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Conserved domains on  [gi|2462619885|ref|XP_054216666|]
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plectin isoform X33 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
19-123 8.49e-77

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: 250.01  E-value: 8.49e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   19 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNI 98
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
                           90       100
                   ....*....|....*....|....*
gi 2462619885   99 RNDDIADGNPKLTLGLIWTIILHFQ 123
Cdd:cd21188     81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
136-241 1.43e-72

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


:

Pssm-ID: 409087  Cd Length: 106  Bit Score: 238.00  E-value: 1.43e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  136 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 215
Cdd:cd21238      1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 2462619885  216 PEDVDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
872-949 6.41e-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: 117.70  E-value: 6.41e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619885  872 LAWQSLRRDVQLIRSWSLATFRTLKPEEQRQALHSLELHYQAFLRDSQDAGGFGPEDRLMAEREYGSCSHHYQQLLQS 949
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
771-837 4.67e-22

SH3 domain; This entry represents an SH3 domain.


:

Pssm-ID: 407754  Cd Length: 65  Bit Score: 91.94  E-value: 4.67e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619885  771 QLKPRhpAHPMRGRLPLLAVCDYKQVEVTVHKGDECQLVGPAQPSHWKVLSSSGSEAAVPSVCFLVP 837
Cdd:pfam17902    1 PLKQR--RSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
596-785 1.11e-18

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: 87.50  E-value: 1.11e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  596 LHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQ 675
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  676 AALQTQWSWMLQLCCCIEAHLKENAAYFQFFSDVREAEGQLQKLQEALRrkySCDRSATVTRLEDLLQDAQDEKEQLNEY 755
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190
                   ....*....|....*....|....*....|
gi 2462619885  756 KGHLSGLAKRAKAVVQLKPRHPAHPMRGRL 785
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2893-2931 9.10e-16

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 73.13  E-value: 9.10e-16
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2893 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 2931
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1656-1694 3.67e-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: 3.67e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 1656 LLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEMNRVL 1694
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2574-2612 3.71e-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: 3.71e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2574 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 2612
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2315-2353 6.72e-15

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 70.82  E-value: 6.72e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2315 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEMNRVL 2353
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1080-1270 1.30e-14

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 75.56  E-value: 1.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1080 EEVLRAHEEQLKEAQaVPATLPELEATKASLKKLRAQAEAQQPTFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1159
Cdd:cd00176     13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1160 AQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLGAWLQDArrrQEQIQAMPLADS-QAVREQLRQEQALLEEIER 1238
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEK---EAALASEDLGKDlESVEELLKKHKELEEELEA 157
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2462619885 1239 HGEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1270
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
500-689 6.02e-14

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 73.63  E-value: 6.02e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  500 LRYLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARSDEGQLSPATRGAY---RDCLGRLD 576
Cdd:cd00176      6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  577 LQYAKLLNSSKARLRSLE---SLHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKEL 653
Cdd:cd00176     86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462619885  654 QNAGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 689
Cdd:cd00176    166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1908-1946 1.36e-13

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 66.97  E-value: 1.36e-13
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 1908 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEFHEKL 1946
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3162-3200 1.28e-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: 1.28e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 3162 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 3200
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1984-2022 1.93e-12

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.89  E-value: 1.93e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 1984 LLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEETSRAL 2022
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1580-1618 2.21e-12

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.50  E-value: 2.21e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 1580 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHKL 1618
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2817-2855 2.85e-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: 2.85e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2817 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 2855
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2650-2688 3.05e-12

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.12  E-value: 3.05e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2650 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 2688
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3238-3276 9.99e-11

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 58.88  E-value: 9.99e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 3238 FLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTAQKL 3276
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
892-1460 3.38e-08

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: 59.95  E-value: 3.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  892 FRTLKPEEQRQALHSLELHYQAFLRDSQDAGgfgpEDRLMAEREYGSCSHHYQQLLQSLEQGAQEESRCQRCISELKDIR 971
Cdd:COG1196    215 YRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  972 LQLEACETRTVHRLRLplDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALpepspAAPTLRSELELTLGK 1051
Cdd:COG1196    291 YELLAELARLEQDIAR--LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-----AEEELEEAEAELAEA 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1052 LEQVRSLSAIYLEKLKTISlviRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDEL 1131
Cdd:COG1196    364 EEALLEAEAELAEAEEELE---ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1132 RGAQEvgeRLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQI 1211
Cdd:COG1196    441 EEALE---EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1212 QAMPLAdsQAVREQLRQEQALLEEIE-----RHGEKVEECQRFAKQYINAIKDYELQLVTY--KAQLEPVASPAKKPKVQ 1284
Cdd:COG1196    518 GLRGLA--GAVAVLIGVEAAYEAALEaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpLDKIRARAALAAALARG 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1285 SGSESVIQEYVDLRTH---------YSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALQQSFLSEKDSLLQ 1355
Cdd:COG1196    596 AIGAAVDLVASDLREAdaryyvlgdTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1356 RERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQE 1435
Cdd:COG1196    676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
                          570       580
                   ....*....|....*....|....*
gi 2462619885 1436 ELLAEENQRLREQLQLLEEQhRAAL 1460
Cdd:COG1196    756 LPEPPDLEELERELERLERE-IEAL 779
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2994-3022 3.71e-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: 3.71e-07
                           10        20
                   ....*....|....*....|....*....
gi 2462619885 2994 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 3022
Cdd:pfam00681   11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
2777-2814 5.81e-07

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 48.25  E-value: 5.81e-07
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2462619885  2777 QKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTA 2814
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2245-2277 2.27e-06

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 46.55  E-value: 2.27e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462619885 2245 ATGFLVDPVRNQRLYVHEAVKAGVVGPELHEQL 2277
Cdd:pfam00681    7 ATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
1945-1981 2.31e-06

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.32  E-value: 2.31e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  1945 KLLSAEKAVTGYRDPYTGQSVSLFQALKKGLIPREQG 1981
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
1617-1653 1.28e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.28e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  1617 KLLSAERAVTGYKDPYTGQQISLFQAMQKGLIVREHG 1653
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1542-1580 2.51e-05

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 43.47  E-value: 2.51e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 1542 YLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTALIL 1580
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
2201-2235 3.18e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.18e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2462619885  2201 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 2235
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
3126-3159 5.35e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 5.35e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2462619885  3126 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 3159
Cdd:smart00250    5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2536-2571 8.91e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.08  E-value: 8.91e-05
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 2462619885  2536 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVA 2571
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2276-2307 9.17e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.08  E-value: 9.17e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2462619885  2276 QLLSAEKAVTGYRDPYSGSTISLFQAMQKGLV 2307
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
PLEC smart00250
Plectin repeat;
2611-2647 1.86e-04

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.86e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  2611 RLLSAERAVTGYRDPYTEQTISLFQAMKKELIPTEEA 2647
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2854-2885 4.12e-03

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.46  E-value: 4.12e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2462619885  2854 KLLSAERAVTGYKDPYSGKLISLFQAMKKGLI 2885
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
 
Name Accession Description Interval E-value
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
19-123 8.49e-77

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: 250.01  E-value: 8.49e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   19 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNI 98
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
                           90       100
                   ....*....|....*....|....*
gi 2462619885   99 RNDDIADGNPKLTLGLIWTIILHFQ 123
Cdd:cd21188     81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
136-241 1.43e-72

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


Pssm-ID: 409087  Cd Length: 106  Bit Score: 238.00  E-value: 1.43e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  136 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 215
Cdd:cd21238      1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 2462619885  216 PEDVDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
20-348 9.06e-47

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 180.14  E-value: 9.06e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   20 RVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLV 96
Cdd:COG5069      8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   97 NIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTSSWRDGRLFNAII 175
Cdd:COG5069     88 NIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALI 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  176 HRHKPLLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS------SLYD----AMPR 242
Cdd:COG5069    165 HDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyiirfGLLEkidiALHR 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  243 VPDVQDGVRANElQLRwQEYRELVLLLLQWMRHHTAAFEERRFPSSFEEIEILWSQFLKFKEME--LPAKEAD-KNRSKG 319
Cdd:COG5069    245 VYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCsrAPLETTDlHSLAGQ 322
                          330       340
                   ....*....|....*....|....*....
gi 2462619885  320 IYQSLEgAVQAGQLKVPPGYHPLDVEKEW 348
Cdd:COG5069    323 ILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
872-949 6.41e-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: 117.70  E-value: 6.41e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619885  872 LAWQSLRRDVQLIRSWSLATFRTLKPEEQRQALHSLELHYQAFLRDSQDAGGFGPEDRLMAEREYGSCSHHYQQLLQS 949
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
24-121 1.63e-25

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: 103.16  E-value: 1.63e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885    24 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKLVNIR 99
Cdd:smart00033    1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 2462619885   100 NDDIADGnPKLTLGLIWTIILH 121
Cdd:smart00033   81 PEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
136-242 9.20e-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: 101.21  E-value: 9.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  136 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 212
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462619885  213 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 242
Cdd:pfam00307   81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
21-124 1.66e-24

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: 100.44  E-value: 1.66e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   21 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-VKLV 96
Cdd:pfam00307    2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
                           90       100
                   ....*....|....*....|....*...
gi 2462619885   97 NIRNDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:pfam00307   82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
771-837 4.67e-22

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 91.94  E-value: 4.67e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619885  771 QLKPRhpAHPMRGRLPLLAVCDYKQVEVTVHKGDECQLVGPAQPSHWKVLSSSGSEAAVPSVCFLVP 837
Cdd:pfam17902    1 PLKQR--RSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
140-236 3.47e-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: 85.06  E-value: 3.47e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   140 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 215
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 2462619885   216 PEDVDVPQPDEKSIITYVSSL 236
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
596-785 1.11e-18

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: 87.50  E-value: 1.11e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  596 LHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQ 675
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  676 AALQTQWSWMLQLCCCIEAHLKENAAYFQFFSDVREAEGQLQKLQEALRrkySCDRSATVTRLEDLLQDAQDEKEQLNEY 755
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190
                   ....*....|....*....|....*....|
gi 2462619885  756 KGHLSGLAKRAKAVVQLKPRHPAHPMRGRL 785
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2893-2931 9.10e-16

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 73.13  E-value: 9.10e-16
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2893 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 2931
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1656-1694 3.67e-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: 3.67e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 1656 LLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEMNRVL 1694
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2574-2612 3.71e-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: 3.71e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2574 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 2612
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2315-2353 6.72e-15

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 70.82  E-value: 6.72e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2315 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEMNRVL 2353
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1080-1270 1.30e-14

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 75.56  E-value: 1.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1080 EEVLRAHEEQLKEAQaVPATLPELEATKASLKKLRAQAEAQQPTFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1159
Cdd:cd00176     13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1160 AQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLGAWLQDArrrQEQIQAMPLADS-QAVREQLRQEQALLEEIER 1238
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEK---EAALASEDLGKDlESVEELLKKHKELEEELEA 157
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2462619885 1239 HGEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1270
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
500-689 6.02e-14

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 73.63  E-value: 6.02e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  500 LRYLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARSDEGQLSPATRGAY---RDCLGRLD 576
Cdd:cd00176      6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  577 LQYAKLLNSSKARLRSLE---SLHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKEL 653
Cdd:cd00176     86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462619885  654 QNAGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 689
Cdd:cd00176    166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1908-1946 1.36e-13

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 66.97  E-value: 1.36e-13
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 1908 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEFHEKL 1946
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3162-3200 1.28e-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: 1.28e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 3162 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 3200
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1984-2022 1.93e-12

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.89  E-value: 1.93e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 1984 LLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEETSRAL 2022
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1580-1618 2.21e-12

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.50  E-value: 2.21e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 1580 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHKL 1618
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2817-2855 2.85e-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: 2.85e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2817 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 2855
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2650-2688 3.05e-12

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.12  E-value: 3.05e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2650 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 2688
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3238-3276 9.99e-11

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 58.88  E-value: 9.99e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 3238 FLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTAQKL 3276
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
944-1274 1.05e-09

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: 64.70  E-value: 1.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  944 QQLLQSLEQGAQEESRCQRCISELKDirlQLEACETRTVHRLRLPLDKEPARECAQ--RIAEQQKAQAEVEGLGKGVARL 1021
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKAERYQALLKEKREYEGyeLLKEKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1022 SAEAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRGTQG----AEEVLRAHEEQLKE 1092
Cdd:TIGR02169  250 EEELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELED 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1093 AQAVPATL-PELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQllerwqavla 1171
Cdd:TIGR02169  320 AEERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------- 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1172 qtdvRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQamplADSQAVREQLRQEQALLEEIerhGEKVEECQRFAK 1251
Cdd:TIGR02169  390 ----YREKLEKLKREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEKEDK---ALEIKKQEWKLE 458
                          330       340
                   ....*....|....*....|...
gi 2462619885 1252 QYINAIKDYELQLVTYKAQLEPV 1274
Cdd:TIGR02169  459 QLAADLSKYEQELYDLKEEYDRV 481
PLEC smart00250
Plectin repeat;
3160-3197 1.13e-09

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 55.95  E-value: 1.13e-09
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2462619885  3160 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 3197
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2891-2927 2.18e-08

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 52.10  E-value: 2.18e-08
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  2891 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 2927
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
892-1460 3.38e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 3.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  892 FRTLKPEEQRQALHSLELHYQAFLRDSQDAGgfgpEDRLMAEREYGSCSHHYQQLLQSLEQGAQEESRCQRCISELKDIR 971
Cdd:COG1196    215 YRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  972 LQLEACETRTVHRLRLplDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALpepspAAPTLRSELELTLGK 1051
Cdd:COG1196    291 YELLAELARLEQDIAR--LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-----AEEELEEAEAELAEA 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1052 LEQVRSLSAIYLEKLKTISlviRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDEL 1131
Cdd:COG1196    364 EEALLEAEAELAEAEEELE---ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1132 RGAQEvgeRLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQI 1211
Cdd:COG1196    441 EEALE---EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1212 QAMPLAdsQAVREQLRQEQALLEEIE-----RHGEKVEECQRFAKQYINAIKDYELQLVTY--KAQLEPVASPAKKPKVQ 1284
Cdd:COG1196    518 GLRGLA--GAVAVLIGVEAAYEAALEaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpLDKIRARAALAAALARG 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1285 SGSESVIQEYVDLRTH---------YSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALQQSFLSEKDSLLQ 1355
Cdd:COG1196    596 AIGAAVDLVASDLREAdaryyvlgdTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1356 RERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQE 1435
Cdd:COG1196    676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
                          570       580
                   ....*....|....*....|....*
gi 2462619885 1436 ELLAEENQRLREQLQLLEEQhRAAL 1460
Cdd:COG1196    756 LPEPPDLEELERELERLERE-IEAL 779
SPEC smart00150
Spectrin repeats;
597-689 5.71e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.10  E-value: 5.71e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   597 HSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQA 676
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90
                    ....*....|...
gi 2462619885   677 ALQTQWSWMLQLC 689
Cdd:smart00150   81 ELNERWEELKELA 93
PLEC smart00250
Plectin repeat;
2572-2607 1.67e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 49.79  E-value: 1.67e-07
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 2462619885  2572 RLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPE 2607
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2994-3022 3.71e-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: 3.71e-07
                           10        20
                   ....*....|....*....|....*....
gi 2462619885 2994 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 3022
Cdd:pfam00681   11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
2777-2814 5.81e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 48.25  E-value: 5.81e-07
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2462619885  2777 QKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTA 2814
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
1654-1690 1.10e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 47.48  E-value: 1.10e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  1654 IRLLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEM 1690
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2245-2277 2.27e-06

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 46.55  E-value: 2.27e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462619885 2245 ATGFLVDPVRNQRLYVHEAVKAGVVGPELHEQL 2277
Cdd:pfam00681    7 ATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
1945-1981 2.31e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.32  E-value: 2.31e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  1945 KLLSAEKAVTGYRDPYTGQSVSLFQALKKGLIPREQG 1981
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2313-2349 2.66e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.32  E-value: 2.66e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  2313 IRLLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEM 2349
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1083-1245 3.07e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 3.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1083 LRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRH---GERDVEVERWRERV 1159
Cdd:COG4717     73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEaleAELAELPERLEELE 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1160 AQlLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPlgAWLQDARRRQEQIqampladsQAVREQLRQEQALLEEIERH 1239
Cdd:COG4717    153 ER-LEELRELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEEL--------EELQQRLAELEEELEEAQEE 221

                   ....*.
gi 2462619885 1240 GEKVEE 1245
Cdd:COG4717    222 LEELEE 227
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2779-2817 4.61e-06

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 45.78  E-value: 4.61e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2779 FLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTAFEL 2817
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
941-1584 8.38e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 8.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  941 HHYQQLLQSLeqgAQEESRCQRCISELKDIRLQLEACETRTVHRLrlpLDKEPARECAQRIAEQQKAQAEVegLGKGVAR 1020
Cdd:TIGR02168  284 EELQKELYAL---ANEISRLEQQKQILRERLANLERQLEELEAQL---EELESKLDELAEELAELEEKLEE--LKEELES 355
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1021 LSAEAEKVLALpepSPAAPTLRSELEltlgklEQVRSLSAIYLEKLKTISLvIRGTQgaeEVLRAHEEQLKEAQAVPATl 1100
Cdd:TIGR02168  356 LEAELEELEAE---LEELESRLEELE------EQLETLRSKVAQLELQIAS-LNNEI---ERLEARLERLEDRRERLQQ- 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1101 pelEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERwqavLAQTDVRQREL 1180
Cdd:TIGR02168  422 ---EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE----LAQLQARLDSL 494
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1181 EQLGRQLRYYRESAdplgAWLQDARRRQEQIQAmPLADSQAVREQLrqEQALLEEIERHGEKVE-ECQRFAKQYINAIKD 1259
Cdd:TIGR02168  495 ERLQENLEGFSEGV----KALLKNQSGLSGILG-VLSELISVDEGY--EAAIEAALGGRLQAVVvENLNAAKKAIAFLKQ 567
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1260 YELQLVTYKA--QLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSE----LTTLTSQYikFISETL-------RRMEEEE 1326
Cdd:TIGR02168  568 NELGRVTFLPldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkaLSYLLGGV--LVVDDLdnalelaKKLRPGY 645
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1327 MQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEA 1406
Cdd:TIGR02168  646 RIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEEL-EEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1407 RRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQR---LREQLQLLEEQHRAALAHSEEVTASQVAATKTLPNGRDA 1483
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1484 LDGPAAEAEpEHSFDGLRRKVSAQRLQEAGILSAEELQRLAQghTTVDELARREDVRHYLQGRSSIAGLLLKATNEKLSV 1563
Cdd:TIGR02168  805 LDELRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEE--QIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
                          650       660
                   ....*....|....*....|.
gi 2462619885 1564 YAALQRQLLSPGTALILLEAQ 1584
Cdd:TIGR02168  882 RASLEEALALLRSELEELSEE 902
PLEC smart00250
Plectin repeat;
2987-3015 1.26e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.26e-05
                            10        20
                    ....*....|....*....|....*....
gi 2462619885  2987 VRKRRVVIVDPETGKEMSVYEAYRKGLID 3015
Cdd:smart00250    6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
PLEC smart00250
Plectin repeat;
1617-1653 1.28e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.28e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  1617 KLLSAERAVTGYKDPYTGQQISLFQAMQKGLIVREHG 1653
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
414-1245 1.51e-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: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  414 GEVERDLDKADSMIRLLFNDVQTLKDGRhpqgEQMYRrvYR-LHERLvaIRTEYNLRLKAgVAAPATQVAQVTLQSVQRR 492
Cdd:TIGR02169  180 EEVEENIERLDLIIDEKRQQLERLRRER----EKAER--YQaLLKEK--REYEGYELLKE-KEALERQKEAIERQLASLE 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  493 PELEDSTLRyLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGshrgLHQSIEEFRAKIERARS------DEGQLSPATRG 566
Cdd:TIGR02169  251 EELEKLTEE-ISELEKRLEEIEQLLEELNKKIKDLGEEEQLR----VKEKIGELEAEIASLERsiaekeRELEDAEERLA 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  567 AYRDCLGRLDLQYAKLLNSSKARLRSLESLHSFVAAATKELMWL-NEKEEEEVGFDwsdrntnmtAKKESYSALMRELEL 645
Cdd:TIGR02169  326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLrAELEEVDKEFA---------ETRDELKDYREKLEK 396
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  646 KEKKIKELQNAGDRLLREDHPARPTVESFQAALQTQWSWMLQLccciEAHLKENAAyfqffsDVREAEGQLQKLQE---A 722
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL----EEEKEDKAL------EIKKQEWKLEQLAAdlsK 466
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  723 LRRKYScDRSATVTRLEDLLQDAQDEKEQLN---------------------------------------EYKGHL-SGL 762
Cdd:TIGR02169  467 YEQELY-DLKEEYDRVEKELSKLQRELAEAEaqaraseervrggraveevlkasiqgvhgtvaqlgsvgeRYATAIeVAA 545
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  763 AKRAKAVV-----------QLKPRHPAhpmrGRLPLLAVCDYKQVEVTVHKGDECQLVGPA----------QPSHWKVLS 821
Cdd:TIGR02169  546 GNRLNNVVveddavakeaiELLKRRKA----GRATFLPLNKMRDERRDLSILSEDGVIGFAvdlvefdpkyEPAFKYVFG 621
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  822 SSGseaavpsvcfLVpppnqEAQEAVTRLEAQHQaLVTLWHQLhVDMKSLLAWQSLRRDVQLIRSwslatfRTLKPEEQR 901
Cdd:TIGR02169  622 DTL----------VV-----EDIEAARRLMGKYR-MVTLEGEL-FEKSGAMTGGSRAPRGGILFS------RSEPAELQR 678
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  902 QA--LHSLElhyqaflrdsqdaggfGPEDRLMAEREygscshHYQQLLQSLEqgaQEESRCQRCISELKDIRLQLEACET 979
Cdd:TIGR02169  679 LRerLEGLK----------------RELSSLQSELR------RIENRLDELS---QELSDASRKIGEIEKEIEQLEQEEE 733
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  980 RTVHRLRLPLDK--EPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPSP---------AAPTLRSELELT 1048
Cdd:TIGR02169  734 KLKERLEELEEDlsSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelsKLEEEVSRIEAR 813
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1049 LGKLEQV---RSLSAIYLEKLKtislvirgtQGAEEVLRAHEEQLKE-AQAVPATLPELEATKASLKKLRAQAEAQQPTF 1124
Cdd:TIGR02169  814 LREIEQKlnrLTLEKEYLEKEI---------QELQEQRIDLKEQIKSiEKEIENLNGKKEELEEELEELEAALRDLESRL 884
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1125 DALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDvrqrELEQLGRQLRYYRESADPLGAWLQDA 1204
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLEDVQAEL 960
                          890       900       910       920
                   ....*....|....*....|....*....|....*....|.
gi 2462619885 1205 RRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHgEKVEE 1245
Cdd:TIGR02169  961 QRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKR-AKLEE 1000
PLEC smart00250
Plectin repeat;
2648-2684 2.28e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.62  E-value: 2.28e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  2648 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDT 2684
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1542-1580 2.51e-05

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 43.47  E-value: 2.51e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 1542 YLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTALIL 1580
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
mukB PRK04863
chromosome partition protein MukB;
1079-1248 2.71e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.34  E-value: 2.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1079 AEEVLRAHEEQLKEAQAVP---ATLPELEatkaslKKLRAQAEAQQptfdaLRDELRGAQEVG-------ERLQQRHGER 1148
Cdd:PRK04863   498 ARELLRRLREQRHLAEQLQqlrMRLSELE------QRLRQQQRAER-----LLAEFCKRLGKNlddedelEQLQEELEAR 566
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1149 dveVERWRERVAQLLERwqavlaQTDVRQrELEQLGRQLRYYRESADplgAWL--QDARRRQEQIQAMPLADSQAVRE-- 1224
Cdd:PRK04863   567 ---LESLSESVSEARER------RMALRQ-QLEQLQARIQRLAARAP---AWLaaQDALARLREQSGEEFEDSQDVTEym 633
                          170       180
                   ....*....|....*....|....*.
gi 2462619885 1225 --QLRQEQALLEEIERHGEKVEECQR 1248
Cdd:PRK04863   634 qqLLERERELTVERDELAARKQALDE 659
PLEC smart00250
Plectin repeat;
2201-2235 3.18e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.18e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2462619885  2201 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 2235
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
3236-3273 3.54e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.54e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2462619885  3236 QRFLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTA 3273
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2817-2851 3.83e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.83e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2462619885  2817 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 2851
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
3126-3159 5.35e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 5.35e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2462619885  3126 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 3159
Cdd:smart00250    5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PTZ00121 PTZ00121
MAEBL; Provisional
991-1420 6.02e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 6.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  991 KEPARECAQRIAEQQKAQAEveglGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTlGKLEQVR---SLSAIYLEKLK 1067
Cdd:PTZ00121  1397 KKKAEEDKKKADELKKAAAA----KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK-KKAEEAKkaeEAKKKAEEAKK 1471
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1068 TISLVIRGTQG--AEEVLRAHEEQLKEA----QAVPATLPELEATKASLKKLRAQAEAQQPTFDAlrDELRGAQEVGERL 1141
Cdd:PTZ00121  1472 ADEAKKKAEEAkkADEAKKKAEEAKKKAdeakKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA--DEAKKAEEKKKAD 1549
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1142 QQRHGE--RDVEVERWRERVAQLLERWQAVLAQTDV-RQRELEQLGRQLRYYRESADPLGAWLQDARrrQEQIQAmplad 1218
Cdd:PTZ00121  1550 ELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEaKKAEEARIEEVMKLYEEEKKMKAEEAKKAE--EAKIKA----- 1622
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1219 sqavrEQLRQEQALLEEIERHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAKKPkvqsgSESVIQEYVDLR 1298
Cdd:PTZ00121  1623 -----EELKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKK-----AEEAKKAEEDEK 1688
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1299 THYSELTTLTSQYIKfiSETLRRMEEEEMQTVQQeqllqetqaLQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKA 1378
Cdd:PTZ00121  1689 KAAEALKKEAEEAKK--AEELKKKEAEEKKKAEE---------LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2462619885 1379 QQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRK 1420
Cdd:PTZ00121  1758 KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
SPEC smart00150
Spectrin repeats;
1088-1181 7.06e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 44.24  E-value: 7.06e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  1088 EQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALrdelrgaQEVGERLQQRHGERDVEVErwrERVAQLLERWQ 1167
Cdd:smart00150   18 EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEAL-------NELGEQLIEEGHPDAEEIE---ERLEELNERWE 87
                            90
                    ....*....|....
gi 2462619885  1168 AVLAQTDVRQRELE 1181
Cdd:smart00150   88 ELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
2536-2571 8.91e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.08  E-value: 8.91e-05
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 2462619885  2536 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVA 2571
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2276-2307 9.17e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.08  E-value: 9.17e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2462619885  2276 QLLSAEKAVTGYRDPYSGSTISLFQAMQKGLV 2307
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
SPEC smart00150
Spectrin repeats;
500-594 1.30e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.47  E-value: 1.30e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   500 LRYLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARSDEGQL---SPATRGAYRDCLGRLD 576
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
                            90
                    ....*....|....*...
gi 2462619885   577 LQYAKLLNSSKARLRSLE 594
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
1580-1613 1.43e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.43e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2462619885  1580 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPE 1613
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2201-2235 1.43e-04

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 41.54  E-value: 1.43e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2462619885 2201 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 2235
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPET 35
PLEC smart00250
Plectin repeat;
2611-2647 1.86e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.86e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  2611 RLLSAERAVTGYRDPYTEQTISLFQAMKKELIPTEEA 2647
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
1908-1942 2.20e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.93  E-value: 2.20e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2462619885  1908 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEF 1942
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
1982-2018 2.22e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.93  E-value: 2.22e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  1982 LRLLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEET 2018
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
Rabaptin pfam03528
Rabaptin;
1080-1377 2.88e-04

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 46.64  E-value: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1080 EEVLRAHEEQLKEAQAVpatlpeLEATKASLKKLRAQ-AEAQqptfdALRDELRGAQEVGERLQQrhgERDVEVER-WRE 1157
Cdd:pfam03528   39 KELYLAKEEDLKRQNAV------LQEAQVELDALQNQlALAR-----AEMENIKAVATVSENTKQ---EAIDEVKSqWQE 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1158 RVAQLlerwQAVLAQTdVRQRE------LEQLGRQLRYYRESADPLGAwlqDARRRqeqiqampLADSQavreqlrQEQA 1231
Cdd:pfam03528  105 EVASL----QAIMKET-VREYEvqfhrrLEQERAQWNQYRESAEREIA---DLRRR--------LSEGQ-------EEEN 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1232 LLEEIERHGEKVEECQRFA---KQYINAIKDYELQLVTYKAQLEpvASPAKK----PKVQSGSESVIQEYVD-LRTHYSE 1303
Cdd:pfam03528  162 LEDEMKKAQEDAEKLRSVVmpmEKEIAALKAKLTEAEDKIKELE--ASKMKElnhyLEAEKSCRTDLEMYVAvLNTQKSV 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1304 LTTLTSQYIKFISETLRRMEEEEMQtvqqeqllqeTQALQQSFLSEKDSLLQRERFIEQEKAKL------EQLFQDEVAK 1377
Cdd:pfam03528  240 LQEDAEKLRKELHEVCHLLEQERQQ----------HNQLKHTWQKANDQFLESQRLLMRDMQRMesvltsEQLRQVEEIK 309
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2536-2574 4.65e-04

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 40.00  E-value: 4.65e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2536 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVARLL 2574
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
1540-1577 1.10e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.00  E-value: 1.10e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2462619885  1540 RHYLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTA 1577
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
596-689 1.83e-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: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  596 LHSFVAAATKELMWLNEKEE----EEVGFDWsdrnTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTV 671
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEAllssEDYGKDL----ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90
                   ....*....|....*...
gi 2462619885  672 ESFQAALQTQWSWMLQLC 689
Cdd:pfam00435   79 QERLEELNERWEQLLELA 96
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
819-1376 2.08e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.94  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  819 VLSSSGSEAAVPSVCFLVPPPNQEAQEAVTRLEAQHQALVTLWHQLHVDMKSLlawqslrRDVQLIRSWSLATFRTLKPE 898
Cdd:pfam05483  246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKEL-------EDIKMSLQRSMSTQKALEED 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  899 EQ--RQALHSLELHYQAFLRDSQDAGGfgPEDRLMAEREYGSCShhYQQLLQSleqgaqEESRCQRCISELKDIRLQLEA 976
Cdd:pfam05483  319 LQiaTKTICQLTEEKEAQMEELNKAKA--AHSFVVTEFEATTCS--LEELLRT------EQQRLEKNEDQLKIITMELQK 388
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  977 CETRTVHRLRLPLDKEPARECAQRI-AEQQKAQAEVEGLGKGVARLSAEAEKVLALPEpSPAAPTLRSELELTLGK---- 1051
Cdd:pfam05483  389 KSSELEEMTKFKNNKEVELEELKKIlAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQ-AREKEIHDLEIQLTAIKtsee 467
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1052 --LEQVRSL-SAIYLEKLKTISLvirgTQGAEEVLRAHEEQLKEAQAVPATLP----ELEATKASLKKLRAQAEAQQPTF 1124
Cdd:pfam05483  468 hyLKEVEDLkTELEKEKLKNIEL----TAHCDKLLLENKELTQEASDMTLELKkhqeDIINCKKQEERMLKQIENLEEKE 543
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1125 DALRDELrgaQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLryyresadplgawlQDA 1204
Cdd:pfam05483  544 MNLRDEL---ESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI--------------ENK 606
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1205 RRRQEQIQAmplaDSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKD-YELQLVTYKAQLEPVASPAKKPKV 1283
Cdd:pfam05483  607 NKNIEELHQ----ENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDnYQKEIEDKKISEEKLLEEVEKAKA 682
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1284 QSGSESVIQEYVDLRTHYSelttltsqyikfISETLRRMEEEEMQtvqqeqllqetqalQQSFLSEKDSLLQRERFIEQE 1363
Cdd:pfam05483  683 IADEAVKLQKEIDKRCQHK------------IAEMVALMEKHKHQ--------------YDKIIEERDSELGLYKNKEQE 736
                          570
                   ....*....|...
gi 2462619885 1364 KAKLEQLFQDEVA 1376
Cdd:pfam05483  737 QSSAKAALEIELS 749
PLEC smart00250
Plectin repeat;
2854-2885 4.12e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.46  E-value: 4.12e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2462619885  2854 KLLSAERAVTGYKDPYSGKLISLFQAMKKGLI 2885
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3132-3162 4.47e-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: 4.47e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462619885 3132 AGILDTETLEKVSITEAMHRNLVDNITGQRL 3162
Cdd:pfam00681    9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
 
Name Accession Description Interval E-value
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
19-123 8.49e-77

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: 250.01  E-value: 8.49e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   19 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNI 98
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
                           90       100
                   ....*....|....*....|....*
gi 2462619885   99 RNDDIADGNPKLTLGLIWTIILHFQ 123
Cdd:cd21188     81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
16-134 3.49e-75

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: 245.70  E-value: 3.49e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   16 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 95
Cdd:cd21235      1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462619885   96 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 134
Cdd:cd21235     81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
5-132 8.90e-74

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: 242.20  E-value: 8.90e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885    5 RAIQNEISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIA 84
Cdd:cd21236      1 QAYENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIA 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2462619885   85 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 132
Cdd:cd21236     81 LDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
136-241 1.43e-72

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


Pssm-ID: 409087  Cd Length: 106  Bit Score: 238.00  E-value: 1.43e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  136 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 215
Cdd:cd21238      1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 2462619885  216 PEDVDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
137-241 1.62e-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: 220.34  E-value: 1.62e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  137 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 216
Cdd:cd21189      1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                           90       100
                   ....*....|....*....|....*
gi 2462619885  217 EDVDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21189     81 EDVDVPEPDEKSIITYVSSLYDVFP 105
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
16-133 1.18e-64

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: 215.67  E-value: 1.18e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   16 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 95
Cdd:cd21237      1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462619885   96 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 133
Cdd:cd21237     81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
137-241 2.24e-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: 2.24e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  137 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 216
Cdd:cd21239      1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
                           90       100
                   ....*....|....*....|....*
gi 2462619885  217 EDVDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21239     80 EDVDVSSPDEKSVITYVSSLYDVFP 104
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
135-241 2.23e-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: 180.24  E-value: 2.23e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  135 DMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 214
Cdd:cd21240      2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
                           90       100
                   ....*....|....*....|....*..
gi 2462619885  215 DPEDVDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21240     81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
21-124 8.92e-51

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: 175.65  E-value: 8.92e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   21 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 99
Cdd:cd21186      2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
                           90       100
                   ....*....|....*....|....*
gi 2462619885  100 NDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21186     82 SNDIVDGNPKLTLGLVWSIILHWQV 106
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
11-120 9.46e-50

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: 172.94  E-value: 9.46e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   11 ISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 89
Cdd:cd21246      6 IKALADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLK 85
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462619885   90 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21246     86 EQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
8-120 4.63e-47

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: 165.16  E-value: 4.63e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885    8 QNEISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALD 86
Cdd:cd21193      3 KGRIRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALA 82
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462619885   87 YLrHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21193     83 FL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
20-348 9.06e-47

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 180.14  E-value: 9.06e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   20 RVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLV 96
Cdd:COG5069      8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   97 NIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTSSWRDGRLFNAII 175
Cdd:COG5069     88 NIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALI 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  176 HRHKPLLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS------SLYD----AMPR 242
Cdd:COG5069    165 HDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyiirfGLLEkidiALHR 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  243 VPDVQDGVRANElQLRwQEYRELVLLLLQWMRHHTAAFEERRFPSSFEEIEILWSQFLKFKEME--LPAKEAD-KNRSKG 319
Cdd:COG5069    245 VYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCsrAPLETTDlHSLAGQ 322
                          330       340
                   ....*....|....*....|....*....
gi 2462619885  320 IYQSLEgAVQAGQLKVPPGYHPLDVEKEW 348
Cdd:COG5069    323 ILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
137-237 6.74e-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: 161.43  E-value: 6.74e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  137 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 216
Cdd:cd21194      2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
                           90       100
                   ....*....|....*....|.
gi 2462619885  217 EDVDVPQPDEKSIITYVSSLY 237
Cdd:cd21194     82 EDVDVARPDEKSIMTYVASYY 102
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
17-124 5.44e-45

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: 159.08  E-value: 5.44e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   17 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLRHRQ 92
Cdd:cd21241      1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2462619885   93 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21241     81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
17-124 4.37e-44

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: 156.58  E-value: 4.37e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   17 ERDRVQKKTFTKWVNKHLikaQRH-----ISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 89
Cdd:cd21190      1 EQERVQKKTFTNWINSHL---AKLsqpivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462619885   90 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21190     78 KRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
137-237 4.59e-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: 4.59e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  137 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 216
Cdd:cd21248      2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
                           90       100
                   ....*....|....*....|.
gi 2462619885  217 EDVDVPQPDEKSIITYVSSLY 237
Cdd:cd21248     82 EDVNVEQPDEKSIITYVVTYY 102
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
9-120 1.79e-42

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: 153.26  E-value: 1.79e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885    9 NEISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDY 87
Cdd:cd21318     26 SRIKALADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQF 105
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2462619885   88 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21318    106 LKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
136-241 5.80e-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: 150.55  E-value: 5.80e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  136 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 215
Cdd:cd21243      4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
                           90       100
                   ....*....|....*....|....*.
gi 2462619885  216 PEDVDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21243     84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
8-120 1.05e-41

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: 150.59  E-value: 1.05e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885    8 QNEISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALD 86
Cdd:cd21317     18 RSRIKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQ 97
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462619885   87 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21317     98 FLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
124-239 5.33e-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: 147.89  E-value: 5.33e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  124 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 203
Cdd:cd21216      1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462619885  204 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 239
Cdd:cd21216     77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
19-120 2.07e-39

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: 142.91  E-value: 2.07e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   19 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVKLVN 97
Cdd:cd21214      3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
                           90       100
                   ....*....|....*....|...
gi 2462619885   98 IRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21214     83 IGAEEIVDGNLKMTLGMIWTIIL 105
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
17-124 8.88e-39

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: 141.51  E-value: 8.88e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   17 ERDRVQKKTFTKWVNKHLIKAQ--RHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 94
Cdd:cd21242      1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 2462619885   95 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21242     81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
133-237 1.36e-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: 140.91  E-value: 1.36e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  133 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 212
Cdd:cd21319      1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
                           90       100
                   ....*....|....*....|....*
gi 2462619885  213 LLDPEDVDVPQPDEKSIITYVSSLY 237
Cdd:cd21319     81 LLDPEDVFTENPDEKSIITYVVAFY 105
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
21-122 1.41e-38

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: 140.61  E-value: 1.41e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   21 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 98
Cdd:cd21215      4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
                           90       100
                   ....*....|....*....|....
gi 2462619885   99 RNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21215     84 GAEDIVDGNLKLILGLLWTLILRF 107
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
133-237 5.00e-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: 139.42  E-value: 5.00e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  133 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 212
Cdd:cd21321      1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
                           90       100
                   ....*....|....*....|....*
gi 2462619885  213 LLDPEDVDVPQPDEKSIITYVSSLY 237
Cdd:cd21321     81 LLDPEDVNVDQPDEKSIITYVATYY 105
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
16-124 1.93e-37

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: 137.75  E-value: 1.93e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   16 DERDRVQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 94
Cdd:cd21231      1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 2462619885   95 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21231     81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
136-237 2.76e-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: 2.76e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  136 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 215
Cdd:cd21249      3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
                           90       100
                   ....*....|....*....|..
gi 2462619885  216 PEDVDVPQPDEKSIITYVSSLY 237
Cdd:cd21249     83 PEDVAVPHPDERSIMTYVSLYY 104
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
121-237 4.09e-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: 4.09e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  121 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQA 200
Cdd:cd21322      1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462619885  201 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 237
Cdd:cd21322     81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
140-241 1.13e-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: 1.13e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  140 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 218
Cdd:cd21187      2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
                           90       100
                   ....*....|....*....|...
gi 2462619885  219 VDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21187     82 VNVEQPDKKSILMYVTSLFQVLP 104
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
8-120 8.77e-35

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: 131.70  E-value: 8.77e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885    8 QNEISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALD 86
Cdd:cd21316     40 RSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQ 119
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462619885   87 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 120
Cdd:cd21316    120 FLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
20-125 2.71e-34

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: 129.11  E-value: 2.71e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQ-VKLV 96
Cdd:cd21311     14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
                           90       100
                   ....*....|....*....|....*....
gi 2462619885   97 NIRNDDIADGNPKLTLGLIWTIILHFQIS 125
Cdd:cd21311     94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
21-124 2.56e-33

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: 125.86  E-value: 2.56e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   21 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 98
Cdd:cd21227      4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
                           90       100
                   ....*....|....*....|....*.
gi 2462619885   99 RNDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21227     84 GNEDIVNGNLKLILGLIWHLILRYQI 109
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
136-234 3.22e-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: 3.22e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  136 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 215
Cdd:cd21192      2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
                           90
                   ....*....|....*....
gi 2462619885  216 PEDVDVPQPDEKSIITYVS 234
Cdd:cd21192     82 VEDVLVDKPDERSIMTYVS 100
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
21-124 1.28e-32

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: 123.58  E-value: 1.28e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   21 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 99
Cdd:cd21232      2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
                           90       100
                   ....*....|....*....|....*
gi 2462619885  100 NDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21232     82 GTDIVDGNHKLTLGLLWSIILHWQV 106
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
137-237 1.39e-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: 1.39e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  137 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 216
Cdd:cd21320      2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
                           90       100
                   ....*....|....*....|.
gi 2462619885  217 EDVDVPQPDEKSIITYVSSLY 237
Cdd:cd21320     82 EDISVDHPDEKSIITYVVTYY 102
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
136-234 6.29e-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: 6.29e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  136 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 215
Cdd:cd21244      4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
                           90
                   ....*....|....*....
gi 2462619885  216 PEDVDVPQPDEKSIITYVS 234
Cdd:cd21244     84 PEDVDVVNPDEKSIMTYVA 102
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
124-239 2.45e-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: 120.33  E-value: 2.45e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  124 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 203
Cdd:cd21291      1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462619885  204 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 239
Cdd:cd21291     77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
140-241 3.91e-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: 3.91e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  140 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 218
Cdd:cd21234      2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
                           90       100
                   ....*....|....*....|...
gi 2462619885  219 VDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21234     82 VAVQLPDKKSIIMYLTSLFEVLP 104
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
17-126 4.11e-31

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: 119.61  E-value: 4.11e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   17 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQ 92
Cdd:cd21191      1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462619885   93 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 126
Cdd:cd21191     81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
140-242 6.32e-31

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


Pssm-ID: 409082  Cd Length: 111  Bit Score: 118.88  E-value: 6.32e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  140 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 217
Cdd:cd21233      2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
                           90       100
                   ....*....|....*....|....*
gi 2462619885  218 DVDVPQPDEKSIITYVSSLYDAMPR 242
Cdd:cd21233     82 DVATAHPDKKSILMYVTSLFQVLPQ 106
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
872-949 6.41e-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: 117.70  E-value: 6.41e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619885  872 LAWQSLRRDVQLIRSWSLATFRTLKPEEQRQALHSLELHYQAFLRDSQDAGGFGPEDRLMAEREYGSCSHHYQQLLQS 949
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
20-122 2.83e-30

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: 116.81  E-value: 2.83e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21183      3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
                           90       100
                   ....*....|....*....|....*.
gi 2462619885   97 NIRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21183     83 NIGSGDIVNGNIKLILGLIWTLILHY 108
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
142-237 3.09e-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: 116.68  E-value: 3.09e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  142 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 220
Cdd:cd21253      6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
                           90
                   ....*....|....*..
gi 2462619885  221 VPQPDEKSIITYVSSLY 237
Cdd:cd21253     86 LKVPDKLSILTYVSQYY 102
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
122-239 8.15e-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: 8.15e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  122 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAF 201
Cdd:cd21290      2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462619885  202 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 239
Cdd:cd21290     78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
140-239 1.35e-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: 111.99  E-value: 1.35e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  140 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 218
Cdd:cd22198      3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
                           90       100
                   ....*....|....*....|.
gi 2462619885  219 VDVPQPDEKSIITYVSSLYDA 239
Cdd:cd22198     83 ASLAVPDKLSMVSYLSQFYEA 103
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
20-122 5.81e-28

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: 110.27  E-value: 5.81e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21228      3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
                           90       100
                   ....*....|....*....|....*.
gi 2462619885   97 NIRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21228     83 SIDSSAIVDGNLKLILGLIWTLILHY 108
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
124-239 1.02e-27

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: 110.18  E-value: 1.02e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  124 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 203
Cdd:cd21287      1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462619885  204 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 239
Cdd:cd21287     77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
11-124 2.06e-27

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


Pssm-ID: 409096  Cd Length: 125  Bit Score: 109.46  E-value: 2.06e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   11 ISSLKDERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDY 87
Cdd:cd21247     10 IRKLQEQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITF 89
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462619885   88 LRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21247     90 LKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
20-125 2.40e-27

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: 109.35  E-value: 2.40e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21310     15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
                           90       100
                   ....*....|....*....|....*....
gi 2462619885   97 NIRNDDIADGNPKLTLGLIWTIILHFQIS 125
Cdd:cd21310     95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
124-239 2.80e-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: 2.80e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  124 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 203
Cdd:cd21289      1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462619885  204 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 239
Cdd:cd21289     77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
124-239 9.27e-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: 9.27e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  124 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 203
Cdd:cd21288      1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462619885  204 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 239
Cdd:cd21288     77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
24-121 1.63e-25

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: 103.16  E-value: 1.63e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885    24 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKLVNIR 99
Cdd:smart00033    1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 2462619885   100 NDDIADGnPKLTLGLIWTIILH 121
Cdd:smart00033   81 PEDLVEG-PKLILGVIWTLISL 101
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
142-237 1.83e-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: 103.00  E-value: 1.83e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  142 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 220
Cdd:cd21197      5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
                           90
                   ....*....|....*..
gi 2462619885  221 VPQPDEKSIITYVSSLY 237
Cdd:cd21197     85 MHVPDRLSIITYVSQYY 101
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
140-240 5.52e-25

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


Pssm-ID: 409075  Cd Length: 103  Bit Score: 101.77  E-value: 5.52e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  140 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 219
Cdd:cd21226      3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
                           90       100
                   ....*....|....*....|.
gi 2462619885  220 DVPQPDEKSIITYVSSLYDAM 240
Cdd:cd21226     83 MTGNPDERSIVLYTSLFYHAF 103
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
136-242 9.20e-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: 101.21  E-value: 9.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  136 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 212
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462619885  213 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 242
Cdd:pfam00307   81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
21-124 1.66e-24

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: 100.44  E-value: 1.66e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   21 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-VKLV 96
Cdd:pfam00307    2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
                           90       100
                   ....*....|....*....|....*...
gi 2462619885   97 NIRNDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:pfam00307   82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
138-237 4.27e-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: 4.27e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  138 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 217
Cdd:cd21252      1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
                           90       100
                   ....*....|....*....|.
gi 2462619885  218 D-VDVPQPDEKSIITYVSSLY 237
Cdd:cd21252     81 DmVSMKVPDCLSIMTYVSQYY 101
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
137-241 4.34e-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: 4.34e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  137 TAKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 216
Cdd:cd21245      3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
                           90       100
                   ....*....|....*....|....*
gi 2462619885  217 EDVDVPQPDEKSIITYVSSLYDAMP 241
Cdd:cd21245     82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
137-237 2.91e-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: 96.73  E-value: 2.91e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  137 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 216
Cdd:cd21198      1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
                           90       100
                   ....*....|....*....|..
gi 2462619885  217 EDVDVPQ-PDEKSIITYVSSLY 237
Cdd:cd21198     80 ADMVLLSvPDKLSVMTYLHQIR 101
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
20-125 4.81e-23

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: 97.08  E-value: 4.81e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21308     19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
                           90       100
                   ....*....|....*....|....*....
gi 2462619885   97 NIRNDDIADGNPKLTLGLIWTIILHFQIS 125
Cdd:cd21308     99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
20-125 6.23e-23

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: 97.07  E-value: 6.23e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   20 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21309     16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
                           90       100
                   ....*....|....*....|....*....
gi 2462619885   97 NIRNDDIADGNPKLTLGLIWTIILHFQIS 125
Cdd:cd21309     96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
137-235 3.10e-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: 93.84  E-value: 3.10e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  137 TAKEKLLLWSQRMVEGYqglRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 215
Cdd:cd21184      1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
                           90       100
                   ....*....|....*....|
gi 2462619885  216 PEDVDVPQPDEKSIITYVSS 235
Cdd:cd21184     78 PEDMVSPNVDELSVMTYLSY 97
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
771-837 4.67e-22

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 91.94  E-value: 4.67e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462619885  771 QLKPRhpAHPMRGRLPLLAVCDYKQVEVTVHKGDECQLVGPAQPSHWKVLSSSGSEAAVPSVCFLVP 837
Cdd:pfam17902    1 PLKQR--RSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
141-238 2.50e-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: 88.56  E-value: 2.50e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  141 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 219
Cdd:cd21195      8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
                           90
                   ....*....|....*....
gi 2462619885  220 DVPQPDEKSIITYVSSLYD 238
Cdd:cd21195     88 SAQEPDKLSMVMYLSKFYE 106
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
137-237 3.87e-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: 3.87e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  137 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 216
Cdd:cd21200      1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
                           90       100
                   ....*....|....*....|...
gi 2462619885  217 EDVDV--PQPDEKSIITYVSSLY 237
Cdd:cd21200     81 EDMVRmgNRPDWKCVFTYVQSLY 103
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
133-238 1.24e-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: 1.24e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  133 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 212
Cdd:cd21251      1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
                           90       100
                   ....*....|....*....|....*..
gi 2462619885  213 LLDPEDV-DVPQPDEKSIITYVSSLYD 238
Cdd:cd21251     81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
137-236 2.65e-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: 85.61  E-value: 2.65e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  137 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 216
Cdd:cd21255      1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
                           90       100
                   ....*....|....*....|.
gi 2462619885  217 ED-VDVPQPDEKSIITYVSSL 236
Cdd:cd21255     80 ADmVLLPIPDKLIVMTYLCQL 100
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
140-236 3.47e-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: 85.06  E-value: 3.47e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   140 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 215
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 2462619885   216 PEDVDVPQPDEKSIITYVSSL 236
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
22-122 7.45e-19

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


Pssm-ID: 409061  Cd Length: 105  Bit Score: 84.17  E-value: 7.45e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   22 QKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVKLVN 97
Cdd:cd21212      1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
                           90       100
                   ....*....|....*....|....*
gi 2462619885   98 IRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21212     81 ITAEDIVDGNLKAILGLFFSLSRYK 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
596-785 1.11e-18

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: 87.50  E-value: 1.11e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  596 LHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQ 675
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  676 AALQTQWSWMLQLCCCIEAHLKENAAYFQFFSDVREAEGQLQKLQEALRrkySCDRSATVTRLEDLLQDAQDEKEQLNEY 755
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190
                   ....*....|....*....|....*....|
gi 2462619885  756 KGHLSGLAKRAKAVVQLKPRHPAHPMRGRL 785
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
23-120 2.46e-18

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: 82.77  E-value: 2.46e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   23 KKTFTKWVNKHL-IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQV-KLVNI 98
Cdd:cd00014      1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
                           90       100
                   ....*....|....*....|...
gi 2462619885   99 RNDDI-ADGNPKLTLGLIWTIIL 120
Cdd:cd00014     81 EPEDLyEKGNLKKVLGTLWALAL 103
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
141-238 3.27e-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: 3.27e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  141 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 219
Cdd:cd21250      8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
                           90
                   ....*....|....*....
gi 2462619885  220 DVPQPDEKSIITYVSSLYD 238
Cdd:cd21250     88 SAEEPDKLSMVMYLSKFYE 106
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
137-236 3.94e-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: 79.51  E-value: 3.94e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  137 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 216
Cdd:cd21254      1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
                           90       100
                   ....*....|....*....|.
gi 2462619885  217 ED-VDVPQPDEKSIITYVSSL 236
Cdd:cd21254     80 SDmVLLAVPDKLTVMTYLYQI 100
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
139-250 1.51e-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: 78.11  E-value: 1.51e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  139 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 218
Cdd:cd21259      3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2462619885  219 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 250
Cdd:cd21259     83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
142-237 4.64e-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: 76.63  E-value: 4.64e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  142 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 220
Cdd:cd21199     13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
                           90
                   ....*....|....*..
gi 2462619885  221 VPQPDEKSIITYVSSLY 237
Cdd:cd21199     92 MERPDWQSVMSYVTAIY 108
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
139-238 6.41e-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: 6.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  139 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 218
Cdd:cd21261      3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
                           90       100
                   ....*....|....*....|..
gi 2462619885  219 VDV--PQPDEKSIITYVSSLYD 238
Cdd:cd21261     83 MMVmgRKPDPMCVFTYVQSLYN 104
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2893-2931 9.10e-16

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 73.13  E-value: 9.10e-16
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2893 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 2931
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
139-242 1.04e-15

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: 75.47  E-value: 1.04e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  139 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 218
Cdd:cd21258      3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
                           90       100
                   ....*....|....*....|....*.
gi 2462619885  219 VDV--PQPDEKSIITYVSSLYDAMPR 242
Cdd:cd21258     83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
19-118 1.09e-15

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


Pssm-ID: 409074  Cd Length: 111  Bit Score: 75.65  E-value: 1.09e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   19 DRVQKKTFTKWVNKHLIKAQ-RHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHR-QV 93
Cdd:cd21225      2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
                           90       100
                   ....*....|....*....|....*
gi 2462619885   94 KLVNIRNDDIADGNPKLTLGLIWTI 118
Cdd:cd21225     82 RVQGIGAEDFVDNNKKLILGLLWTL 106
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1656-1694 3.67e-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: 3.67e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 1656 LLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEMNRVL 1694
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2574-2612 3.71e-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: 3.71e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2574 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 2612
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
22-122 4.60e-15

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


Pssm-ID: 409062  Cd Length: 107  Bit Score: 73.49  E-value: 4.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   22 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRHRQV 93
Cdd:cd21213      1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
                           90       100
                   ....*....|....*....|....*....
gi 2462619885   94 KLVNIRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21213     77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2315-2353 6.72e-15

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 70.82  E-value: 6.72e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2315 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEMNRVL 2353
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
16-121 9.40e-15

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 72.70  E-value: 9.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   16 DERDrvqKKTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHKLQNVQIAL 85
Cdd:cd21219      2 GSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVENCNYAV 71
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2462619885   86 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 121
Cdd:cd21219     72 DLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1080-1270 1.30e-14

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 75.56  E-value: 1.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1080 EEVLRAHEEQLKEAQaVPATLPELEATKASLKKLRAQAEAQQPTFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1159
Cdd:cd00176     13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1160 AQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLGAWLQDArrrQEQIQAMPLADS-QAVREQLRQEQALLEEIER 1238
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEK---EAALASEDLGKDlESVEELLKKHKELEEELEA 157
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2462619885 1239 HGEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1270
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
137-237 1.37e-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: 1.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  137 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 216
Cdd:cd21256     14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
                           90       100
                   ....*....|....*....|..
gi 2462619885  217 ED-VDVPQPDEKSIITYVSSLY 237
Cdd:cd21256     93 NEmVRTERPDWQSVMTYVTAIY 114
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
139-240 1.83e-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: 72.04  E-value: 1.83e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  139 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 218
Cdd:cd21260      3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
                           90       100
                   ....*....|....*....|...
gi 2462619885  219 -VDVPQPDEKSIITYVSSLYDAM 240
Cdd:cd21260     83 mVRMSVPDSKCVYTYIQELYRSL 105
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
137-234 5.61e-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: 70.49  E-value: 5.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  137 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 215
Cdd:cd21230      1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPgLCPDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
                           90
                   ....*....|....*....
gi 2462619885  216 PEDVDVPQPDEKSIITYVS 234
Cdd:cd21230     78 PEEIINPNVDEMSVMTYLS 96
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
500-689 6.02e-14

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 73.63  E-value: 6.02e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  500 LRYLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARSDEGQLSPATRGAY---RDCLGRLD 576
Cdd:cd00176      6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  577 LQYAKLLNSSKARLRSLE---SLHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKEL 653
Cdd:cd00176     86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462619885  654 QNAGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 689
Cdd:cd00176    166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
137-237 1.24e-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: 69.67  E-value: 1.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  137 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 216
Cdd:cd21257      8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
                           90       100
                   ....*....|....*....|..
gi 2462619885  217 ED-VDVPQPDEKSIITYVSSLY 237
Cdd:cd21257     87 SEmMYTDRPDWQSVMQYVAQIY 108
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1908-1946 1.36e-13

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 66.97  E-value: 1.36e-13
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 1908 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEFHEKL 1946
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
40-119 3.54e-13

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: 68.39  E-value: 3.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   40 HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQV----KLVNIRNDDIADGNPKLT 111
Cdd:cd21223     25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104

                   ....*...
gi 2462619885  112 LGLIWTII 119
Cdd:cd21223    105 LALLWRII 112
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3162-3200 1.28e-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: 1.28e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 3162 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 3200
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
24-125 1.44e-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: 66.88  E-value: 1.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   24 KTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21298      9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
                           90       100
                   ....*....|....*....|....*....
gi 2462619885   97 NIRNDDIADGNPKLTLGLIWTIILHFQIS 125
Cdd:cd21298     87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1984-2022 1.93e-12

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.89  E-value: 1.93e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 1984 LLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEETSRAL 2022
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1580-1618 2.21e-12

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.50  E-value: 2.21e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 1580 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHKL 1618
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
139-234 2.25e-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: 65.87  E-value: 2.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  139 KEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 217
Cdd:cd21229      5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPgLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
                           90
                   ....*....|....*..
gi 2462619885  218 DVDVPQPDEKSIITYVS 234
Cdd:cd21229     82 DLSSPHLDELSGMTYLS 98
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2817-2855 2.85e-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: 2.85e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2817 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 2855
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
139-239 2.87e-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: 65.45  E-value: 2.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  139 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 218
Cdd:cd21196      5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
                           90       100
                   ....*....|....*....|.
gi 2462619885  219 VdVPQPDEKSIITYVSSLYDA 239
Cdd:cd21196     85 V-VAGSDPLGLIAYLSHFHSA 104
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2650-2688 3.05e-12

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.12  E-value: 3.05e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2650 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 2688
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
139-238 3.16e-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: 65.44  E-value: 3.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  139 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 214
Cdd:cd00014      1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
                           90       100
                   ....*....|....*....|....
gi 2462619885  215 DPEDVdVPQPDEKSIITYVSSLYD 238
Cdd:cd00014     81 EPEDL-YEKGNLKKVLGTLWALAL 103
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
17-116 5.37e-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: 5.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   17 ERDRvQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQNVQIALDYL 88
Cdd:cd21300      4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYAVELG 80
                           90       100
                   ....*....|....*....|....*...
gi 2462619885   89 RHRQVKLVNIRNDDIADGNPKLTLGLIW 116
Cdd:cd21300     81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3238-3276 9.99e-11

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 58.88  E-value: 9.99e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 3238 FLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTAQKL 3276
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
23-119 2.77e-10

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


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 60.28  E-value: 2.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   23 KKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDYL 88
Cdd:cd21217      3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462619885   89 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 119
Cdd:cd21217     83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
14-122 5.41e-10

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: 59.52  E-value: 5.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   14 LKDERDRVQ--KKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNVQIALDY 87
Cdd:cd21222      7 FDEAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALEL 86
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462619885   88 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21222     87 MEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
944-1274 1.05e-09

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: 64.70  E-value: 1.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  944 QQLLQSLEQGAQEESRCQRCISELKDirlQLEACETRTVHRLRLPLDKEPARECAQ--RIAEQQKAQAEVEGLGKGVARL 1021
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKAERYQALLKEKREYEGyeLLKEKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1022 SAEAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRGTQG----AEEVLRAHEEQLKE 1092
Cdd:TIGR02169  250 EEELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELED 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1093 AQAVPATL-PELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQllerwqavla 1171
Cdd:TIGR02169  320 AEERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------- 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1172 qtdvRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQamplADSQAVREQLRQEQALLEEIerhGEKVEECQRFAK 1251
Cdd:TIGR02169  390 ----YREKLEKLKREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEKEDK---ALEIKKQEWKLE 458
                          330       340
                   ....*....|....*....|...
gi 2462619885 1252 QYINAIKDYELQLVTYKAQLEPV 1274
Cdd:TIGR02169  459 QLAADLSKYEQELYDLKEEYDRV 481
PLEC smart00250
Plectin repeat;
3160-3197 1.13e-09

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 55.95  E-value: 1.13e-09
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2462619885  3160 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 3197
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
137-239 1.36e-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: 1.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  137 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 215
Cdd:cd21314     11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPgLCPDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
                           90       100
                   ....*....|....*....|....
gi 2462619885  216 PEDVDVPQPDEKSIITYVSSLYDA 239
Cdd:cd21314     88 PEEIVDPNVDEHSVMTYLSQFPKA 111
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
22-121 4.04e-09

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: 56.74  E-value: 4.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   22 QKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21299      5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
                           90       100
                   ....*....|....*....|....*
gi 2462619885   97 NIRNDDIADGNPKLTLGLIWTIILH 121
Cdd:cd21299     83 NVAGNDIVQGNKKLILALLWQLMRY 107
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
132-234 4.97e-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: 4.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  132 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 210
Cdd:cd21315     11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPgLCPDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
                           90       100
                   ....*....|....*....|....
gi 2462619885  211 TRLLDPEDVDVPQPDEKSIITYVS 234
Cdd:cd21315     88 PQLIKPEEMVNPKVDELSMMTYLS 111
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
132-239 1.26e-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: 1.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  132 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 210
Cdd:cd21313      3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPgLCPDWESWDPQKPVDNAREAMQQADDWLGV 79
                           90       100
                   ....*....|....*....|....*....
gi 2462619885  211 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 239
Cdd:cd21313     80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
24-118 2.09e-08

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


Pssm-ID: 409135  Cd Length: 105  Bit Score: 54.65  E-value: 2.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   24 KTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQVKL 95
Cdd:cd21286      3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARGVNV 78
                           90       100
                   ....*....|....*....|...
gi 2462619885   96 VNIRNDDIADGNPKLTLGLIWTI 118
Cdd:cd21286     79 QGLSAEEIRNGNLKAILGLFFSL 101
PLEC smart00250
Plectin repeat;
2891-2927 2.18e-08

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 52.10  E-value: 2.18e-08
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  2891 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 2927
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
141-236 3.30e-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: 55.00  E-value: 3.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  141 KLLL-WSQrMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNL-----------------------EN 196
Cdd:cd21224      3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462619885  197 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 236
Cdd:cd21224     82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
892-1460 3.38e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 3.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  892 FRTLKPEEQRQALHSLELHYQAFLRDSQDAGgfgpEDRLMAEREYGSCSHHYQQLLQSLEQGAQEESRCQRCISELKDIR 971
Cdd:COG1196    215 YRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  972 LQLEACETRTVHRLRLplDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALpepspAAPTLRSELELTLGK 1051
Cdd:COG1196    291 YELLAELARLEQDIAR--LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-----AEEELEEAEAELAEA 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1052 LEQVRSLSAIYLEKLKTISlviRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDEL 1131
Cdd:COG1196    364 EEALLEAEAELAEAEEELE---ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1132 RGAQEvgeRLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQI 1211
Cdd:COG1196    441 EEALE---EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1212 QAMPLAdsQAVREQLRQEQALLEEIE-----RHGEKVEECQRFAKQYINAIKDYELQLVTY--KAQLEPVASPAKKPKVQ 1284
Cdd:COG1196    518 GLRGLA--GAVAVLIGVEAAYEAALEaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpLDKIRARAALAAALARG 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1285 SGSESVIQEYVDLRTH---------YSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALQQSFLSEKDSLLQ 1355
Cdd:COG1196    596 AIGAAVDLVASDLREAdaryyvlgdTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1356 RERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQE 1435
Cdd:COG1196    676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
                          570       580
                   ....*....|....*....|....*
gi 2462619885 1436 ELLAEENQRLREQLQLLEEQhRAAL 1460
Cdd:COG1196    756 LPEPPDLEELERELERLERE-IEAL 779
SPEC smart00150
Spectrin repeats;
597-689 5.71e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.10  E-value: 5.71e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   597 HSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQA 676
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90
                    ....*....|...
gi 2462619885   677 ALQTQWSWMLQLC 689
Cdd:smart00150   81 ELNERWEELKELA 93
PLEC smart00250
Plectin repeat;
2572-2607 1.67e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 49.79  E-value: 1.67e-07
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 2462619885  2572 RLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPE 2607
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
17-124 1.74e-07

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: 52.70  E-value: 1.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   17 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRMRFHKLQNVQIALDYLR 89
Cdd:cd21331     18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVELGK 95
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2462619885   90 HR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 124
Cdd:cd21331     96 HPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2994-3022 3.71e-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: 3.71e-07
                           10        20
                   ....*....|....*....|....*....
gi 2462619885 2994 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 3022
Cdd:pfam00681   11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
2777-2814 5.81e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 48.25  E-value: 5.81e-07
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2462619885  2777 QKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTA 2814
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
1654-1690 1.10e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 47.48  E-value: 1.10e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  1654 IRLLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEM 1690
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
22-130 1.85e-06

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


Pssm-ID: 409174  Cd Length: 148  Bit Score: 50.06  E-value: 1.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   22 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 88
Cdd:cd21325     25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462619885   89 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 130
Cdd:cd21325    105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
132-239 2.23e-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: 2.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  132 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 210
Cdd:cd21312      7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPgLCPDWDSWDASKPVTNAREAMQQADDWLGI 83
                           90       100
                   ....*....|....*....|....*....
gi 2462619885  211 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 239
Cdd:cd21312     84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2245-2277 2.27e-06

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 46.55  E-value: 2.27e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462619885 2245 ATGFLVDPVRNQRLYVHEAVKAGVVGPELHEQL 2277
Cdd:pfam00681    7 ATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
1945-1981 2.31e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.32  E-value: 2.31e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  1945 KLLSAEKAVTGYRDPYTGQSVSLFQALKKGLIPREQG 1981
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2313-2349 2.66e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.32  E-value: 2.66e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  2313 IRLLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEM 2349
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
22-129 2.85e-06

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


Pssm-ID: 409172  Cd Length: 145  Bit Score: 49.66  E-value: 2.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   22 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 88
Cdd:cd21323     25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2462619885   89 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 129
Cdd:cd21323    105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
19-118 2.94e-06

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: 48.81  E-value: 2.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   19 DRVQKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHRQVK 94
Cdd:cd21285      8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
                           90       100
                   ....*....|....*....|....
gi 2462619885   95 LVNIRNDDIADGNPKLTLGLIWTI 118
Cdd:cd21285     88 IQGLSAEEIRNGNLKAILGLFFSL 111
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1083-1245 3.07e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 3.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1083 LRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRH---GERDVEVERWRERV 1159
Cdd:COG4717     73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEaleAELAELPERLEELE 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1160 AQlLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPlgAWLQDARRRQEQIqampladsQAVREQLRQEQALLEEIERH 1239
Cdd:COG4717    153 ER-LEELRELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEEL--------EELQQRLAELEEELEEAQEE 221

                   ....*.
gi 2462619885 1240 GEKVEE 1245
Cdd:COG4717    222 LEELEE 227
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1044-1260 3.11e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 3.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1044 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLkklraqaEAQQPT 1123
Cdd:COG4913    614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-------DASSDD 686
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1124 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLlerwqavlaqtdvrQRELEQLGRQLRYYRESADPLGAWLQD 1203
Cdd:COG4913    687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLELRALLE 752
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462619885 1204 ARRRQEQIQAMPladsQAVREQLRQEQ-ALLEEIERHGEKVEEC-QRFAKQYINAIKDY 1260
Cdd:COG4913    753 ERFAAALGDAVE----RELRENLEERIdALRARLNRAEEELERAmRAFNREWPAETADL 807
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2779-2817 4.61e-06

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 45.78  E-value: 4.61e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2779 FLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTAFEL 2817
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
941-1584 8.38e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 8.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  941 HHYQQLLQSLeqgAQEESRCQRCISELKDIRLQLEACETRTVHRLrlpLDKEPARECAQRIAEQQKAQAEVegLGKGVAR 1020
Cdd:TIGR02168  284 EELQKELYAL---ANEISRLEQQKQILRERLANLERQLEELEAQL---EELESKLDELAEELAELEEKLEE--LKEELES 355
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1021 LSAEAEKVLALpepSPAAPTLRSELEltlgklEQVRSLSAIYLEKLKTISLvIRGTQgaeEVLRAHEEQLKEAQAVPATl 1100
Cdd:TIGR02168  356 LEAELEELEAE---LEELESRLEELE------EQLETLRSKVAQLELQIAS-LNNEI---ERLEARLERLEDRRERLQQ- 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1101 pelEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERwqavLAQTDVRQREL 1180
Cdd:TIGR02168  422 ---EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE----LAQLQARLDSL 494
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1181 EQLGRQLRYYRESAdplgAWLQDARRRQEQIQAmPLADSQAVREQLrqEQALLEEIERHGEKVE-ECQRFAKQYINAIKD 1259
Cdd:TIGR02168  495 ERLQENLEGFSEGV----KALLKNQSGLSGILG-VLSELISVDEGY--EAAIEAALGGRLQAVVvENLNAAKKAIAFLKQ 567
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1260 YELQLVTYKA--QLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSE----LTTLTSQYikFISETL-------RRMEEEE 1326
Cdd:TIGR02168  568 NELGRVTFLPldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkaLSYLLGGV--LVVDDLdnalelaKKLRPGY 645
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1327 MQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEA 1406
Cdd:TIGR02168  646 RIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEEL-EEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1407 RRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQR---LREQLQLLEEQHRAALAHSEEVTASQVAATKTLPNGRDA 1483
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1484 LDGPAAEAEpEHSFDGLRRKVSAQRLQEAGILSAEELQRLAQghTTVDELARREDVRHYLQGRSSIAGLLLKATNEKLSV 1563
Cdd:TIGR02168  805 LDELRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEE--QIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
                          650       660
                   ....*....|....*....|.
gi 2462619885 1564 YAALQRQLLSPGTALILLEAQ 1584
Cdd:TIGR02168  882 RASLEEALALLRSELEELSEE 902
PLEC smart00250
Plectin repeat;
2987-3015 1.26e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.26e-05
                            10        20
                    ....*....|....*....|....*....
gi 2462619885  2987 VRKRRVVIVDPETGKEMSVYEAYRKGLID 3015
Cdd:smart00250    6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
PLEC smart00250
Plectin repeat;
1617-1653 1.28e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.28e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  1617 KLLSAERAVTGYKDPYTGQQISLFQAMQKGLIVREHG 1653
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
414-1245 1.51e-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: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  414 GEVERDLDKADSMIRLLFNDVQTLKDGRhpqgEQMYRrvYR-LHERLvaIRTEYNLRLKAgVAAPATQVAQVTLQSVQRR 492
Cdd:TIGR02169  180 EEVEENIERLDLIIDEKRQQLERLRRER----EKAER--YQaLLKEK--REYEGYELLKE-KEALERQKEAIERQLASLE 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  493 PELEDSTLRyLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGshrgLHQSIEEFRAKIERARS------DEGQLSPATRG 566
Cdd:TIGR02169  251 EELEKLTEE-ISELEKRLEEIEQLLEELNKKIKDLGEEEQLR----VKEKIGELEAEIASLERsiaekeRELEDAEERLA 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  567 AYRDCLGRLDLQYAKLLNSSKARLRSLESLHSFVAAATKELMWL-NEKEEEEVGFDwsdrntnmtAKKESYSALMRELEL 645
Cdd:TIGR02169  326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLrAELEEVDKEFA---------ETRDELKDYREKLEK 396
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  646 KEKKIKELQNAGDRLLREDHPARPTVESFQAALQTQWSWMLQLccciEAHLKENAAyfqffsDVREAEGQLQKLQE---A 722
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL----EEEKEDKAL------EIKKQEWKLEQLAAdlsK 466
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  723 LRRKYScDRSATVTRLEDLLQDAQDEKEQLN---------------------------------------EYKGHL-SGL 762
Cdd:TIGR02169  467 YEQELY-DLKEEYDRVEKELSKLQRELAEAEaqaraseervrggraveevlkasiqgvhgtvaqlgsvgeRYATAIeVAA 545
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  763 AKRAKAVV-----------QLKPRHPAhpmrGRLPLLAVCDYKQVEVTVHKGDECQLVGPA----------QPSHWKVLS 821
Cdd:TIGR02169  546 GNRLNNVVveddavakeaiELLKRRKA----GRATFLPLNKMRDERRDLSILSEDGVIGFAvdlvefdpkyEPAFKYVFG 621
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  822 SSGseaavpsvcfLVpppnqEAQEAVTRLEAQHQaLVTLWHQLhVDMKSLLAWQSLRRDVQLIRSwslatfRTLKPEEQR 901
Cdd:TIGR02169  622 DTL----------VV-----EDIEAARRLMGKYR-MVTLEGEL-FEKSGAMTGGSRAPRGGILFS------RSEPAELQR 678
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  902 QA--LHSLElhyqaflrdsqdaggfGPEDRLMAEREygscshHYQQLLQSLEqgaQEESRCQRCISELKDIRLQLEACET 979
Cdd:TIGR02169  679 LRerLEGLK----------------RELSSLQSELR------RIENRLDELS---QELSDASRKIGEIEKEIEQLEQEEE 733
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  980 RTVHRLRLPLDK--EPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPSP---------AAPTLRSELELT 1048
Cdd:TIGR02169  734 KLKERLEELEEDlsSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelsKLEEEVSRIEAR 813
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1049 LGKLEQV---RSLSAIYLEKLKtislvirgtQGAEEVLRAHEEQLKE-AQAVPATLPELEATKASLKKLRAQAEAQQPTF 1124
Cdd:TIGR02169  814 LREIEQKlnrLTLEKEYLEKEI---------QELQEQRIDLKEQIKSiEKEIENLNGKKEELEEELEELEAALRDLESRL 884
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1125 DALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDvrqrELEQLGRQLRYYRESADPLGAWLQDA 1204
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLEDVQAEL 960
                          890       900       910       920
                   ....*....|....*....|....*....|....*....|.
gi 2462619885 1205 RRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHgEKVEE 1245
Cdd:TIGR02169  961 QRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKR-AKLEE 1000
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
22-129 1.70e-05

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: 47.31  E-value: 1.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   22 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 88
Cdd:cd21324     25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2462619885   89 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 129
Cdd:cd21324    105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
17-125 1.84e-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: 46.52  E-value: 1.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   17 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQIALDY 87
Cdd:cd21329      2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462619885   88 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 125
Cdd:cd21329     78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
PLEC smart00250
Plectin repeat;
2648-2684 2.28e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.62  E-value: 2.28e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  2648 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDT 2684
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
841-1473 2.32e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 2.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  841 QEAQEAVTRLEAQHQALVTLWHQLHVdmksllAWQSLRRDVQLIrswslatfrtlkpeEQRQALHSLELHYQ-AFLRDSQ 919
Cdd:TIGR02168  354 ESLEAELEELEAELEELESRLEELEE------QLETLRSKVAQL--------------ELQIASLNNEIERLeARLERLE 413
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  920 DAggfgpEDRLMAEREygscshhyqQLLQSLEQGAQEEsrCQRCISELKDIRLQLEACETRTVHRL------------RL 987
Cdd:TIGR02168  414 DR-----RERLQQEIE---------ELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALeelreeleeaeqAL 477
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  988 PLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEK-------VLALPEPspaAPTLRSELELTLGKLEQ---VRS 1057
Cdd:TIGR02168  478 DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvLSELISV---DEGYEAAIEAALGGRLQavvVEN 554
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1058 LSAI-----YLEK--LKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLKKlraqaeAQQPTFDALR-- 1128
Cdd:TIGR02168  555 LNAAkkaiaFLKQneLGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRK------ALSYLLGGVLvv 628
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1129 DELRGAQEVGERLqqRHGERDV----EVERWRERVAQLLERWQAVLAQtdvRQRELEQLGRQLRYYRESADPLGAWLQDA 1204
Cdd:TIGR02168  629 DDLDNALELAKKL--RPGYRIVtldgDLVRPGGVITGGSAKTNSSILE---RRREIEELEEKIEELEEKIAELEKALAEL 703
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1205 RRRQEQIQAMpLADSQAVREQLRQEQALL-EEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEP-----VASPA 1278
Cdd:TIGR02168  704 RKELEELEEE-LEQLRKELEELSRQISALrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeelAEAEA 782
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1279 KKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQEtqaLQQSFLSEKDSLLQRER 1358
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED---LEEQIEELSEDIESLAA 859
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1359 FIEQEKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELL 1438
Cdd:TIGR02168  860 EIEELEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
                          650       660       670
                   ....*....|....*....|....*....|....*
gi 2462619885 1439 AEENQRLREQLQLLEEqhrAALAHSEEVTASQVAA 1473
Cdd:TIGR02168  939 DNLQERLSEEYSLTLE---EAEALENKIEDDEEEA 970
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1542-1580 2.51e-05

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 43.47  E-value: 2.51e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 1542 YLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTALIL 1580
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
mukB PRK04863
chromosome partition protein MukB;
1079-1248 2.71e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.34  E-value: 2.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1079 AEEVLRAHEEQLKEAQAVP---ATLPELEatkaslKKLRAQAEAQQptfdaLRDELRGAQEVG-------ERLQQRHGER 1148
Cdd:PRK04863   498 ARELLRRLREQRHLAEQLQqlrMRLSELE------QRLRQQQRAER-----LLAEFCKRLGKNlddedelEQLQEELEAR 566
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1149 dveVERWRERVAQLLERwqavlaQTDVRQrELEQLGRQLRYYRESADplgAWL--QDARRRQEQIQAMPLADSQAVRE-- 1224
Cdd:PRK04863   567 ---LESLSESVSEARER------RMALRQ-QLEQLQARIQRLAARAP---AWLaaQDALARLREQSGEEFEDSQDVTEym 633
                          170       180
                   ....*....|....*....|....*.
gi 2462619885 1225 --QLRQEQALLEEIERHGEKVEECQR 1248
Cdd:PRK04863   634 qqLLERERELTVERDELAARKQALDE 659
PLEC smart00250
Plectin repeat;
2201-2235 3.18e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.18e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2462619885  2201 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 2235
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
3236-3273 3.54e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.54e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2462619885  3236 QRFLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTA 3273
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2817-2851 3.83e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.83e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2462619885  2817 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 2851
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
CH_PARVA_B_rpt2 cd21306
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
21-122 4.68e-05

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


Pssm-ID: 409155  Cd Length: 121  Bit Score: 45.49  E-value: 4.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   21 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21306     16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
                           90       100
                   ....*....|....*....|....*.
gi 2462619885   97 NIRNDDIADGNPKLTLGLIWTIILHF 122
Cdd:cd21306     96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
PLEC smart00250
Plectin repeat;
3126-3159 5.35e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 5.35e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2462619885  3126 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 3159
Cdd:smart00250    5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PTZ00121 PTZ00121
MAEBL; Provisional
991-1420 6.02e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 6.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  991 KEPARECAQRIAEQQKAQAEveglGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTlGKLEQVR---SLSAIYLEKLK 1067
Cdd:PTZ00121  1397 KKKAEEDKKKADELKKAAAA----KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK-KKAEEAKkaeEAKKKAEEAKK 1471
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1068 TISLVIRGTQG--AEEVLRAHEEQLKEA----QAVPATLPELEATKASLKKLRAQAEAQQPTFDAlrDELRGAQEVGERL 1141
Cdd:PTZ00121  1472 ADEAKKKAEEAkkADEAKKKAEEAKKKAdeakKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA--DEAKKAEEKKKAD 1549
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1142 QQRHGE--RDVEVERWRERVAQLLERWQAVLAQTDV-RQRELEQLGRQLRYYRESADPLGAWLQDARrrQEQIQAmplad 1218
Cdd:PTZ00121  1550 ELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEaKKAEEARIEEVMKLYEEEKKMKAEEAKKAE--EAKIKA----- 1622
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1219 sqavrEQLRQEQALLEEIERHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAKKPkvqsgSESVIQEYVDLR 1298
Cdd:PTZ00121  1623 -----EELKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKK-----AEEAKKAEEDEK 1688
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1299 THYSELTTLTSQYIKfiSETLRRMEEEEMQTVQQeqllqetqaLQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKA 1378
Cdd:PTZ00121  1689 KAAEALKKEAEEAKK--AEELKKKEAEEKKKAEE---------LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2462619885 1379 QQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRK 1420
Cdd:PTZ00121  1758 KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
SPEC smart00150
Spectrin repeats;
1088-1181 7.06e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 44.24  E-value: 7.06e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  1088 EQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALrdelrgaQEVGERLQQRHGERDVEVErwrERVAQLLERWQ 1167
Cdd:smart00150   18 EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEAL-------NELGEQLIEEGHPDAEEIE---ERLEELNERWE 87
                            90
                    ....*....|....
gi 2462619885  1168 AVLAQTDVRQRELE 1181
Cdd:smart00150   88 ELKELAEERRQKLE 101
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1110-1590 8.88e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 8.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1110 LKKLRAQAEAqqptfdALRdelrgAQEVGERLQQRhgerdvEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRy 1189
Cdd:COG1196    202 LEPLERQAEK------AER-----YRELKEELKEL------EAELLLLKLRELEAELEELEAELEELEAELEELEAELA- 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1190 yresadplgawLQDARRRQEQIQAmpLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKA 1269
Cdd:COG1196    264 -----------ELEAELEELRLEL--EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1270 QLEpvaspakkpKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALQQSFLSE 1349
Cdd:COG1196    331 ELE---------ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1350 KDSLLQRERFIEQEKAKLEQLfqdevakaqqlreeqqrqqqqmeqerqrlvASMEEARRRQHEAEEGVRRKQEELQQLEQ 1429
Cdd:COG1196    402 LEELEEAEEALLERLERLEEE------------------------------LEELEEALAELEEEEEEEEEALEEAAEEE 451
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1430 QRRQQEELLAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRL 1509
Cdd:COG1196    452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG 531
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1510 QEAGILSAEELQRLAQG-HTTVDELARREDVRHYLQGR--SSIAGLLLKATNEKLSVYAALQRQLLSPGTALILLEAQAA 1586
Cdd:COG1196    532 VEAAYEAALEAALAAALqNIVVEDDEVAAAAIEYLKAAkaGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611

                   ....
gi 2462619885 1587 SGFL 1590
Cdd:COG1196    612 DARY 615
PLEC smart00250
Plectin repeat;
2536-2571 8.91e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.08  E-value: 8.91e-05
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 2462619885  2536 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVA 2571
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
22-119 8.95e-05

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


Pssm-ID: 409141  Cd Length: 145  Bit Score: 45.35  E-value: 8.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   22 QKKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 88
Cdd:cd21292     25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462619885   89 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 119
Cdd:cd21292    105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
PTZ00121 PTZ00121
MAEBL; Provisional
948-1457 9.09e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 9.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  948 QSLEQGAQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEK 1027
Cdd:PTZ00121  1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK 1384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1028 VLAlpEPSPAAPTLRSELELTLGKLEQVRSLSAiylEKLKTISLvirgTQGAEEVLRAhEEQLKEAQavpatlpelEATK 1107
Cdd:PTZ00121  1385 KKA--EEKKKADEAKKKAEEDKKKADELKKAAA---AKKKADEA----KKKAEEKKKA-DEAKKKAE---------EAKK 1445
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1108 ASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHG--ERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGR 1185
Cdd:PTZ00121  1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD 1525
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1186 QLRYYRESADPlgawlQDARRRQEQIQAMPLADSQAVR---EQLRQEQALLEEIERHGE--KVEECQRFAKQYINAIKDY 1260
Cdd:PTZ00121  1526 EAKKAEEAKKA-----DEAKKAEEKKKADELKKAEELKkaeEKKKAEEAKKAEEDKNMAlrKAEEAKKAEEARIEEVMKL 1600
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1261 ELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQ 1340
Cdd:PTZ00121  1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1341 ALQQSFLSEKDSLLQRErfiEQEKAKLEQL---FQDEVAKAQqlreEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGV 1417
Cdd:PTZ00121  1681 KKAEEDEKKAAEALKKE---AEEAKKAEELkkkEAEEKKKAE----ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 2462619885 1418 RRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHR 1457
Cdd:PTZ00121  1754 EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
PLEC smart00250
Plectin repeat;
2276-2307 9.17e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.08  E-value: 9.17e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2462619885  2276 QLLSAEKAVTGYRDPYSGSTISLFQAMQKGLV 2307
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1001-1182 9.35e-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: 9.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1001 IAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAE 1080
Cdd:cd00176     39 LKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1081 EVLRAHEEQLKEAQAvpatlPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERwrERVA 1160
Cdd:cd00176    117 DLEQWLEEKEAALAS-----EDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIE--EKLE 189
                          170       180
                   ....*....|....*....|..
gi 2462619885 1161 QLLERWQAVLAQTDVRQRELEQ 1182
Cdd:cd00176    190 ELNERWEELLELAEERQKKLEE 211
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1079-1245 9.91e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 9.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1079 AEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRaqaeaqqptfDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1158
Cdd:PRK02224   239 ADEVLEEHEERREELETLEAEIEDLRETIAETERER----------EELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1159 VAQLLERWQAVLAQTDVRQRELEQ-------LGRQLRYYRESADPLGAWLQDARRRQEQIQamplADSQAVREQLRQEQA 1231
Cdd:PRK02224   309 AEAVEARREELEDRDEELRDRLEEcrvaaqaHNEEAESLREDADDLEERAEELREEAAELE----SELEEAREAVEDRRE 384
                          170
                   ....*....|....
gi 2462619885 1232 LLEEIERHGEKVEE 1245
Cdd:PRK02224   385 EIEELEEEIEELRE 398
SPEC smart00150
Spectrin repeats;
500-594 1.30e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.47  E-value: 1.30e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   500 LRYLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARSDEGQL---SPATRGAYRDCLGRLD 576
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
                            90
                    ....*....|....*...
gi 2462619885   577 LQYAKLLNSSKARLRSLE 594
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
1580-1613 1.43e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.43e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2462619885  1580 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPE 1613
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2201-2235 1.43e-04

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 41.54  E-value: 1.43e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2462619885 2201 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 2235
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPET 35
PLEC smart00250
Plectin repeat;
2611-2647 1.86e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.86e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  2611 RLLSAERAVTGYRDPYTEQTISLFQAMKKELIPTEEA 2647
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
159-236 1.88e-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: 43.06  E-value: 1.88e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619885  159 DNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 236
Cdd:cd21185     20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
PLEC smart00250
Plectin repeat;
1908-1942 2.20e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.93  E-value: 2.20e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2462619885  1908 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEF 1942
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
1982-2018 2.22e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.93  E-value: 2.22e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2462619885  1982 LRLLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEET 2018
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1097-1328 2.64e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 2.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1097 PATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQevgERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVR 1176
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL---SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1177 QRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPL--------ADSQAVREQLRQEQALLEEIERHGEKVEECQR 1248
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripeiqAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1249 FAKQYINAIKDY----ELQLVTYKAQLEpvASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEE 1324
Cdd:TIGR02169  830 YLEKEIQELQEQridlKEQIKSIEKEIE--NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907

                   ....
gi 2462619885 1325 EEMQ 1328
Cdd:TIGR02169  908 LEAQ 911
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
966-1207 2.69e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 2.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  966 ELKDIRLQLEAcETRTVHRLrlpldkEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpepSPAAPTLRSEL 1045
Cdd:COG4913    236 DLERAHEALED-AREQIELL------EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL----EAELEELRAEL 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1046 ELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEvlraheEQLKEaqavpatlpELEATKASLKKLRAQAEAQQPTFD 1125
Cdd:COG4913    305 ARLEAELERLEARLDALREELDELEAQIRGNGGDRL------EQLER---------EIERLERELEERERRRARLEALLA 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1126 ALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQllERWQAVLAQTDVRqRELEQLGRQLRYYRESADPLGAWLQDAR 1205
Cdd:COG4913    370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEE--ALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLALR 446

                   ..
gi 2462619885 1206 RR 1207
Cdd:COG4913    447 DA 448
Rabaptin pfam03528
Rabaptin;
1080-1377 2.88e-04

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 46.64  E-value: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1080 EEVLRAHEEQLKEAQAVpatlpeLEATKASLKKLRAQ-AEAQqptfdALRDELRGAQEVGERLQQrhgERDVEVER-WRE 1157
Cdd:pfam03528   39 KELYLAKEEDLKRQNAV------LQEAQVELDALQNQlALAR-----AEMENIKAVATVSENTKQ---EAIDEVKSqWQE 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1158 RVAQLlerwQAVLAQTdVRQRE------LEQLGRQLRYYRESADPLGAwlqDARRRqeqiqampLADSQavreqlrQEQA 1231
Cdd:pfam03528  105 EVASL----QAIMKET-VREYEvqfhrrLEQERAQWNQYRESAEREIA---DLRRR--------LSEGQ-------EEEN 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1232 LLEEIERHGEKVEECQRFA---KQYINAIKDYELQLVTYKAQLEpvASPAKK----PKVQSGSESVIQEYVD-LRTHYSE 1303
Cdd:pfam03528  162 LEDEMKKAQEDAEKLRSVVmpmEKEIAALKAKLTEAEDKIKELE--ASKMKElnhyLEAEKSCRTDLEMYVAvLNTQKSV 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1304 LTTLTSQYIKFISETLRRMEEEEMQtvqqeqllqeTQALQQSFLSEKDSLLQRERFIEQEKAKL------EQLFQDEVAK 1377
Cdd:pfam03528  240 LQEDAEKLRKELHEVCHLLEQERQQ----------HNQLKHTWQKANDQFLESQRLLMRDMQRMesvltsEQLRQVEEIK 309
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2536-2574 4.65e-04

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 40.00  E-value: 4.65e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462619885 2536 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVARLL 2574
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1042-1240 5.06e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 5.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1042 RSELELTLGKLEQVRSLsaiyLEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAvpaTLPELEATKASLKKLRAQAEAQQ 1121
Cdd:COG4913    633 LEALEAELDALQERREA----LQRLAEYSWDEIDVASAEREIAELEAELERLDA---SSDDLAALEEQLEELEAELEELE 705
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1122 PTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERV-----AQLLERWQAvLAQTDVRQRELEQLGRQLRYYRESADP 1196
Cdd:COG4913    706 EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelrALLEERFAA-ALGDAVERELRENLEERIDALRARLNR 784
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2462619885 1197 LGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHG 1240
Cdd:COG4913    785 AEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG 828
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1085-1280 6.77e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 6.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1085 AHEEQLKEAQAvpatlpELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLE 1164
Cdd:COG4942     17 AQADAAAEAEA------ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1165 RWQAVLAQTDVRQRELEQLGRQLrYYRESADPLGAWL-----QDARRRQEQIQAMpladSQAVREQLRQEQALLEEIERH 1239
Cdd:COG4942     91 EIAELRAELEAQKEELAELLRAL-YRLGRQPPLALLLspedfLDAVRRLQYLKYL----APARREQAEELRADLAELAAL 165
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2462619885 1240 GEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKK 1280
Cdd:COG4942    166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
942-1375 8.49e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 8.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  942 HYQQLLQSLEQGAQEESRCQRCISELKDIRLQLEACE-----TRTVHRLRLPLDKEPAR--ECAQRIAEQQKAQAEVEGL 1014
Cdd:COG4717     89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAELPERleELEERLEELRELEEELEEL 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1015 GKGVARLSAEAEKVLALPEPSpaaptLRSELELTLGKLEQVRSLSAIYLEKLKTislvirgtqgAEEVLRAHEEQLKEAQ 1094
Cdd:COG4717    169 EAELAELQEELEELLEQLSLA-----TEEELQDLAEELEELQQRLAELEEELEE----------AQEELEELEEELEQLE 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1095 AVPATLPELEATKASLKKLRAQA-----EAQQPTFDALRDELRGAQEVGERLQQRHGERDVeveRWRERVAQLLERWQAV 1169
Cdd:COG4717    234 NELEAAALEERLKEARLLLLIAAallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQAL 310
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1170 LAQTDVRQRELEQLGRQLRYYRE-SADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQE-QALLEEIerHGEKVEECQ 1247
Cdd:COG4717    311 PALEELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiAALLAEA--GVEDEEELR 388
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1248 RFAKQYiNAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETlrrmeEEEM 1327
Cdd:COG4717    389 AALEQA-EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAEL-----EAEL 462
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462619885 1328 QTVQQEQLLQETQALQQSFLSEKDSLLQR-------ERFIEQEKAKLEQLFQDEV 1375
Cdd:COG4717    463 EQLEEDGELAELLQELEELKAELRELAEEwaalklaLELLEEAREEYREERLPPV 517
COG4995 COG4995
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
1118-1579 1.04e-03

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


Pssm-ID: 444019 [Multi-domain]  Cd Length: 711  Bit Score: 44.96  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1118 EAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPL 1197
Cdd:COG4995      1 LLALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1198 GAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASP 1277
Cdd:COG4995     81 ALAALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1278 AKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRE 1357
Cdd:COG4995    161 AAAALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLAL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1358 RFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEEL 1437
Cdd:COG4995    241 LALAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1438 LAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRLQEAGILSA 1517
Cdd:COG4995    321 AALLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAAL 400
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619885 1518 EELQRLAQGHTTVDELARREDVRHYLQGRSSIAGLL-LKATNEKLSVYAALQRQLLSPGTALI 1579
Cdd:COG4995    401 LALAAAQLLRLLLAALALLLALAAYAAARLALLALIeYIILPDRLYAFVQLYQLLIAPIEAEL 463
PLEC smart00250
Plectin repeat;
1540-1577 1.10e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.00  E-value: 1.10e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2462619885  1540 RHYLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTA 1577
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
16-119 1.15e-03

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: 41.66  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   16 DERDRVQkktFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEvlsgDSLP-------------REKGRM 73
Cdd:cd21294      4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLIN----DSVPdtidervlnkpprKNKPLN 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2462619885   74 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 119
Cdd:cd21294     77 NFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
COG5283 COG5283
Phage-related tail protein [Mobilome: prophages, transposons];
1082-1214 1.17e-03

Phage-related tail protein [Mobilome: prophages, transposons];


Pssm-ID: 444094 [Multi-domain]  Cd Length: 747  Bit Score: 44.85  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1082 VLRAHEEQLKEAqavpatlpeLEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQ 1161
Cdd:COG5283      4 ILGAVDKPFKSA---------LESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQ 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462619885 1162 LLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAM 1214
Cdd:COG5283     75 AGIDTRQLSAAQRRLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQRL 127
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
28-118 1.40e-03

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 41.13  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   28 KWVNKHLIKAQR---HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRhrQVKLVN-IRN 100
Cdd:cd21218     17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
                           90
                   ....*....|....*...
gi 2462619885  101 DDIADGNPKLTLGLIWTI 118
Cdd:cd21218     95 EDIVSGNPRLNLAFVATL 112
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
17-125 1.50e-03

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: 41.13  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   17 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL---------SGDSLPREKGRMRfhKLQNVQIALDY 87
Cdd:cd21330      9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462619885   88 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 125
Cdd:cd21330     85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
596-689 1.83e-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: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  596 LHSFVAAATKELMWLNEKEE----EEVGFDWsdrnTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTV 671
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEAllssEDYGKDL----ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90
                   ....*....|....*...
gi 2462619885  672 ESFQAALQTQWSWMLQLC 689
Cdd:pfam00435   79 QERLEELNERWEQLLELA 96
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
24-236 1.83e-03

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 44.16  E-value: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   24 KTFTKWVNKHLIKAQrhISDLYEDLRDGHNLISLLEVLSGD---SLPREKGR-------MRFHKLQNVQIALDYLRHRQV 93
Cdd:COG5069    382 RVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAVDLGITEGF 459
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   94 KLVNIRNDDIADGNpKLTLGLIW-------TIILHFQISDiqvsgqsEDMTAKEKLLLWSQRMVEGY---QGLRCDNFTS 163
Cdd:COG5069    460 SLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKD-------GCGLSDSDLCAWLGSLGLKGdkeEGIRSFGDPA 531
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  164 SWRDGRLFNAIIHRHKPLLIDMNKVyRQTNLENLDQA-------FSVAERDLGVTRLLDPEDVDVPQPdEKSIITYVSSL 236
Cdd:COG5069    532 GSVSGVFYLDVLKGIHSELVDYDLV-TRGFTEFDDIAdarslaiSSKILRSLGAIIKFLPEDINGVRP-RLDVLTFIESL 609
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
819-1376 2.08e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.94  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  819 VLSSSGSEAAVPSVCFLVPPPNQEAQEAVTRLEAQHQALVTLWHQLHVDMKSLlawqslrRDVQLIRSWSLATFRTLKPE 898
Cdd:pfam05483  246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKEL-------EDIKMSLQRSMSTQKALEED 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  899 EQ--RQALHSLELHYQAFLRDSQDAGGfgPEDRLMAEREYGSCShhYQQLLQSleqgaqEESRCQRCISELKDIRLQLEA 976
Cdd:pfam05483  319 LQiaTKTICQLTEEKEAQMEELNKAKA--AHSFVVTEFEATTCS--LEELLRT------EQQRLEKNEDQLKIITMELQK 388
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  977 CETRTVHRLRLPLDKEPARECAQRI-AEQQKAQAEVEGLGKGVARLSAEAEKVLALPEpSPAAPTLRSELELTLGK---- 1051
Cdd:pfam05483  389 KSSELEEMTKFKNNKEVELEELKKIlAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQ-AREKEIHDLEIQLTAIKtsee 467
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1052 --LEQVRSL-SAIYLEKLKTISLvirgTQGAEEVLRAHEEQLKEAQAVPATLP----ELEATKASLKKLRAQAEAQQPTF 1124
Cdd:pfam05483  468 hyLKEVEDLkTELEKEKLKNIEL----TAHCDKLLLENKELTQEASDMTLELKkhqeDIINCKKQEERMLKQIENLEEKE 543
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1125 DALRDELrgaQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLryyresadplgawlQDA 1204
Cdd:pfam05483  544 MNLRDEL---ESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI--------------ENK 606
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1205 RRRQEQIQAmplaDSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKD-YELQLVTYKAQLEPVASPAKKPKV 1283
Cdd:pfam05483  607 NKNIEELHQ----ENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDnYQKEIEDKKISEEKLLEEVEKAKA 682
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1284 QSGSESVIQEYVDLRTHYSelttltsqyikfISETLRRMEEEEMQtvqqeqllqetqalQQSFLSEKDSLLQRERFIEQE 1363
Cdd:pfam05483  683 IADEAVKLQKEIDKRCQHK------------IAEMVALMEKHKHQ--------------YDKIIEERDSELGLYKNKEQE 736
                          570
                   ....*....|...
gi 2462619885 1364 KAKLEQLFQDEVA 1376
Cdd:pfam05483  737 QSSAKAALEIELS 749
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1103-1420 2.12e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 2.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1103 LEATKASLKKLRAQAE-AQQptFDALRDELRGAQE--VGERLQQRHGERDvEVERWRERVAQLLERWQAVLAQTDVrqrE 1179
Cdd:TIGR02168  195 LNELERQLKSLERQAEkAER--YKELKAELRELELalLVLRLEELREELE-ELQEELKEAEEELEELTAELQELEE---K 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1180 LEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKD 1259
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1260 YELQLVTYKAQLEpvASPAKKPKVQSGSESVIQEYVDLRTHYSELTtltsQYIKFISETLRRMEEE-EMQTVQQEQLLQE 1338
Cdd:TIGR02168  349 LKEELESLEAELE--ELEAELEELESRLEELEEQLETLRSKVAQLE----LQIASLNNEIERLEARlERLEDRRERLQQE 422
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1339 TQALQQSFLSEKDSLLQRErfIEQEKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVR 1418
Cdd:TIGR02168  423 IEELLKKLEEAELKELQAE--LEELEEELEEL-QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499

                   ..
gi 2462619885 1419 RK 1420
Cdd:TIGR02168  500 NL 501
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
932-1244 2.51e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  932 AEREYGSCSHHYQQLLQSLEQGAQEESRCQRCISELKDIRLQLEACETRTvhrlrLPLDKEPARECAQRIAEQQKAQAEV 1011
Cdd:COG4717    137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL-----SLATEEELQDLAEELEELQQRLAEL 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1012 EglgKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISL-VIRGTQGAEEVLRAHEEQL 1090
Cdd:COG4717    212 E---EELEEAQEELEE-------------LEEELEQLENELEAAALEERLKEARLLLLIAaALLALLGLGGSLLSLILTI 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1091 KEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRgAQEVGERLQQRHGERDVEVERWRErVAQLLERWQAVL 1170
Cdd:COG4717    276 AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE-EEELEELLAALGLPPDLSPEELLE-LLDRIEELQELL 353
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1171 AQTDVRQRELEQLGRQLRYYR-------ESADPLGAWLQDARRRQEQIQAMpladsQAVREQLRQEQALLEEIERHGEKV 1243
Cdd:COG4717    354 REAEELEEELQLEELEQEIAAllaeagvEDEEELRAALEQAEEYQELKEEL-----EELEEQLEELLGELEELLEALDEE 428

                   .
gi 2462619885 1244 E 1244
Cdd:COG4717    429 E 429
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
23-81 3.55e-03

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


Pssm-ID: 409070  Cd Length: 106  Bit Score: 39.56  E-value: 3.55e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462619885   23 KKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREK----GRMRFHKLQNV 81
Cdd:cd21221      3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVV 65
PLEC smart00250
Plectin repeat;
2854-2885 4.12e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.46  E-value: 4.12e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2462619885  2854 KLLSAERAVTGYKDPYSGKLISLFQAMKKGLI 2885
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3132-3162 4.47e-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: 4.47e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462619885 3132 AGILDTETLEKVSITEAMHRNLVDNITGQRL 3162
Cdd:pfam00681    9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1041-1235 4.57e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 4.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1041 LRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEvLRAHEEQLKEAQAvpatlpELEATKASLKKLRAQAE-- 1118
Cdd:COG3206    180 LEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQ-LSELESQLAEARA------ELAEAEARLAALRAQLGsg 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1119 -------AQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVA----QLLERWQAVLAQTDVR----QRELEQL 1183
Cdd:COG3206    253 pdalpelLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAalraQLQQEAQRILASLEAElealQAREASL 332
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462619885 1184 GRQLRYYRESADPLGAWLQDARRRQEQIQAmpladSQAVREQL--RQEQALLEE 1235
Cdd:COG3206    333 QAQLAQLEARLAELPELEAELRRLEREVEV-----ARELYESLlqRLEEARLAE 381
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1097-1412 5.31e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 5.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1097 PATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVR 1176
Cdd:COG4372     20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1177 QRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQR-------- 1248
Cdd:COG4372    100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelqalsea 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1249 FAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEEMQ 1328
Cdd:COG4372    180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1329 TVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARR 1408
Cdd:COG4372    260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339

                   ....
gi 2462619885 1409 RQHE 1412
Cdd:COG4372    340 ADLL 343
CH_PARVA_rpt2 cd21337
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ...
21-123 5.66e-03

second calponin homology (CH) domain found in alpha-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. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin 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: 409186  Cd Length: 129  Bit Score: 39.59  E-value: 5.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   21 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR----FHKLQNVQIALDYLRHRQVKLV 96
Cdd:cd21337     20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEKP 99
                           90       100
                   ....*....|....*....|....*..
gi 2462619885   97 NIRNDDIADGNPKLTLGLIWTIILHFQ 123
Cdd:cd21337    100 KPRPEDIVNCDLKSTLRVLYNLFTKYR 126
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
1101-1272 5.88e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 42.03  E-value: 5.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1101 PELEATKASLKKLRAQAEAQQPTFDALRDelrgaqevgeRLQQRHGERDVEverwRERVAQLLERWQAVLAQTDVRQREL 1180
Cdd:pfam00529   54 TDYQAALDSAEAQLAKAQAQVARLQAELD----------RLQALESELAIS----RQDYDGATAQLRAAQAAVKAAQAQL 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1181 EQLGRQLRYYRESAdPLGAW----LQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEierhgekveecqrFAKQYINA 1256
Cdd:pfam00529  120 AQAQIDLARRRVLA-PIGGIsresLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAE-------------NQAEVRSE 185
                          170
                   ....*....|....*.
gi 2462619885 1257 IKDYELQLVTYKAQLE 1272
Cdd:pfam00529  186 LSGAQLQIAEAEAELK 201
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1083-1182 6.52e-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: 6.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1083 LRAHEEQLKEAQAVpATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGErdvEVERWRERVAQL 1162
Cdd:pfam00435   10 ADDLESWIEEKEAL-LSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHY---ASEEIQERLEEL 85
                           90       100
                   ....*....|....*....|
gi 2462619885 1163 LERWQAVLAQTDVRQRELEQ 1182
Cdd:pfam00435   86 NERWEQLLELAAERKQKLEE 105
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
1068-1272 7.49e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 7.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1068 TISLVIRGTQGAEEVLRAHEEQLKEAQAvpatlpELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEvgerlqqrhge 1147
Cdd:COG3883      3 ALALAAPTPAFADPQIQAKQKELSELQA------ELEAAQAELDALQAELEELNEEYNELQAELEALQA----------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1148 rdvEVERWRERVAQllerwqavlAQTDVRQRElEQLGRQLRYYRESADPLGAW--------LQDARRRQEQIQAMPLADS 1219
Cdd:COG3883     66 ---EIDKLQAEIAE---------AEAEIEERR-EELGERARALYRSGGSVSYLdvllgsesFSDFLDRLSALSKIADADA 132
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462619885 1220 QAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLE 1272
Cdd:COG3883    133 DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
SPEC smart00150
Spectrin repeats;
1190-1256 8.91e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 38.46  E-value: 8.91e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619885  1190 YRESADPLGAWLQDArrrQEQIQAMPLA-DSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINA 1256
Cdd:smart00150    3 FLRDADELEAWLEEK---EQLLASEDLGkDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE 67
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
22-119 8.99e-03

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


Pssm-ID: 409142  Cd Length: 116  Bit Score: 38.66  E-value: 8.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885   22 QKKTFTKWVNKHL---------IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDY 87
Cdd:cd21293      2 EKGSYVDHINRYLgddpflkqfLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2462619885   88 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 119
Cdd:cd21293     82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
943-1537 9.03e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.88  E-value: 9.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885  943 YQQLLQSLEQGAQEESRCQRCISELKDIRLQLEACEtrtvhRLRLPLDKEPAREcaqRIAEQQKAQAEVEglgkgvarls 1022
Cdd:TIGR00618  245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLE-----ETQERINRARKAA---PLAAHIKAVTQIE---------- 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1023 AEAEKVLAlpepspaaptlrsELELTLGKLEQVRSLSAIYLEKlktiSLVIRGTQGAEEVLRAHEEQLKEAQAVPAT-LP 1101
Cdd:TIGR00618  307 QQAQRIHT-------------ELQSKMRSRAKLLMKRAAHVKQ----QSSIEEQRRLLQTLHSQEIHIRDAHEVATSiRE 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1102 ELEATKASLKKLRAQAeaQQPTfdALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLerwqAVLAQTDVRQRELE 1181
Cdd:TIGR00618  370 ISCQQHTLTQHIHTLQ--QQKT--TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA----HAKKQQELQQRYAE 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1182 QLgrqlryyresadplgawlQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYE 1261
Cdd:TIGR00618  442 LC------------------AAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP 503
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1262 LQLVTYKAQLEPVA-----SPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQyIKFISETLRRMEE------------ 1324
Cdd:TIGR00618  504 CPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQsfsiltqcdnrs 582
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1325 -EEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIE-------QEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQER 1396
Cdd:TIGR00618  583 kEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKlqpeqdlQDVRLHLQQCSQELALKLTALHALQLTLTQERVRE 662
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462619885 1397 QRLVASMEEARRRQHeaeegVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQ-------LLEEQHRAALAHSEEVTAS 1469
Cdd:TIGR00618  663 HALSIRVLPKELLAS-----RQLALQKMQSEKEQLTYWKEMLAQCQTLLRELEThieeydrEFNEIENASSSLGSDLAAR 737
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462619885 1470 QVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRLQEAGILSAEELQRLAQGHTTVDELARRE 1537
Cdd:TIGR00618  738 EDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLE 805
 
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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