPYTEQTISLFQAMKKDLIPAEEA 2692
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
1662-1698 4.52e-04

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.16  E-value: 4.52e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  1662 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVREHG 1698
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
1913-1945 9.83e-04

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.00  E-value: 9.83e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1777507480  1913 RRALRGSSVIAGVWLEEAGQKLSIYEALRKDLL 1945
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
PLEC smart00250
Plectin repeat;
2899-2930 4.84e-03

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.08  E-value: 4.84e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1777507480  2899 KLLSAERAVTGYKDPYSGKLISLFQAMKKGLI 2930
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
PLEC smart00250
Plectin repeat;
3319-3356 7.69e-03

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 36.69  E-value: 7.69e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507480  3319 QKLRDVSAYSKYLTCPKTKLKISYKDALDRSMVEEGTG 3356
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
 
Name Accession Description Interval E-value
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
68-184 7.52e-74

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: 241.54  E-value: 7.52e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   68 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprekGRMRFHKLQNVQIALD 147
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRER------------GRMRFHRLQNVQTALD 68
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507480  148 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 184
Cdd:cd21188     69 FLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
197-302 1.02e-72

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: 238.38  E-value: 1.02e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  197 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 276
Cdd:cd21238      1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 1777507480  277 PEDVDVPQPDEKSIITYVSSLYDAMP 302
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
64-409 2.35e-45

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 175.90  E-value: 2.35e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   64 ADERDRVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLprerdvIRSSRLPRekgrMRFHKLQNV 142
Cdd:COG5069      3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNA------GEYNETPE----TRIHVMENV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  143 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDN 221
Cdd:COG5069     73 SGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFD 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  222 FTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS--- 295
Cdd:COG5069    150 FFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyi 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  296 ---SLYD----AMPRVPDVQDGVKANElQLRwQEYRELVVLLLQWVRQHTAAFEERRFPSSFEEIEILWCQFLKFKETE- 367
Cdd:COG5069    230 irfGLLEkidiALHRVYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCs 307
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1777507480  368 -LPAKEAD-KNRSKGIFQSLEgAVQAGQLKVPPGYHPLDVEKEW 409
Cdd:COG5069    308 rAPLETTDlHSLAGQILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
917-994 4.20e-31

Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.


Pssm-ID: 465730  Cd Length: 78  Bit Score: 118.09  E-value: 4.20e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777507480  917 LAWQSLSRDVQLIRSWSLVTFRTLKPEEQRQALRSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSRHYQQLLQS 994
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
197-303 4.91e-25

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: 101.98  E-value: 4.91e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  197 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 273
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1777507480  274 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 303
Cdd:pfam00307   81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
73-182 4.86e-24

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: 98.93  E-value: 4.86e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480    73 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVirssrlprEKGRMRFHKLQNVQIALDYLRH 151
Cdd:smart00033    1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVD-KKKV--------AASLSRFKKIENINLALSFAEK 71
                            90       100       110
                    ....*....|....*....|....*....|.
gi 1777507480   152 RQVKLVNIRNDDIADGnPKLTLGLIWTIILH 182
Cdd:smart00033   72 LGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
816-882 2.34e-23

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 95.79  E-value: 2.34e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1777507480  816 QLKPRSpaHPVRGRVPLLAVCDYKQVEVTVHKGDECQLVGPAQPFHWKVLSSSGSEAAVPSVCFLIP 882
Cdd:pfam17902    1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
70-185 2.66e-23

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: 96.97  E-value: 2.66e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   70 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLPrerdvirssrlPREKGRMRFHKLQNVQIALD 147
Cdd:pfam00307    2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVD-----------KKKLNKSEFDKLENINLALD 70
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1777507480  148 YLRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 185
Cdd:pfam00307   71 VAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
201-297 2.81e-19

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: 85.45  E-value: 2.81e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   201 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 276
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 1777507480   277 PEDVDVPQPDEKSIITYVSSL 297
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
641-819 2.32e-17

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: 83.65  E-value: 2.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  641 LHGFVAAATKELMWLSEKEDEEVGFDWSERSTNTAAKKDSYSALMRELELKEKKIKEIQSTGDRLLREDHPARPTVESFQ 720
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  721 AALQTQWSWMLQLCCCVEAHLKENTAYFQFFSDVREAEEQLRKLQETLRRKYTCDrsiTVTRLEDLLQDAQDEKDQLNEY 800
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
                          170
                   ....*....|....*....
gi 1777507480  801 RGHLSGLAKRAKAIVQLKP 819
Cdd:cd00176    159 EPRLKSLNELAEELLEEGH 177
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2938-2976 1.21e-15

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 72.75  E-value: 1.21e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2938 LLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEMNEIL 2976
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2360-2398 2.24e-15

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 71.98  E-value: 2.24e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2360 LLEAQIATGGIIDPVHSHRLPVDVAFQRGYFDEEMSRIL 2398
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1701-1739 3.94e-15

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 71.20  E-value: 3.94e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 1701 LLEAQIATGGIIDPVHSHRVPVDVAFQRGYFDEEMSRVL 1739
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2619-2657 1.93e-14

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 69.28  E-value: 1.93e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2619 LLEAQAATGFLLDPVKGDRLTVDEAVRKGLVGPELHDRL 2657
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1125-1315 1.55e-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: 72.48  E-value: 1.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1125 EDVLKAHEEQLKEAQaVPATLPELEATKAALKKLRAQAEAQQPVFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1204
Cdd:cd00176     13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1205 TQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLDSWLQDAKRRQEQIQAVPLANSqvVREQLRQEKALLEEIERH 1284
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLES--VEELLKKHKELEEELEAH 158
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1777507480 1285 GEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1315
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2029-2067 2.35e-13

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 66.20  E-value: 2.35e-13
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2029 LLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDEETHTAL 2067
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2284-2322 1.24e-12

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 64.27  E-value: 1.24e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2284 LLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPELHEKL 2322
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3207-3245 1.30e-12

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 64.27  E-value: 1.30e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 3207 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 3245
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2862-2900 2.89e-12

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.12  E-value: 2.89e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2862 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 2900
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2695-2733 3.06e-12

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.12  E-value: 3.06e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2695 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTYDQL 2733
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
937-1505 2.59e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 2.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  937 FRTLKPEEQRQALRSLELHYQAFLRDSQDAGgfgpEDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIR 1016
Cdd:COG1196    215 YRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1017 LQLEACETRTVHRLRLplDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALpepspAAPTLRSELELTLGK 1096
Cdd:COG1196    291 YELLAELARLEQDIAR--LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-----AEEELEEAEAELAEA 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1097 LEQVRSLSAIYLEKLKTISlviRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDEL 1176
Cdd:COG1196    364 EEALLEAEAELAEAEEELE---ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1177 RGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQtdvRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQI 1256
Cdd:COG1196    441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE---LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1257 QAVPLAnsQVVREQLRQEKALLEEIE-----RHGEKVEECQRFAKQYINAIKDYELQLVT-YKAQLEPVASPAKKPKVQS 1330
Cdd:COG1196    518 GLRGLA--GAVAVLIGVEAAYEAALEaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARG 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1331 GSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRERFIEQEKA 1410
Cdd:COG1196    596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1411 KLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAEEN--- 1487
Cdd:COG1196    676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAlee 755
                          570       580
                   ....*....|....*....|....*
gi 1777507480 1488 -------QRLRERLQHLEEEhRAAL 1505
Cdd:COG1196    756 lpeppdlEELERELERLERE-IEAL 779
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1625-1663 2.63e-11

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 60.42  E-value: 2.63e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 1625 LLEAQAASGFLLDPVRNRQLTVNEAVKEGVVGPELHHKL 1663
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3283-3321 9.40e-10

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 56.18  E-value: 9.40e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 3283 FLEVQYLTGGLIEPDAPGRVPLEEALQRGTVDARTAQKL 3321
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
989-1319 9.88e-10

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: 65.09  E-value: 9.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  989 QQLLQSLEQGEQEESRCQRCISELKDirlQLEACETRTVHRLRLPLDKEPARECAQ--RIAEQQKAQAEVEGLGKGVARL 1066
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKAERYQALLKEKREYEGyeLLKEKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1067 SAEAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRSTQG----AEDVLKAHEEQLKE 1137
Cdd:TIGR02169  250 EEELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELED 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1138 AQAVPATL-PELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQllerwqavla 1216
Cdd:TIGR02169  320 AEERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------- 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1217 qtdvRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQavplANSQVVREQLrqeKALLEEIERHGEKVEECQRFAK 1296
Cdd:TIGR02169  390 ----YREKLEKLKREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKI---NELEEEKEDKALEIKKQEWKLE 458
                          330       340
                   ....*....|....*....|...
gi 1777507480 1297 QYINAIKDYELQLVTYKAQLEPV 1319
Cdd:TIGR02169  459 QLAADLSKYEQELYDLKEEYDRV 481
PLEC smart00250
Plectin repeat;
3205-3242 1.49e-09

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 55.57  E-value: 1.49e-09
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507480  3205 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 3242
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1957-1991 4.32e-09

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 54.26  E-value: 4.32e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1777507480 1957 QAGTGHIVDPTTSARLTVAEAVRAGLVGPELHEKL 1991
Cdd:pfam00681    5 QAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
886-1518 1.26e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.23  E-value: 1.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  886 QEAQEAIARLEAQHQALVALWHQLHTDMKSL-LAWQSLSRDVQLIrswslvtfrtlkpEEQRQALRSLELHYQAFLRDSQ 964
Cdd:TIGR02168  347 EELKEELESLEAELEELEAELEELESRLEELeEQLETLRSKVAQL-------------ELQIASLNNEIERLEARLERLE 413
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  965 DAggfgpEDRLQAEREygscsrhyqQLLQSLEQGEQEEsrCQRCISELKDIRLQLEACETRTVHRL------------RL 1032
Cdd:TIGR02168  414 DR-----RERLQQEIE---------ELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALeelreeleeaeqAL 477
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1033 PLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEK----VLALPEPSPAAPTLRSELELTLGKLEQ---VRSLSA 1105
Cdd:TIGR02168  478 DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgiLGVLSELISVDEGYEAAIEAALGGRLQavvVENLNA 557
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1106 I-----YLEK--LKTISLVIRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKAALKKlraqaeAQQPVFDALR--DEL 1176
Cdd:TIGR02168  558 AkkaiaFLKQneLGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRK------ALSYLLGGVLvvDDL 631
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1177 RGAQEVGERLqqRHGERDV----EVERWRERVTQLLERWQAVLAQtdvRQRELEQLGRQLRYYRESADPLDSWLQDAKRR 1252
Cdd:TIGR02168  632 DNALELAKKL--RPGYRIVtldgDLVRPGGVITGGSAKTNSSILE---RRREIEELEEKIEELEEKIAELEKALAELRKE 706
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1253 QEQIQAVPLANSQVVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEP-----VASPAKKPK 1327
Cdd:TIGR02168  707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeelAEAEAEIEE 786
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1328 VQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQEtqaLRQSFLSEKDSLLQRERFIEQ 1407
Cdd:TIGR02168  787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED---LEEQIEELSEDIESLAAEIEE 863
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1408 EKAKLEQLfQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAEEN 1487
Cdd:TIGR02168  864 LEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
                          650       660       670
                   ....*....|....*....|....*....|.
gi 1777507480 1488 QRLRERLQHLEEEhraALAHSEEVPASQATA 1518
Cdd:TIGR02168  943 ERLSEEYSLTLEE---AEALENKIEDDEEEA 970
PLEC smart00250
Plectin repeat;
2936-2972 2.59e-08

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 52.10  E-value: 2.59e-08
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  2936 IRLLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEM 2972
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
SPEC smart00150
Spectrin repeats;
642-734 8.47e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.72  E-value: 8.47e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   642 HGFVAAATKELMWLSEKEDEEVGFDWSERSTNTAAKKDSYSALMRELELKEKKIKEIQSTGDRLLREDHPARPTVESFQA 721
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90
                    ....*....|...
gi 1777507480   722 ALQTQWSWMLQLC 734
Cdd:smart00150   81 ELNERWEELKELA 93
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3039-3067 3.76e-07

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 48.86  E-value: 3.76e-07
                           10        20
                   ....*....|....*....|....*....
gi 1777507480 3039 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 3067
Cdd:pfam00681   11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
2358-2394 7.52e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 47.86  E-value: 7.52e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  2358 IRLLEAQIATGGIIDPVHSHRLPVDVAFQRGYFDEEM 2394
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
944-1656 7.74e-07

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: 55.51  E-value: 7.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  944 EQRQALRSLE-----LHYQAFLRDSQDAGGfgPEDRLQAEREYGSCSRHYQQLLQSLEQGEQEESrcqrcISELKDIRL- 1017
Cdd:pfam15921  332 ELREAKRMYEdkieeLEKQLVLANSELTEA--RTERDQFSQESGNLDDQLQKLLADLHKREKELS-----LEKEQNKRLw 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1018 QLEACETRTVHRLRLPLDK---EPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVlalpepspaaPTLRSELELTL 1094
Cdd:pfam15921  405 DRDTGNSITIDHLRRELDDrnmEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKV----------SSLTAQLESTK 474
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1095 GKLEQVrslsaiyLEKLKTISLVIRSTQGAEDVLKAHEEQLKEAqavpatlpeLEATKAALKKLRAQAEAQQPVFDALRD 1174
Cdd:pfam15921  475 EMLRKV-------VEELTAKKMTLESSERTVSDLTASLQEKERA---------IEATNAEITKLRSRVDLKLQELQHLKN 538
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1175 E---LRGAQEVGERLQQRHGERDVEVERWR---ERVTQLLERWQ----AVLAQTDVRQRELEQLGRQLRYYRESADPLDS 1244
Cdd:pfam15921  539 EgdhLRNVQTECEALKLQMAEKDKVIEILRqqiENMTQLVGQHGrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDA 618
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1245 WLQD--AKRRQEQIQAVPLANSQvvREQLRQEKALLEEIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVASP 1322
Cdd:pfam15921  619 KIREleARVSDLELEKVKLVNAG--SERLRAVKDIKQERDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETT 693
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1323 AKKPKVQsgsesviqeyvdLRTRYSELTTLTSqyikfiseTLRRMEEEEMQTVQQEQLLQETQALRQ----------SFL 1392
Cdd:pfam15921  694 TNKLKMQ------------LKSAQSELEQTRN--------TLKSMEGSDGHAMKVAMGMQKQITAKRgqidalqskiQFL 753
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1393 SEKDSLLQRER-FIEQEKAKLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQlVASMEEA---------------RRQQR 1456
Cdd:pfam15921  754 EEAMTNANKEKhFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEK-VANMEVAldkaslqfaecqdiiQRQEQ 832
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1457 EAeegVRRKQEELQRLEEQRQQQEKllaeENQRLRERLQHLEEEHRaalAHSeEVPASQATATKALPNGRDAldgPATET 1536
Cdd:pfam15921  833 ES---VRLKLQHTLDVKELQGPGYT----SNSSMKPRLLQPASFTR---THS-NVPSSQSTASFLSHHSRKT---NALKE 898
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1537 EPEHAFDGLRQKV--PAQQLQEVGILSAEELQRLVQG-------RTTVAELEQREDV----RCYLQGRSSIAGLLLqpSN 1603
Cdd:pfam15921  899 DPTRDLKQLLQELrsVINEEPTVQLSKAEDKGRAPSLgalddrvRDCIIESSLRSDIchssSNSLQTEGSKSSETC--SR 976
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1777507480 1604 EKLSVYAALRRQLLS----PGTALILLEAQAASGFLLDPVRNRQLTVNEAVKEGVVG 1656
Cdd:pfam15921  977 EPVLLHAGELEDPSScftfPSTASPSVKNSASRSFHSSPKKSPVHSLLTSSAEGSIG 1033
PLEC smart00250
Plectin repeat;
1699-1735 1.84e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.71  E-value: 1.84e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  1699 IRLLEAQIATGGIIDPVHSHRVPVDVAFQRGYFDEEM 1735
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
2822-2859 2.21e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.71  E-value: 2.21e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507480  2822 QKFLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTA 2859
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2027-2063 2.46e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.32  E-value: 2.46e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  2027 LRLLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDEET 2063
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
2617-2652 2.91e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.32  E-value: 2.91e-06
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1777507480  2617 RLLLEAQAATGFLLDPVKGDRLTVDEAVRKGLVGPE 2652
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2824-2862 3.44e-06

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 46.17  E-value: 3.44e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2824 FLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTAFEL 2862
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1147-1349 4.89e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 4.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1147 ELEATKAALKKLRAQAEAQQPV------FDALRDELRGAQEVGERLQQRHGERdvEVERWRERVTQLLERWQAVLAQTDV 1220
Cdd:COG4913    236 DLERAHEALEDAREQIELLEPIrelaerYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELER 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1221 RQRELEQLGRQLRyyresadpldswlqdakRRQEQIQAVplansqvvreQLRQEKALLEEIERHGEKVEECQRFAKQYIN 1300
Cdd:COG4913    314 LEARLDALREELD-----------------ELEAQIRGN----------GGDRLEQLEREIERLERELEERERRRARLEA 366
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1777507480 1301 AIKDYELQLVTYKAQLEPVASPAK--KPKVQSGSESVIQEYVDLRTRYSEL 1349
Cdd:COG4913    367 LLAALGLPLPASAEEFAALRAEAAalLEALEEELEALEEALAEAEAALRDL 417
PLEC smart00250
Plectin repeat;
2246-2281 1.36e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.36e-05
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1777507480  2246 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTA 2281
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2693-2730 1.40e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.40e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507480  2693 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTY 2730
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3032-3060 1.51e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.51e-05
                            10        20
                    ....*....|....*....|....*....
gi 1777507480  3032 VRKRRVVIVDPETGKEMSVYEAYRKGLID 3060
Cdd:smart00250    6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
PTZ00121 PTZ00121
MAEBL; Provisional
941-1516 1.57e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  941 KPEEQRQAL---RSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSR-----HYQQLLQSLEQGEQ-EESRCQRCISE 1011
Cdd:PTZ00121  1177 KAEAARKAEevrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKaeavkKAEEAKKDAEEAKKaEEERNNEEIRK 1256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1012 LKDIRLQ--------LEACETRTVHRLRLPLDKEPARECAQ----RIAEQQKAQAE----VEGLGKGV--ARLSAEAEKV 1073
Cdd:PTZ00121  1257 FEEARMAhfarrqaaIKAEEARKADELKKAEEKKKADEAKKaeekKKADEAKKKAEeakkADEAKKKAeeAKKKADAAKK 1336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1074 LAlPEPSPAAPTLRSELELTLGKLEQVRslsaiylEKLKTISLVIRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKA 1153
Cdd:PTZ00121  1337 KA-EEAKKAAEAAKAEAEAAADEAEAAE-------EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1154 ALKKlraqAEAQQPVFDALR---DELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQlgr 1230
Cdd:PTZ00121  1409 ELKK----AAAAKKKADEAKkkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE--- 1481
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1231 qlryyRESADPLDSWLQDAKRRQEQIQAVPLANSQVVREQLRQEKALLEEIERHGE--KVEEcqrfAKQYINAIKDYELQ 1308
Cdd:PTZ00121  1482 -----AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakKADE----AKKAEEKKKADELK 1552
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1309 LVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLR----TRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQET 1384
Cdd:PTZ00121  1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1385 QALRQSFLSEKDSLLQRERFIEQE------KAKLEQLFQEEVAKAQKLReeqqRQQQQMEQEKQQLVASMEEARR--QQR 1456
Cdd:PTZ00121  1633 KKVEQLKKKEAEEKKKAEELKKAEeenkikAAEEAKKAEEDKKKAEEAK----KAEEDEKKAAEALKKEAEEAKKaeELK 1708
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1777507480 1457 EAEEGVRRKQEE---LQRLEEQRQQQEKLLAEENQRLRERLQhLEEEHRAALAHSEEVPASQA 1516
Cdd:PTZ00121  1709 KKEAEEKKKAEElkkAEEENKIKAEEAKKEAEEDKKKAEEAK-KDEEEKKKIAHLKKEEEKKA 1770
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2246-2284 1.64e-05

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 44.24  E-value: 1.64e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2246 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTATLL 2284
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1587-1625 2.13e-05

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 43.86  E-value: 2.13e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 1587 YLQGRSSIAGLLLQPSNEKLSVYAALRRQLLSPGTALIL 1625
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC smart00150
Spectrin repeats;
545-639 2.67e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.40  E-value: 2.67e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   545 LRYLQDLLAWVGENQRRVDSAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARTDEGQL---SPATRGAYRDCLGRLD 621
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
                            90
                    ....*....|....*...
gi 1777507480   622 LQYAKLLNSSKARLRSLE 639
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
2580-2616 3.35e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.35e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  2580 RYLYGTGCVAGVYLPGSRQTLTVYQALKKGLLSAEVA 2616
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2862-2896 4.72e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.85  E-value: 4.72e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1777507480  2862 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 2896
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
2321-2357 6.21e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 6.21e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  2321 KLLSAEKAVTGYKDPYTGEQISLFQAMKKGLVLREHG 2357
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3171-3204 6.59e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 6.59e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1777507480  3171 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 3204
Cdd:smart00250    5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
SPEC smart00150
Spectrin repeats;
1133-1226 9.30e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.86  E-value: 9.30e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  1133 EQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALrdelrgaQEVGERLQQRHGERDVEVErwrERVTQLLERWQ 1212
Cdd:smart00150   18 EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEAL-------NELGEQLIEEGHPDAEEIE---ERLEELNERWE 87
                            90
                    ....*....|....
gi 1777507480  1213 AVLAQTDVRQRELE 1226
Cdd:smart00150   88 ELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
1990-2026 1.20e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.70  E-value: 1.20e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  1990 KLLLAERAVTGYKDPYSGQSVSLFQALKKGLIPREQG 2026
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2282-2317 1.76e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.76e-04
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1777507480  2282 TLLLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPE 2317
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
PLEC smart00250
Plectin repeat;
2656-2692 1.89e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.89e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  2656 RLLSAERAVTGYRDPYTEQTISLFQAMKKDLIPAEEA 2692
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3281-3318 2.19e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.93  E-value: 2.19e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507480  3281 QRFLEVQYLTGGLIEPDAPGRVPLEEALQRGTVDARTA 3318
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2581-2619 3.09e-04

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 40.39  E-value: 3.09e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2581 YLYGTGCVAGVYLPGSRQTLTVYQALKKGLLSAEVARLL 2619
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
1625-1658 3.61e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.16  E-value: 3.61e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1777507480  1625 LLEAQAASGFLLDPVRNRQLTVNEAVKEGVVGPE 1658
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
PLEC smart00250
Plectin repeat;
1662-1698 4.52e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.16  E-value: 4.52e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  1662 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVREHG 1698
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
1913-1945 9.83e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.00  E-value: 9.83e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1777507480  1913 RRALRGSSVIAGVWLEEAGQKLSIYEALRKDLL 1945
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
654-734 1.75e-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: 40.38  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  654 WLSEKE----DEEVGFDWSErstnTAAKKDSYSALMRELELKEKKIKEIQSTGDRLLREDHPARPTVESFQAALQTQWSW 729
Cdd:pfam00435   16 WIEEKEallsSEDYGKDLES----VQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERWEQ 91

                   ....*
gi 1777507480  730 MLQLC 734
Cdd:pfam00435   92 LLELA 96
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3177-3207 4.53e-03

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 37.31  E-value: 4.53e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1777507480 3177 AGILDTETLEKVSITEAMHRNLVDNITGQRL 3207
Cdd:pfam00681    9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
2899-2930 4.84e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.08  E-value: 4.84e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1777507480  2899 KLLSAERAVTGYKDPYSGKLISLFQAMKKGLI 2930
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1147-1227 6.61e-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: 38.84  E-value: 6.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1147 ELEATKAALKKLRAQAEAqqpvFDALRDELRGAQEVGERLQQRHGErdvEVERWRERVTQLLERWQAVLAQTDVRQRELE 1226
Cdd:pfam00435   32 DLESVQALLKKHKALEAE----LAAHQDRVEALNELAEKLIDEGHY---ASEEIQERLEELNERWEQLLELAAERKQKLE 104

                   .
gi 1777507480 1227 Q 1227
Cdd:pfam00435  105 E 105
PLEC smart00250
Plectin repeat;
3319-3356 7.69e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 36.69  E-value: 7.69e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507480  3319 QKLRDVSAYSKYLTCPKTKLKISYKDALDRSMVEEGTG 3356
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
 
Name Accession Description Interval E-value
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
68-184 7.52e-74

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: 241.54  E-value: 7.52e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   68 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprekGRMRFHKLQNVQIALD 147
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRER------------GRMRFHRLQNVQTALD 68
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507480  148 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 184
Cdd:cd21188     69 FLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
197-302 1.02e-72

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: 238.38  E-value: 1.02e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  197 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 276
Cdd:cd21238      1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 1777507480  277 PEDVDVPQPDEKSIITYVSSLYDAMP 302
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
65-195 5.02e-72

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: 236.85  E-value: 5.02e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   65 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpreKGRMRFHKLQNVQI 144
Cdd:cd21235      1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE------------KGRMRFHKLQNVQI 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1777507480  145 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 195
Cdd:cd21235     69 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
57-193 4.87e-70

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: 231.41  E-value: 4.87e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   57 ERAVIRIADERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpreKGRMRF 136
Cdd:cd21236      4 ENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPRE------------KGRMRF 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1777507480  137 HKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 193
Cdd:cd21236     72 HRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
198-302 6.38e-66

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: 218.80  E-value: 6.38e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  198 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 277
Cdd:cd21189      1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                           90       100
                   ....*....|....*....|....*
gi 1777507480  278 EDVDVPQPDEKSIITYVSSLYDAMP 302
Cdd:cd21189     81 EDVDVPEPDEKSIITYVSSLYDVFP 105
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
65-194 1.41e-61

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: 206.81  E-value: 1.41e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   65 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGdslprerdvirsSRLPREKGRMRFHKLQNVQI 144
Cdd:cd21237      1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSG------------VKLPREKGRMRFHRLQNVQI 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1777507480  145 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 194
Cdd:cd21237     69 ALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
198-302 1.87e-57

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: 194.43  E-value: 1.87e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  198 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 277
Cdd:cd21239      1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
                           90       100
                   ....*....|....*....|....*
gi 1777507480  278 EDVDVPQPDEKSIITYVSSLYDAMP 302
Cdd:cd21239     80 EDVDVSSPDEKSVITYVSSLYDVFP 104
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
196-302 3.82e-52

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: 179.47  E-value: 3.82e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  196 DMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 275
Cdd:cd21240      2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
                           90       100
                   ....*....|....*....|....*..
gi 1777507480  276 DPEDVDVPQPDEKSIITYVSSLYDAMP 302
Cdd:cd21240     81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
57-181 5.68e-48

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: 167.93  E-value: 5.68e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   57 ERAVIR-IADERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMR 135
Cdd:cd21246      2 ERSRIKaLADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKP-----------TKGKMR 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1777507480  136 FHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 181
Cdd:cd21246     71 IHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
70-185 7.43e-48

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: 167.17  E-value: 7.43e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   70 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGdslprerdvirsSRLPREKGRMRFHKLQNVQIALDY 148
Cdd:cd21186      2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTG------------KKLKPEKGRMRVHHLNNVNRALQV 69
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507480  149 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 185
Cdd:cd21186     70 LEQNNVKLVNISSNDIVDGNPKLTLGLVWSIILHWQV 106
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
198-298 5.52e-46

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: 161.81  E-value: 5.52e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  198 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 277
Cdd:cd21194      2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
                           90       100
                   ....*....|....*....|.
gi 1777507480  278 EDVDVPQPDEKSIITYVSSLY 298
Cdd:cd21194     82 EDVDVARPDEKSIMTYVASYY 102
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
64-409 2.35e-45

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 175.90  E-value: 2.35e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   64 ADERDRVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLprerdvIRSSRLPRekgrMRFHKLQNV 142
Cdd:COG5069      3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNA------GEYNETPE----TRIHVMENV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  143 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDN 221
Cdd:COG5069     73 SGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFD 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  222 FTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS--- 295
Cdd:COG5069    150 FFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyi 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  296 ---SLYD----AMPRVPDVQDGVKANElQLRwQEYRELVVLLLQWVRQHTAAFEERRFPSSFEEIEILWCQFLKFKETE- 367
Cdd:COG5069    230 irfGLLEkidiALHRVYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCs 307
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1777507480  368 -LPAKEAD-KNRSKGIFQSLEgAVQAGQLKVPPGYHPLDVEKEW 409
Cdd:COG5069    308 rAPLETTDlHSLAGQILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
198-298 3.80e-44

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: 156.40  E-value: 3.80e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  198 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 277
Cdd:cd21248      2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
                           90       100
                   ....*....|....*....|.
gi 1777507480  278 EDVDVPQPDEKSIITYVSSLY 298
Cdd:cd21248     82 EDVNVEQPDEKSIITYVVTYY 102
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
57-181 4.64e-44

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: 156.69  E-value: 4.64e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   57 ERAVIR-IADERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMR 135
Cdd:cd21193      2 EKGRIRaLQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKP-----------NRGRLR 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1777507480  136 FHKLQNVQIALDYLrHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 181
Cdd:cd21193     71 VQKIENVNKALAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
66-185 3.01e-42

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: 151.37  E-value: 3.01e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   66 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDslprerdvirssRLPREKGRM--RFHKLQN 141
Cdd:cd21241      1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGE------------KLPCEKGRRlkRVHFLSN 68
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1777507480  142 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 185
Cdd:cd21241     69 INTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
197-302 7.42e-42

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: 150.16  E-value: 7.42e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  197 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 276
Cdd:cd21243      4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
                           90       100
                   ....*....|....*....|....*.
gi 1777507480  277 PEDVDVPQPDEKSIITYVSSLYDAMP 302
Cdd:cd21243     84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
185-300 4.32e-41

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: 148.28  E-value: 4.32e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  185 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 264
Cdd:cd21216      1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507480  265 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 300
Cdd:cd21216     77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
66-185 5.32e-41

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: 147.72  E-value: 5.32e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   66 ERDRVQKKTFTKWVNKHLikaQRH-----ISDLYEDLRDGHNLISLLEVLSGDslprerdvirssRLPREKGRM--RFHK 138
Cdd:cd21190      1 EQERVQKKTFTNWINSHL---AKLsqpivINDLFVDIKDGTALLRLLEVLSGQ------------KLPIESGRVlqRAHK 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1777507480  139 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 185
Cdd:cd21190     66 LSNIRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
63-181 2.62e-40

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: 147.09  E-value: 2.62e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   63 IADERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMRFHKLQNV 142
Cdd:cd21318     31 LADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKP-----------TRGRMRIHSLENV 99
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1777507480  143 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 181
Cdd:cd21318    100 DKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
57-181 1.75e-39

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: 144.43  E-value: 1.75e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   57 ERAVIR-IADERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMR 135
Cdd:cd21317     17 ERSRIKaLADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKP-----------TKGRMR 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1777507480  136 FHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 181
Cdd:cd21317     86 IHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
194-298 1.11e-38

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: 141.30  E-value: 1.11e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  194 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 273
Cdd:cd21319      1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
                           90       100
                   ....*....|....*....|....*
gi 1777507480  274 LLDPEDVDVPQPDEKSIITYVSSLY 298
Cdd:cd21319     81 LLDPEDVFTENPDEKSIITYVVAFY 105
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
68-181 3.33e-38

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: 139.45  E-value: 3.33e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   68 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerdvirssrlPREKGRMRFHKLQNVQIALD 147
Cdd:cd21214      3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLP-----------KPERGKMRFHKIANVNKALD 71
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1777507480  148 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 181
Cdd:cd21214     72 FIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
194-298 4.17e-38

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: 139.81  E-value: 4.17e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  194 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 273
Cdd:cd21321      1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
                           90       100
                   ....*....|....*....|....*
gi 1777507480  274 LLDPEDVDVPQPDEKSIITYVSSLY 298
Cdd:cd21321     81 LLDPEDVNVDQPDEKSIITYVATYY 105
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
197-298 2.77e-37

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: 136.92  E-value: 2.77e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  197 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 276
Cdd:cd21249      3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
                           90       100
                   ....*....|....*....|..
gi 1777507480  277 PEDVDVPQPDEKSIITYVSSLY 298
Cdd:cd21249     83 PEDVAVPHPDERSIMTYVSLYY 104
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
70-183 9.37e-37

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: 135.61  E-value: 9.37e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   70 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprEKGRMRFHKLQNVQIALDYL 149
Cdd:cd21215      4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYN----------KNPKMRVQKLENVNKALEFI 73
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1777507480  150 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 183
Cdd:cd21215     74 KSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
66-185 3.28e-36

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: 134.19  E-value: 3.28e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   66 ERDRVQKKTFTKWVNKHLIKAQ--RHISDLYEDLRDGHNLISLLEVLSGDslprerdvirssRLPREKGRMRFHKLQNVQ 143
Cdd:cd21242      1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQ------------QLPREKGHNVFQCRSNIE 68
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1777507480  144 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 185
Cdd:cd21242     69 TALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
182-298 4.14e-36

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: 134.41  E-value: 4.14e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  182 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQA 261
Cdd:cd21322      1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507480  262 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 298
Cdd:cd21322     81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
201-302 1.37e-35

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: 132.17  E-value: 1.37e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  201 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 279
Cdd:cd21187      2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
                           90       100
                   ....*....|....*....|...
gi 1777507480  280 VDVPQPDEKSIITYVSSLYDAMP 302
Cdd:cd21187     82 VNVEQPDKKSILMYVTSLFQVLP 104
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
65-185 1.57e-34

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: 129.27  E-value: 1.57e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   65 DERDRVQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGdslprerdvirsSRLPREKGRMRFHKLQNVQ 143
Cdd:cd21231      1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTG------------QKLVKEKGSTRVHALNNVN 68
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1777507480  144 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 185
Cdd:cd21231     69 KALQVLQKNNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
197-295 4.46e-33

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: 124.84  E-value: 4.46e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  197 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 276
Cdd:cd21192      2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
                           90
                   ....*....|....*....
gi 1777507480  277 PEDVDVPQPDEKSIITYVS 295
Cdd:cd21192     82 VEDVLVDKPDERSIMTYVS 100
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
57-181 5.40e-33

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: 126.70  E-value: 5.40e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   57 ERAVIR-IADERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMR 135
Cdd:cd21316     39 ERSRIKaLADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKP-----------TKGRMR 107
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1777507480  136 FHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 181
Cdd:cd21316    108 IHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
198-298 1.18e-32

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: 123.67  E-value: 1.18e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  198 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 277
Cdd:cd21320      2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
                           90       100
                   ....*....|....*....|.
gi 1777507480  278 EDVDVPQPDEKSIITYVSSLY 298
Cdd:cd21320     82 EDISVDHPDEKSIITYVVTYY 102
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
69-186 2.78e-32

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: 123.33  E-value: 2.78e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   69 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpREKGRMRFHKLQNVQIALDY 148
Cdd:cd21311     14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKF----------NKRPTFRSQKLENVSVALKF 83
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1777507480  149 LRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 186
Cdd:cd21311     84 LEEDEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
70-185 4.63e-32

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: 122.01  E-value: 4.63e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   70 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRerdVIRssrlpreKGRMRFHKLQNVQIALDYL 149
Cdd:cd21227      4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGR---VIK-------KPLNQHQKLENVTLALKAM 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1777507480  150 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 185
Cdd:cd21227     74 AEDGIKLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
197-295 7.09e-32

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: 121.48  E-value: 7.09e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  197 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 276
Cdd:cd21244      4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
                           90
                   ....*....|....*....
gi 1777507480  277 PEDVDVPQPDEKSIITYVS 295
Cdd:cd21244     84 PEDVDVVNPDEKSIMTYVA 102
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
185-300 2.07e-31

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: 120.71  E-value: 2.07e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  185 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 264
Cdd:cd21291      1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507480  265 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 300
Cdd:cd21291     77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
201-302 3.70e-31

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: 119.29  E-value: 3.70e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  201 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 279
Cdd:cd21234      2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
                           90       100
                   ....*....|....*....|...
gi 1777507480  280 VDVPQPDEKSIITYVSSLYDAMP 302
Cdd:cd21234     82 VAVQLPDKKSIIMYLTSLFEVLP 104
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
917-994 4.20e-31

Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.


Pssm-ID: 465730  Cd Length: 78  Bit Score: 118.09  E-value: 4.20e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777507480  917 LAWQSLSRDVQLIRSWSLVTFRTLKPEEQRQALRSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSRHYQQLLQS 994
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
201-303 6.92e-31

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: 118.88  E-value: 6.92e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  201 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 278
Cdd:cd21233      2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
                           90       100
                   ....*....|....*....|....*
gi 1777507480  279 DVDVPQPDEKSIITYVSSLYDAMPR 303
Cdd:cd21233     82 DVATAHPDKKSILMYVTSLFQVLPQ 106
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
203-298 2.56e-30

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: 117.06  E-value: 2.56e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  203 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 281
Cdd:cd21253      6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
                           90
                   ....*....|....*..
gi 1777507480  282 VPQPDEKSIITYVSSLY 298
Cdd:cd21253     86 LKVPDKLSILTYVSQYY 102
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
70-185 4.57e-30

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: 116.26  E-value: 4.57e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   70 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprekGRMRFHKLQNVQIALDY 148
Cdd:cd21232      2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKER------------GSTRVHALNNVNRVLQV 69
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507480  149 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 185
Cdd:cd21232     70 LHQNNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
183-300 7.94e-30

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: 116.34  E-value: 7.94e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  183 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAF 262
Cdd:cd21290      2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1777507480  263 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 300
Cdd:cd21290     78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
66-187 7.95e-30

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


Pssm-ID: 409040  Cd Length: 114  Bit Score: 116.14  E-value: 7.95e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   66 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRErdvIRSSRlprekgrMRFHKLQNVQ 143
Cdd:cd21191      1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQE---YKPSS-------HRIFRLNNIA 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1777507480  144 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 187
Cdd:cd21191     71 KALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
69-183 4.10e-29

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: 113.73  E-value: 4.10e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   69 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlprEKGRMRFHKLQNVQIALDY 148
Cdd:cd21183      3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYN---------RRPAFQQHYLENVSTALKF 73
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1777507480  149 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 183
Cdd:cd21183     74 IEADHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
201-300 1.11e-28

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: 112.38  E-value: 1.11e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  201 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 279
Cdd:cd22198      3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
                           90       100
                   ....*....|....*....|.
gi 1777507480  280 VDVPQPDEKSIITYVSSLYDA 300
Cdd:cd22198     83 ASLAVPDKLSMVSYLSQFYEA 103
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
185-300 9.38e-28

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: 110.56  E-value: 9.38e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  185 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 264
Cdd:cd21287      1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507480  265 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 300
Cdd:cd21287     77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
185-300 3.42e-27

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: 109.04  E-value: 3.42e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  185 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 264
Cdd:cd21289      1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507480  265 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 300
Cdd:cd21289     77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
69-183 1.21e-26

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: 106.80  E-value: 1.21e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   69 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlprEKGRMRFHKLQNVQIALDY 148
Cdd:cd21228      3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYN---------KRPTFRQMKLENVSVALEF 73
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1777507480  149 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 183
Cdd:cd21228     74 LERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
69-186 5.42e-26

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: 105.50  E-value: 5.42e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   69 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlPREKgrMRFHKLQNVQIALDY 148
Cdd:cd21310     15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYH-------PRPN--FRQMKLENVSVALEF 85
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1777507480  149 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 186
Cdd:cd21310     86 LDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
185-300 1.05e-25

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: 104.77  E-value: 1.05e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  185 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 264
Cdd:cd21288      1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507480  265 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 300
Cdd:cd21288     77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
203-298 1.45e-25

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: 103.39  E-value: 1.45e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  203 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 281
Cdd:cd21197      5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
                           90
                   ....*....|....*..
gi 1777507480  282 VPQPDEKSIITYVSSLY 298
Cdd:cd21197     85 MHVPDRLSIITYVSQYY 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
197-303 4.91e-25

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: 101.98  E-value: 4.91e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  197 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 273
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1777507480  274 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 303
Cdd:pfam00307   81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
201-301 1.08e-24

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: 101.00  E-value: 1.08e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  201 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 280
Cdd:cd21226      3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
                           90       100
                   ....*....|....*....|.
gi 1777507480  281 DVPQPDEKSIITYVSSLYDAM 301
Cdd:cd21226     83 MTGNPDERSIVLYTSLFYHAF 103
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
62-185 1.93e-24

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: 100.99  E-value: 1.93e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   62 RIADERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGRMRFHKL 139
Cdd:cd21247     12 KLQEQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRP-----------SRGKMRVHFL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1777507480  140 QNVQIALDYLRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 185
Cdd:cd21247     81 ENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
199-298 4.59e-24

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: 99.17  E-value: 4.59e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  199 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 278
Cdd:cd21252      1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
                           90       100
                   ....*....|....*....|.
gi 1777507480  279 D-VDVPQPDEKSIITYVSSLY 298
Cdd:cd21252     81 DmVSMKVPDCLSIMTYVSQYY 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
73-182 4.86e-24

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: 98.93  E-value: 4.86e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480    73 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVirssrlprEKGRMRFHKLQNVQIALDYLRH 151
Cdd:smart00033    1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVD-KKKV--------AASLSRFKKIENINLALSFAEK 71
                            90       100       110
                    ....*....|....*....|....*....|.
gi 1777507480   152 RQVKLVNIRNDDIADGnPKLTLGLIWTIILH 182
Cdd:smart00033   72 LGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
198-302 4.89e-24

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: 99.09  E-value: 4.89e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  198 TAKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 277
Cdd:cd21245      3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
                           90       100
                   ....*....|....*....|....*
gi 1777507480  278 EDVDVPQPDEKSIITYVSSLYDAMP 302
Cdd:cd21245     82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
198-298 2.18e-23

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: 97.11  E-value: 2.18e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  198 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 277
Cdd:cd21198      1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
                           90       100
                   ....*....|....*....|..
gi 1777507480  278 EDVDVPQ-PDEKSIITYVSSLY 298
Cdd:cd21198     80 ADMVLLSvPDKLSVMTYLHQIR 101
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
816-882 2.34e-23

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 95.79  E-value: 2.34e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1777507480  816 QLKPRSpaHPVRGRVPLLAVCDYKQVEVTVHKGDECQLVGPAQPFHWKVLSSSGSEAAVPSVCFLIP 882
Cdd:pfam17902    1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
70-185 2.66e-23

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: 96.97  E-value: 2.66e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   70 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLPrerdvirssrlPREKGRMRFHKLQNVQIALD 147
Cdd:pfam00307    2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVD-----------KKKLNKSEFDKLENINLALD 70
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1777507480  148 YLRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 185
Cdd:pfam00307   71 VAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
198-296 2.30e-22

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


Pssm-ID: 409033  Cd Length: 103  Bit Score: 94.23  E-value: 2.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  198 TAKEKLLLWSQRMVEGYqglRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 276
Cdd:cd21184      1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
                           90       100
                   ....*....|....*....|
gi 1777507480  277 PEDVDVPQPDEKSIITYVSS 296
Cdd:cd21184     78 PEDMVSPNVDELSVMTYLSY 97
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
69-186 4.00e-22

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: 94.38  E-value: 4.00e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   69 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlprEKGRMRFHKLQNVQIALDY 148
Cdd:cd21308     19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHN---------QRPTFRQMQLENVSVALEF 89
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1777507480  149 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 186
Cdd:cd21308     90 LDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
69-186 9.62e-22

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: 93.61  E-value: 9.62e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   69 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlpREKGRMRFHKLQNVQIALDY 148
Cdd:cd21309     16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKY---------HQRPTFRQMQLENVSVALEF 86
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1777507480  149 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 186
Cdd:cd21309     87 LDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
202-299 1.97e-20

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: 88.94  E-value: 1.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  202 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 280
Cdd:cd21195      8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
                           90
                   ....*....|....*....
gi 1777507480  281 DVPQPDEKSIITYVSSLYD 299
Cdd:cd21195     88 SAQEPDKLSMVMYLSKFYE 106
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
198-298 3.10e-20

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: 88.17  E-value: 3.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  198 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 277
Cdd:cd21200      1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
                           90       100
                   ....*....|....*....|...
gi 1777507480  278 EDVDV--PQPDEKSIITYVSSLY 298
Cdd:cd21200     81 EDMVRmgNRPDWKCVFTYVQSLY 103
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
194-299 1.12e-19

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: 86.93  E-value: 1.12e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  194 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 273
Cdd:cd21251      1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
                           90       100
                   ....*....|....*....|....*..
gi 1777507480  274 LLDPEDV-DVPQPDEKSIITYVSSLYD 299
Cdd:cd21251     81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
198-297 1.99e-19

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: 85.99  E-value: 1.99e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  198 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 277
Cdd:cd21255      1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
                           90       100
                   ....*....|....*....|.
gi 1777507480  278 ED-VDVPQPDEKSIITYVSSL 297
Cdd:cd21255     80 ADmVLLPIPDKLIVMTYLCQL 100
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
201-297 2.81e-19

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: 85.45  E-value: 2.81e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   201 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 276
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 1777507480   277 PEDVDVPQPDEKSIITYVSSL 297
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
641-819 2.32e-17

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: 83.65  E-value: 2.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  641 LHGFVAAATKELMWLSEKEDEEVGFDWSERSTNTAAKKDSYSALMRELELKEKKIKEIQSTGDRLLREDHPARPTVESFQ 720
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  721 AALQTQWSWMLQLCCCVEAHLKENTAYFQFFSDVREAEEQLRKLQETLRRKYTCDrsiTVTRLEDLLQDAQDEKDQLNEY 800
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
                          170
                   ....*....|....*....
gi 1777507480  801 RGHLSGLAKRAKAIVQLKP 819
Cdd:cd00176    159 EPRLKSLNELAEELLEEGH 177
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
202-299 2.68e-17

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: 79.92  E-value: 2.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  202 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 280
Cdd:cd21250      8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
                           90
                   ....*....|....*....
gi 1777507480  281 DVPQPDEKSIITYVSSLYD 299
Cdd:cd21250     88 SAEEPDKLSMVMYLSKFYE 106
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
198-297 3.22e-17

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: 79.90  E-value: 3.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  198 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 277
Cdd:cd21254      1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
                           90       100
                   ....*....|....*....|.
gi 1777507480  278 ED-VDVPQPDEKSIITYVSSL 297
Cdd:cd21254     80 SDmVLLAVPDKLTVMTYLYQI 100
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
71-183 3.80e-17

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: 79.55  E-value: 3.80e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   71 QKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPRerdvirssrlPREKGRMRFHKLQNVQIALDY 148
Cdd:cd21212      1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPG----------IHSRPKTRAQKLENIQACLQF 70
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1777507480  149 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 183
Cdd:cd21212     71 LAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
72-181 3.94e-17

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: 79.30  E-value: 3.94e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   72 KKTFTKWVNKHL-IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpREKGRMRFHKLQNVQIALDYLR 150
Cdd:cd00014      1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKI----------NKKPKSPFKKRENINLFLNACK 70
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1777507480  151 HRQV-KLVNIRNDDI-ADGNPKLTLGLIWTIIL 181
Cdd:cd00014     71 KLGLpELDLFEPEDLyEKGNLKKVLGTLWALAL 103
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
200-311 1.15e-16

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: 78.49  E-value: 1.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  200 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 279
Cdd:cd21259      3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1777507480  280 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 311
Cdd:cd21259     83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
203-298 3.48e-16

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: 77.02  E-value: 3.48e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  203 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 281
Cdd:cd21199     13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
                           90
                   ....*....|....*..
gi 1777507480  282 VPQPDEKSIITYVSSLY 298
Cdd:cd21199     92 MERPDWQSVMSYVTAIY 108
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
200-299 5.04e-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: 76.16  E-value: 5.04e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  200 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 279
Cdd:cd21261      3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
                           90       100
                   ....*....|....*....|..
gi 1777507480  280 VDV--PQPDEKSIITYVSSLYD 299
Cdd:cd21261     83 MMVmgRKPDPMCVFTYVQSLYN 104
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
200-303 8.19e-16

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: 75.86  E-value: 8.19e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  200 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 279
Cdd:cd21258      3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
                           90       100
                   ....*....|....*....|....*.
gi 1777507480  280 VDV--PQPDEKSIITYVSSLYDAMPR 303
Cdd:cd21258     83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2938-2976 1.21e-15

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 72.75  E-value: 1.21e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2938 LLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEMNEIL 2976
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2360-2398 2.24e-15

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 71.98  E-value: 2.24e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2360 LLEAQIATGGIIDPVHSHRLPVDVAFQRGYFDEEMSRIL 2398
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1701-1739 3.94e-15

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 71.20  E-value: 3.94e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 1701 LLEAQIATGGIIDPVHSHRVPVDVAFQRGYFDEEMSRVL 1739
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
68-179 4.57e-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: 73.72  E-value: 4.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   68 DRVQKKTFTKWVNKHLIKAQ-RHISDLYEDLRDGHNLISLLEVLSGDSLPRERDVIRSSRLPRekgrmrfhkLQNVQIAL 146
Cdd:cd21225      2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEPKNRIQM---------IQNLHLAM 72
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1777507480  147 DYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTI 179
Cdd:cd21225     73 LFIEEDlKIRVQGIGAEDFVDNNKKLILGLLWTL 106
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
64-182 4.74e-15

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: 73.86  E-value: 4.74e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   64 ADERDrvqKKTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLsgDSLprERDVIRSSRLPREKGRMRFHKLQNVQ 143
Cdd:cd21219      1 EGSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVL--DKI--QPGCVNWKKVNKPKPLNKFKKVENCN 68
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1777507480  144 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 182
Cdd:cd21219     69 YAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
71-183 7.65e-15

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


Pssm-ID: 409062  Cd Length: 107  Bit Score: 73.10  E-value: 7.65e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   71 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerDVIRSsrlPREKGRMRfhklQNVQIALDY 148
Cdd:cd21213      1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLP---GIDWN---PTTDAERK----ENVEKVLQF 70
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1777507480  149 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 183
Cdd:cd21213     71 MASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
198-298 1.18e-14

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: 72.80  E-value: 1.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  198 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 277
Cdd:cd21256     14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
                           90       100
                   ....*....|....*....|..
gi 1777507480  278 ED-VDVPQPDEKSIITYVSSLY 298
Cdd:cd21256     93 NEmVRTERPDWQSVMTYVTAIY 114
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
200-301 1.45e-14

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: 72.42  E-value: 1.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  200 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 279
Cdd:cd21260      3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
                           90       100
                   ....*....|....*....|...
gi 1777507480  280 -VDVPQPDEKSIITYVSSLYDAM 301
Cdd:cd21260     83 mVRMSVPDSKCVYTYIQELYRSL 105
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2619-2657 1.93e-14

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 69.28  E-value: 1.93e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2619 LLEAQAATGFLLDPVKGDRLTVDEAVRKGLVGPELHDRL 2657
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
198-295 9.26e-14

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: 69.72  E-value: 9.26e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  198 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI----DMNKVYRqtnLENLDQAFSVAERDLGVTR 273
Cdd:cd21230      1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
                           90       100
                   ....*....|....*....|..
gi 1777507480  274 LLDPEDVDVPQPDEKSIITYVS 295
Cdd:cd21230     75 LITPEEIINPNVDEMSVMTYLS 96
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
198-298 1.05e-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: 70.06  E-value: 1.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  198 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 277
Cdd:cd21257      8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
                           90       100
                   ....*....|....*....|..
gi 1777507480  278 ED-VDVPQPDEKSIITYVSSLY 298
Cdd:cd21257     87 SEmMYTDRPDWQSVMQYVAQIY 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1125-1315 1.55e-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: 72.48  E-value: 1.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1125 EDVLKAHEEQLKEAQaVPATLPELEATKAALKKLRAQAEAQQPVFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1204
Cdd:cd00176     13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1205 TQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLDSWLQDAKRRQEQIQAVPLANSqvVREQLRQEKALLEEIERH 1284
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLES--VEELLKKHKELEEELEAH 158
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1777507480 1285 GEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1315
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2029-2067 2.35e-13

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 66.20  E-value: 2.35e-13
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2029 LLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDEETHTAL 2067
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
545-734 3.64e-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: 71.32  E-value: 3.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  545 LRYLQDLLAWVGENQRRVDSAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARTDEGQLSPATRGAY---RDCLGRLD 621
Cdd:cd00176      6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  622 LQYAKLLNSSKARLRSLE---SLHGFVAAATKELMWLSEKEDEEVGFDWSERSTNTAAKKDSYSALMRELELKEKKIKEI 698
Cdd:cd00176     86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1777507480  699 QSTGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 734
Cdd:cd00176    166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
73-186 5.15e-13

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: 68.03  E-value: 5.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   73 KTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLsgdslprERDVIRSSRLPREKGRMR--FHKLQNVQIALDYLR 150
Cdd:cd21298      9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKI-------KPGVVDWSRVNKPFKKLGanMKKIENCNYAVELGK 79
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1777507480  151 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 186
Cdd:cd21298     80 KLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2284-2322 1.24e-12

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 64.27  E-value: 1.24e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2284 LLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPELHEKL 2322
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3207-3245 1.30e-12

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 64.27  E-value: 1.30e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 3207 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 3245
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
200-299 1.70e-12

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: 66.21  E-value: 1.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  200 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 275
Cdd:cd00014      1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
                           90       100
                   ....*....|....*....|....
gi 1777507480  276 DPEDVdVPQPDEKSIITYVSSLYD 299
Cdd:cd00014     81 EPEDL-YEKGNLKKVLGTLWALAL 103
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
200-300 2.09e-12

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: 65.84  E-value: 2.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  200 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 279
Cdd:cd21196      5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
                           90       100
                   ....*....|....*....|.
gi 1777507480  280 VdVPQPDEKSIITYVSSLYDA 300
Cdd:cd21196     85 V-VAGSDPLGLIAYLSHFHSA 104
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2862-2900 2.89e-12

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.12  E-value: 2.89e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2862 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 2900
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2695-2733 3.06e-12

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.12  E-value: 3.06e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2695 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTYDQL 2733
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
200-295 4.21e-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: 4.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  200 KEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 278
Cdd:cd21229      5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
                           90
                   ....*....|....*..
gi 1777507480  279 DVDVPQPDEKSIITYVS 295
Cdd:cd21229     82 DLSSPHLDELSGMTYLS 98
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
66-177 1.21e-11

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: 64.37  E-value: 1.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   66 ERDRvQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSgdslPRERDVIRSSRLPREKGRMRFHKLQNVQIA 145
Cdd:cd21300      4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVI----PGSVNWKKVNKAPASAEISRFKAVENTNYA 76
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1777507480  146 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIW 177
Cdd:cd21300     77 VELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
89-180 2.10e-11

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: 63.38  E-value: 2.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   89 HISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirsSRLPrEKGRMRfhKLQNVQIALDYLRHRQV----KLVNIRNDDI 164
Cdd:cd21223     25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSK-----LRVP-AISRLQ--KLHNVEVALKALKEAGVlrggDGGGITAKDI 96
                           90
                   ....*....|....*.
gi 1777507480  165 ADGNPKLTLGLIWTII 180
Cdd:cd21223     97 VDGHREKTLALLWRII 112
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
937-1505 2.59e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 2.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  937 FRTLKPEEQRQALRSLELHYQAFLRDSQDAGgfgpEDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIR 1016
Cdd:COG1196    215 YRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1017 LQLEACETRTVHRLRLplDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALpepspAAPTLRSELELTLGK 1096
Cdd:COG1196    291 YELLAELARLEQDIAR--LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-----AEEELEEAEAELAEA 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1097 LEQVRSLSAIYLEKLKTISlviRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDEL 1176
Cdd:COG1196    364 EEALLEAEAELAEAEEELE---ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1177 RGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQtdvRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQI 1256
Cdd:COG1196    441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE---LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1257 QAVPLAnsQVVREQLRQEKALLEEIE-----RHGEKVEECQRFAKQYINAIKDYELQLVT-YKAQLEPVASPAKKPKVQS 1330
Cdd:COG1196    518 GLRGLA--GAVAVLIGVEAAYEAALEaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARG 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1331 GSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRERFIEQEKA 1410
Cdd:COG1196    596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1411 KLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAEEN--- 1487
Cdd:COG1196    676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAlee 755
                          570       580
                   ....*....|....*....|....*
gi 1777507480 1488 -------QRLRERLQHLEEEhRAAL 1505
Cdd:COG1196    756 lpeppdlEELERELERLERE-IEAL 779
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1625-1663 2.63e-11

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 60.42  E-value: 2.63e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 1625 LLEAQAASGFLLDPVRNRQLTVNEAVKEGVVGPELHHKL 1663
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3283-3321 9.40e-10

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 56.18  E-value: 9.40e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 3283 FLEVQYLTGGLIEPDAPGRVPLEEALQRGTVDARTAQKL 3321
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
989-1319 9.88e-10

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: 65.09  E-value: 9.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  989 QQLLQSLEQGEQEESRCQRCISELKDirlQLEACETRTVHRLRLPLDKEPARECAQ--RIAEQQKAQAEVEGLGKGVARL 1066
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKAERYQALLKEKREYEGyeLLKEKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1067 SAEAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRSTQG----AEDVLKAHEEQLKE 1137
Cdd:TIGR02169  250 EEELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELED 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1138 AQAVPATL-PELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQllerwqavla 1216
Cdd:TIGR02169  320 AEERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------- 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1217 qtdvRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQavplANSQVVREQLrqeKALLEEIERHGEKVEECQRFAK 1296
Cdd:TIGR02169  390 ----YREKLEKLKREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKI---NELEEEKEDKALEIKKQEWKLE 458
                          330       340
                   ....*....|....*....|...
gi 1777507480 1297 QYINAIKDYELQLVTYKAQLEPV 1319
Cdd:TIGR02169  459 QLAADLSKYEQELYDLKEEYDRV 481
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
72-180 1.07e-09

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: 58.35  E-value: 1.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   72 KKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERdvirssRLPREKGRMRFHKLQNV 142
Cdd:cd21217      3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTID-ER------KLNKKKPKNIFEATENL 75
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1777507480  143 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 180
Cdd:cd21217     76 NLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
198-300 1.31e-09

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: 58.16  E-value: 1.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  198 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 276
Cdd:cd21314     11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
                           90       100
                   ....*....|....*....|....
gi 1777507480  277 PEDVDVPQPDEKSIITYVSSLYDA 300
Cdd:cd21314     88 PEEIVDPNVDEHSVMTYLSQFPKA 111
PLEC smart00250
Plectin repeat;
3205-3242 1.49e-09

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 55.57  E-value: 1.49e-09
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507480  3205 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 3242
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1957-1991 4.32e-09

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 54.26  E-value: 4.32e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1777507480 1957 QAGTGHIVDPTTSARLTVAEAVRAGLVGPELHEKL 1991
Cdd:pfam00681    5 QAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
193-295 4.85e-09

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: 56.71  E-value: 4.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  193 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 271
Cdd:cd21315     11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
                           90       100
                   ....*....|....*....|....
gi 1777507480  272 TRLLDPEDVDVPQPDEKSIITYVS 295
Cdd:cd21315     88 PQLIKPEEMVNPKVDELSMMTYLS 111
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
66-185 5.50e-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: 56.93  E-value: 5.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   66 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSSRLPREKGRMRfhKLQNVQIA 145
Cdd:cd21331     18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIK---VPVDWNKVNKPPYPKLGANMK--KLENCNYA 90
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1777507480  146 LDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 185
Cdd:cd21331     91 VELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
193-300 1.22e-08

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


Pssm-ID: 409162  Cd Length: 110  Bit Score: 55.48  E-value: 1.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  193 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 271
Cdd:cd21313      3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
                           90       100
                   ....*....|....*....|....*....
gi 1777507480  272 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 300
Cdd:cd21313     80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
886-1518 1.26e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.23  E-value: 1.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  886 QEAQEAIARLEAQHQALVALWHQLHTDMKSL-LAWQSLSRDVQLIrswslvtfrtlkpEEQRQALRSLELHYQAFLRDSQ 964
Cdd:TIGR02168  347 EELKEELESLEAELEELEAELEELESRLEELeEQLETLRSKVAQL-------------ELQIASLNNEIERLEARLERLE 413
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  965 DAggfgpEDRLQAEREygscsrhyqQLLQSLEQGEQEEsrCQRCISELKDIRLQLEACETRTVHRL------------RL 1032
Cdd:TIGR02168  414 DR-----RERLQQEIE---------ELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALeelreeleeaeqAL 477
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1033 PLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEK----VLALPEPSPAAPTLRSELELTLGKLEQ---VRSLSA 1105
Cdd:TIGR02168  478 DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgiLGVLSELISVDEGYEAAIEAALGGRLQavvVENLNA 557
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1106 I-----YLEK--LKTISLVIRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKAALKKlraqaeAQQPVFDALR--DEL 1176
Cdd:TIGR02168  558 AkkaiaFLKQneLGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRK------ALSYLLGGVLvvDDL 631
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1177 RGAQEVGERLqqRHGERDV----EVERWRERVTQLLERWQAVLAQtdvRQRELEQLGRQLRYYRESADPLDSWLQDAKRR 1252
Cdd:TIGR02168  632 DNALELAKKL--RPGYRIVtldgDLVRPGGVITGGSAKTNSSILE---RRREIEELEEKIEELEEKIAELEKALAELRKE 706
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1253 QEQIQAVPLANSQVVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEP-----VASPAKKPK 1327
Cdd:TIGR02168  707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeelAEAEAEIEE 786
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1328 VQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQEtqaLRQSFLSEKDSLLQRERFIEQ 1407
Cdd:TIGR02168  787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED---LEEQIEELSEDIESLAAEIEE 863
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1408 EKAKLEQLfQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAEEN 1487
Cdd:TIGR02168  864 LEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
                          650       660       670
                   ....*....|....*....|....*....|.
gi 1777507480 1488 QRLRERLQHLEEEhraALAHSEEVPASQATA 1518
Cdd:TIGR02168  943 ERLSEEYSLTLEE---AEALENKIEDDEEEA 970
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
202-297 1.32e-08

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: 56.16  E-value: 1.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  202 KLLL-WSQrMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNL-----------------------EN 257
Cdd:cd21224      3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1777507480  258 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 297
Cdd:cd21224     82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
PLEC smart00250
Plectin repeat;
2936-2972 2.59e-08

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 52.10  E-value: 2.59e-08
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  2936 IRLLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEM 2972
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
64-183 2.60e-08

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: 54.90  E-value: 2.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   64 ADERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDVIRSSRLPrekgrmrfHKLQNVQ 143
Cdd:cd21222     10 APEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPLHEYHLTPSTDD--------EKLHNVK 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1777507480  144 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 183
Cdd:cd21222     82 LALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
71-182 2.64e-08

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: 54.43  E-value: 2.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   71 QKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirSSRLPRekgRMRFHKLQNVQIALDYLR 150
Cdd:cd21299      5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKH----ANKPPI---KMPFKKVENCNQVVKIGK 75
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1777507480  151 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 182
Cdd:cd21299     76 QLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
SPEC smart00150
Spectrin repeats;
642-734 8.47e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.72  E-value: 8.47e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   642 HGFVAAATKELMWLSEKEDEEVGFDWSERSTNTAAKKDSYSALMRELELKEKKIKEIQSTGDRLLREDHPARPTVESFQA 721
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90
                    ....*....|...
gi 1777507480   722 ALQTQWSWMLQLC 734
Cdd:smart00150   81 ELNERWEELKELA 93
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
73-179 9.77e-08

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: 52.72  E-value: 9.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   73 KTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLpreRDVirsSRLPREKGRMrfhkLQNVQIALDYLR 150
Cdd:cd21286      3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKV---EDI---NGCPRSQSQM----IENVDVCLSFLA 72
                           90       100
                   ....*....|....*....|....*....
gi 1777507480  151 HRQVKLVNIRNDDIADGNPKLTLGLIWTI 179
Cdd:cd21286     73 ARGVNVQGLSAEEIRNGNLKAILGLFFSL 101
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3039-3067 3.76e-07

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 48.86  E-value: 3.76e-07
                           10        20
                   ....*....|....*....|....*....
gi 1777507480 3039 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 3067
Cdd:pfam00681   11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
886-1522 5.69e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 5.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  886 QEAQEAIARLEAQHQALVALWhqlhtdmksllawqslsrdvqlirswslvtfrtlkpEEQRQALRSLELHYQAflrdsqd 965
Cdd:COG1196    249 EELEAELEELEAELAELEAEL------------------------------------EELRLELEELELELEE------- 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  966 aggfgpedrLQAEreygscsrhYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEAcetrtvhrlrlpldkeparECAQR 1045
Cdd:COG1196    286 ---------AQAE---------EYELLAELARLEQDIARLEERRRELEERLEELEE-------------------ELAEL 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1046 IAEQQKAQAEVEGLGKGVARLSAEAEKVLALpepspAAPTLRSELELTLGKLEQVRSLSAIYLEKLktislvirSTQGAE 1125
Cdd:COG1196    329 EEELEELEEELEELEEELEEAEEELEEAEAE-----LAEAEEALLEAEAELAEAEEELEELAEELL--------EALRAA 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1126 DVLKAHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVT 1205
Cdd:COG1196    396 AELAAQLEELEEAEE------ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1206 QLLERWQAVLAQtdvRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQAVPLAnsQVVREQLRQEKALLEEIE--- 1282
Cdd:COG1196    470 EEAALLEAALAE---LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA--GAVAVLIGVEAAYEAALEaal 544
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1283 --RHGEKVEECQRFAKQYINAIKDYELQLVT-YKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKF 1359
Cdd:COG1196    545 aaALQNIVVEDDEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1360 ISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRERFIEQEKAKLEQLFQEEVAKAQKLReeqqrqqqqmeq 1439
Cdd:COG1196    625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE------------ 692
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1440 ekqqlvASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAEENQRLRERLQHLEEEHRAALAHSEEVPASQATAT 1519
Cdd:COG1196    693 ------LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766

                   ...
gi 1777507480 1520 KAL 1522
Cdd:COG1196    767 REL 769
PLEC smart00250
Plectin repeat;
2358-2394 7.52e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 47.86  E-value: 7.52e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  2358 IRLLEAQIATGGIIDPVHSHRLPVDVAFQRGYFDEEM 2394
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
944-1656 7.74e-07

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: 55.51  E-value: 7.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  944 EQRQALRSLE-----LHYQAFLRDSQDAGGfgPEDRLQAEREYGSCSRHYQQLLQSLEQGEQEESrcqrcISELKDIRL- 1017
Cdd:pfam15921  332 ELREAKRMYEdkieeLEKQLVLANSELTEA--RTERDQFSQESGNLDDQLQKLLADLHKREKELS-----LEKEQNKRLw 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1018 QLEACETRTVHRLRLPLDK---EPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVlalpepspaaPTLRSELELTL 1094
Cdd:pfam15921  405 DRDTGNSITIDHLRRELDDrnmEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKV----------SSLTAQLESTK 474
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1095 GKLEQVrslsaiyLEKLKTISLVIRSTQGAEDVLKAHEEQLKEAqavpatlpeLEATKAALKKLRAQAEAQQPVFDALRD 1174
Cdd:pfam15921  475 EMLRKV-------VEELTAKKMTLESSERTVSDLTASLQEKERA---------IEATNAEITKLRSRVDLKLQELQHLKN 538
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1175 E---LRGAQEVGERLQQRHGERDVEVERWR---ERVTQLLERWQ----AVLAQTDVRQRELEQLGRQLRYYRESADPLDS 1244
Cdd:pfam15921  539 EgdhLRNVQTECEALKLQMAEKDKVIEILRqqiENMTQLVGQHGrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDA 618
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1245 WLQD--AKRRQEQIQAVPLANSQvvREQLRQEKALLEEIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVASP 1322
Cdd:pfam15921  619 KIREleARVSDLELEKVKLVNAG--SERLRAVKDIKQERDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETT 693
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1323 AKKPKVQsgsesviqeyvdLRTRYSELTTLTSqyikfiseTLRRMEEEEMQTVQQEQLLQETQALRQ----------SFL 1392
Cdd:pfam15921  694 TNKLKMQ------------LKSAQSELEQTRN--------TLKSMEGSDGHAMKVAMGMQKQITAKRgqidalqskiQFL 753
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1393 SEKDSLLQRER-FIEQEKAKLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQlVASMEEA---------------RRQQR 1456
Cdd:pfam15921  754 EEAMTNANKEKhFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEK-VANMEVAldkaslqfaecqdiiQRQEQ 832
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1457 EAeegVRRKQEELQRLEEQRQQQEKllaeENQRLRERLQHLEEEHRaalAHSeEVPASQATATKALPNGRDAldgPATET 1536
Cdd:pfam15921  833 ES---VRLKLQHTLDVKELQGPGYT----SNSSMKPRLLQPASFTR---THS-NVPSSQSTASFLSHHSRKT---NALKE 898
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1537 EPEHAFDGLRQKV--PAQQLQEVGILSAEELQRLVQG-------RTTVAELEQREDV----RCYLQGRSSIAGLLLqpSN 1603
Cdd:pfam15921  899 DPTRDLKQLLQELrsVINEEPTVQLSKAEDKGRAPSLgalddrvRDCIIESSLRSDIchssSNSLQTEGSKSSETC--SR 976
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1777507480 1604 EKLSVYAALRRQLLS----PGTALILLEAQAASGFLLDPVRNRQLTVNEAVKEGVVG 1656
Cdd:pfam15921  977 EPVLLHAGELEDPSScftfPSTASPSVKNSASRSFHSSPKKSPVHSLLTSSAEGSIG 1033
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
987-1530 8.18e-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: 8.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  987 HYQQLLQSLEQGEQEESRCQRcisELKDIRLQLEACETR-TVHRLRLPLDKEparecaqriaEQQKAQAEVEGLGKGVAR 1065
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEE---ELEELTAELQELEEKlEELRLEVSELEE----------EIEELQKELYALANEISR 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1066 LsaEAEKVLAlpepSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGaedVLKAHEEQLKEAQAvpatl 1145
Cdd:TIGR02168  300 L--EQQKQIL----RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE---ELESLEAELEELEA----- 365
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1146 pELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERwqAVLAQTDVRQREL 1225
Cdd:TIGR02168  366 -ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK--LEEAELKELQAEL 442
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1226 EQLGRQLRYYRESADPLDSWLQDAKRRQEQI-QAVPLANSQVvrEQLRQEKALLEEIERHGEKVEECQRFAK-------- 1296
Cdd:TIGR02168  443 EELEEELEELQEELERLEEALEELREELEEAeQALDAAEREL--AQLQARLDSLERLQENLEGFSEGVKALLknqsglsg 520
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1297 ------QYINAIKDYELQLVTY-------------KAQLEPVASPAKK---------------PKVQSGSESVIQEYVDL 1342
Cdd:TIGR02168  521 ilgvlsELISVDEGYEAAIEAAlggrlqavvvenlNAAKKAIAFLKQNelgrvtflpldsikgTEIQGNDREILKNIEGF 600
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1343 RTRYSELTTLTSQYIK---------FISETL-------RRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRERFIE 1406
Cdd:TIGR02168  601 LGVAKDLVKFDPKLRKalsyllggvLVVDDLdnalelaKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIE 680
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1407 QEKAKLEQLfQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAEE 1486
Cdd:TIGR02168  681 ELEEKIEEL-EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*..
gi 1777507480 1487 NQR---LRERLQHLEEEHRAALAHSEEVPASQATATKALPNGRDALD 1530
Cdd:TIGR02168  760 EAEieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
71-191 1.29e-06

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


Pssm-ID: 409174  Cd Length: 148  Bit Score: 50.83  E-value: 1.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   71 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRLPrekgrmrFHKLQN 141
Cdd:cd21325     25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTID-ERAINKKKLTP-------FIIQEN 96
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1777507480  142 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 191
Cdd:cd21325     97 LNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
71-190 1.75e-06

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: 50.04  E-value: 1.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   71 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRLPrekgrmrFHKLQN 141
Cdd:cd21323     25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTID-ERAINKKKLTP-------FTISEN 96
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1777507480  142 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 190
Cdd:cd21323     97 LNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
PLEC smart00250
Plectin repeat;
1699-1735 1.84e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.71  E-value: 1.84e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  1699 IRLLEAQIATGGIIDPVHSHRVPVDVAFQRGYFDEEM 1735
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
2822-2859 2.21e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.71  E-value: 2.21e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507480  2822 QKFLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTA 2859
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2027-2063 2.46e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.32  E-value: 2.46e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  2027 LRLLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDEET 2063
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1036-1416 2.55e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 2.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1036 KEPARECAQRIAEQQKAQAEVEG----LGKGVARLSAEAEKVLALPEpspaaptLRSELE-----LTLGKLEQVRslsai 1106
Cdd:TIGR02168  171 KERRKETERKLERTRENLDRLEDilneLERQLKSLERQAEKAERYKE-------LKAELRelelaLLVLRLEELR----- 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1107 ylEKLKTISLVIRStqgAEDVLKAHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERL 1186
Cdd:TIGR02168  239 --EELEELQEELKE---AEEELEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL 307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1187 QQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQAVPLANSQV 1266
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1267 VREQLRQEKALLEEIERhgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRY 1346
Cdd:TIGR02168  388 VAQLELQIASLNNEIER-----------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1347 SELTTLTSQyikfISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRERFIEQEKAKLEQLF 1416
Cdd:TIGR02168  457 ERLEEALEE----LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGIL 522
PLEC smart00250
Plectin repeat;
2617-2652 2.91e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.32  E-value: 2.91e-06
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1777507480  2617 RLLLEAQAATGFLLDPVKGDRLTVDEAVRKGLVGPE 2652
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
193-300 2.94e-06

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


Pssm-ID: 409161  Cd Length: 114  Bit Score: 48.65  E-value: 2.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  193 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 271
Cdd:cd21312      7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
                           90       100
                   ....*....|....*....|....*....
gi 1777507480  272 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 300
Cdd:cd21312     84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2824-2862 3.44e-06

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 46.17  E-value: 3.44e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2824 FLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTAFEL 2862
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
66-186 4.57e-06

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: 48.44  E-value: 4.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   66 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSSRLPREKGRMRfhKLQNVQIA 145
Cdd:cd21329      2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMTR---VPVDWGHVNKPPYPALGGNMK--KIENCNYA 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1777507480  146 LDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 186
Cdd:cd21329     75 VELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1147-1349 4.89e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 4.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1147 ELEATKAALKKLRAQAEAQQPV------FDALRDELRGAQEVGERLQQRHGERdvEVERWRERVTQLLERWQAVLAQTDV 1220
Cdd:COG4913    236 DLERAHEALEDAREQIELLEPIrelaerYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELER 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1221 RQRELEQLGRQLRyyresadpldswlqdakRRQEQIQAVplansqvvreQLRQEKALLEEIERHGEKVEECQRFAKQYIN 1300
Cdd:COG4913    314 LEARLDALREELD-----------------ELEAQIRGN----------GGDRLEQLEREIERLERELEERERRRARLEA 366
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1777507480 1301 AIKDYELQLVTYKAQLEPVASPAK--KPKVQSGSESVIQEYVDLRTRYSEL 1349
Cdd:COG4913    367 LLAALGLPLPASAEEFAALRAEAAalLEALEEELEALEEALAEAEAALRDL 417
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1145-1504 5.54e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 5.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1145 LPELEATKAALKKLRAQAEAqqpvFDALRDELRGAQEVGERLQQRHGERDVEVERWR--ERVTQLLERWQAVLAQTDVRQ 1222
Cdd:COG4717     70 LKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELP 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1223 RELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQAVPLANSQVVREQLRQekaLLEEIERHGEKVEECQRFAKQYINAI 1302
Cdd:COG4717    146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAELEEELEEAQEEL 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1303 KDYELQLVTYKAQLEPVASPAK--KPKVQSGSESVI-------QEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQ 1373
Cdd:COG4717    223 EELEEELEQLENELEAAALEERlkEARLLLLIAAALlallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1374 TVQQEQLLQETQALRQ----SFLSEKD-SLLQRERFIEQEKAKLEQLFQ--EEVAKAQKLREEQQRQQQQMEQEKQQLVA 1446
Cdd:COG4717    303 EAEELQALPALEELEEeeleELLAALGlPPDLSPEELLELLDRIEELQEllREAEELEEELQLEELEQEIAALLAEAGVE 382
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1777507480 1447 SMEEARRQQREAEEGV----RRKQEELQRLEEQRQQQEKLLAEENQRLRERLQHLEEEHRAA 1504
Cdd:COG4717    383 DEEELRAALEQAEEYQelkeELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEEL 444
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1128-1501 7.43e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 7.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1128 LKAHEEQLKEAQAVPATL-PELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQ 1206
Cdd:TIGR02168  686 IEELEEKIAELEKALAELrKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1207 LLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLDSWLqDAKRRQEQIQAVPLANSQVVREQLRQEKALLE-EIERHG 1285
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL-DELRAELTLLNEEAANLRERLESLERRIAATErRLEDLE 844
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1286 EKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSELttltsqyikfiSETLR 1365
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELE---------ALLNERASLEEALALLRSELEEL-----------SEELR 904
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1366 RMEEEemqtvqqeqllqeTQALRQSfLSEKDSLLqrerfiEQEKAKLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQLV 1445
Cdd:TIGR02168  905 ELESK-------------RSELRRE-LEELREKL------AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1777507480 1446 ASMEEARRQQREAEEGVRRkqeelqrleeqrQQQEKLLA-EENQRLRERLQHLEEEH 1501
Cdd:TIGR02168  965 DDEEEARRRLKRLENKIKE------------LGPVNLAAiEEYEELKERYDFLTAQK 1009
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1105-1305 8.12e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 8.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1105 AIYLEKLKTISLVIRSTQGAEDVLKAHEEQLKEAQAVPATL----------PELEATKAALKKLRAQAEAQQPVFDALRD 1174
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeidvASAEREIAELEAELERLDASSDDLAALEE 692
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1175 ELRGAQEVGERLQQRHGERDVEVERWRERVTQLlerwqavlaqtdvrQRELEQLGRQLRYYRESADPLDSWLQDAKRRQE 1254
Cdd:COG4913    693 QLEELEAELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLELRALLEERFAAA 758
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1777507480 1255 QIQAVPlansQVVREQLRQE-KALLEEIERHGEKVEEC-QRFAKQYINAIKDY 1305
Cdd:COG4913    759 LGDAVE----RELRENLEERiDALRARLNRAEEELERAmRAFNREWPAETADL 807
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
71-190 9.60e-06

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


Pssm-ID: 409173  Cd Length: 145  Bit Score: 48.08  E-value: 9.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   71 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRLPrekgrmrFHKLQN 141
Cdd:cd21324     25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTID-ERTINKKKLTP-------FTIQEN 96
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1777507480  142 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 190
Cdd:cd21324     97 LNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
943-1501 1.16e-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: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  943 EEQRQALRSLELHYQAFLRDSQDAGgfgpEDRLQAEREygscSRHYQQLLQSLEQGEQEESRcqrcisELKDIRLQLEAC 1022
Cdd:COG1196    270 EELRLELEELELELEEAQAEEYELL----AELARLEQD----IARLEERRRELEERLEELEE------ELAELEEELEEL 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1023 ETRTVHRLRLPLDKEPARECAQ--RIAEQQKAQAEVEGLGKGVARLSAEAEKVLALpepSPAAPTLRSELELTLGKLEQV 1100
Cdd:COG1196    336 EEELEELEEELEEAEEELEEAEaeLAEAEEALLEAEAELAEAEEELEELAEELLEA---LRAAAELAAQLEELEEAEEAL 412
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1101 RSLSAIYLEKLKTISLVIRSTQGAEDVLKAHEEQLKEAQAvpATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQ 1180
Cdd:COG1196    413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA--ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1181 EVGERLQQRHGERDVEVERWRE--------RVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLDSWLQDAKRR 1252
Cdd:COG1196    491 ARLLLLLEAEADYEGFLEGVKAalllaglrGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAK 570
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1253 QEQIQAVPLANSQVVREQLRQEKALLEEIERHGEKVEECQRFAKQYinAIKDYELQLVTYKAQLEPVASPAKKpkVQSGS 1332
Cdd:COG1196    571 AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY--VLGDTLLGRTLVAARLEAALRRAVT--LAGRL 646
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1333 ESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRERFIEQEKAKL 1412
Cdd:COG1196    647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1413 EQLFQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEgvrrkqeelqrleeqrqqqeK--------LLA 1484
Cdd:COG1196    727 EEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER--------------------EiealgpvnLLA 786
                          570
                   ....*....|....*...
gi 1777507480 1485 -EENQRLRERLQHLEEEH 1501
Cdd:COG1196    787 iEEYEELEERYDFLSEQR 804
PLEC smart00250
Plectin repeat;
2246-2281 1.36e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.36e-05
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1777507480  2246 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTA 2281
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
65-180 1.38e-05

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: 47.06  E-value: 1.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   65 DERDRVQkktFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEvlsgDSLPRERDVIRSSRLPRE-KGRM 134
Cdd:cd21294      4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLIN----DSVPDTIDERVLNKPPRKnKPLN 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1777507480  135 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 180
Cdd:cd21294     77 NFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
PLEC smart00250
Plectin repeat;
2693-2730 1.40e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.40e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507480  2693 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTY 2730
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3032-3060 1.51e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.51e-05
                            10        20
                    ....*....|....*....|....*....
gi 1777507480  3032 VRKRRVVIVDPETGKEMSVYEAYRKGLID 3060
Cdd:smart00250    6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
PTZ00121 PTZ00121
MAEBL; Provisional
941-1516 1.57e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  941 KPEEQRQAL---RSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSR-----HYQQLLQSLEQGEQ-EESRCQRCISE 1011
Cdd:PTZ00121  1177 KAEAARKAEevrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKaeavkKAEEAKKDAEEAKKaEEERNNEEIRK 1256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1012 LKDIRLQ--------LEACETRTVHRLRLPLDKEPARECAQ----RIAEQQKAQAE----VEGLGKGV--ARLSAEAEKV 1073
Cdd:PTZ00121  1257 FEEARMAhfarrqaaIKAEEARKADELKKAEEKKKADEAKKaeekKKADEAKKKAEeakkADEAKKKAeeAKKKADAAKK 1336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1074 LAlPEPSPAAPTLRSELELTLGKLEQVRslsaiylEKLKTISLVIRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKA 1153
Cdd:PTZ00121  1337 KA-EEAKKAAEAAKAEAEAAADEAEAAE-------EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1154 ALKKlraqAEAQQPVFDALR---DELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQlgr 1230
Cdd:PTZ00121  1409 ELKK----AAAAKKKADEAKkkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE--- 1481
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1231 qlryyRESADPLDSWLQDAKRRQEQIQAVPLANSQVVREQLRQEKALLEEIERHGE--KVEEcqrfAKQYINAIKDYELQ 1308
Cdd:PTZ00121  1482 -----AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakKADE----AKKAEEKKKADELK 1552
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1309 LVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLR----TRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQET 1384
Cdd:PTZ00121  1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1385 QALRQSFLSEKDSLLQRERFIEQE------KAKLEQLFQEEVAKAQKLReeqqRQQQQMEQEKQQLVASMEEARR--QQR 1456
Cdd:PTZ00121  1633 KKVEQLKKKEAEEKKKAEELKKAEeenkikAAEEAKKAEEDKKKAEEAK----KAEEDEKKAAEALKKEAEEAKKaeELK 1708
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1777507480 1457 EAEEGVRRKQEE---LQRLEEQRQQQEKLLAEENQRLRERLQhLEEEHRAALAHSEEVPASQA 1516
Cdd:PTZ00121  1709 KKEAEEKKKAEElkkAEEENKIKAEEAKKEAEEDKKKAEEAK-KDEEEKKKIAHLKKEEEKKA 1770
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2246-2284 1.64e-05

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 44.24  E-value: 1.64e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2246 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTATLL 2284
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
973-1290 1.95e-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: 50.84  E-value: 1.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  973 DRLQAEREYgscSRHYQQLLQSLEQGEQEESrcqrcISELKDIRLQLEACEtrtvhrlrlpldkepaRECAQRIAEQQKA 1052
Cdd:TIGR02169  201 ERLRREREK---AERYQALLKEKREYEGYEL-----LKEKEALERQKEAIE----------------RQLASLEEELEKL 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1053 QAEVEGLGKGVA----RLSAEAEKVLALPEPSPAAptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEDVL 1128
Cdd:TIGR02169  257 TEEISELEKRLEeieqLLEELNKKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1129 KAHEEQLKEAQA-----VPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGE----------- 1192
Cdd:TIGR02169  335 LAEIEELEREIEeerkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINElkreldrlqee 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1193 ---RDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLryyRESADPLDSWLQDAKRRQEQIQAVPLANSQVVRE 1269
Cdd:TIGR02169  415 lqrLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL---EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
                          330       340
                   ....*....|....*....|...
gi 1777507480 1270 --QLRQEKALLEEIERHGEKVEE 1290
Cdd:TIGR02169  492 laEAEAQARASEERVRGGRAVEE 514
PTZ00121 PTZ00121
MAEBL; Provisional
1036-1465 2.02e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1036 KEPARECAQRIAEQQKAQAEveglGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTlGKLEQVRSLSAIYlEKLKTIS 1115
Cdd:PTZ00121  1397 KKKAEEDKKKADELKKAAAA----KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK-KKAEEAKKAEEAK-KKAEEAK 1470
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1116 LVIRSTQGAEDVLKAhEEQLKEAQAVPATLPELEATKAALKK---LRAQAEAQQPvfDALR--------DELRGAQEVGE 1184
Cdd:PTZ00121  1471 KADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAAEAKKKadeAKKAEEAKKA--DEAKkaeeakkaDEAKKAEEKKK 1547
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1185 RLQQRHGE--RDVEVERWRERVTQLLERWQAVLAQTDV-RQRELEQLGRQLRYYRESADPLDSWLQdaKRRQEQIQAvpl 1261
Cdd:PTZ00121  1548 ADELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEaKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEAKIKA--- 1622
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1262 ansqvvrEQLRQEKALLEEIERHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAKKPkvqsgSESVIQEYVD 1341
Cdd:PTZ00121  1623 -------EELKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKK-----AEEAKKAEED 1686
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1342 LRTRYSELTTLTSQYIKfiSETLRRMEEEEMQTVQQeqllqetqaLRQSFLSEKDSLLQRERFIEQEKAKLEQLFQEEVA 1421
Cdd:PTZ00121  1687 EKKAAEALKKEAEEAKK--AEELKKKEAEEKKKAEE---------LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 1777507480 1422 KAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRK 1465
Cdd:PTZ00121  1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1587-1625 2.13e-05

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 43.86  E-value: 2.13e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 1587 YLQGRSSIAGLLLQPSNEKLSVYAALRRQLLSPGTALIL 1625
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
68-179 2.45e-05

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: 46.11  E-value: 2.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   68 DRVQKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLpreRDVirsSRLPREKGRMrfhkLQNVQIA 145
Cdd:cd21285      8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKI---EDI---NGCPKNRSQM----IENIDAC 77
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1777507480  146 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTI 179
Cdd:cd21285     78 LSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
66-186 2.63e-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: 46.14  E-value: 2.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   66 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSSRLPREKGRMRfhKLQNVQIA 145
Cdd:cd21330      9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIK---VPVDWNRVNKPPYPKLGENMK--KLENCNYA 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1777507480  146 LDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 186
Cdd:cd21330     82 VELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
SPEC smart00150
Spectrin repeats;
545-639 2.67e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.40  E-value: 2.67e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   545 LRYLQDLLAWVGENQRRVDSAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARTDEGQL---SPATRGAYRDCLGRLD 621
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
                            90
                    ....*....|....*...
gi 1777507480   622 LQYAKLLNSSKARLRSLE 639
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
2580-2616 3.35e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.35e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  2580 RYLYGTGCVAGVYLPGSRQTLTVYQALKKGLLSAEVA 2616
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PTZ00121 PTZ00121
MAEBL; Provisional
1000-1583 4.33e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 4.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1000 QEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPAR--ECAQRIAEQQKAQaeveglgkgVARLSAEAEKVlalp 1077
Cdd:PTZ00121  1112 EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKrvEIARKAEDARKAE---------EARKAEDAKKA---- 1178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1078 EPSPAAPTLRSELELTlgKLEQVRSL-SAIYLEKLKTISLVIRSTQG--AEDVLKAHEEQLKEAQAVPA----TLPELEA 1150
Cdd:PTZ00121  1179 EAARKAEEVRKAEELR--KAEDARKAeAARKAEEERKAEEARKAEDAkkAEAVKKAEEAKKDAEEAKKAeeerNNEEIRK 1256
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1151 TKAALKKLRAQAEAQQPVFDALR-DELRGAQEV--GERLQQRHGERDVE------------------VERWRERVTQLLE 1209
Cdd:PTZ00121  1257 FEEARMAHFARRQAAIKAEEARKaDELKKAEEKkkADEAKKAEEKKKADeakkkaeeakkadeakkkAEEAKKKADAAKK 1336
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1210 RWQAVLAQTDVRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQ--AVPLANSQVVREQLRQEKALLEEIERHGE- 1286
Cdd:PTZ00121  1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkAEEKKKADEAKKKAEEDKKKADELKKAAAa 1416
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1287 --KVEECQRFA----------KQYINAIKDYELQlvtYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTlTS 1354
Cdd:PTZ00121  1417 kkKADEAKKKAeekkkadeakKKAEEAKKADEAK---KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKK-KA 1492
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1355 QYIKFISETLRRMEEEEMQTVQQEQLLQETQA--LRQSFLSEK-------------DSLLQRERFIE-QEKAKLEQLFQE 1418
Cdd:PTZ00121  1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdeAKKAEEAKKadeakkaeekkkaDELKKAEELKKaEEKKKAEEAKKA 1572
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1419 EVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREA--EEGVRRKQEELQRLEEQ--RQQQEKLLAEENQRLRERL 1494
Cdd:PTZ00121  1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEkkKVEQLKKKEAEEKKKAEEL 1652
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1495 QHLEEEHR---AALAHSEEVPASQA-TATKALPNGRDALDGPATETEPEHAFDGLRQKVP-----AQQL---QEVGILSA 1562
Cdd:PTZ00121  1653 KKAEEENKikaAEEAKKAEEDKKKAeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAeekkkAEELkkaEEENKIKA 1732
                          650       660
                   ....*....|....*....|.
gi 1777507480 1563 EELQRLVQGRTTVAELEQRED 1583
Cdd:PTZ00121  1733 EEAKKEAEEDKKKAEEAKKDE 1753
PLEC smart00250
Plectin repeat;
2862-2896 4.72e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.85  E-value: 4.72e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1777507480  2862 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 2896
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
2321-2357 6.21e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 6.21e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  2321 KLLSAEKAVTGYKDPYTGEQISLFQAMKKGLVLREHG 2357
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3171-3204 6.59e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 6.59e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1777507480  3171 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 3204
Cdd:smart00250    5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
SPEC smart00150
Spectrin repeats;
1133-1226 9.30e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.86  E-value: 9.30e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  1133 EQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALrdelrgaQEVGERLQQRHGERDVEVErwrERVTQLLERWQ 1212
Cdd:smart00150   18 EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEAL-------NELGEQLIEEGHPDAEEIE---ERLEELNERWE 87
                            90
                    ....*....|....
gi 1777507480  1213 AVLAQTDVRQRELE 1226
Cdd:smart00150   88 ELKELAEERRQKLE 101
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
886-1248 9.43e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 9.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  886 QEAQEAIARLEAQHQALVALWHQLHTDMKSLLAWQSLSRDVQ-LIRSWSLVTFRTLKPEEQRQALRSLELHYQAFLRDSQ 964
Cdd:COG4913    606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERReALQRLAEYSWDEIDVASAEREIAELEAELERLDASSD 685
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  965 DAGGFgpEDRL-QAEREYGSCSRHYQQLLQSLEQGEQEESRCQRcisELKDIRLQLEACETRTVHRLRLPLDKEPARECA 1043
Cdd:COG4913    686 DLAAL--EEQLeELEAELEELEEELDELKGEIGRLEKELEQAEE---ELDELQDRLEAAEDLARLELRALLEERFAAALG 760
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1044 QRIAEQ--QKAQAEVEGLGKGVARLSAEAEKVLAlpEPSPAAPTLRSELELTLGKLEQvrslsaiYLEKLKTIslvirst 1121
Cdd:COG4913    761 DAVERElrENLEERIDALRARLNRAEEELERAMR--AFNREWPAETADLDADLESLPE-------YLALLDRL------- 824
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1122 qgAEDVLKAHEEQLKEAQAVpATLPELEATKAALKKLRAQAEAQqpvFDALRDELRGAQ-EVGERLQQR-HGERDVEVER 1199
Cdd:COG4913    825 --EEDGLPEYEERFKELLNE-NSIEFVADLLSKLRRAIREIKER---IDPLNDSLKRIPfGPGRYLRLEaRPRPDPEVRE 898
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1200 WRERVTQLLER-WQAVLAQTDVRQRELEQLGRQLRyyRESADPLDSWLQD 1248
Cdd:COG4913    899 FRQELRAVTSGaSLFDEELSEARFAALKRLIERLR--SEEEESDRRWRAR 946
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1046-1227 9.84e-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: 46.28  E-value: 9.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1046 IAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAE 1125
Cdd:cd00176     39 LKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1126 DVLKAHEEQLKEAQA--VPATLPELEATKAALKKLRAQAEAQQPVFDALRDElrgaqevGERLQQRHGERDVEVERwrER 1203
Cdd:cd00176    117 DLEQWLEEKEAALASedLGKDLESVEELLKKHKELEEELEAHEPRLKSLNEL-------AEELLEEGHPDADEEIE--EK 187
                          170       180
                   ....*....|....*....|....
gi 1777507480 1204 VTQLLERWQAVLAQTDVRQRELEQ 1227
Cdd:cd00176    188 LEELNERWEELLELAEERQKKLEE 211
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
71-180 1.15e-04

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


Pssm-ID: 409141  Cd Length: 145  Bit Score: 44.96  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   71 QKKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRLPrekgrmrFHKLQN 141
Cdd:cd21292     25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTID-ERAINKKKLTV-------FTIHEN 96
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1777507480  142 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 180
Cdd:cd21292     97 LTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
PLEC smart00250
Plectin repeat;
1990-2026 1.20e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.70  E-value: 1.20e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  1990 KLLLAERAVTGYKDPYSGQSVSLFQALKKGLIPREQG 2026
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PTZ00121 PTZ00121
MAEBL; Provisional
1118-1585 1.23e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1118 IRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQ----AEAQQPVFDALR-DELRGAQEVGERLQQRHGE 1192
Cdd:PTZ00121  1130 AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEdakkAEAARKAEEVRKaEELRKAEDARKAEAARKAE 1209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1193 RDVEVERWR----ERVTQLLERWQAVLAQTD-VRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQAVPLANSQVV 1267
Cdd:PTZ00121  1210 EERKAEEARkaedAKKAEAVKKAEEAKKDAEeAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK 1289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1268 R--EQLR--QEKALLEEIERHGE---KVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYV 1340
Cdd:PTZ00121  1290 KkaDEAKkaEEKKKADEAKKKAEeakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1341 DLRT----RYSELTTLTSQYIKFISETLRRMEE-----EEMQTVQQEQLLQETQALRQSFLSEKDSLLQRErfieQEKAK 1411
Cdd:PTZ00121  1370 EKKKeeakKKADAAKKKAEEKKKADEAKKKAEEdkkkaDELKKAAAAKKKADEAKKKAEEKKKADEAKKKA----EEAKK 1445
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1412 LEQLFQ--EEVAKAQKLREEQQRQQQQMEqekqqLVASMEEARRQ---QREAEEGvRRKQEELQRLEEQRQQQEKLLAEE 1486
Cdd:PTZ00121  1446 ADEAKKkaEEAKKAEEAKKKAEEAKKADE-----AKKKAEEAKKAdeaKKKAEEA-KKKADEAKKAAEAKKKADEAKKAE 1519
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1487 NQRLRERLQHLEEEHRA-ALAHSEEV-PASQATATKALPNGRDALDGPATETEPEHAFDGLRQKVPAQQLQEVGI----- 1559
Cdd:PTZ00121  1520 EAKKADEAKKAEEAKKAdEAKKAEEKkKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIeevmk 1599
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1777507480 1560 -------LSAEELQRLVQGRTTVAELEQREDVR 1585
Cdd:PTZ00121  1600 lyeeekkMKAEEAKKAEEAKIKAEELKKAEEEK 1632
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
220-297 1.48e-04

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: 43.45  E-value: 1.48e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777507480  220 DNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 297
Cdd:cd21185     20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
PLEC smart00250
Plectin repeat;
2282-2317 1.76e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.76e-04
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1777507480  2282 TLLLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPE 2317
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
PLEC smart00250
Plectin repeat;
2656-2692 1.89e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.89e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  2656 RLLSAERAVTGYRDPYTEQTISLFQAMKKDLIPAEEA 2692
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3281-3318 2.19e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.93  E-value: 2.19e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507480  3281 QRFLEVQYLTGGLIEPDAPGRVPLEEALQRGTVDARTA 3318
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
978-1283 2.37e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 47.25  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  978 EREYGSCSRHYQQLLQSLEQGEQEEsRCQRCISELK-DIRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQ----QKA 1052
Cdd:COG3096    326 EQDYQAASDHLNLVQTALRQQEKIE-RYQEDLEELTeRLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQladyQQA 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1053 -----------QAEVEGLGKgvarlsaeAEKVLALPEPSPAA-----PTLRSELEL---TLGKLEQVRSLSAIYLEKLKT 1113
Cdd:COG3096    405 ldvqqtraiqyQQAVQALEK--------ARALCGLPDLTPENaedylAAFRAKEQQateEVLELEQKLSVADAARRQFEK 476
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1114 ISLVIRSTQGAEDVLKAHEEqlkeAQAVPATLPELEATKAALKKLRAQ-AEAQQpvfdaLRDELRGAQEVGERLQQRHG- 1191
Cdd:COG3096    477 AYELVCKIAGEVERSQAWQT----ARELLRRYRSQQALAQRLQQLRAQlAELEQ-----RLRQQQNAERLLEEFCQRIGq 547
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1192 ------ERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdPLdsWL--QDAKRRQEQIQAVPLAN 1263
Cdd:COG3096    548 qldaaeELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARA-PA--WLaaQDALERLREQSGEALAD 624
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1777507480 1264 SQVV-----------------REQLRQEKALLE-EIER 1283
Cdd:COG3096    625 SQEVtaamqqllerereatveRDELAARKQALEsQIER 662
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
977-1290 2.82e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 2.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  977 AEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEA----------CETRTVHRLRLPLDKEPARECAQRI 1046
Cdd:TIGR02169  714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSelkelearieELEEDLHKLEEALNDLEARLSHSRI 793
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1047 aeqQKAQAEVEGLGKGVARLSAEAEkvlalpepspaaptlrsELELTLGKLEQVRSlsaiYLEKLKtislvirstQGAED 1126
Cdd:TIGR02169  794 ---PEIQAELSKLEEEVSRIEARLR-----------------EIEQKLNRLTLEKE----YLEKEI---------QELQE 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1127 VLKAHEEQLKE-AQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVT 1205
Cdd:TIGR02169  841 QRIDLKEQIKSiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1206 QLLERWQAVLAQTDvrqrELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQAVPLANSQVVREQLRQEKALLEEIERHg 1285
Cdd:TIGR02169  921 ELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKR- 995

                   ....*
gi 1777507480 1286 EKVEE 1290
Cdd:TIGR02169  996 AKLEE 1000
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2581-2619 3.09e-04

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 40.39  E-value: 3.09e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507480 2581 YLYGTGCVAGVYLPGSRQTLTVYQALKKGLLSAEVARLL 2619
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
943-1289 3.16e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 3.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  943 EEQRQALRSLELHYQAFLRDSQDAGGFGP--EDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLE 1020
Cdd:COG4717    101 EEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE 180
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1021 ACETRTvhrlrLPLDKEPARECAQRIAEQQKAQAEVEglgKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQV 1100
Cdd:COG4717    181 ELLEQL-----SLATEEELQDLAEELEELQQRLAELE---EELEEAQEELEE-------------LEEELEQLENELEAA 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1101 RSLSAIYLEKLKTISL-VIRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRgA 1179
Cdd:COG4717    240 ALEERLKEARLLLLIAaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE-E 318
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1180 QEVGERLQQRHGERDVEVERWRERVtQLLERWQAVLAQTDVRQRELEQLGRQLRYYR-------ESADPLDSWLQDAKRR 1252
Cdd:COG4717    319 EELEELLAALGLPPDLSPEELLELL-DRIEELQELLREAEELEEELQLEELEQEIAAllaeagvEDEEELRAALEQAEEY 397
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1777507480 1253 QEQIQAVplansQVVREQLRQEKALLEEIERHGEKVE 1289
Cdd:COG4717    398 QELKEEL-----EELEEQLEELLGELEELLEALDEEE 429
PLEC smart00250
Plectin repeat;
1625-1658 3.61e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.16  E-value: 3.61e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1777507480  1625 LLEAQAASGFLLDPVRNRQLTVNEAVKEGVVGPE 1658
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
73-297 4.46e-04

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 46.09  E-value: 4.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   73 KTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLSGDSLPRERDVIRSSRLPREKGRM-RFHKLQNVQIALDYLRH 151
Cdd:COG5069    382 RVFTFWLNSLDVSPE--ITNLFGDLRDQ---LILLQALSKKLMPMTVTHKLVKKQPASGIEEnRFKAFENENYAVDLGIT 456
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  152 RQVKLVNIRNDDIADGNpKLTLGLIW-------TIILHFQISDiqvsgqsEDMTAKEKLLLWSQRMVEGY---QGLRCDN 221
Cdd:COG5069    457 EGFSLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKD-------GCGLSDSDLCAWLGSLGLKGdkeEGIRSFG 528
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  222 FTSSWRDGRLFNAIIHRHKPMLIDMNKVyRQTNLENLDQA-------FSVAERDLGVTRLLDPEDVDVPQPdEKSIITYV 294
Cdd:COG5069    529 DPAGSVSGVFYLDVLKGIHSELVDYDLV-TRGFTEFDDIAdarslaiSSKILRSLGAIIKFLPEDINGVRP-RLDVLTFI 606

                   ...
gi 1777507480  295 SSL 297
Cdd:COG5069    607 ESL 609
PLEC smart00250
Plectin repeat;
1662-1698 4.52e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.16  E-value: 4.52e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507480  1662 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVREHG 1698
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1202-1635 5.91e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 5.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1202 ERVTQLLERWQAVLAQtdVRQReLEQLGRQ----LRY--YRESADPLDSWL-----QDAKRRQEQIQAVpLANSQVVREQ 1270
Cdd:COG1196    182 EATEENLERLEDILGE--LERQ-LEPLERQaekaERYreLKEELKELEAELlllklRELEAELEELEAE-LEELEAELEE 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1271 LRQEKALLE-EIERHGEKVEEcqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKkpkvqsgsESVIQEYVDLRTRYSEL 1349
Cdd:COG1196    258 LEAELAELEaELEELRLELEE----LELELEEAQAEEYELLAELARLEQDIARLE--------ERRRELEERLEELEEEL 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1350 TTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRERFIEQEKAKLEQLFQEEVAKAQKLREE 1429
Cdd:COG1196    326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1430 QQRQQQQMEQEKQQLVA-SMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAEENQRLRERLQHLEEEHRAALAHS 1508
Cdd:COG1196    406 EEAEEALLERLERLEEElEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1509 EEVPASQATATKALPNGRDALDGPATETEPEHAFDGLRQKVPAQQ-----LQEVGILSAEELQRLVQGRTTVAELEQRED 1583
Cdd:COG1196    486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveaaYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1777507480 1584 VRCYLQGRSSIAGLLLQPSNEKLSvyAALRRQLLSPGTALILLEAQAASGFL 1635
Cdd:COG1196    566 LKAAKAGRATFLPLDKIRARAALA--AALARGAIGAAVDLVASDLREADARY 615
CH_PARVA_B_rpt2 cd21306
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
70-183 6.19e-04

second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-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. 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: 409155  Cd Length: 121  Bit Score: 42.41  E-value: 6.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   70 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerdvIRSSRLPREKGRmrfHKLQNVQIALDYL 149
Cdd:cd21306     16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVP-----LHSFHLTPTSFE---QKVHNVQFAFELM 87
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1777507480  150 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 183
Cdd:cd21306     88 QDAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1205-1511 8.72e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 8.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1205 TQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQAvplaNSQVVREQLRQEKALLEEIERH 1284
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK----EIEQLEQEEEKLKERLEELEED 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1285 ----GEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVA---SPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyi 1357
Cdd:TIGR02169  746 lsslEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-- 823
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1358 kfiSETLRRMEEEEMQTvqqeqllqetqaLRQSFLSEKDSLLQRERFIEQEKAKLEQLfQEEVAKAQKLREEQQRQQQQM 1437
Cdd:TIGR02169  824 ---LTLEKEYLEKEIQE------------LQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDL 887
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1438 EQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAE-----------------------ENQRLRERL 1494
Cdd:TIGR02169  888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedpkgedeeipeeelsledvqaELQRVEEEI 967
                          330
                   ....*....|....*..
gi 1777507480 1495 QHLEEEHRAALAHSEEV 1511
Cdd:TIGR02169  968 RALEPVNMLAIQEYEEV 984
PLEC smart00250
Plectin repeat;
1913-1945 9.83e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.00  E-value: 9.83e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1777507480  1913 RRALRGSSVIAGVWLEEAGQKLSIYEALRKDLL 1945
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1011-1252 1.38e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1011 ELKDIRLQLEAcETRTVHRLrlpldkEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpepSPAAPTLRSEL 1090
Cdd:COG4913    236 DLERAHEALED-AREQIELL------EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL----EAELEELRAEL 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1091 ELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEdvlkahEEQLKEaqavpatlpELEATKAALKKLRAQAEAQQPVFD 1170
Cdd:COG4913    305 ARLEAELERLEARLDALREELDELEAQIRGNGGDR------LEQLER---------EIERLERELEERERRRARLEALLA 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1171 ALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQllERWQAVLAQTDVRqRELEQLGRQLRYYRESADPLDSWLQDAK 1250
Cdd:COG4913    370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEE--ALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLALR 446

                   ..
gi 1777507480 1251 RR 1252
Cdd:COG4913    447 DA 448
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1089-1583 1.58e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1089 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQG-AEDVLKAHEEQLKEAQAVPATLPELEATKAALKKLRaqaeaqqp 1167
Cdd:PRK02224   203 DLHERLNGLESELAELDEEIERYEEQREQARETRDeADEVLEEHEERREELETLEAEIEDLRETIAETERER-------- 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1168 vfDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLdswLQ 1247
Cdd:PRK02224   275 --EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL---RE 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1248 DAKRRQEQiqavplansqvvREQLRQEKALLE-EIERHGEKVEECQrfakqyiNAIKDYELQLVTYKAQLEpvASPAKKP 1326
Cdd:PRK02224   350 DADDLEER------------AEELREEAAELEsELEEAREAVEDRR-------EEIEELEEEIEELRERFG--DAPVDLG 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1327 KVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEE----EEMQTVQQEqllqetqalrqsflSEKDSLLQRE 1402
Cdd:PRK02224   409 NAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpECGQPVEGS--------------PHVETIEEDR 474
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1403 RFIEQEKAKLEQLFQEEVAKAQKLreeqqrqqqqmeqekqqlvASMEEARRQQREAEEgvrrkqeelqrLEEQRQQQEKL 1482
Cdd:PRK02224   475 ERVEELEAELEDLEEEVEEVEERL-------------------ERAEDLVEAEDRIER-----------LEERREDLEEL 524
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1483 LAEENQRLRERLQHLEEEHRAALAHSEEVPASQATATKALPNGRDALDGPAT----ETEPEHAFDGLRQKVPAQQLQEVg 1558
Cdd:PRK02224   525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAElnskLAELKERIESLERIRTLLAAIAD- 603
                          490       500
                   ....*....|....*....|....*.
gi 1777507480 1559 ilSAEELQRLVQGRTTVAELE-QRED 1583
Cdd:PRK02224   604 --AEDEIERLREKREALAELNdERRE 627
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
654-734 1.75e-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: 40.38  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  654 WLSEKE----DEEVGFDWSErstnTAAKKDSYSALMRELELKEKKIKEIQSTGDRLLREDHPARPTVESFQAALQTQWSW 729
Cdd:pfam00435   16 WIEEKEallsSEDYGKDLES----VQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERWEQ 91

                   ....*
gi 1777507480  730 MLQLC 734
Cdd:pfam00435   92 LLELA 96
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1130-1367 2.58e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1130 AHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLE 1209
Cdd:COG4942     17 AQADAAAEAEA------ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1210 RWQAVLAQTDVRQRELEQLGRQLrYYRESADPLDSWL-----QDAKRRQEQIQAVplanSQVVREQLRQEKALLEEIERH 1284
Cdd:COG4942     91 EIAELRAELEAQKEELAELLRAL-YRLGRQPPLALLLspedfLDAVRRLQYLKYL----APARREQAEELRADLAELAAL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1285 GEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKvqsgsESVIQEYVDLRTRYSELTTLTSQYIKFISETL 1364
Cdd:COG4942    166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL-----AELAAELAELQQEAEELEALIARLEAEAAAAA 240

                   ...
gi 1777507480 1365 RRM 1367
Cdd:COG4942    241 ERT 243
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
988-1582 2.72e-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: 43.80  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  988 YQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACEtrtvhRLRLPLDKEPAREcaqRIAEQQKAQAEVEglgkgvarls 1067
Cdd:TIGR00618  245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLE-----ETQERINRARKAA---PLAAHIKAVTQIE---------- 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1068 AEAEKVLAlpepspaaptlrsELELTLGKLEQVRSLSAIYLEKlktiSLVIRSTQGAEDVLKAHEEQLKEAQAVPAT-LP 1146
Cdd:TIGR00618  307 QQAQRIHT-------------ELQSKMRSRAKLLMKRAAHVKQ----QSSIEEQRRLLQTLHSQEIHIRDAHEVATSiRE 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1147 ELEATKAALKKLRAQAEAQQpvfdALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLerwqAVLAQTDVRQRELE 1226
Cdd:TIGR00618  370 ISCQQHTLTQHIHTLQQQKT----TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA----HAKKQQELQQRYAE 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1227 QLGrqlryyresadpldswLQDAKRRQEQIQAVPLANSqvVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYE 1306
Cdd:TIGR00618  442 LCA----------------AAITCTAQCEKLEKIHLQE--SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP 503
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1307 LQLVTYKAQLEPVA-----SPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLL 1381
Cdd:TIGR00618  504 CPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSK 583
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1382 QETQALRQ---SFLSEKDSLLQRERFIEQEKAKLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREA 1458
Cdd:TIGR00618  584 EDIPNLQNitvRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREH 663
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1459 EEGVR-----------RKQEELQRLEEQRQQQEKLLAEENQRLRERLQHLEEEHR-------AALAHSEEVPASQATATK 1520
Cdd:TIGR00618  664 ALSIRvlpkellasrqLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRefneienASSSLGSDLAAREDALNQ 743
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1777507480 1521 ALPNGRDALDGPATETEPEHAFDGLRQKVPAQQLQEVGILSAEELQRLVQGRTTVAELEQRE 1582
Cdd:TIGR00618  744 SLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLE 805
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
885-1499 2.93e-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: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  885 NQEAQEAIARlEAQHQALVALWhQLHTDMKSLLAWQSLSRDVQlirsWSLVTFRTLKPEE------------QRQALRsL 952
Cdd:TIGR00618  223 VLEKELKHLR-EALQQTQQSHA-YLTQKREAQEEQLKKQQLLK----QLRARIEELRAQEavleetqerinrARKAAP-L 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  953 ELHYQAFLRDSQDAGGFGPEDRLQaEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRL 1032
Cdd:TIGR00618  296 AAHIKAVTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1033 PLDKEPARECAQRI-AEQQKAQAevegLGKGVARLSAEAEKVLALPEPSPAAP----TLRSELELTLGKLEQVRSLSAIY 1107
Cdd:TIGR00618  375 HTLTQHIHTLQQQKtTLTQKLQS----LCKELDILQREQATIDTRTSAFRDLQgqlaHAKKQQELQQRYAELCAAAITCT 450
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1108 LEKLKtisLVIRSTQGAEDVLKAHEEQLKEAQAVpaTLPELEATKAALKKLRAQAEAQQPVFDALR---------DELRG 1178
Cdd:TIGR00618  451 AQCEK---LEKIHLQESAQSLKEREQQLQTKEQI--HLQETRKKAVVLARLLELQEEPCPLCGSCIhpnparqdiDNPGP 525
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1179 AQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLdswLQDAKRRQEQIQA 1258
Cdd:TIGR00618  526 LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL---QNITVRLQDLTEK 602
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1259 VPLANSQVVREQLRQEKALLEEIERHGEKVEE--CQRFAKQYINAIKDYELQLvTYKAQLEPVASPAKKPKvQSGsESVI 1336
Cdd:TIGR00618  603 LSEAEDMLACEQHALLRKLQPEQDLQDVRLHLqqCSQELALKLTALHALQLTL-TQERVREHALSIRVLPK-ELL-ASRQ 679
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1337 QEYVDLRTRYSELTTLTSQyIKFISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQ------RERFIEQEKA 1410
Cdd:TIGR00618  680 LALQKMQSEKEQLTYWKEM-LAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNqslkelMHQARTVLKA 758
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1411 KL---EQLFQEEVAKAQKLR-----EEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRrkQEELQRLEEQRQQQEKL 1482
Cdd:TIGR00618  759 RTeahFNNNEEVTAALQTGAelshlAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL--NLQCETLVQEEEQFLSR 836
                          650       660
                   ....*....|....*....|
gi 1777507480 1483 LAEENQRL---RERLQHLEE 1499
Cdd:TIGR00618  837 LEEKSATLgeiTHQLLKYEE 856
COG4995 COG4995
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
1163-1624 3.13e-03

Uncharacterized conserved protein, contains CHAT domain [Function unknown];


Pssm-ID: 444019 [Multi-domain]  Cd Length: 711  Bit Score: 43.42  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1163 EAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPL 1242
Cdd:COG4995      1 LLALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1243 DSWLQDAKRRQEQIQAVPLANSQVVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASP 1322
Cdd:COG4995     81 ALAALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1323 AKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRE 1402
Cdd:COG4995    161 AAAALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLAL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1403 RFIEQEKAKLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKL 1482
Cdd:COG4995    241 LALAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1483 LAEENQRLRERLQHLEEEHRAALAHSEEVPASQATATKALPNGRDALDGPATETEPEHAFDGLRQKVPAQQLQEVGILSA 1562
Cdd:COG4995    321 AALLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAAL 400
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1777507480 1563 EELQRLVQGRTTVAELEQREDVRCYLQGRSSIAGLL-LQPSNEKLSVYAALRRQLLSPGTALI 1624
Cdd:COG4995    401 LALAAAQLLRLLLAALALLLALAAYAAARLALLALIeYIILPDRLYAFVQLYQLLIAPIEAEL 463
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
978-1540 3.69e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 43.20  E-value: 3.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480  978 EREYGSCSRHYQQLLQSLEQGEQEEsrCQRCISELKDIRLQLEACETRTvhrlrlpldkeparecAQRIAEQQKAQAEVE 1057
Cdd:pfam07111  139 QRELEEIQRLHQEQLSSLTQAHEEA--LSSLTSKAEGLEKSLNSLETKR----------------AGEAKQLAEAQKEAE 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1058 GLGKGVARLSAEAEKVLALPE--------------PSPAAPTLRSELELTLGKLEQVR-SLSAiyleklkTISLVIRSTQ 1122
Cdd:pfam07111  201 LLRKQLSKTQEELEAQVTLVEslrkyvgeqvppevHSQTWELERQELLDTMQHLQEDRaDLQA-------TVELLQVRVQ 273
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1123 GAEDVLKAHEEQLKEaQAVPATLPELEATKAALKKLRAQAEAqqpVFdALRDELRgAQEvgerLQQRHgerdvEVERWRE 1202
Cdd:pfam07111  274 SLTHMLALQEEELTR-KIQPSDSLEPEFPKKCRSLLNRWREK---VF-ALMVQLK-AQD----LEHRD-----SVKQLRG 338
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1203 RVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLDSWL---QDAKRRQEQIQAVPLANSQVVREQLRQEKALLE 1279
Cdd:pfam07111  339 QVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELsraQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLE 418
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1280 -EIERHGEKVEECQRFAKQYINAIKDYEL-------QLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTT 1351
Cdd:pfam07111  419 tTMTRVEQAVARIPSLSNRLSYAVRKVHTikglmarKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQ 498
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1352 LTSQYIKfiSETLRRMEEEEmqtVQQEQLLQETQALRQSFLSEKDSL----------LQRERFIEQEKAKLEQ-LFQEEV 1420
Cdd:pfam07111  499 LSAHLIQ--QEVGRAREQGE---AERQQLSEVAQQLEQELQRAQESLasvgqqlevaRQGQQESTEEAASLRQeLTQQQE 573
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1421 AKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLL----AEENQRLRERLQH 1496
Cdd:pfam07111  574 IYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQdearKEEGQRLARRVQE 653
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1777507480 1497 LEEEHRAALAHSEE----VPASQATATKALPNGRD---ALDGPATETEPEH 1540
Cdd:pfam07111  654 LERDKNLMLATLQQegllSRYKQQRLLAVLPSGLDkksVVSSPRPECSASA 704
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1101-1290 4.10e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 4.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1101 RSLSAIYLEKLKTISLVIRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQpvfdALRDELRGAQ 1180
Cdd:COG4717     53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL----EKLEKLLQLL 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1181 EVGERLQQRHGERDVEVERWrERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPldSWLQDAKRRQEQIQAvp 1260
Cdd:COG4717    129 PLYQELEALEAELAELPERL-EELEERLEELRELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEELEE-- 203
                          170       180       190
                   ....*....|....*....|....*....|
gi 1777507480 1261 lansqvVREQLRQEKALLEEIERHGEKVEE 1290
Cdd:COG4717    204 ------LQQRLAELEEELEEAQEELEELEE 227
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3177-3207 4.53e-03

Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.


Pssm-ID: 459901  Cd Length: 39  Bit Score: 37.31  E-value: 4.53e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1777507480 3177 AGILDTETLEKVSITEAMHRNLVDNITGQRL 3207
Cdd:pfam00681    9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
2899-2930 4.84e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.08  E-value: 4.84e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1777507480  2899 KLLSAERAVTGYKDPYSGKLISLFQAMKKGLI 2930
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1147-1516 5.25e-03

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: 42.65  E-value: 5.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1147 ELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERlqqrhgERDVEVERWRERVTQLLERWQAVLAQTDVRQRELE 1226
Cdd:pfam02463  167 LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQ------AKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1227 QLGRQLRYYRESadpLDSWLQDAKRRQEQIQAVplanSQVVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYE 1306
Cdd:pfam02463  241 LLQELLRDEQEE---IESSKQEIEKEEEKLAQV----LKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1307 LQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEmqtvqqeqllQETQA 1386
Cdd:pfam02463  314 EKLKESEKEKK---------KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLE----------QLEEE 374
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1387 LRQSFLSEKDSLLQRERFIEQEKAKLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEgvrRKQ 1466
Cdd:pfam02463  375 LLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTE---EKE 451
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1467 EELQRLEEQRQQQEKLLAEENQRLRERLQHLEEEHRAALAHSEEVPASQA 1516
Cdd:pfam02463  452 ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK 501
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1147-1227 6.61e-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: 38.84  E-value: 6.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1147 ELEATKAALKKLRAQAEAqqpvFDALRDELRGAQEVGERLQQRHGErdvEVERWRERVTQLLERWQAVLAQTDVRQRELE 1226
Cdd:pfam00435   32 DLESVQALLKKHKALEAE----LAAHQDRVEALNELAEKLIDEGHY---ASEEIQERLEELNERWEQLLELAAERKQKLE 104

                   .
gi 1777507480 1227 Q 1227
Cdd:pfam00435  105 E 105
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
1113-1317 6.62e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 6.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1113 TISLVIRSTQGAEDVLKAHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEvgerlqqrhge 1192
Cdd:COG3883      3 ALALAAPTPAFADPQIQAKQKELSELQA------ELEAAQAELDALQAELEELNEEYNELQAELEALQA----------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1193 rdvEVERWRERVTQllerwqavlAQTDVRQRElEQLGRQLRYYRESADPLDSW--------LQDAKRRQEQIQAVPLANS 1264
Cdd:COG3883     66 ---EIDKLQAEIAE---------AEAEIEERR-EELGERARALYRSGGSVSYLdvllgsesFSDFLDRLSALSKIADADA 132
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1777507480 1265 QVVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLE 1317
Cdd:COG3883    133 DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
PLEC smart00250
Plectin repeat;
3319-3356 7.69e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 36.69  E-value: 7.69e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507480  3319 QKLRDVSAYSKYLTCPKTKLKISYKDALDRSMVEEGTG 3356
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
72-131 8.55e-03

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409070  Cd Length: 106  Bit Score: 38.41  E-value: 8.55e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480   72 KKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErDVIRSSRLPREK 131
Cdd:cd21221      3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVP-EVAQSEEGQKQK 61
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
1136-1500 9.51e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 9.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1136 KEAQAVPATLPELEA-----------------TKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERdVEVE 1198
Cdd:pfam17380  221 KEVQGMPHTLAPYEKmerrkesfnlaedvttmTPEYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEK-MEQE 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1199 RWR---ERVTQLLERWQAVLAQTDVRQRELEQ----LGRQLRYYRESADPLDS-WLQDAKRRQEQIQAVPLAnsqVVREQ 1270
Cdd:pfam17380  300 RLRqekEEKAREVERRRKLEEAEKARQAEMDRqaaiYAEQERMAMERERELERiRQEERKRELERIRQEEIA---MEISR 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1271 LRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVaspakKPKVQSGSESVIQEYVDLRTRYSELT 1350
Cdd:pfam17380  377 MRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI-----RAEQEEARQREVRRLEEERAREMERV 451
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1351 TLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALRQSflsekdsllQRERFIEQEKAKLEQLFQEEVAKAQKLREeq 1430
Cdd:pfam17380  452 RLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEE---------QRRKILEKELEERKQAMIEEERKRKLLEK-- 520
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507480 1431 qrqqqqmeqekqqlvaSMEEarRQQREAEEGVRRKQEELQRLEEQRqqqekllaEENQRLRERLQHLEEE 1500
Cdd:pfam17380  521 ----------------EMEE--RQKAIYEEERRREAEEERRKQQEM--------EERRRIQEQMRKATEE 564
 
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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