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Conserved domains on  [gi|1777507490|ref|XP_031546374|]
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plectin isoform X13 [Vicugna pacos]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
175-280 1.57e-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: 237.61  E-value: 1.57e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  175 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 254
Cdd:cd21238      1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 1777507490  255 PEDVDVPQPDEKSIITYVSSLYDAMP 280
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
41-162 4.60e-72

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: 236.14  E-value: 4.60e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   41 DRVQKKTFTKWVNKHLIKHWRaeaqrHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprekGRMRFHKLQNV 120
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARR-----RVVDLFEDLRDGHNLISLLEVLSGESLPRER------------GRMRFHRLQNV 63
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1777507490  121 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 162
Cdd:cd21188     64 QTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
895-972 4.21e-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: 4.21e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777507490  895 LAWQSLSRDVQLIRSWSLVTFRTLKPEEQRQALRSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSRHYQQLLQS 972
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
794-860 2.28e-23

SH3 domain; This entry represents an SH3 domain.


:

Pssm-ID: 407754  Cd Length: 65  Bit Score: 95.79  E-value: 2.28e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1777507490  794 QLKPRSpaHPVRGRVPLLAVCDYKQVEVTVHKGDECQLVGPAQPFHWKVLSSSGSEAAVPSVCFLIP 860
Cdd:pfam17902    1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
619-797 2.28e-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: 2.28e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  619 LHGFVAAATKELMWLSEKEDEEVGFDWSERSTNTAAKKDSYSALMRELELKEKKIKEIQSTGDRLLREDHPARPTVESFQ 698
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  699 AALQTQWSWMLQLCCCVEAHLKENTAYFQFFSDVREAEEQLRKLQETLRRKYTCDrsiTVTRLEDLLQDAQDEKDQLNEY 778
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
                          170
                   ....*....|....*....
gi 1777507490  779 RGHLSGLAKRAKAIVQLKP 797
Cdd:cd00176    159 EPRLKSLNELAEELLEEGH 177
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2916-2954 1.18e-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: 1.18e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2916 LLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEMNEIL 2954
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2338-2376 2.18e-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: 2.18e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2338 LLEAQIATGGIIDPVHSHRLPVDVAFQRGYFDEEMSRIL 2376
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1679-1717 3.80e-15

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 71.59  E-value: 3.80e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 1679 LLEAQIATGGIIDPVHSHRVPVDVAFQRGYFDEEMSRVL 1717
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2597-2635 1.87e-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: 1.87e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2597 LLEAQAATGFLLDPVKGDRLTVDEAVRKGLVGPELHDRL 2635
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1103-1293 1.37e-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: 1.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1103 EDVLKAHEEQLKEAQaVPATLPELEATKAALKKLRAQAEAQQPVFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1182
Cdd:cd00176     13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1183 TQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLDSWLQDAKRRQEQIQAVPLANSqvVREQLRQEKALLEEIERH 1262
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLES--VEELLKKHKELEEELEAH 158
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1777507490 1263 GEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1293
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2007-2045 2.27e-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: 2.27e-13
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2007 LLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDEETHTAL 2045
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2262-2300 1.18e-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: 1.18e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2262 LLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPELHEKL 2300
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3185-3223 1.23e-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: 1.23e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 3185 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 3223
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2840-2878 2.79e-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: 2.79e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2840 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 2878
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2673-2711 2.96e-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: 2.96e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2673 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTYDQL 2711
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
915-1483 2.23e-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: 70.35  E-value: 2.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  915 FRTLKPEEQRQALRSLELHYQAFLRDSQDAGgfgpEDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIR 994
Cdd:COG1196    215 YRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  995 LQLEACETRTVHRLRLplDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALpepspAAPTLRSELELTLGK 1074
Cdd:COG1196    291 YELLAELARLEQDIAR--LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-----AEEELEEAEAELAEA 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1075 LEQVRSLSAIYLEKLKTISlviRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDEL 1154
Cdd:COG1196    364 EEALLEAEAELAEAEEELE---ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1155 RGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQtdvRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQI 1234
Cdd:COG1196    441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE---LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1235 QAVPLAnsQVVREQLRQEKALLEEIE-----RHGEKVEECQRFAKQYINAIKDYELQLVT-YKAQLEPVASPAKKPKVQS 1308
Cdd:COG1196    518 GLRGLA--GAVAVLIGVEAAYEAALEaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARG 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1309 GSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRERFIEQEKA 1388
Cdd:COG1196    596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1389 KLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAEEN--- 1465
Cdd:COG1196    676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAlee 755
                          570       580
                   ....*....|....*....|....*
gi 1777507490 1466 -------QRLRERLQHLEEEhRAAL 1483
Cdd:COG1196    756 lpeppdlEELERELERLERE-IEAL 779
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1603-1641 2.54e-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: 2.54e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 1603 LLEAQAASGFLLDPVRNRQLTVNEAVKEGVVGPELHHKL 1641
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3261-3299 9.07e-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: 9.07e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 3261 FLEVQYLTGGLIEPDAPGRVPLEEALQRGTVDARTAQKL 3299
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1935-1969 4.21e-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: 4.21e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1777507490 1935 QAGTGHIVDPTTSARLTVAEAVRAGLVGPELHEKL 1969
Cdd:pfam00681    5 QAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3017-3045 3.70e-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: 3.70e-07
                           10        20
                   ....*....|....*....|....*....
gi 1777507490 3017 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 3045
Cdd:pfam00681   11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
2800-2837 2.13e-06

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.71  E-value: 2.13e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507490  2800 QKFLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTA 2837
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2224-2259 1.30e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.30e-05
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1777507490  2224 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTA 2259
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1565-1603 2.06e-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: 2.06e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 1565 YLQGRSSIAGLLLQPSNEKLSVYAALRRQLLSPGTALIL 1603
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC smart00150
Spectrin repeats;
523-617 2.48e-05

Spectrin repeats;


:

Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.78  E-value: 2.48e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   523 LRYLQDLLAWVGENQRRVDSAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARTDEGQL---SPATRGAYRDCLGRLD 599
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
                            90
                    ....*....|....*...
gi 1777507490   600 LQYAKLLNSSKARLRSLE 617
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
2558-2594 3.26e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.26e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  2558 RYLYGTGCVAGVYLPGSRQTLTVYQALKKGLLSAEVA 2594
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2299-2335 5.94e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 5.94e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  2299 KLLSAEKAVTGYKDPYTGEQISLFQAMKKGLVLREHG 2335
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3149-3182 6.36e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 6.36e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1777507490  3149 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 3182
Cdd:smart00250    5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
1968-2004 1.16e-04

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.70  E-value: 1.16e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  1968 KLLLAERAVTGYKDPYSGQSVSLFQALKKGLIPREQG 2004
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2634-2670 1.78e-04

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.78e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  2634 RLLSAERAVTGYRDPYTEQTISLFQAMKKDLIPAEEA 2670
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
1640-1676 4.28e-04

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.16  E-value: 4.28e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  1640 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVREHG 1676
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
1891-1923 9.49e-04

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.00  E-value: 9.49e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1777507490  1891 RRALRGSSVIAGVWLEEAGQKLSIYEALRKDLL 1923
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
PLEC smart00250
Plectin repeat;
2877-2908 4.63e-03

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.08  E-value: 4.63e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1777507490  2877 KLLSAERAVTGYKDPYSGKLISLFQAMKKGLI 2908
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
PLEC smart00250
Plectin repeat;
3297-3334 7.28e-03

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 36.69  E-value: 7.28e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507490  3297 QKLRDVSAYSKYLTCPKTKLKISYKDALDRSMVEEGTG 3334
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
 
Name Accession Description Interval E-value
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
175-280 1.57e-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: 237.61  E-value: 1.57e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  175 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 254
Cdd:cd21238      1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 1777507490  255 PEDVDVPQPDEKSIITYVSSLYDAMP 280
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
41-162 4.60e-72

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: 236.14  E-value: 4.60e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   41 DRVQKKTFTKWVNKHLIKHWRaeaqrHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprekGRMRFHKLQNV 120
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARR-----RVVDLFEDLRDGHNLISLLEVLSGESLPRER------------GRMRFHRLQNV 63
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1777507490  121 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 162
Cdd:cd21188     64 QTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
36-387 9.54e-45

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 174.36  E-value: 9.54e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   36 EQDERDRVQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLprerdvIRSSRLPRekgrMRFH 115
Cdd:COG5069      2 EAKKWQKVQKKTFTKWTNEKLIS----GGQKEFGDLDTDLKDGVKLAQLLEALQKDNA------GEYNETPE----TRIH 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  116 KLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-G 194
Cdd:COG5069     68 VMENVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpE 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  195 LRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITY 271
Cdd:COG5069    145 VDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTY 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  272 VS------SLYD----AMPRVPDVQDGVKANElQLRwQEYRELVVLLLQWVRQHTAAFEERRFPSSFEEIEILWCQFLKF 341
Cdd:COG5069    225 VSwyiirfGLLEkidiALHRVYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQL 302
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1777507490  342 KETE--LPAKEAD-KNRSKGIFQSLEgAVQAGQLKVPPGYHPLDVEKEW 387
Cdd:COG5069    303 NALCsrAPLETTDlHSLAGQILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
895-972 4.21e-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: 4.21e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777507490  895 LAWQSLSRDVQLIRSWSLVTFRTLKPEEQRQALRSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSRHYQQLLQS 972
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
175-281 4.88e-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: 4.88e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  175 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 251
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1777507490  252 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 281
Cdd:pfam00307   81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
794-860 2.28e-23

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 95.79  E-value: 2.28e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1777507490  794 QLKPRSpaHPVRGRVPLLAVCDYKQVEVTVHKGDECQLVGPAQPFHWKVLSSSGSEAAVPSVCFLIP 860
Cdd:pfam17902    1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
46-160 7.06e-23

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: 95.46  E-value: 7.06e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490    46 KTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVirssrlprEKGRMRFHKLQNVQIALD 125
Cdd:smart00033    1 KTLLRWVNSLLAE----YDKPPVTNFSSDLKDGVALCALLNSLSPGLVD-KKKV--------AASLSRFKKIENINLALS 67
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1777507490   126 YLRHRQVKLVNIRNDDIADGnPKLTLGLIWTIILH 160
Cdd:smart00033   68 FAEKLGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
43-163 1.24e-22

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: 95.05  E-value: 1.24e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   43 VQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerdvirssrlPREKGRMRFHKLQNVQI 122
Cdd:pfam00307    2 ELEKELLRWINSHLAE---YGPGVRVTNFTTDLRDGLALCALLNKLAPGLVD-----------KKKLNKSEFDKLENINL 67
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1777507490  123 ALDYLRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 163
Cdd:pfam00307   68 ALDVAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
179-275 2.79e-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: 2.79e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   179 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 254
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 1777507490   255 PEDVDVPQPDEKSIITYVSSL 275
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
619-797 2.28e-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: 2.28e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  619 LHGFVAAATKELMWLSEKEDEEVGFDWSERSTNTAAKKDSYSALMRELELKEKKIKEIQSTGDRLLREDHPARPTVESFQ 698
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  699 AALQTQWSWMLQLCCCVEAHLKENTAYFQFFSDVREAEEQLRKLQETLRRKYTCDrsiTVTRLEDLLQDAQDEKDQLNEY 778
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
                          170
                   ....*....|....*....
gi 1777507490  779 RGHLSGLAKRAKAIVQLKP 797
Cdd:cd00176    159 EPRLKSLNELAEELLEEGH 177
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2916-2954 1.18e-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: 1.18e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2916 LLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEMNEIL 2954
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2338-2376 2.18e-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: 2.18e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2338 LLEAQIATGGIIDPVHSHRLPVDVAFQRGYFDEEMSRIL 2376
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1679-1717 3.80e-15

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 71.59  E-value: 3.80e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 1679 LLEAQIATGGIIDPVHSHRVPVDVAFQRGYFDEEMSRVL 1717
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2597-2635 1.87e-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: 1.87e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2597 LLEAQAATGFLLDPVKGDRLTVDEAVRKGLVGPELHDRL 2635
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1103-1293 1.37e-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: 1.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1103 EDVLKAHEEQLKEAQaVPATLPELEATKAALKKLRAQAEAQQPVFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1182
Cdd:cd00176     13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1183 TQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLDSWLQDAKRRQEQIQAVPLANSqvVREQLRQEKALLEEIERH 1262
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLES--VEELLKKHKELEEELEAH 158
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1777507490 1263 GEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1293
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2007-2045 2.27e-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: 2.27e-13
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2007 LLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDEETHTAL 2045
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2262-2300 1.18e-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: 1.18e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2262 LLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPELHEKL 2300
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3185-3223 1.23e-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: 1.23e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 3185 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 3223
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2840-2878 2.79e-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: 2.79e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2840 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 2878
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2673-2711 2.96e-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: 2.96e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2673 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTYDQL 2711
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
915-1483 2.23e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.35  E-value: 2.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  915 FRTLKPEEQRQALRSLELHYQAFLRDSQDAGgfgpEDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIR 994
Cdd:COG1196    215 YRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  995 LQLEACETRTVHRLRLplDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALpepspAAPTLRSELELTLGK 1074
Cdd:COG1196    291 YELLAELARLEQDIAR--LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-----AEEELEEAEAELAEA 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1075 LEQVRSLSAIYLEKLKTISlviRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDEL 1154
Cdd:COG1196    364 EEALLEAEAELAEAEEELE---ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1155 RGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQtdvRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQI 1234
Cdd:COG1196    441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE---LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1235 QAVPLAnsQVVREQLRQEKALLEEIE-----RHGEKVEECQRFAKQYINAIKDYELQLVT-YKAQLEPVASPAKKPKVQS 1308
Cdd:COG1196    518 GLRGLA--GAVAVLIGVEAAYEAALEaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARG 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1309 GSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRERFIEQEKA 1388
Cdd:COG1196    596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1389 KLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAEEN--- 1465
Cdd:COG1196    676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAlee 755
                          570       580
                   ....*....|....*....|....*
gi 1777507490 1466 -------QRLRERLQHLEEEhRAAL 1483
Cdd:COG1196    756 lpeppdlEELERELERLERE-IEAL 779
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1603-1641 2.54e-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: 2.54e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 1603 LLEAQAASGFLLDPVRNRQLTVNEAVKEGVVGPELHHKL 1641
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
967-1297 8.08e-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: 8.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  967 QQLLQSLEQGEQEESRCQRCISELKDirlQLEACETRTVHRLRLPLDKEPARECAQ--RIAEQQKAQAEVEGLGKGVARL 1044
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKAERYQALLKEKREYEGyeLLKEKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1045 SAEAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRSTQG----AEDVLKAHEEQLKE 1115
Cdd:TIGR02169  250 EEELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELED 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1116 AQAVPATL-PELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQllerwqavla 1194
Cdd:TIGR02169  320 AEERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------- 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1195 qtdvRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQavplANSQVVREQLrqeKALLEEIERHGEKVEECQRFAK 1274
Cdd:TIGR02169  390 ----YREKLEKLKREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKI---NELEEEKEDKALEIKKQEWKLE 458
                          330       340
                   ....*....|....*....|...
gi 1777507490 1275 QYINAIKDYELQLVTYKAQLEPV 1297
Cdd:TIGR02169  459 QLAADLSKYEQELYDLKEEYDRV 481
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3261-3299 9.07e-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: 9.07e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 3261 FLEVQYLTGGLIEPDAPGRVPLEEALQRGTVDARTAQKL 3299
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
3183-3220 1.37e-09

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 55.57  E-value: 1.37e-09
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507490  3183 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 3220
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1935-1969 4.21e-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: 4.21e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1777507490 1935 QAGTGHIVDPTTSARLTVAEAVRAGLVGPELHEKL 1969
Cdd:pfam00681    5 QAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
864-1496 9.74e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.61  E-value: 9.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  864 QEAQEAIARLEAQHQALVALWHQLHTDMKSL-LAWQSLSRDVQLIrswslvtfrtlkpEEQRQALRSLELHYQAFLRDSQ 942
Cdd:TIGR02168  347 EELKEELESLEAELEELEAELEELESRLEELeEQLETLRSKVAQL-------------ELQIASLNNEIERLEARLERLE 413
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  943 DAggfgpEDRLQAEREygscsrhyqQLLQSLEQGEQEEsrCQRCISELKDIRLQLEACETRTVHRL------------RL 1010
Cdd:TIGR02168  414 DR-----RERLQQEIE---------ELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALeelreeleeaeqAL 477
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1011 PLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEK----VLALPEPSPAAPTLRSELELTLGKLEQ---VRSLSA 1083
Cdd:TIGR02168  478 DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgiLGVLSELISVDEGYEAAIEAALGGRLQavvVENLNA 557
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1084 I-----YLEK--LKTISLVIRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKAALKKlraqaeAQQPVFDALR--DEL 1154
Cdd:TIGR02168  558 AkkaiaFLKQneLGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRK------ALSYLLGGVLvvDDL 631
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1155 RGAQEVGERLqqRHGERDV----EVERWRERVTQLLERWQAVLAQtdvRQRELEQLGRQLRYYRESADPLDSWLQDAKRR 1230
Cdd:TIGR02168  632 DNALELAKKL--RPGYRIVtldgDLVRPGGVITGGSAKTNSSILE---RRREIEELEEKIEELEEKIAELEKALAELRKE 706
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1231 QEQIQAVPLANSQVVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEP-----VASPAKKPK 1305
Cdd:TIGR02168  707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeelAEAEAEIEE 786
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1306 VQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQEtqaLRQSFLSEKDSLLQRERFIEQ 1385
Cdd:TIGR02168  787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED---LEEQIEELSEDIESLAAEIEE 863
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1386 EKAKLEQLfQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAEEN 1465
Cdd:TIGR02168  864 LEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
                          650       660       670
                   ....*....|....*....|....*....|.
gi 1777507490 1466 QRLRERLQHLEEEhraALAHSEEVPASQATA 1496
Cdd:TIGR02168  943 ERLSEEYSLTLEE---AEALENKIEDDEEEA 970
PLEC smart00250
Plectin repeat;
2914-2950 2.43e-08

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 52.10  E-value: 2.43e-08
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  2914 IRLLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEM 2950
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
SPEC smart00150
Spectrin repeats;
620-712 8.17e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.72  E-value: 8.17e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   620 HGFVAAATKELMWLSEKEDEEVGFDWSERSTNTAAKKDSYSALMRELELKEKKIKEIQSTGDRLLREDHPARPTVESFQA 699
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90
                    ....*....|...
gi 1777507490   700 ALQTQWSWMLQLC 712
Cdd:smart00150   81 ELNERWEELKELA 93
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3017-3045 3.70e-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: 3.70e-07
                           10        20
                   ....*....|....*....|....*....
gi 1777507490 3017 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 3045
Cdd:pfam00681   11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
922-1634 5.54e-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: 55.89  E-value: 5.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  922 EQRQALRSLE-----LHYQAFLRDSQDAGGfgPEDRLQAEREYGSCSRHYQQLLQSLEQGEQEESrcqrcISELKDIRL- 995
Cdd:pfam15921  332 ELREAKRMYEdkieeLEKQLVLANSELTEA--RTERDQFSQESGNLDDQLQKLLADLHKREKELS-----LEKEQNKRLw 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  996 QLEACETRTVHRLRLPLDK---EPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVlalpepspaaPTLRSELELTL 1072
Cdd:pfam15921  405 DRDTGNSITIDHLRRELDDrnmEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKV----------SSLTAQLESTK 474
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1073 GKLEQVrslsaiyLEKLKTISLVIRSTQGAEDVLKAHEEQLKEAqavpatlpeLEATKAALKKLRAQAEAQQPVFDALRD 1152
Cdd:pfam15921  475 EMLRKV-------VEELTAKKMTLESSERTVSDLTASLQEKERA---------IEATNAEITKLRSRVDLKLQELQHLKN 538
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1153 E---LRGAQEVGERLQQRHGERDVEVERWR---ERVTQLLERWQ----AVLAQTDVRQRELEQLGRQLRYYRESADPLDS 1222
Cdd:pfam15921  539 EgdhLRNVQTECEALKLQMAEKDKVIEILRqqiENMTQLVGQHGrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDA 618
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1223 WLQD--AKRRQEQIQAVPLANSQvvREQLRQEKALLEEIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVASP 1300
Cdd:pfam15921  619 KIREleARVSDLELEKVKLVNAG--SERLRAVKDIKQERDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETT 693
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1301 AKKPKVQsgsesviqeyvdLRTRYSELTTLTSqyikfiseTLRRMEEEEMQTVQQEQLLQETQALRQ----------SFL 1370
Cdd:pfam15921  694 TNKLKMQ------------LKSAQSELEQTRN--------TLKSMEGSDGHAMKVAMGMQKQITAKRgqidalqskiQFL 753
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1371 SEKDSLLQRER-FIEQEKAKLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQlVASMEEA---------------RRQQR 1434
Cdd:pfam15921  754 EEAMTNANKEKhFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEK-VANMEVAldkaslqfaecqdiiQRQEQ 832
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1435 EAeegVRRKQEELQRLEEQRQQQEKllaeENQRLRERLQHLEEEHRaalAHSeEVPASQATATKALPNGRDAldgPATET 1514
Cdd:pfam15921  833 ES---VRLKLQHTLDVKELQGPGYT----SNSSMKPRLLQPASFTR---THS-NVPSSQSTASFLSHHSRKT---NALKE 898
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1515 EPEHAFDGLRQKV--PAQQLQEVGILSAEELQRLVQG-------RTTVAELEQREDV----RCYLQGRSSIAGLLLqpSN 1581
Cdd:pfam15921  899 DPTRDLKQLLQELrsVINEEPTVQLSKAEDKGRAPSLgalddrvRDCIIESSLRSDIchssSNSLQTEGSKSSETC--SR 976
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1777507490 1582 EKLSVYAALRRQLLS----PGTALILLEAQAASGFLLDPVRNRQLTVNEAVKEGVVG 1634
Cdd:pfam15921  977 EPVLLHAGELEDPSScftfPSTASPSVKNSASRSFHSSPKKSPVHSLLTSSAEGSIG 1033
PLEC smart00250
Plectin repeat;
2336-2372 7.12e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 47.86  E-value: 7.12e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  2336 IRLLEAQIATGGIIDPVHSHRLPVDVAFQRGYFDEEM 2372
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
1677-1713 1.74e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.71  E-value: 1.74e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  1677 IRLLEAQIATGGIIDPVHSHRVPVDVAFQRGYFDEEM 1713
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
2800-2837 2.13e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.71  E-value: 2.13e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507490  2800 QKFLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTA 2837
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2005-2041 2.33e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.32  E-value: 2.33e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  2005 LRLLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDEET 2041
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
2595-2630 2.75e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.32  E-value: 2.75e-06
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1777507490  2595 RLLLEAQAATGFLLDPVKGDRLTVDEAVRKGLVGPE 2630
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2802-2840 3.32e-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: 3.32e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2802 FLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTAFEL 2840
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1125-1327 4.54e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 4.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1125 ELEATKAALKKLRAQAEAQQPV------FDALRDELRGAQEVGERLQQRHGERdvEVERWRERVTQLLERWQAVLAQTDV 1198
Cdd:COG4913    236 DLERAHEALEDAREQIELLEPIrelaerYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELER 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1199 RQRELEQLGRQLRyyresadpldswlqdakRRQEQIQAVplansqvvreQLRQEKALLEEIERHGEKVEECQRFAKQYIN 1278
Cdd:COG4913    314 LEARLDALREELD-----------------ELEAQIRGN----------GGDRLEQLEREIERLERELEERERRRARLEA 366
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1777507490 1279 AIKDYELQLVTYKAQLEPVASPAK--KPKVQSGSESVIQEYVDLRTRYSEL 1327
Cdd:COG4913    367 LLAALGLPLPASAEEFAALRAEAAalLEALEEELEALEEALAEAEAALRDL 417
PLEC smart00250
Plectin repeat;
2224-2259 1.30e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.30e-05
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1777507490  2224 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTA 2259
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2671-2708 1.32e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.32e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507490  2671 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTY 2708
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3010-3038 1.42e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.42e-05
                            10        20
                    ....*....|....*....|....*....
gi 1777507490  3010 VRKRRVVIVDPETGKEMSVYEAYRKGLID 3038
Cdd:smart00250    6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
PTZ00121 PTZ00121
MAEBL; Provisional
919-1494 1.47e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  919 KPEEQRQAL---RSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSR-----HYQQLLQSLEQGEQ-EESRCQRCISE 989
Cdd:PTZ00121  1177 KAEAARKAEevrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKaeavkKAEEAKKDAEEAKKaEEERNNEEIRK 1256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  990 LKDIRLQ--------LEACETRTVHRLRLPLDKEPARECAQ----RIAEQQKAQAE----VEGLGKGV--ARLSAEAEKV 1051
Cdd:PTZ00121  1257 FEEARMAhfarrqaaIKAEEARKADELKKAEEKKKADEAKKaeekKKADEAKKKAEeakkADEAKKKAeeAKKKADAAKK 1336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1052 LAlPEPSPAAPTLRSELELTLGKLEQVRslsaiylEKLKTISLVIRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKA 1131
Cdd:PTZ00121  1337 KA-EEAKKAAEAAKAEAEAAADEAEAAE-------EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1132 ALKKlraqAEAQQPVFDALR---DELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQlgr 1208
Cdd:PTZ00121  1409 ELKK----AAAAKKKADEAKkkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE--- 1481
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1209 qlryyRESADPLDSWLQDAKRRQEQIQAVPLANSQVVREQLRQEKALLEEIERHGE--KVEEcqrfAKQYINAIKDYELQ 1286
Cdd:PTZ00121  1482 -----AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakKADE----AKKAEEKKKADELK 1552
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1287 LVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLR----TRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQET 1362
Cdd:PTZ00121  1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1363 QALRQSFLSEKDSLLQRERFIEQE------KAKLEQLFQEEVAKAQKLReeqqRQQQQMEQEKQQLVASMEEARR--QQR 1434
Cdd:PTZ00121  1633 KKVEQLKKKEAEEKKKAEELKKAEeenkikAAEEAKKAEEDKKKAEEAK----KAEEDEKKAAEALKKEAEEAKKaeELK 1708
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1777507490 1435 EAEEGVRRKQEE---LQRLEEQRQQQEKLLAEENQRLRERLQhLEEEHRAALAHSEEVPASQA 1494
Cdd:PTZ00121  1709 KKEAEEKKKAEElkkAEEENKIKAEEAKKEAEEDKKKAEEAK-KDEEEKKKIAHLKKEEEKKA 1770
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2224-2262 1.56e-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: 1.56e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2224 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTATLL 2262
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1565-1603 2.06e-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: 2.06e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 1565 YLQGRSSIAGLLLQPSNEKLSVYAALRRQLLSPGTALIL 1603
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC smart00150
Spectrin repeats;
523-617 2.48e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.78  E-value: 2.48e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   523 LRYLQDLLAWVGENQRRVDSAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARTDEGQL---SPATRGAYRDCLGRLD 599
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
                            90
                    ....*....|....*...
gi 1777507490   600 LQYAKLLNSSKARLRSLE 617
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
2558-2594 3.26e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.26e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  2558 RYLYGTGCVAGVYLPGSRQTLTVYQALKKGLLSAEVA 2594
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2840-2874 4.47e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.85  E-value: 4.47e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1777507490  2840 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 2874
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
2299-2335 5.94e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 5.94e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  2299 KLLSAEKAVTGYKDPYTGEQISLFQAMKKGLVLREHG 2335
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3149-3182 6.36e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 6.36e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1777507490  3149 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 3182
Cdd:smart00250    5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
SPEC smart00150
Spectrin repeats;
1111-1204 8.63e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 44.24  E-value: 8.63e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  1111 EQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALrdelrgaQEVGERLQQRHGERDVEVErwrERVTQLLERWQ 1190
Cdd:smart00150   18 EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEAL-------NELGEQLIEEGHPDAEEIE---ERLEELNERWE 87
                            90
                    ....*....|....
gi 1777507490  1191 AVLAQTDVRQRELE 1204
Cdd:smart00150   88 ELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
1968-2004 1.16e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.70  E-value: 1.16e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  1968 KLLLAERAVTGYKDPYSGQSVSLFQALKKGLIPREQG 2004
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2260-2295 1.65e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.65e-04
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1777507490  2260 TLLLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPE 2295
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
PLEC smart00250
Plectin repeat;
2634-2670 1.78e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.78e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  2634 RLLSAERAVTGYRDPYTEQTISLFQAMKKDLIPAEEA 2670
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3259-3296 2.13e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.93  E-value: 2.13e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507490  3259 QRFLEVQYLTGGLIEPDAPGRVPLEEALQRGTVDARTA 3296
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2559-2597 3.01e-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: 3.01e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2559 YLYGTGCVAGVYLPGSRQTLTVYQALKKGLLSAEVARLL 2597
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
1603-1636 3.48e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.54  E-value: 3.48e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1777507490  1603 LLEAQAASGFLLDPVRNRQLTVNEAVKEGVVGPE 1636
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
PLEC smart00250
Plectin repeat;
1640-1676 4.28e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.16  E-value: 4.28e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  1640 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVREHG 1676
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
1891-1923 9.49e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.00  E-value: 9.49e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1777507490  1891 RRALRGSSVIAGVWLEEAGQKLSIYEALRKDLL 1923
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
36-275 1.29e-03

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 44.55  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   36 EQDERDRVQKKTFTKWVNKHLIKHwraeaqrHISDLYEDLRDGhnlISLLEVLSGDSLPRERDVIRSSRLPREKGRM-RF 114
Cdd:COG5069    372 EFDAEGEFEARVFTFWLNSLDVSP-------EITNLFGDLRDQ---LILLQALSKKLMPMTVTHKLVKKQPASGIEEnRF 441
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  115 HKLQNVQIALDYLRHRQVKLVNIRNDDIADGNpKLTLGLIW-------TIILHFQISDiqvsgqsEDMTAKEKLLLWSQR 187
Cdd:COG5069    442 KAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKD-------GCGLSDSDLCAWLGS 513
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  188 MVEGY---QGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVyRQTNLENLDQA-------FSVAERDLGVTRLLDPED 257
Cdd:COG5069    514 LGLKGdkeEGIRSFGDPAGSVSGVFYLDVLKGIHSELVDYDLV-TRGFTEFDDIAdarslaiSSKILRSLGAIIKFLPED 592
                          250
                   ....*....|....*...
gi 1777507490  258 VDVPQPdEKSIITYVSSL 275
Cdd:COG5069    593 INGVRP-RLDVLTFIESL 609
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
632-712 1.68e-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: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  632 WLSEKE----DEEVGFDWSErstnTAAKKDSYSALMRELELKEKKIKEIQSTGDRLLREDHPARPTVESFQAALQTQWSW 707
Cdd:pfam00435   16 WIEEKEallsSEDYGKDLES----VQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERWEQ 91

                   ....*
gi 1777507490  708 MLQLC 712
Cdd:pfam00435   92 LLELA 96
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3155-3185 4.28e-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: 4.28e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1777507490 3155 AGILDTETLEKVSITEAMHRNLVDNITGQRL 3185
Cdd:pfam00681    9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
2877-2908 4.63e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.08  E-value: 4.63e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1777507490  2877 KLLSAERAVTGYKDPYSGKLISLFQAMKKGLI 2908
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1125-1205 6.57e-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: 6.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1125 ELEATKAALKKLRAQAEAqqpvFDALRDELRGAQEVGERLQQRHGErdvEVERWRERVTQLLERWQAVLAQTDVRQRELE 1204
Cdd:pfam00435   32 DLESVQALLKKHKALEAE----LAAHQDRVEALNELAEKLIDEGHY---ASEEIQERLEELNERWEQLLELAAERKQKLE 104

                   .
gi 1777507490 1205 Q 1205
Cdd:pfam00435  105 E 105
PLEC smart00250
Plectin repeat;
3297-3334 7.28e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 36.69  E-value: 7.28e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507490  3297 QKLRDVSAYSKYLTCPKTKLKISYKDALDRSMVEEGTG 3334
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
 
Name Accession Description Interval E-value
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
175-280 1.57e-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: 237.61  E-value: 1.57e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  175 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 254
Cdd:cd21238      1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 1777507490  255 PEDVDVPQPDEKSIITYVSSLYDAMP 280
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
41-162 4.60e-72

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: 236.14  E-value: 4.60e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   41 DRVQKKTFTKWVNKHLIKHWRaeaqrHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprekGRMRFHKLQNV 120
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARR-----RVVDLFEDLRDGHNLISLLEVLSGESLPRER------------GRMRFHRLQNV 63
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1777507490  121 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 162
Cdd:cd21188     64 QTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
38-173 1.19e-69

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: 229.91  E-value: 1.19e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   38 DERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpreKGRMRFHKL 117
Cdd:cd21235      1 DERDRVQKKTFTKWVNKHLIK-----AQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE------------KGRMRFHKL 63
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777507490  118 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 173
Cdd:cd21235     64 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
37-171 2.04e-67

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: 224.09  E-value: 2.04e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   37 QDERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpreKGRMRFHK 116
Cdd:cd21236     11 KDERDKVQKKTFTKWINQHLMK-----VRKHVNDLYEDLRDGHNLISLLEVLSGDTLPRE------------KGRMRFHR 73
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1777507490  117 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 171
Cdd:cd21236     74 LQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
176-280 5.87e-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: 5.87e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  176 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 255
Cdd:cd21189      1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                           90       100
                   ....*....|....*....|....*
gi 1777507490  256 EDVDVPQPDEKSIITYVSSLYDAMP 280
Cdd:cd21189     81 EDVDVPEPDEKSIITYVSSLYDVFP 105
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
38-172 1.93e-59

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: 200.64  E-value: 1.93e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   38 DERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGdslprerdvirsSRLPREKGRMRFHKL 117
Cdd:cd21237      1 DERDRVQKKTFTKWVNKHLMK-----VRKHINDLYEDLRDGHNLISLLEVLSG------------VKLPREKGRMRFHRL 63
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1777507490  118 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 172
Cdd:cd21237     64 QNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
176-280 1.86e-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: 1.86e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  176 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 255
Cdd:cd21239      1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
                           90       100
                   ....*....|....*....|....*
gi 1777507490  256 EDVDVPQPDEKSIITYVSSLYDAMP 280
Cdd:cd21239     80 EDVDVSSPDEKSVITYVSSLYDVFP 104
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
174-280 3.31e-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: 3.31e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  174 DMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 253
Cdd:cd21240      2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
                           90       100
                   ....*....|....*....|....*..
gi 1777507490  254 DPEDVDVPQPDEKSIITYVSSLYDAMP 280
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 ...
30-159 4.89e-46

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: 162.54  E-value: 4.89e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   30 RRRVQDEQDERDRVQKKTFTKWVNKHLIKHwraeaQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEK 109
Cdd:cd21246      3 RSRIKALADEREAVQKKTFTKWVNSHLARV-----GCRINDLYTDLRDGRMLIKLLEVLSGERLPKP-----------TK 66
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1777507490  110 GRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 159
Cdd:cd21246     67 GKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
176-276 5.48e-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: 5.48e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  176 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 255
Cdd:cd21194      2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
                           90       100
                   ....*....|....*....|.
gi 1777507490  256 EDVDVPQPDEKSIITYVSSLY 276
Cdd:cd21194     82 EDVDVARPDEKSIMTYVASYY 102
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
43-163 6.71e-46

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: 161.40  E-value: 6.71e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   43 VQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGdslprerdvirsSRLPREKGRMRFHKLQNVQI 122
Cdd:cd21186      2 VQKKTFTKWINSQLSK----ANKPPIKDLFEDLRDGTRLLALLEVLTG------------KKLKPEKGRMRVHHLNNVNR 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1777507490  123 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 163
Cdd:cd21186     66 ALQVLEQNNVKLVNISSNDIVDGNPKLTLGLVWSIILHWQV 106
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
36-387 9.54e-45

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 174.36  E-value: 9.54e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   36 EQDERDRVQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLprerdvIRSSRLPRekgrMRFH 115
Cdd:COG5069      2 EAKKWQKVQKKTFTKWTNEKLIS----GGQKEFGDLDTDLKDGVKLAQLLEALQKDNA------GEYNETPE----TRIH 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  116 KLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-G 194
Cdd:COG5069     68 VMENVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpE 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  195 LRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITY 271
Cdd:COG5069    145 VDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTY 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  272 VS------SLYD----AMPRVPDVQDGVKANElQLRwQEYRELVVLLLQWVRQHTAAFEERRFPSSFEEIEILWCQFLKF 341
Cdd:COG5069    225 VSwyiirfGLLEkidiALHRVYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQL 302
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1777507490  342 KETE--LPAKEAD-KNRSKGIFQSLEgAVQAGQLKVPPGYHPLDVEKEW 387
Cdd:COG5069    303 NALCsrAPLETTDlHSLAGQILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
176-276 3.77e-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: 3.77e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  176 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 255
Cdd:cd21248      2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
                           90       100
                   ....*....|....*....|.
gi 1777507490  256 EDVDVPQPDEKSIITYVSSLY 276
Cdd:cd21248     82 EDVNVEQPDEKSIITYVVTYY 102
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
30-159 3.11e-43

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: 154.38  E-value: 3.11e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   30 RRRVQDEQDERDRVQKKTFTKWVNKHLIKHwraeaQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEK 109
Cdd:cd21193      3 KGRIRALQEERINIQKKTFTKWINSFLEKA-----NLEIGDLFTDLSDGKLLLKLLEIISGEKLGKP-----------NR 66
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1777507490  110 GRMRFHKLQNVQIALDYLrHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 159
Cdd:cd21193     67 GRLRVQKIENVNKALAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
39-163 2.31e-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: 151.76  E-value: 2.31e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   39 ERDRVQKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDslprerdvirssRLPREKGRM--RFHK 116
Cdd:cd21241      1 EQERVQKKTFTNWINSYLAKR---KPPMKVEDLFEDIKDGTKLLALLEVLSGE------------KLPCEKGRRlkRVHF 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1777507490  117 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 163
Cdd:cd21241     66 LSNINTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
175-280 6.95e-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: 6.95e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  175 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 254
Cdd:cd21243      4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
                           90       100
                   ....*....|....*....|....*.
gi 1777507490  255 PEDVDVPQPDEKSIITYVSSLYDAMP 280
Cdd:cd21243     84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
39-163 2.13e-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: 148.87  E-value: 2.13e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   39 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhISDLYEDLRDGHNLISLLEVLSGDslprerdvirssRLPREKGRM--RFHK 116
Cdd:cd21190      1 EQERVQKKTFTNWINSHLAKLSQPIV---INDLFVDIKDGTALLRLLEVLSGQ------------KLPIESGRVlqRAHK 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1777507490  117 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 163
Cdd:cd21190     66 LSNIRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
163-278 4.29e-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: 4.29e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  163 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 242
Cdd:cd21216      1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507490  243 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 278
Cdd:cd21216     77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
172-276 1.10e-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: 1.10e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  172 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 251
Cdd:cd21319      1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
                           90       100
                   ....*....|....*....|....*
gi 1777507490  252 LLDPEDVDVPQPDEKSIITYVSSLY 276
Cdd:cd21319     81 LLDPEDVFTENPDEKSIITYVVAFY 105
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
30-159 1.27e-38

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: 141.73  E-value: 1.27e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   30 RRRVQDEQDERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEK 109
Cdd:cd21317     18 RSRIKALADEREAVQKKTFTKWVNSHL-----ARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKP-----------TK 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1777507490  110 GRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 159
Cdd:cd21317     82 GRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
32-159 4.14e-38

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: 140.55  E-value: 4.14e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   32 RVQDEQDERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGR 111
Cdd:cd21318     27 RIKALADEREAVQKKTFTKWVNSHL-----ARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKP-----------TRGR 90
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1777507490  112 MRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 159
Cdd:cd21318     91 MRIHSLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
172-276 4.14e-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: 4.14e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  172 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 251
Cdd:cd21321      1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
                           90       100
                   ....*....|....*....|....*
gi 1777507490  252 LLDPEDVDVPQPDEKSIITYVSSLY 276
Cdd:cd21321     81 LLDPEDVNVDQPDEKSIITYVATYY 105
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
175-276 2.92e-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: 2.92e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  175 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 254
Cdd:cd21249      3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
                           90       100
                   ....*....|....*....|..
gi 1777507490  255 PEDVDVPQPDEKSIITYVSSLY 276
Cdd:cd21249     83 PEDVAVPHPDERSIMTYVSLYY 104
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
39-163 5.11e-37

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: 136.50  E-value: 5.11e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   39 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhISDLYEDLRDGHNLISLLEVLSGDslprerdvirssRLPREKGRMRFHKLQ 118
Cdd:cd21242      1 EQEQTQKRTFTNWINSQLAKHSPPSV---VSDLFTDIQDGHRLLDLLEVLSGQ------------QLPREKGHNVFQCRS 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1777507490  119 NVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 163
Cdd:cd21242     66 NIETALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
160-276 4.00e-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: 4.00e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  160 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQA 239
Cdd:cd21322      1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507490  240 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 276
Cdd:cd21322     81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
41-159 4.81e-36

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: 133.28  E-value: 4.81e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   41 DRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerdvirssrlPREKGRMRFHKLQNV 120
Cdd:cd21214      3 EKQQRKTFTAWCNSHLRK-----AGTQIENIEEDFRDGLKLMLLLEVISGERLP-----------KPERGKMRFHKIANV 66
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1777507490  121 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 159
Cdd:cd21214     67 NKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
179-280 1.40e-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: 1.40e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  179 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 257
Cdd:cd21187      2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
                           90       100
                   ....*....|....*....|...
gi 1777507490  258 VDVPQPDEKSIITYVSSLYDAMP 280
Cdd:cd21187     82 VNVEQPDKKSILMYVTSLFQVLP 104
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
43-161 1.12e-34

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: 129.44  E-value: 1.12e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   43 VQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprEKGRMRFHKLQNVQI 122
Cdd:cd21215      4 VQKKTFTKWLNTKL-----SSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYN----------KNPKMRVQKLENVNK 68
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1777507490  123 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 161
Cdd:cd21215     69 ALEFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
38-163 1.04e-33

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: 126.96  E-value: 1.04e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   38 DERDRVQKKTFTKWVNKHLIKHWRaeaqRHISDLYEDLRDGHNLISLLEVLSGdslprerdvirsSRLPREKGRMRFHKL 117
Cdd:cd21231      1 YEREDVQKKTFTKWINAQFAKFGK----PPIEDLFTDLQDGRRLLELLEGLTG------------QKLVKEKGSTRVHAL 64
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1777507490  118 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 163
Cdd:cd21231     65 NNVNKALQVLQKNNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
175-273 3.90e-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: 125.23  E-value: 3.90e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  175 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 254
Cdd:cd21192      2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
                           90
                   ....*....|....*....
gi 1777507490  255 PEDVDVPQPDEKSIITYVS 273
Cdd:cd21192     82 VEDVLVDKPDERSIMTYVS 100
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
176-276 1.17e-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: 1.17e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  176 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 255
Cdd:cd21320      2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
                           90       100
                   ....*....|....*....|.
gi 1777507490  256 EDVDVPQPDEKSIITYVSSLY 276
Cdd:cd21320     82 EDISVDHPDEKSIITYVVTYY 102
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
175-273 6.64e-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: 121.87  E-value: 6.64e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  175 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 254
Cdd:cd21244      4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
                           90
                   ....*....|....*....
gi 1777507490  255 PEDVDVPQPDEKSIITYVS 273
Cdd:cd21244     84 PEDVDVVNPDEKSIMTYVA 102
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
163-278 2.05e-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: 2.05e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  163 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 242
Cdd:cd21291      1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507490  243 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 278
Cdd:cd21291     77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
30-159 2.60e-31

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: 121.69  E-value: 2.60e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   30 RRRVQDEQDERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEK 109
Cdd:cd21316     40 RSRIKALADEREAVQKKTFTKWVNSHL-----ARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKP-----------TK 103
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1777507490  110 GRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 159
Cdd:cd21316    104 GRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
179-280 3.78e-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: 3.78e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  179 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 257
Cdd:cd21234      2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
                           90       100
                   ....*....|....*....|...
gi 1777507490  258 VDVPQPDEKSIITYVSSLYDAMP 280
Cdd:cd21234     82 VAVQLPDKKSIIMYLTSLFEVLP 104
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
895-972 4.21e-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: 4.21e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777507490  895 LAWQSLSRDVQLIRSWSLVTFRTLKPEEQRQALRSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSRHYQQLLQS 972
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
179-281 7.43e-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: 7.43e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  179 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 256
Cdd:cd21233      2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
                           90       100
                   ....*....|....*....|....*
gi 1777507490  257 DVDVPQPDEKSIITYVSSLYDAMPR 281
Cdd:cd21233     82 DVATAHPDKKSILMYVTSLFQVLPQ 106
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
43-163 8.88e-31

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: 118.54  E-value: 8.88e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   43 VQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRerdVIRssrlpreKGRMRFHKLQNVQI 122
Cdd:cd21227      4 IQKNTFTNWVNEQL-----KPTGMSVEDLATDLEDGVKLIALVEILQGRKLGR---VIK-------KPLNQHQKLENVTL 68
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1777507490  123 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 163
Cdd:cd21227     69 ALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
181-276 2.54e-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: 2.54e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  181 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 259
Cdd:cd21253      6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
                           90
                   ....*....|....*..
gi 1777507490  260 VPQPDEKSIITYVSSLY 276
Cdd:cd21253     86 LKVPDKLSILTYVSQYY 102
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
42-164 3.86e-30

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: 117.17  E-value: 3.86e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   42 RVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprEKGRMRFHKLQNVQ 121
Cdd:cd21311     14 RIQQNTFTRWANEHLKT-----ANKHIADLETDLSDGLRLIALVEVLSGKKFPKFN----------KRPTFRSQKLENVS 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1777507490  122 IALDYLRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 164
Cdd:cd21311     79 VALKFLEEDEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
161-278 7.74e-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: 7.74e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  161 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAF 240
Cdd:cd21290      2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1777507490  241 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 278
Cdd:cd21290     78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
39-165 1.26e-29

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


Pssm-ID: 409040  Cd Length: 114  Bit Score: 115.37  E-value: 1.26e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   39 ERDRVQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvIRSSRlprekgrMRFHKLQ 118
Cdd:cd21191      1 ERENVQKRTFTRWINLHLEK---CNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQE---YKPSS-------HRIFRLN 67
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1777507490  119 NVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 165
Cdd:cd21191     68 NIAKALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
43-163 2.51e-29

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: 114.34  E-value: 2.51e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   43 VQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlprekGRMRFHKLQNVQI 122
Cdd:cd21232      2 VQKKTFTKWINARFSK----SGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKER------------GSTRVHALNNVNR 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1777507490  123 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 163
Cdd:cd21232     66 VLQVLHQNNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
179-278 1.09e-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: 1.09e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  179 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 257
Cdd:cd22198      3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
                           90       100
                   ....*....|....*....|.
gi 1777507490  258 VDVPQPDEKSIITYVSSLYDA 278
Cdd:cd22198     83 ASLAVPDKLSMVSYLSQFYEA 103
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
163-278 9.23e-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: 9.23e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  163 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 242
Cdd:cd21287      1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507490  243 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 278
Cdd:cd21287     77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
42-161 1.07e-27

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: 109.49  E-value: 1.07e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   42 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlprEKGRMRFHKLQNVQ 121
Cdd:cd21183      3 RIQANTFTRWCNEHL-----KERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYN---------RRPAFQQHYLENVS 68
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1777507490  122 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 161
Cdd:cd21183     69 TALKFIEADHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
163-278 3.08e-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: 3.08e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  163 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 242
Cdd:cd21289      1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507490  243 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 278
Cdd:cd21289     77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
163-278 8.81e-26

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: 8.81e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  163 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 242
Cdd:cd21288      1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507490  243 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 278
Cdd:cd21288     77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
181-276 1.44e-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: 1.44e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  181 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 259
Cdd:cd21197      5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
                           90
                   ....*....|....*..
gi 1777507490  260 VPQPDEKSIITYVSSLY 276
Cdd:cd21197     85 MHVPDRLSIITYVSQYY 101
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
32-163 3.55e-25

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: 102.91  E-value: 3.55e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   32 RVQDEQDERDRVQKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlprEKGR 111
Cdd:cd21247      9 HIRKLQEQRMTMQKKTFTKWMNNVFSKN---GAKIEITDIYTELKDGIHLLRLLELISGEQLPRP-----------SRGK 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1777507490  112 MRFHKLQNVQIALDYLRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 163
Cdd:cd21247     75 MRVHFLENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
175-281 4.88e-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: 4.88e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  175 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 251
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1777507490  252 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 281
Cdd:pfam00307   81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
42-161 9.86e-25

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: 101.03  E-value: 9.86e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   42 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlprEKGRMRFHKLQNVQ 121
Cdd:cd21228      3 KIQQNTFTRWCNEHL-----KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYN---------KRPTFRQMKLENVS 68
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1777507490  122 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 161
Cdd:cd21228     69 VALEFLERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
179-279 1.11e-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: 1.11e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  179 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 258
Cdd:cd21226      3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
                           90       100
                   ....*....|....*....|.
gi 1777507490  259 DVPQPDEKSIITYVSSLYDAM 279
Cdd:cd21226     83 MTGNPDERSIVLYTSLFYHAF 103
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
177-276 4.30e-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: 4.30e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  177 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 256
Cdd:cd21252      1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
                           90       100
                   ....*....|....*....|.
gi 1777507490  257 D-VDVPQPDEKSIITYVSSLY 276
Cdd:cd21252     81 DmVSMKVPDCLSIMTYVSQYY 101
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
176-280 4.72e-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: 4.72e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  176 TAKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 255
Cdd:cd21245      3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
                           90       100
                   ....*....|....*....|....*
gi 1777507490  256 EDVDVPQPDEKSIITYVSSLYDAMP 280
Cdd:cd21245     82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
42-164 4.85e-24

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: 99.72  E-value: 4.85e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   42 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlPREKgrMRFHKLQNVQ 121
Cdd:cd21310     15 KIQQNTFTRWCNEHL-----KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYH-------PRPN--FRQMKLENVS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1777507490  122 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 164
Cdd:cd21310     81 VALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
176-276 2.17e-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: 2.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  176 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 255
Cdd:cd21198      1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
                           90       100
                   ....*....|....*....|..
gi 1777507490  256 EDVDVPQ-PDEKSIITYVSSLY 276
Cdd:cd21198     80 ADMVLLSvPDKLSVMTYLHQIR 101
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
794-860 2.28e-23

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 95.79  E-value: 2.28e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1777507490  794 QLKPRSpaHPVRGRVPLLAVCDYKQVEVTVHKGDECQLVGPAQPFHWKVLSSSGSEAAVPSVCFLIP 860
Cdd:pfam17902    1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
46-160 7.06e-23

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: 95.46  E-value: 7.06e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490    46 KTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrERDVirssrlprEKGRMRFHKLQNVQIALD 125
Cdd:smart00033    1 KTLLRWVNSLLAE----YDKPPVTNFSSDLKDGVALCALLNSLSPGLVD-KKKV--------AASLSRFKKIENINLALS 67
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1777507490   126 YLRHRQVKLVNIRNDDIADGnPKLTLGLIWTIILH 160
Cdd:smart00033   68 FAEKLGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
43-163 1.24e-22

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: 95.05  E-value: 1.24e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   43 VQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerdvirssrlPREKGRMRFHKLQNVQI 122
Cdd:pfam00307    2 ELEKELLRWINSHLAE---YGPGVRVTNFTTDLRDGLALCALLNKLAPGLVD-----------KKKLNKSEFDKLENINL 67
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1777507490  123 ALDYLRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 163
Cdd:pfam00307   68 ALDVAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
176-274 2.29e-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: 2.29e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  176 TAKEKLLLWSQRMVEGYqglRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 254
Cdd:cd21184      1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
                           90       100
                   ....*....|....*....|
gi 1777507490  255 PEDVDVPQPDEKSIITYVSS 274
Cdd:cd21184     78 PEDMVSPNVDELSVMTYLSY 97
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
180-277 1.96e-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: 1.96e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  180 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 258
Cdd:cd21195      8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
                           90
                   ....*....|....*....
gi 1777507490  259 DVPQPDEKSIITYVSSLYD 277
Cdd:cd21195     88 SAQEPDKLSMVMYLSKFYE 106
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
176-276 3.08e-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: 3.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  176 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 255
Cdd:cd21200      1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
                           90       100
                   ....*....|....*....|...
gi 1777507490  256 EDVDV--PQPDEKSIITYVSSLY 276
Cdd:cd21200     81 EDMVRmgNRPDWKCVFTYVQSLY 103
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
42-164 3.34e-20

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: 88.99  E-value: 3.34e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   42 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDvirssrlprEKGRMRFHKLQNVQ 121
Cdd:cd21308     19 KIQQNTFTRWCNEHL-----KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHN---------QRPTFRQMQLENVS 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1777507490  122 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 164
Cdd:cd21308     85 VALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
42-164 7.22e-20

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: 88.21  E-value: 7.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   42 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirssrlpREKGRMRFHKLQNVQ 121
Cdd:cd21309     16 KIQQNTFTRWCNEHL-----KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKY---------HQRPTFRQMQLENVS 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1777507490  122 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 164
Cdd:cd21309     82 VALEFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
172-277 1.02e-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: 1.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  172 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 251
Cdd:cd21251      1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
                           90       100
                   ....*....|....*....|....*..
gi 1777507490  252 LLDPEDV-DVPQPDEKSIITYVSSLYD 277
Cdd:cd21251     81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
176-275 2.05e-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: 2.05e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  176 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 255
Cdd:cd21255      1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
                           90       100
                   ....*....|....*....|.
gi 1777507490  256 ED-VDVPQPDEKSIITYVSSL 275
Cdd:cd21255     80 ADmVLLPIPDKLIVMTYLCQL 100
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
179-275 2.79e-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: 2.79e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   179 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 254
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 1777507490   255 PEDVDVPQPDEKSIITYVSSL 275
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
619-797 2.28e-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: 2.28e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  619 LHGFVAAATKELMWLSEKEDEEVGFDWSERSTNTAAKKDSYSALMRELELKEKKIKEIQSTGDRLLREDHPARPTVESFQ 698
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  699 AALQTQWSWMLQLCCCVEAHLKENTAYFQFFSDVREAEEQLRKLQETLRRKYTCDrsiTVTRLEDLLQDAQDEKDQLNEY 778
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
                          170
                   ....*....|....*....
gi 1777507490  779 RGHLSGLAKRAKAIVQLKP 797
Cdd:cd00176    159 EPRLKSLNELAEELLEEGH 177
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
180-277 2.63e-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: 2.63e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  180 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 258
Cdd:cd21250      8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
                           90
                   ....*....|....*....
gi 1777507490  259 DVPQPDEKSIITYVSSLYD 277
Cdd:cd21250     88 SAEEPDKLSMVMYLSKFYE 106
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
176-275 3.20e-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: 3.20e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  176 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 255
Cdd:cd21254      1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
                           90       100
                   ....*....|....*....|.
gi 1777507490  256 ED-VDVPQPDEKSIITYVSSL 275
Cdd:cd21254     80 SDmVLLAVPDKLTVMTYLYQI 100
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
178-289 1.14e-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: 1.14e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  178 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 257
Cdd:cd21259      3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1777507490  258 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 289
Cdd:cd21259     83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
44-161 1.19e-16

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: 78.01  E-value: 1.19e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   44 QKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRerdvirssrlPREKGRMRFHKLQNVQIA 123
Cdd:cd21212      1 EIEIYTDWANHYLEKG---GHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPG----------IHSRPKTRAQKLENIQAC 67
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1777507490  124 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 161
Cdd:cd21212     68 LQFLAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
45-159 1.47e-16

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: 77.76  E-value: 1.47e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   45 KKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRErdvirssrlpREKGRMRFHKLQNVQIAL 124
Cdd:cd00014      1 EEELLKWINEVLGE----ELPVSITDLFESLRDGVLLCKLINKLSPGSIPKI----------NKKPKSPFKKRENINLFL 66
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507490  125 DYLRHRQV-KLVNIRNDDI-ADGNPKLTLGLIWTIIL 159
Cdd:cd00014     67 NACKKLGLpELDLFEPEDLyEKGNLKKVLGTLWALAL 103
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
181-276 3.46e-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: 3.46e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  181 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 259
Cdd:cd21199     13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
                           90
                   ....*....|....*..
gi 1777507490  260 VPQPDEKSIITYVSSLY 276
Cdd:cd21199     92 MERPDWQSVMSYVTAIY 108
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
178-277 5.01e-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: 5.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  178 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 257
Cdd:cd21261      3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
                           90       100
                   ....*....|....*....|..
gi 1777507490  258 VDV--PQPDEKSIITYVSSLYD 277
Cdd:cd21261     83 MMVmgRKPDPMCVFTYVQSLYN 104
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
178-281 8.13e-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: 8.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  178 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 257
Cdd:cd21258      3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
                           90       100
                   ....*....|....*....|....*.
gi 1777507490  258 VDV--PQPDEKSIITYVSSLYDAMPR 281
Cdd:cd21258     83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2916-2954 1.18e-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: 1.18e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2916 LLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEMNEIL 2954
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2338-2376 2.18e-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: 2.18e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2338 LLEAQIATGGIIDPVHSHRLPVDVAFQRGYFDEEMSRIL 2376
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1679-1717 3.80e-15

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 71.59  E-value: 3.80e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 1679 LLEAQIATGGIIDPVHSHRVPVDVAFQRGYFDEEMSRVL 1717
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
176-276 1.17e-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: 1.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  176 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 255
Cdd:cd21256     14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
                           90       100
                   ....*....|....*....|..
gi 1777507490  256 ED-VDVPQPDEKSIITYVSSLY 276
Cdd:cd21256     93 NEmVRTERPDWQSVMTYVTAIY 114
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
35-160 1.30e-14

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: 72.31  E-value: 1.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   35 DEQDERdrvqkkTFTKWVNKHLIKHwraeaqrHISDLYEDLRDGhnlISLLEVLsgDSLprERDVIRSSRLPREKGRMRF 114
Cdd:cd21219      2 GSREER------AFRMWLNSLGLDP-------LINNLYEDLRDG---LVLLQVL--DKI--QPGCVNWKKVNKPKPLNKF 61
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1777507490  115 HKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 160
Cdd:cd21219     62 KKVENCNYAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
178-279 1.44e-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: 1.44e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  178 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 257
Cdd:cd21260      3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
                           90       100
                   ....*....|....*....|...
gi 1777507490  258 -VDVPQPDEKSIITYVSSLYDAM 279
Cdd:cd21260     83 mVRMSVPDSKCVYTYIQELYRSL 105
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
44-161 1.69e-14

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


Pssm-ID: 409062  Cd Length: 107  Bit Score: 71.95  E-value: 1.69e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   44 QKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPrerDVIRSsrlPREKGRMRfhklQNVQIA 123
Cdd:cd21213      1 QLQAYVAWVNSQLKKR---PGIRPVQDLRRDLRDGVALAQLIEILAGEKLP---GIDWN---PTTDAERK----ENVEKV 67
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1777507490  124 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 161
Cdd:cd21213     68 LQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2597-2635 1.87e-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: 1.87e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2597 LLEAQAATGFLLDPVKGDRLTVDEAVRKGLVGPELHDRL 2635
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
176-273 9.20e-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: 9.20e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  176 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI----DMNKVYRqtnLENLDQAFSVAERDLGVTR 251
Cdd:cd21230      1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
                           90       100
                   ....*....|....*....|..
gi 1777507490  252 LLDPEDVDVPQPDEKSIITYVS 273
Cdd:cd21230     75 LITPEEIINPNVDEMSVMTYLS 96
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
176-276 1.04e-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: 1.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  176 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 255
Cdd:cd21257      8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
                           90       100
                   ....*....|....*....|..
gi 1777507490  256 ED-VDVPQPDEKSIITYVSSLY 276
Cdd:cd21257     87 SEmMYTDRPDWQSVMQYVAQIY 108
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
41-157 1.10e-13

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: 69.87  E-value: 1.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   41 DRVQKKTFTKWVNKHLIKhwRAEAQrhISDLYEDLRDGHNLISLLEVLSGDSLPRERDVIRSSRLPRekgrmrfhkLQNV 120
Cdd:cd21225      2 EKVQIKAFTAWVNSVLEK--RGIPK--ISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEPKNRIQM---------IQNL 68
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1777507490  121 QIALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTI 157
Cdd:cd21225     69 HLAMLFIEEDlKIRVQGIGAEDFVDNNKKLILGLLWTL 106
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1103-1293 1.37e-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: 1.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1103 EDVLKAHEEQLKEAQaVPATLPELEATKAALKKLRAQAEAQQPVFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1182
Cdd:cd00176     13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1183 TQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLDSWLQDAKRRQEQIQAVPLANSqvVREQLRQEKALLEEIERH 1262
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLES--VEELLKKHKELEEELEAH 158
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1777507490 1263 GEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1293
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2007-2045 2.27e-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: 2.27e-13
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2007 LLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDEETHTAL 2045
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
523-712 3.38e-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: 3.38e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  523 LRYLQDLLAWVGENQRRVDSAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARTDEGQLSPATRGAY---RDCLGRLD 599
Cdd:cd00176      6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  600 LQYAKLLNSSKARLRSLE---SLHGFVAAATKELMWLSEKEDEEVGFDWSERSTNTAAKKDSYSALMRELELKEKKIKEI 676
Cdd:cd00176     86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1777507490  677 QSTGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 712
Cdd:cd00176    166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2262-2300 1.18e-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: 1.18e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2262 LLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPELHEKL 2300
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3185-3223 1.23e-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: 1.23e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 3185 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 3223
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
178-277 1.62e-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: 1.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  178 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 253
Cdd:cd00014      1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
                           90       100
                   ....*....|....*....|....
gi 1777507490  254 DPEDVdVPQPDEKSIITYVSSLYD 277
Cdd:cd00014     81 EPEDL-YEKGNLKKVLGTLWALAL 103
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
178-278 2.07e-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: 2.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  178 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 257
Cdd:cd21196      5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
                           90       100
                   ....*....|....*....|.
gi 1777507490  258 VdVPQPDEKSIITYVSSLYDA 278
Cdd:cd21196     85 V-VAGSDPLGLIAYLSHFHSA 104
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2840-2878 2.79e-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: 2.79e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2840 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 2878
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2673-2711 2.96e-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: 2.96e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2673 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTYDQL 2711
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
178-273 4.19e-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: 4.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  178 KEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 256
Cdd:cd21229      5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
                           90
                   ....*....|....*..
gi 1777507490  257 DVDVPQPDEKSIITYVS 273
Cdd:cd21229     82 DLSSPHLDELSGMTYLS 98
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
46-164 7.17e-12

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: 64.95  E-value: 7.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   46 KTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLsgdslprERDVIRSSRLPREKGRMR--FHKLQNVQIA 123
Cdd:cd21298      9 KTYRNWMNS-------LGVNPFVNHLYSDLRDGLVLLQLYDKI-------KPGVVDWSRVNKPFKKLGanMKKIENCNYA 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1777507490  124 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 164
Cdd:cd21298     75 VELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
63-158 1.91e-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: 1.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   63 EAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirsSRLPrEKGRMRfhKLQNVQIALDYLRHRQV----KLVNIR 138
Cdd:cd21223     21 EFDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSK-----LRVP-AISRLQ--KLHNVEVALKALKEAGVlrggDGGGIT 92
                           90       100
                   ....*....|....*....|
gi 1777507490  139 NDDIADGNPKLTLGLIWTII 158
Cdd:cd21223     93 AKDIVDGHREKTLALLWRII 112
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
915-1483 2.23e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.35  E-value: 2.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  915 FRTLKPEEQRQALRSLELHYQAFLRDSQDAGgfgpEDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIR 994
Cdd:COG1196    215 YRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  995 LQLEACETRTVHRLRLplDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALpepspAAPTLRSELELTLGK 1074
Cdd:COG1196    291 YELLAELARLEQDIAR--LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-----AEEELEEAEAELAEA 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1075 LEQVRSLSAIYLEKLKTISlviRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDEL 1154
Cdd:COG1196    364 EEALLEAEAELAEAEEELE---ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1155 RGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQtdvRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQI 1234
Cdd:COG1196    441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE---LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1235 QAVPLAnsQVVREQLRQEKALLEEIE-----RHGEKVEECQRFAKQYINAIKDYELQLVT-YKAQLEPVASPAKKPKVQS 1308
Cdd:COG1196    518 GLRGLA--GAVAVLIGVEAAYEAALEaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARG 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1309 GSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRERFIEQEKA 1388
Cdd:COG1196    596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1389 KLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAEEN--- 1465
Cdd:COG1196    676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAlee 755
                          570       580
                   ....*....|....*....|....*
gi 1777507490 1466 -------QRLRERLQHLEEEhRAAL 1483
Cdd:COG1196    756 lpeppdlEELERELERLERE-IEAL 779
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1603-1641 2.54e-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: 2.54e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 1603 LLEAQAASGFLLDPVRNRQLTVNEAVKEGVVGPELHHKL 1641
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
36-155 5.30e-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: 62.44  E-value: 5.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   36 EQDERDRVqkktFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSgdslPRERDVIRSSRLPREKGRMRFH 115
Cdd:cd21300      4 EGEREARV----FTLWLNS-------LDVEPAVNDLFEDLRDGLILLQAYDKVI----PGSVNWKKVNKAPASAEISRFK 68
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1777507490  116 KLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIW 155
Cdd:cd21300     69 AVENTNYAVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
967-1297 8.08e-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: 8.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  967 QQLLQSLEQGEQEESRCQRCISELKDirlQLEACETRTVHRLRLPLDKEPARECAQ--RIAEQQKAQAEVEGLGKGVARL 1044
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKAERYQALLKEKREYEGyeLLKEKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1045 SAEAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRSTQG----AEDVLKAHEEQLKE 1115
Cdd:TIGR02169  250 EEELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELED 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1116 AQAVPATL-PELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQllerwqavla 1194
Cdd:TIGR02169  320 AEERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------- 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1195 qtdvRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQavplANSQVVREQLrqeKALLEEIERHGEKVEECQRFAK 1274
Cdd:TIGR02169  390 ----YREKLEKLKREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKI---NELEEEKEDKALEIKKQEWKLE 458
                          330       340
                   ....*....|....*....|...
gi 1777507490 1275 QYINAIKDYELQLVTYKAQLEPV 1297
Cdd:TIGR02169  459 QLAADLSKYEQELYDLKEEYDRV 481
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3261-3299 9.07e-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: 9.07e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 3261 FLEVQYLTGGLIEPDAPGRVPLEEALQRGTVDARTAQKL 3299
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
45-158 1.02e-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: 1.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   45 KKTFTKWVNKHL-----IKHWRAEAQRHiSDLYEDLRDGHNLISLLEVLSGDSLPrERdvirssRLPREKGRMRFHKLQN 119
Cdd:cd21217      3 KEAFVEHINSLLaddpdLKHLLPIDPDG-DDLFEALRDGVLLCKLINKIVPGTID-ER------KLNKKKPKNIFEATEN 74
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1777507490  120 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 158
Cdd:cd21217     75 LNLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
176-278 1.30e-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: 1.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  176 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 254
Cdd:cd21314     11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
                           90       100
                   ....*....|....*....|....
gi 1777507490  255 PEDVDVPQPDEKSIITYVSSLYDA 278
Cdd:cd21314     88 PEEIVDPNVDEHSVMTYLSQFPKA 111
PLEC smart00250
Plectin repeat;
3183-3220 1.37e-09

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 55.57  E-value: 1.37e-09
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507490  3183 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 3220
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1935-1969 4.21e-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: 4.21e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1777507490 1935 QAGTGHIVDPTTSARLTVAEAVRAGLVGPELHEKL 1969
Cdd:pfam00681    5 QAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
171-273 4.82e-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: 4.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  171 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 249
Cdd:cd21315     11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
                           90       100
                   ....*....|....*....|....
gi 1777507490  250 TRLLDPEDVDVPQPDEKSIITYVS 273
Cdd:cd21315     88 PQLIKPEEMVNPKVDELSMMTYLS 111
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
864-1496 9.74e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.61  E-value: 9.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  864 QEAQEAIARLEAQHQALVALWHQLHTDMKSL-LAWQSLSRDVQLIrswslvtfrtlkpEEQRQALRSLELHYQAFLRDSQ 942
Cdd:TIGR02168  347 EELKEELESLEAELEELEAELEELESRLEELeEQLETLRSKVAQL-------------ELQIASLNNEIERLEARLERLE 413
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  943 DAggfgpEDRLQAEREygscsrhyqQLLQSLEQGEQEEsrCQRCISELKDIRLQLEACETRTVHRL------------RL 1010
Cdd:TIGR02168  414 DR-----RERLQQEIE---------ELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALeelreeleeaeqAL 477
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1011 PLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEK----VLALPEPSPAAPTLRSELELTLGKLEQ---VRSLSA 1083
Cdd:TIGR02168  478 DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgiLGVLSELISVDEGYEAAIEAALGGRLQavvVENLNA 557
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1084 I-----YLEK--LKTISLVIRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKAALKKlraqaeAQQPVFDALR--DEL 1154
Cdd:TIGR02168  558 AkkaiaFLKQneLGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRK------ALSYLLGGVLvvDDL 631
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1155 RGAQEVGERLqqRHGERDV----EVERWRERVTQLLERWQAVLAQtdvRQRELEQLGRQLRYYRESADPLDSWLQDAKRR 1230
Cdd:TIGR02168  632 DNALELAKKL--RPGYRIVtldgDLVRPGGVITGGSAKTNSSILE---RRREIEELEEKIEELEEKIAELEKALAELRKE 706
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1231 QEQIQAVPLANSQVVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEP-----VASPAKKPK 1305
Cdd:TIGR02168  707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeelAEAEAEIEE 786
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1306 VQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQEtqaLRQSFLSEKDSLLQRERFIEQ 1385
Cdd:TIGR02168  787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED---LEEQIEELSEDIESLAAEIEE 863
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1386 EKAKLEQLfQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAEEN 1465
Cdd:TIGR02168  864 LEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
                          650       660       670
                   ....*....|....*....|....*....|.
gi 1777507490 1466 QRLRERLQHLEEEhraALAHSEEVPASQATA 1496
Cdd:TIGR02168  943 ERLSEEYSLTLEE---AEALENKIEDDEEEA 970
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
171-278 1.21e-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: 1.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  171 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 249
Cdd:cd21313      3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
                           90       100
                   ....*....|....*....|....*....
gi 1777507490  250 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 278
Cdd:cd21313     80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
180-275 1.41e-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: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  180 KLLL-WSQrMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNL-----------------------EN 235
Cdd:cd21224      3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1777507490  236 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 275
Cdd:cd21224     82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
PLEC smart00250
Plectin repeat;
2914-2950 2.43e-08

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 52.10  E-value: 2.43e-08
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  2914 IRLLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEM 2950
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
39-163 4.80e-08

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: 54.24  E-value: 4.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   39 ERDRVQKKTFTKWVNKHLIkhwraeaQRHISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSSRLPREKGRMRfhKLQ 118
Cdd:cd21331     18 EGETREERTFRNWMNSLGV-------NPHVNHLYGDLQDALVILQLYEKIK---VPVDWNKVNKPPYPKLGANMK--KLE 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1777507490  119 NVQIALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 163
Cdd:cd21331     86 NCNYAVELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
SPEC smart00150
Spectrin repeats;
620-712 8.17e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.72  E-value: 8.17e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   620 HGFVAAATKELMWLSEKEDEEVGFDWSERSTNTAAKKDSYSALMRELELKEKKIKEIQSTGDRLLREDHPARPTVESFQA 699
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90
                    ....*....|...
gi 1777507490   700 ALQTQWSWMLQLC 712
Cdd:smart00150   81 ELNERWEELKELA 93
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
34-160 1.17e-07

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


Pssm-ID: 409148  Cd Length: 114  Bit Score: 52.50  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   34 QDEQDERdrvqkkTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERdvirSSRLPRekgRMR 113
Cdd:cd21299      1 ETSREER------CFRLWINS-------LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKH----ANKPPI---KMP 60
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1777507490  114 FHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 160
Cdd:cd21299     61 FKKVENCNQVVKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3017-3045 3.70e-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: 3.70e-07
                           10        20
                   ....*....|....*....|....*....
gi 1777507490 3017 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 3045
Cdd:pfam00681   11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
864-1500 4.32e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 4.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  864 QEAQEAIARLEAQHQALVALWhqlhtdmksllawqslsrdvqlirswslvtfrtlkpEEQRQALRSLELHYQAflrdsqd 943
Cdd:COG1196    249 EELEAELEELEAELAELEAEL------------------------------------EELRLELEELELELEE------- 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  944 aggfgpedrLQAEreygscsrhYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEAcetrtvhrlrlpldkeparECAQR 1023
Cdd:COG1196    286 ---------AQAE---------EYELLAELARLEQDIARLEERRRELEERLEELEE-------------------ELAEL 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1024 IAEQQKAQAEVEGLGKGVARLSAEAEKVLALpepspAAPTLRSELELTLGKLEQVRSLSAIYLEKLktislvirSTQGAE 1103
Cdd:COG1196    329 EEELEELEEELEELEEELEEAEEELEEAEAE-----LAEAEEALLEAEAELAEAEEELEELAEELL--------EALRAA 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1104 DVLKAHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVT 1183
Cdd:COG1196    396 AELAAQLEELEEAEE------ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1184 QLLERWQAVLAQtdvRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQAVPLAnsQVVREQLRQEKALLEEIE--- 1260
Cdd:COG1196    470 EEAALLEAALAE---LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA--GAVAVLIGVEAAYEAALEaal 544
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1261 --RHGEKVEECQRFAKQYINAIKDYELQLVT-YKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKF 1337
Cdd:COG1196    545 aaALQNIVVEDDEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1338 ISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRERFIEQEKAKLEQLFQEEVAKAQKLReeqqrqqqqmeq 1417
Cdd:COG1196    625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE------------ 692
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1418 ekqqlvASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAEENQRLRERLQHLEEEHRAALAHSEEVPASQATAT 1497
Cdd:COG1196    693 ------LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766

                   ...
gi 1777507490 1498 KAL 1500
Cdd:COG1196    767 REL 769
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
46-157 4.56e-07

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


Pssm-ID: 409135  Cd Length: 105  Bit Score: 50.80  E-value: 4.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   46 KTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLpreRDVirsSRLPREKGRMrfhkLQNVQIALD 125
Cdd:cd21286      3 KIYTDWANHYLAK---SGHKRLIKDLQQDIADGVLLAEIIQIIANEKV---EDI---NGCPRSQSQM----IENVDVCLS 69
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1777507490  126 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTI 157
Cdd:cd21286     70 FLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 101
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
35-161 4.77e-07

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


Pssm-ID: 409071  Cd Length: 121  Bit Score: 51.05  E-value: 4.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   35 DEQDERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRERDVIRSSRLPrekgrmrf 114
Cdd:cd21222      8 DEAPEKLAEVKELLLQFVNKHL-----AKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPLHEYHLTPSTDD-------- 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1777507490  115 HKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 161
Cdd:cd21222     75 EKLHNVKLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
922-1634 5.54e-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: 55.89  E-value: 5.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  922 EQRQALRSLE-----LHYQAFLRDSQDAGGfgPEDRLQAEREYGSCSRHYQQLLQSLEQGEQEESrcqrcISELKDIRL- 995
Cdd:pfam15921  332 ELREAKRMYEdkieeLEKQLVLANSELTEA--RTERDQFSQESGNLDDQLQKLLADLHKREKELS-----LEKEQNKRLw 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  996 QLEACETRTVHRLRLPLDK---EPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVlalpepspaaPTLRSELELTL 1072
Cdd:pfam15921  405 DRDTGNSITIDHLRRELDDrnmEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKV----------SSLTAQLESTK 474
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1073 GKLEQVrslsaiyLEKLKTISLVIRSTQGAEDVLKAHEEQLKEAqavpatlpeLEATKAALKKLRAQAEAQQPVFDALRD 1152
Cdd:pfam15921  475 EMLRKV-------VEELTAKKMTLESSERTVSDLTASLQEKERA---------IEATNAEITKLRSRVDLKLQELQHLKN 538
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1153 E---LRGAQEVGERLQQRHGERDVEVERWR---ERVTQLLERWQ----AVLAQTDVRQRELEQLGRQLRYYRESADPLDS 1222
Cdd:pfam15921  539 EgdhLRNVQTECEALKLQMAEKDKVIEILRqqiENMTQLVGQHGrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDA 618
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1223 WLQD--AKRRQEQIQAVPLANSQvvREQLRQEKALLEEIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVASP 1300
Cdd:pfam15921  619 KIREleARVSDLELEKVKLVNAG--SERLRAVKDIKQERDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETT 693
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1301 AKKPKVQsgsesviqeyvdLRTRYSELTTLTSqyikfiseTLRRMEEEEMQTVQQEQLLQETQALRQ----------SFL 1370
Cdd:pfam15921  694 TNKLKMQ------------LKSAQSELEQTRN--------TLKSMEGSDGHAMKVAMGMQKQITAKRgqidalqskiQFL 753
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1371 SEKDSLLQRER-FIEQEKAKLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQlVASMEEA---------------RRQQR 1434
Cdd:pfam15921  754 EEAMTNANKEKhFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEK-VANMEVAldkaslqfaecqdiiQRQEQ 832
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1435 EAeegVRRKQEELQRLEEQRQQQEKllaeENQRLRERLQHLEEEHRaalAHSeEVPASQATATKALPNGRDAldgPATET 1514
Cdd:pfam15921  833 ES---VRLKLQHTLDVKELQGPGYT----SNSSMKPRLLQPASFTR---THS-NVPSSQSTASFLSHHSRKT---NALKE 898
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1515 EPEHAFDGLRQKV--PAQQLQEVGILSAEELQRLVQG-------RTTVAELEQREDV----RCYLQGRSSIAGLLLqpSN 1581
Cdd:pfam15921  899 DPTRDLKQLLQELrsVINEEPTVQLSKAEDKGRAPSLgalddrvRDCIIESSLRSDIchssSNSLQTEGSKSSETC--SR 976
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1777507490 1582 EKLSVYAALRRQLLS----PGTALILLEAQAASGFLLDPVRNRQLTVNEAVKEGVVG 1634
Cdd:pfam15921  977 EPVLLHAGELEDPSScftfPSTASPSVKNSASRSFHSSPKKSPVHSLLTSSAEGSIG 1033
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
965-1508 5.85e-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: 55.83  E-value: 5.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  965 HYQQLLQSLEQGEQEESRCQRcisELKDIRLQLEACETR-TVHRLRLPLDKEparecaqriaEQQKAQAEVEGLGKGVAR 1043
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEE---ELEELTAELQELEEKlEELRLEVSELEE----------EIEELQKELYALANEISR 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1044 LsaEAEKVLAlpepSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGaedVLKAHEEQLKEAQAvpatl 1123
Cdd:TIGR02168  300 L--EQQKQIL----RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE---ELESLEAELEELEA----- 365
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1124 pELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERwqAVLAQTDVRQREL 1203
Cdd:TIGR02168  366 -ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK--LEEAELKELQAEL 442
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1204 EQLGRQLRYYRESADPLDSWLQDAKRRQEQI-QAVPLANSQVvrEQLRQEKALLEEIERHGEKVEECQRFAK-------- 1274
Cdd:TIGR02168  443 EELEEELEELQEELERLEEALEELREELEEAeQALDAAEREL--AQLQARLDSLERLQENLEGFSEGVKALLknqsglsg 520
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1275 ------QYINAIKDYELQLVTY-------------KAQLEPVASPAKK---------------PKVQSGSESVIQEYVDL 1320
Cdd:TIGR02168  521 ilgvlsELISVDEGYEAAIEAAlggrlqavvvenlNAAKKAIAFLKQNelgrvtflpldsikgTEIQGNDREILKNIEGF 600
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1321 RTRYSELTTLTSQYIK---------FISETL-------RRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRERFIE 1384
Cdd:TIGR02168  601 LGVAKDLVKFDPKLRKalsyllggvLVVDDLdnalelaKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIE 680
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1385 QEKAKLEQLfQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAEE 1464
Cdd:TIGR02168  681 ELEEKIEEL-EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*..
gi 1777507490 1465 NQR---LRERLQHLEEEHRAALAHSEEVPASQATATKALPNGRDALD 1508
Cdd:TIGR02168  760 EAEieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
PLEC smart00250
Plectin repeat;
2336-2372 7.12e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 47.86  E-value: 7.12e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  2336 IRLLEAQIATGGIIDPVHSHRLPVDVAFQRGYFDEEM 2372
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
1677-1713 1.74e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.71  E-value: 1.74e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  1677 IRLLEAQIATGGIIDPVHSHRVPVDVAFQRGYFDEEM 1713
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1014-1394 2.00e-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: 53.91  E-value: 2.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1014 KEPARECAQRIAEQQKAQAEVEG----LGKGVARLSAEAEKVLALPEpspaaptLRSELE-----LTLGKLEQVRslsai 1084
Cdd:TIGR02168  171 KERRKETERKLERTRENLDRLEDilneLERQLKSLERQAEKAERYKE-------LKAELRelelaLLVLRLEELR----- 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1085 ylEKLKTISLVIRStqgAEDVLKAHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERL 1164
Cdd:TIGR02168  239 --EELEELQEELKE---AEEELEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL 307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1165 QQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQAVPLANSQV 1244
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1245 VREQLRQEKALLEEIERhgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRY 1324
Cdd:TIGR02168  388 VAQLELQIASLNNEIER-----------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1325 SELTTLTSQyikfISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRERFIEQEKAKLEQLF 1394
Cdd:TIGR02168  457 ERLEEALEE----LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGIL 522
PLEC smart00250
Plectin repeat;
2800-2837 2.13e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.71  E-value: 2.13e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507490  2800 QKFLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTA 2837
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2005-2041 2.33e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.32  E-value: 2.33e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  2005 LRLLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDEET 2041
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
171-278 2.68e-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: 49.03  E-value: 2.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  171 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 249
Cdd:cd21312      7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
                           90       100
                   ....*....|....*....|....*....
gi 1777507490  250 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 278
Cdd:cd21312     84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
PLEC smart00250
Plectin repeat;
2595-2630 2.75e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.32  E-value: 2.75e-06
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1777507490  2595 RLLLEAQAATGFLLDPVKGDRLTVDEAVRKGLVGPE 2630
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2802-2840 3.32e-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: 3.32e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2802 FLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTAFEL 2840
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1125-1327 4.54e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 4.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1125 ELEATKAALKKLRAQAEAQQPV------FDALRDELRGAQEVGERLQQRHGERdvEVERWRERVTQLLERWQAVLAQTDV 1198
Cdd:COG4913    236 DLERAHEALEDAREQIELLEPIrelaerYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELER 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1199 RQRELEQLGRQLRyyresadpldswlqdakRRQEQIQAVplansqvvreQLRQEKALLEEIERHGEKVEECQRFAKQYIN 1278
Cdd:COG4913    314 LEARLDALREELD-----------------ELEAQIRGN----------GGDRLEQLEREIERLERELEERERRRARLEA 366
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1777507490 1279 AIKDYELQLVTYKAQLEPVASPAK--KPKVQSGSESVIQEYVDLRTRYSEL 1327
Cdd:COG4913    367 LLAALGLPLPASAEEFAALRAEAAalLEALEEELEALEEALAEAEAALRDL 417
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1123-1482 5.19e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 5.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1123 LPELEATKAALKKLRAQAEAqqpvFDALRDELRGAQEVGERLQQRHGERDVEVERWR--ERVTQLLERWQAVLAQTDVRQ 1200
Cdd:COG4717     70 LKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELP 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1201 RELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQAVPLANSQVVREQLRQekaLLEEIERHGEKVEECQRFAKQYINAI 1280
Cdd:COG4717    146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAELEEELEEAQEEL 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1281 KDYELQLVTYKAQLEPVASPAK--KPKVQSGSESVI-------QEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQ 1351
Cdd:COG4717    223 EELEEELEQLENELEAAALEERlkEARLLLLIAAALlallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1352 TVQQEQLLQETQALRQ----SFLSEKD-SLLQRERFIEQEKAKLEQLFQ--EEVAKAQKLREEQQRQQQQMEQEKQQLVA 1424
Cdd:COG4717    303 EAEELQALPALEELEEeeleELLAALGlPPDLSPEELLELLDRIEELQEllREAEELEEELQLEELEQEIAALLAEAGVE 382
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1777507490 1425 SMEEARRQQREAEEGV----RRKQEELQRLEEQRQQQEKLLAEENQRLRERLQHLEEEHRAA 1482
Cdd:COG4717    383 DEEELRAALEQAEEYQelkeELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEEL 444
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1106-1479 5.68e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 5.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1106 LKAHEEQLKEAQAVPATL-PELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQ 1184
Cdd:TIGR02168  686 IEELEEKIAELEKALAELrKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1185 LLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLDSWLqDAKRRQEQIQAVPLANSQVVREQLRQEKALLE-EIERHG 1263
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL-DELRAELTLLNEEAANLRERLESLERRIAATErRLEDLE 844
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1264 EKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSELttltsqyikfiSETLR 1343
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELE---------ALLNERASLEEALALLRSELEEL-----------SEELR 904
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1344 RMEEEemqtvqqeqllqeTQALRQSfLSEKDSLLqrerfiEQEKAKLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQLV 1423
Cdd:TIGR02168  905 ELESK-------------RSELRRE-LEELREKL------AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1777507490 1424 ASMEEARRQQREAEEGVRRkqeelqrleeqrQQQEKLLA-EENQRLRERLQHLEEEH 1479
Cdd:TIGR02168  965 DDEEEARRRLKRLENKIKE------------LGPVNLAAiEEYEELKERYDFLTAQK 1009
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1083-1283 7.86e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.22  E-value: 7.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1083 AIYLEKLKTISLVIRSTQGAEDVLKAHEEQLKEAQAVPATL----------PELEATKAALKKLRAQAEAQQPVFDALRD 1152
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeidvASAEREIAELEAELERLDASSDDLAALEE 692
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1153 ELRGAQEVGERLQQRHGERDVEVERWRERVTQLlerwqavlaqtdvrQRELEQLGRQLRYYRESADPLDSWLQDAKRRQE 1232
Cdd:COG4913    693 QLEELEAELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLELRALLEERFAAA 758
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1777507490 1233 QIQAVPlansQVVREQLRQE-KALLEEIERHGEKVEEC-QRFAKQYINAIKDY 1283
Cdd:COG4913    759 LGDAVE----RELRENLEERiDALRARLNRAEEELERAmRAFNREWPAETADL 807
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
921-1479 9.56e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 9.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  921 EEQRQALRSLELHYQAFLRDSQDAGgfgpEDRLQAEREygscSRHYQQLLQSLEQGEQEESRcqrcisELKDIRLQLEAC 1000
Cdd:COG1196    270 EELRLELEELELELEEAQAEEYELL----AELARLEQD----IARLEERRRELEERLEELEE------ELAELEEELEEL 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1001 ETRTVHRLRLPLDKEPARECAQ--RIAEQQKAQAEVEGLGKGVARLSAEAEKVLALpepSPAAPTLRSELELTLGKLEQV 1078
Cdd:COG1196    336 EEELEELEEELEEAEEELEEAEaeLAEAEEALLEAEAELAEAEEELEELAEELLEA---LRAAAELAAQLEELEEAEEAL 412
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1079 RSLSAIYLEKLKTISLVIRSTQGAEDVLKAHEEQLKEAQAvpATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQ 1158
Cdd:COG1196    413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA--ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1159 EVGERLQQRHGERDVEVERWRE--------RVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLDSWLQDAKRR 1230
Cdd:COG1196    491 ARLLLLLEAEADYEGFLEGVKAalllaglrGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAK 570
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1231 QEQIQAVPLANSQVVREQLRQEKALLEEIERHGEKVEECQRFAKQYinAIKDYELQLVTYKAQLEPVASPAKKpkVQSGS 1310
Cdd:COG1196    571 AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY--VLGDTLLGRTLVAARLEAALRRAVT--LAGRL 646
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1311 ESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRERFIEQEKAKL 1390
Cdd:COG1196    647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1391 EQLFQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEgvrrkqeelqrleeqrqqqeK--------LLA 1462
Cdd:COG1196    727 EEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER--------------------EiealgpvnLLA 786
                          570
                   ....*....|....*...
gi 1777507490 1463 -EENQRLRERLQHLEEEH 1479
Cdd:COG1196    787 iEEYEELEERYDFLSEQR 804
PLEC smart00250
Plectin repeat;
2224-2259 1.30e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.30e-05
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1777507490  2224 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTA 2259
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2671-2708 1.32e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.32e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507490  2671 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTY 2708
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3010-3038 1.42e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.42e-05
                            10        20
                    ....*....|....*....|....*....
gi 1777507490  3010 VRKRRVVIVDPETGKEMSVYEAYRKGLID 3038
Cdd:smart00250    6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
PTZ00121 PTZ00121
MAEBL; Provisional
919-1494 1.47e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  919 KPEEQRQAL---RSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSR-----HYQQLLQSLEQGEQ-EESRCQRCISE 989
Cdd:PTZ00121  1177 KAEAARKAEevrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKaeavkKAEEAKKDAEEAKKaEEERNNEEIRK 1256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  990 LKDIRLQ--------LEACETRTVHRLRLPLDKEPARECAQ----RIAEQQKAQAE----VEGLGKGV--ARLSAEAEKV 1051
Cdd:PTZ00121  1257 FEEARMAhfarrqaaIKAEEARKADELKKAEEKKKADEAKKaeekKKADEAKKKAEeakkADEAKKKAeeAKKKADAAKK 1336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1052 LAlPEPSPAAPTLRSELELTLGKLEQVRslsaiylEKLKTISLVIRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKA 1131
Cdd:PTZ00121  1337 KA-EEAKKAAEAAKAEAEAAADEAEAAE-------EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1132 ALKKlraqAEAQQPVFDALR---DELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQlgr 1208
Cdd:PTZ00121  1409 ELKK----AAAAKKKADEAKkkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE--- 1481
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1209 qlryyRESADPLDSWLQDAKRRQEQIQAVPLANSQVVREQLRQEKALLEEIERHGE--KVEEcqrfAKQYINAIKDYELQ 1286
Cdd:PTZ00121  1482 -----AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakKADE----AKKAEEKKKADELK 1552
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1287 LVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLR----TRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQET 1362
Cdd:PTZ00121  1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1363 QALRQSFLSEKDSLLQRERFIEQE------KAKLEQLFQEEVAKAQKLReeqqRQQQQMEQEKQQLVASMEEARR--QQR 1434
Cdd:PTZ00121  1633 KKVEQLKKKEAEEKKKAEELKKAEeenkikAAEEAKKAEEDKKKAEEAK----KAEEDEKKAAEALKKEAEEAKKaeELK 1708
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1777507490 1435 EAEEGVRRKQEE---LQRLEEQRQQQEKLLAEENQRLRERLQhLEEEHRAALAHSEEVPASQA 1494
Cdd:PTZ00121  1709 KKEAEEKKKAEElkkAEEENKIKAEEAKKEAEEDKKKAEEAK-KDEEEKKKIAHLKKEEEKKA 1770
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
951-1268 1.55e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 1.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  951 DRLQAEREYgscSRHYQQLLQSLEQGEQEESrcqrcISELKDIRLQLEACEtrtvhrlrlpldkepaRECAQRIAEQQKA 1030
Cdd:TIGR02169  201 ERLRREREK---AERYQALLKEKREYEGYEL-----LKEKEALERQKEAIE----------------RQLASLEEELEKL 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1031 QAEVEGLGKGVA----RLSAEAEKVLALPEPSPAAptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEDVL 1106
Cdd:TIGR02169  257 TEEISELEKRLEeieqLLEELNKKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1107 KAHEEQLKEAQA-----VPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGE----------- 1170
Cdd:TIGR02169  335 LAEIEELEREIEeerkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINElkreldrlqee 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1171 ---RDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLryyRESADPLDSWLQDAKRRQEQIQAVPLANSQVVRE 1247
Cdd:TIGR02169  415 lqrLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL---EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
                          330       340
                   ....*....|....*....|...
gi 1777507490 1248 --QLRQEKALLEEIERHGEKVEE 1268
Cdd:TIGR02169  492 laEAEAQARASEERVRGGRAVEE 514
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2224-2262 1.56e-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: 1.56e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2224 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTATLL 2262
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
71-158 1.83e-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: 46.67  E-value: 1.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   71 LYEDLRDGHNLISLLEvlsgDSLPRERDVIRSSRLPRE-KGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKL 149
Cdd:cd21294     38 LFDECKDGLVLSKLIN----DSVPDTIDERVLNKPPRKnKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHL 113

                   ....*....
gi 1777507490  150 TLGLIWTII 158
Cdd:cd21294    114 ILGLIWQII 122
PTZ00121 PTZ00121
MAEBL; Provisional
1014-1443 1.97e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 1.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1014 KEPARECAQRIAEQQKAQAEveglGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTlGKLEQVRSLSAIYlEKLKTIS 1093
Cdd:PTZ00121  1397 KKKAEEDKKKADELKKAAAA----KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK-KKAEEAKKAEEAK-KKAEEAK 1470
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1094 LVIRSTQGAEDVLKAhEEQLKEAQAVPATLPELEATKAALKK---LRAQAEAQQPvfDALR--------DELRGAQEVGE 1162
Cdd:PTZ00121  1471 KADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAAEAKKKadeAKKAEEAKKA--DEAKkaeeakkaDEAKKAEEKKK 1547
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1163 RLQQRHGE--RDVEVERWRERVTQLLERWQAVLAQTDV-RQRELEQLGRQLRYYRESADPLDSWLQdaKRRQEQIQAvpl 1239
Cdd:PTZ00121  1548 ADELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEaKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEAKIKA--- 1622
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1240 ansqvvrEQLRQEKALLEEIERHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAKKPkvqsgSESVIQEYVD 1319
Cdd:PTZ00121  1623 -------EELKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKK-----AEEAKKAEED 1686
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1320 LRTRYSELTTLTSQYIKfiSETLRRMEEEEMQTVQQeqllqetqaLRQSFLSEKDSLLQRERFIEQEKAKLEQLFQEEVA 1399
Cdd:PTZ00121  1687 EKKAAEALKKEAEEAKK--AEELKKKEAEEKKKAEE---------LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 1777507490 1400 KAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRK 1443
Cdd:PTZ00121  1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1565-1603 2.06e-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: 2.06e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 1565 YLQGRSSIAGLLLQPSNEKLSVYAALRRQLLSPGTALIL 1603
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC smart00150
Spectrin repeats;
523-617 2.48e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.78  E-value: 2.48e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   523 LRYLQDLLAWVGENQRRVDSAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARTDEGQL---SPATRGAYRDCLGRLD 599
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
                            90
                    ....*....|....*...
gi 1777507490   600 LQYAKLLNSSKARLRSLE 617
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
2558-2594 3.26e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.26e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  2558 RYLYGTGCVAGVYLPGSRQTLTVYQALKKGLLSAEVA 2594
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PTZ00121 PTZ00121
MAEBL; Provisional
978-1561 3.95e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 3.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  978 QEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPAR--ECAQRIAEQQKAQaeveglgkgVARLSAEAEKVlalp 1055
Cdd:PTZ00121  1112 EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKrvEIARKAEDARKAE---------EARKAEDAKKA---- 1178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1056 EPSPAAPTLRSELELTlgKLEQVRSL-SAIYLEKLKTISLVIRSTQG--AEDVLKAHEEQLKEAQAVPA----TLPELEA 1128
Cdd:PTZ00121  1179 EAARKAEEVRKAEELR--KAEDARKAeAARKAEEERKAEEARKAEDAkkAEAVKKAEEAKKDAEEAKKAeeerNNEEIRK 1256
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1129 TKAALKKLRAQAEAQQPVFDALR-DELRGAQEV--GERLQQRHGERDVE------------------VERWRERVTQLLE 1187
Cdd:PTZ00121  1257 FEEARMAHFARRQAAIKAEEARKaDELKKAEEKkkADEAKKAEEKKKADeakkkaeeakkadeakkkAEEAKKKADAAKK 1336
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1188 RWQAVLAQTDVRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQ--AVPLANSQVVREQLRQEKALLEEIERHGE- 1264
Cdd:PTZ00121  1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkAEEKKKADEAKKKAEEDKKKADELKKAAAa 1416
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1265 --KVEECQRFA----------KQYINAIKDYELQlvtYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTlTS 1332
Cdd:PTZ00121  1417 kkKADEAKKKAeekkkadeakKKAEEAKKADEAK---KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKK-KA 1492
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1333 QYIKFISETLRRMEEEEMQTVQQEQLLQETQA--LRQSFLSEK-------------DSLLQRERFIE-QEKAKLEQLFQE 1396
Cdd:PTZ00121  1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdeAKKAEEAKKadeakkaeekkkaDELKKAEELKKaEEKKKAEEAKKA 1572
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1397 EVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREA--EEGVRRKQEELQRLEEQ--RQQQEKLLAEENQRLRERL 1472
Cdd:PTZ00121  1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELKKAEEEkkKVEQLKKKEAEEKKKAEEL 1652
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1473 QHLEEEHR---AALAHSEEVPASQA-TATKALPNGRDALDGPATETEPEHAFDGLRQKVP-----AQQL---QEVGILSA 1540
Cdd:PTZ00121  1653 KKAEEENKikaAEEAKKAEEDKKKAeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAeekkkAEELkkaEEENKIKA 1732
                          650       660
                   ....*....|....*....|.
gi 1777507490 1541 EELQRLVQGRTTVAELEQRED 1561
Cdd:PTZ00121  1733 EEAKKEAEEDKKKAEEAKKDE 1753
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
44-168 4.03e-05

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: 46.19  E-value: 4.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   44 QKKTFTKWVNKHL-----IKHWRAEAQRHISdLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRLPrekgrmrFHKLQ 118
Cdd:cd21323     25 EKVAFVNWINKALegdpdCKHVVPMNPTDES-LFKSLADGILLCKMINLSQPDTID-ERAINKKKLTP-------FTISE 95
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1777507490  119 NVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 168
Cdd:cd21323     96 NLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
39-164 4.29e-05

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: 45.36  E-value: 4.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   39 ERDRVQKKTFTKWVNKHLIKHWraeaqrhISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSSRLPREKGRMRfhKLQ 118
Cdd:cd21329      2 EGESSEERTFRNWMNSLGVNPY-------VNHLYSDLCDALVIFQLYEMTR---VPVDWGHVNKPPYPALGGNMK--KIE 69
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1777507490  119 NVQIALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 164
Cdd:cd21329     70 NCNYAVELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
PLEC smart00250
Plectin repeat;
2840-2874 4.47e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.85  E-value: 4.47e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1777507490  2840 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 2874
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
2299-2335 5.94e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 5.94e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  2299 KLLSAEKAVTGYKDPYTGEQISLFQAMKKGLVLREHG 2335
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
44-169 5.96e-05

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


Pssm-ID: 409174  Cd Length: 148  Bit Score: 45.82  E-value: 5.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   44 QKKTFTKWVNKHLIKHWRAeaqRHI-------SDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRLPrekgrmrFHK 116
Cdd:cd21325     25 EKYAFVNWINKALENDPDC---RHVipmnpntDDLFKAVGDGIVLCKMINLSVPDTID-ERAINKKKLTP-------FII 93
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1777507490  117 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 169
Cdd:cd21325     94 QENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
PLEC smart00250
Plectin repeat;
3149-3182 6.36e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 6.36e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1777507490  3149 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 3182
Cdd:smart00250    5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
SPEC smart00150
Spectrin repeats;
1111-1204 8.63e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 44.24  E-value: 8.63e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  1111 EQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALrdelrgaQEVGERLQQRHGERDVEVErwrERVTQLLERWQ 1190
Cdd:smart00150   18 EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEAL-------NELGEQLIEEGHPDAEEIE---ERLEELNERWE 87
                            90
                    ....*....|....
gi 1777507490  1191 AVLAQTDVRQRELE 1204
Cdd:smart00150   88 ELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1024-1205 9.25e-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: 46.67  E-value: 9.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1024 IAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAE 1103
Cdd:cd00176     39 LKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1104 DVLKAHEEQLKEAQA--VPATLPELEATKAALKKLRAQAEAQQPVFDALRDElrgaqevGERLQQRHGERDVEVERwrER 1181
Cdd:cd00176    117 DLEQWLEEKEAALASedLGKDLESVEELLKKHKELEEELEAHEPRLKSLNEL-------AEELLEEGHPDADEEIE--EK 187
                          170       180
                   ....*....|....*....|....
gi 1777507490 1182 VTQLLERWQAVLAQTDVRQRELEQ 1205
Cdd:cd00176    188 LEELNERWEELLELAEERQKKLEE 211
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
864-1226 9.45e-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: 9.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  864 QEAQEAIARLEAQHQALVALWHQLHTDMKSLLAWQSLSRDVQ-LIRSWSLVTFRTLKPEEQRQALRSLELHYQAFLRDSQ 942
Cdd:COG4913    606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERReALQRLAEYSWDEIDVASAEREIAELEAELERLDASSD 685
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  943 DAGGFgpEDRL-QAEREYGSCSRHYQQLLQSLEQGEQEESRCQRcisELKDIRLQLEACETRTVHRLRLPLDKEPARECA 1021
Cdd:COG4913    686 DLAAL--EEQLeELEAELEELEEELDELKGEIGRLEKELEQAEE---ELDELQDRLEAAEDLARLELRALLEERFAAALG 760
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1022 QRIAEQ--QKAQAEVEGLGKGVARLSAEAEKVLAlpEPSPAAPTLRSELELTLGKLEQvrslsaiYLEKLKTIslvirst 1099
Cdd:COG4913    761 DAVERElrENLEERIDALRARLNRAEEELERAMR--AFNREWPAETADLDADLESLPE-------YLALLDRL------- 824
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1100 qgAEDVLKAHEEQLKEAQAVpATLPELEATKAALKKLRAQAEAQqpvFDALRDELRGAQ-EVGERLQQR-HGERDVEVER 1177
Cdd:COG4913    825 --EEDGLPEYEERFKELLNE-NSIEFVADLLSKLRRAIREIKER---IDPLNDSLKRIPfGPGRYLRLEaRPRPDPEVRE 898
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1178 WRERVTQLLER-WQAVLAQTDVRQRELEQLGRQLRyyRESADPLDSWLQD 1226
Cdd:COG4913    899 FRQELRAVTSGaSLFDEELSEARFAALKRLIERLR--SEEEESDRRWRAR 946
PLEC smart00250
Plectin repeat;
1968-2004 1.16e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.70  E-value: 1.16e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  1968 KLLLAERAVTGYKDPYSGQSVSLFQALKKGLIPREQG 2004
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PTZ00121 PTZ00121
MAEBL; Provisional
1096-1563 1.30e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1096 IRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQ----AEAQQPVFDALR-DELRGAQEVGERLQQRHGE 1170
Cdd:PTZ00121  1130 AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEdakkAEAARKAEEVRKaEELRKAEDARKAEAARKAE 1209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1171 RDVEVERWR----ERVTQLLERWQAVLAQTD-VRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQAVPLANSQVV 1245
Cdd:PTZ00121  1210 EERKAEEARkaedAKKAEAVKKAEEAKKDAEeAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK 1289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1246 R--EQLR--QEKALLEEIERHGE---KVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYV 1318
Cdd:PTZ00121  1290 KkaDEAKkaEEKKKADEAKKKAEeakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1319 DLRT----RYSELTTLTSQYIKFISETLRRMEE-----EEMQTVQQEQLLQETQALRQSFLSEKDSLLQRErfieQEKAK 1389
Cdd:PTZ00121  1370 EKKKeeakKKADAAKKKAEEKKKADEAKKKAEEdkkkaDELKKAAAAKKKADEAKKKAEEKKKADEAKKKA----EEAKK 1445
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1390 LEQLFQ--EEVAKAQKLREEQQRQQQQMEqekqqLVASMEEARRQ---QREAEEGvRRKQEELQRLEEQRQQQEKLLAEE 1464
Cdd:PTZ00121  1446 ADEAKKkaEEAKKAEEAKKKAEEAKKADE-----AKKKAEEAKKAdeaKKKAEEA-KKKADEAKKAAEAKKKADEAKKAE 1519
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1465 NQRLRERLQHLEEEHRA-ALAHSEEV-PASQATATKALPNGRDALDGPATETEPEHAFDGLRQKVPAQQLQEVGI----- 1537
Cdd:PTZ00121  1520 EAKKADEAKKAEEAKKAdEAKKAEEKkKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIeevmk 1599
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1777507490 1538 -------LSAEELQRLVQGRTTVAELEQREDVR 1563
Cdd:PTZ00121  1600 lyeeekkMKAEEAKKAEEAKIKAEELKKAEEEK 1632
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
41-157 1.38e-04

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: 44.18  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   41 DRVQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLpreRDVirsSRLPREKGRMrfhkLQNV 120
Cdd:cd21285      8 NGFDKQIYTDWANHYLAK---SGHKRLIKDLQQDVTDGVLLAEIIQVVANEKI---EDI---NGCPKNRSQM----IENI 74
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1777507490  121 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTI 157
Cdd:cd21285     75 DACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
198-275 1.47e-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: 1.47e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777507490  198 DNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 275
Cdd:cd21185     20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
PLEC smart00250
Plectin repeat;
2260-2295 1.65e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.65e-04
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1777507490  2260 TLLLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPE 2295
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
PLEC smart00250
Plectin repeat;
2634-2670 1.78e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.78e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  2634 RLLSAERAVTGYRDPYTEQTISLFQAMKKDLIPAEEA 2670
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3259-3296 2.13e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.93  E-value: 2.13e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507490  3259 QRFLEVQYLTGGLIEPDAPGRVPLEEALQRGTVDARTA 3296
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
956-1261 2.14e-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: 2.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  956 EREYGSCSRHYQQLLQSLEQGEQEEsRCQRCISELK-DIRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQ----QKA 1030
Cdd:COG3096    326 EQDYQAASDHLNLVQTALRQQEKIE-RYQEDLEELTeRLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQladyQQA 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1031 -----------QAEVEGLGKgvarlsaeAEKVLALPEPSPAA-----PTLRSELEL---TLGKLEQVRSLSAIYLEKLKT 1091
Cdd:COG3096    405 ldvqqtraiqyQQAVQALEK--------ARALCGLPDLTPENaedylAAFRAKEQQateEVLELEQKLSVADAARRQFEK 476
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1092 ISLVIRSTQGAEDVLKAHEEqlkeAQAVPATLPELEATKAALKKLRAQ-AEAQQpvfdaLRDELRGAQEVGERLQQRHG- 1169
Cdd:COG3096    477 AYELVCKIAGEVERSQAWQT----ARELLRRYRSQQALAQRLQQLRAQlAELEQ-----RLRQQQNAERLLEEFCQRIGq 547
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1170 ------ERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdPLdsWL--QDAKRRQEQIQAVPLAN 1241
Cdd:COG3096    548 qldaaeELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARA-PA--WLaaQDALERLREQSGEALAD 624
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1777507490 1242 SQVV-----------------REQLRQEKALLE-EIER 1261
Cdd:COG3096    625 SQEVtaamqqllerereatveRDELAARKQALEsQIER 662
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
955-1268 2.23e-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: 47.37  E-value: 2.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  955 AEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEA----------CETRTVHRLRLPLDKEPARECAQRI 1024
Cdd:TIGR02169  714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSelkelearieELEEDLHKLEEALNDLEARLSHSRI 793
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1025 aeqQKAQAEVEGLGKGVARLSAEAEkvlalpepspaaptlrsELELTLGKLEQVRSlsaiYLEKLKtislvirstQGAED 1104
Cdd:TIGR02169  794 ---PEIQAELSKLEEEVSRIEARLR-----------------EIEQKLNRLTLEKE----YLEKEI---------QELQE 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1105 VLKAHEEQLKE-AQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVT 1183
Cdd:TIGR02169  841 QRIDLKEQIKSiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1184 QLLERWQAVLAQTDvrqrELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQAVPLANSQVVREQLRQEKALLEEIERHg 1263
Cdd:TIGR02169  921 ELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKR- 995

                   ....*
gi 1777507490 1264 EKVEE 1268
Cdd:TIGR02169  996 AKLEE 1000
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
44-168 2.69e-04

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


Pssm-ID: 409173  Cd Length: 145  Bit Score: 43.84  E-value: 2.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   44 QKKTFTKWVNKHLIKHWRAeaqRHI-------SDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRLPrekgrmrFHK 116
Cdd:cd21324     25 EKYAFVNWINKALENDPDC---KHVipmnpntDDLFKAVGDGIVLCKMINFSVPDTID-ERTINKKKLTP-------FTI 93
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1777507490  117 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 168
Cdd:cd21324     94 QENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
921-1267 2.81e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 2.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  921 EEQRQALRSLELHYQAFLRDSQDAGGFGP--EDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLE 998
Cdd:COG4717    101 EEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE 180
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  999 ACETRTvhrlrLPLDKEPARECAQRIAEQQKAQAEVEglgKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQV 1078
Cdd:COG4717    181 ELLEQL-----SLATEEELQDLAEELEELQQRLAELE---EELEEAQEELEE-------------LEEELEQLENELEAA 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1079 RSLSAIYLEKLKTISL-VIRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRgA 1157
Cdd:COG4717    240 ALEERLKEARLLLLIAaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE-E 318
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1158 QEVGERLQQRHGERDVEVERWRERVtQLLERWQAVLAQTDVRQRELEQLGRQLRYYR-------ESADPLDSWLQDAKRR 1230
Cdd:COG4717    319 EELEELLAALGLPPDLSPEELLELL-DRIEELQELLREAEELEEELQLEELEQEIAAllaeagvEDEEELRAALEQAEEY 397
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1777507490 1231 QEQIQAVplansQVVREQLRQEKALLEEIERHGEKVE 1267
Cdd:COG4717    398 QELKEEL-----EELEEQLEELLGELEELLEALDEEE 429
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2559-2597 3.01e-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: 3.01e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1777507490 2559 YLYGTGCVAGVYLPGSRQTLTVYQALKKGLLSAEVARLL 2597
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
1603-1636 3.48e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.54  E-value: 3.48e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1777507490  1603 LLEAQAASGFLLDPVRNRQLTVNEAVKEGVVGPE 1636
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
39-164 4.09e-04

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


Pssm-ID: 409179  Cd Length: 125  Bit Score: 43.05  E-value: 4.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   39 ERDRVQKKTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSgdsLPRERDVIRSSRLPREKGRMRfhKLQ 118
Cdd:cd21330      9 EGETREERTFRNWMNS-------LGVNPRVNHLYSDLSDALVIFQLYEKIK---VPVDWNRVNKPPYPKLGENMK--KLE 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1777507490  119 NVQIALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 164
Cdd:cd21330     77 NCNYAVELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
PLEC smart00250
Plectin repeat;
1640-1676 4.28e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.16  E-value: 4.28e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1777507490  1640 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVREHG 1676
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1180-1613 5.30e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 5.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1180 ERVTQLLERWQAVLAQtdVRQReLEQLGRQ----LRY--YRESADPLDSWL-----QDAKRRQEQIQAVpLANSQVVREQ 1248
Cdd:COG1196    182 EATEENLERLEDILGE--LERQ-LEPLERQaekaERYreLKEELKELEAELlllklRELEAELEELEAE-LEELEAELEE 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1249 LRQEKALLE-EIERHGEKVEEcqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKkpkvqsgsESVIQEYVDLRTRYSEL 1327
Cdd:COG1196    258 LEAELAELEaELEELRLELEE----LELELEEAQAEEYELLAELARLEQDIARLE--------ERRRELEERLEELEEEL 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1328 TTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRERFIEQEKAKLEQLFQEEVAKAQKLREE 1407
Cdd:COG1196    326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1408 QQRQQQQMEQEKQQLVA-SMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAEENQRLRERLQHLEEEHRAALAHS 1486
Cdd:COG1196    406 EEAEEALLERLERLEEElEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1487 EEVPASQATATKALPNGRDALDGPATETEPEHAFDGLRQKVPAQQ-----LQEVGILSAEELQRLVQGRTTVAELEQRED 1561
Cdd:COG1196    486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveaaYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1777507490 1562 VRCYLQGRSSIAGLLLQPSNEKLSvyAALRRQLLSPGTALILLEAQAASGFL 1613
Cdd:COG1196    566 LKAAKAGRATFLPLDKIRARAALA--AALARGAIGAAVDLVASDLREADARY 615
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1183-1489 7.63e-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: 7.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1183 TQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQAvplaNSQVVREQLRQEKALLEEIERH 1262
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK----EIEQLEQEEEKLKERLEELEED 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1263 ----GEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVA---SPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyi 1335
Cdd:TIGR02169  746 lsslEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-- 823
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1336 kfiSETLRRMEEEEMQTvqqeqllqetqaLRQSFLSEKDSLLQRERFIEQEKAKLEQLfQEEVAKAQKLREEQQRQQQQM 1415
Cdd:TIGR02169  824 ---LTLEKEYLEKEIQE------------LQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDL 887
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1416 EQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLLAE-----------------------ENQRLRERL 1472
Cdd:TIGR02169  888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedpkgedeeipeeelsledvqaELQRVEEEI 967
                          330
                   ....*....|....*..
gi 1777507490 1473 QHLEEEHRAALAHSEEV 1489
Cdd:TIGR02169  968 RALEPVNMLAIQEYEEV 984
PLEC smart00250
Plectin repeat;
1891-1923 9.49e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.00  E-value: 9.49e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1777507490  1891 RRALRGSSVIAGVWLEEAGQKLSIYEALRKDLL 1923
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1067-1561 1.17e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.03  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1067 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQG-AEDVLKAHEEQLKEAQAVPATLPELEATKAALKKLRaqaeaqqp 1145
Cdd:PRK02224   203 DLHERLNGLESELAELDEEIERYEEQREQARETRDeADEVLEEHEERREELETLEAEIEDLRETIAETERER-------- 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1146 vfDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLdswLQ 1225
Cdd:PRK02224   275 --EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL---RE 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1226 DAKRRQEQiqavplansqvvREQLRQEKALLE-EIERHGEKVEECQrfakqyiNAIKDYELQLVTYKAQLEpvASPAKKP 1304
Cdd:PRK02224   350 DADDLEER------------AEELREEAAELEsELEEAREAVEDRR-------EEIEELEEEIEELRERFG--DAPVDLG 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1305 KVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEE----EEMQTVQQEqllqetqalrqsflSEKDSLLQRE 1380
Cdd:PRK02224   409 NAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpECGQPVEGS--------------PHVETIEEDR 474
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1381 RFIEQEKAKLEQLFQEEVAKAQKLreeqqrqqqqmeqekqqlvASMEEARRQQREAEEgvrrkqeelqrLEEQRQQQEKL 1460
Cdd:PRK02224   475 ERVEELEAELEDLEEEVEEVEERL-------------------ERAEDLVEAEDRIER-----------LEERREDLEEL 524
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1461 LAEENQRLRERLQHLEEEHRAALAHSEEVPASQATATKALPNGRDALDGPAT----ETEPEHAFDGLRQKVPAQQLQEVg 1536
Cdd:PRK02224   525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAElnskLAELKERIESLERIRTLLAAIAD- 603
                          490       500
                   ....*....|....*....|....*.
gi 1777507490 1537 ilSAEELQRLVQGRTTVAELE-QRED 1561
Cdd:PRK02224   604 --AEDEIERLREKREALAELNdERRE 627
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
36-275 1.29e-03

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 44.55  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   36 EQDERDRVQKKTFTKWVNKHLIKHwraeaqrHISDLYEDLRDGhnlISLLEVLSGDSLPRERDVIRSSRLPREKGRM-RF 114
Cdd:COG5069    372 EFDAEGEFEARVFTFWLNSLDVSP-------EITNLFGDLRDQ---LILLQALSKKLMPMTVTHKLVKKQPASGIEEnRF 441
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  115 HKLQNVQIALDYLRHRQVKLVNIRNDDIADGNpKLTLGLIW-------TIILHFQISDiqvsgqsEDMTAKEKLLLWSQR 187
Cdd:COG5069    442 KAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKD-------GCGLSDSDLCAWLGS 513
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  188 MVEGY---QGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVyRQTNLENLDQA-------FSVAERDLGVTRLLDPED 257
Cdd:COG5069    514 LGLKGdkeEGIRSFGDPAGSVSGVFYLDVLKGIHSELVDYDLV-TRGFTEFDDIAdarslaiSSKILRSLGAIIKFLPED 592
                          250
                   ....*....|....*...
gi 1777507490  258 VDVPQPdEKSIITYVSSL 275
Cdd:COG5069    593 INGVRP-RLDVLTFIESL 609
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
989-1230 1.34e-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: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  989 ELKDIRLQLEAcETRTVHRLrlpldkEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpepSPAAPTLRSEL 1068
Cdd:COG4913    236 DLERAHEALED-AREQIELL------EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL----EAELEELRAEL 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1069 ELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEdvlkahEEQLKEaqavpatlpELEATKAALKKLRAQAEAQQPVFD 1148
Cdd:COG4913    305 ARLEAELERLEARLDALREELDELEAQIRGNGGDR------LEQLER---------EIERLERELEERERRRARLEALLA 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1149 ALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQllERWQAVLAQTDVRqRELEQLGRQLRYYRESADPLDSWLQDAK 1228
Cdd:COG4913    370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEE--ALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLALR 446

                   ..
gi 1777507490 1229 RR 1230
Cdd:COG4913    447 DA 448
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
632-712 1.68e-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: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  632 WLSEKE----DEEVGFDWSErstnTAAKKDSYSALMRELELKEKKIKEIQSTGDRLLREDHPARPTVESFQAALQTQWSW 707
Cdd:pfam00435   16 WIEEKEallsSEDYGKDLES----VQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERWEQ 91

                   ....*
gi 1777507490  708 MLQLC 712
Cdd:pfam00435   92 LLELA 96
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
44-158 2.25e-03

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: 41.11  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490   44 QKKTFTKWVNKHLIKHwrAEAQRHI------SDLYEDLRDGHNLISLLEVLSGDSLPrERDVIRSSRLPrekgrmrFHKL 117
Cdd:cd21292     25 EKVAFVNWINKNLGDD--PDCKHLLpmdpntDDLFEKVKDGILLCKMINLSVPDTID-ERAINKKKLTV-------FTIH 94
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1777507490  118 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 158
Cdd:cd21292     95 ENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1108-1345 2.31e-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: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1108 AHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLE 1187
Cdd:COG4942     17 AQADAAAEAEA------ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1188 RWQAVLAQTDVRQRELEQLGRQLrYYRESADPLDSWL-----QDAKRRQEQIQAVplanSQVVREQLRQEKALLEEIERH 1262
Cdd:COG4942     91 EIAELRAELEAQKEELAELLRAL-YRLGRQPPLALLLspedfLDAVRRLQYLKYL----APARREQAEELRADLAELAAL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1263 GEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKvqsgsESVIQEYVDLRTRYSELTTLTSQYIKFISETL 1342
Cdd:COG4942    166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL-----AELAAELAELQQEAEELEALIARLEAEAAAAA 240

                   ...
gi 1777507490 1343 RRM 1345
Cdd:COG4942    241 ERT 243
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
863-1477 2.55e-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: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  863 NQEAQEAIARlEAQHQALVALWhQLHTDMKSLLAWQSLSRDVQlirsWSLVTFRTLKPEE------------QRQALRsL 930
Cdd:TIGR00618  223 VLEKELKHLR-EALQQTQQSHA-YLTQKREAQEEQLKKQQLLK----QLRARIEELRAQEavleetqerinrARKAAP-L 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  931 ELHYQAFLRDSQDAGGFGPEDRLQaEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRL 1010
Cdd:TIGR00618  296 AAHIKAVTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1011 PLDKEPARECAQRI-AEQQKAQAevegLGKGVARLSAEAEKVLALPEPSPAAP----TLRSELELTLGKLEQVRSLSAIY 1085
Cdd:TIGR00618  375 HTLTQHIHTLQQQKtTLTQKLQS----LCKELDILQREQATIDTRTSAFRDLQgqlaHAKKQQELQQRYAELCAAAITCT 450
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1086 LEKLKtisLVIRSTQGAEDVLKAHEEQLKEAQAVpaTLPELEATKAALKKLRAQAEAQQPVFDALR---------DELRG 1156
Cdd:TIGR00618  451 AQCEK---LEKIHLQESAQSLKEREQQLQTKEQI--HLQETRKKAVVLARLLELQEEPCPLCGSCIhpnparqdiDNPGP 525
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1157 AQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLdswLQDAKRRQEQIQA 1236
Cdd:TIGR00618  526 LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL---QNITVRLQDLTEK 602
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1237 VPLANSQVVREQLRQEKALLEEIERHGEKVEE--CQRFAKQYINAIKDYELQLvTYKAQLEPVASPAKKPKvQSGsESVI 1314
Cdd:TIGR00618  603 LSEAEDMLACEQHALLRKLQPEQDLQDVRLHLqqCSQELALKLTALHALQLTL-TQERVREHALSIRVLPK-ELL-ASRQ 679
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1315 QEYVDLRTRYSELTTLTSQyIKFISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQ------RERFIEQEKA 1388
Cdd:TIGR00618  680 LALQKMQSEKEQLTYWKEM-LAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNqslkelMHQARTVLKA 758
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1389 KL---EQLFQEEVAKAQKLR-----EEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRrkQEELQRLEEQRQQQEKL 1460
Cdd:TIGR00618  759 RTeahFNNNEEVTAALQTGAelshlAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL--NLQCETLVQEEEQFLSR 836
                          650       660
                   ....*....|....*....|
gi 1777507490 1461 LAEENQRL---RERLQHLEE 1477
Cdd:TIGR00618  837 LEEKSATLgeiTHQLLKYEE 856
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
966-1560 2.79e-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: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  966 YQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACEtrtvhRLRLPLDKEPAREcaqRIAEQQKAQAEVEglgkgvarls 1045
Cdd:TIGR00618  245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLE-----ETQERINRARKAA---PLAAHIKAVTQIE---------- 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1046 AEAEKVLAlpepspaaptlrsELELTLGKLEQVRSLSAIYLEKlktiSLVIRSTQGAEDVLKAHEEQLKEAQAVPAT-LP 1124
Cdd:TIGR00618  307 QQAQRIHT-------------ELQSKMRSRAKLLMKRAAHVKQ----QSSIEEQRRLLQTLHSQEIHIRDAHEVATSiRE 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1125 ELEATKAALKKLRAQAEAQQpvfdALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLerwqAVLAQTDVRQRELE 1204
Cdd:TIGR00618  370 ISCQQHTLTQHIHTLQQQKT----TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA----HAKKQQELQQRYAE 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1205 QLGrqlryyresadpldswLQDAKRRQEQIQAVPLANSqvVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYE 1284
Cdd:TIGR00618  442 LCA----------------AAITCTAQCEKLEKIHLQE--SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP 503
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1285 LQLVTYKAQLEPVA-----SPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLL 1359
Cdd:TIGR00618  504 CPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSK 583
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1360 QETQALRQ---SFLSEKDSLLQRERFIEQEKAKLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREA 1436
Cdd:TIGR00618  584 EDIPNLQNitvRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREH 663
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1437 EEGVR-----------RKQEELQRLEEQRQQQEKLLAEENQRLRERLQHLEEEHR-------AALAHSEEVPASQATATK 1498
Cdd:TIGR00618  664 ALSIRvlpkellasrqLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRefneienASSSLGSDLAAREDALNQ 743
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1777507490 1499 ALPNGRDALDGPATETEPEHAFDGLRQKVPAQQLQEVGILSAEELQRLVQGRTTVAELEQRE 1560
Cdd:TIGR00618  744 SLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLE 805
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
956-1518 3.04e-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: 43.59  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490  956 EREYGSCSRHYQQLLQSLEQGEQEEsrCQRCISELKDIRLQLEACETRTvhrlrlpldkeparecAQRIAEQQKAQAEVE 1035
Cdd:pfam07111  139 QRELEEIQRLHQEQLSSLTQAHEEA--LSSLTSKAEGLEKSLNSLETKR----------------AGEAKQLAEAQKEAE 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1036 GLGKGVARLSAEAEKVLALPE--------------PSPAAPTLRSELELTLGKLEQVR-SLSAiyleklkTISLVIRSTQ 1100
Cdd:pfam07111  201 LLRKQLSKTQEELEAQVTLVEslrkyvgeqvppevHSQTWELERQELLDTMQHLQEDRaDLQA-------TVELLQVRVQ 273
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1101 GAEDVLKAHEEQLKEaQAVPATLPELEATKAALKKLRAQAEAqqpVFdALRDELRgAQEvgerLQQRHgerdvEVERWRE 1180
Cdd:pfam07111  274 SLTHMLALQEEELTR-KIQPSDSLEPEFPKKCRSLLNRWREK---VF-ALMVQLK-AQD----LEHRD-----SVKQLRG 338
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1181 RVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLDSWL---QDAKRRQEQIQAVPLANSQVVREQLRQEKALLE 1257
Cdd:pfam07111  339 QVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELsraQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLE 418
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1258 -EIERHGEKVEECQRFAKQYINAIKDYEL-------QLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTT 1329
Cdd:pfam07111  419 tTMTRVEQAVARIPSLSNRLSYAVRKVHTikglmarKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQ 498
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1330 LTSQYIKfiSETLRRMEEEEmqtVQQEQLLQETQALRQSFLSEKDSL----------LQRERFIEQEKAKLEQ-LFQEEV 1398
Cdd:pfam07111  499 LSAHLIQ--QEVGRAREQGE---AERQQLSEVAQQLEQELQRAQESLasvgqqlevaRQGQQESTEEAASLRQeLTQQQE 573
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1399 AKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKLL----AEENQRLRERLQH 1474
Cdd:pfam07111  574 IYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQdearKEEGQRLARRVQE 653
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1777507490 1475 LEEEHRAALAHSEE----VPASQATATKALPNGRD---ALDGPATETEPEH 1518
Cdd:pfam07111  654 LERDKNLMLATLQQegllSRYKQQRLLAVLPSGLDkksVVSSPRPECSASA 704
COG4995 COG4995
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
1141-1602 3.27e-03

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


Pssm-ID: 444019 [Multi-domain]  Cd Length: 711  Bit Score: 43.42  E-value: 3.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1141 EAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPL 1220
Cdd:COG4995      1 LLALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1221 DSWLQDAKRRQEQIQAVPLANSQVVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASP 1300
Cdd:COG4995     81 ALAALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1301 AKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRE 1380
Cdd:COG4995    161 AAAALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLAL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1381 RFIEQEKAKLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEGVRRKQEELQRLEEQRQQQEKL 1460
Cdd:COG4995    241 LALAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1461 LAEENQRLRERLQHLEEEHRAALAHSEEVPASQATATKALPNGRDALDGPATETEPEHAFDGLRQKVPAQQLQEVGILSA 1540
Cdd:COG4995    321 AALLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAAL 400
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1777507490 1541 EELQRLVQGRTTVAELEQREDVRCYLQGRSSIAGLL-LQPSNEKLSVYAALRRQLLSPGTALI 1602
Cdd:COG4995    401 LALAAAQLLRLLLAALALLLALAAYAAARLALLALIeYIILPDRLYAFVQLYQLLIAPIEAEL 463
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1079-1268 3.65e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1079 RSLSAIYLEKLKTISLVIRSTQGAEDVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQpvfdALRDELRGAQ 1158
Cdd:COG4717     53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL----EKLEKLLQLL 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1159 EVGERLQQRHGERDVEVERWrERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPldSWLQDAKRRQEQIQAvp 1238
Cdd:COG4717    129 PLYQELEALEAELAELPERL-EELEERLEELRELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEELEE-- 203
                          170       180       190
                   ....*....|....*....|....*....|
gi 1777507490 1239 lansqvVREQLRQEKALLEEIERHGEKVEE 1268
Cdd:COG4717    204 ------LQQRLAELEEELEEAQEELEELEE 227
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3155-3185 4.28e-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: 4.28e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1777507490 3155 AGILDTETLEKVSITEAMHRNLVDNITGQRL 3185
Cdd:pfam00681    9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1125-1494 4.48e-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: 43.04  E-value: 4.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1125 ELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERlqqrhgERDVEVERWRERVTQLLERWQAVLAQTDVRQRELE 1204
Cdd:pfam02463  167 LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQ------AKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1205 QLGRQLRYYRESadpLDSWLQDAKRRQEQIQAVplanSQVVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYE 1284
Cdd:pfam02463  241 LLQELLRDEQEE---IESSKQEIEKEEEKLAQV----LKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1285 LQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEEmqtvqqeqllQETQA 1364
Cdd:pfam02463  314 EKLKESEKEKK---------KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLE----------QLEEE 374
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1365 LRQSFLSEKDSLLQRERFIEQEKAKLEQLFQEEVAKAQKLREEQQRQQQQMEQEKQQLVASMEEARRQQREAEEgvrRKQ 1444
Cdd:pfam02463  375 LLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTE---EKE 451
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1445 EELQRLEEQRQQQEKLLAEENQRLRERLQHLEEEHRAALAHSEEVPASQA 1494
Cdd:pfam02463  452 ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK 501
PLEC smart00250
Plectin repeat;
2877-2908 4.63e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.08  E-value: 4.63e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1777507490  2877 KLLSAERAVTGYKDPYSGKLISLFQAMKKGLI 2908
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
1091-1295 5.63e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 5.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1091 TISLVIRSTQGAEDVLKAHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEvgerlqqrhge 1170
Cdd:COG3883      3 ALALAAPTPAFADPQIQAKQKELSELQA------ELEAAQAELDALQAELEELNEEYNELQAELEALQA----------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1171 rdvEVERWRERVTQllerwqavlAQTDVRQRElEQLGRQLRYYRESADPLDSW--------LQDAKRRQEQIQAVPLANS 1242
Cdd:COG3883     66 ---EIDKLQAEIAE---------AEAEIEERR-EELGERARALYRSGGSVSYLdvllgsesFSDFLDRLSALSKIADADA 132
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1777507490 1243 QVVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLE 1295
Cdd:COG3883    133 DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1125-1205 6.57e-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: 6.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1125 ELEATKAALKKLRAQAEAqqpvFDALRDELRGAQEVGERLQQRHGErdvEVERWRERVTQLLERWQAVLAQTDVRQRELE 1204
Cdd:pfam00435   32 DLESVQALLKKHKALEAE----LAAHQDRVEALNELAEKLIDEGHY---ASEEIQERLEELNERWEQLLELAAERKQKLE 104

                   .
gi 1777507490 1205 Q 1205
Cdd:pfam00435  105 E 105
PLEC smart00250
Plectin repeat;
3297-3334 7.28e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 36.69  E-value: 7.28e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1777507490  3297 QKLRDVSAYSKYLTCPKTKLKISYKDALDRSMVEEGTG 3334
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
1114-1478 8.54e-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: 42.03  E-value: 8.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1114 KEAQAVPATLPELEA-----------------TKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERdVEVE 1176
Cdd:pfam17380  221 KEVQGMPHTLAPYEKmerrkesfnlaedvttmTPEYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEK-MEQE 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1177 RWRERVTQL---LERWQAVLAQTDVRQRELEQ----LGRQLRYYRESADPLDS-WLQDAKRRQEQIQAVPLAnsqVVREQ 1248
Cdd:pfam17380  300 RLRQEKEEKareVERRRKLEEAEKARQAEMDRqaaiYAEQERMAMERERELERiRQEERKRELERIRQEEIA---MEISR 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1249 LRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVaspakKPKVQSGSESVIQEYVDLRTRYSELT 1328
Cdd:pfam17380  377 MRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI-----RAEQEEARQREVRRLEEERAREMERV 451
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1329 TLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALRQSflsekdsllQRERFIEQEKAKLEQLFQEEVAKAQKLREeq 1408
Cdd:pfam17380  452 RLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEE---------QRRKILEKELEERKQAMIEEERKRKLLEK-- 520
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1409 qrqqqqmeqekqqlvaSMEEarRQQREAEEGVRRKQEELQRLEEQRqqqekllaEENQRLRERLQHLEEE 1478
Cdd:pfam17380  521 ----------------EMEE--RQKAIYEEERRREAEEERRKQQEM--------EERRRIQEQMRKATEE 564
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1107-1393 9.38e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 9.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1107 KAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLL 1186
Cdd:COG4372      7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1187 ERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLDSWLQDAKRRQEQIQAVPLANSQVVREQLRQEKALLEEIERHGEKV 1266
Cdd:COG4372     87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1267 EECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQ---SGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLR 1343
Cdd:COG4372    167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKlieSLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1777507490 1344 RMEEEEMQTVQQEQLLQETQALRQSFLSEKDSLLQRERFIEQEKAKLEQL 1393
Cdd:COG4372    247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELK 296
 
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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