NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2217372302|ref|XP_047277845|]
View 

plectin isoform X31 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
13-140 5.65e-78

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: 254.14  E-value: 5.65e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   13 QAYEEVREKYKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIA 92
Cdd:cd21236      1 QAYENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIA 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2217372302   93 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 140
Cdd:cd21236     81 LDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
144-249 1.52e-72

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


:

Pssm-ID: 409087  Cd Length: 106  Bit Score: 237.61  E-value: 1.52e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  144 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 223
Cdd:cd21238      1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 2217372302  224 PEDVDVPQPDEKSIITYVSSLYDAMP 249
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
880-957 6.24e-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: 6.24e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217372302  880 LAWQSLRRDVQLIRSWSLATFRTLKPEEQRQALHSLELHYQAFLRDSQDAGGFGPEDRLMAEREYGSCSHHYQQLLQS 957
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
779-845 4.68e-22

SH3 domain; This entry represents an SH3 domain.


:

Pssm-ID: 407754  Cd Length: 65  Bit Score: 91.94  E-value: 4.68e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217372302  779 QLKPRhpAHPMRGRLPLLAVCDYKQVEVTVHKGDECQLVGPAQPSHWKVLSSSGSEAAVPSVCFLVP 845
Cdd:pfam17902    1 PLKQR--RSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
604-793 1.15e-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: 1.15e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  604 LHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQ 683
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  684 AALQTQWSWMLQLCCCIEAHLKENAAYFQFFSDVREAEGQLQKLQEALRrkySCDRSATVTRLEDLLQDAQDEKEQLNEY 763
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190
                   ....*....|....*....|....*....|
gi 2217372302  764 KGHLSGLAKRAKAVVQLKPRHPAHPMRGRL 793
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2901-2939 9.12e-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: 9.12e-16
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 2901 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 2939
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1664-1702 3.68e-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: 3.68e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 1664 LLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEMNRVL 1702
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2582-2620 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 2217372302 2582 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 2620
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2323-2361 6.73e-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: 6.73e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 2323 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEMNRVL 2361
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1088-1278 1.34e-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: 1.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1088 EEVLRAHEEQLKEAQaVPATLPELEATKASLKKLRAQAEAQQPTFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1167
Cdd:cd00176     13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1168 AQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLGAWLQDArrrQEQIQAMPLADS-QAVREQLRQEQALLEEIER 1246
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEK---EAALASEDLGKDlESVEELLKKHKELEEELEA 157
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2217372302 1247 HGEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1278
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
508-697 6.45e-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: 6.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  508 LRYLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARSDEGQLSPATRGAY---RDCLGRLD 584
Cdd:cd00176      6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  585 LQYAKLLNSSKARLRSLE---SLHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKEL 661
Cdd:cd00176     86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2217372302  662 QNAGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 697
Cdd:cd00176    166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1916-1954 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 2217372302 1916 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEFHEKL 1954
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3170-3208 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 2217372302 3170 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 3208
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1992-2030 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 2217372302 1992 LLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEETSRAL 2030
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1588-1626 2.22e-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: 2.22e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 1588 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHKL 1626
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2825-2863 2.86e-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: 2.86e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 2825 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 2863
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2658-2696 3.06e-12

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.12  E-value: 3.06e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 2658 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 2696
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3246-3284 1.00e-10

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: 1.00e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 3246 FLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTAQKL 3284
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
900-1468 3.44e-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: 59.57  E-value: 3.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  900 FRTLKPEEQRQALHSLELHYQAFLRDSQDAGgfgpEDRLMAEREYGSCSHHYQQLLQSLEQGAQEESRCQRCISELKDIR 979
Cdd:COG1196    215 YRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  980 LQLEACETRTVHRLRLplDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALpepspAAPTLRSELELTLGK 1059
Cdd:COG1196    291 YELLAELARLEQDIAR--LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-----AEEELEEAEAELAEA 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1060 LEQVRSLSAIYLEKLKTISlviRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDEL 1139
Cdd:COG1196    364 EEALLEAEAELAEAEEELE---ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1140 RGAQEvgeRLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQI 1219
Cdd:COG1196    441 EEALE---EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1220 QAMPLAdsQAVREQLRQEQALLEEIE-----RHGEKVEECQRFAKQYINAIKDYELQLVTY--KAQLEPVASPAKKPKVQ 1292
Cdd:COG1196    518 GLRGLA--GAVAVLIGVEAAYEAALEaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpLDKIRARAALAAALARG 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1293 SGSESVIQEYVDLRTH---------YSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALQQSFLSEKDSLLQ 1363
Cdd:COG1196    596 AIGAAVDLVASDLREAdaryyvlgdTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1364 RERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQE 1443
Cdd:COG1196    676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
                          570       580
                   ....*....|....*....|....*
gi 2217372302 1444 ELLAEENQRLREQLQLLEEQhRAAL 1468
Cdd:COG1196    756 LPEPPDLEELERELERLERE-IEAL 779
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3002-3030 3.72e-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: 3.72e-07
                           10        20
                   ....*....|....*....|....*....
gi 2217372302 3002 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 3030
Cdd:pfam00681   11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
2785-2822 5.82e-07

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 48.25  E-value: 5.82e-07
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2217372302  2785 QKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTA 2822
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2253-2285 2.28e-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: 2.28e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2217372302 2253 ATGFLVDPVRNQRLYVHEAVKAGVVGPELHEQL 2285
Cdd:pfam00681    7 ATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
1953-1989 2.30e-06

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.71  E-value: 2.30e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  1953 KLLSAEKAVTGYRDPYTGQSVSLFQALKKGLIPREQG 1989
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
1625-1661 1.27e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.27e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  1625 KLLSAERAVTGYKDPYTGQQISLFQAMQKGLIVREHG 1661
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1550-1588 2.52e-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: 2.52e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 1550 YLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTALIL 1588
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
2209-2243 3.18e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.18e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2217372302  2209 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 2243
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
3134-3167 5.36e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 5.36e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2217372302  3134 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 3167
Cdd:smart00250    5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2544-2579 8.93e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.08  E-value: 8.93e-05
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 2217372302  2544 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVA 2579
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2284-2315 9.11e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.08  E-value: 9.11e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2217372302  2284 QLLSAEKAVTGYRDPYSGSTISLFQAMQKGLV 2315
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
PLEC smart00250
Plectin repeat;
2619-2655 1.85e-04

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.85e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  2619 RLLSAERAVTGYRDPYTEQTISLFQAMKKELIPTEEA 2655
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2862-2893 4.09e-03

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.46  E-value: 4.09e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2217372302  2862 KLLSAERAVTGYKDPYSGKLISLFQAMKKGLI 2893
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
 
Name Accession Description Interval E-value
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
13-140 5.65e-78

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: 254.14  E-value: 5.65e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   13 QAYEEVREKYKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIA 92
Cdd:cd21236      1 QAYENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIA 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2217372302   93 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 140
Cdd:cd21236     81 LDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
144-249 1.52e-72

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


Pssm-ID: 409087  Cd Length: 106  Bit Score: 237.61  E-value: 1.52e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  144 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 223
Cdd:cd21238      1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 2217372302  224 PEDVDVPQPDEKSIITYVSSLYDAMP 249
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
28-356 8.92e-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: 8.92e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   28 RVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLV 104
Cdd:COG5069      8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  105 NIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTSSWRDGRLFNAII 183
Cdd:COG5069     88 NIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALI 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  184 HRHKPLLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS------SLYD----AMPR 250
Cdd:COG5069    165 HDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyiirfGLLEkidiALHR 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  251 VPDVQDGVRANElQLRwQEYRELVLLLLQWMRHHTAAFEERRFPSSFEEIEILWSQFLKFKEME--LPAKEAD-KNRSKG 327
Cdd:COG5069    245 VYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCsrAPLETTDlHSLAGQ 322
                          330       340
                   ....*....|....*....|....*....
gi 2217372302  328 IYQSLEgAVQAGQLKVPPGYHPLDVEKEW 356
Cdd:COG5069    323 ILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
880-957 6.24e-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: 6.24e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217372302  880 LAWQSLRRDVQLIRSWSLATFRTLKPEEQRQALHSLELHYQAFLRDSQDAGGFGPEDRLMAEREYGSCSHHYQQLLQS 957
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
32-129 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 2217372302    32 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKLVNIR 107
Cdd:smart00033    1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 2217372302   108 NDDIADGnPKLTLGLIWTIILH 129
Cdd:smart00033   81 PEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
144-250 9.22e-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: 9.22e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  144 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 220
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2217372302  221 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 250
Cdd:pfam00307   81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
29-132 1.67e-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: 1.67e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   29 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-VKLV 104
Cdd:pfam00307    2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
                           90       100
                   ....*....|....*....|....*...
gi 2217372302  105 NIRNDDIADGNPKLTLGLIWTIILHFQI 132
Cdd:pfam00307   82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
779-845 4.68e-22

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 91.94  E-value: 4.68e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217372302  779 QLKPRhpAHPMRGRLPLLAVCDYKQVEVTVHKGDECQLVGPAQPSHWKVLSSSGSEAAVPSVCFLVP 845
Cdd:pfam17902    1 PLKQR--RSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
148-244 3.48e-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: 3.48e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   148 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 223
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 2217372302   224 PEDVDVPQPDEKSIITYVSSL 244
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
604-793 1.15e-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: 1.15e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  604 LHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQ 683
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  684 AALQTQWSWMLQLCCCIEAHLKENAAYFQFFSDVREAEGQLQKLQEALRrkySCDRSATVTRLEDLLQDAQDEKEQLNEY 763
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190
                   ....*....|....*....|....*....|
gi 2217372302  764 KGHLSGLAKRAKAVVQLKPRHPAHPMRGRL 793
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2901-2939 9.12e-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: 9.12e-16
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 2901 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 2939
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1664-1702 3.68e-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: 3.68e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 1664 LLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEMNRVL 1702
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2582-2620 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 2217372302 2582 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 2620
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2323-2361 6.73e-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: 6.73e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 2323 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEMNRVL 2361
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1088-1278 1.34e-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: 1.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1088 EEVLRAHEEQLKEAQaVPATLPELEATKASLKKLRAQAEAQQPTFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1167
Cdd:cd00176     13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1168 AQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLGAWLQDArrrQEQIQAMPLADS-QAVREQLRQEQALLEEIER 1246
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEK---EAALASEDLGKDlESVEELLKKHKELEEELEA 157
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2217372302 1247 HGEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1278
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
508-697 6.45e-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: 6.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  508 LRYLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARSDEGQLSPATRGAY---RDCLGRLD 584
Cdd:cd00176      6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  585 LQYAKLLNSSKARLRSLE---SLHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKEL 661
Cdd:cd00176     86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2217372302  662 QNAGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 697
Cdd:cd00176    166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1916-1954 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 2217372302 1916 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEFHEKL 1954
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3170-3208 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 2217372302 3170 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 3208
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1992-2030 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 2217372302 1992 LLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEETSRAL 2030
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1588-1626 2.22e-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: 2.22e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 1588 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHKL 1626
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2825-2863 2.86e-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: 2.86e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 2825 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 2863
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2658-2696 3.06e-12

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.12  E-value: 3.06e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 2658 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 2696
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3246-3284 1.00e-10

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: 1.00e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 3246 FLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTAQKL 3284
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
952-1282 1.06e-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: 1.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  952 QQLLQSLEQGAQEESRCQRCISELKDirlQLEACETRTVHRLRLPLDKEPARECAQ--RIAEQQKAQAEVEGLGKGVARL 1029
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKAERYQALLKEKREYEGyeLLKEKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1030 SAEAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRGTQG----AEEVLRAHEEQLKE 1100
Cdd:TIGR02169  250 EEELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELED 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1101 AQAVPATL-PELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQllerwqavla 1179
Cdd:TIGR02169  320 AEERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------- 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1180 qtdvRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQamplADSQAVREQLRQEQALLEEIerhGEKVEECQRFAK 1259
Cdd:TIGR02169  390 ----YREKLEKLKREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEKEDK---ALEIKKQEWKLE 458
                          330       340
                   ....*....|....*....|...
gi 2217372302 1260 QYINAIKDYELQLVTYKAQLEPV 1282
Cdd:TIGR02169  459 QLAADLSKYEQELYDLKEEYDRV 481
PLEC smart00250
Plectin repeat;
3168-3205 1.12e-09

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 55.95  E-value: 1.12e-09
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2217372302  3168 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 3205
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2899-2935 2.17e-08

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 52.10  E-value: 2.17e-08
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  2899 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 2935
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
900-1468 3.44e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 3.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  900 FRTLKPEEQRQALHSLELHYQAFLRDSQDAGgfgpEDRLMAEREYGSCSHHYQQLLQSLEQGAQEESRCQRCISELKDIR 979
Cdd:COG1196    215 YRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  980 LQLEACETRTVHRLRLplDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALpepspAAPTLRSELELTLGK 1059
Cdd:COG1196    291 YELLAELARLEQDIAR--LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-----AEEELEEAEAELAEA 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1060 LEQVRSLSAIYLEKLKTISlviRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDEL 1139
Cdd:COG1196    364 EEALLEAEAELAEAEEELE---ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1140 RGAQEvgeRLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQI 1219
Cdd:COG1196    441 EEALE---EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1220 QAMPLAdsQAVREQLRQEQALLEEIE-----RHGEKVEECQRFAKQYINAIKDYELQLVTY--KAQLEPVASPAKKPKVQ 1292
Cdd:COG1196    518 GLRGLA--GAVAVLIGVEAAYEAALEaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpLDKIRARAALAAALARG 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1293 SGSESVIQEYVDLRTH---------YSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALQQSFLSEKDSLLQ 1363
Cdd:COG1196    596 AIGAAVDLVASDLREAdaryyvlgdTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1364 RERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQE 1443
Cdd:COG1196    676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
                          570       580
                   ....*....|....*....|....*
gi 2217372302 1444 ELLAEENQRLREQLQLLEEQhRAAL 1468
Cdd:COG1196    756 LPEPPDLEELERELERLERE-IEAL 779
SPEC smart00150
Spectrin repeats;
605-697 6.07e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.10  E-value: 6.07e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   605 HSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQA 684
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90
                    ....*....|...
gi 2217372302   685 ALQTQWSWMLQLC 697
Cdd:smart00150   81 ELNERWEELKELA 93
PLEC smart00250
Plectin repeat;
2580-2615 1.66e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 49.79  E-value: 1.66e-07
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 2217372302  2580 RLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPE 2615
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3002-3030 3.72e-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: 3.72e-07
                           10        20
                   ....*....|....*....|....*....
gi 2217372302 3002 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 3030
Cdd:pfam00681   11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
2785-2822 5.82e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 48.25  E-value: 5.82e-07
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2217372302  2785 QKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTA 2822
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
1662-1698 1.09e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 47.48  E-value: 1.09e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  1662 IRLLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEM 1698
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2253-2285 2.28e-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: 2.28e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2217372302 2253 ATGFLVDPVRNQRLYVHEAVKAGVVGPELHEQL 2285
Cdd:pfam00681    7 ATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
1953-1989 2.30e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.71  E-value: 2.30e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  1953 KLLSAEKAVTGYRDPYTGQSVSLFQALKKGLIPREQG 1989
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2321-2357 2.64e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.32  E-value: 2.64e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  2321 IRLLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEM 2357
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1052-1268 3.12e-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: 3.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1052 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLkklraqaEAQQPT 1131
Cdd:COG4913    614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-------DASSDD 686
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1132 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLlerwqavlaqtdvrQRELEQLGRQLRYYRESADPLGAWLQD 1211
Cdd:COG4913    687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLELRALLE 752
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217372302 1212 ARRRQEQIQAMPladsQAVREQLRQEQ-ALLEEIERHGEKVEEC-QRFAKQYINAIKDY 1268
Cdd:COG4913    753 ERFAAALGDAVE----RELRENLEERIdALRARLNRAEEELERAmRAFNREWPAETADL 807
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2787-2825 4.62e-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: 4.62e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 2787 FLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTAFEL 2825
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
949-1592 8.55e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 8.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  949 HHYQQLLQSLeqgAQEESRCQRCISELKDIRLQLEACETRTVHRLrlpLDKEPARECAQRIAEQQKAQAEVegLGKGVAR 1028
Cdd:TIGR02168  284 EELQKELYAL---ANEISRLEQQKQILRERLANLERQLEELEAQL---EELESKLDELAEELAELEEKLEE--LKEELES 355
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1029 LSAEAEKVLALpepSPAAPTLRSELEltlgklEQVRSLSAIYLEKLKTISLvIRGTQgaeEVLRAHEEQLKEAQAVPATl 1108
Cdd:TIGR02168  356 LEAELEELEAE---LEELESRLEELE------EQLETLRSKVAQLELQIAS-LNNEI---ERLEARLERLEDRRERLQQ- 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1109 pelEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERwqavLAQTDVRQREL 1188
Cdd:TIGR02168  422 ---EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE----LAQLQARLDSL 494
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1189 EQLGRQLRYYRESAdplgAWLQDARRRQEQIQAmPLADSQAVREQLrqEQALLEEIERHGEKVE-ECQRFAKQYINAIKD 1267
Cdd:TIGR02168  495 ERLQENLEGFSEGV----KALLKNQSGLSGILG-VLSELISVDEGY--EAAIEAALGGRLQAVVvENLNAAKKAIAFLKQ 567
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1268 YELQLVTYKA--QLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSE----LTTLTSQYikFISETL-------RRMEEEE 1334
Cdd:TIGR02168  568 NELGRVTFLPldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkaLSYLLGGV--LVVDDLdnalelaKKLRPGY 645
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1335 MQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEA 1414
Cdd:TIGR02168  646 RIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEEL-EEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1415 RRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQR---LREQLQLLEEQHRAALAHSEEVTASQVAATKTLPNGRDA 1491
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1492 LDGPAAEAEpEHSFDGLRRKVSAQRLQEAGILSAEELQRLAQghTTVDELARREDVRHYLQGRSSIAGLLLKATNEKLSV 1571
Cdd:TIGR02168  805 LDELRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEE--QIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
                          650       660
                   ....*....|....*....|.
gi 2217372302 1572 YAALQRQLLSPGTALILLEAQ 1592
Cdd:TIGR02168  882 RASLEEALALLRSELEELSEE 902
PLEC smart00250
Plectin repeat;
2995-3023 1.27e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.27e-05
                            10        20
                    ....*....|....*....|....*....
gi 2217372302  2995 VRKRRVVIVDPETGKEMSVYEAYRKGLID 3023
Cdd:smart00250    6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
PLEC smart00250
Plectin repeat;
1625-1661 1.27e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.27e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  1625 KLLSAERAVTGYKDPYTGQQISLFQAMQKGLIVREHG 1661
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
422-1253 1.65e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  422 GEVERDLDKADSMIRLLFNDVQTLKDGRhpqgEQMYRrvYR-LHERLvaIRTEYNLRLKAgVAAPATQVAQVTLQSVQRR 500
Cdd:TIGR02169  180 EEVEENIERLDLIIDEKRQQLERLRRER----EKAER--YQaLLKEK--REYEGYELLKE-KEALERQKEAIERQLASLE 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  501 PELEDSTLRyLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGshrgLHQSIEEFRAKIERARS------DEGQLSPATRG 574
Cdd:TIGR02169  251 EELEKLTEE-ISELEKRLEEIEQLLEELNKKIKDLGEEEQLR----VKEKIGELEAEIASLERsiaekeRELEDAEERLA 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  575 AYRDCLGRLDLQYAKLLNSSKARLRSLESLHSFVAAATKELMWL-NEKEEEEVGFDwsdrntnmtAKKESYSALMRELEL 653
Cdd:TIGR02169  326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLrAELEEVDKEFA---------ETRDELKDYREKLEK 396
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  654 KEKKIKELQNAGDRLLREDHPARPTVESFQAALQTQWSWMLQLccciEAHLKENAAyfqffsDVREAEGQLQKLQE---A 730
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL----EEEKEDKAL------EIKKQEWKLEQLAAdlsK 466
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  731 LRRKYScDRSATVTRLEDLLQDAQDEKEQLN---------------------------------------EYKGHL-SGL 770
Cdd:TIGR02169  467 YEQELY-DLKEEYDRVEKELSKLQRELAEAEaqaraseervrggraveevlkasiqgvhgtvaqlgsvgeRYATAIeVAA 545
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  771 AKRAKAVV-----------QLKPRHPAhpmrGRLPLLAVCDYKQVEVTVHKGDECQLVGPA----------QPSHWKVLS 829
Cdd:TIGR02169  546 GNRLNNVVveddavakeaiELLKRRKA----GRATFLPLNKMRDERRDLSILSEDGVIGFAvdlvefdpkyEPAFKYVFG 621
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  830 SSGseaavpsvcfLVpppnqEAQEAVTRLEAQHQaLVTLWHQLhVDMKSLLAWQSLRRDVQLIRSwslatfRTLKPEEQR 909
Cdd:TIGR02169  622 DTL----------VV-----EDIEAARRLMGKYR-MVTLEGEL-FEKSGAMTGGSRAPRGGILFS------RSEPAELQR 678
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  910 QA--LHSLElhyqaflrdsqdaggfGPEDRLMAEREygscshHYQQLLQSLEqgaQEESRCQRCISELKDIRLQLEACET 987
Cdd:TIGR02169  679 LRerLEGLK----------------RELSSLQSELR------RIENRLDELS---QELSDASRKIGEIEKEIEQLEQEEE 733
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  988 RTVHRLRLPLDK--EPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPSP---------AAPTLRSELELT 1056
Cdd:TIGR02169  734 KLKERLEELEEDlsSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelsKLEEEVSRIEAR 813
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1057 LGKLEQV---RSLSAIYLEKLKtislvirgtQGAEEVLRAHEEQLKE-AQAVPATLPELEATKASLKKLRAQAEAQQPTF 1132
Cdd:TIGR02169  814 LREIEQKlnrLTLEKEYLEKEI---------QELQEQRIDLKEQIKSiEKEIENLNGKKEELEEELEELEAALRDLESRL 884
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1133 DALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDvrqrELEQLGRQLRYYRESADPLGAWLQDA 1212
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLEDVQAEL 960
                          890       900       910       920
                   ....*....|....*....|....*....|....*....|.
gi 2217372302 1213 RRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHgEKVEE 1253
Cdd:TIGR02169  961 QRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKR-AKLEE 1000
PLEC smart00250
Plectin repeat;
2656-2692 2.26e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.62  E-value: 2.26e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  2656 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDT 2692
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1550-1588 2.52e-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: 2.52e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 1550 YLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTALIL 1588
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
mukB PRK04863
chromosome partition protein MukB;
1087-1256 2.74e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.34  E-value: 2.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1087 AEEVLRAHEEQLKEAQAVP---ATLPELEatkaslKKLRAQAEAQQptfdaLRDELRGAQEVG-------ERLQQRHGER 1156
Cdd:PRK04863   498 ARELLRRLREQRHLAEQLQqlrMRLSELE------QRLRQQQRAER-----LLAEFCKRLGKNlddedelEQLQEELEAR 566
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1157 dveVERWRERVAQLLERwqavlaQTDVRQrELEQLGRQLRYYRESADplgAWL--QDARRRQEQIQAMPLADSQAVRE-- 1232
Cdd:PRK04863   567 ---LESLSESVSEARER------RMALRQ-QLEQLQARIQRLAARAP---AWLaaQDALARLREQSGEEFEDSQDVTEym 633
                          170       180
                   ....*....|....*....|....*.
gi 2217372302 1233 --QLRQEQALLEEIERHGEKVEECQR 1256
Cdd:PRK04863   634 qqLLERERELTVERDELAARKQALDE 659
PLEC smart00250
Plectin repeat;
2209-2243 3.18e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.18e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2217372302  2209 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 2243
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
3244-3281 3.55e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.55e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2217372302  3244 QRFLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTA 3281
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2825-2859 3.80e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.80e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2217372302  2825 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 2859
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
3134-3167 5.36e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 5.36e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2217372302  3134 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 3167
Cdd:smart00250    5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PTZ00121 PTZ00121
MAEBL; Provisional
999-1428 7.26e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 7.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  999 KEPARECAQRIAEQQKAQAEveglGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTlGKLEQVR---SLSAIYLEKLK 1075
Cdd:PTZ00121  1397 KKKAEEDKKKADELKKAAAA----KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK-KKAEEAKkaeEAKKKAEEAKK 1471
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1076 TISLVIRGTQG--AEEVLRAHEEQLKEA----QAVPATLPELEATKASLKKLRAQAEAQQPTFDAlrDELRGAQEVGERL 1149
Cdd:PTZ00121  1472 ADEAKKKAEEAkkADEAKKKAEEAKKKAdeakKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA--DEAKKAEEKKKAD 1549
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1150 QQRHGE--RDVEVERWRERVAQLLERWQAVLAQTDV-RQRELEQLGRQLRYYRESADPLGAWLQDARrrQEQIQAmplad 1226
Cdd:PTZ00121  1550 ELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEaKKAEEARIEEVMKLYEEEKKMKAEEAKKAE--EAKIKA----- 1622
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1227 sqavrEQLRQEQALLEEIERHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAKKPkvqsgSESVIQEYVDLR 1306
Cdd:PTZ00121  1623 -----EELKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKK-----AEEAKKAEEDEK 1688
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1307 THYSELTTLTSQYIKfiSETLRRMEEEEMQTVQQeqllqetqaLQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKA 1386
Cdd:PTZ00121  1689 KAAEALKKEAEEAKK--AEELKKKEAEEKKKAEE---------LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2217372302 1387 QQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRK 1428
Cdd:PTZ00121  1758 KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
SPEC smart00150
Spectrin repeats;
1096-1189 7.43e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 44.24  E-value: 7.43e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  1096 EQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALrdelrgaQEVGERLQQRHGERDVEVErwrERVAQLLERWQ 1175
Cdd:smart00150   18 EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEAL-------NELGEQLIEEGHPDAEEIE---ERLEELNERWE 87
                            90
                    ....*....|....
gi 2217372302  1176 AVLAQTDVRQRELE 1189
Cdd:smart00150   88 ELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
2544-2579 8.93e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.08  E-value: 8.93e-05
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 2217372302  2544 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVA 2579
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2284-2315 9.11e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.08  E-value: 9.11e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2217372302  2284 QLLSAEKAVTGYRDPYSGSTISLFQAMQKGLV 2315
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
SPEC smart00150
Spectrin repeats;
508-602 1.32e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.47  E-value: 1.32e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   508 LRYLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARSDEGQL---SPATRGAYRDCLGRLD 584
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
                            90
                    ....*....|....*...
gi 2217372302   585 LQYAKLLNSSKARLRSLE 602
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
1588-1621 1.42e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.42e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2217372302  1588 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPE 1621
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2209-2243 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 2217372302 2209 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 2243
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPET 35
PLEC smart00250
Plectin repeat;
2619-2655 1.85e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.85e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  2619 RLLSAERAVTGYRDPYTEQTISLFQAMKKELIPTEEA 2655
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
1916-1950 2.18e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.93  E-value: 2.18e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2217372302  1916 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEF 1950
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
1990-2026 2.20e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.93  E-value: 2.20e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  1990 LRLLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEET 2026
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
Rabaptin pfam03528
Rabaptin;
1088-1385 2.91e-04

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 46.64  E-value: 2.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1088 EEVLRAHEEQLKEAQAVpatlpeLEATKASLKKLRAQ-AEAQqptfdALRDELRGAQEVGERLQQrhgERDVEVER-WRE 1165
Cdd:pfam03528   39 KELYLAKEEDLKRQNAV------LQEAQVELDALQNQlALAR-----AEMENIKAVATVSENTKQ---EAIDEVKSqWQE 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1166 RVAQLlerwQAVLAQTdVRQRE------LEQLGRQLRYYRESADPLGAwlqDARRRqeqiqampLADSQavreqlrQEQA 1239
Cdd:pfam03528  105 EVASL----QAIMKET-VREYEvqfhrrLEQERAQWNQYRESAEREIA---DLRRR--------LSEGQ-------EEEN 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1240 LLEEIERHGEKVEECQRFA---KQYINAIKDYELQLVTYKAQLEpvASPAKK----PKVQSGSESVIQEYVD-LRTHYSE 1311
Cdd:pfam03528  162 LEDEMKKAQEDAEKLRSVVmpmEKEIAALKAKLTEAEDKIKELE--ASKMKElnhyLEAEKSCRTDLEMYVAvLNTQKSV 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1312 LTTLTSQYIKFISETLRRMEEEEMQtvqqeqllqeTQALQQSFLSEKDSLLQRERFIEQEKAKL------EQLFQDEVAK 1385
Cdd:pfam03528  240 LQEDAEKLRKELHEVCHLLEQERQQ----------HNQLKHTWQKANDQFLESQRLLMRDMQRMesvltsEQLRQVEEIK 309
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2544-2582 4.66e-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: 4.66e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 2544 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVARLL 2582
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
1548-1585 1.11e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.00  E-value: 1.11e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2217372302  1548 RHYLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTA 1585
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
604-697 1.87e-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: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  604 LHSFVAAATKELMWLNEKEE----EEVGFDWsdrnTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTV 679
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEAllssEDYGKDL----ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90
                   ....*....|....*...
gi 2217372302  680 ESFQAALQTQWSWMLQLC 697
Cdd:pfam00435   79 QERLEELNERWEQLLELA 96
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
827-1384 2.18e-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: 2.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  827 VLSSSGSEAAVPSVCFLVPPPNQEAQEAVTRLEAQHQALVTLWHQLHVDMKSLlawqslrRDVQLIRSWSLATFRTLKPE 906
Cdd:pfam05483  246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKEL-------EDIKMSLQRSMSTQKALEED 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  907 EQ--RQALHSLELHYQAFLRDSQDAGGfgPEDRLMAEREYGSCShhYQQLLQSleqgaqEESRCQRCISELKDIRLQLEA 984
Cdd:pfam05483  319 LQiaTKTICQLTEEKEAQMEELNKAKA--AHSFVVTEFEATTCS--LEELLRT------EQQRLEKNEDQLKIITMELQK 388
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  985 CETRTVHRLRLPLDKEPARECAQRI-AEQQKAQAEVEGLGKGVARLSAEAEKVLALPEpSPAAPTLRSELELTLGK---- 1059
Cdd:pfam05483  389 KSSELEEMTKFKNNKEVELEELKKIlAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQ-AREKEIHDLEIQLTAIKtsee 467
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1060 --LEQVRSL-SAIYLEKLKTISLvirgTQGAEEVLRAHEEQLKEAQAVPATLP----ELEATKASLKKLRAQAEAQQPTF 1132
Cdd:pfam05483  468 hyLKEVEDLkTELEKEKLKNIEL----TAHCDKLLLENKELTQEASDMTLELKkhqeDIINCKKQEERMLKQIENLEEKE 543
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1133 DALRDELrgaQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLryyresadplgawlQDA 1212
Cdd:pfam05483  544 MNLRDEL---ESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI--------------ENK 606
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1213 RRRQEQIQAmplaDSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKD-YELQLVTYKAQLEPVASPAKKPKV 1291
Cdd:pfam05483  607 NKNIEELHQ----ENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDnYQKEIEDKKISEEKLLEEVEKAKA 682
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1292 QSGSESVIQEYVDLRTHYSelttltsqyikfISETLRRMEEEEMQtvqqeqllqetqalQQSFLSEKDSLLQRERFIEQE 1371
Cdd:pfam05483  683 IADEAVKLQKEIDKRCQHK------------IAEMVALMEKHKHQ--------------YDKIIEERDSELGLYKNKEQE 736
                          570
                   ....*....|...
gi 2217372302 1372 KAKLEQLFQDEVA 1384
Cdd:pfam05483  737 QSSAKAALEIELS 749
PLEC smart00250
Plectin repeat;
2862-2893 4.09e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.46  E-value: 4.09e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2217372302  2862 KLLSAERAVTGYKDPYSGKLISLFQAMKKGLI 2893
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3140-3170 4.48e-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: 4.48e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2217372302 3140 AGILDTETLEKVSITEAMHRNLVDNITGQRL 3170
Cdd:pfam00681    9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
 
Name Accession Description Interval E-value
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
13-140 5.65e-78

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: 254.14  E-value: 5.65e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   13 QAYEEVREKYKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIA 92
Cdd:cd21236      1 QAYENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIA 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2217372302   93 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 140
Cdd:cd21236     81 LDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
27-131 8.51e-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: 8.51e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   27 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNI 106
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
                           90       100
                   ....*....|....*....|....*
gi 2217372302  107 RNDDIADGNPKLTLGLIWTIILHFQ 131
Cdd:cd21188     81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
24-142 3.50e-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: 3.50e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   24 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 103
Cdd:cd21235      1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2217372302  104 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 142
Cdd:cd21235     81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
144-249 1.52e-72

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


Pssm-ID: 409087  Cd Length: 106  Bit Score: 237.61  E-value: 1.52e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  144 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 223
Cdd:cd21238      1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 2217372302  224 PEDVDVPQPDEKSIITYVSSLYDAMP 249
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
145-249 1.63e-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: 1.63e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  145 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 224
Cdd:cd21189      1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                           90       100
                   ....*....|....*....|....*
gi 2217372302  225 EDVDVPQPDEKSIITYVSSLYDAMP 249
Cdd:cd21189     81 EDVDVPEPDEKSIITYVSSLYDVFP 105
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
24-141 1.13e-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: 1.13e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   24 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 103
Cdd:cd21237      1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2217372302  104 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 141
Cdd:cd21237     81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
145-249 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 2217372302  145 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 224
Cdd:cd21239      1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
                           90       100
                   ....*....|....*....|....*
gi 2217372302  225 EDVDVPQPDEKSIITYVSSLYDAMP 249
Cdd:cd21239     80 EDVDVSSPDEKSVITYVSSLYDVFP 104
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
143-249 2.28e-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: 2.28e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  143 DMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 222
Cdd:cd21240      2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
                           90       100
                   ....*....|....*....|....*..
gi 2217372302  223 DPEDVDVPQPDEKSIITYVSSLYDAMP 249
Cdd:cd21240     81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
29-132 8.94e-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: 8.94e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   29 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 107
Cdd:cd21186      2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
                           90       100
                   ....*....|....*....|....*
gi 2217372302  108 NDDIADGNPKLTLGLIWTIILHFQI 132
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 ...
15-128 4.43e-49

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: 171.01  E-value: 4.43e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   15 YEEVREK-YKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIA 92
Cdd:cd21246      1 FERSRIKaLADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKA 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2217372302   93 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 128
Cdd:cd21246     81 LQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
28-356 8.92e-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: 8.92e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   28 RVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLV 104
Cdd:COG5069      8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  105 NIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTSSWRDGRLFNAII 183
Cdd:COG5069     88 NIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALI 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  184 HRHKPLLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS------SLYD----AMPR 250
Cdd:COG5069    165 HDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyiirfGLLEkidiALHR 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  251 VPDVQDGVRANElQLRwQEYRELVLLLLQWMRHHTAAFEERRFPSSFEEIEILWSQFLKFKEME--LPAKEAD-KNRSKG 327
Cdd:COG5069    245 VYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCsrAPLETTDlHSLAGQ 322
                          330       340
                   ....*....|....*....|....*....
gi 2217372302  328 IYQSLEgAVQAGQLKVPPGYHPLDVEKEW 356
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 ...
145-245 6.76e-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: 6.76e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  145 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 224
Cdd:cd21194      2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
                           90       100
                   ....*....|....*....|.
gi 2217372302  225 EDVDVPQPDEKSIITYVSSLY 245
Cdd:cd21194     82 EDVDVARPDEKSIMTYVASYY 102
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
15-128 1.47e-45

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: 160.92  E-value: 1.47e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   15 YEEVR-EKYKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIA 92
Cdd:cd21193      1 FEKGRiRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKA 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2217372302   93 LDYLrHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 128
Cdd:cd21193     81 LAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
25-132 5.35e-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: 5.35e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   25 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLRHRQ 100
Cdd:cd21241      1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2217372302  101 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 132
Cdd:cd21241     81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
25-132 3.54e-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: 156.96  E-value: 3.54e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   25 ERDRVQKKTFTKWVNKHLikaQRH-----ISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 97
Cdd:cd21190      1 EQERVQKKTFTNWINSHL---AKLsqpivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2217372302   98 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 132
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 ...
145-245 4.61e-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: 4.61e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  145 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 224
Cdd:cd21248      2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
                           90       100
                   ....*....|....*....|.
gi 2217372302  225 EDVDVPQPDEKSIITYVSSLY 245
Cdd:cd21248     82 EDVNVEQPDEKSIITYVVTYY 102
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
144-249 6.04e-42

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


Pssm-ID: 409092  Cd Length: 109  Bit Score: 150.16  E-value: 6.04e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  144 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 223
Cdd:cd21243      4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
                           90       100
                   ....*....|....*....|....*.
gi 2217372302  224 PEDVDVPQPDEKSIITYVSSLYDAMP 249
Cdd:cd21243     84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
4-128 3.29e-41

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: 149.41  E-value: 3.29e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302    4 PLPDEQDFIQAYEEVREK-YKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRM 81
Cdd:cd21318     12 PWDEPAATAKLFECSRIKaLADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRM 91
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2217372302   82 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 128
Cdd:cd21318     92 RIHSLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
132-247 5.34e-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: 5.34e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  132 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 211
Cdd:cd21216      1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2217372302  212 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 247
Cdd:cd21216     77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
15-128 1.11e-40

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: 147.51  E-value: 1.11e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   15 YEEVREK-YKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIA 92
Cdd:cd21317     16 FERSRIKaLADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKA 95
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2217372302   93 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 128
Cdd:cd21317     96 LQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
27-128 2.08e-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: 2.08e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   27 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVKLVN 105
Cdd:cd21214      3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
                           90       100
                   ....*....|....*....|...
gi 2217372302  106 IRNDDIADGNPKLTLGLIWTIIL 128
Cdd:cd21214     83 IGAEEIVDGNLKMTLGMIWTIIL 105
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
25-132 8.90e-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: 8.90e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   25 ERDRVQKKTFTKWVNKHLIKAQ--RHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 102
Cdd:cd21242      1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 2217372302  103 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 132
Cdd:cd21242     81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
141-245 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 2217372302  141 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 220
Cdd:cd21319      1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
                           90       100
                   ....*....|....*....|....*
gi 2217372302  221 LLDPEDVDVPQPDEKSIITYVSSLY 245
Cdd:cd21319     81 LLDPEDVFTENPDEKSIITYVVAFY 105
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
29-130 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 2217372302   29 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 106
Cdd:cd21215      4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
                           90       100
                   ....*....|....*....|....
gi 2217372302  107 RNDDIADGNPKLTLGLIWTIILHF 130
Cdd:cd21215     84 GAEDIVDGNLKLILGLLWTLILRF 107
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
141-245 5.01e-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: 5.01e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  141 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 220
Cdd:cd21321      1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
                           90       100
                   ....*....|....*....|....*
gi 2217372302  221 LLDPEDVDVPQPDEKSIITYVSSLY 245
Cdd:cd21321     81 LLDPEDVNVDQPDEKSIITYVATYY 105
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
24-132 1.83e-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: 1.83e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   24 DERDRVQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 102
Cdd:cd21231      1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 2217372302  103 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 132
Cdd:cd21231     81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
144-245 2.77e-37

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


Pssm-ID: 409098  Cd Length: 109  Bit Score: 136.92  E-value: 2.77e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  144 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 223
Cdd:cd21249      3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
                           90       100
                   ....*....|....*....|..
gi 2217372302  224 PEDVDVPQPDEKSIITYVSSLY 245
Cdd:cd21249     83 PEDVAVPHPDERSIMTYVSLYY 104
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
129-245 4.26e-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: 4.26e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  129 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQA 208
Cdd:cd21322      1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2217372302  209 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 245
Cdd:cd21322     81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
148-249 1.14e-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: 1.14e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  148 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 226
Cdd:cd21187      2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
                           90       100
                   ....*....|....*....|...
gi 2217372302  227 VDVPQPDEKSIITYVSSLYDAMP 249
Cdd:cd21187     82 VNVEQPDKKSILMYVTSLFQVLP 104
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
28-133 2.33e-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: 2.33e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   28 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQ-VKLV 104
Cdd:cd21311     14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
                           90       100
                   ....*....|....*....|....*....
gi 2217372302  105 NIRNDDIADGNPKLTLGLIWTIILHFQIS 133
Cdd:cd21311     94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
7-128 1.35e-33

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


Pssm-ID: 409165  Cd Length: 154  Bit Score: 128.24  E-value: 1.35e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302    7 DEQDFIQAYEEVREK-YKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFH 84
Cdd:cd21316     30 NENSSARLFERSRIKaLADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIH 109
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2217372302   85 KLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 128
Cdd:cd21316    110 CLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
29-132 2.42e-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: 2.42e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   29 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 106
Cdd:cd21227      4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
                           90       100
                   ....*....|....*....|....*.
gi 2217372302  107 RNDDIADGNPKLTLGLIWTIILHFQI 132
Cdd:cd21227     84 GNEDIVNGNLKLILGLIWHLILRYQI 109
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
144-242 3.23e-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: 3.23e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  144 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 223
Cdd:cd21192      2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
                           90
                   ....*....|....*....
gi 2217372302  224 PEDVDVPQPDEKSIITYVS 242
Cdd:cd21192     82 VEDVLVDKPDERSIMTYVS 100
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
29-132 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 2217372302   29 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 107
Cdd:cd21232      2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
                           90       100
                   ....*....|....*....|....*
gi 2217372302  108 NDDIADGNPKLTLGLIWTIILHFQI 132
Cdd:cd21232     82 GTDIVDGNHKLTLGLLWSIILHWQV 106
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
145-245 1.40e-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: 1.40e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  145 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 224
Cdd:cd21320      2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
                           90       100
                   ....*....|....*....|.
gi 2217372302  225 EDVDVPQPDEKSIITYVSSLY 245
Cdd:cd21320     82 EDISVDHPDEKSIITYVVTYY 102
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
144-242 6.24e-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: 6.24e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  144 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 223
Cdd:cd21244      4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
                           90
                   ....*....|....*....
gi 2217372302  224 PEDVDVPQPDEKSIITYVS 242
Cdd:cd21244     84 PEDVDVVNPDEKSIMTYVA 102
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
132-247 2.46e-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: 2.46e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  132 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 211
Cdd:cd21291      1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2217372302  212 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 247
Cdd:cd21291     77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
25-134 3.81e-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: 3.81e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   25 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQ 100
Cdd:cd21191      1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2217372302  101 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 134
Cdd:cd21191     81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
148-249 3.92e-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: 3.92e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  148 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 226
Cdd:cd21234      2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
                           90       100
                   ....*....|....*....|...
gi 2217372302  227 VDVPQPDEKSIITYVSSLYDAMP 249
Cdd:cd21234     82 VAVQLPDKKSIIMYLTSLFEVLP 104
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
148-250 5.47e-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: 119.26  E-value: 5.47e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  148 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 225
Cdd:cd21233      2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
                           90       100
                   ....*....|....*....|....*
gi 2217372302  226 DVDVPQPDEKSIITYVSSLYDAMPR 250
Cdd:cd21233     82 DVATAHPDKKSILMYVTSLFQVLPQ 106
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
880-957 6.24e-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: 6.24e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217372302  880 LAWQSLRRDVQLIRSWSLATFRTLKPEEQRQALHSLELHYQAFLRDSQDAGGFGPEDRLMAEREYGSCSHHYQQLLQS 957
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
28-130 2.67e-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: 117.20  E-value: 2.67e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   28 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 104
Cdd:cd21183      3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
                           90       100
                   ....*....|....*....|....*.
gi 2217372302  105 NIRNDDIADGNPKLTLGLIWTIILHF 130
Cdd:cd21183     83 NIGSGDIVNGNIKLILGLIWTLILHY 108
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
150-245 3.10e-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: 3.10e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  150 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 228
Cdd:cd21253      6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
                           90
                   ....*....|....*..
gi 2217372302  229 VPQPDEKSIITYVSSLY 245
Cdd:cd21253     86 LKVPDKLSILTYVSQYY 102
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
130-247 8.33e-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: 8.33e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  130 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAF 209
Cdd:cd21290      2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2217372302  210 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 247
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 ...
148-247 1.36e-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: 1.36e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  148 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 226
Cdd:cd22198      3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
                           90       100
                   ....*....|....*....|.
gi 2217372302  227 VDVPQPDEKSIITYVSSLYDA 247
Cdd:cd22198     83 ASLAVPDKLSMVSYLSQFYEA 103
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
28-130 5.66e-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: 5.66e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   28 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 104
Cdd:cd21228      3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
                           90       100
                   ....*....|....*....|....*.
gi 2217372302  105 NIRNDDIADGNPKLTLGLIWTIILHF 130
Cdd:cd21228     83 SIDSSAIVDGNLKLILGLIWTLILHY 108
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
132-247 1.07e-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: 1.07e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  132 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 211
Cdd:cd21287      1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2217372302  212 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 247
Cdd:cd21287     77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
28-133 2.43e-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: 2.43e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   28 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHRQVKLV 104
Cdd:cd21310     15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
                           90       100
                   ....*....|....*....|....*....
gi 2217372302  105 NIRNDDIADGNPKLTLGLIWTIILHFQIS 133
Cdd:cd21310     95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
132-247 3.19e-27

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


Pssm-ID: 409138  Cd Length: 124  Bit Score: 109.04  E-value: 3.19e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  132 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 211
Cdd:cd21289      1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2217372302  212 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 247
Cdd:cd21289     77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
13-132 5.89e-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: 108.31  E-value: 5.89e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   13 QAYEEVR-EKYKDERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQN 88
Cdd:cd21247      3 TEYEKGHiRKLQEQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLEN 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2217372302   89 VQIALDYLRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 132
Cdd:cd21247     83 NSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
132-247 9.39e-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: 9.39e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  132 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 211
Cdd:cd21288      1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2217372302  212 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 247
Cdd:cd21288     77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
32-129 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 2217372302    32 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKLVNIR 107
Cdd:smart00033    1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 2217372302   108 NDDIADGnPKLTLGLIWTIILH 129
Cdd:smart00033   81 PEDLVEG-PKLILGVIWTLISL 101
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
150-245 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 2217372302  150 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 228
Cdd:cd21197      5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
                           90
                   ....*....|....*..
gi 2217372302  229 VPQPDEKSIITYVSSLY 245
Cdd:cd21197     85 MHVPDRLSIITYVSQYY 101
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
148-248 5.65e-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: 5.65e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  148 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 227
Cdd:cd21226      3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
                           90       100
                   ....*....|....*....|.
gi 2217372302  228 DVPQPDEKSIITYVSSLYDAM 248
Cdd:cd21226     83 MTGNPDERSIVLYTSLFYHAF 103
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
144-250 9.22e-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: 9.22e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  144 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 220
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2217372302  221 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 250
Cdd:pfam00307   81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
29-132 1.67e-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: 1.67e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   29 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-VKLV 104
Cdd:pfam00307    2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
                           90       100
                   ....*....|....*....|....*...
gi 2217372302  105 NIRNDDIADGNPKLTLGLIWTIILHFQI 132
Cdd:pfam00307   82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
146-245 4.28e-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: 4.28e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  146 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 225
Cdd:cd21252      1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
                           90       100
                   ....*....|....*....|.
gi 2217372302  226 D-VDVPQPDEKSIITYVSSLY 245
Cdd:cd21252     81 DmVSMKVPDCLSIMTYVSQYY 101
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
145-249 4.35e-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: 4.35e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  145 TAKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 224
Cdd:cd21245      3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
                           90       100
                   ....*....|....*....|....*
gi 2217372302  225 EDVDVPQPDEKSIITYVSSLYDAMP 249
Cdd:cd21245     82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
145-245 2.92e-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: 2.92e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  145 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 224
Cdd:cd21198      1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
                           90       100
                   ....*....|....*....|..
gi 2217372302  225 EDVDVPQ-PDEKSIITYVSSLY 245
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 ...
28-133 4.83e-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: 4.83e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   28 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 104
Cdd:cd21308     19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
                           90       100
                   ....*....|....*....|....*....
gi 2217372302  105 NIRNDDIADGNPKLTLGLIWTIILHFQIS 133
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 ...
28-133 6.06e-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: 6.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   28 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 104
Cdd:cd21309     16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
                           90       100
                   ....*....|....*....|....*....
gi 2217372302  105 NIRNDDIADGNPKLTLGLIWTIILHFQIS 133
Cdd:cd21309     96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
145-243 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 2217372302  145 TAKEKLLLWSQRMVEGYqglRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 223
Cdd:cd21184      1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
                           90       100
                   ....*....|....*....|
gi 2217372302  224 PEDVDVPQPDEKSIITYVSS 243
Cdd:cd21184     78 PEDMVSPNVDELSVMTYLSY 97
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
779-845 4.68e-22

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 91.94  E-value: 4.68e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217372302  779 QLKPRhpAHPMRGRLPLLAVCDYKQVEVTVHKGDECQLVGPAQPSHWKVLSSSGSEAAVPSVCFLVP 845
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), ...
149-246 2.51e-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: 2.51e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  149 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 227
Cdd:cd21195      8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
                           90
                   ....*....|....*....
gi 2217372302  228 DVPQPDEKSIITYVSSLYD 246
Cdd:cd21195     88 SAQEPDKLSMVMYLSKFYE 106
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
145-245 3.88e-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: 3.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  145 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 224
Cdd:cd21200      1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
                           90       100
                   ....*....|....*....|...
gi 2217372302  225 EDVDV--PQPDEKSIITYVSSLY 245
Cdd:cd21200     81 EDMVRmgNRPDWKCVFTYVQSLY 103
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
141-246 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 2217372302  141 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 220
Cdd:cd21251      1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
                           90       100
                   ....*....|....*....|....*..
gi 2217372302  221 LLDPEDV-DVPQPDEKSIITYVSSLYD 246
Cdd:cd21251     81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
145-244 2.66e-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: 2.66e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  145 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 224
Cdd:cd21255      1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
                           90       100
                   ....*....|....*....|.
gi 2217372302  225 ED-VDVPQPDEKSIITYVSSL 244
Cdd:cd21255     80 ADmVLLPIPDKLIVMTYLCQL 100
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
148-244 3.48e-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: 3.48e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   148 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 223
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 2217372302   224 PEDVDVPQPDEKSIITYVSSL 244
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
30-130 7.32e-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: 7.32e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   30 QKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVKLVN 105
Cdd:cd21212      1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
                           90       100
                   ....*....|....*....|....*
gi 2217372302  106 IRNDDIADGNPKLTLGLIWTIILHF 130
Cdd:cd21212     81 ITAEDIVDGNLKAILGLFFSLSRYK 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
604-793 1.15e-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: 1.15e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  604 LHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQ 683
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  684 AALQTQWSWMLQLCCCIEAHLKENAAYFQFFSDVREAEGQLQKLQEALRrkySCDRSATVTRLEDLLQDAQDEKEQLNEY 763
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190
                   ....*....|....*....|....*....|
gi 2217372302  764 KGHLSGLAKRAKAVVQLKPRHPAHPMRGRL 793
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
31-128 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 2217372302   31 KKTFTKWVNKHL-IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQV-KLVNI 106
Cdd:cd00014      1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
                           90       100
                   ....*....|....*....|...
gi 2217372302  107 RNDDI-ADGNPKLTLGLIWTIIL 128
Cdd:cd00014     81 EPEDLyEKGNLKKVLGTLWALAL 103
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
149-246 3.31e-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: 3.31e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  149 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 227
Cdd:cd21250      8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
                           90
                   ....*....|....*....
gi 2217372302  228 DVPQPDEKSIITYVSSLYD 246
Cdd:cd21250     88 SAEEPDKLSMVMYLSKFYE 106
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
145-244 3.95e-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: 3.95e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  145 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 224
Cdd:cd21254      1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
                           90       100
                   ....*....|....*....|.
gi 2217372302  225 ED-VDVPQPDEKSIITYVSSL 244
Cdd:cd21254     80 SDmVLLAVPDKLTVMTYLYQI 100
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
147-258 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 2217372302  147 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 226
Cdd:cd21259      3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2217372302  227 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 258
Cdd:cd21259     83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
150-245 4.66e-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: 4.66e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  150 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 228
Cdd:cd21199     13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
                           90
                   ....*....|....*..
gi 2217372302  229 VPQPDEKSIITYVSSLY 245
Cdd:cd21199     92 MERPDWQSVMSYVTAIY 108
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
147-246 6.42e-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: 6.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  147 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 226
Cdd:cd21261      3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
                           90       100
                   ....*....|....*....|..
gi 2217372302  227 VDV--PQPDEKSIITYVSSLYD 246
Cdd:cd21261     83 MMVmgRKPDPMCVFTYVQSLYN 104
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2901-2939 9.12e-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: 9.12e-16
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 2901 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 2939
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
147-250 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 2217372302  147 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 226
Cdd:cd21258      3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
                           90       100
                   ....*....|....*....|....*.
gi 2217372302  227 VDV--PQPDEKSIITYVSSLYDAMPR 250
Cdd:cd21258     83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
27-126 1.11e-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: 1.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   27 DRVQKKTFTKWVNKHLIKAQ-RHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHR-QV 101
Cdd:cd21225      2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
                           90       100
                   ....*....|....*....|....*
gi 2217372302  102 KLVNIRNDDIADGNPKLTLGLIWTI 126
Cdd:cd21225     82 RVQGIGAEDFVDNNKKLILGLLWTL 106
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1664-1702 3.68e-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: 3.68e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 1664 LLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEMNRVL 1702
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2582-2620 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 2217372302 2582 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 2620
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
30-130 4.61e-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: 4.61e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   30 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRHRQV 101
Cdd:cd21213      1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
                           90       100
                   ....*....|....*....|....*....
gi 2217372302  102 KLVNIRNDDIADGNPKLTLGLIWTIILHF 130
Cdd:cd21213     77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2323-2361 6.73e-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: 6.73e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 2323 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEMNRVL 2361
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
24-129 9.43e-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: 9.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   24 DERDrvqKKTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHKLQNVQIAL 93
Cdd:cd21219      2 GSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVENCNYAV 71
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2217372302   94 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 129
Cdd:cd21219     72 DLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1088-1278 1.34e-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: 1.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1088 EEVLRAHEEQLKEAQaVPATLPELEATKASLKKLRAQAEAQQPTFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1167
Cdd:cd00176     13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1168 AQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLGAWLQDArrrQEQIQAMPLADS-QAVREQLRQEQALLEEIER 1246
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEK---EAALASEDLGKDlESVEELLKKHKELEEELEA 157
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2217372302 1247 HGEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1278
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
145-245 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 2217372302  145 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 224
Cdd:cd21256     14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
                           90       100
                   ....*....|....*....|..
gi 2217372302  225 ED-VDVPQPDEKSIITYVSSLY 245
Cdd:cd21256     93 NEmVRTERPDWQSVMTYVTAIY 114
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
147-248 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 2217372302  147 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 226
Cdd:cd21260      3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
                           90       100
                   ....*....|....*....|...
gi 2217372302  227 -VDVPQPDEKSIITYVSSLYDAM 248
Cdd:cd21260     83 mVRMSVPDSKCVYTYIQELYRSL 105
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
145-242 5.63e-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: 5.63e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  145 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 223
Cdd:cd21230      1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPgLCPDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
                           90
                   ....*....|....*....
gi 2217372302  224 PEDVDVPQPDEKSIITYVS 242
Cdd:cd21230     78 PEEIINPNVDEMSVMTYLS 96
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
508-697 6.45e-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: 6.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  508 LRYLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARSDEGQLSPATRGAY---RDCLGRLD 584
Cdd:cd00176      6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  585 LQYAKLLNSSKARLRSLE---SLHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKEL 661
Cdd:cd00176     86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2217372302  662 QNAGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 697
Cdd:cd00176    166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
145-245 1.25e-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: 1.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  145 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 224
Cdd:cd21257      8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
                           90       100
                   ....*....|....*....|..
gi 2217372302  225 ED-VDVPQPDEKSIITYVSSLY 245
Cdd:cd21257     87 SEmMYTDRPDWQSVMQYVAQIY 108
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1916-1954 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 2217372302 1916 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEFHEKL 1954
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
48-127 3.38e-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: 3.38e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   48 HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQV----KLVNIRNDDIADGNPKLT 119
Cdd:cd21223     25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104

                   ....*...
gi 2217372302  120 LGLIWTII 127
Cdd:cd21223    105 LALLWRII 112
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
15-133 3.45e-13

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


Pssm-ID: 409147  Cd Length: 117  Bit Score: 68.42  E-value: 3.45e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   15 YEEVREKykderdrvqkKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQ 87
Cdd:cd21298      2 IEETREE----------KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIE 69
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2217372302   88 NVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 133
Cdd:cd21298     70 NCNYAVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3170-3208 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 2217372302 3170 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 3208
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1992-2030 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 2217372302 1992 LLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEETSRAL 2030
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1588-1626 2.22e-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: 2.22e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 1588 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHKL 1626
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
147-242 2.26e-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: 2.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  147 KEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 225
Cdd:cd21229      5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPgLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
                           90
                   ....*....|....*..
gi 2217372302  226 DVDVPQPDEKSIITYVS 242
Cdd:cd21229     82 DLSSPHLDELSGMTYLS 98
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2825-2863 2.86e-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: 2.86e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 2825 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 2863
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
147-247 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 2217372302  147 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 226
Cdd:cd21196      5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
                           90       100
                   ....*....|....*....|.
gi 2217372302  227 VdVPQPDEKSIITYVSSLYDA 247
Cdd:cd21196     85 V-VAGSDPLGLIAYLSHFHSA 104
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2658-2696 3.06e-12

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 63.12  E-value: 3.06e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 2658 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 2696
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
147-246 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 2217372302  147 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 222
Cdd:cd00014      1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
                           90       100
                   ....*....|....*....|....
gi 2217372302  223 DPEDVdVPQPDEKSIITYVSSLYD 246
Cdd:cd00014     81 EPEDL-YEKGNLKKVLGTLWALAL 103
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
25-124 5.28e-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: 5.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   25 ERDRvQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQNVQIALDYL 96
Cdd:cd21300      4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYAVELG 80
                           90       100
                   ....*....|....*....|....*...
gi 2217372302   97 RHRQVKLVNIRNDDIADGNPKLTLGLIW 124
Cdd:cd21300     81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3246-3284 1.00e-10

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: 1.00e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 3246 FLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTAQKL 3284
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
31-127 2.78e-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: 2.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   31 KKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDYL 96
Cdd:cd21217      3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2217372302   97 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 127
Cdd:cd21217     83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
20-130 3.79e-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: 59.91  E-value: 3.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   20 EKYKDERDRVQ--KKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNVQIAL 93
Cdd:cd21222      5 DLFDEAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLAL 84
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2217372302   94 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 130
Cdd:cd21222     85 ELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
952-1282 1.06e-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: 1.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  952 QQLLQSLEQGAQEESRCQRCISELKDirlQLEACETRTVHRLRLPLDKEPARECAQ--RIAEQQKAQAEVEGLGKGVARL 1029
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKAERYQALLKEKREYEGyeLLKEKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1030 SAEAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRGTQG----AEEVLRAHEEQLKE 1100
Cdd:TIGR02169  250 EEELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELED 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1101 AQAVPATL-PELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQllerwqavla 1179
Cdd:TIGR02169  320 AEERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------- 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1180 qtdvRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQamplADSQAVREQLRQEQALLEEIerhGEKVEECQRFAK 1259
Cdd:TIGR02169  390 ----YREKLEKLKREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEKEDK---ALEIKKQEWKLE 458
                          330       340
                   ....*....|....*....|...
gi 2217372302 1260 QYINAIKDYELQLVTYKAQLEPV 1282
Cdd:TIGR02169  459 QLAADLSKYEQELYDLKEEYDRV 481
PLEC smart00250
Plectin repeat;
3168-3205 1.12e-09

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 55.95  E-value: 1.12e-09
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2217372302  3168 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 3205
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
145-247 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 2217372302  145 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 223
Cdd:cd21314     11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPgLCPDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
                           90       100
                   ....*....|....*....|....
gi 2217372302  224 PEDVDVPQPDEKSIITYVSSLYDA 247
Cdd:cd21314     88 PEEIVDPNVDEHSVMTYLSQFPKA 111
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
30-129 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 2217372302   30 QKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLRHRQVKLV 104
Cdd:cd21299      5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
                           90       100
                   ....*....|....*....|....*
gi 2217372302  105 NIRNDDIADGNPKLTLGLIWTIILH 129
Cdd:cd21299     83 NVAGNDIVQGNKKLILALLWQLMRY 107
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
140-242 4.98e-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: 4.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  140 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 218
Cdd:cd21315     11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPgLCPDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
                           90       100
                   ....*....|....*....|....
gi 2217372302  219 TRLLDPEDVDVPQPDEKSIITYVS 242
Cdd:cd21315     88 PQLIKPEEMVNPKVDELSMMTYLS 111
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
140-247 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 2217372302  140 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 218
Cdd:cd21313      3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPgLCPDWESWDPQKPVDNAREAMQQADDWLGV 79
                           90       100
                   ....*....|....*....|....*....
gi 2217372302  219 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 247
Cdd:cd21313     80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
32-126 2.10e-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: 2.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   32 KTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQVKL 103
Cdd:cd21286      3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARGVNV 78
                           90       100
                   ....*....|....*....|...
gi 2217372302  104 VNIRNDDIADGNPKLTLGLIWTI 126
Cdd:cd21286     79 QGLSAEEIRNGNLKAILGLFFSL 101
PLEC smart00250
Plectin repeat;
2899-2935 2.17e-08

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 52.10  E-value: 2.17e-08
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  2899 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 2935
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
149-244 3.15e-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: 3.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  149 KLLL-WSQrMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNL-----------------------EN 204
Cdd:cd21224      3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217372302  205 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 244
Cdd:cd21224     82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
900-1468 3.44e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 3.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  900 FRTLKPEEQRQALHSLELHYQAFLRDSQDAGgfgpEDRLMAEREYGSCSHHYQQLLQSLEQGAQEESRCQRCISELKDIR 979
Cdd:COG1196    215 YRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  980 LQLEACETRTVHRLRLplDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALpepspAAPTLRSELELTLGK 1059
Cdd:COG1196    291 YELLAELARLEQDIAR--LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-----AEEELEEAEAELAEA 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1060 LEQVRSLSAIYLEKLKTISlviRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDEL 1139
Cdd:COG1196    364 EEALLEAEAELAEAEEELE---ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1140 RGAQEvgeRLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQI 1219
Cdd:COG1196    441 EEALE---EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1220 QAMPLAdsQAVREQLRQEQALLEEIE-----RHGEKVEECQRFAKQYINAIKDYELQLVTY--KAQLEPVASPAKKPKVQ 1292
Cdd:COG1196    518 GLRGLA--GAVAVLIGVEAAYEAALEaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpLDKIRARAALAAALARG 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1293 SGSESVIQEYVDLRTH---------YSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALQQSFLSEKDSLLQ 1363
Cdd:COG1196    596 AIGAAVDLVASDLREAdaryyvlgdTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1364 RERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQE 1443
Cdd:COG1196    676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
                          570       580
                   ....*....|....*....|....*
gi 2217372302 1444 ELLAEENQRLREQLQLLEEQhRAAL 1468
Cdd:COG1196    756 LPEPPDLEELERELERLERE-IEAL 779
SPEC smart00150
Spectrin repeats;
605-697 6.07e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.10  E-value: 6.07e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   605 HSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQA 684
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90
                    ....*....|...
gi 2217372302   685 ALQTQWSWMLQLC 697
Cdd:smart00150   81 ELNERWEELKELA 93
PLEC smart00250
Plectin repeat;
2580-2615 1.66e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 49.79  E-value: 1.66e-07
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 2217372302  2580 RLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPE 2615
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 ...
25-132 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 2217372302   25 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRMRFHKLQNVQIALDYLR 97
Cdd:cd21331     18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVELGK 95
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2217372302   98 HR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 132
Cdd:cd21331     96 HPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3002-3030 3.72e-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: 3.72e-07
                           10        20
                   ....*....|....*....|....*....
gi 2217372302 3002 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 3030
Cdd:pfam00681   11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
2785-2822 5.82e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 48.25  E-value: 5.82e-07
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2217372302  2785 QKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTA 2822
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
16-138 8.23e-07

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: 51.21  E-value: 8.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   16 EEVREKYKDErdrvQKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMR 82
Cdd:cd21325     15 EGTQHSYSEE----EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTP 90
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217372302   83 FHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 138
Cdd:cd21325     91 FIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
16-137 1.01e-06

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


Pssm-ID: 409172  Cd Length: 145  Bit Score: 50.81  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   16 EEVREKYKDErdrvQKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMR 82
Cdd:cd21323     15 EGTQHSYSEE----EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTP 90
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217372302   83 FHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 137
Cdd:cd21323     91 FTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
PLEC smart00250
Plectin repeat;
1662-1698 1.09e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 47.48  E-value: 1.09e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  1662 IRLLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEM 1698
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
140-247 2.24e-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: 2.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  140 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 218
Cdd:cd21312      7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPgLCPDWDSWDASKPVTNAREAMQQADDWLGI 83
                           90       100
                   ....*....|....*....|....*....
gi 2217372302  219 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 247
Cdd:cd21312     84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2253-2285 2.28e-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: 2.28e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2217372302 2253 ATGFLVDPVRNQRLYVHEAVKAGVVGPELHEQL 2285
Cdd:pfam00681    7 ATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
21-126 2.29e-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: 49.19  E-value: 2.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   21 KYKDERDRVQKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYL 96
Cdd:cd21285      2 KSWEAENGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFL 81
                           90       100       110
                   ....*....|....*....|....*....|
gi 2217372302   97 RHRQVKLVNIRNDDIADGNPKLTLGLIWTI 126
Cdd:cd21285     82 AAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
PLEC smart00250
Plectin repeat;
1953-1989 2.30e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.71  E-value: 2.30e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  1953 KLLSAEKAVTGYRDPYTGQSVSLFQALKKGLIPREQG 1989
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2321-2357 2.64e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 46.32  E-value: 2.64e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  2321 IRLLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEM 2357
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1052-1268 3.12e-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: 3.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1052 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLkklraqaEAQQPT 1131
Cdd:COG4913    614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-------DASSDD 686
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1132 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLlerwqavlaqtdvrQRELEQLGRQLRYYRESADPLGAWLQD 1211
Cdd:COG4913    687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLELRALLE 752
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217372302 1212 ARRRQEQIQAMPladsQAVREQLRQEQ-ALLEEIERHGEKVEEC-QRFAKQYINAIKDY 1268
Cdd:COG4913    753 ERFAAALGDAVE----RELRENLEERIdALRARLNRAEEELERAmRAFNREWPAETADL 807
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1091-1253 3.23e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 3.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1091 LRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRH---GERDVEVERWRERV 1167
Cdd:COG4717     73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEaleAELAELPERLEELE 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1168 AQlLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPlgAWLQDARRRQEQIqampladsQAVREQLRQEQALLEEIERH 1247
Cdd:COG4717    153 ER-LEELRELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEEL--------EELQQRLAELEEELEEAQEE 221

                   ....*.
gi 2217372302 1248 GEKVEE 1253
Cdd:COG4717    222 LEELEE 227
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2787-2825 4.62e-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: 4.62e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 2787 FLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTAFEL 2825
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
949-1592 8.55e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 8.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  949 HHYQQLLQSLeqgAQEESRCQRCISELKDIRLQLEACETRTVHRLrlpLDKEPARECAQRIAEQQKAQAEVegLGKGVAR 1028
Cdd:TIGR02168  284 EELQKELYAL---ANEISRLEQQKQILRERLANLERQLEELEAQL---EELESKLDELAEELAELEEKLEE--LKEELES 355
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1029 LSAEAEKVLALpepSPAAPTLRSELEltlgklEQVRSLSAIYLEKLKTISLvIRGTQgaeEVLRAHEEQLKEAQAVPATl 1108
Cdd:TIGR02168  356 LEAELEELEAE---LEELESRLEELE------EQLETLRSKVAQLELQIAS-LNNEI---ERLEARLERLEDRRERLQQ- 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1109 pelEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERwqavLAQTDVRQREL 1188
Cdd:TIGR02168  422 ---EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE----LAQLQARLDSL 494
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1189 EQLGRQLRYYRESAdplgAWLQDARRRQEQIQAmPLADSQAVREQLrqEQALLEEIERHGEKVE-ECQRFAKQYINAIKD 1267
Cdd:TIGR02168  495 ERLQENLEGFSEGV----KALLKNQSGLSGILG-VLSELISVDEGY--EAAIEAALGGRLQAVVvENLNAAKKAIAFLKQ 567
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1268 YELQLVTYKA--QLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSE----LTTLTSQYikFISETL-------RRMEEEE 1334
Cdd:TIGR02168  568 NELGRVTFLPldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkaLSYLLGGV--LVVDDLdnalelaKKLRPGY 645
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1335 MQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEA 1414
Cdd:TIGR02168  646 RIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEEL-EEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1415 RRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQR---LREQLQLLEEQHRAALAHSEEVTASQVAATKTLPNGRDA 1491
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1492 LDGPAAEAEpEHSFDGLRRKVSAQRLQEAGILSAEELQRLAQghTTVDELARREDVRHYLQGRSSIAGLLLKATNEKLSV 1571
Cdd:TIGR02168  805 LDELRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEE--QIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
                          650       660
                   ....*....|....*....|.
gi 2217372302 1572 YAALQRQLLSPGTALILLEAQ 1592
Cdd:TIGR02168  882 RASLEEALALLRSELEELSEE 902
PLEC smart00250
Plectin repeat;
2995-3023 1.27e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.27e-05
                            10        20
                    ....*....|....*....|....*....
gi 2217372302  2995 VRKRRVVIVDPETGKEMSVYEAYRKGLID 3023
Cdd:smart00250    6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
PLEC smart00250
Plectin repeat;
1625-1661 1.27e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.40  E-value: 1.27e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  1625 KLLSAERAVTGYKDPYTGQQISLFQAMQKGLIVREHG 1661
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
422-1253 1.65e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  422 GEVERDLDKADSMIRLLFNDVQTLKDGRhpqgEQMYRrvYR-LHERLvaIRTEYNLRLKAgVAAPATQVAQVTLQSVQRR 500
Cdd:TIGR02169  180 EEVEENIERLDLIIDEKRQQLERLRRER----EKAER--YQaLLKEK--REYEGYELLKE-KEALERQKEAIERQLASLE 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  501 PELEDSTLRyLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGshrgLHQSIEEFRAKIERARS------DEGQLSPATRG 574
Cdd:TIGR02169  251 EELEKLTEE-ISELEKRLEEIEQLLEELNKKIKDLGEEEQLR----VKEKIGELEAEIASLERsiaekeRELEDAEERLA 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  575 AYRDCLGRLDLQYAKLLNSSKARLRSLESLHSFVAAATKELMWL-NEKEEEEVGFDwsdrntnmtAKKESYSALMRELEL 653
Cdd:TIGR02169  326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLrAELEEVDKEFA---------ETRDELKDYREKLEK 396
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  654 KEKKIKELQNAGDRLLREDHPARPTVESFQAALQTQWSWMLQLccciEAHLKENAAyfqffsDVREAEGQLQKLQE---A 730
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL----EEEKEDKAL------EIKKQEWKLEQLAAdlsK 466
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  731 LRRKYScDRSATVTRLEDLLQDAQDEKEQLN---------------------------------------EYKGHL-SGL 770
Cdd:TIGR02169  467 YEQELY-DLKEEYDRVEKELSKLQRELAEAEaqaraseervrggraveevlkasiqgvhgtvaqlgsvgeRYATAIeVAA 545
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  771 AKRAKAVV-----------QLKPRHPAhpmrGRLPLLAVCDYKQVEVTVHKGDECQLVGPA----------QPSHWKVLS 829
Cdd:TIGR02169  546 GNRLNNVVveddavakeaiELLKRRKA----GRATFLPLNKMRDERRDLSILSEDGVIGFAvdlvefdpkyEPAFKYVFG 621
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  830 SSGseaavpsvcfLVpppnqEAQEAVTRLEAQHQaLVTLWHQLhVDMKSLLAWQSLRRDVQLIRSwslatfRTLKPEEQR 909
Cdd:TIGR02169  622 DTL----------VV-----EDIEAARRLMGKYR-MVTLEGEL-FEKSGAMTGGSRAPRGGILFS------RSEPAELQR 678
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  910 QA--LHSLElhyqaflrdsqdaggfGPEDRLMAEREygscshHYQQLLQSLEqgaQEESRCQRCISELKDIRLQLEACET 987
Cdd:TIGR02169  679 LRerLEGLK----------------RELSSLQSELR------RIENRLDELS---QELSDASRKIGEIEKEIEQLEQEEE 733
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  988 RTVHRLRLPLDK--EPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPSP---------AAPTLRSELELT 1056
Cdd:TIGR02169  734 KLKERLEELEEDlsSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelsKLEEEVSRIEAR 813
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1057 LGKLEQV---RSLSAIYLEKLKtislvirgtQGAEEVLRAHEEQLKE-AQAVPATLPELEATKASLKKLRAQAEAQQPTF 1132
Cdd:TIGR02169  814 LREIEQKlnrLTLEKEYLEKEI---------QELQEQRIDLKEQIKSiEKEIENLNGKKEELEEELEELEAALRDLESRL 884
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1133 DALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDvrqrELEQLGRQLRYYRESADPLGAWLQDA 1212
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLEDVQAEL 960
                          890       900       910       920
                   ....*....|....*....|....*....|....*....|.
gi 2217372302 1213 RRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHgEKVEE 1253
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 ...
30-137 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 2217372302   30 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 96
Cdd:cd21324     25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2217372302   97 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 137
Cdd:cd21324    105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
25-133 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 2217372302   25 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQIALDY 95
Cdd:cd21329      2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2217372302   96 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 133
Cdd:cd21329     78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
PLEC smart00250
Plectin repeat;
2656-2692 2.26e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.62  E-value: 2.26e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  2656 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDT 2692
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
849-1481 2.33e-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: 2.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  849 QEAQEAVTRLEAQHQALVTLWHQLHVdmksllAWQSLRRDVQLIrswslatfrtlkpeEQRQALHSLELHYQ-AFLRDSQ 927
Cdd:TIGR02168  354 ESLEAELEELEAELEELESRLEELEE------QLETLRSKVAQL--------------ELQIASLNNEIERLeARLERLE 413
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  928 DAggfgpEDRLMAEREygscshhyqQLLQSLEQGAQEEsrCQRCISELKDIRLQLEACETRTVHRL------------RL 995
Cdd:TIGR02168  414 DR-----RERLQQEIE---------ELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALeelreeleeaeqAL 477
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  996 PLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEK----VLALPEPSPAAPTLRSELELTLGKLEQ---VRSLSA 1068
Cdd:TIGR02168  478 DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgiLGVLSELISVDEGYEAAIEAALGGRLQavvVENLNA 557
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1069 I-----YLEK--LKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLKKlraqaeAQQPTFDALR--DEL 1139
Cdd:TIGR02168  558 AkkaiaFLKQneLGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRK------ALSYLLGGVLvvDDL 631
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1140 RGAQEVGERLqqRHGERDV----EVERWRERVAQLLERWQAVLAQtdvRQRELEQLGRQLRYYRESADPLGAWLQDARRR 1215
Cdd:TIGR02168  632 DNALELAKKL--RPGYRIVtldgDLVRPGGVITGGSAKTNSSILE---RRREIEELEEKIEELEEKIAELEKALAELRKE 706
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1216 QEQIQAMpLADSQAVREQLRQEQALL-EEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEP-----VASPAKKP 1289
Cdd:TIGR02168  707 LEELEEE-LEQLRKELEELSRQISALrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeelAEAEAEIE 785
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1290 KVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQEtqaLQQSFLSEKDSLLQRERFIE 1369
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED---LEEQIEELSEDIESLAAEIE 862
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1370 QEKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEE 1449
Cdd:TIGR02168  863 ELEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
                          650       660       670
                   ....*....|....*....|....*....|..
gi 2217372302 1450 NQRLREQLQLLEEqhrAALAHSEEVTASQVAA 1481
Cdd:TIGR02168  942 QERLSEEYSLTLE---EAEALENKIEDDEEEA 970
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1550-1588 2.52e-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: 2.52e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 1550 YLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTALIL 1588
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
mukB PRK04863
chromosome partition protein MukB;
1087-1256 2.74e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.34  E-value: 2.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1087 AEEVLRAHEEQLKEAQAVP---ATLPELEatkaslKKLRAQAEAQQptfdaLRDELRGAQEVG-------ERLQQRHGER 1156
Cdd:PRK04863   498 ARELLRRLREQRHLAEQLQqlrMRLSELE------QRLRQQQRAER-----LLAEFCKRLGKNlddedelEQLQEELEAR 566
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1157 dveVERWRERVAQLLERwqavlaQTDVRQrELEQLGRQLRYYRESADplgAWL--QDARRRQEQIQAMPLADSQAVRE-- 1232
Cdd:PRK04863   567 ---LESLSESVSEARER------RMALRQ-QLEQLQARIQRLAARAP---AWLaaQDALARLREQSGEEFEDSQDVTEym 633
                          170       180
                   ....*....|....*....|....*.
gi 2217372302 1233 --QLRQEQALLEEIERHGEKVEECQR 1256
Cdd:PRK04863   634 qqLLERERELTVERDELAARKQALDE 659
PLEC smart00250
Plectin repeat;
2209-2243 3.18e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.18e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2217372302  2209 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 2243
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
3244-3281 3.55e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.55e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2217372302  3244 QRFLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTA 3281
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2825-2859 3.80e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 3.80e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2217372302  2825 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 2859
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 ...
29-130 4.78e-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: 4.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   29 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLRHRQVKLV 104
Cdd:cd21306     16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
                           90       100
                   ....*....|....*....|....*.
gi 2217372302  105 NIRNDDIADGNPKLTLGLIWTIILHF 130
Cdd:cd21306     96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
PLEC smart00250
Plectin repeat;
3134-3167 5.36e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 5.36e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2217372302  3134 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 3167
Cdd:smart00250    5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
22-127 7.20e-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: 7.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   22 YKDErdrvQKKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQN 88
Cdd:cd21292     21 YSEE----EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHEN 96
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2217372302   89 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 127
Cdd:cd21292     97 LTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
PTZ00121 PTZ00121
MAEBL; Provisional
999-1428 7.26e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 7.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  999 KEPARECAQRIAEQQKAQAEveglGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTlGKLEQVR---SLSAIYLEKLK 1075
Cdd:PTZ00121  1397 KKKAEEDKKKADELKKAAAA----KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK-KKAEEAKkaeEAKKKAEEAKK 1471
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1076 TISLVIRGTQG--AEEVLRAHEEQLKEA----QAVPATLPELEATKASLKKLRAQAEAQQPTFDAlrDELRGAQEVGERL 1149
Cdd:PTZ00121  1472 ADEAKKKAEEAkkADEAKKKAEEAKKKAdeakKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA--DEAKKAEEKKKAD 1549
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1150 QQRHGE--RDVEVERWRERVAQLLERWQAVLAQTDV-RQRELEQLGRQLRYYRESADPLGAWLQDARrrQEQIQAmplad 1226
Cdd:PTZ00121  1550 ELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEaKKAEEARIEEVMKLYEEEKKMKAEEAKKAE--EAKIKA----- 1622
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1227 sqavrEQLRQEQALLEEIERHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAKKPkvqsgSESVIQEYVDLR 1306
Cdd:PTZ00121  1623 -----EELKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKK-----AEEAKKAEEDEK 1688
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1307 THYSELTTLTSQYIKfiSETLRRMEEEEMQTVQQeqllqetqaLQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKA 1386
Cdd:PTZ00121  1689 KAAEALKKEAEEAKK--AEELKKKEAEEKKKAEE---------LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2217372302 1387 QQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRK 1428
Cdd:PTZ00121  1758 KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
SPEC smart00150
Spectrin repeats;
1096-1189 7.43e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 44.24  E-value: 7.43e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  1096 EQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALrdelrgaQEVGERLQQRHGERDVEVErwrERVAQLLERWQ 1175
Cdd:smart00150   18 EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEAL-------NELGEQLIEEGHPDAEEIE---ERLEELNERWE 87
                            90
                    ....*....|....
gi 2217372302  1176 AVLAQTDVRQRELE 1189
Cdd:smart00150   88 ELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
2544-2579 8.93e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.08  E-value: 8.93e-05
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 2217372302  2544 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVA 2579
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
2284-2315 9.11e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.08  E-value: 9.11e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2217372302  2284 QLLSAEKAVTGYRDPYSGSTISLFQAMQKGLV 2315
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1118-1598 9.13e-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: 9.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1118 LKKLRAQAEAqqptfdALRdelrgAQEVGERLQQRhgerdvEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRy 1197
Cdd:COG1196    202 LEPLERQAEK------AER-----YRELKEELKEL------EAELLLLKLRELEAELEELEAELEELEAELEELEAELA- 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1198 yresadplgawLQDARRRQEQIQAmpLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKA 1277
Cdd:COG1196    264 -----------ELEAELEELRLEL--EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1278 QLEpvaspakkpKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALQQSFLSE 1357
Cdd:COG1196    331 ELE---------ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1358 KDSLLQRERFIEQEKAKLEQLfqdevakaqqlreeqqrqqqqmeqerqrlvASMEEARRRQHEAEEGVRRKQEELQQLEQ 1437
Cdd:COG1196    402 LEELEEAEEALLERLERLEEE------------------------------LEELEEALAELEEEEEEEEEALEEAAEEE 451
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1438 QRRQQEELLAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRL 1517
Cdd:COG1196    452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG 531
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1518 QEAGILSAEELQRLAQG-HTTVDELARREDVRHYLQGR--SSIAGLLLKATNEKLSVYAALQRQLLSPGTALILLEAQAA 1594
Cdd:COG1196    532 VEAAYEAALEAALAAALqNIVVEDDEVAAAAIEYLKAAkaGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611

                   ....
gi 2217372302 1595 SGFL 1598
Cdd:COG1196    612 DARY 615
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1009-1190 1.00e-04

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 46.28  E-value: 1.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1009 IAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAE 1088
Cdd:cd00176     39 LKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1089 EVLRAHEEQLKEAQAvpatlPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERwrERVA 1168
Cdd:cd00176    117 DLEQWLEEKEAALAS-----EDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIE--EKLE 189
                          170       180
                   ....*....|....*....|..
gi 2217372302 1169 QLLERWQAVLAQTDVRQRELEQ 1190
Cdd:cd00176    190 ELNERWEELLELAEERQKKLEE 211
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1087-1253 1.00e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 1.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1087 AEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRaqaeaqqptfDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1166
Cdd:PRK02224   239 ADEVLEEHEERREELETLEAEIEDLRETIAETERER----------EELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1167 VAQLLERWQAVLAQTDVRQRELEQ-------LGRQLRYYRESADPLGAWLQDARRRQEQIQamplADSQAVREQLRQEQA 1239
Cdd:PRK02224   309 AEAVEARREELEDRDEELRDRLEEcrvaaqaHNEEAESLREDADDLEERAEELREEAAELE----SELEEAREAVEDRRE 384
                          170
                   ....*....|....
gi 2217372302 1240 LLEEIERHGEKVEE 1253
Cdd:PRK02224   385 EIEELEEEIEELRE 398
PTZ00121 PTZ00121
MAEBL; Provisional
956-1465 1.06e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  956 QSLEQGAQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEK 1035
Cdd:PTZ00121  1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK 1384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1036 VLAlpEPSPAAPTLRSELELTLGKLEQVRSLSAiylEKLKTISLvirgTQGAEEVLRAhEEQLKEAQavpatlpelEATK 1115
Cdd:PTZ00121  1385 KKA--EEKKKADEAKKKAEEDKKKADELKKAAA---AKKKADEA----KKKAEEKKKA-DEAKKKAE---------EAKK 1445
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1116 ASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHG--ERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGR 1193
Cdd:PTZ00121  1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD 1525
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1194 QLRYYRESADPlgawlQDARRRQEQIQAMPLADSQAVR---EQLRQEQALLEEIERHGE--KVEECQRFAKQYINAIKDY 1268
Cdd:PTZ00121  1526 EAKKAEEAKKA-----DEAKKAEEKKKADELKKAEELKkaeEKKKAEEAKKAEEDKNMAlrKAEEAKKAEEARIEEVMKL 1600
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1269 ELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQ 1348
Cdd:PTZ00121  1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1349 ALQQSFLSEKDSLLQRErfiEQEKAKLEQL---FQDEVAKAQqlreEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGV 1425
Cdd:PTZ00121  1681 KKAEEDEKKAAEALKKE---AEEAKKAEELkkkEAEEKKKAE----ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 2217372302 1426 RRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHR 1465
Cdd:PTZ00121  1754 EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
SPEC smart00150
Spectrin repeats;
508-602 1.32e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.47  E-value: 1.32e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   508 LRYLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARSDEGQL---SPATRGAYRDCLGRLD 584
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
                            90
                    ....*....|....*...
gi 2217372302   585 LQYAKLLNSSKARLRSLE 602
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
1588-1621 1.42e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.42e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2217372302  1588 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPE 1621
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2209-2243 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 2217372302 2209 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 2243
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPET 35
PLEC smart00250
Plectin repeat;
2619-2655 1.85e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 1.85e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  2619 RLLSAERAVTGYRDPYTEQTISLFQAMKKELIPTEEA 2655
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
167-244 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 2217372302  167 DNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 244
Cdd:cd21185     20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
PLEC smart00250
Plectin repeat;
1916-1950 2.18e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.93  E-value: 2.18e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2217372302  1916 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEF 1950
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
1990-2026 2.20e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.93  E-value: 2.20e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2217372302  1990 LRLLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEET 2026
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
974-1215 2.77e-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: 2.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  974 ELKDIRLQLEAcETRTVHRLrlpldkEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpepSPAAPTLRSEL 1053
Cdd:COG4913    236 DLERAHEALED-AREQIELL------EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL----EAELEELRAEL 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1054 ELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEvlraheEQLKEaqavpatlpELEATKASLKKLRAQAEAQQPTFD 1133
Cdd:COG4913    305 ARLEAELERLEARLDALREELDELEAQIRGNGGDRL------EQLER---------EIERLERELEERERRRARLEALLA 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1134 ALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQllERWQAVLAQTDVRqRELEQLGRQLRYYRESADPLGAWLQDAR 1213
Cdd:COG4913    370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEE--ALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLALR 446

                   ..
gi 2217372302 1214 RR 1215
Cdd:COG4913    447 DA 448
Rabaptin pfam03528
Rabaptin;
1088-1385 2.91e-04

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 46.64  E-value: 2.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1088 EEVLRAHEEQLKEAQAVpatlpeLEATKASLKKLRAQ-AEAQqptfdALRDELRGAQEVGERLQQrhgERDVEVER-WRE 1165
Cdd:pfam03528   39 KELYLAKEEDLKRQNAV------LQEAQVELDALQNQlALAR-----AEMENIKAVATVSENTKQ---EAIDEVKSqWQE 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1166 RVAQLlerwQAVLAQTdVRQRE------LEQLGRQLRYYRESADPLGAwlqDARRRqeqiqampLADSQavreqlrQEQA 1239
Cdd:pfam03528  105 EVASL----QAIMKET-VREYEvqfhrrLEQERAQWNQYRESAEREIA---DLRRR--------LSEGQ-------EEEN 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1240 LLEEIERHGEKVEECQRFA---KQYINAIKDYELQLVTYKAQLEpvASPAKK----PKVQSGSESVIQEYVD-LRTHYSE 1311
Cdd:pfam03528  162 LEDEMKKAQEDAEKLRSVVmpmEKEIAALKAKLTEAEDKIKELE--ASKMKElnhyLEAEKSCRTDLEMYVAvLNTQKSV 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1312 LTTLTSQYIKFISETLRRMEEEEMQtvqqeqllqeTQALQQSFLSEKDSLLQRERFIEQEKAKL------EQLFQDEVAK 1385
Cdd:pfam03528  240 LQEDAEKLRKELHEVCHLLEQERQQ----------HNQLKHTWQKANDQFLESQRLLMRDMQRMesvltsEQLRQVEEIK 309
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1105-1336 2.93e-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: 2.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1105 PATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQevgERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVR 1184
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL---SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1185 QRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPL--------ADSQAVREQLRQEQALLEEIERHGEKVEECQR 1256
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripeiqAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1257 FAKQYINAIKDY----ELQLVTYKAQLEpvASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEE 1332
Cdd:TIGR02169  830 YLEKEIQELQEQridlKEQIKSIEKEIE--NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907

                   ....
gi 2217372302 1333 EEMQ 1336
Cdd:TIGR02169  908 LEAQ 911
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2544-2582 4.66e-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: 4.66e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217372302 2544 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVARLL 2582
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1050-1248 4.95e-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: 4.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1050 RSELELTLGKLEQVRSLsaiyLEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAvpaTLPELEATKASLKKLRAQAEAQQ 1129
Cdd:COG4913    633 LEALEAELDALQERREA----LQRLAEYSWDEIDVASAEREIAELEAELERLDA---SSDDLAALEEQLEELEAELEELE 705
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1130 PTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERV-----AQLLERWQAvLAQTDVRQRELEQLGRQLRYYRESADP 1204
Cdd:COG4913    706 EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelrALLEERFAA-ALGDAVERELRENLEERIDALRARLNR 784
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2217372302 1205 LGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHG 1248
Cdd:COG4913    785 AEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG 828
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1093-1288 6.79e-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: 6.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1093 AHEEQLKEAQAvpatlpELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLE 1172
Cdd:COG4942     17 AQADAAAEAEA------ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1173 RWQAVLAQTDVRQRELEQLGRQLrYYRESADPLGAWL-----QDARRRQEQIQAMpladSQAVREQLRQEQALLEEIERH 1247
Cdd:COG4942     91 EIAELRAELEAQKEELAELLRAL-YRLGRQPPLALLLspedfLDAVRRLQYLKYL----APARREQAEELRADLAELAAL 165
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2217372302 1248 GEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKK 1288
Cdd:COG4942    166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
950-1383 9.03e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 9.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  950 HYQQLLQSLEQGAQEESRCQRCISELKDIRLQLEACE-----TRTVHRLRLPLDKEPAR--ECAQRIAEQQKAQAEVEGL 1022
Cdd:COG4717     89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAELPERleELEERLEELRELEEELEEL 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1023 GKGVARLSAEAEKVLALPEPSpaaptLRSELELTLGKLEQVRSLSAIYLEKLKTislvirgtqgAEEVLRAHEEQLKEAQ 1102
Cdd:COG4717    169 EAELAELQEELEELLEQLSLA-----TEEELQDLAEELEELQQRLAELEEELEE----------AQEELEELEEELEQLE 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1103 AVPATLPELEATKASLKKLRAQA-----EAQQPTFDALRDELRGAQEVGERLQQRHGERDVeveRWRERVAQLLERWQAV 1177
Cdd:COG4717    234 NELEAAALEERLKEARLLLLIAAallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQAL 310
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1178 LAQTDVRQRELEQLGRQLRYYRE-SADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQE-QALLEEIerHGEKVEECQ 1255
Cdd:COG4717    311 PALEELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiAALLAEA--GVEDEEELR 388
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1256 RFAKQYiNAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETlrrmeEEEM 1335
Cdd:COG4717    389 AALEQA-EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAEL-----EAEL 462
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217372302 1336 QTVQQEQLLQETQALQQSFLSEKDSLLQR-------ERFIEQEKAKLEQLFQDEV 1383
Cdd:COG4717    463 EQLEEDGELAELLQELEELKAELRELAEEwaalklaLELLEEAREEYREERLPPV 517
COG4995 COG4995
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
1126-1587 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 2217372302 1126 EAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPL 1205
Cdd:COG4995      1 LLALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1206 GAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASP 1285
Cdd:COG4995     81 ALAALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1286 AKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRE 1365
Cdd:COG4995    161 AAAALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLAL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1366 RFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEEL 1445
Cdd:COG4995    241 LALAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1446 LAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRLQEAGILSA 1525
Cdd:COG4995    321 AALLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAAL 400
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217372302 1526 EELQRLAQGHTTVDELARREDVRHYLQGRSSIAGLL-LKATNEKLSVYAALQRQLLSPGTALI 1587
Cdd:COG4995    401 LALAAAQLLRLLLAALALLLALAAYAAARLALLALIeYIILPDRLYAFVQLYQLLIAPIEAEL 463
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
16-244 1.09e-03

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 44.93  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   16 EEVRE-KYKDERDRVQKKTFTKWVNKHLIKAQrhISDLYEDLRDGHNLISLLEVLSGD---SLPREKGR-------MRFH 84
Cdd:COG5069    365 EEKPEiEEFDAEGEFEARVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFK 442
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   85 KLQNVQIALDYLRHRQVKLVNIRNDDIADGNpKLTLGLIW-------TIILHFQISDiqvsgqsEDMTAKEKLLLWSQRM 157
Cdd:COG5069    443 AFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKD-------GCGLSDSDLCAWLGSL 514
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  158 VEGY---QGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVyRQTNLENLDQA-------FSVAERDLGVTRLLDPEDV 227
Cdd:COG5069    515 GLKGdkeEGIRSFGDPAGSVSGVFYLDVLKGIHSELVDYDLV-TRGFTEFDDIAdarslaiSSKILRSLGAIIKFLPEDI 593
                          250
                   ....*....|....*..
gi 2217372302  228 DVPQPdEKSIITYVSSL 244
Cdd:COG5069    594 NGVRP-RLDVLTFIESL 609
PLEC smart00250
Plectin repeat;
1548-1585 1.11e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.00  E-value: 1.11e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2217372302  1548 RHYLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTA 1585
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
24-127 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 2217372302   24 DERDRVQkktFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEvlsgDSLP-------------REKGRM 81
Cdd:cd21294      4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLIN----DSVPdtidervlnkpprKNKPLN 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2217372302   82 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 127
Cdd:cd21294     77 NFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
COG5283 COG5283
Phage-related tail protein [Mobilome: prophages, transposons];
1090-1222 1.15e-03

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


Pssm-ID: 444094 [Multi-domain]  Cd Length: 747  Bit Score: 44.85  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1090 VLRAHEEQLKEAqavpatlpeLEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQ 1169
Cdd:COG5283      4 ILGAVDKPFKSA---------LESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQ 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217372302 1170 LLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAM 1222
Cdd:COG5283     75 AGIDTRQLSAAQRRLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQRL 127
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
36-126 1.38e-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: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   36 KWVNKHLIKAQR---HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRhrQVKLVN-IRN 108
Cdd:cd21218     17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
                           90
                   ....*....|....*...
gi 2217372302  109 DDIADGNPKLTLGLIWTI 126
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 ...
25-133 1.51e-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: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   25 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL---------SGDSLPREKGRMRfhKLQNVQIALDY 95
Cdd:cd21330      9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2217372302   96 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 133
Cdd:cd21330     85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
604-697 1.87e-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: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  604 LHSFVAAATKELMWLNEKEE----EEVGFDWsdrnTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTV 679
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEAllssEDYGKDL----ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90
                   ....*....|....*...
gi 2217372302  680 ESFQAALQTQWSWMLQLC 697
Cdd:pfam00435   79 QERLEELNERWEQLLELA 96
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
827-1384 2.18e-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: 2.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  827 VLSSSGSEAAVPSVCFLVPPPNQEAQEAVTRLEAQHQALVTLWHQLHVDMKSLlawqslrRDVQLIRSWSLATFRTLKPE 906
Cdd:pfam05483  246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKEL-------EDIKMSLQRSMSTQKALEED 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  907 EQ--RQALHSLELHYQAFLRDSQDAGGfgPEDRLMAEREYGSCShhYQQLLQSleqgaqEESRCQRCISELKDIRLQLEA 984
Cdd:pfam05483  319 LQiaTKTICQLTEEKEAQMEELNKAKA--AHSFVVTEFEATTCS--LEELLRT------EQQRLEKNEDQLKIITMELQK 388
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  985 CETRTVHRLRLPLDKEPARECAQRI-AEQQKAQAEVEGLGKGVARLSAEAEKVLALPEpSPAAPTLRSELELTLGK---- 1059
Cdd:pfam05483  389 KSSELEEMTKFKNNKEVELEELKKIlAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQ-AREKEIHDLEIQLTAIKtsee 467
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1060 --LEQVRSL-SAIYLEKLKTISLvirgTQGAEEVLRAHEEQLKEAQAVPATLP----ELEATKASLKKLRAQAEAQQPTF 1132
Cdd:pfam05483  468 hyLKEVEDLkTELEKEKLKNIEL----TAHCDKLLLENKELTQEASDMTLELKkhqeDIINCKKQEERMLKQIENLEEKE 543
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1133 DALRDELrgaQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLryyresadplgawlQDA 1212
Cdd:pfam05483  544 MNLRDEL---ESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI--------------ENK 606
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1213 RRRQEQIQAmplaDSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKD-YELQLVTYKAQLEPVASPAKKPKV 1291
Cdd:pfam05483  607 NKNIEELHQ----ENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDnYQKEIEDKKISEEKLLEEVEKAKA 682
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1292 QSGSESVIQEYVDLRTHYSelttltsqyikfISETLRRMEEEEMQtvqqeqllqetqalQQSFLSEKDSLLQRERFIEQE 1371
Cdd:pfam05483  683 IADEAVKLQKEIDKRCQHK------------IAEMVALMEKHKHQ--------------YDKIIEERDSELGLYKNKEQE 736
                          570
                   ....*....|...
gi 2217372302 1372 KAKLEQLFQDEVA 1384
Cdd:pfam05483  737 QSSAKAALEIELS 749
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1111-1428 2.20e-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: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1111 LEATKASLKKLRAQAE-AQQptFDALRDELRGAQE--VGERLQQRHGERDvEVERWRERVAQLLERWQAVLAQTDVrqrE 1187
Cdd:TIGR02168  195 LNELERQLKSLERQAEkAER--YKELKAELRELELalLVLRLEELREELE-ELQEELKEAEEELEELTAELQELEE---K 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1188 LEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKD 1267
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1268 YELQLVTYKAQLEpvASPAKKPKVQSGSESVIQEYVDLRTHYSELTtltsQYIKFISETLRRMEEE-EMQTVQQEQLLQE 1346
Cdd:TIGR02168  349 LKEELESLEAELE--ELEAELEELESRLEELEEQLETLRSKVAQLE----LQIASLNNEIERLEARlERLEDRRERLQQE 422
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1347 TQALQQSFLSEKDSLLQRErfIEQEKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVR 1426
Cdd:TIGR02168  423 IEELLKKLEEAELKELQAE--LEELEEELEEL-QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499

                   ..
gi 2217372302 1427 RK 1428
Cdd:TIGR02168  500 NL 501
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
940-1252 2.63e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  940 AEREYGSCSHHYQQLLQSLEQGAQEESRCQRCISELKDIRLQLEACETRTvhrlrLPLDKEPARECAQRIAEQQKAQAEV 1019
Cdd:COG4717    137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL-----SLATEEELQDLAEELEELQQRLAEL 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1020 EglgKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISL-VIRGTQGAEEVLRAHEEQL 1098
Cdd:COG4717    212 E---EELEEAQEELEE-------------LEEELEQLENELEAAALEERLKEARLLLLIAaALLALLGLGGSLLSLILTI 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1099 KEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRgAQEVGERLQQRHGERDVEVERWRErVAQLLERWQAVL 1178
Cdd:COG4717    276 AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE-EEELEELLAALGLPPDLSPEELLE-LLDRIEELQELL 353
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1179 AQTDVRQRELEQLGRQLRYYR-------ESADPLGAWLQDARRRQEQIQAMpladsQAVREQLRQEQALLEEIERHGEKV 1251
Cdd:COG4717    354 REAEELEEELQLEELEQEIAAllaeagvEDEEELRAALEQAEEYQELKEEL-----EELEEQLEELLGELEELLEALDEE 428

                   .
gi 2217372302 1252 E 1252
Cdd:COG4717    429 E 429
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
31-89 3.60e-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: 3.60e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217372302   31 KKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREK----GRMRFHKLQNV 89
Cdd:cd21221      3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVV 65
PLEC smart00250
Plectin repeat;
2862-2893 4.09e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.46  E-value: 4.09e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2217372302  2862 KLLSAERAVTGYKDPYSGKLISLFQAMKKGLI 2893
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1049-1243 4.28e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 4.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1049 LRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEvLRAHEEQLKEAQAvpatlpELEATKASLKKLRAQAE-- 1126
Cdd:COG3206    180 LEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQ-LSELESQLAEARA------ELAEAEARLAALRAQLGsg 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1127 -------AQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVA----QLLERWQAVLAQTDVR----QRELEQL 1191
Cdd:COG3206    253 pdalpelLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAalraQLQQEAQRILASLEAElealQAREASL 332
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2217372302 1192 GRQLRYYRESADPLGAWLQDARRRQEQIQAmpladSQAVREQL--RQEQALLEE 1243
Cdd:COG3206    333 QAQLAQLEARLAELPELEAELRRLEREVEV-----ARELYESLlqRLEEARLAE 381
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3140-3170 4.48e-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: 4.48e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2217372302 3140 AGILDTETLEKVSITEAMHRNLVDNITGQRL 3170
Cdd:pfam00681    9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1105-1420 5.47e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 5.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1105 PATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVR 1184
Cdd:COG4372     20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1185 QRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQR-------- 1256
Cdd:COG4372    100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelqalsea 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1257 FAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEEMQ 1336
Cdd:COG4372    180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1337 TVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARR 1416
Cdd:COG4372    260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339

                   ....
gi 2217372302 1417 RQHE 1420
Cdd:COG4372    340 ADLL 343
CH_PARVA_rpt2 cd21337
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ...
29-131 5.67e-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: 5.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   29 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR----FHKLQNVQIALDYLRHRQVKLV 104
Cdd:cd21337     20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEKP 99
                           90       100
                   ....*....|....*....|....*..
gi 2217372302  105 NIRNDDIADGNPKLTLGLIWTIILHFQ 131
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 ...
1109-1280 5.90e-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: 5.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1109 PELEATKASLKKLRAQAEAQQPTFDALRDelrgaqevgeRLQQRHGERDVEverwRERVAQLLERWQAVLAQTDVRQREL 1188
Cdd:pfam00529   54 TDYQAALDSAEAQLAKAQAQVARLQAELD----------RLQALESELAIS----RQDYDGATAQLRAAQAAVKAAQAQL 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1189 EQLGRQLRYYRESAdPLGAW----LQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEierhgekveecqrFAKQYINA 1264
Cdd:pfam00529  120 AQAQIDLARRRVLA-PIGGIsresLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAE-------------NQAEVRSE 185
                          170
                   ....*....|....*.
gi 2217372302 1265 IKDYELQLVTYKAQLE 1280
Cdd:pfam00529  186 LSGAQLQIAEAEAELK 201
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1091-1190 6.80e-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: 6.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1091 LRAHEEQLKEAQAVpATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGErdvEVERWRERVAQL 1170
Cdd:pfam00435   10 ADDLESWIEEKEAL-LSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHY---ASEEIQERLEEL 85
                           90       100
                   ....*....|....*....|
gi 2217372302 1171 LERWQAVLAQTDVRQRELEQ 1190
Cdd:pfam00435   86 NERWEQLLELAAERKQKLEE 105
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
1076-1280 7.45e-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: 7.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1076 TISLVIRGTQGAEEVLRAHEEQLKEAQAvpatlpELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEvgerlqqrhge 1155
Cdd:COG3883      3 ALALAAPTPAFADPQIQAKQKELSELQA------ELEAAQAELDALQAELEELNEEYNELQAELEALQA----------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1156 rdvEVERWRERVAQllerwqavlAQTDVRQRElEQLGRQLRYYRESADPLGAW--------LQDARRRQEQIQAMPLADS 1227
Cdd:COG3883     66 ---EIDKLQAEIAE---------AEAEIEERR-EELGERARALYRSGGSVSYLdvllgsesFSDFLDRLSALSKIADADA 132
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217372302 1228 QAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLE 1280
Cdd:COG3883    133 DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
30-127 9.01e-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: 9.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302   30 QKKTFTKWVNKHL---------IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDY 95
Cdd:cd21293      2 EKGSYVDHINRYLgddpflkqfLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2217372302   96 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 127
Cdd:cd21293     82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
SPEC smart00150
Spectrin repeats;
1198-1264 9.28e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 38.46  E-value: 9.28e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217372302  1198 YRESADPLGAWLQDArrrQEQIQAMPLA-DSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINA 1264
Cdd:smart00150    3 FLRDADELEAWLEEK---EQLLASEDLGkDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE 67
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
951-1545 9.68e-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: 9.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302  951 YQQLLQSLEQGAQEESRCQRCISELKDIRLQLEACEtrtvhRLRLPLDKEPAREcaqRIAEQQKAQAEVEglgkgvarls 1030
Cdd:TIGR00618  245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLE-----ETQERINRARKAA---PLAAHIKAVTQIE---------- 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1031 AEAEKVLAlpepspaaptlrsELELTLGKLEQVRSLSAIYLEKlktiSLVIRGTQGAEEVLRAHEEQLKEAQAVPAT-LP 1109
Cdd:TIGR00618  307 QQAQRIHT-------------ELQSKMRSRAKLLMKRAAHVKQ----QSSIEEQRRLLQTLHSQEIHIRDAHEVATSiRE 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1110 ELEATKASLKKLRAQAeaQQPTfdALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLerwqAVLAQTDVRQRELE 1189
Cdd:TIGR00618  370 ISCQQHTLTQHIHTLQ--QQKT--TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA----HAKKQQELQQRYAE 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1190 QLgrqlryyresadplgawlQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYE 1269
Cdd:TIGR00618  442 LC------------------AAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP 503
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1270 LQLVTYKAQLEPVA-----SPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQyIKFISETLRRMEE------------ 1332
Cdd:TIGR00618  504 CPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQ-RASLKEQMQEIQQsfsiltqcdnrs 582
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1333 -EEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIE-------QEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQER 1404
Cdd:TIGR00618  583 kEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKlqpeqdlQDVRLHLQQCSQELALKLTALHALQLTLTQERVRE 662
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217372302 1405 QRLVASMEEARRRQHeaeegVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQ-------LLEEQHRAALAHSEEVTAS 1477
Cdd:TIGR00618  663 HALSIRVLPKELLAS-----RQLALQKMQSEKEQLTYWKEMLAQCQTLLRELEThieeydrEFNEIENASSSLGSDLAAR 737
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217372302 1478 QVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRLQEAGILSAEELQRLAQGHTTVDELARRE 1545
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH