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Conserved domains on  [gi|2496167637|ref|XP_055359435|]
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plectin isoform X19 [Betta splendens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
1113-1229 9.19e-74

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


:

Pssm-ID: 409037  Cd Length: 105  Bit Score: 241.54  E-value: 9.19e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1113 DRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPREKGRMRFHKLQNVQIALD 1192
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGE------------SLPRERGRMRFHRLQNVQTALD 68
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2496167637 1193 FLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 1229
Cdd:cd21188     69 FLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
1246-1351 2.87e-65

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).


The actual alignment was detected with superfamily member cd21238:

Pssm-ID: 469584  Cd Length: 106  Bit Score: 217.20  E-value: 2.87e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1246 MSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21238      1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 2496167637 1326 PEDVDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
S10_plectin pfam03501
Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the ...
7-99 4.91e-49

Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the cytoskeletal muscle protein plectin as well as the ribosomal S10 protein. This domain may be involved in RNA binding.


:

Pssm-ID: 427337  Cd Length: 92  Bit Score: 170.39  E-value: 4.91e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637    7 MPLRELRAIYEVLFRDGVMVAKKDkRPQIKHPEVqDVSNLQVIRAMGSLKSRGYVKETFAWRHFYWYLTNEGIVYLRDYL 86
Cdd:pfam03501    1 IPKENRKAIYEYLFKEGVLVAKKD-FNLPKHPEL-NVPNLQVIKAMQSLKSRGYVKEQFAWRHYYWYLTNEGIEYLREYL 78
                           90
                   ....*....|...
gi 2496167637   87 HLPPEIVPASLQR 99
Cdd:pfam03501   79 HLPAEIVPATLKR 91
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
1981-2058 5.99e-43

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: 152.37  E-value: 5.99e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2496167637 1981 LSWQYLMKDFTLIRSWNITMLKTMKPEEYRLILRNLELHYQDFMRDSQDSQLFGPDDRMQIEGDYTKSTQHFDSLLRS 2058
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
1880-1946 2.10e-24

SH3 domain; This entry represents an SH3 domain.


:

Pssm-ID: 407754  Cd Length: 65  Bit Score: 98.87  E-value: 2.10e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2496167637 1880 QLKPRNptTPIKGNLPVQAVCDFKQVEITVHKGDECALLNNSQPSKWKVMNRSGSEAVVPSVCFLVP 1946
Cdd:pfam17902    1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1705-1891 8.32e-17

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 82.49  E-value: 8.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1705 LHAFVSAATKELMWLNDKEEEEVNYDWSDKNTNMTVKKENYSGLMRELELREKKVNDIQAMGDRLVKDGHPGKKTVEAFT 1784
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1785 AALQTQWSWILQLCCCVEAHLKENTAYYQFFTDVKDAQDKMKKMQENMKkkySCDRTTTATRLEDLLQDAVDEKEQLNEF 1864
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180
                   ....*....|....*....|....*..
gi 2496167637 1865 KTQVAGLNKRAKSIIQLKPRNPTTPIK 1891
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIE 185
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3996-4034 8.80e-16

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 73.52  E-value: 8.80e-16
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3996 LLEAQIATGGIIDPEESHRLPVEVAYKRGFFDEEMNEIL 4034
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3350-3388 1.90e-14

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 69.66  E-value: 1.90e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3350 LLEAQAASGFIVDPVKNQCLSVDEAVKSGVVGPELHEKL 3388
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3682-3720 5.95e-14

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 68.51  E-value: 5.95e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3682 LLETQAATGFIIDPIKNETLTVDEAVRKGVVGPEIHDKL 3720
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2692-2729 8.13e-14

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 68.12  E-value: 8.13e-14
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2496167637 2692 LLEAQAATGYMLDPINNHKLSVNEAVKEGLIGPELHNK 2729
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
4270-4308 9.99e-13

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 65.04  E-value: 9.99e-13
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 4270 LLEAQACTGGIIDPTTGERFTVTVATEKGLVDKAMVDRL 4308
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3020-3057 2.14e-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: 2.14e-12
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2496167637 3020 LEAQAGTGYVVDPVHNQHYTVDEAVKAGVVGPELHEKL 3057
Cdd:pfam00681    2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3920-3958 6.53e-11

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 59.65  E-value: 6.53e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3920 LLEAQAATGYIIDPIKSLKLTVNEAVSMGTVGPEFKDKL 3958
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2768-2805 6.86e-11

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 59.65  E-value: 6.86e-11
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2496167637 2768 VLEAQLATGGIIDPLNSHRVPNEIAYKQGQYDAEMNKI 2805
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2263-2573 9.36e-11

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 68.54  E-value: 9.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2263 ERDAELDQHRQHLSSLQDrwkavftQIDLRQRELDQLGRQLgyyresydwlirwiADAKQRQENIQAVPITDSKTLKEQL 2342
Cdd:TIGR02168  674 ERRREIEELEEKIEELEE-------KIAELEKALAELRKEL--------------EELEEELEQLRKELEELSRQISALR 732
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2343 AKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVayKAQVEPLTSPLKKTKLDSASDNIIQEYVTLRTRYSELMT 2422
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE--EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2423 LTSQYIKFITDTQRRLEDEEmadAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLEsQFEEEIKKAKALKDEQD 2502
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLE---RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESELEALLNERASLE 886
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2496167637 2503 RQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERkRLEQERVLADENQ-KLREKLQQMEEAQK 2573
Cdd:TIGR02168  887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL-RLEGLEVRIDNLQeRLSEEYSLTLEEAE 957
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3426-3464 1.14e-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: 1.14e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3426 LLEAQMVSGGIIDPVNSHRVPNDTAYQKNILSKEVAKTL 3464
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3759-3796 1.50e-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: 1.50e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2496167637 3759 LEAQTSTGGIIDPEFQFHLPADVAIQRGYINKETNEKL 3796
Cdd:pfam00681    2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
4346-4384 1.41e-09

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 55.80  E-value: 1.41e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 4346 FLEVQYLTGGLIEPEAQGRVSLDESIRKGTIDARTAQKL 4384
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3095-3133 2.20e-09

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 55.41  E-value: 2.20e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3095 LLDAQMTTGGIIDPVKSHRVPHDVACNRSYFDDEMKQHL 3133
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
4097-4125 7.18e-07

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 48.48  E-value: 7.18e-07
                           10        20
                   ....*....|....*....|....*....
gi 2496167637 4097 IVDPETGKEMTVYEAYRKGLIDHQTYIEL 4125
Cdd:pfam00681   11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3882-3920 8.56e-07

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 48.09  E-value: 8.56e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3882 YLEGTSCIAGVYLESNKERLSIYQAMKKNMIRPGTAFEL 3920
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC smart00150
Spectrin repeats;
1609-1703 2.50e-06

Spectrin repeats;


:

Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.87  E-value: 2.50e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  1609 LRYVQDLLEWVQENQRRIDEAEWGSDLPSVESQLGSHRGLHQTVEDFRSKIERAKADENQL---SPISRGKYREYLGRLD 1685
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
                            90
                    ....*....|....*...
gi 2496167637  1686 LQYAKLLNSSKSRLRNLD 1703
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
3957-3988 2.22e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.01  E-value: 2.22e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2496167637  3957 KLLSAERAVTGYRDPYTGKTISLFQAMKKGLI 3988
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
PLEC smart00250
Plectin repeat;
3056-3092 2.33e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.01  E-value: 2.33e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2496167637  3056 KLLSAERAVTGYRDPYTGKTVSLFQAMKKDLIPKEQG 3092
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1398-1721 4.59e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 4.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1398 YEEIEL-IWRQFLKFKETELPVKETDKNRSKQIYQTFESAVSAgqvkvppgyhpidVEKEWGRLHVAILERERLLRIEFE 1476
Cdd:TIGR02168  222 LRELELaLLVLRLEELREELEELQEELKEAEEELEELTAELQE-------------LEEKLEELRLEVSELEEEIEELQK 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1477 RLERLQRIVNKVQMESGSCDEQLGNLE-TLLQTDIRLLNAGKPAQHTAEIERELDKADNTIRLLFNDVQILKDGRHPQAE 1555
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLErQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1556 QMYRRVFRIHERLVNLRSDYNLRLKSTTS-AIQATRLSPQESSMKARpelddvtlryVQDLLEWVQENQRRIDEAEwgsd 1634
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVAQLELQIASlNNEIERLEARLERLEDR----------RERLQQEIEELLKKLEEAE---- 434
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1635 LPSVESQLGSH-RGLHQTVEDFRSKIERAKADENQLSPISRgKYREYLGRLDlQYAKLLNSSKSRLRNLDSLHAFVSAAT 1713
Cdd:TIGR02168  435 LKELQAELEELeEELEELQEELERLEEALEELREELEEAEQ-ALDAAERELA-QLQARLDSLERLQENLEGFSEGVKALL 512

                   ....*...
gi 2496167637 1714 KELMWLND 1721
Cdd:TIGR02168  513 KNQSGLSG 520
PLEC smart00250
Plectin repeat;
4231-4267 6.66e-05

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.85  E-value: 6.66e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2496167637  4231 DPSEETVPIAGILDTETLEKVSVTEAMHRNLVDNITG 4267
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3387-3418 2.06e-04

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 2.06e-04
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2496167637  3387 KLLSAEKAVTGYKDPFTGKTISLFEAMQKDLI 3418
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
PLEC smart00250
Plectin repeat;
2731-2761 5.19e-04

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.16  E-value: 5.19e-04
                            10        20        30
                    ....*....|....*....|....*....|.
gi 2496167637  2731 LSAEKAVVGYKDPYSGGKISVFEAMKKGLMD 2761
Cdd:smart00250    4 LEAQSAIGGIIDPETGQKLSVEEALRRGLID 34
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
338-613 7.76e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 45.68  E-value: 7.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  338 IKATAESDGVQSHVGITTAAVQSTTvlTAPITKKTvnkdviEEKAKEAIAHEVKSTELKSTVETPAKMKPQAVATVASVQ 417
Cdd:pfam05109  405 ITRTATNATTTTHKVIFSKAPESTT--TSPTLNTT------GFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSP 476
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  418 ESYDTNDTSTPVITKPVKEEKAKKKKATEESVKLAEVKIPGQEKATKTDKVSVPTKAKPGSTTGKPVVSDNVETPKvvqe 497
Cdd:pfam05109  477 TPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPT---- 552
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  498 PSDATPTSVNISEKPKSEV--LSKAAESSILEVTTSVRTGLTSSRTNAevvQVATDKTTIKEKRTTQDVMTlthvekdge 575
Cdd:pfam05109  553 PNATSPTPAVTTPTPNATIptLGKTSPTSAVTTPTPNATSPTVGETSP---QANTTNHTLGGTSSTPVVTS--------- 620
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2496167637  576 iapeDPKDPTPAPPSVQEDATTYHKSQNDVGIEAVKET 613
Cdd:pfam05109  621 ----PPKNATSAVTTGQHNITSSSTSSMSLRPSSISET 654
PLEC smart00250
Plectin repeat;
3643-3679 2.25e-03

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 38.23  E-value: 2.25e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2496167637  3643 KQYLYGTGCVAGFT-TDSGSKMSIYQAMKRGFIQPDVA 3679
Cdd:smart00250    1 QRLLEAQSAIGGIIdPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3311-3347 2.48e-03

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 38.23  E-value: 2.48e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2496167637  3311 KYLQGSESIAGIYLEPTKENISIYQAMKKKLLRHNTG 3347
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
 
Name Accession Description Interval E-value
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
1113-1229 9.19e-74

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


Pssm-ID: 409037  Cd Length: 105  Bit Score: 241.54  E-value: 9.19e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1113 DRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPREKGRMRFHKLQNVQIALD 1192
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGE------------SLPRERGRMRFHRLQNVQTALD 68
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2496167637 1193 FLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 1229
Cdd:cd21188     69 FLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
1246-1351 2.87e-65

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: 217.20  E-value: 2.87e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1246 MSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21238      1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 2496167637 1326 PEDVDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
S10_plectin pfam03501
Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the ...
7-99 4.91e-49

Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the cytoskeletal muscle protein plectin as well as the ribosomal S10 protein. This domain may be involved in RNA binding.


Pssm-ID: 427337  Cd Length: 92  Bit Score: 170.39  E-value: 4.91e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637    7 MPLRELRAIYEVLFRDGVMVAKKDkRPQIKHPEVqDVSNLQVIRAMGSLKSRGYVKETFAWRHFYWYLTNEGIVYLRDYL 86
Cdd:pfam03501    1 IPKENRKAIYEYLFKEGVLVAKKD-FNLPKHPEL-NVPNLQVIKAMQSLKSRGYVKEQFAWRHYYWYLTNEGIEYLREYL 78
                           90
                   ....*....|...
gi 2496167637   87 HLPPEIVPASLQR 99
Cdd:pfam03501   79 HLPAEIVPATLKR 91
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
1981-2058 5.99e-43

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: 152.37  E-value: 5.99e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2496167637 1981 LSWQYLMKDFTLIRSWNITMLKTMKPEEYRLILRNLELHYQDFMRDSQDSQLFGPDDRMQIEGDYTKSTQHFDSLLRS 2058
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1109-1457 2.09e-40

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 161.65  E-value: 2.09e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1109 EDERDRVQKKTFTKWVNKHLIKS-QRHVTDLYEDLRDGHNLISLLEVLsGDTLLSERDVARsvrlprekgRMRFHKLQNV 1187
Cdd:COG5069      3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEAL-QKDNAGEYNETP---------ETRIHVMENV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1188 QIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILhfqvSSSISDIQvngQSEDMSAKEKLLLWSQRMTDGYQ-GI 1266
Cdd:COG5069     73 SGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLIS----RLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEV 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1267 RCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLE--NLEQAFNVAEKDLGVTRLLDPEDV-DVPHPDEKSIITYV 1343
Cdd:COG5069    146 DTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYV 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1344 SSLYDAMPRTDAHDgISTTELE-----LRW----REYYELVtlLIQWIRHHVMIFEER---QFPTSYEEIELIWRQFLKF 1411
Cdd:COG5069    226 SWYIIRFGLLEKID-IALHRVYrlleaDETliqlRLPYEII--LLRLLNLIHLKQANWkvvNFSKDVSDGENYTDLLNQL 302
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2496167637 1412 KETE--LPVKETD-KNRSKQIYQTFESaVSAGQVKVPPGYHPIDVEKEW 1457
Cdd:COG5069    303 NALCsrAPLETTDlHSLAGQILQNAEK-YDCRKYLPPAGNPKLDLAFVA 350
PTZ00034 PTZ00034
40S ribosomal protein S10; Provisional
5-139 1.32e-36

40S ribosomal protein S10; Provisional


Pssm-ID: 173331  Cd Length: 124  Bit Score: 135.92  E-value: 1.32e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637    5 MLMPLRELRAIYEVLFRDGVMVAKKDkRPQIKHPEVqDVSNLQVIRAMGSLKSRGYVKETFAWRHFYWYLTNEGIVYLRD 84
Cdd:PTZ00034     2 VYVPKANRKAIYRYLFKEGVIVCKKD-PKGPWHPEL-NVPNLHVMMLMRSLKSRGLVKEQFAWQHYYYYLTDEGIEYLRT 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2496167637   85 YLHLPPEIVPASLQRVRRPASTLAIARGARvqsvegptsyvPKPGRNNEAESEGA 139
Cdd:PTZ00034    80 YLHLPPDVFPATHKKKSVNFERKTEEEGSR-----------GGRGGRGRGRGYGR 123
COG5045 COG5045
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis];
5-105 9.97e-30

Ribosomal protein S10E [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227378  Cd Length: 105  Bit Score: 115.79  E-value: 9.97e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637    5 MLMPLRELRAIYEVLFRDGVMVAKKDKRpQIKHPEVqDVSNLQVIRAMGSLKSRGYVKETFAWRHFYWYLTNEGIVYLRD 84
Cdd:COG5045      1 MLVPKENRYKIHQRLFQKGVAVAKKDFN-LGKHREL-EIPNLHVIKAMQSLISYGYVKTIHVWRHSYYTLTPEGVEYLRE 78
                           90       100
                   ....*....|....*....|.
gi 2496167637   85 YLHLPPEIVPASLQRVRRPAS 105
Cdd:COG5045     79 YLVLPDEGVPSTEAPAVSPTQ 99
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
1246-1352 1.05e-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: 104.29  E-value: 1.05e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1246 MSAKEKLLLWSQRMTDGY-QGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVY--RQTNLENLEQAFNVAEKDLGVTR 1322
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2496167637 1323 -LLDPEDVDvpHPDEKSIITYVSSLYDAMPR 1352
Cdd:pfam00307   81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
1880-1946 2.10e-24

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 98.87  E-value: 2.10e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2496167637 1880 QLKPRNptTPIKGNLPVQAVCDFKQVEITVHKGDECALLNNSQPSKWKVMNRSGSEAVVPSVCFLVP 1946
Cdd:pfam17902    1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
1118-1227 3.95e-24

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 99.70  E-value: 3.95e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  1118 KTFTKWVNKHLIKS-QRHVTDLYEDLRDGHNLISLLEVLSGDTLlSERDVARSvrlprekgRMRFHKLQNVQIALDFLRH 1196
Cdd:smart00033    1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLV-DKKKVAAS--------LSRFKKIENINLALSFAEK 71
                            90       100       110
                    ....*....|....*....|....*....|.
gi 2496167637  1197 RQVKLVNIRNDDIADGnPKLTLGLIWTIILH 1227
Cdd:smart00033   72 LGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
1115-1229 1.28e-22

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 95.43  E-value: 1.28e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1115 VQKKTFTKWVNKHLIKSQRH--VTDLYEDLRDGHNLISLLEVLSGDtLLSERDVARSvrlprekgrmRFHKLQNVQIALD 1192
Cdd:pfam00307    2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPG-LVDKKKLNKS----------EFDKLENINLALD 70
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2496167637 1193 FLRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 1229
Cdd:pfam00307   71 VAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
1250-1346 2.35e-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: 85.83  E-value: 2.35e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  1250 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTN----LENLEQAFNVAEKDLGVTRLLD 1325
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 2496167637  1326 PEDVDVPHPDEKSIITYVSSL 1346
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1705-1891 8.32e-17

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 82.49  E-value: 8.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1705 LHAFVSAATKELMWLNDKEEEEVNYDWSDKNTNMTVKKENYSGLMRELELREKKVNDIQAMGDRLVKDGHPGKKTVEAFT 1784
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1785 AALQTQWSWILQLCCCVEAHLKENTAYYQFFTDVKDAQDKMKKMQENMKkkySCDRTTTATRLEDLLQDAVDEKEQLNEF 1864
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180
                   ....*....|....*....|....*..
gi 2496167637 1865 KTQVAGLNKRAKSIIQLKPRNPTTPIK 1891
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIE 185
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3996-4034 8.80e-16

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 73.52  E-value: 8.80e-16
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3996 LLEAQIATGGIIDPEESHRLPVEVAYKRGFFDEEMNEIL 4034
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3350-3388 1.90e-14

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 69.66  E-value: 1.90e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3350 LLEAQAASGFIVDPVKNQCLSVDEAVKSGVVGPELHEKL 3388
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3682-3720 5.95e-14

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 68.51  E-value: 5.95e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3682 LLETQAATGFIIDPIKNETLTVDEAVRKGVVGPEIHDKL 3720
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2692-2729 8.13e-14

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 68.12  E-value: 8.13e-14
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2496167637 2692 LLEAQAATGYMLDPINNHKLSVNEAVKEGLIGPELHNK 2729
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
4270-4308 9.99e-13

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 65.04  E-value: 9.99e-13
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 4270 LLEAQACTGGIIDPTTGERFTVTVATEKGLVDKAMVDRL 4308
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3020-3057 2.14e-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: 2.14e-12
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2496167637 3020 LEAQAGTGYVVDPVHNQHYTVDEAVKAGVVGPELHEKL 3057
Cdd:pfam00681    2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3920-3958 6.53e-11

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 59.65  E-value: 6.53e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3920 LLEAQAATGYIIDPIKSLKLTVNEAVSMGTVGPEFKDKL 3958
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2768-2805 6.86e-11

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 59.65  E-value: 6.86e-11
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2496167637 2768 VLEAQLATGGIIDPLNSHRVPNEIAYKQGQYDAEMNKI 2805
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2263-2573 9.36e-11

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: 68.54  E-value: 9.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2263 ERDAELDQHRQHLSSLQDrwkavftQIDLRQRELDQLGRQLgyyresydwlirwiADAKQRQENIQAVPITDSKTLKEQL 2342
Cdd:TIGR02168  674 ERRREIEELEEKIEELEE-------KIAELEKALAELRKEL--------------EELEEELEQLRKELEELSRQISALR 732
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2343 AKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVayKAQVEPLTSPLKKTKLDSASDNIIQEYVTLRTRYSELMT 2422
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE--EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2423 LTSQYIKFITDTQRRLEDEEmadAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLEsQFEEEIKKAKALKDEQD 2502
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLE---RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESELEALLNERASLE 886
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2496167637 2503 RQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERkRLEQERVLADENQ-KLREKLQQMEEAQK 2573
Cdd:TIGR02168  887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL-RLEGLEVRIDNLQeRLSEEYSLTLEEAE 957
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3426-3464 1.14e-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: 1.14e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3426 LLEAQMVSGGIIDPVNSHRVPNDTAYQKNILSKEVAKTL 3464
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3759-3796 1.50e-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: 1.50e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2496167637 3759 LEAQTSTGGIIDPEFQFHLPADVAIQRGYINKETNEKL 3796
Cdd:pfam00681    2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2336-2579 7.65e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.73  E-value: 7.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2336 KTLKEQ---------LAKEKKLLEeIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEpltspLKKTKLDSASDNI 2406
Cdd:COG1196    203 EPLERQaekaeryreLKEELKELE-AELLLLKLRELEAELEELEAELEELEAELEELEAELA-----ELEAELEELRLEL 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2407 IQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQ 2486
Cdd:COG1196    277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2487 fEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQEL--ERKRLEQERV-LADENQKLRE 2563
Cdd:COG1196    357 -EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALleRLERLEEELEeLEEALAELEE 435
                          250
                   ....*....|....*.
gi 2496167637 2564 KLQQMEEAQKSTLITE 2579
Cdd:COG1196    436 EEEEEEEALEEAAEEE 451
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
4346-4384 1.41e-09

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 55.80  E-value: 1.41e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 4346 FLEVQYLTGGLIEPEAQGRVSLDESIRKGTIDARTAQKL 4384
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2045-2573 1.83e-09

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 64.61  E-value: 1.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2045 YTKSTQHFDSLLRSMEKGLVVRHKGQQDETLCKNYISEVKDLRLRIEDCEARTVARIRKPVEKEPLKECIQKTAEQAKVQ 2124
Cdd:pfam02463  379 KKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQEL 458
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2125 VELEgLKKDLDKVSTKTQDILNSPQpsatapVLRSELELTVQKMDHAYMLSSVYLEKLKTVEMVIRNT-----------Q 2193
Cdd:pfam02463  459 KLLK-DELELKKSEDLLKETQLVKL------QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggriisahgrL 531
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2194 GAEGVLKQYENCLREVHTVPNDVKEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAVSDKMSRVHSERDAELDQHRQ 2273
Cdd:pfam02463  532 GDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2274 HLSSLQDRWKAVFTQIDLRQRELDQLGRQLGyyrESYDWLIRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIE 2353
Cdd:pfam02463  612 TLEADEDDKRAKVVEGILKDTELTKLKESAK---AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE 688
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2354 KNKDKVDECQKYAKAYIDIIKdyELQLVAYKAQVEpltspLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSqyikfITD 2433
Cdd:pfam02463  689 LAKEEILRRQLEIKKKEQREK--EELKKLKLEAEE-----LLADRVQEAQDKINEELKLLKQKIDEEEEEEE-----KSR 756
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2434 TQRRLEDEEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDrQRQQMEEEKL 2513
Cdd:pfam02463  757 LKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIE-QEEKIKEEEL 835
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2496167637 2514 KLKATMDAALNKQKEA--EKDILNKQKEMQELERKRLEQERVLADEnQKLREKLQQMEEAQK 2573
Cdd:pfam02463  836 EELALELKEEQKLEKLaeEELERLEEEITKEELLQELLLKEEELEE-QKLKDELESKEEKEK 896
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3095-3133 2.20e-09

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 55.41  E-value: 2.20e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3095 LLDAQMTTGGIIDPVKSHRVPHDVACNRSYFDDEMKQHL 3133
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
4268-4305 2.65e-09

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 55.18  E-value: 2.65e-09
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2496167637  4268 QRLLEAQACTGGIIDPTTGERFTVTVATEKGLVDKAMV 4305
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PTZ00121 PTZ00121
MAEBL; Provisional
2094-2604 3.63e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.62  E-value: 3.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2094 EARTVARIRKPVEKEPLKEcIQKTAEQAKVQVEL----EGLKKDLDKVSTKTQDILNSPQPS-ATAPVLRSELELTVQKM 2168
Cdd:PTZ00121  1288 EKKKADEAKKAEEKKKADE-AKKKAEEAKKADEAkkkaEEAKKKADAAKKKAEEAKKAAEAAkAEAEAAADEAEAAEEKA 1366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2169 DHAYMLSSVYLEKLKTVEMVIRNTQGAEGVLKQYEnclrEVHTVPNDVKEVETYRTNLKKMRAEAEAEQPVfdsleEELK 2248
Cdd:PTZ00121  1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE----EDKKKADELKKAAAAKKKADEAKKKAEEKKKA-----DEAK 1437
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2249 KASAVSDKMSRVhsERDAELDQHRQHLSSLQDRwkavftqidlrQRELDQLGRQLGYYRESyDWLIRWIADAKQRQENIQ 2328
Cdd:PTZ00121  1438 KKAEEAKKADEA--KKKAEEAKKAEEAKKKAEE-----------AKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAK 1503
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2329 AVPITDSKTLKEQLAKEKKLLEEIEK--NKDKVDECQKY--AKAYIDIIKDYELQLVAYKAQVEPLTSPLKKTKLDSASD 2404
Cdd:PTZ00121  1504 KAAEAKKKADEAKKAEEAKKADEAKKaeEAKKADEAKKAeeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2405 NIIQEyvTLRTRYSELMTLTSQYIKFITDTQRRLEDEEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDE----- 2479
Cdd:PTZ00121  1584 EEAKK--AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEeenki 1661
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2480 -KKKLESQFEEEIKKAKAL-KDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADE 2557
Cdd:PTZ00121  1662 kAAEEAKKAEEDKKKAEEAkKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 2496167637 2558 NQKLREKLQQMEEAQKSTLITEKHVTVVETVLNGQNAGDVLDGVEKR 2604
Cdd:PTZ00121  1742 DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2212-2386 7.56e-09

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 59.00  E-value: 7.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2212 VPNDVKEVETYRTNLKKMRAEAEAEQPVFDSLEEElkkasavSDKMSRVHSErdaELDQHRQHLSSLQDRWKAVFTQIDL 2291
Cdd:cd00176     28 YGDDLESVEALLKKHEALEAELAAHEERVEALNEL-------GEQLIEEGHP---DAEEIQERLEELNQRWEELRELAEE 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2292 RQRELDQLGRQLGYYRESYDwLIRWIADAKQRQENIQavPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYID 2371
Cdd:cd00176     98 RRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLE 174
                          170
                   ....*....|....*
gi 2496167637 2372 IIKDYELQLVAYKAQ 2386
Cdd:cd00176    175 EGHPDADEEIEEKLE 189
SPEC smart00150
Spectrin repeats;
1706-1798 8.72e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 55.80  E-value: 8.72e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  1706 HAFVSAATKELMWLNDKEEEEVNYDWSDKNTNMTVKKENYSGLMRELELREKKVNDIQAMGDRLVKDGHPGKKTVEAFTA 1785
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90
                    ....*....|...
gi 2496167637  1786 ALQTQWSWILQLC 1798
Cdd:smart00150   81 ELNERWEELKELA 93
PLEC smart00250
Plectin repeat;
3994-4030 3.58e-08

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 52.10  E-value: 3.58e-08
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2496167637  3994 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGFFDEEM 4030
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
2111-2830 4.13e-07

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 56.98  E-value: 4.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2111 KECIQKTAEQAKVQVELEGLKKDLDKVSTKTQDILNSPQPSAtapvlrSELELTVQKMDHAyMLSSVYLEKLKTVEMVIR 2190
Cdd:TIGR01612 1104 EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYI------DEIKAQINDLEDV-ADKAISNDDPEEIEKKIE 1176
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2191 NTQGAegvLKQYENCLREVHTVPNDVKEVETYRTNLKKMRA-------------------EAEAEQPVFDSLEEELKKAS 2251
Cdd:TIGR01612 1177 NIVTK---IDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGinlsygknlgklflekideEKKKSEHMIKAMEAYIEDLD 1253
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2252 AVSDKMSRVHSERDAELDQHRQ----HLSSLQDRWKAVFTQ------IDLRQRELDQLGrqlGYYRES-----YDWLIRW 2316
Cdd:TIGR01612 1254 EIKEKSPEIENEMGIEMDIKAEmetfNISHDDDKDHHIISKkhdeniSDIREKSLKIIE---DFSEESdindiKKELQKN 1330
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2317 IADAKQRQENIQAV--------PITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDyelqlvayKAQVE 2388
Cdd:TIGR01612 1331 LLDAQKHNSDINLYlneianiyNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD--------DINLE 1402
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2389 PLTSPLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRL----EDEEMADAQQKQIeremtvlqqtflt 2464
Cdd:TIGR01612 1403 ECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVlllfKNIEMADNKSQHI------------- 1469
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2465 ekeMLLKKEKLIEDEKKKLeSQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKatmdaalnKQKEAEKDILNKQKEMQ--- 2541
Cdd:TIGR01612 1470 ---LKIKKDNATNDHDFNI-NELKEHIDKSKGCKDEADKNAKAIEKNKELFE--------QYKKDVTELLNKYSALAikn 1537
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2542 ELERKRLEQERVLaDENQKLREK--LQQMEEAQKSTLITEKHVTVVETVLNGQNAGDVLDGVEKRPDPMafdgirdkvpA 2619
Cdd:TIGR01612 1538 KFAKTKKDSEIII-KEIKDAHKKfiLEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENF----------E 1606
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2620 SRLLDIGVLPKKEFDLLKngkttakelgETENLRKilkgknsiagiltpsnQKMTIYQASKEKKITP-GTAMILLEAqaa 2698
Cdd:TIGR01612 1607 NKFLKISDIKKKINDCLK----------ETESIEK----------------KISSFSIDSQDTELKEnGDNLNSLQE--- 1657
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2699 tgyMLDPINNHKLSVNEAVKEgliGPELHNKMLSAEKAVVGYKDPYsggKISVFEAMKKGLMDHDHAIRVLEAQLATG-- 2776
Cdd:TIGR01612 1658 ---FLESLKDQKKNIEDKKKE---LDELDSEIEKIEIDVDQHKKNY---EIGIIEKIKEIAIANKEEIESIKELIEPTie 1728
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2496167637 2777 GIIDPLNSHRV----PNEiayKQGQYDAEMNKIME---NPSDDTKGYFDPSTQEPLTYSEL 2830
Cdd:TIGR01612 1729 NLISSFNTNDLegidPNE---KLEEYNTEIGDIYEefiELYNIIAGCLETVSKEPITYDEI 1786
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
4097-4125 7.18e-07

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 48.48  E-value: 7.18e-07
                           10        20
                   ....*....|....*....|....*....
gi 2496167637 4097 IVDPETGKEMTVYEAYRKGLIDHQTYIEL 4125
Cdd:pfam00681   11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3882-3920 8.56e-07

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 48.09  E-value: 8.56e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3882 YLEGTSCIAGVYLESNKERLSIYQAMKKNMIRPGTAFEL 3920
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
3881-3917 9.43e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 47.86  E-value: 9.43e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2496167637  3881 KYLEGTSCIAGVYLESNKERLSIYQAMKKNMIRPGTA 3917
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
SPEC smart00150
Spectrin repeats;
1609-1703 2.50e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.87  E-value: 2.50e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  1609 LRYVQDLLEWVQENQRRIDEAEWGSDLPSVESQLGSHRGLHQTVEDFRSKIERAKADENQL---SPISRGKYREYLGRLD 1685
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
                            90
                    ....*....|....*...
gi 2496167637  1686 LQYAKLLNSSKSRLRNLD 1703
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
3680-3716 9.63e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 45.17  E-value: 9.63e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2496167637  3680 LNLLETQAATGFIIDPIKNETLTVDEAVRKGVVGPEI 3716
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
4090-4118 1.38e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.78  E-value: 1.38e-05
                            10        20
                    ....*....|....*....|....*....
gi 2496167637  4090 VRKRRVVIVDPETGKEMTVYEAYRKGLID 4118
Cdd:smart00250    6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
PLEC smart00250
Plectin repeat;
3957-3988 2.22e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.01  E-value: 2.22e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2496167637  3957 KLLSAERAVTGYRDPYTGKTISLFQAMKKGLI 3988
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
PLEC smart00250
Plectin repeat;
3056-3092 2.33e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.01  E-value: 2.33e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2496167637  3056 KLLSAERAVTGYRDPYTGKTVSLFQAMKKDLIPKEQG 3092
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3350-3383 4.50e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 4.50e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2496167637  3350 LLEAQAASGFIVDPVKNQCLSVDEAVKSGVVGPE 3383
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1398-1721 4.59e-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: 50.06  E-value: 4.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1398 YEEIEL-IWRQFLKFKETELPVKETDKNRSKQIYQTFESAVSAgqvkvppgyhpidVEKEWGRLHVAILERERLLRIEFE 1476
Cdd:TIGR02168  222 LRELELaLLVLRLEELREELEELQEELKEAEEELEELTAELQE-------------LEEKLEELRLEVSELEEEIEELQK 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1477 RLERLQRIVNKVQMESGSCDEQLGNLE-TLLQTDIRLLNAGKPAQHTAEIERELDKADNTIRLLFNDVQILKDGRHPQAE 1555
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLErQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1556 QMYRRVFRIHERLVNLRSDYNLRLKSTTS-AIQATRLSPQESSMKARpelddvtlryVQDLLEWVQENQRRIDEAEwgsd 1634
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVAQLELQIASlNNEIERLEARLERLEDR----------RERLQQEIEELLKKLEEAE---- 434
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1635 LPSVESQLGSH-RGLHQTVEDFRSKIERAKADENQLSPISRgKYREYLGRLDlQYAKLLNSSKSRLRNLDSLHAFVSAAT 1713
Cdd:TIGR02168  435 LKELQAELEELeEELEELQEELERLEEALEELREELEEAEQ-ALDAAERELA-QLQARLDSLERLQENLEGFSEGVKALL 512

                   ....*...
gi 2496167637 1714 KELMWLND 1721
Cdd:TIGR02168  513 KNQSGLSG 520
PLEC smart00250
Plectin repeat;
4231-4267 6.66e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.85  E-value: 6.66e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2496167637  4231 DPSEETVPIAGILDTETLEKVSVTEAMHRNLVDNITG 4267
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
4344-4381 8.51e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 8.51e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2496167637  4344 QRFLEVQYLTGGLIEPEAQGRVSLDESIRKGTIDARTA 4381
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1705-1798 1.59e-04

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 43.85  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1705 LHAFVSAATKELMWLNDKEEEEVNYDWSDKNTNMTVKKENYSGLMRELELREKKVNDIQAMGDRLVKDGHPGKKTVEAFT 1784
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERL 82
                           90
                   ....*....|....
gi 2496167637 1785 AALQTQWSWILQLC 1798
Cdd:pfam00435   83 EELNERWEQLLELA 96
PLEC smart00250
Plectin repeat;
3387-3418 2.06e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 2.06e-04
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2496167637  3387 KLLSAEKAVTGYKDPFTGKTISLFEAMQKDLI 3418
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
2406-2574 2.19e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 46.55  E-value: 2.19e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  2406 IIQEYVTLRTRYSELMTLTSQYIKfitdTQRRLEDEEM--------ADAQQKQIEREMTVLQQtfltEKEMLLKKEKLIE 2477
Cdd:smart00787  100 LFKEYFSASPDVKLLMDKQFQLVK----TFARLEAKKMwyewrmklLEGLKEGLDENLEGLKE----DYKLLMKELELLN 171
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  2478 DEKKKLESQFEEEIKKAKALKdeqdrqrqQMEEEKLKLKAT-MDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLAD 2556
Cdd:smart00787  172 SIKPKLRDRKDALEEELRQLK--------QLEDELEDCDPTeLDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIED 243
                           170
                    ....*....|....*...
gi 2496167637  2557 ENQKLREKLQQMEEAQKS 2574
Cdd:smart00787  244 LTNKKSELNTEIAEAEKK 261
PLEC smart00250
Plectin repeat;
2692-2725 2.51e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.93  E-value: 2.51e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2496167637  2692 LLEAQAATGYMLDPINNHKLSVNEAVKEGLIGPE 2725
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
PLEC smart00250
Plectin repeat;
2731-2761 5.19e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.16  E-value: 5.19e-04
                            10        20        30
                    ....*....|....*....|....*....|.
gi 2496167637  2731 LSAEKAVVGYKDPYSGGKISVFEAMKKGLMD 2761
Cdd:smart00250    4 LEAQSAIGGIIDPETGQKLSVEEALRRGLID 34
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
4239-4270 5.62e-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: 5.62e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2496167637 4239 IAGILDTETLEKVSVTEAMHRNLVDNITGQRL 4270
Cdd:pfam00681    8 TGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
3020-3052 5.90e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.16  E-value: 5.90e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2496167637  3020 LEAQAGTGYVVDPVHNQHYTVDEAVKAGVVGPE 3052
Cdd:smart00250    4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
338-613 7.76e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 45.68  E-value: 7.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  338 IKATAESDGVQSHVGITTAAVQSTTvlTAPITKKTvnkdviEEKAKEAIAHEVKSTELKSTVETPAKMKPQAVATVASVQ 417
Cdd:pfam05109  405 ITRTATNATTTTHKVIFSKAPESTT--TSPTLNTT------GFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSP 476
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  418 ESYDTNDTSTPVITKPVKEEKAKKKKATEESVKLAEVKIPGQEKATKTDKVSVPTKAKPGSTTGKPVVSDNVETPKvvqe 497
Cdd:pfam05109  477 TPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPT---- 552
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  498 PSDATPTSVNISEKPKSEV--LSKAAESSILEVTTSVRTGLTSSRTNAevvQVATDKTTIKEKRTTQDVMTlthvekdge 575
Cdd:pfam05109  553 PNATSPTPAVTTPTPNATIptLGKTSPTSAVTTPTPNATSPTVGETSP---QANTTNHTLGGTSSTPVVTS--------- 620
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2496167637  576 iapeDPKDPTPAPPSVQEDATTYHKSQNDVGIEAVKET 613
Cdd:pfam05109  621 ----PPKNATSAVTTGQHNITSSSTSSMSLRPSSISET 654
PLEC smart00250
Plectin repeat;
2766-2802 9.18e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.39  E-value: 9.18e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2496167637  2766 IRVLEAQLATGGIIDPLNSHRVPNEIAYKQGQYDAEM 2802
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
PLEC smart00250
Plectin repeat;
3426-3461 2.20e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 38.62  E-value: 2.20e-03
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 2496167637  3426 LLEAQMVSGGIIDPVNSHRVPNDTAYQKNILSKEVA 3461
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3643-3679 2.25e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 38.23  E-value: 2.25e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2496167637  3643 KQYLYGTGCVAGFT-TDSGSKMSIYQAMKRGFIQPDVA 3679
Cdd:smart00250    1 QRLLEAQSAIGGIIdPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3311-3347 2.48e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 38.23  E-value: 2.48e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2496167637  3311 KYLQGSESIAGIYLEPTKENISIYQAMKKKLLRHNTG 3347
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
rplD PRK14907
50S ribosomal protein L4; Provisional
389-545 3.96e-03

50S ribosomal protein L4; Provisional


Pssm-ID: 184900 [Multi-domain]  Cd Length: 295  Bit Score: 42.63  E-value: 3.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  389 EVKSTELKSTVE--TPAKMKPQAVATVASVQEsydTNDTSTPVITKPvkEEKAKKKKATEESVKLAEVKIpgqEKATKTD 466
Cdd:PRK14907     3 ETKKTTKKKTTEekKPAAKKATTSKETAKTKK---TAKTTSTKAAKK--AAKVKKTKSVKTTTKKVTVKF---EKTESVK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  467 KVSVPTKakpgsTTGKPVVSDNVETPKVVQEPSDAT-PTSVNISEKPKSEvlskAAESSILEVTTSVRTGLTSSRTNAEV 545
Cdd:PRK14907    75 KESVAKK-----TVKKEAVSAEVFEASNKLFKNTSKlPKKLFASEKIYSQ----AIFDTILSERASRRQGTHKVKTRAEV 145
SH3_Tec_like cd11768
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ...
1896-1940 5.02e-03

Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212702 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 5.02e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2496167637 1896 VQAVCDFKQVE---ITVHKGDECALLNNSQPSKWKVMNRSGSEAVVPS 1940
Cdd:cd11768      2 VVALYDFQPIEpgdLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPS 49
PLEC smart00250
Plectin repeat;
3759-3792 5.09e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.46  E-value: 5.09e-03
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2496167637  3759 LEAQTSTGGIIDPEFQFHLPADVAIQRGYINKET 3792
Cdd:smart00250    4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
 
Name Accession Description Interval E-value
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
1113-1229 9.19e-74

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


Pssm-ID: 409037  Cd Length: 105  Bit Score: 241.54  E-value: 9.19e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1113 DRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPREKGRMRFHKLQNVQIALD 1192
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGE------------SLPRERGRMRFHRLQNVQTALD 68
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2496167637 1193 FLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 1229
Cdd:cd21188     69 FLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
1110-1244 4.62e-70

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: 231.45  E-value: 4.62e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1110 DERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlserdvarsvrlPREKGRMRFHKLQNVQI 1189
Cdd:cd21235      1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSL------------PREKGRMRFHKLQNVQI 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2496167637 1190 ALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQvsssISDIQVNGQSE 1244
Cdd:cd21235     69 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ----ISDIQVSGQSE 119
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
1110-1242 1.48e-66

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: 221.78  E-value: 1.48e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1110 DERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlserdvarsvrlPREKGRMRFHKLQNVQI 1189
Cdd:cd21236     12 DERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTL------------PREKGRMRFHRLQNVQI 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2496167637 1190 ALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQvsssISDIQVNGQ 1242
Cdd:cd21236     80 ALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQ----ISDIHVTGE 128
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
1246-1351 2.87e-65

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: 217.20  E-value: 2.87e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1246 MSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21238      1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 2496167637 1326 PEDVDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
1247-1351 5.77e-64

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: 213.41  E-value: 5.77e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21189      1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                           90       100
                   ....*....|....*....|....*
gi 2496167637 1327 EDVDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21189     81 EDVDVPEPDEKSIITYVSSLYDVFP 105
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
1110-1243 4.26e-59

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


Pssm-ID: 409086  Cd Length: 118  Bit Score: 200.26  E-value: 4.26e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1110 DERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGdtllserdvarsVRLPREKGRMRFHKLQNVQI 1189
Cdd:cd21237      1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSG------------VKLPREKGRMRFHRLQNVQI 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2496167637 1190 ALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQvsssISDIQVNGQS 1243
Cdd:cd21237     69 ALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQ----ISDIYISGES 118
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
1247-1351 1.49e-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: 195.21  E-value: 1.49e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 1326
Cdd:cd21239      1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
                           90       100
                   ....*....|....*....|....*
gi 2496167637 1327 EDVDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21239     80 EDVDVSSPDEKSVITYVSSLYDVFP 104
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
1245-1351 2.49e-50

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: 174.46  E-value: 2.49e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1245 DMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLL 1324
Cdd:cd21240      2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
                           90       100
                   ....*....|....*....|....*..
gi 2496167637 1325 DPEDVDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21240     81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
S10_plectin pfam03501
Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the ...
7-99 4.91e-49

Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the cytoskeletal muscle protein plectin as well as the ribosomal S10 protein. This domain may be involved in RNA binding.


Pssm-ID: 427337  Cd Length: 92  Bit Score: 170.39  E-value: 4.91e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637    7 MPLRELRAIYEVLFRDGVMVAKKDkRPQIKHPEVqDVSNLQVIRAMGSLKSRGYVKETFAWRHFYWYLTNEGIVYLRDYL 86
Cdd:pfam03501    1 IPKENRKAIYEYLFKEGVLVAKKD-FNLPKHPEL-NVPNLQVIKAMQSLKSRGYVKEQFAWRHYYWYLTNEGIEYLREYL 78
                           90
                   ....*....|...
gi 2496167637   87 HLPPEIVPASLQR 99
Cdd:pfam03501   79 HLPAEIVPATLKR 91
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
1115-1230 1.81e-48

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


Pssm-ID: 409035  Cd Length: 107  Bit Score: 169.10  E-value: 1.81e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1115 VQKKTFTKWVNKHLIKSQR-HVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPREKGRMRFHKLQNVQIALDF 1193
Cdd:cd21186      2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGK------------KLKPEKGRMRVHHLNNVNRALQV 69
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2496167637 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21186     70 LEQNNVKLVNISSNDIVDGNPKLTLGLVWSIILHWQV 106
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
1247-1347 1.25e-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: 163.74  E-value: 1.25e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21194      2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
                           90       100
                   ....*....|....*....|.
gi 2496167637 1327 EDVDVPHPDEKSIITYVSSLY 1347
Cdd:cd21194     82 EDVDVARPDEKSIMTYVASYY 102
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
1110-1226 3.20e-46

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


Pssm-ID: 409095  Cd Length: 117  Bit Score: 163.31  E-value: 3.20e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1110 DERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPR-EKGRMRFHKLQNVQ 1188
Cdd:cd21246     11 DEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGE------------RLPKpTKGKMRIHCLENVD 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2496167637 1189 IALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1226
Cdd:cd21246     79 KALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
1247-1347 5.23e-45

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: 159.10  E-value: 5.23e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21248      2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
                           90       100
                   ....*....|....*....|.
gi 2496167637 1327 EDVDVPHPDEKSIITYVSSLY 1347
Cdd:cd21248     82 EDVNVEQPDEKSIITYVVTYY 102
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
1981-2058 5.99e-43

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: 152.37  E-value: 5.99e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2496167637 1981 LSWQYLMKDFTLIRSWNITMLKTMKPEEYRLILRNLELHYQDFMRDSQDSQLFGPDDRMQIEGDYTKSTQHFDSLLRS 2058
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
1111-1230 4.56e-42

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


Pssm-ID: 409090  Cd Length: 113  Bit Score: 151.37  E-value: 4.56e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1111 ERDRVQKKTFTKWVNKHLIKSQR--HVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPREKGRM--RFHKLQN 1186
Cdd:cd21241      1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGE------------KLPCEKGRRlkRVHFLSN 68
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2496167637 1187 VQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21241     69 INTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
1108-1226 1.80e-41

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: 149.75  E-value: 1.80e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1108 IEDERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPR-EKGRMRFHKLQN 1186
Cdd:cd21193      9 LQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGE------------KLGKpNRGRLRVQKIEN 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2496167637 1187 VQIALDFLrHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1226
Cdd:cd21193     77 VNKALAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1109-1457 2.09e-40

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 161.65  E-value: 2.09e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1109 EDERDRVQKKTFTKWVNKHLIKS-QRHVTDLYEDLRDGHNLISLLEVLsGDTLLSERDVARsvrlprekgRMRFHKLQNV 1187
Cdd:COG5069      3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEAL-QKDNAGEYNETP---------ETRIHVMENV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1188 QIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILhfqvSSSISDIQvngQSEDMSAKEKLLLWSQRMTDGYQ-GI 1266
Cdd:COG5069     73 SGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLIS----RLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEV 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1267 RCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLE--NLEQAFNVAEKDLGVTRLLDPEDV-DVPHPDEKSIITYV 1343
Cdd:COG5069    146 DTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYV 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1344 SSLYDAMPRTDAHDgISTTELE-----LRW----REYYELVtlLIQWIRHHVMIFEER---QFPTSYEEIELIWRQFLKF 1411
Cdd:COG5069    226 SWYIIRFGLLEKID-IALHRVYrlleaDETliqlRLPYEII--LLRLLNLIHLKQANWkvvNFSKDVSDGENYTDLLNQL 302
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2496167637 1412 KETE--LPVKETD-KNRSKQIYQTFESaVSAGQVKVPPGYHPIDVEKEW 1457
Cdd:COG5069    303 NALCsrAPLETTDlHSLAGQILQNAEK-YDCRKYLPPAGNPKLDLAFVA 350
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
1246-1351 3.29e-40

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: 145.54  E-value: 3.29e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1246 MSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21243      4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
                           90       100
                   ....*....|....*....|....*.
gi 2496167637 1326 PEDVDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21243     84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
1234-1349 7.84e-40

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: 144.81  E-value: 7.84e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1234 ISDIQVngqsEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNV 1313
Cdd:cd21216      1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2496167637 1314 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21216     77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
1243-1347 1.52e-39

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: 143.99  E-value: 1.52e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1243 SEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTR 1322
Cdd:cd21319      1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
                           90       100
                   ....*....|....*....|....*
gi 2496167637 1323 LLDPEDVDVPHPDEKSIITYVSSLY 1347
Cdd:cd21319     81 LLDPEDVFTENPDEKSIITYVVAFY 105
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
1111-1230 2.52e-39

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: 143.48  E-value: 2.52e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1111 ERDRVQKKTFTKWVNKHLIK--SQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPREKGRM--RFHKLQN 1186
Cdd:cd21190      1 EQERVQKKTFTNWINSHLAKlsQPIVINDLFVDIKDGTALLRLLEVLSGQ------------KLPIESGRVlqRAHKLSN 68
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2496167637 1187 VQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21190     69 IRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
1087-1226 2.89e-39

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


Pssm-ID: 409166  Cd Length: 132  Bit Score: 144.04  E-value: 2.89e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1087 ADKAEWDH--SLGEPEEKTWPNFIEDERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllser 1164
Cdd:cd21317      1 LADDDWDNdnSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGE------ 74
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2496167637 1165 dvarsvRLPR-EKGRMRFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1226
Cdd:cd21317     75 ------QLPKpTKGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
1108-1226 1.55e-38

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


Pssm-ID: 409167  Cd Length: 139  Bit Score: 142.09  E-value: 1.55e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1108 IEDERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPR-EKGRMRFHKLQN 1186
Cdd:cd21318     31 LADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGE------------QLPKpTRGRMRIHSLEN 98
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2496167637 1187 VQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1226
Cdd:cd21318     99 VDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
1246-1347 1.35e-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: 138.46  E-value: 1.35e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1246 MSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21249      3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
                           90       100
                   ....*....|....*....|..
gi 2496167637 1326 PEDVDVPHPDEKSIITYVSSLY 1347
Cdd:cd21249     83 PEDVAVPHPDERSIMTYVSLYY 104
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
1243-1355 1.95e-37

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: 138.27  E-value: 1.95e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1243 SEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTR 1322
Cdd:cd21321      1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2496167637 1323 LLDPEDVDVPHPDEKSIITYVSSLYDAMPRTDA 1355
Cdd:cd21321     81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKMKA 113
PTZ00034 PTZ00034
40S ribosomal protein S10; Provisional
5-139 1.32e-36

40S ribosomal protein S10; Provisional


Pssm-ID: 173331  Cd Length: 124  Bit Score: 135.92  E-value: 1.32e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637    5 MLMPLRELRAIYEVLFRDGVMVAKKDkRPQIKHPEVqDVSNLQVIRAMGSLKSRGYVKETFAWRHFYWYLTNEGIVYLRD 84
Cdd:PTZ00034     2 VYVPKANRKAIYRYLFKEGVIVCKKD-PKGPWHPEL-NVPNLHVMMLMRSLKSRGLVKEQFAWQHYYYYLTDEGIEYLRT 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2496167637   85 YLHLPPEIVPASLQRVRRPASTLAIARGARvqsvegptsyvPKPGRNNEAESEGA 139
Cdd:PTZ00034    80 YLHLPPDVFPATHKKKSVNFERKTEEEGSR-----------GGRGGRGRGRGYGR 123
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
1237-1355 1.17e-35

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: 133.64  E-value: 1.17e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1237 IQVNGQSEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEK 1316
Cdd:cd21322      7 IETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQ 86
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2496167637 1317 DLGVTRLLDPEDVDVPHPDEKSIITYVSSLYDAMPRTDA 1355
Cdd:cd21322     87 HLGLTKLLDPEDVNMEAPDEKSIITYVVSFYHYFSKMKA 125
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
1115-1228 1.43e-35

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: 132.52  E-value: 1.43e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1115 VQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlserdvARSVRLPRekgrMRFHKLQNVQIALDFL 1194
Cdd:cd21215      4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESL------GRYNKNPK----MRVQKLENVNKALEFI 73
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2496167637 1195 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 1228
Cdd:cd21215     74 KSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
1113-1226 2.13e-35

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: 131.74  E-value: 2.13e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1113 DRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLLserdvarsvrlPREKGRMRFHKLQNVQIALD 1192
Cdd:cd21214      3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLP-----------KPERGKMRFHKIANVNKALD 71
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2496167637 1193 FLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1226
Cdd:cd21214     72 FIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
1111-1230 2.66e-35

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: 131.88  E-value: 2.66e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1111 ERDRVQKKTFTKWVNKHLIKSQ--RHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPREKGRMRFHKLQNVQ 1188
Cdd:cd21242      1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQ------------QLPREKGHNVFQCRSNIE 68
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2496167637 1189 IALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21242     69 TALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
1247-1347 1.80e-34

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: 129.45  E-value: 1.80e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21320      2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
                           90       100
                   ....*....|....*....|.
gi 2496167637 1327 EDVDVPHPDEKSIITYVSSLY 1347
Cdd:cd21320     82 EDISVDHPDEKSIITYVVTYY 102
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
1250-1351 2.79e-34

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: 128.70  E-value: 2.79e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1250 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED 1328
Cdd:cd21187      2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
                           90       100
                   ....*....|....*....|...
gi 2496167637 1329 VDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21187     82 VNVEQPDKKSILMYVTSLFQVLP 104
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
1110-1230 8.07e-34

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


Pssm-ID: 409080  Cd Length: 111  Bit Score: 127.73  E-value: 8.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1110 DERDRVQKKTFTKWVNKHLIKSQR-HVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPREKGRMRFHKLQNVQ 1188
Cdd:cd21231      1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQ------------KLVKEKGSTRVHALNNVN 68
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2496167637 1189 IALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21231     69 KALQVLQKNNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
1246-1344 1.56e-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: 126.77  E-value: 1.56e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1246 MSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21192      2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
                           90
                   ....*....|....*....
gi 2496167637 1326 PEDVDVPHPDEKSIITYVS 1344
Cdd:cd21192     82 VEDVLVDKPDERSIMTYVS 100
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
1246-1344 1.45e-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: 123.79  E-value: 1.45e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1246 MSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21244      4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
                           90
                   ....*....|....*....
gi 2496167637 1326 PEDVDVPHPDEKSIITYVS 1344
Cdd:cd21244     84 PEDVDVVNPDEKSIMTYVA 102
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
1088-1226 1.49e-32

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: 125.54  E-value: 1.49e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1088 DKAEWDH--SLGEPEEKTWPNFIEDERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserd 1165
Cdd:cd21316     24 DVDEWDNenSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGE------- 96
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2496167637 1166 varsvRLPR-EKGRMRFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 1226
Cdd:cd21316     97 -----RLPKpTKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
1115-1230 7.94e-31

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


Pssm-ID: 409076  Cd Length: 109  Bit Score: 118.93  E-value: 7.94e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1115 VQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGdtllseRDVARSVRLPRekgrMRFHKLQNVQIALDFL 1194
Cdd:cd21227      4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQG------RKLGRVIKKPL----NQHQKLENVTLALKAM 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2496167637 1195 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21227     74 AEDGIKLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
1234-1349 1.90e-30

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: 118.01  E-value: 1.90e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1234 ISDIQvngqSEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNV 1313
Cdd:cd21291      1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2496167637 1314 AEKDLGVTRLLDPEDV-DVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21291     77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
1111-1230 2.38e-30

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


Pssm-ID: 409040  Cd Length: 114  Bit Score: 117.68  E-value: 2.38e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1111 ERDRVQKKTFTKWVNKHLIKSQR--HVTDLYEDLRDGHNLISLLEVLSGDTLLSERdvarsvrlprEKGRMRFHKLQNVQ 1188
Cdd:cd21191      1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEY----------KPSSHRIFRLNNIA 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2496167637 1189 IALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21191     71 KALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQI 112
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
1250-1352 4.76e-30

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: 116.95  E-value: 4.76e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1250 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTN-LENLEQAFNVAEKDLGVTRLLDPE 1327
Cdd:cd21233      2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
                           90       100
                   ....*....|....*....|....*
gi 2496167637 1328 DVDVPHPDEKSIITYVSSLYDAMPR 1352
Cdd:cd21233     82 DVATAHPDKKSILMYVTSLFQVLPQ 106
COG5045 COG5045
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis];
5-105 9.97e-30

Ribosomal protein S10E [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227378  Cd Length: 105  Bit Score: 115.79  E-value: 9.97e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637    5 MLMPLRELRAIYEVLFRDGVMVAKKDKRpQIKHPEVqDVSNLQVIRAMGSLKSRGYVKETFAWRHFYWYLTNEGIVYLRD 84
Cdd:COG5045      1 MLVPKENRYKIHQRLFQKGVAVAKKDFN-LGKHREL-EIPNLHVIKAMQSLISYGYVKTIHVWRHSYYTLTPEGVEYLRE 78
                           90       100
                   ....*....|....*....|.
gi 2496167637   85 YLHLPPEIVPASLQRVRRPAS 105
Cdd:COG5045     79 YLVLPDEGVPSTEAPAVSPTQ 99
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
1114-1231 2.70e-29

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: 115.24  E-value: 2.70e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1114 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLPREKGR--MRFHKLQNVQIAL 1191
Cdd:cd21311     14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGK------------KFPKFNKRptFRSQKLENVSVAL 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2496167637 1192 DFLRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQVS 1231
Cdd:cd21311     82 KFLEEDEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
1115-1230 5.97e-29

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


Pssm-ID: 409081  Cd Length: 107  Bit Score: 113.57  E-value: 5.97e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1115 VQKKTFTKWVNKHLIKSQR-HVTDLYEDLRDGHNLISLLEVLSGDTLlserdvarsvrlPREKGRMRFHKLQNVQIALDF 1193
Cdd:cd21232      2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSL------------PKERGSTRVHALNNVNRVLQV 69
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2496167637 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21232     70 LHQNNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
1250-1351 7.26e-29

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: 113.13  E-value: 7.26e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1250 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED 1328
Cdd:cd21234      2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
                           90       100
                   ....*....|....*....|...
gi 2496167637 1329 VDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21234     82 VAVQLPDKKSIIMYLTSLFEVLP 104
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
1252-1347 2.20e-28

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: 111.67  E-value: 2.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1252 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED-VD 1330
Cdd:cd21253      6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
                           90
                   ....*....|....*..
gi 2496167637 1331 VPHPDEKSIITYVSSLY 1347
Cdd:cd21253     86 LKVPDKLSILTYVSQYY 102
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
1114-1228 2.42e-28

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: 111.80  E-value: 2.42e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1114 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlserdvarsVRLPREKGRMRFHKLQNVQIALDF 1193
Cdd:cd21183      3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPL---------KRSYNRRPAFQQHYLENVSTALKF 73
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2496167637 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 1228
Cdd:cd21183     74 IEADHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
1234-1349 1.06e-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: 110.56  E-value: 1.06e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1234 ISDIQVngqsEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNV 1313
Cdd:cd21287      1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2496167637 1314 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21287     77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
1233-1349 2.14e-27

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: 109.79  E-value: 2.14e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1233 SISDIQVngqsEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFN 1312
Cdd:cd21290      3 AIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFE 78
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2496167637 1313 VAEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21290     79 VAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
1114-1228 7.55e-26

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


Pssm-ID: 409077  Cd Length: 108  Bit Score: 104.88  E-value: 7.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1114 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSgdtllsERDVARSVRlprEKGRMRFHKLQNVQIALDF 1193
Cdd:cd21228      3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLS------QKRMYKKYN---KRPTFRQMKLENVSVALEF 73
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2496167637 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 1228
Cdd:cd21228     74 LERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
1246-1352 1.05e-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: 104.29  E-value: 1.05e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1246 MSAKEKLLLWSQRMTDGY-QGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVY--RQTNLENLEQAFNVAEKDLGVTR 1322
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2496167637 1323 -LLDPEDVDvpHPDEKSIITYVSSLYDAMPR 1352
Cdd:pfam00307   81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
1250-1349 1.08e-25

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: 104.29  E-value: 1.08e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1250 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED- 1328
Cdd:cd22198      3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
                           90       100
                   ....*....|....*....|.
gi 2496167637 1329 VDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd22198     83 ASLAVPDKLSMVSYLSQFYEA 103
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
1234-1349 1.24e-25

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: 104.81  E-value: 1.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1234 ISDIQVngqsEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNV 1313
Cdd:cd21289      1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2496167637 1314 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21289     77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
1114-1231 1.89e-25

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: 104.34  E-value: 1.89e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1114 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvaRSVRLPREKGRMRFHKLQNVQIALDF 1193
Cdd:cd21310     15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQK---------KMYRKYHPRPNFRQMKLENVSVALEF 85
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2496167637 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQVS 1231
Cdd:cd21310     86 LDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
1247-1347 1.99e-24

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: 100.58  E-value: 1.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 1326
Cdd:cd21198      1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
                           90       100
                   ....*....|....*....|....
gi 2496167637 1327 EDV---DVphPDEKSIITYVSSLY 1347
Cdd:cd21198     80 ADMvllSV--PDKLSVMTYLHQIR 101
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
1880-1946 2.10e-24

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 98.87  E-value: 2.10e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2496167637 1880 QLKPRNptTPIKGNLPVQAVCDFKQVEITVHKGDECALLNNSQPSKWKVMNRSGSEAVVPSVCFLVP 1946
Cdd:pfam17902    1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
1250-1350 2.24e-24

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


Pssm-ID: 409075  Cd Length: 103  Bit Score: 100.23  E-value: 2.24e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1250 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPEDV 1329
Cdd:cd21226      3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
                           90       100
                   ....*....|....*....|.
gi 2496167637 1330 DVPHPDEKSIITYVSSLYDAM 1350
Cdd:cd21226     83 MTGNPDERSIVLYTSLFYHAF 103
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
1234-1349 2.86e-24

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: 100.92  E-value: 2.86e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1234 ISDIQVngqsEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNV 1313
Cdd:cd21288      1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2496167637 1314 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21288     77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
1118-1227 3.95e-24

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 99.70  E-value: 3.95e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  1118 KTFTKWVNKHLIKS-QRHVTDLYEDLRDGHNLISLLEVLSGDTLlSERDVARSvrlprekgRMRFHKLQNVQIALDFLRH 1196
Cdd:smart00033    1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLV-DKKKVAAS--------LSRFKKIENINLALSFAEK 71
                            90       100       110
                    ....*....|....*....|....*....|.
gi 2496167637  1197 RQVKLVNIRNDDIADGnPKLTLGLIWTIILH 1227
Cdd:smart00033   72 LGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
1252-1347 7.41e-24

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: 98.76  E-value: 7.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1252 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED-VD 1330
Cdd:cd21197      5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
                           90
                   ....*....|....*..
gi 2496167637 1331 VPHPDEKSIITYVSSLY 1347
Cdd:cd21197     85 MHVPDRLSIITYVSQYY 101
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
1096-1230 1.62e-23

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


Pssm-ID: 409096  Cd Length: 125  Bit Score: 98.68  E-value: 1.62e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1096 LGEPEEKTWPNFIEDERDRVQKKTFTKWVNKHLIKSQRHV--TDLYEDLRDGHNLISLLEVLSGDtllserdvarsvRLP 1173
Cdd:cd21247      1 MDTEYEKGHIRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGE------------QLP 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2496167637 1174 R-EKGRMRFHKLQNVQIALDFLRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQV 1230
Cdd:cd21247     69 RpSRGKMRVHFLENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
1248-1351 2.03e-23

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: 97.55  E-value: 2.03e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1248 AKEKLLLWSQRMTDGYqGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPE 1327
Cdd:cd21245      4 AIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPE 82
                           90       100
                   ....*....|....*....|....
gi 2496167637 1328 DVDVPHPDEKSIITYVSSLYDAMP 1351
Cdd:cd21245     83 DVMVDSPDEQSIMTYVAQFLEHFP 106
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
1115-1229 1.28e-22

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 95.43  E-value: 1.28e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1115 VQKKTFTKWVNKHLIKSQRH--VTDLYEDLRDGHNLISLLEVLSGDtLLSERDVARSvrlprekgrmRFHKLQNVQIALD 1192
Cdd:pfam00307    2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPG-LVDKKKLNKS----------EFDKLENINLALD 70
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2496167637 1193 FLRHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 1229
Cdd:pfam00307   71 VAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
1247-1347 1.79e-21

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


Pssm-ID: 409049  Cd Length: 107  Bit Score: 92.02  E-value: 1.79e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21200      1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
                           90       100
                   ....*....|....*....|...
gi 2496167637 1327 EDVDV--PHPDEKSIITYVSSLY 1347
Cdd:cd21200     81 EDMVRmgNRPDWKCVFTYVQSLY 103
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
1114-1234 3.17e-21

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: 92.45  E-value: 3.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1114 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvaRSVRLPREKGRMRFHKLQNVQIALDF 1193
Cdd:cd21309     16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQK---------RMYRKYHQRPTFRQMQLENVSVALEF 86
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2496167637 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQVSSSI 1234
Cdd:cd21309     87 LDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSISMPV 127
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
1114-1231 1.16e-20

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


Pssm-ID: 409157  Cd Length: 129  Bit Score: 90.53  E-value: 1.16e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1114 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLLserdvarsvRLPREKGRMRFHKLQNVQIALDF 1193
Cdd:cd21308     19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMH---------RKHNQRPTFRQMQLENVSVALEF 89
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2496167637 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQVS 1231
Cdd:cd21308     90 LDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
1248-1347 1.89e-20

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: 89.16  E-value: 1.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1248 AKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPE 1327
Cdd:cd21252      1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
                           90       100
                   ....*....|....*....|.
gi 2496167637 1328 D-VDVPHPDEKSIITYVSSLY 1347
Cdd:cd21252     81 DmVSMKVPDCLSIMTYVSQYY 101
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
1251-1348 5.84e-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: 88.17  E-value: 5.84e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1251 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD-PEDV 1329
Cdd:cd21195      8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
                           90
                   ....*....|....*....
gi 2496167637 1330 DVPHPDEKSIITYVSSLYD 1348
Cdd:cd21195     88 SAQEPDKLSMVMYLSKFYE 106
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
1247-1346 8.93e-20

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: 87.15  E-value: 8.93e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 1326
Cdd:cd21255      1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
                           90       100
                   ....*....|....*....|.
gi 2496167637 1327 ED-VDVPHPDEKSIITYVSSL 1346
Cdd:cd21255     80 ADmVLLPIPDKLIVMTYLCQL 100
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
1250-1346 2.35e-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: 85.83  E-value: 2.35e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  1250 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTN----LENLEQAFNVAEKDLGVTRLLD 1325
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 2496167637  1326 PEDVDVPHPDEKSIITYVSSL 1346
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
1247-1345 3.49e-19

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


Pssm-ID: 409033  Cd Length: 103  Bit Score: 85.37  E-value: 3.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTDGYqgiRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVY-RQTNLENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21184      1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
                           90       100
                   ....*....|....*....|
gi 2496167637 1326 PEDVDVPHPDEKSIITYVSS 1345
Cdd:cd21184     78 PEDMVSPNVDELSVMTYLSY 97
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
1247-1346 2.09e-18

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


Pssm-ID: 409103  Cd Length: 107  Bit Score: 83.36  E-value: 2.09e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 1326
Cdd:cd21254      1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
                           90       100
                   ....*....|....*....|.
gi 2496167637 1327 ED-VDVPHPDEKSIITYVSSL 1346
Cdd:cd21254     80 SDmVLLAVPDKLTVMTYLYQI 100
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
1243-1348 4.79e-18

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


Pssm-ID: 409100 [Multi-domain]  Cd Length: 111  Bit Score: 82.69  E-value: 4.79e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1243 SEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTR 1322
Cdd:cd21251      1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
                           90       100
                   ....*....|....*....|....*..
gi 2496167637 1323 LLDPEDV-DVPHPDEKSIITYVSSLYD 1348
Cdd:cd21251     81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
1247-1347 1.09e-17

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: 81.58  E-value: 1.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21259      1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80
                           90       100
                   ....*....|....*....|..
gi 2496167637 1327 ED-VDVPHPDEKSIITYVSSLY 1347
Cdd:cd21259     81 EDmVRMREPDWKCVYTYIQEFY 102
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
1247-1348 2.18e-17

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: 80.39  E-value: 2.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21261      1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEV 80
                           90       100
                   ....*....|....*....|....
gi 2496167637 1327 EDVDV--PHPDEKSIITYVSSLYD 1348
Cdd:cd21261     81 EDMMVmgRKPDPMCVFTYVQSLYN 104
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
1247-1352 5.07e-17

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


Pssm-ID: 409107  Cd Length: 111  Bit Score: 79.71  E-value: 5.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21258      1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEV 80
                           90       100
                   ....*....|....*....|....*...
gi 2496167637 1327 EDVDV--PHPDEKSIITYVSSLYDAMPR 1352
Cdd:cd21258     81 EDMMImgKKPDSKCVFTYVQSLYNHLRR 108
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
1116-1228 6.53e-17

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


Pssm-ID: 409061  Cd Length: 105  Bit Score: 79.16  E-value: 6.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1116 QKKTFTKWVNKHLIKS--QRHVTDLYEDLRDGHNLISLLEVLSGDTllserdVARSVRLPRekgrMRFHKLQNVQIALDF 1193
Cdd:cd21212      1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEK------VPGIHSRPK----TRAQKLENIQACLQF 70
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2496167637 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 1228
Cdd:cd21212     71 LAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1705-1891 8.32e-17

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 82.49  E-value: 8.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1705 LHAFVSAATKELMWLNDKEEEEVNYDWSDKNTNMTVKKENYSGLMRELELREKKVNDIQAMGDRLVKDGHPGKKTVEAFT 1784
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1785 AALQTQWSWILQLCCCVEAHLKENTAYYQFFTDVKDAQDKMKKMQENMKkkySCDRTTTATRLEDLLQDAVDEKEQLNEF 1864
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180
                   ....*....|....*....|....*..
gi 2496167637 1865 KTQVAGLNKRAKSIIQLKPRNPTTPIK 1891
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIE 185
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
1117-1226 1.25e-16

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 78.15  E-value: 1.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1117 KKTFTKWVNKHL-IKSQRHVTDLYEDLRDGHNLISLLEVLSGDtllserdvarSVRLPREKGRMRFHKLQNVQIALDFLR 1195
Cdd:cd00014      1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPG----------SIPKINKKPKSPFKKRENINLFLNACK 70
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2496167637 1196 HRQV-KLVNIRNDDI-ADGNPKLTLGLIWTIIL 1226
Cdd:cd00014     71 KLGLpELDLFEPEDLyEKGNLKKVLGTLWALAL 103
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
1249-1350 2.89e-16

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: 77.82  E-value: 2.89e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1249 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED 1328
Cdd:cd21260      3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
                           90       100
                   ....*....|....*....|...
gi 2496167637 1329 -VDVPHPDEKSIITYVSSLYDAM 1350
Cdd:cd21260     83 mVRMSVPDSKCVYTYIQELYRSL 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1609-1798 3.79e-16

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 80.57  E-value: 3.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1609 LRYVQDLLEWVQENQRRIDEAEWGSDLPSVESQLGSHRGLHQTVEDFRSKIERAKADENQLspISRGKY-----REYLGR 1683
Cdd:cd00176      6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQL--IEEGHPdaeeiQERLEE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1684 LDLQYAKLLNSSKSRLRNLD---SLHAFVSAATKELMWLNDKEEEEVNYDWSDKNTNMTVKKENYSGLMRELELREKKVN 1760
Cdd:cd00176     84 LNQRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLK 163
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2496167637 1761 DIQAMGDRLVKDGHPGK-KTVEAFTAALQTQWSWILQLC 1798
Cdd:cd00176    164 SLNELAEELLEEGHPDAdEEIEEKLEELNERWEELLELA 202
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
1251-1348 5.87e-16

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


Pssm-ID: 409099 [Multi-domain]  Cd Length: 110  Bit Score: 76.46  E-value: 5.87e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1251 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD-PEDV 1329
Cdd:cd21250      8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
                           90
                   ....*....|....*....
gi 2496167637 1330 DVPHPDEKSIITYVSSLYD 1348
Cdd:cd21250     88 SAEEPDKLSMVMYLSKFYE 106
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3996-4034 8.80e-16

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 73.52  E-value: 8.80e-16
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3996 LLEAQIATGGIIDPEESHRLPVEVAYKRGFFDEEMNEIL 4034
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
1247-1347 4.65e-15

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


Pssm-ID: 409048  Cd Length: 112  Bit Score: 73.93  E-value: 4.65e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEkDLGVTRLLDP 1326
Cdd:cd21199      8 SKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTI 86
                           90       100
                   ....*....|....*....|..
gi 2496167637 1327 ED-VDVPHPDEKSIITYVSSLY 1347
Cdd:cd21199     87 DEmVSMERPDWQSVMSYVTAIY 108
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
1116-1228 1.69e-14

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


Pssm-ID: 409062  Cd Length: 107  Bit Score: 72.33  E-value: 1.69e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1116 QKKTFTKWVNKHLIK--SQRHVTDLYEDLRDGHNLISLLEVLSGDTLlSERDVArsvrlPREKGRMRfhklQNVQIALDF 1193
Cdd:cd21213      1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKL-PGIDWN-----PTTDAERK----ENVEKVLQF 70
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2496167637 1194 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 1228
Cdd:cd21213     71 MASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3350-3388 1.90e-14

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 69.66  E-value: 1.90e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3350 LLEAQAASGFIVDPVKNQCLSVDEAVKSGVVGPELHEKL 3388
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
1247-1347 3.84e-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: 71.64  E-value: 3.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 1326
Cdd:cd21256     14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGIKSTLDI 92
                           90       100
                   ....*....|....*....|..
gi 2496167637 1327 ED-VDVPHPDEKSIITYVSSLY 1347
Cdd:cd21256     93 NEmVRTERPDWQSVMTYVTAIY 114
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3682-3720 5.95e-14

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 68.51  E-value: 5.95e-14
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3682 LLETQAATGFIIDPIKNETLTVDEAVRKGVVGPEIHDKL 3720
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2692-2729 8.13e-14

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 68.12  E-value: 8.13e-14
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2496167637 2692 LLEAQAATGYMLDPINNHKLSVNEAVKEGLIGPELHNK 2729
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
1113-1224 1.04e-13

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


Pssm-ID: 409074  Cd Length: 111  Bit Score: 70.25  E-value: 1.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1113 DRVQKKTFTKWVNKHLIKSQ-RHVTDLYEDLRDGHNLISLLEVLSGDTLLSERDVARSVRLPRekgrmrfhkLQNVQIAL 1191
Cdd:cd21225      2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDLEPKNRIQM---------IQNLHLAM 72
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2496167637 1192 DFLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTI 1224
Cdd:cd21225     73 LFIEEDlKIRVQGIGAEDFVDNNKKLILGLLWTL 106
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
1134-1225 1.45e-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: 69.93  E-value: 1.45e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1134 HVTDLYEDLRDGHNLISLLEVLSGDTLLSERDVARSVRLPRekgrmrfhKLQNVQIALDFLRHRQV----KLVNIRNDDI 1209
Cdd:cd21223     25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVPAISRLQ--------KLHNVEVALKALKEAGVlrggDGGGITAKDI 96
                           90
                   ....*....|....*.
gi 2496167637 1210 ADGNPKLTLGLIWTII 1225
Cdd:cd21223     97 VDGHREKTLALLWRII 112
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
1109-1227 1.59e-13

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: 69.62  E-value: 1.59e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1109 EDERDrvqKKTFTKWVNKHLIKSQRHvtDLYEDLRDGhnlISLLEVLsgDTLLSERDVARSVRLPREKGRMRfhKLQNVQ 1188
Cdd:cd21219      1 EGSRE---ERAFRMWLNSLGLDPLIN--NLYEDLRDG---LVLLQVL--DKIQPGCVNWKKVNKPKPLNKFK--KVENCN 68
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2496167637 1189 IALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 1227
Cdd:cd21219     69 YAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
1247-1347 1.87e-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: 1.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 1326
Cdd:cd21257      8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VGIKPSLEL 86
                           90       100
                   ....*....|....*....|..
gi 2496167637 1327 ED-VDVPHPDEKSIITYVSSLY 1347
Cdd:cd21257     87 SEmMYTDRPDWQSVMQYVAQIY 108
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
1247-1344 4.46e-13

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: 68.18  E-value: 4.46e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTN-LENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21230      1 TPKQRLLGWIQ---NKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLIT 77
                           90
                   ....*....|....*....
gi 2496167637 1326 PEDVDVPHPDEKSIITYVS 1344
Cdd:cd21230     78 PEEIINPNVDEMSVMTYLS 96
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
1249-1348 8.01e-13

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: 67.36  E-value: 8.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1249 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMgKVYRQTN----LENLEQAFNVAEK-DLGVTRL 1323
Cdd:cd00014      1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPK-INKKPKSpfkkRENINLFLNACKKlGLPELDL 79
                           90       100
                   ....*....|....*....|....*
gi 2496167637 1324 LDPEDVdVPHPDEKSIITYVSSLYD 1348
Cdd:cd00014     80 FEPEDL-YEKGNLKKVLGTLWALAL 103
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
4270-4308 9.99e-13

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 65.04  E-value: 9.99e-13
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 4270 LLEAQACTGGIIDPTTGERFTVTVATEKGLVDKAMVDRL 4308
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
1108-1224 1.48e-12

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


Pssm-ID: 409147  Cd Length: 117  Bit Score: 66.88  E-value: 1.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1108 IEDERDrvqKKTFTKWVNKHLIKSqrHVTDLYEDLRDGHNLISLLEVLSGDTLLSERdvarsVRLPREKGRMRFHKLQNV 1187
Cdd:cd21298      2 IEETRE---EKTYRNWMNSLGVNP--FVNHLYSDLRDGLVLLQLYDKIKPGVVDWSR-----VNKPFKKLGANMKKIENC 71
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2496167637 1188 QIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTI 1224
Cdd:cd21298     72 NYAVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQL 108
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3020-3057 2.14e-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: 2.14e-12
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2496167637 3020 LEAQAGTGYVVDPVHNQHYTVDEAVKAGVVGPELHEKL 3057
Cdd:pfam00681    2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
1111-1222 5.71e-12

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: 65.52  E-value: 5.71e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1111 ERDRvQKKTFTKWVNKhlIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlserDVARSVRLPREKGRMRFHKLQNVQIA 1190
Cdd:cd21300      4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSV----NWKKVNKAPASAEISRFKAVENTNYA 76
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2496167637 1191 LDFLRHRQVKLVNIRNDDIADGNPKLTLGLIW 1222
Cdd:cd21300     77 VELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
1249-1344 7.10e-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: 64.71  E-value: 7.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1249 KEKLLLWSQRMtdgYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLI-DMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPE 1327
Cdd:cd21229      5 KKLMLAWLQAV---LPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
                           90
                   ....*....|....*..
gi 2496167637 1328 DVDVPHPDEKSIITYVS 1344
Cdd:cd21229     82 DLSSPHLDELSGMTYLS 98
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
1247-1349 1.18e-11

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: 64.30  E-value: 1.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 1326
Cdd:cd21196      3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSA 82
                           90       100
                   ....*....|....*....|...
gi 2496167637 1327 EDVdVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21196     83 QAV-VAGSDPLGLIAYLSHFHSA 104
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3920-3958 6.53e-11

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 59.65  E-value: 6.53e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3920 LLEAQAATGYIIDPIKSLKLTVNEAVSMGTVGPEFKDKL 3958
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
2768-2805 6.86e-11

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 59.65  E-value: 6.86e-11
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2496167637 2768 VLEAQLATGGIIDPLNSHRVPNEIAYKQGQYDAEMNKI 2805
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2263-2573 9.36e-11

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: 68.54  E-value: 9.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2263 ERDAELDQHRQHLSSLQDrwkavftQIDLRQRELDQLGRQLgyyresydwlirwiADAKQRQENIQAVPITDSKTLKEQL 2342
Cdd:TIGR02168  674 ERRREIEELEEKIEELEE-------KIAELEKALAELRKEL--------------EELEEELEQLRKELEELSRQISALR 732
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2343 AKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVayKAQVEPLTSPLKKTKLDSASDNIIQEYVTLRTRYSELMT 2422
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE--EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2423 LTSQYIKFITDTQRRLEDEEmadAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLEsQFEEEIKKAKALKDEQD 2502
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLE---RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESELEALLNERASLE 886
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2496167637 2503 RQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERkRLEQERVLADENQ-KLREKLQQMEEAQK 2573
Cdd:TIGR02168  887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL-RLEGLEVRIDNLQeRLSEEYSLTLEEAE 957
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3426-3464 1.14e-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: 1.14e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3426 LLEAQMVSGGIIDPVNSHRVPNDTAYQKNILSKEVAKTL 3464
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3759-3796 1.50e-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: 1.50e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2496167637 3759 LEAQTSTGGIIDPEFQFHLPADVAIQRGYINKETNEKL 3796
Cdd:pfam00681    2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2336-2579 7.65e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.73  E-value: 7.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2336 KTLKEQ---------LAKEKKLLEeIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEpltspLKKTKLDSASDNI 2406
Cdd:COG1196    203 EPLERQaekaeryreLKEELKELE-AELLLLKLRELEAELEELEAELEELEAELEELEAELA-----ELEAELEELRLEL 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2407 IQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQ 2486
Cdd:COG1196    277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2487 fEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQEL--ERKRLEQERV-LADENQKLRE 2563
Cdd:COG1196    357 -EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALleRLERLEEELEeLEEALAELEE 435
                          250
                   ....*....|....*.
gi 2496167637 2564 KLQQMEEAQKSTLITE 2579
Cdd:COG1196    436 EEEEEEEALEEAAEEE 451
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2339-2583 9.41e-10

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: 65.46  E-value: 9.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2339 KEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDY-ELQLVAYKAQVEPLtsplkKTKLDsASDNIIQEYVTLRTRY 2417
Cdd:TIGR02168  185 RENLDRLEDILNELERQLKSLERQAEKAERYKELKAELrELELALLVLRLEEL-----REELE-ELQEELKEAEEELEEL 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2418 SELMTLTSQYIkfitdTQRRLEDEEMadaqqkqiEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLEsQFEEEIKKAKAL 2497
Cdd:TIGR02168  259 TAELQELEEKL-----EELRLEVSEL--------EEEIEELQKELYALANEISRLEQQKQILRERLA-NLERQLEELEAQ 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2498 KDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQKSTLI 2577
Cdd:TIGR02168  325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404

                   ....*.
gi 2496167637 2578 TEKHVT 2583
Cdd:TIGR02168  405 LEARLE 410
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
4346-4384 1.41e-09

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 55.80  E-value: 1.41e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 4346 FLEVQYLTGGLIEPEAQGRVSLDESIRKGTIDARTAQKL 4384
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
2101-2579 1.43e-09

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 64.66  E-value: 1.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2101 IRKPVEKEPLKECIQKTAE-QAKVQVELEGLKKDLDKVSTKTQDILNSpqpsatapVLRSELELTVQKMDHAYMLSsvyl 2179
Cdd:TIGR04523  120 NKLEVELNKLEKQKKENKKnIDKFLTEIKKKEKELEKLNNKYNDLKKQ--------KEELENELNLLEKEKLNIQK---- 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2180 eKLKTVEMVIRNTQGAEGVLKQYENCLREVHTVPNDVKE-VETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAVSDKMS 2258
Cdd:TIGR04523  188 -NIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKqNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2259 RVHSERDAELDQHRQHLSSL-------------------QDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWLIRWIAD 2319
Cdd:TIGR04523  267 KQLSEKQKELEQNNKKIKELekqlnqlkseisdlnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2320 AKQRQENIQavpiTDSKTLKEQLAKEKKLLEEIEK-NKDKVDECQKYAKAyidiIKDYELQLVAYKAQVEPLTSPLKK-- 2396
Cdd:TIGR04523  347 LKKELTNSE----SENSEKQRELEEKQNEIEKLKKeNQSYKQEIKNLESQ----INDLESKIQNQEKLNQQKDEQIKKlq 418
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2397 -----------------TKLDSASDNIIQEYVTLRTRYSELMTLTS---QYIKFIT-----------DTQRRLEDEE--- 2442
Cdd:TIGR04523  419 qekellekeierlketiIKNNSEIKDLTNQDSVKELIIKNLDNTREsleTQLKVLSrsinkikqnleQKQKELKSKEkel 498
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2443 -MADAQQKQIEREMTVL--QQTFLTEKEMLLKKEKL-IEDEKKKLESQFEE---EIKKA--KALKDEQDRQRQQMEEEKL 2513
Cdd:TIGR04523  499 kKLNEEKKELEEKVKDLtkKISSLKEKIEKLESEKKeKESKISDLEDELNKddfELKKEnlEKEIDEKNKEIEELKQTQK 578
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2496167637 2514 KLKATMDAA--LNKQKEAEKDILNKQKEMQELERKRLEQERVLAD-ENQKLREKLQQMEEAqKSTLITE 2579
Cdd:TIGR04523  579 SLKKKQEEKqeLIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKkENEKLSSIIKNIKSK-KNKLKQE 646
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2045-2573 1.83e-09

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 64.61  E-value: 1.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2045 YTKSTQHFDSLLRSMEKGLVVRHKGQQDETLCKNYISEVKDLRLRIEDCEARTVARIRKPVEKEPLKECIQKTAEQAKVQ 2124
Cdd:pfam02463  379 KKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQEL 458
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2125 VELEgLKKDLDKVSTKTQDILNSPQpsatapVLRSELELTVQKMDHAYMLSSVYLEKLKTVEMVIRNT-----------Q 2193
Cdd:pfam02463  459 KLLK-DELELKKSEDLLKETQLVKL------QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggriisahgrL 531
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2194 GAEGVLKQYENCLREVHTVPNDVKEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAVSDKMSRVHSERDAELDQHRQ 2273
Cdd:pfam02463  532 GDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2274 HLSSLQDRWKAVFTQIDLRQRELDQLGRQLGyyrESYDWLIRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIE 2353
Cdd:pfam02463  612 TLEADEDDKRAKVVEGILKDTELTKLKESAK---AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE 688
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2354 KNKDKVDECQKYAKAYIDIIKdyELQLVAYKAQVEpltspLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSqyikfITD 2433
Cdd:pfam02463  689 LAKEEILRRQLEIKKKEQREK--EELKKLKLEAEE-----LLADRVQEAQDKINEELKLLKQKIDEEEEEEE-----KSR 756
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2434 TQRRLEDEEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDrQRQQMEEEKL 2513
Cdd:pfam02463  757 LKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIE-QEEKIKEEEL 835
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2496167637 2514 KLKATMDAALNKQKEA--EKDILNKQKEMQELERKRLEQERVLADEnQKLREKLQQMEEAQK 2573
Cdd:pfam02463  836 EELALELKEEQKLEKLaeEELERLEEEITKEELLQELLLKEEELEE-QKLKDELESKEEKEK 896
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3095-3133 2.20e-09

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 55.41  E-value: 2.20e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3095 LLDAQMTTGGIIDPVKSHRVPHDVACNRSYFDDEMKQHL 3133
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2348-2580 2.29e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.19  E-value: 2.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2348 LLEEIEKNKDKV-DECQKyAKAYIDI---IKDYELQLVAYK-----AQVEpltspLKKTKLDSASDNIIQEYVTLRTRYS 2418
Cdd:COG1196    194 ILGELERQLEPLeRQAEK-AERYRELkeeLKELEAELLLLKlreleAELE-----ELEAELEELEAELEELEAELAELEA 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2419 ELMTLTSQYIKFITDTQRRLEDEEMADAQQKQIEREMTV-------LQQTFLTEKEMLLKKEKLIEDEKKKLESQfEEEI 2491
Cdd:COG1196    268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARleerrreLEERLEELEEELAELEEELEELEEELEEL-EEEL 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2492 KKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEA 2571
Cdd:COG1196    347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426

                   ....*....
gi 2496167637 2572 QKSTLITEK 2580
Cdd:COG1196    427 EEALAELEE 435
PLEC smart00250
Plectin repeat;
4268-4305 2.65e-09

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 55.18  E-value: 2.65e-09
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2496167637  4268 QRLLEAQACTGGIIDPTTGERFTVTVATEKGLVDKAMV 4305
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PTZ00121 PTZ00121
MAEBL; Provisional
2094-2604 3.63e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.62  E-value: 3.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2094 EARTVARIRKPVEKEPLKEcIQKTAEQAKVQVEL----EGLKKDLDKVSTKTQDILNSPQPS-ATAPVLRSELELTVQKM 2168
Cdd:PTZ00121  1288 EKKKADEAKKAEEKKKADE-AKKKAEEAKKADEAkkkaEEAKKKADAAKKKAEEAKKAAEAAkAEAEAAADEAEAAEEKA 1366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2169 DHAYMLSSVYLEKLKTVEMVIRNTQGAEGVLKQYEnclrEVHTVPNDVKEVETYRTNLKKMRAEAEAEQPVfdsleEELK 2248
Cdd:PTZ00121  1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE----EDKKKADELKKAAAAKKKADEAKKKAEEKKKA-----DEAK 1437
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2249 KASAVSDKMSRVhsERDAELDQHRQHLSSLQDRwkavftqidlrQRELDQLGRQLGYYRESyDWLIRWIADAKQRQENIQ 2328
Cdd:PTZ00121  1438 KKAEEAKKADEA--KKKAEEAKKAEEAKKKAEE-----------AKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAK 1503
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2329 AVPITDSKTLKEQLAKEKKLLEEIEK--NKDKVDECQKY--AKAYIDIIKDYELQLVAYKAQVEPLTSPLKKTKLDSASD 2404
Cdd:PTZ00121  1504 KAAEAKKKADEAKKAEEAKKADEAKKaeEAKKADEAKKAeeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2405 NIIQEyvTLRTRYSELMTLTSQYIKFITDTQRRLEDEEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDE----- 2479
Cdd:PTZ00121  1584 EEAKK--AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEeenki 1661
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2480 -KKKLESQFEEEIKKAKAL-KDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADE 2557
Cdd:PTZ00121  1662 kAAEEAKKAEEDKKKAEEAkKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 2496167637 2558 NQKLREKLQQMEEAQKSTLITEKHVTVVETVLNGQNAGDVLDGVEKR 2604
Cdd:PTZ00121  1742 DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
1117-1225 4.92e-09

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


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 56.81  E-value: 4.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1117 KKTFTKWVNKHLIKSQ---------RHVTDLYEDLRDGHNLISLLEVLSGDTLlSERdvarsvRLPREKGRMRFHKLQNV 1187
Cdd:cd21217      3 KEAFVEHINSLLADDPdlkhllpidPDGDDLFEALRDGVLLCKLINKIVPGTI-DER------KLNKKKPKNIFEATENL 75
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2496167637 1188 QIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1225
Cdd:cd21217     76 NLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
2081-2579 5.30e-09

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: 62.82  E-value: 5.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2081 SEVKDLRLRIEDCEARTVARIRK-PVEKEPLKECIQKtaeQAKVQVELEGLKKDLDKvSTKTQDILNSPQPSATAPV--L 2157
Cdd:pfam05483  254 NKMKDLTFLLEESRDKANQLEEKtKLQDENLKELIEK---KDHLTKELEDIKMSLQR-SMSTQKALEEDLQIATKTIcqL 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2158 RSELELTVQKMDHAYMLSSVYLEKLKTVEMVIrntqgaegvlkqyENCLR-EVHTVPNDVKEVETYRTNLKKMRAEAEAE 2236
Cdd:pfam05483  330 TEEKEAQMEELNKAKAAHSFVVTEFEATTCSL-------------EELLRtEQQRLEKNEDQLKIITMELQKKSSELEEM 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2237 QPVFDSLEEELkkasavsDKMSRVHSERDAELDQHRQH---LSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWL 2313
Cdd:pfam05483  397 TKFKNNKEVEL-------EELKKILAEDEKLLDEKKQFekiAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2314 IRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEE-------IEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQ 2386
Cdd:pfam05483  470 LKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEasdmtleLKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDE 549
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2387 VEPLTSPLK------KTKLDSASDNIIQEYVTLRTRYSELMTLT-------------SQYIKFITDTQRRLEDEEMADAQ 2447
Cdd:pfam05483  550 LESVREEFIqkgdevKCKLDKSEENARSIEYEVLKKEKQMKILEnkcnnlkkqienkNKNIEELHQENKALKKKGSAENK 629
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2448 Q--------KQIEREMTVLQQTFlteKEMLLKKEKLIEDeKKKLESQFEEEIKKAKALKDEqdrqrqqmeeeklklkatm 2519
Cdd:pfam05483  630 QlnayeikvNKLELELASAKQKF---EEIIDNYQKEIED-KKISEEKLLEEVEKAKAIADE------------------- 686
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2496167637 2520 daALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQK---LREKLQQMEEAQKSTLITE 2579
Cdd:pfam05483  687 --AVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSelgLYKNKEQEQSSAKAALEIE 747
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2212-2386 7.56e-09

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 59.00  E-value: 7.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2212 VPNDVKEVETYRTNLKKMRAEAEAEQPVFDSLEEElkkasavSDKMSRVHSErdaELDQHRQHLSSLQDRWKAVFTQIDL 2291
Cdd:cd00176     28 YGDDLESVEALLKKHEALEAELAAHEERVEALNEL-------GEQLIEEGHP---DAEEIQERLEELNQRWEELRELAEE 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2292 RQRELDQLGRQLGYYRESYDwLIRWIADAKQRQENIQavPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYID 2371
Cdd:cd00176     98 RRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLE 174
                          170
                   ....*....|....*
gi 2496167637 2372 IIKDYELQLVAYKAQ 2386
Cdd:cd00176    175 EGHPDADEEIEEKLE 189
SPEC smart00150
Spectrin repeats;
1706-1798 8.72e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 55.80  E-value: 8.72e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  1706 HAFVSAATKELMWLNDKEEEEVNYDWSDKNTNMTVKKENYSGLMRELELREKKVNDIQAMGDRLVKDGHPGKKTVEAFTA 1785
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90
                    ....*....|...
gi 2496167637  1786 ALQTQWSWILQLC 1798
Cdd:smart00150   81 ELNERWEELKELA 93
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
2091-2571 1.02e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 62.06  E-value: 1.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2091 EDCEARTvARIRKPVEKEPLKECIQKT-AEQAKVQVELEgLKKDLDKvSTKTQDILNSpqpsATAPVLRSELE---LTVQ 2166
Cdd:pfam15921  357 ELTEART-ERDQFSQESGNLDDQLQKLlADLHKREKELS-LEKEQNK-RLWDRDTGNS----ITIDHLRRELDdrnMEVQ 429
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2167 KMDHayMLSSVYLEKLKTVEMVIRNTQGAEGVLKQYENCLREVHTVPNDVKEVETYRTnLKKMRAEAeAEQPVFD---SL 2243
Cdd:pfam15921  430 RLEA--LLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELT-AKKMTLES-SERTVSDltaSL 505
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2244 EEELKKASAVSDKMSRVHSERDAELdQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWLIRWIADAKQR 2323
Cdd:pfam15921  506 QEKERAIEATNAEITKLRSRVDLKL-QELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRT 584
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2324 QENIQavpiTDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIdiiKDYELQLVAYkaqVEPLTSPLKKTK-LDSA 2402
Cdd:pfam15921  585 AGAMQ----VEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV---SDLELEKVKL---VNAGSERLRAVKdIKQE 654
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2403 SDNIIQEYVTLRtrySELMTLTSQYIKFITDTQRRLEDEEMADAQQK-QIEREMTVLQQTFLTEKEMllkkekliedekk 2481
Cdd:pfam15921  655 RDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKmQLKSAQSELEQTRNTLKSM------------- 718
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2482 klESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQEL-----ERKRLEQE-RVLA 2555
Cdd:pfam15921  719 --EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELstvatEKNKMAGElEVLR 796
                          490
                   ....*....|....*.
gi 2496167637 2556 DENQKLREKLQQMEEA 2571
Cdd:pfam15921  797 SQERRLKEKVANMEVA 812
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2327-2579 1.41e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.61  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2327 IQAVPITDSKTLKEQL-AKEKKLL-EEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEplTSPLKKTKLDSASD 2404
Cdd:TIGR02168  207 RQAEKAERYKELKAELrELELALLvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE--ELRLEVSELEEEIE 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2405 NIIQEYVTLRTRYSELmtltSQYIKFITDTQRRLEDeemadaQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLE 2484
Cdd:TIGR02168  285 ELQKELYALANEISRL----EQQKQILRERLANLER------QLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2485 SqFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDI--LNKQKEMQELERKRLEQE-RVLADENQKL 2561
Cdd:TIGR02168  355 S-LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIerLEARLERLEDRRERLQQEiEELLKKLEEA 433
                          250
                   ....*....|....*...
gi 2496167637 2562 REKLQQMEEAQKSTLITE 2579
Cdd:TIGR02168  434 ELKELQAELEELEEELEE 451
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2317-2557 1.67e-08

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: 60.16  E-value: 1.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2317 IADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEPLTSPLKK 2396
Cdd:COG4942     22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2397 TKlDSASDNIIQEYVTlrTRYSELMTLTSQyiKFITDTQRRLED-EEMADAQQKQIERemtvLQQTflteKEMLLKKEKL 2475
Cdd:COG4942    102 QK-EELAELLRALYRL--GRQPPLALLLSP--EDFLDAVRRLQYlKYLAPARREQAEE----LRAD----LAELAALRAE 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2476 IEDEKKKLEsqfeeeikkakALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELER--KRLEQERV 2553
Cdd:COG4942    169 LEAERAELE-----------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAliARLEAEAA 237

                   ....
gi 2496167637 2554 LADE 2557
Cdd:COG4942    238 AAAE 241
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
2123-2583 2.63e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 60.52  E-value: 2.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2123 VQVELEGLKKDldkVSTKTQDILNSPQPSATAPVLRSELELT--VQKMDHAYMLSSVYLEKLKTVE--------MVIRNT 2192
Cdd:pfam15921  243 VEDQLEALKSE---SQNKIELLLQQHQDRIEQLISEHEVEITglTEKASSARSQANSIQSQLEIIQeqarnqnsMYMRQL 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2193 QGAEGVLKQYENCLREVHTVPND-VKEVETYRTNLKKMRAEAEAEQPVFD----SLEEELKKAsavsdkMSRVHsERDAE 2267
Cdd:pfam15921  320 SDLESTVSQLRSELREAKRMYEDkIEELEKQLVLANSELTEARTERDQFSqesgNLDDQLQKL------LADLH-KREKE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2268 LDQHRQHLSSLQDRWKAVFTQIDLRQRELDQlgRQLGYYR----------ESYDWLIRWIADAKQRQENIQAVpitDSKT 2337
Cdd:pfam15921  393 LSLEKEQNKRLWDRDTGNSITIDHLRRELDD--RNMEVQRleallkamksECQGQMERQMAAIQGKNESLEKV---SSLT 467
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2338 LKEQLAKE--KKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVepltsplkkTKLDSASDNIIQEYVTLRT 2415
Cdd:pfam15921  468 AQLESTKEmlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEI---------TKLRSRVDLKLQELQHLKN 538
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2416 RYSELMTLTSQYIKFitdTQRRLEDEEMADAQQKQIEREMTVLQQTFLTEKEMLLKK---EKLIEDEKKklesqfeeEIK 2492
Cdd:pfam15921  539 EGDHLRNVQTECEAL---KLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKaqlEKEINDRRL--------ELQ 607
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2493 KAKALKDEQDRQRQQMEE-------EKLKL--------------KATMDAALNKQKEAEKDI--------------LNKQ 2537
Cdd:pfam15921  608 EFKILKDKKDAKIRELEArvsdlelEKVKLvnagserlravkdiKQERDQLLNEVKTSRNELnslsedyevlkrnfRNKS 687
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2538 KEMQELERKRLEQERVLADENQKLREKLQQME----EAQKSTLITEKHVT 2583
Cdd:pfam15921  688 EEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdgHAMKVAMGMQKQIT 737
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
1242-1344 3.03e-08

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: 54.79  E-value: 3.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1242 QSEDMSAKEKLLLWSQ-RMTDgyqgIRCDNFTTSWRDGKLFNAVIHKNYPRLI-DMGKVYRQTNLENLEQAFNVAEKDLG 1319
Cdd:cd21315     11 DGKGPTPKQRLLGWIQsKVPD----LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLD 86
                           90       100
                   ....*....|....*....|....*
gi 2496167637 1320 VTRLLDPEDVDVPHPDEKSIITYVS 1344
Cdd:cd21315     87 VPQLIKPEEMVNPKVDELSMMTYLS 111
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2077-2571 3.23e-08

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: 60.47  E-value: 3.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2077 KNYISEVKDLRLRIEDCEaRTVARIRKpvEKEPLKECIQKT-AEQAKVQVELEGLKKDLDKVSTKTQDilnspqpsatap 2155
Cdd:TIGR02169  325 AKLEAEIDKLLAEIEELE-REIEEERK--RRDKLTEEYAELkEELEDLRAELEEVDKEFAETRDELKD------------ 389
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2156 vLRSELELTVQKMDHAYMLSSVYLEKLKTVEMVIRNtqgAEGVLKQYENCLREVHTVPNDV-KEVETYRTNLKKMRAEAE 2234
Cdd:TIGR02169  390 -YREKLEKLKREINELKRELDRLQEELQRLSEELAD---LNAAIAGIEAKINELEEEKEDKaLEIKKQEWKLEQLAADLS 465
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2235 AEQPVFDSLEEELKKasaVSDKMSRVHSERDaELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWLI 2314
Cdd:TIGR02169  466 KYEQELYDLKEEYDR---VEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAI 541
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2315 RWIADAKqrqenIQAVPITDSKTLKE--QLAKEKKL--LEEIEKNKDKVDECQKyAKAYIDIIKDYELQLVAYKAQVEP- 2389
Cdd:TIGR02169  542 EVAAGNR-----LNNVVVEDDAVAKEaiELLKRRKAgrATFLPLNKMRDERRDL-SILSEDGVIGFAVDLVEFDPKYEPa 615
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2390 ----LTSPLKKTKLDSASDNIIQ-EYVTLRTRYSE---LMTLTSQYIKFITDTQRRLEDE-EMADAQQKQIEREMTVLQQ 2460
Cdd:TIGR02169  616 fkyvFGDTLVVEDIEAARRLMGKyRMVTLEGELFEksgAMTGGSRAPRGGILFSRSEPAElQRLRERLEGLKRELSSLQS 695
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2461 TFLTEKEMLLKKEKLIEDEKKKLE------SQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDIL 2534
Cdd:TIGR02169  696 ELRRIENRLDELSQELSDASRKIGeiekeiEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 2496167637 2535 NKQKEMQELERkRLEQERV--LADENQKLREKLQQMEEA 2571
Cdd:TIGR02169  776 KLEEALNDLEA-RLSHSRIpeIQAELSKLEEEVSRIEAR 813
PLEC smart00250
Plectin repeat;
3994-4030 3.58e-08

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 52.10  E-value: 3.58e-08
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2496167637  3994 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGFFDEEM 4030
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
1095-1228 4.22e-08

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


Pssm-ID: 409180  Cd Length: 134  Bit Score: 55.01  E-value: 4.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1095 SLGEPEEK--TWpNFIEDERDrvQKKTFTKWVNKHLIKSqrHVTDLYEDLRDGHNLISLLEVLSGDTllserDVARSVRL 1172
Cdd:cd21331      3 ALTKPENQdiDW-TLLEGETR--EERTFRNWMNSLGVNP--HVNHLYGDLQDALVILQLYEKIKVPV-----DWNKVNKP 72
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2496167637 1173 PREKGRMRFHKLQNVQIALDFLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 1228
Cdd:cd21331     73 PYPKLGANMKKLENCNYAVELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRY 129
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
1118-1224 4.51e-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: 53.88  E-value: 4.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1118 KTFTKWVNKHLIKS--QRHVTDLYEDLRDGHNLISLLEVLSGDTLLSERDVarsvrlPREKGRMrfhkLQNVQIALDFLR 1195
Cdd:cd21286      3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGC------PRSQSQM----IENVDVCLSFLA 72
                           90       100
                   ....*....|....*....|....*....
gi 2496167637 1196 HRQVKLVNIRNDDIADGNPKLTLGLIWTI 1224
Cdd:cd21286     73 ARGVNVQGLSAEEIRNGNLKAILGLFFSL 101
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
1108-1228 4.83e-08

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


Pssm-ID: 409071  Cd Length: 121  Bit Score: 54.13  E-value: 4.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1108 IEDERDRVQ--KKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTL-LSERdvarsvrlpREKGRMRFHKL 1184
Cdd:cd21222      7 FDEAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVpLHEY---------HLTPSTDDEKL 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2496167637 1185 QNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 1228
Cdd:cd21222     78 HNVKLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
2435-2579 6.31e-08

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 58.81  E-value: 6.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2435 QRRLEDEEMADAQQKQIEREmtvLQQTFLTEkEMLLKKEKLiEDEKKKLEsqfEEEIKKAKALKDEQDRQRQQMEEEKLK 2514
Cdd:pfam15709  360 QRRLQQEQLERAEKMREELE---LEQQRRFE-EIRLRKQRL-EEERQRQE---EEERKQRLQLQAAQERARQQQEEFRRK 431
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2496167637 2515 LKATMDAalNKQKEAEKDILNKQKEmQELERKRLEQERVLAD--ENQKLREKLQQMEEAQKSTLITE 2579
Cdd:pfam15709  432 LQELQRK--KQQEEAERAEAEKQRQ-KELEMQLAEEQKRLMEmaEEERLEYQRQKQEAEEKARLEAE 495
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
1109-1227 6.31e-08

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


Pssm-ID: 409148  Cd Length: 114  Bit Score: 53.66  E-value: 6.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1109 EDERDrvqKKTFTKWVNKHLIKSqrHVTDLYEDLRDGhnlISLLEVLsgDTLLSERDVARSVRLPREKgrMRFHKLQNVQ 1188
Cdd:cd21299      1 ETSRE---ERCFRLWINSLGIDT--YVNNVFEDVRDG---WVLLEVL--DKVSPGSVNWKHANKPPIK--MPFKKVENCN 68
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2496167637 1189 IALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 1227
Cdd:cd21299     69 QVVKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
1247-1349 6.61e-08

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: 53.92  E-value: 6.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1247 SAKEKLLLWSQRMTdgyQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTN-LENLEQAFNVAEKDLGVTRLLD 1325
Cdd:cd21314     11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQpVQNAREAMQQADDWLGVPQVIA 87
                           90       100
                   ....*....|....*....|....
gi 2496167637 1326 PEDVDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21314     88 PEEIVDPNVDEHSVMTYLSQFPKA 111
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
2102-2573 7.54e-08

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: 59.21  E-value: 7.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2102 RKPVEKEPLKECIQKTAEQAKVQVELEGLKKDLDKVSTKTQDILNSPQPSATAPVLRSELELTVQKMDHAymlssvyLEK 2181
Cdd:TIGR00618  220 RKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRA-------RKA 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2182 LKTVEMVIRNTQgaegVLKQYENCLREVHTVPNDVKEVETYRTNLKKMRAEAEAEQPVFDSL--EEELKKASAVSDKMSR 2259
Cdd:TIGR00618  293 APLAAHIKAVTQ----IEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLhsQEIHIRDAHEVATSIR 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2260 VHSERDAELDQH----RQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWLIRWIAD--AKQRQENIQAVPIT 2333
Cdd:TIGR00618  369 EISCQQHTLTQHihtlQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQqeLQQRYAELCAAAIT 448
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2334 D---SKTLKEQLAKE--KKLLEEIEKNKDKVDECQKYAKayidiIKDYELQlVAYKAQVEPltSPLKKTKLD-----SAS 2403
Cdd:TIGR00618  449 CtaqCEKLEKIHLQEsaQSLKEREQQLQTKEQIHLQETR-----KKAVVLA-RLLELQEEP--CPLCGSCIHpnparQDI 520
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2404 DN----------IIQEYVTLRTR----YSELMTLTSQyIKFITDTQRRLEDEEMADAQQKQ-IEREMTVLQQTfltEKEM 2468
Cdd:TIGR00618  521 DNpgpltrrmqrGEQTYAQLETSeedvYHQLTSERKQ-RASLKEQMQEIQQSFSILTQCDNrSKEDIPNLQNI---TVRL 596
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2469 LLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAA----LNKQKEAEKDILNKQKEMQELE 2544
Cdd:TIGR00618  597 QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAlqltLTQERVREHALSIRVLPKELLA 676
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 2496167637 2545 RKRLEQERV-------------LADENQKLREKLQQMEEAQK 2573
Cdd:TIGR00618  677 SRQLALQKMqsekeqltywkemLAQCQTLLRELETHIEEYDR 718
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2435-2573 8.34e-08

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 57.62  E-value: 8.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2435 QRRLEDEEMADAQQKQIE----REMTVLQQTFLTEKEMLLKKEKLIED--------EKKKLESQFEEEIKKAKALKD-EQ 2501
Cdd:pfam13868  107 VERIQEEDQAEAEEKLEKqrqlREEIDEFNEEQAEWKELEKEEEREEDerileylkEKAEREEEREAEREEIEEEKErEI 186
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2496167637 2502 DRQRQQMEEEKlKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQK 2573
Cdd:pfam13868  187 ARLRAQQEKAQ-DEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAE 257
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
2123-2528 8.44e-08

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: 58.96  E-value: 8.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2123 VQVELEGLKKDLDKVSTKTQDILNSPQPSATAPVLRSELELTVQKMDHAYMLSSVYLEKLKTVEMVIRNTQGAE----GV 2198
Cdd:pfam05483  365 LRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEqeliFL 444
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2199 LKQYEnclREVHTVPNDVKEVET----YRTNLKKMRAEAEAEQPVFDSLEEELKKASAVSDKMSRVHSERDAELDQHRQH 2274
Cdd:pfam05483  445 LQARE---KEIHDLEIQLTAIKTseehYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQED 521
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2275 LSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESY----DWLIRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLE 2350
Cdd:pfam05483  522 IINCKKQEERMLKQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKK 601
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2351 EIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEPLTSPLK--KTKLDSASDNIiQEYVTLRTRYSELMTLTSQYI 2428
Cdd:pfam05483  602 QIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAsaKQKFEEIIDNY-QKEIEDKKISEEKLLEEVEKA 680
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2429 KFITDTQRRLEDEEMADAQQKQIEreMTVLQQT-------FLTEKEMLLKKEKLIEDEKKKLESQFEEEIK--KAKALKD 2499
Cdd:pfam05483  681 KAIADEAVKLQKEIDKRCQHKIAE--MVALMEKhkhqydkIIEERDSELGLYKNKEQEQSSAKAALEIELSniKAELLSL 758
                          410       420
                   ....*....|....*....|....*....
gi 2496167637 2500 EQDRQRQQMEEEKLKLKATMDAALNKQKE 2528
Cdd:pfam05483  759 KKQLEIEKEEKEKLKMEAKENTAILKDKK 787
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2215-2532 1.36e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 1.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2215 DVKEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAvsdkmsrVHSERDAELDQHRQHLSSLQDRWKAVFTQIDLRQR 2294
Cdd:COG1196    223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEA-------ELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2295 ELDQLGRQLGYYRESydwlirwIADAKQRQENIQAvpitDSKTLKEQLAKEKKLLEEIEKNKDKVDEcqkyakayidIIK 2374
Cdd:COG1196    296 ELARLEQDIARLEER-------RRELEERLEELEE----ELAELEEELEELEEELEELEEELEEAEE----------ELE 354
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2375 DYELQLVAYKAQVEpltsplkktKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEMADAQQKQIERE 2454
Cdd:COG1196    355 EAEAELAEAEEALL---------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2496167637 2455 MTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLkATMDAALNKQKEAEKD 2532
Cdd:COG1196    426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL-AEAAARLLLLLEAEAD 502
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2081-2593 1.51e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 1.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2081 SEVKDLRLRIEDCEARtvARIRKPVEKEPLKECIQKTAEQAKVQVELEGLKKDLDKVSTKTQdilnspqpsatapVLRSE 2160
Cdd:TIGR02168  288 KELYALANEISRLEQQ--KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE-------------ELKEE 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2161 LELTVQKMDHAYMLSSVYLEKLKTVEMVIRNTQGAEGVLKQYENCLRevhtvpNDVKEVETYRTNLKKMRAEAEAEQPvf 2240
Cdd:TIGR02168  353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN------NEIERLEARLERLEDRRERLQQEIE-- 424
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2241 dslEEELKKASAVSDKMSRVHSERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYR------------- 2307
Cdd:TIGR02168  425 ---ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslerlqenl 501
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2308 ESYDWLIRWIADAKQRQENIQAVpITDSKTLKE--QLAKEKKLLEEIEknkDKVDECQKYAKAYIDIIKDYELQlvayKA 2385
Cdd:TIGR02168  502 EGFSEGVKALLKNQSGLSGILGV-LSELISVDEgyEAAIEAALGGRLQ---AVVVENLNAAKKAIAFLKQNELG----RV 573
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2386 QVEPLTSpLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQY---IKFITDTQRRLEDEEMADAQQKQIEREMT--VLQQ 2460
Cdd:TIGR02168  574 TFLPLDS-IKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkaLSYLLGGVLVVDDLDNALELAKKLRPGYRivTLDG 652
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2461 TFLT----------EKEM-LLKKEKLIEDEKKKLEsQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEA 2529
Cdd:TIGR02168  653 DLVRpggvitggsaKTNSsILERRREIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL 731
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2496167637 2530 EKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQKSTLITEKHVTVVETVLNGQN 2593
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK 795
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2232-2599 2.06e-07

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 57.67  E-value: 2.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2232 EAEAEQPVFDSLEEELKKASAVSDKMSRVHSERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYREsyd 2311
Cdd:pfam02463  160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE--- 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2312 wlirwiadaKQRQENIQavpitDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEplt 2391
Cdd:pfam02463  237 ---------ERIDLLQE-----LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK--- 299
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2392 spLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEMADAQQKQIEREMTVLQQTFLTEKEMLLK 2471
Cdd:pfam02463  300 --SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLA 377
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2472 KEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELErkrleqe 2551
Cdd:pfam02463  378 KKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEK------- 450
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 2496167637 2552 rvLADENQKLREKLQQMEEAQKSTLITEKHVTVVETVLNGQNAGDVLD 2599
Cdd:pfam02463  451 --EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2225-2575 2.28e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.38  E-value: 2.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2225 NLKKMRAEAEAEQpvfDSLEEELKKASAVSDKMSrvhsERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELdqlgRQLG 2304
Cdd:PRK03918   166 NLGEVIKEIKRRI---ERLEKFIKRTENIEELIK----EKEKELEEVLREINEISSELPELREELEKLEKEV----KELE 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2305 YYRESYDWLIRWIADAKQRQENIQAvpitDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDY-------- 2376
Cdd:PRK03918   235 ELKEEIEELEKELESLEGSKRKLEE----KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYeeyldelr 310
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2377 --ELQLVAYKAQVEPLTSPLKK-TKLDSASDNIIQEYVTLRTRYSELMTLTSQY--IKFITDTQRRLEdEEMADAQQKQI 2451
Cdd:PRK03918   311 eiEKRLSRLEEEINGIEERIKElEEKEERLEELKKKLKELEKRLEELEERHELYeeAKAKKEELERLK-KRLTGLTPEKL 389
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2452 EREMTVLQqtflTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDR----QRQQMEEEKLKLKATMDAALNKQK 2527
Cdd:PRK03918   390 EKELEELE----KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEYTAELKRIE 465
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 2496167637 2528 EAEKDILNKQKEMQElERKRLEQERVLADENQKLREKLQQMEEAQKST 2575
Cdd:PRK03918   466 KELKEIEEKERKLRK-ELRELEKVLKKESELIKLKELAEQLKELEEKL 512
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2321-2571 2.45e-07

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 57.06  E-value: 2.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2321 KQRQENIQavpitdsKTLKEQLAKEKK-LLEEIEKNKdKVDECQKYAKAYID----IIKDYELQLVAYKAQVEPLTSPLK 2395
Cdd:pfam17380  287 RQQQEKFE-------KMEQERLRQEKEeKAREVERRR-KLEEAEKARQAEMDrqaaIYAEQERMAMERERELERIRQEER 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2396 KTKLDsasdNIIQEYVTL---RTRYSELMTLTSQY----IKFITDTQRR---LEDEEMADAQQKQIEREMTVLQQTFLTE 2465
Cdd:pfam17380  359 KRELE----RIRQEEIAMeisRMRELERLQMERQQknerVRQELEAARKvkiLEEERQRKIQQQKVEMEQIRAEQEEARQ 434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2466 KEM-LLKKEKLIEDEKKKLES-----------QFEEEIKKAKALKDEQDRQRQQMEEEKLKL--------KATMDAALNK 2525
Cdd:pfam17380  435 REVrRLEEERAREMERVRLEEqerqqqverlrQQEEERKRKKLELEKEKRDRKRAEEQRRKIlekeleerKQAMIEEERK 514
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2496167637 2526 QKEAEKDILNKQKEMQELERKR-LEQERVLADENQKLREKLQQMEEA 2571
Cdd:pfam17380  515 RKLLEKEMEERQKAIYEEERRReAEEERRKQQEMEERRRIQEQMRKA 561
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
2473-2661 2.52e-07

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 57.14  E-value: 2.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2473 EKLIEdekkKLESQ---FEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKE--------MQ 2541
Cdd:PRK00409   519 NELIA----SLEELereLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKeadeiikeLR 594
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2542 ELERKRLEQ--ERVLADENQKLREKLQQMEEAQKSTLITEKHVTVVETV--LNGQNAGDVLdgvEKRPDPMA---FDGIR 2614
Cdd:PRK00409   595 QLQKGGYASvkAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEVkyLSLGQKGEVL---SIPDDKEAivqAGIMK 671
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2496167637 2615 DKVPASRLLDIGVLPKKEfdllKNGKTTAKELGETENLRKILKGKNS 2661
Cdd:PRK00409   672 MKVPLSDLEKIQKPKKKK----KKKPKTVKPKPRTVSLELDLRGMRY 714
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
1242-1349 2.94e-07

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: 51.63  E-value: 2.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1242 QSEDMSAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLI-DMGKVYRQTNLENLEQAFNVAEKDLGV 1320
Cdd:cd21313      3 DAKKQTPKQRLLGWIQ---NKIPYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
                           90       100
                   ....*....|....*....|....*....
gi 2496167637 1321 TRLLDPEDVDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21313     80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2182-2573 3.27e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 56.70  E-value: 3.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2182 LKTVEMVIRNTQGAEGVLKQYENCLREVHTVPNDVKEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAVSDKMSRVH 2261
Cdd:COG4717     70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2262 serdaELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYY-RESYDWLIRWIADAKQRQENIQavpiTDSKTLKE 2340
Cdd:COG4717    150 -----ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAtEEELQDLAEELEELQQRLAELE----EELEEAQE 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2341 QLAKEKKLLEEIEKNKDKVDECQKYAKAYID----------------------------------IIKDYELQLVAYKAQ 2386
Cdd:COG4717    221 ELEELEEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlglLALLFLLLAREKASL 300
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2387 VEPLTSPLKKTKLDSASDNIIQEYVTLRTRYSEL-MTLTSQYIKFITDTQRRLE--DEEMADAQQKQIEREMT-VLQQTF 2462
Cdd:COG4717    301 GKEAEELQALPALEELEEEELEELLAALGLPPDLsPEELLELLDRIEELQELLReaEELEEELQLEELEQEIAaLLAEAG 380
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2463 LTEKEMLLKKEKL------IEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKlkatmdaalNKQKEAEKDILNK 2536
Cdd:COG4717    381 VEDEEELRAALEQaeeyqeLKEELEELEEQLEELLGELEELLEALDEEELEEELEELE---------EELEELEEELEEL 451
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2496167637 2537 QKEMQELER--KRLEQERVLADENQKLREKLQQMEEAQK 2573
Cdd:COG4717    452 REELAELEAelEQLEEDGELAELLQELEELKAELRELAE 490
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
2111-2830 4.13e-07

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 56.98  E-value: 4.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2111 KECIQKTAEQAKVQVELEGLKKDLDKVSTKTQDILNSPQPSAtapvlrSELELTVQKMDHAyMLSSVYLEKLKTVEMVIR 2190
Cdd:TIGR01612 1104 EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYI------DEIKAQINDLEDV-ADKAISNDDPEEIEKKIE 1176
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2191 NTQGAegvLKQYENCLREVHTVPNDVKEVETYRTNLKKMRA-------------------EAEAEQPVFDSLEEELKKAS 2251
Cdd:TIGR01612 1177 NIVTK---IDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGinlsygknlgklflekideEKKKSEHMIKAMEAYIEDLD 1253
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2252 AVSDKMSRVHSERDAELDQHRQ----HLSSLQDRWKAVFTQ------IDLRQRELDQLGrqlGYYRES-----YDWLIRW 2316
Cdd:TIGR01612 1254 EIKEKSPEIENEMGIEMDIKAEmetfNISHDDDKDHHIISKkhdeniSDIREKSLKIIE---DFSEESdindiKKELQKN 1330
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2317 IADAKQRQENIQAV--------PITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDyelqlvayKAQVE 2388
Cdd:TIGR01612 1331 LLDAQKHNSDINLYlneianiyNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD--------DINLE 1402
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2389 PLTSPLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRL----EDEEMADAQQKQIeremtvlqqtflt 2464
Cdd:TIGR01612 1403 ECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVlllfKNIEMADNKSQHI------------- 1469
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2465 ekeMLLKKEKLIEDEKKKLeSQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKatmdaalnKQKEAEKDILNKQKEMQ--- 2541
Cdd:TIGR01612 1470 ---LKIKKDNATNDHDFNI-NELKEHIDKSKGCKDEADKNAKAIEKNKELFE--------QYKKDVTELLNKYSALAikn 1537
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2542 ELERKRLEQERVLaDENQKLREK--LQQMEEAQKSTLITEKHVTVVETVLNGQNAGDVLDGVEKRPDPMafdgirdkvpA 2619
Cdd:TIGR01612 1538 KFAKTKKDSEIII-KEIKDAHKKfiLEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENF----------E 1606
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2620 SRLLDIGVLPKKEFDLLKngkttakelgETENLRKilkgknsiagiltpsnQKMTIYQASKEKKITP-GTAMILLEAqaa 2698
Cdd:TIGR01612 1607 NKFLKISDIKKKINDCLK----------ETESIEK----------------KISSFSIDSQDTELKEnGDNLNSLQE--- 1657
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2699 tgyMLDPINNHKLSVNEAVKEgliGPELHNKMLSAEKAVVGYKDPYsggKISVFEAMKKGLMDHDHAIRVLEAQLATG-- 2776
Cdd:TIGR01612 1658 ---FLESLKDQKKNIEDKKKE---LDELDSEIEKIEIDVDQHKKNY---EIGIIEKIKEIAIANKEEIESIKELIEPTie 1728
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2496167637 2777 GIIDPLNSHRV----PNEiayKQGQYDAEMNKIME---NPSDDTKGYFDPSTQEPLTYSEL 2830
Cdd:TIGR01612 1729 NLISSFNTNDLegidPNE---KLEEYNTEIGDIYEefiELYNIIAGCLETVSKEPITYDEI 1786
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
4097-4125 7.18e-07

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 48.48  E-value: 7.18e-07
                           10        20
                   ....*....|....*....|....*....
gi 2496167637 4097 IVDPETGKEMTVYEAYRKGLIDHQTYIEL 4125
Cdd:pfam00681   11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
3882-3920 8.56e-07

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 48.09  E-value: 8.56e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2496167637 3882 YLEGTSCIAGVYLESNKERLSIYQAMKKNMIRPGTAFEL 3920
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PLEC smart00250
Plectin repeat;
3881-3917 9.43e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 47.86  E-value: 9.43e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2496167637  3881 KYLEGTSCIAGVYLESNKERLSIYQAMKKNMIRPGTA 3917
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
2250-2734 1.06e-06

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 55.36  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2250 ASAVSDKMSRVHSERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWLIRWIADAKQRQENIQA 2329
Cdd:TIGR00618  182 ALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQL 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2330 vpitdsktLKEQLAKEKKL---LEEIEKNKDKVDECQKYA------KAYIDIIKDYELQLVAYKAQVEPLTSPLKKTKld 2400
Cdd:TIGR00618  262 --------LKQLRARIEELraqEAVLEETQERINRARKAAplaahiKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA-- 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2401 sasdNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEMADaQQKQIEREMTVLQQ--TFLTEKEMLLKKEKLIED 2478
Cdd:TIGR00618  332 ----AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISC-QQHTLTQHIHTLQQqkTTLTQKLQSLCKELDILQ 406
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2479 EKKklesqfeeeikkakALKDEQDRQRQQMEEEKLKLKATMDAalnKQKEAEKDILNKQKEMQELERKRLEQERVladeN 2558
Cdd:TIGR00618  407 REQ--------------ATIDTRTSAFRDLQGQLAHAKKQQEL---QQRYAELCAAAITCTAQCEKLEKIHLQES----A 465
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2559 QKLREKLQQMEEAQKSTLITEKHVTVVETVLNGQNAGD-VLDGVEKRPDPMAFDGIRDKVPASRLLDIGVLPKKefdLLK 2637
Cdd:TIGR00618  466 QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPcPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQ---LET 542
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2638 NGKTTAKELGETENLRKILKGKnsiAGILTPSNQKMTIyQASKEKKITPGTAMILLEAQAATGyMLDPINNHKLSVNEAV 2717
Cdd:TIGR00618  543 SEEDVYHQLTSERKQRASLKEQ---MQEIQQSFSILTQ-CDNRSKEDIPNLQNITVRLQDLTE-KLSEAEDMLACEQHAL 617
                          490
                   ....*....|....*..
gi 2496167637 2718 KEGLiGPELHNKMLSAE 2734
Cdd:TIGR00618  618 LRKL-QPEQDLQDVRLH 633
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2183-2570 1.37e-06

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 54.98  E-value: 1.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2183 KTVEMVIRNTQGAEGVLKQYENCLREVHTVPNDVKEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAVSDKMSR--- 2259
Cdd:pfam02463  657 GLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKine 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2260 -------VHSERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWLirwiADAKQRQENIQAVPI 2332
Cdd:pfam02463  737 elkllkqKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLK----AQEEELRALEEELKE 812
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2333 TDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAK-AYIDIIKDYELQLV-AYKAQVEPLTSPLKKTKLDSASDNIIQEY 2410
Cdd:pfam02463  813 EAELLEEEQLLIEQEEKIKEEELEELALELKEEQKlEKLAEEELERLEEEiTKEELLQELLLKEEELEEQKLKDELESKE 892
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2411 VTLRTRYSELMTLTSQYIKFITDTQRRLEDEEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEE 2490
Cdd:pfam02463  893 EKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL 972
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2491 IKKAKALKDEQDRQRQQMEEEKLKLKatmdaalnkQKEAEKDIlnKQKEMQELERKRLEQERVLADENQKLREKLQQMEE 2570
Cdd:pfam02463  973 GKVNLMAIEEFEEKEERYNKDELEKE---------RLEEEKKK--LIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLE 1041
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2413-2699 1.50e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.75  E-value: 1.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2413 LRTRYSELMTLTSQYIKFITDTQRRLEDE-EMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLE------S 2485
Cdd:COG4372     18 LRPKTGILIAALSEQLRKALFELDKLQEElEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQaaqaelA 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2486 QFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELErkrlEQERVLADENQKLREKL 2565
Cdd:COG4372     98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE----EQLESLQEELAALEQEL 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2566 QQMEEAQKSTLITEKHVTVVETVLNGQNAGDVLDGVEKRPDPMAfDGIRDKVPASRLLDIGVLPKKEFDLLKNGKTTAKE 2645
Cdd:COG4372    174 QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELA-EELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2496167637 2646 LGETENLRKILKGKNSIAGILTPSNQKMTIYQASKEKKITPGTAMILLEAQAAT 2699
Cdd:COG4372    253 EEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAA 306
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
1101-1225 1.86e-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: 50.43  E-value: 1.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1101 EKTWPNFIEDErdrvqKKTFTKWVNK---------HLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlSERDVARSVR 1171
Cdd:cd21323     15 EGTQHSYSEEE-----KVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTI-DERAINKKKL 88
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2496167637 1172 LPrekgrmrFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1225
Cdd:cd21323     89 TP-------FTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQII 135
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
2447-2578 2.21e-06

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 49.87  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2447 QQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDekkKLESQFEEEIKK-AKALKDEQDRqRQQMEEEKLKLKAT-MDAALN 2524
Cdd:pfam12474    8 QKDRFEQERQQLKKRYEKELEQLERQQKQQIE---KLEQRQTQELRRlPKRIRAEQKK-RLKMFRESLKQEKKeLKQEVE 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2496167637 2525 KQ-KEAEKDILNKQKEMQELErKRLEQERVLADENQKLREKLQQMEEAQKSTLIT 2578
Cdd:pfam12474   84 KLpKFQRKEAKRQRKEELELE-QKHEELEFLQAQSEALERELQQLQNEKRKELAE 137
PRK12704 PRK12704
phosphodiesterase; Provisional
2441-2579 2.28e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 53.63  E-value: 2.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2441 EEMADAQQKQIEREMTVLqqtfltekemllKKEKLIE--DEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEeklKLKAT 2518
Cdd:PRK12704    37 EEEAKRILEEAKKEAEAI------------KKEALLEakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEE---NLDRK 101
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2496167637 2519 MDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLrEKLQQM--EEAqKSTLITE 2579
Cdd:PRK12704   102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLtaEEA-KEILLEK 162
SPEC smart00150
Spectrin repeats;
1609-1703 2.50e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.87  E-value: 2.50e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  1609 LRYVQDLLEWVQENQRRIDEAEWGSDLPSVESQLGSHRGLHQTVEDFRSKIERAKADENQL---SPISRGKYREYLGRLD 1685
Cdd:smart00150    4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
                            90
                    ....*....|....*...
gi 2496167637  1686 LQYAKLLNSSKSRLRNLD 1703
Cdd:smart00150   84 ERWEELKELAEERRQKLE 101
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
2456-2569 2.99e-06

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 52.29  E-value: 2.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2456 TVLQQtFLTEKE-----------MLLKKEKLIEDEKKKlesqfEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALN 2524
Cdd:pfam02841  176 EVLQE-FLQSKEaveeailqtdqALTAKEKAIEAERAK-----AEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLI 249
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2496167637 2525 KQKEAEKDILNKQKEMQeLERKRLEQERVL----ADENQKLREKLQQME 2569
Cdd:pfam02841  250 EKMEAEREQLLAEQERM-LEHKLQEQEELLkegfKTEAESLQKEIQDLK 297
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2088-2574 3.32e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 3.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2088 LRIEDCE--ARTVARIRKPV--EKEPLKECIQKTAEqakVQVELEGLKKDLDKVSTKTQDIlnspqpSATAPVLRSELEL 2163
Cdd:PRK03918   155 LGLDDYEnaYKNLGEVIKEIkrRIERLEKFIKRTEN---IEELIKEKEKELEEVLREINEI------SSELPELREELEK 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2164 TVQKMDHAYMLSSVYLEKLKTVEMVIRNTQGAEGVLKQYENCLREVHtvpNDVKEVETYRTNLKKMRAEAEAEQPVFDSL 2243
Cdd:PRK03918   226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK---KEIEELEEKVKELKELKEKAEEYIKLSEFY 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2244 EEELKKASAVSDKMSRVHSER-------------DAELDQHRQHLSSLQDR------WKAVFTQIDLRQRELDQLGRQLG 2304
Cdd:PRK03918   303 EEYLDELREIEKRLSRLEEEIngieerikeleekEERLEELKKKLKELEKRleeleeRHELYEEAKAKKEELERLKKRLT 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2305 YYreSYDWLIRWIADAKQRQENIQA--VPITDSK-TLKEQLAKEKKLLEEIEKNKDKVDECQKyakayiDIIKDYELQLV 2381
Cdd:PRK03918   383 GL--TPEKLEKELEELEKAKEEIEEeiSKITARIgELKKEIKELKKAIEELKKAKGKCPVCGR------ELTEEHRKELL 454
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2382 A-YKAQVEPLTSPLKKtkLDSASDNIIQEYVTLRTRYSELMTLTSQY--IKFITDTQRRLEDEEMADAQQKQIEREmTVL 2458
Cdd:PRK03918   455 EeYTAELKRIEKELKE--IEEKERKLRKELRELEKVLKKESELIKLKelAEQLKELEEKLKKYNLEELEKKAEEYE-KLK 531
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2459 QQTFLTEKEML-----LKKEKLIEDEKKKLESQFEE-EIKKAKALKDEQDRQRQQMEEEKLKLKATMDA--ALNKQKEAE 2530
Cdd:PRK03918   532 EKLIKLKGEIKslkkeLEKLEELKKKLAELEKKLDElEEELAELLKELEELGFESVEELEERLKELEPFynEYLELKDAE 611
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 2496167637 2531 KDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQKS 2574
Cdd:PRK03918   612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2225-2595 4.52e-06

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: 53.15  E-value: 4.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2225 NLKKMRAEAEAEQPVFDSLEEELKKasavsdkmsrvhseRDAELDQHRQHLSSLQDRWKAVFTQI-DLRQRELDQLGRQL 2303
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEK--------------LTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKI 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2304 GYYRESYDWLIRWIADAKQRQENIQavpitdsktlkeqlAKEKKLLEEIEKNKDKVDECQKyakayidiikdyelQLVAY 2383
Cdd:TIGR02169  297 GELEAEIASLERSIAEKERELEDAE--------------ERLAKLEAEIDKLLAEIEELER--------------EIEEE 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2384 KAQVEPLTSPLKKTKldsasdniiQEYVTLRTRYSELMTltsqyikfitdTQRRLEDEemadaqQKQIEREMTVLQQtfl 2463
Cdd:TIGR02169  349 RKRRDKLTEEYAELK---------EELEDLRAELEEVDK-----------EFAETRDE------LKDYREKLEKLKR--- 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2464 tEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKAtmdaalnKQKEAEKDILNKQKEMQEL 2543
Cdd:TIGR02169  400 -EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK-------QEWKLEQLAADLSKYEQEL 471
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2496167637 2544 ERKRLEQERVlADENQKLREKLQQMEEAQKSTLITEKHVTVVETVLNGQNAG 2595
Cdd:TIGR02169  472 YDLKEEYDRV-EKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG 522
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2223-2599 4.63e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 4.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2223 RTNLKKMRAEAE-AEQpvFDSLEEELKKASAVSdkMSRVHSERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGR 2301
Cdd:COG1196    199 ERQLEPLERQAEkAER--YRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2302 QLGYYRESYDWLIRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKyakayidiikdyelQLV 2381
Cdd:COG1196    275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE--------------ELE 340
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2382 AYKAQVEpltsplkktKLDSASDNIIQEYVTLRTRYSELMTLTSQYIkfitDTQRRLEDEEMadAQQKQIEREMTVLQQT 2461
Cdd:COG1196    341 ELEEELE---------EAEEELEEAEAELAEAEEALLEAEAELAEAE----EELEELAEELL--EALRAAAELAAQLEEL 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2462 FLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQME--EEKLKLKATMDAALNKQKEAEKDILNKQKE 2539
Cdd:COG1196    406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEleEEEEALLELLAELLEEAALLEAALAELLEE 485
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2496167637 2540 MQELERKRLEQERVLADENQKLREKLQQMEEAQKSTLITEKHV---------TVVETVLNGQNAGDVLD 2599
Cdd:COG1196    486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVligveaayeAALEAALAAALQNIVVE 554
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
2439-2569 4.64e-06

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 49.10  E-value: 4.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2439 EDEEMADAQQKQIERemtvLQQTFLTEKEMLLKKEKLiedEKKKLESQFEEEIK-KAKALKDEQDRQRQQMEEEKLKLKa 2517
Cdd:pfam12474   26 ELEQLERQQKQQIEK----LEQRQTQELRRLPKRIRA---EQKKRLKMFRESLKqEKKELKQEVEKLPKFQRKEAKRQR- 97
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2496167637 2518 tMDAALNKQKEAEKDILNKQKEMQELERKRLEQERvladenqklREKLQQME 2569
Cdd:pfam12474   98 -KEELELEQKHEELEFLQAQSEALERELQQLQNEK---------RKELAEHE 139
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
2335-2586 5.50e-06

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 52.55  E-value: 5.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2335 SKTLKEQLAKEKKLLEEIEKnkdkvdecQKYAKAYIDIikdyELQLVAYKAQVEPLTSPLKKTKLDSASDNIIQEYVTLR 2414
Cdd:pfam06160  206 KTELPDQLEELKEGYREMEE--------EGYALEHLNV----DKEIQQLEEQLEENLALLENLELDEAEEALEEIEERID 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2415 TRYsELMTLTSQYIKFITDTQRRLEDE-EMADAQQKQIEREMTVLQQTF-LTEKEmlLKKEKLIEDEKKKLESQFEEEIK 2492
Cdd:pfam06160  274 QLY-DLLEKEVDAKKYVEKNLPEIEDYlEHAEEQNKELKEELERVQQSYtLNENE--LERVRGLEKQLEELEKRYDEIVE 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2493 KAK-------ALKDEQDRQRQQM---EEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERkRLEQER---------- 2552
Cdd:pfam06160  351 RLEekevaysELQEELEEILEQLeeiEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKR-LVEKSNlpglpesyld 429
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2496167637 2553 ---VLADENQKLREKLQQ----MEEAQKSTLITEKHVTVVE 2586
Cdd:pfam06160  430 yffDVSDEIEDLADELNEvplnMDEVNRLLDEAQDDVDTLY 470
PRK12704 PRK12704
phosphodiesterase; Provisional
2480-2589 5.88e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.47  E-value: 5.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2480 KKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLkLKATmDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQ 2559
Cdd:PRK12704    26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEAL-LEAK-EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
                           90       100       110
                   ....*....|....*....|....*....|
gi 2496167637 2560 KLREKLQQMEEAQKSTLITEKHVTVVETVL 2589
Cdd:PRK12704   104 LLEKREEELEKKEKELEQKQQELEKKEEEL 133
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
2334-2573 6.23e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 51.45  E-value: 6.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2334 DSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDiikdyelQLVAYKAQVEPLTSPLKKTKldSASDNIIQEYVTL 2413
Cdd:COG1340      6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAE-------KRDELNAQVKELREEAQELR--EKRDELNEKVKEL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2414 RTRYSELMTLTSQYIKFITDTQRRLEDEEMADAQQKQIEREMTVLQQTFLT-------EKEMLLK---KEKLIEDEKKKL 2483
Cdd:COG1340     77 KEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTevlspeeEKELVEKikeLEKELEKAKKAL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2484 E--SQFEEEIKKAKALKDEQDRQRQQMEE---EKLKLKATMDAALNK----QKEAE---KDILNKQKEMQELERKRLEQE 2551
Cdd:COG1340    157 EknEKLKELRAELKELRKEAEEIHKKIKElaeEAQELHEEMIELYKEadelRKEADelhKEIVEAQEKADELHEEIIELQ 236
                          250       260
                   ....*....|....*....|..
gi 2496167637 2552 RVLADENQKLREKLQQMEEAQK 2573
Cdd:COG1340    237 KELRELRKELKKLRKKQRALKR 258
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
2432-2571 6.62e-06

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 50.47  E-value: 6.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2432 TDTQRRLEDEEMADAQQ---------KQIERemtvlQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKaKALKDEQD 2502
Cdd:pfam13904   38 LTYARKLEGLKLERQPLeayenwlaaKQRQR-----QKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQR-KARQQTKK 111
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2496167637 2503 RQRQQMEEEKLKLKATMDAALNKQKEAE-KDILNK--QKEMQELERKRLEQERVLADENQKLREKLQQMEEA 2571
Cdd:pfam13904  112 REESHKQKAAESASKSLAKPERKVSQEEaKEVLQEweRKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKA 183
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2262-2574 8.80e-06

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: 52.38  E-value: 8.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2262 SERDAELDQHRQHLsslqdrwKAVFTQIDLRQRELDQLGRQLGYYRESYDWLIRWIADAKQRQENIQAVPITDSKTLKEQ 2341
Cdd:TIGR02169  166 AEFDRKKEKALEEL-------EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQ 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2342 LAKEKKLLEEIEKNKDKVD-ECQKYAKAYIDIIKDyelqLVAYKAQVEPLTSplkktkldsasdniiQEYVTLRTRYSEL 2420
Cdd:TIGR02169  239 KEAIERQLASLEEELEKLTeEISELEKRLEEIEQL----LEELNKKIKDLGE---------------EEQLRVKEKIGEL 299
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2421 MTLTSQYIKFITDTQRRLEDeemADAQQKQI--EREMTVLQQTFLTEK--EMLLKKEKLIE------DEKKKLESQFEEE 2490
Cdd:TIGR02169  300 EAEIASLERSIAEKERELED---AEERLAKLeaEIDKLLAEIEELEREieEERKRRDKLTEeyaelkEELEDLRAELEEV 376
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2491 IKKAKALKDEQDRQRQQME---EEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLE--------QERVLADEnQ 2559
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEleeekedkALEIKKQE-W 455
                          330
                   ....*....|....*
gi 2496167637 2560 KLREKLQQMEEAQKS 2574
Cdd:TIGR02169  456 KLEQLAADLSKYEQE 470
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2217-2563 9.62e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.08  E-value: 9.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2217 KEVETYRTnLKKMRAEAEAEQpvfDSLEEELKKASAVSDKMSRVHSERD--AELDQHRQHLSSLQDR----------WKA 2284
Cdd:COG4717     85 EKEEEYAE-LQEELEELEEEL---EELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERleeleerleeLRE 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2285 VFTQIDLRQRELDQLGRQLGYYRESYDWLIRW-IADAKQRQENIQAvpitDSKTLKEQLAKEKKLLEEIEKNKDKVdECQ 2363
Cdd:COG4717    161 LEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQ----RLAELEEELEEAQEELEELEEELEQL-ENE 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2364 KYAKAYIDIIKDYELQLVA---------------------------------------YKAQVEPLTSPLKKTKLDSASD 2404
Cdd:COG4717    236 LEAAALEERLKEARLLLLIaaallallglggsllsliltiagvlflvlgllallflllAREKASLGKEAEELQALPALEE 315
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2405 NIIQEYVTLRTRY----SELMTLTSQYIKFITDTQRRLE--DEEMADAQQKQIEREMT-VLQQTFLTEKEMLLKKEKL-- 2475
Cdd:COG4717    316 LEEEELEELLAALglppDLSPEELLELLDRIEELQELLReaEELEEELQLEELEQEIAaLLAEAGVEDEEELRAALEQae 395
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2476 ----IEDEKKKLESQFEEEIKKAKALKDEQDRQrqQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELE------R 2545
Cdd:COG4717    396 eyqeLKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQLEedgelaE 473
                          410
                   ....*....|....*...
gi 2496167637 2546 KRLEQERVLADENQKLRE 2563
Cdd:COG4717    474 LLQELEELKAELRELAEE 491
PLEC smart00250
Plectin repeat;
3680-3716 9.63e-06

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 45.17  E-value: 9.63e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2496167637  3680 LNLLETQAATGFIIDPIKNETLTVDEAVRKGVVGPEI 3716
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
1116-1225 1.27e-05

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


Pssm-ID: 409174  Cd Length: 148  Bit Score: 48.13  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1116 QKKTFTKWVNK---------HLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlSERDVARSVRLPrekgrmrFHKLQN 1186
Cdd:cd21325     25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTI-DERAINKKKLTP-------FIIQEN 96
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2496167637 1187 VQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1225
Cdd:cd21325     97 LNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 135
PLEC smart00250
Plectin repeat;
4090-4118 1.38e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.78  E-value: 1.38e-05
                            10        20
                    ....*....|....*....|....*....
gi 2496167637  4090 VRKRRVVIVDPETGKEMTVYEAYRKGLID 4118
Cdd:smart00250    6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
1113-1224 1.50e-05

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


Pssm-ID: 409134  Cd Length: 121  Bit Score: 47.27  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1113 DRVQKKTFTKWVNKHLIKS--QRHVTDLYEDLRDGHNLISLLEVLSGDTLlseRDVARSvrlPREKGRMrfhkLQNVQIA 1190
Cdd:cd21285      8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKI---EDINGC---PKNRSQM----IENIDAC 77
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2496167637 1191 LDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTI 1224
Cdd:cd21285     78 LSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2263-2598 1.76e-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: 51.21  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2263 ERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWLIRWIADAKQRQENIQAvpitDSKTLKEQL 2342
Cdd:TIGR02168  222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK----ELYALANEI 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2343 AKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEPLTSPLKKtKLDSASDNIIQEYVTLRTRYSELMT 2422
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE-ELESLEAELEELEAELEELESRLEE 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2423 LTSQYIKFITDTQRRLEDEEMADAQQKQIEREMTVLQ---QTFLTEKEMLLKkeKLIEDEKKKLESQFEEEIKKAKALKD 2499
Cdd:TIGR02168  377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrrERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQE 454
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2500 EQDRQRQQME---EEKLKLKATMDAALNK--QKEAEKDILnkqKEMQELERKRLEQERVLADENQKLREKLQQMeeaqkS 2574
Cdd:TIGR02168  455 ELERLEEALEelrEELEEAEQALDAAERElaQLQARLDSL---ERLQENLEGFSEGVKALLKNQSGLSGILGVL-----S 526
                          330       340
                   ....*....|....*....|....*.
gi 2496167637 2575 TLIT--EKHVTVVETVLnGQNAGDVL 2598
Cdd:TIGR02168  527 ELISvdEGYEAAIEAAL-GGRLQAVV 551
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
1269-1346 2.18e-05

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: 46.14  E-value: 2.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1269 DNFTTSWRDGKLFNAVIHK------NYPRLIdmgkvyRQTNLENLEQAFNvAEKDLGVTRLLDPEDVDVPHPDEKSIITY 1342
Cdd:cd21185     20 NNFTTDWNDGRLLCGLVNAlggsvpGWPNLD------PEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAY 92

                   ....
gi 2496167637 1343 VSSL 1346
Cdd:cd21185     93 AAQL 96
PLEC smart00250
Plectin repeat;
3957-3988 2.22e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.01  E-value: 2.22e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2496167637  3957 KLLSAERAVTGYRDPYTGKTISLFQAMKKGLI 3988
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
PLEC smart00250
Plectin repeat;
3056-3092 2.33e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 44.01  E-value: 2.33e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2496167637  3056 KLLSAERAVTGYRDPYTGKTVSLFQAMKKDLIPKEQG 3092
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2339-2574 2.42e-05

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: 50.15  E-value: 2.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2339 KEQLAKE-KKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEPLTSPLKKTKldsasdniiqeyvtlrtry 2417
Cdd:COG4942     22 AAEAEAElEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE------------------- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2418 SELMTLTSQyikfITDTQRRLEdeemadAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESqfeeeikkAKAL 2497
Cdd:COG4942     83 AELAELEKE----IAELRAELE------AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY--------LKYL 144
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2496167637 2498 KDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQKS 2574
Cdd:COG4942    145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
2441-2552 2.67e-05

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 47.48  E-value: 2.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2441 EEMADAQQKQIEREMTVLQQtfLTEKEmllkKEKLIEDEKKKLESQFEEEikkakALKDEQDRQRQQMEEEKLKLKATMD 2520
Cdd:pfam15236   45 EERERKRQKALEHQNAIKKQ--LEEKE----RQKKLEEERRRQEEQEEEE-----RLRREREEEQKQFEEERRKQKEKEE 113
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2496167637 2521 AALNKQKEA----EKDILNKQKEMQELERKRLEQER 2552
Cdd:pfam15236  114 AMTRKTQALlqamQKAQELAQRLKQEQRIRELAEKG 149
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2435-2567 2.98e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 49.53  E-value: 2.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2435 QRRLEDEEMADAQQKQIEREmtvlqqtfltekEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQD------------ 2502
Cdd:pfam13868  149 EEREEDERILEYLKEKAERE------------EEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDelraklyqeeqe 216
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2496167637 2503 ---RQRQQMEEEK-LKLKATMDAALNKQKEAEKDILNKQKEMQELERKRL-----EQERVLADENQKLREKLQQ 2567
Cdd:pfam13868  217 rkeRQKEREEAEKkARQRQELQQAREEQIELKERRLAEEAEREEEEFERMlrkqaEDEEIEQEEAEKRRMKRLE 290
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
1116-1225 4.11e-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: 46.50  E-value: 4.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1116 QKKTFTKWVN---------KHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlSERDVARsvrlpreKGRMRFHKLQN 1186
Cdd:cd21292     25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTI-DERAINK-------KKLTVFTIHEN 96
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2496167637 1187 VQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1225
Cdd:cd21292     97 LTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
PLEC smart00250
Plectin repeat;
3350-3383 4.50e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 43.24  E-value: 4.50e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2496167637  3350 LLEAQAASGFIVDPVKNQCLSVDEAVKSGVVGPE 3383
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1398-1721 4.59e-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: 50.06  E-value: 4.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1398 YEEIEL-IWRQFLKFKETELPVKETDKNRSKQIYQTFESAVSAgqvkvppgyhpidVEKEWGRLHVAILERERLLRIEFE 1476
Cdd:TIGR02168  222 LRELELaLLVLRLEELREELEELQEELKEAEEELEELTAELQE-------------LEEKLEELRLEVSELEEEIEELQK 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1477 RLERLQRIVNKVQMESGSCDEQLGNLE-TLLQTDIRLLNAGKPAQHTAEIERELDKADNTIRLLFNDVQILKDGRHPQAE 1555
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLErQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1556 QMYRRVFRIHERLVNLRSDYNLRLKSTTS-AIQATRLSPQESSMKARpelddvtlryVQDLLEWVQENQRRIDEAEwgsd 1634
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVAQLELQIASlNNEIERLEARLERLEDR----------RERLQQEIEELLKKLEEAE---- 434
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1635 LPSVESQLGSH-RGLHQTVEDFRSKIERAKADENQLSPISRgKYREYLGRLDlQYAKLLNSSKSRLRNLDSLHAFVSAAT 1713
Cdd:TIGR02168  435 LKELQAELEELeEELEELQEELERLEEALEELREELEEAEQ-ALDAAERELA-QLQARLDSLERLQENLEGFSEGVKALL 512

                   ....*...
gi 2496167637 1714 KELMWLND 1721
Cdd:TIGR02168  513 KNQSGLSG 520
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
1116-1225 4.63e-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: 46.54  E-value: 4.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1116 QKKTFTKWVNK---------HLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlSERDVARSVRLPrekgrmrFHKLQN 1186
Cdd:cd21324     25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTI-DERTINKKKLTP-------FTIQEN 96
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2496167637 1187 VQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1225
Cdd:cd21324     97 LNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 135
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
2473-2567 5.03e-05

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 46.03  E-value: 5.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2473 EKLIE--DEKKKLESQFEeeiKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQ 2550
Cdd:pfam03938    8 QKILEesPEGKAAQAQLE---KKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQE 84
                           90
                   ....*....|....*..
gi 2496167637 2551 ervLADENQKLREKLQQ 2567
Cdd:pfam03938   85 ---LQKKQQELLQPIQD 98
COG4487 COG4487
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
2328-2515 5.26e-05

Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];


Pssm-ID: 443580 [Multi-domain]  Cd Length: 425  Bit Score: 49.17  E-value: 5.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2328 QAVPITDS------KTLKEQLAKE-KKLLEEIEKNKDKVDECQKYAKAYID-IIKDYELQLVAYKAQVEpltSPLKKTKL 2399
Cdd:COG4487     11 TVFKLDESlyadivKQRRAEFEKElAERLADAAKREAALELAEAKAKAQLQeQVAEKDAEIAELRARLE---AEERKKAL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2400 DSASDNIIQEYV---TLRTRYSELMTLTSQYIKFItDTQRRLEDE--EMADAQQKQIEREMTVLQ-QTFLTEKEMLLKKE 2473
Cdd:COG4487     88 AVAEEKEKELAAlqeALAEKDAKLAELQAKELELL-KKERELEDAkrEAELTVEKERDEELDELKeKLKKEEEEKQLAEK 166
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2496167637 2474 KLIEDEKKKlesQFEEEIKKAKALKDEQDRQRQQMEEEKLKL 2515
Cdd:COG4487    167 SLKVAEYEK---QLKDMQEQIEELKRKKEQGSTQLQGEVLEL 205
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
2437-2542 6.38e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 49.44  E-value: 6.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2437 RLEDEEMaDAQQKQIEREMtVLQQTFLTEKEMLLKKEKLIEdEKKKLESQFEEEIKKA-KALKDEQD------RQRQQME 2509
Cdd:PRK00409   524 SLEELER-ELEQKAEEAEA-LLKEAEKLKEELEEKKEKLQE-EEDKLLEEAEKEAQQAiKEAKKEADeiikelRQLQKGG 600
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2496167637 2510 EEKLKLKATMDA--ALNKQKEAEKDILNKQKEMQE 2542
Cdd:PRK00409   601 YASVKAHELIEArkRLNKANEKKEKKKKKQKEKQE 635
PLEC smart00250
Plectin repeat;
4231-4267 6.66e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.85  E-value: 6.66e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2496167637  4231 DPSEETVPIAGILDTETLEKVSVTEAMHRNLVDNITG 4267
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
2254-2684 7.11e-05

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: 49.33  E-value: 7.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2254 SDKMSRVHSERDAELDQHRqhlsslqdRWKaVFTQIDLRQREldqlgrqlgyyresydwlirwiadaKQRQENIQAVPIT 2333
Cdd:pfam05483   73 SEGLSRLYSKLYKEAEKIK--------KWK-VSIEAELKQKE-------------------------NKLQENRKIIEAQ 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2334 DSKTLKEQLAKEK---KLLEEIEKNKDKVDEcQKYAKAYIDIIKdyelQLVAYKAQvepltsplKKTKLDSASDNIIQEY 2410
Cdd:pfam05483  119 RKAIQELQFENEKvslKLEEEIQENKDLIKE-NNATRHLCNLLK----ETCARSAE--------KTKKYEYEREETRQVY 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2411 VTLRTRYSELMTLTSQ------------YIKFITDTQR--RLEDEEMADAQQKQIEREMTVLQqtfLTEKEMLLKKEKLI 2476
Cdd:pfam05483  186 MDLNNNIEKMILAFEElrvqaenarlemHFKLKEDHEKiqHLEEEYKKEINDKEKQVSLLLIQ---ITEKENKMKDLTFL 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2477 EDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELErkrleqervlad 2556
Cdd:pfam05483  263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLT------------ 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2557 enqklREKLQQMEEAQK-----STLITEKHVTV--VETVLNGQNagdvlDGVEKRPDPMAFDGIRDKVPASRLldigvlp 2629
Cdd:pfam05483  331 -----EEKEAQMEELNKakaahSFVVTEFEATTcsLEELLRTEQ-----QRLEKNEDQLKIITMELQKKSSEL------- 393
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2630 kKEFDLLKNGKTTAKE-----LGETENLRKILKGKNSIAGILTPSNQKMTIYQASKEKKI 2684
Cdd:pfam05483  394 -EEMTKFKNNKEVELEelkkiLAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEI 452
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
1109-1225 8.29e-05

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


Pssm-ID: 409143  Cd Length: 125  Bit Score: 45.13  E-value: 8.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1109 EDERdrvqkKTFTKWVNK---------HLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLlserdVARSVRLPREKGRM 1179
Cdd:cd21294      5 EDER-----REFTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTI-----DERVLNKPPRKNKP 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2496167637 1180 --RFHKLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 1225
Cdd:cd21294     75 lnNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2230-2495 8.39e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 8.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2230 RAEAEAEQpvfDSLEEELKKASAVSDKMsrvhserDAELDQHRQHLSSLQDRWKAVFTQIDLR--QRELDQLGRQLGYYR 2307
Cdd:COG4913    612 LAALEAEL---AELEEELAEAEERLEAL-------EAELDALQERREALQRLAEYSWDEIDVAsaEREIAELEAELERLD 681
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2308 ESYDWLI---RWIADAKQRQENIQAVpITDSKTLKEQLAKEKK-LLEEIEKNKDKVDECQKYAKAYidiikdYELQLVAY 2383
Cdd:COG4913    682 ASSDDLAaleEQLEELEAELEELEEE-LDELKGEIGRLEKELEqAEEELDELQDRLEAAEDLARLE------LRALLEER 754
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2384 KAQVepltspLKKTKLDSASDNIIQEYVTLRTR----YSELMTLTSQYIK----FITDTQRRLEDEEMADAQQKQIERE- 2454
Cdd:COG4913    755 FAAA------LGDAVERELRENLEERIDALRARlnraEEELERAMRAFNRewpaETADLDADLESLPEYLALLDRLEEDg 828
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2496167637 2455 MTVLQQTFlteKEMLLKKEkliEDEKKKLESQFEEEIKKAK 2495
Cdd:COG4913    829 LPEYEERF---KELLNENS---IEFVADLLSKLRRAIREIK 863
PLEC smart00250
Plectin repeat;
4344-4381 8.51e-05

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 42.47  E-value: 8.51e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2496167637  4344 QRFLEVQYLTGGLIEPEAQGRVSLDESIRKGTIDARTA 4381
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
2488-2602 9.48e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 9.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2488 EEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKrleqervLADENQKLREKLQQ 2567
Cdd:COG3883     15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE-------IAEAEAEIEERREE 87
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2496167637 2568 MEEAQKSTLITEKHVTVVETVLNGQNAGDVLDGVE 2602
Cdd:COG3883     88 LGERARALYRSGGSVSYLDVLLGSESFSDFLDRLS 122
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2433-2573 9.65e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.58  E-value: 9.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2433 DTQRRLEDEEMADAQQKQIEREMTVL--QQTFLTEKEMLLKKEKLiEDEKKKLESQFEEEIkkAKALKDEQDRQRQQMEE 2510
Cdd:pfam17380  311 EVERRRKLEEAEKARQAEMDRQAAIYaeQERMAMERERELERIRQ-EERKRELERIRQEEI--AMEISRMRELERLQMER 387
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2511 EKL--KLKATMDAA-------------LNKQKEAEKDILNKQKEMQELERKRLEQERVL--------ADENQKLREKLQQ 2567
Cdd:pfam17380  388 QQKneRVRQELEAArkvkileeerqrkIQQQKVEMEQIRAEQEEARQREVRRLEEERARemervrleEQERQQQVERLRQ 467

                   ....*.
gi 2496167637 2568 MEEAQK 2573
Cdd:pfam17380  468 QEEERK 473
BRE1 pfam08647
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a ...
2476-2576 9.75e-05

BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a transcriptional activator through direct activator interactions.


Pssm-ID: 462547 [Multi-domain]  Cd Length: 95  Bit Score: 44.11  E-value: 9.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2476 IEDEKKKLESQFEEEIKKAKALKDEQdrqrQQMEEEKLKLKATMDAALNKQKEAEKDilnkqKEMQELERKRLeqeRVLA 2555
Cdd:pfam08647    1 LQTELVKLEQAFEELSEQLDKKVKDL----TILEEKKLRLEAEKAKADQKYFAAMRS-----KDALENENKKL---NTLL 68
                           90       100
                   ....*....|....*....|.
gi 2496167637 2556 DENQKLREKLQQMEEAQKSTL 2576
Cdd:pfam08647   69 SKSSELIEQLKETEKEFVRKL 89
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2217-2544 1.16e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.58  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2217 KEVETYRTNLKKMRAEAEAEQpvfdSLEEELKKASAVSDKMSRVHSERDAELDQHRQHLSSLQD---RWKAVFTQIDlRQ 2293
Cdd:pfam17380  303 QEKEEKAREVERRRKLEEAEK----ARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELeriRQEEIAMEIS-RM 377
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2294 RELD--QLGRQLG--YYRESYDWLIRWIADAKQRQENIQAVPITDSKTLKEQL-AKE---KKLLEEIEKNKDKVDECQKY 2365
Cdd:pfam17380  378 RELErlQMERQQKneRVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEeARQrevRRLEEERAREMERVRLEEQE 457
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2366 AKAYIDIIKDYELQlvaykaqvepltsplkktkldsasdniiqeyvtlRTRYSELMTLTSQYIKFITDTQRRLEDEEMAD 2445
Cdd:pfam17380  458 RQQQVERLRQQEEE----------------------------------RKRKKLELEKEKRDRKRAEEQRRKILEKELEE 503
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2446 AQQKQIEREmtvlQQTFLTEKEMLLKKEKLIEDEKKKLEsqfEEEIKKAKALKDEQDRQRQQME--EEKLKLKAtmdaaL 2523
Cdd:pfam17380  504 RKQAMIEEE----RKRKLLEKEMEERQKAIYEEERRREA---EEERRKQQEMEERRRIQEQMRKatEERSRLEA-----M 571
                          330       340
                   ....*....|....*....|.
gi 2496167637 2524 NKQKEAEKDILNKQKEMQELE 2544
Cdd:pfam17380  572 EREREMMRQIVESEKARAEYE 592
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
2322-2589 1.35e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 48.25  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2322 QRQENIQAVPITDsktLKEQLAKEKKLLEEIEKNKDKVDEcqkyakayidIIKDYELQLVAYKAQVEPLTSPL--KKTKL 2399
Cdd:pfam01576  179 SKLKNKHEAMISD---LEERLKKEEKGRQELEKAKRKLEG----------ESTDLQEQIAELQAQIAELRAQLakKEEEL 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2400 DSASDNIIQEYVTLRTRYSELMTLTSQyikfITDTQRRLEDEEMADAQQKQIEREM--------TVLQQTFLT---EKEM 2468
Cdd:pfam01576  246 QAALARLEEETAQKNNALKKIRELEAQ----ISELQEDLESERAARNKAEKQRRDLgeelealkTELEDTLDTtaaQQEL 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2469 LLKKE-------KLIEDEKKKLESQ--------------FEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQK 2527
Cdd:pfam01576  322 RSKREqevtelkKALEEETRSHEAQlqemrqkhtqaleeLTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ 401
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2528 EAEKDILNKQKEMQELERKRLEQERVLADENQKLrEKLQQ--------MEEAQKSTLITEKHVTVVETVL 2589
Cdd:pfam01576  402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKL-SKLQSelesvsslLNEAEGKNIKLSKDVSSLESQL 470
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
2457-2580 1.36e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 47.19  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2457 VLQQtFLTEKEM-----LLKKEKLIEDEKKKlesqfEEEIKKAKALKdeqdRQRQQMEEEKLKLKATMDAALNKQKEAEK 2531
Cdd:cd16269    171 VLQE-FLQSKEAeaeaiLQADQALTEKEKEI-----EAERAKAEAAE----QERKLLEEQQRELEQKLEDQERSYEEHLR 240
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2496167637 2532 DIlnKQKEMQELERKRLEQERVLaDENQKLREKLQQMEEAQKSTLITEK 2580
Cdd:cd16269    241 QL--KEKMEEERENLLKEQERAL-ESKLKEQEALLEEGFKEQAELLQEE 286
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
1236-1349 1.39e-04

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: 44.41  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1236 DIQVNGQSEDMSAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLI-DMGKVYRQTNLENLEQAFNVA 1314
Cdd:cd21312      1 DEEEDEEAKKQTPKQRLLGWIQ---NKLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQA 77
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2496167637 1315 EKDLGVTRLLDPEDVDVPHPDEKSIITYVSSLYDA 1349
Cdd:cd21312     78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
2114-2574 1.44e-04

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 48.51  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2114 IQKTAEQAKvqveLEGLKKDLDKVSTKTQDIlnspqPSATAPVLRSELELTVQKmdhaymLSSVYLEKLKTVEMVIRNTq 2193
Cdd:TIGR01612  689 IDNTEDKAK----LDDLKSKIDKEYDKIQNM-----ETATVELHLSNIENKKNE------LLDIIVEIKKHIHGEINKD- 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2194 gAEGVLKQYENCLREVHTVPNDVK----EVETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAVSDKMSRVHSERDAELD 2269
Cdd:TIGR01612  753 -LNKILEDFKNKEKELSNKINDYAkekdELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIF 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2270 QHRQHLSSLQDRwkaVFTQIDLRQRELDQLGRQLGYYRESYDWLIRWI-ADAKQRQENIQAVPITDSKTLKEQLAKE--- 2345
Cdd:TIGR01612  832 KIINEMKFMKDD---FLNKVDKFINFENNCKEKIDSEHEQFAELTNKIkAEISDDKLNDYEKKFNDSKSLINEINKSiee 908
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2346 ------------------KKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVE-PLTSplKKTKLD------ 2400
Cdd:TIGR01612  909 eyqnintlkkvdeyikicENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDnTLID--KINELDkafkda 986
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2401 -----SASDNIIQEYV-------------TLRTRYSELMTLTSQYIKFITDTQRRLEDEEMA---------DAQQKQIER 2453
Cdd:TIGR01612  987 slndyEAKNNELIKYFndlkanlgknkenMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAihtsiyniiDEIEKEIGK 1066
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2454 EMTVLQQTFLTEKEMLLK-----KEKL----IEDEKKKLESQFEEEIKK----AKALKDEQDRQRQQMEEEKLKLKATMD 2520
Cdd:TIGR01612 1067 NIELLNKEILEEAEINITnfneiKEKLkhynFDDFGKEENIKYADEINKikddIKNLDQKIDHHIKALEEIKKKSENYID 1146
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2496167637 2521 ---AALNK-QKEAEKDILNKQKEmqELERK------RLEQERVLADENQKLREKLQQMEEAQKS 2574
Cdd:TIGR01612 1147 eikAQINDlEDVADKAISNDDPE--EIEKKienivtKIDKKKNIYDEIKKLLNEIAEIEKDKTS 1208
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2432-2594 1.50e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2432 TDTQRRLEDEEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLEsQFEEEIKKAKALKDEQDRQRQQMEEE 2511
Cdd:TIGR02168  705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT-ELEAEIEELEERLEEAEEELAEAEAE 783
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2512 KLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQKSTLITEKHVTVVETVLNG 2591
Cdd:TIGR02168  784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863

                   ...
gi 2496167637 2592 QNA 2594
Cdd:TIGR02168  864 LEE 866
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1705-1798 1.59e-04

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 43.85  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1705 LHAFVSAATKELMWLNDKEEEEVNYDWSDKNTNMTVKKENYSGLMRELELREKKVNDIQAMGDRLVKDGHPGKKTVEAFT 1784
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERL 82
                           90
                   ....*....|....
gi 2496167637 1785 AALQTQWSWILQLC 1798
Cdd:pfam00435   83 EELNERWEQLLELA 96
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
2415-2576 1.69e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 48.25  E-value: 1.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2415 TRYSELMTLTSQYIKFITDTQRRLEDE--EMADAQQkQIEREMTVLQQTFLTEKEM----------LLKKEKLIEDEKKK 2482
Cdd:pfam01576    1 TRQEEEMQAKEEELQKVKERQQKAESElkELEKKHQ-QLCEEKNALQEQLQAETELcaeaeemrarLAARKQELEEILHE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2483 LESQFEEEIKKAKALKDEQDRQRQQM--------EEE----KLKL-KATMDAalnKQKEAEKDIL------NK-QKEMQE 2542
Cdd:pfam01576   80 LESRLEEEEERSQQLQNEKKKMQQHIqdleeqldEEEaarqKLQLeKVTTEA---KIKKLEEDILlledqnSKlSKERKL 156
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2496167637 2543 LERKRLEQERVLADENQKLR--EKLQQMEEAQKSTL 2576
Cdd:pfam01576  157 LEERISEFTSNLAEEEEKAKslSKLKNKHEAMISDL 192
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2215-2354 1.81e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2215 DVKEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKAsavsdkmsrvhserDAELDQHRQHLSSLQDRWKAVFTQIDLRQR 2294
Cdd:COG4913    662 DVASAEREIAELEAELERLDASSDDLAALEEQLEEL--------------EAELEELEEELDELKGEIGRLEKELEQAEE 727
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2295 ELDQLGRQLGYYRESYDWLIRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEK 2354
Cdd:COG4913    728 ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
2123-2579 1.88e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 47.89  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2123 VQVELEGLKKDLDKVSTKTQDILN------SPQP----------SATAPVLRSELELTVQKMDHAYMLSSVYLEKLKTV- 2185
Cdd:pfam10174    8 LQRENELLRRELDIKESKLGSSMNsiktfwSPELkkeralrkeeAARISVLKEQYRVTQEENQHLQLTIQALQDELRAQr 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2186 --------EMVIRNTQGAEGVLKQY---ENCLREVHTVPNDVKEVETYRTNLKKMRAEAEAEQPVFDSLEEELKK----- 2249
Cdd:pfam10174   88 dlnqllqqDFTTSPVDGEDKFSTPElteENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKlleml 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2250 -ASAVSDKMSRVHSERDAELDQHRQHLSSLQdrwkavfTQIDLRQRELDQLGRQLgyyresydwlirwiadakQRQENIQ 2328
Cdd:pfam10174  168 qSKGLPKKSGEEDWERTRRIAEAEMQLGHLE-------VLLDQKEKENIHLREEL------------------HRRNQLQ 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2329 AVPiTDSKTLKEQL-AKEKKLLEEIEKNKDKVDECQ--KYAKAYIDIIKDYEL-QLVAYKAQvepltSPLKKTKLDSASD 2404
Cdd:pfam10174  223 PDP-AKTKALQTVIeMKDTKISSLERNIRDLEDEVQmlKTNGLLHTEDREEEIkQMEVYKSH-----SKFMKNKIDQLKQ 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2405 NIIQ---EYVTLRTRyseLMTLTSQ------YIKFITDT-----QR-------------RLEDEE-MADAQQKQIeREMT 2456
Cdd:pfam10174  297 ELSKkesELLALQTK---LETLTNQnsdckqHIEVLKESltakeQRaailqtevdalrlRLEEKEsFLNKKTKQL-QDLT 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2457 VLQQTFLTE----KEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQrQQMEEEKlklkATMDAALNKQKEA--- 2529
Cdd:pfam10174  373 EEKSTLAGEirdlKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERV-KSLQTDS----SNTDTALTTLEEAlse 447
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2496167637 2530 -EKDILNKQKEMQELERKRLEQERVLADENQKLREKL--QQMEEAQKSTLITE 2579
Cdd:pfam10174  448 kERIIERLKEQREREDRERLEELESLKKENKDLKEKVsaLQPELTEKESSLID 500
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
2478-2567 2.00e-04

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 45.21  E-value: 2.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2478 DEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEkdILNKQKEMQELERKRLEQervLADE 2557
Cdd:COG2825     39 PEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLSEEERQKKERE--LQKKQQELQRKQQEAQQD---LQKR 113
                           90
                   ....*....|
gi 2496167637 2558 NQKLREKLQQ 2567
Cdd:COG2825    114 QQELLQPILE 123
PLEC smart00250
Plectin repeat;
3387-3418 2.06e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 41.31  E-value: 2.06e-04
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2496167637  3387 KLLSAEKAVTGYKDPFTGKTISLFEAMQKDLI 3418
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
2406-2574 2.19e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 46.55  E-value: 2.19e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  2406 IIQEYVTLRTRYSELMTLTSQYIKfitdTQRRLEDEEM--------ADAQQKQIEREMTVLQQtfltEKEMLLKKEKLIE 2477
Cdd:smart00787  100 LFKEYFSASPDVKLLMDKQFQLVK----TFARLEAKKMwyewrmklLEGLKEGLDENLEGLKE----DYKLLMKELELLN 171
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  2478 DEKKKLESQFEEEIKKAKALKdeqdrqrqQMEEEKLKLKAT-MDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLAD 2556
Cdd:smart00787  172 SIKPKLRDRKDALEEELRQLK--------QLEDELEDCDPTeLDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIED 243
                           170
                    ....*....|....*...
gi 2496167637  2557 ENQKLREKLQQMEEAQKS 2574
Cdd:smart00787  244 LTNKKSELNTEIAEAEKK 261
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
2476-2571 2.37e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 43.75  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2476 IEDEKKKLES---QFEEEIKKAK-ALKDEQDR------QRQQMEEEKLKLKATMDAAlnkqkEAEKDILNKQKEMQELER 2545
Cdd:pfam20492    4 AEREKQELEErlkQYEEETKKAQeELEESEETaeeleeERRQAEEEAERLEQKRQEA-----EEEKERLEESAEMEAEEK 78
                           90       100
                   ....*....|....*....|....*.
gi 2496167637 2546 KRLEQERVLADenqklrEKLQQMEEA 2571
Cdd:pfam20492   79 EQLEAELAEAQ------EEIARLEEE 98
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
2398-2565 2.38e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.07  E-value: 2.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2398 KLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDeemADAQQKQIEREMTVLQQ----------TFLTEKE 2467
Cdd:COG1579     14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED---LEKEIKRLELEIEEVEArikkyeeqlgNVRNNKE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2468 ML-LKKEklIEDEKKKLeSQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDIlnkQKEMQELERK 2546
Cdd:COG1579     91 YEaLQKE--IESLKRRI-SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL---EAELEELEAE 164
                          170
                   ....*....|....*....
gi 2496167637 2547 RLEQERVLADENQKLREKL 2565
Cdd:COG1579    165 REELAAKIPPELLALYERI 183
PLEC smart00250
Plectin repeat;
2692-2725 2.51e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.93  E-value: 2.51e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2496167637  2692 LLEAQAATGYMLDPINNHKLSVNEAVKEGLIGPE 2725
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
2335-2570 2.57e-04

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 47.26  E-value: 2.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2335 SKTLKEQLAKEKKlleEIEKNKDKVDEcqkyAKAYIDIIKDYElQLVAYKAQVEPLTS-PLKKTKLDSASDNIIQEYVTL 2413
Cdd:COG5185    277 SKRLNENANNLIK---QFENTKEKIAE----YTKSIDIKKATE-SLEEQLAAAEAEQElEESKRETETGIQNLTAEIEQG 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2414 RTRYSELMTLTSQYIKFITDTQRRLEDEEMADAQQKQIEremtvlqqtflTEKEMLLKKEKLIEDEKKKLESQFEEEIKk 2493
Cdd:COG5185    349 QESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIE-----------STKESLDEIPQNQRGYAQEILATLEDTLK- 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2494 akalkdEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQE-----RVLADENQKLREKLQQM 2568
Cdd:COG5185    417 ------AADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAydeinRSVRSKKEDLNEELTQI 490

                   ..
gi 2496167637 2569 EE 2570
Cdd:COG5185    491 ES 492
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
2262-2546 3.00e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 46.06  E-value: 3.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2262 SERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWLIRWIADAKQRQENIQAvpitDSKTLKEQ 2341
Cdd:COG1340     18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE----KLNELREE 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2342 LAKEKKLLEEIEKNKDKVDECQKyakayidiikdyELQLVAYKAQVEPLTspLKKTKldsasdNIIQEYVTLRTRYSELM 2421
Cdd:COG1340     94 LDELRKELAELNKAGGSIDKLRK------------EIERLEWRQQTEVLS--PEEEK------ELVEKIKELEKELEKAK 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2422 TLTSQYIKfITDTQRRLEDEEMadaQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLES---QFEEEIKKAKALK 2498
Cdd:COG1340    154 KALEKNEK-LKELRAELKELRK---EAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADElhkEIVEAQEKADELH 229
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2499 DEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKE--MQELERK 2546
Cdd:COG1340    230 EEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEeiFEKLKKG 279
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
1117-1194 3.29e-04

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: 43.03  E-value: 3.29e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2496167637 1117 KKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTlLSERDVARSVRLPRekgrmrfHKLQNVQIALDFL 1194
Cdd:cd21221      3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEK-LEVPEVAQSEEGQK-------QKLAVVLACVNFL 72
PRK01156 PRK01156
chromosome segregation protein; Provisional
2201-2567 3.43e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 46.82  E-value: 3.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2201 QYENCLREVHTVPNDVKEVETYRTN----------LKKMRAEAEAEQP-VFDSLEEELKKASAVSDKMSRVHSERDAELD 2269
Cdd:PRK01156   340 DYIKKKSRYDDLNNQILELEGYEMDynsylksiesLKKKIEEYSKNIErMSAFISEILKIQEIDPDAIKKELNEINVKLQ 419
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2270 QHRQHLSSLQDRWKAVFTQIDLRQRELDQL---------GRQLGyYRESYDWLIRWIADAKQRQENIQAVPItDSKTLKE 2340
Cdd:PRK01156   420 DISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcGTTLG-EEKSNHIINHYNEKKSRLEEKIREIEI-EVKDIDE 497
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2341 QLAKEKKLLEEIEKnkdkvDECQKYAKAYiDIIKDYELQLVAYKAQVEPLT-SPLKKTKLDSASDNIIQEyvTLRTRYSE 2419
Cdd:PRK01156   498 KIVDLKKRKEYLES-----EEINKSINEY-NKIESARADLEDIKIKINELKdKHDKYEEIKNRYKSLKLE--DLDSKRTS 569
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2420 LMTLTSQYIKFITDTQRRLEDEemADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQfeeeIKKAKALKD 2499
Cdd:PRK01156   570 WLNALAVISLIDIETNRSRSNE--IKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNK----YNEIQENKI 643
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2496167637 2500 EQDRQRQQMEEEKlKLKATMDAALNKQKEAEKDILNKQKEMQELeRKRLEQERVLADENQKLREKLQQ 2567
Cdd:PRK01156   644 LIEKLRGKIDNYK-KQIAEIDSIIPDLKEITSRINDIEDNLKKS-RKALDDAKANRARLESTIEILRT 709
Rabaptin pfam03528
Rabaptin;
2225-2516 3.51e-04

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 46.64  E-value: 3.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2225 NLKKMRAEAEAEQPVFDSLEEELKKASAVSDKMSRVH--SER------DAELDQHRQHLSSLQDRWKAVFTQIDLR-QRE 2295
Cdd:pfam03528   48 DLKRQNAVLQEAQVELDALQNQLALARAEMENIKAVAtvSENtkqeaiDEVKSQWQEEVASLQAIMKETVREYEVQfHRR 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2296 LDQLGRQLGYYRESYDwliRWIADAKQRQENIQAVPITDSKTLKEQLAKEK------KLLEEIEKNKDKVDECQkyakay 2369
Cdd:pfam03528  128 LEQERAQWNQYRESAE---REIADLRRRLSEGQEEENLEDEMKKAQEDAEKlrsvvmPMEKEIAALKAKLTEAE------ 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2370 iDIIKDYElqlvayKAQVEPLTSPLKKTKldSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEMadaQQK 2449
Cdd:pfam03528  199 -DKIKELE------ASKMKELNHYLEAEK--SCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQ---QHN 266
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2496167637 2450 QIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKakalKDEQDRQRQQMEEEKLKLK 2516
Cdd:pfam03528  267 QLKHTWQKANDQFLESQRLLMRDMQRMESVLTSEQLRQVEEIKK----KDQEEHKRARTHKEKETLK 329
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
2275-2577 3.59e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 47.14  E-value: 3.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2275 LSSLQDRWKAVFTQIDLRQRELDQLGRQLGYyresydwliRWIADAKQRQENIQAVPiTDSKTLKEQLAKEKKLLEEIEk 2354
Cdd:pfam12128  260 LSHLHFGYKSDETLIASRQEERQETSAELNQ---------LLRTLDDQWKEKRDELN-GELSAADAAVAKDRSELEALE- 328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2355 nkdkvDECQKYAKAYIDIIKDYELQLVAYKAQVEPLTSPLKKtkLDSASDNIIQEYVTLRTRYSElmtltsQYIKFITDT 2434
Cdd:pfam12128  329 -----DQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA--LTGKHQDVTAKYNRRRSKIKE------QNNRDIAGI 395
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2435 QRRLEDEEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEklIEDEKKKLESQFEEeikkakaLKDEQDrQRQQMEEEKLK 2514
Cdd:pfam12128  396 KDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLE--FNEEEYRLKSRLGE-------LKLRLN-QATATPELLLQ 465
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2496167637 2515 LKAT---MDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLRE------KLQQMEEAQKSTLI 2577
Cdd:pfam12128  466 LENFderIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEErqsaldELELQLFPQAGTLL 537
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
1111-1231 3.66e-04

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


Pssm-ID: 409178  Cd Length: 118  Bit Score: 43.05  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1111 ERDRVQKKTFTKWVNKHLIKSqrHVTDLYEDLRDGHNLISLLEVlsgdtllserdvarsVRLPREKGRM----------R 1180
Cdd:cd21329      2 EGESSEERTFRNWMNSLGVNP--YVNHLYSDLCDALVIFQLYEM---------------TRVPVDWGHVnkppypalggN 64
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2496167637 1181 FHKLQNVQIALDFLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQVS 1231
Cdd:cd21329     65 MKKIENCNYAVELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
2317-2532 3.69e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 3.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2317 IADAKQRQENIQAvpitDSKTLKEQLakeKKLLEEIEKNKDKVDEcqkyAKAYIDIIKDyelQLVAYKAQVEPLTSPLKK 2396
Cdd:COG3883     18 IQAKQKELSELQA----ELEAAQAEL---DALQAELEELNEEYNE----LQAELEALQA---EIDKLQAEIAEAEAEIEE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2397 TKlDSASDNIIQEYVTLRTRYSELMTLTSQ----------YIKFITDTQRRLEDEemADAQQKQIEREMTVLQQtfltEK 2466
Cdd:COG3883     84 RR-EELGERARALYRSGGSVSYLDVLLGSEsfsdfldrlsALSKIADADADLLEE--LKADKAELEAKKAELEA----KL 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2496167637 2467 EMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKD 2532
Cdd:COG3883    157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1118-1249 3.95e-04

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 46.47  E-value: 3.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1118 KTFTKWVNKHLIKSQrhVTDLYEDLRDGhnlISLLEVLSGDTLLSERDVARSVRLPREKGRM-RFHKLQNVQIALDFLRH 1196
Cdd:COG5069    382 RVFTFWLNSLDVSPE--ITNLFGDLRDQ---LILLQALSKKLMPMTVTHKLVKKQPASGIEEnRFKAFENENYAVDLGIT 456
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2496167637 1197 RQVKLVNIRNDDIADGNpKLTLGLIW-------TIILHFQVSSS--ISDIQVNGQSEDMSAK 1249
Cdd:COG5069    457 EGFSLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKDGcgLSDSDLCAWLGSLGLK 517
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
2441-2573 4.20e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 45.95  E-value: 4.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2441 EEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQfeeEIKKAKALKDEQDRQRQQMEEEKLKlKATMD 2520
Cdd:PRK09510    69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ---EQKKQAEEAAKQAALKQKQAEEAAA-KAAAA 144
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2496167637 2521 AALnkQKEAEKDILNKQKEMQELERKRLEQERvlADENQKLREKLQQMEEAQK 2573
Cdd:PRK09510   145 AKA--KAEAEAKRAAAAAKKAAAEAKKKAEAE--AAKKAAAEAKKKAEAEAAA 193
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2338-2566 4.28e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 4.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2338 LKEQLAKEKkllEEIEKNKDKVDEcqkyakAYIDIIKDYELQLVAYKAQVEPLTSplKKTKLDSASdniiQEYVTLRTRY 2417
Cdd:COG4717     47 LLERLEKEA---DELFKPQGRKPE------LNLKELKELEEELKEAEEKEEEYAE--LQEELEELE----EELEELEAEL 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2418 SELMTLTSQYikfitdtqRRLEDEEMADAQQKQIEREMTVLQQtfltEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKAL 2497
Cdd:COG4717    112 EELREELEKL--------EKLLQLLPLYQELEALEAELAELPE----RLEELEERLEELRELEEELEELEAELAELQEEL 179
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2496167637 2498 KDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERK--RLEQERVLADENQKLREKLQ 2566
Cdd:COG4717    180 EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEleQLENELEAAALEERLKEARL 250
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2390-2580 4.34e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.89  E-value: 4.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2390 LTSPLKKTKLDSASdNIIQEYVTLRTRYSELMTLTSQYIKFITDT-----QRRLEDEEMADA----QQKQIERE----MT 2456
Cdd:pfam02463  149 MMKPERRLEIEEEA-AGSRLKRKKKEALKKLIEETENLAELIIDLeelklQELKLKEQAKKAleyyQLKEKLELeeeyLL 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2457 VLQQTFLTEKEMLLKKEKLI----EDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEK- 2531
Cdd:pfam02463  228 YLDYLKLNEERIDLLQELLRdeqeEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLEr 307
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2496167637 2532 --DILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQKSTLITEK 2580
Cdd:pfam02463  308 rkVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE 358
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
2320-2563 4.66e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 46.10  E-value: 4.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2320 AKQRQENIQAVPITDSKTLKEQLAKE---KKLLEEIEKNKDKVDECQ-KYAKAyidiikdyELQLVAYKAQVEPLTSPLK 2395
Cdd:pfam15709  293 IDGRSSPTQTFVVTGNMESEEERSEEdpsKALLEKREQEKASRDRLRaERAEM--------RRLEVERKRREQEEQRRLQ 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2396 KTKLDSAsDNIIQEYVTLRTRYSELMTLTSQYIKfitDTQRRLEDEEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKL 2475
Cdd:pfam15709  365 QEQLERA-EKMREELELEQQRRFEEIRLRKQRLE---EERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQ 440
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2476 IEDEKKKLES---QFEEEIKkakaLKDEQDRQRQQMEEEKLKLKAtmdaalNKQKEAEKdilnKQKEMQELERKRLEQER 2552
Cdd:pfam15709  441 QEEAERAEAEkqrQKELEMQ----LAEEQKRLMEMAEEERLEYQR------QKQEAEEK----ARLEAEERRQKEEEAAR 506
                          250
                   ....*....|.
gi 2496167637 2553 VLADENQKLRE 2563
Cdd:pfam15709  507 LALEEAMKQAQ 517
PLEC smart00250
Plectin repeat;
2731-2761 5.19e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.16  E-value: 5.19e-04
                            10        20        30
                    ....*....|....*....|....*....|.
gi 2496167637  2731 LSAEKAVVGYKDPYSGGKISVFEAMKKGLMD 2761
Cdd:smart00250    4 LEAQSAIGGIIDPETGQKLSVEEALRRGLID 34
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2242-2581 5.22e-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: 46.60  E-value: 5.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2242 SLEEELKKASAVSDKMSRVHSERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQlgyyresydwlirwIADAK 2321
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE--------------EEKLK 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2322 QRQENIQAvpitdsktlkeqlaKEKKLLEEIEKNKDKVDEcqkyakaYIDIIKDYELQLVAYKAQVEPLTsplkktklDS 2401
Cdd:TIGR02169  737 ERLEELEE--------------DLSSLEQEIENVKSELKE-------LEARIEELEEDLHKLEEALNDLE--------AR 787
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2402 ASDNIIQEYVtlrtryselmtltsQYIKFITDTQRRLEdeemadAQQKQIEREMTVLQQtfltekemllkKEKLIEDEKK 2481
Cdd:TIGR02169  788 LSHSRIPEIQ--------------AELSKLEEEVSRIE------ARLREIEQKLNRLTL-----------EKEYLEKEIQ 836
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2482 KLESQFEEeikkakaLKDEQDRQRQQMEEEKLKLKatmdaalnkqkEAEKDILNKQKEMQELE--RKRLEQERvlaDENQ 2559
Cdd:TIGR02169  837 ELQEQRID-------LKEQIKSIEKEIENLNGKKE-----------ELEEELEELEAALRDLEsrLGDLKKER---DELE 895
                          330       340
                   ....*....|....*....|..
gi 2496167637 2560 KLREKLQQMEEAQKSTLITEKH 2581
Cdd:TIGR02169  896 AQLRELERKIEELEAQIEKKRK 917
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
4239-4270 5.62e-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: 5.62e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2496167637 4239 IAGILDTETLEKVSVTEAMHRNLVDNITGQRL 4270
Cdd:pfam00681    8 TGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2447-2580 5.71e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 5.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2447 QQKQIEREMTVLQQTFLTEKEMLLKKEKLIE-----DEKKKLESQFEEEIKKAKALKD------EQDRQRQQMEEEKLKL 2515
Cdd:COG4717     96 ELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEELEErleelrELEEELEELEAELAEL 175
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2496167637 2516 KATMDAALNKQKEAEKDILNK-QKEMQELERKRLEQERVLADENQKLREKLQQMEEAQKSTLITEK 2580
Cdd:COG4717    176 QEELEELLEQLSLATEEELQDlAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
PLEC smart00250
Plectin repeat;
3020-3052 5.90e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 40.16  E-value: 5.90e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2496167637  3020 LEAQAGTGYVVDPVHNQHYTVDEAVKAGVVGPE 3052
Cdd:smart00250    4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2441-2581 6.13e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.12  E-value: 6.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2441 EEMADAQQKQIEREMTVLQQtFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMD 2520
Cdd:pfam02463  148 AMMKPERRLEIEEEAAGSRL-KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYL 226
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2496167637 2521 AALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQKSTLITEKH 2581
Cdd:pfam02463  227 LYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEE 287
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
2341-2523 6.53e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.53  E-value: 6.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2341 QLAKE-KKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEPLTSPLKK--TKLDSASDNiiqeyvtlrtry 2417
Cdd:COG1579     21 RLEHRlKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeEQLGNVRNN------------ 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2418 SELMTLTSQyIKFITDTQRRLEDEEMAdaqqkqieremtvlqqtFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKAL 2497
Cdd:COG1579     89 KEYEALQKE-IESLKRRISDLEDEILE-----------------LMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
                          170       180
                   ....*....|....*....|....*.
gi 2496167637 2498 KDEQDRQRQQMEEEKLKLKATMDAAL 2523
Cdd:COG1579    151 LAELEAELEELEAEREELAAKIPPEL 176
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
2053-2567 6.91e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 46.19  E-value: 6.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2053 DSLLRSMEKGLVVRHKGQQDETLCKnyisEVKDLRLRIEDCEARTVARIRKPVEKEPLKECIQKTAEQAKVQVELEGLKK 2132
Cdd:TIGR00606  477 DQELRKAERELSKAEKNSLTETLKK----EVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR 552
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2133 DL-----DKVSTKTQDILNSPQPSATAPVLRSELELTVQKMDHAymlsSVYLEKLKTVEMVIRNT-QGAEGVLKQYENCL 2206
Cdd:TIGR00606  553 KIksrhsDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKL----NKELASLEQNKNHINNElESKEEQLSSYEDKL 628
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2207 REVHTVPNDVKEVETYRTNLKKM---RAEAEAEQPVFDSLEEELKKASA----VSDKMSRVHSERDAELDQHRQHLSSLQ 2279
Cdd:TIGR00606  629 FDVCGSQDEESDLERLKEEIEKSskqRAMLAGATAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRLAP 708
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2280 DRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWLIRWIADAKQRQENIQavpiTDSKTLKEQLAKEKKLLEEIEKNKDKV 2359
Cdd:TIGR00606  709 DKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVN----RDIQRLKNDIEEQETLLGTIMPEEESA 784
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2360 DECQkyakAYIDIIKDYELQLVAYKAQVEPLTSPLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLE 2439
Cdd:TIGR00606  785 KVCL----TDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQ 860
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2440 DEEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQM-EEEKLKLKAT 2518
Cdd:TIGR00606  861 HLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIsSKETSNKKAQ 940
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2496167637 2519 MDAALNKQKEAE-----KDILNKQKEMQELERKRLEQE----RVLADENQKLREKLQQ 2567
Cdd:TIGR00606  941 DKVNDIKEKVKNihgymKDIENKIQDGKDDYLKQKETElntvNAQLEECEKHQEKINE 998
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
2337-2586 7.06e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 45.60  E-value: 7.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2337 TLKEQLAKEKKLLEEIeknKDKVDECQKYAKAYIDIIKD---------Y-------ELQLVAYKAQVEPLTSPLKKTKLD 2400
Cdd:PRK04778   202 QLEEELAALEQIMEEI---PELLKELQTELPDQLQELKAgyrelveegYhldhldiEKEIQDLKEQIDENLALLEELDLD 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2401 SASDNI--IQEyvTLRTRYsELMTLTSQYIKFITDTQRRL-EDEEMADAQQKQIEREMTVLQQTF-LTEKEmlLKKEKLI 2476
Cdd:PRK04778   279 EAEEKNeeIQE--RIDQLY-DILEREVKARKYVEKNSDTLpDFLEHAKEQNKELKEEIDRVKQSYtLNESE--LESVRQL 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2477 EDEKKKLESQFE---EEIKKAKA----LKDEQDRQRQQM---EEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELER- 2545
Cdd:PRK04778   354 EKQLESLEKQYDeitERIAEQEIayseLQEELEEILKQLeeiEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRy 433
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2496167637 2546 --KR---------LEQERVLADENQKLREKLQQ----MEEAQKSTLITEKHVTVVE 2586
Cdd:PRK04778   434 leKSnlpglpedyLEMFFEVSDEIEALAEELEEkpinMEAVNRLLEEATEDVETLE 489
mukB PRK04863
chromosome partition protein MukB;
2216-2570 7.23e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.10  E-value: 7.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2216 VKEVETYRTNLKKMRAEAEAEQPVFDSLEEELkkaSAVSDKMSRVH-SERDAE-LDQHRQHLSSLQDRWKAVFTQIDLRQ 2293
Cdd:PRK04863   299 RRQLAAEQYRLVEMARELAELNEAESDLEQDY---QAASDHLNLVQtALRQQEkIERYQADLEELEERLEEQNEVVEEAD 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2294 RELDQLGRQLGYYRESYDWLIRWIADAKQRQENIQavpitdSKTLKEQLAKEkkLLEEIEKNKDKVDECQKYAKAYIDii 2373
Cdd:PRK04863   376 EQQEENEARAEAAEEEVDELKSQLADYQQALDVQQ------TRAIQYQQAVQ--ALERAKQLCGLPDLTADNAEDWLE-- 445
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2374 kdyelqlvAYKAQVEPLTSPLK--KTKLDSASDniiqeyvtLRTRYSELMTLT---------SQYIKFITDTQRRLEDEE 2442
Cdd:PRK04863   446 --------EFQAKEQEATEELLslEQKLSVAQA--------AHSQFEQAYQLVrkiagevsrSEAWDVARELLRRLREQR 509
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2443 MADAQQKQIEREMTVLQQTF---------LTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKL 2513
Cdd:PRK04863   510 HLAEQLQQLRMRLSELEQRLrqqqraerlLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLE 589
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2514 KLKA-------------TMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEE 2570
Cdd:PRK04863   590 QLQAriqrlaarapawlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDE 659
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
2446-2573 7.42e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.53  E-value: 7.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2446 AQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLeSQFEEEIKKAKALKdEQDRQRQ------------QMEEEKL 2513
Cdd:COG1579     24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-KRLELEIEEVEARI-KKYEEQLgnvrnnkeyealQKEIESL 101
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2514 KLKatMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQK 2573
Cdd:COG1579    102 KRR--ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
338-613 7.76e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 45.68  E-value: 7.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  338 IKATAESDGVQSHVGITTAAVQSTTvlTAPITKKTvnkdviEEKAKEAIAHEVKSTELKSTVETPAKMKPQAVATVASVQ 417
Cdd:pfam05109  405 ITRTATNATTTTHKVIFSKAPESTT--TSPTLNTT------GFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSP 476
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  418 ESYDTNDTSTPVITKPVKEEKAKKKKATEESVKLAEVKIPGQEKATKTDKVSVPTKAKPGSTTGKPVVSDNVETPKvvqe 497
Cdd:pfam05109  477 TPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPT---- 552
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  498 PSDATPTSVNISEKPKSEV--LSKAAESSILEVTTSVRTGLTSSRTNAevvQVATDKTTIKEKRTTQDVMTlthvekdge 575
Cdd:pfam05109  553 PNATSPTPAVTTPTPNATIptLGKTSPTSAVTTPTPNATSPTVGETSP---QANTTNHTLGGTSSTPVVTS--------- 620
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2496167637  576 iapeDPKDPTPAPPSVQEDATTYHKSQNDVGIEAVKET 613
Cdd:pfam05109  621 ----PPKNATSAVTTGQHNITSSSTSSMSLRPSSISET 654
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
2442-2580 8.03e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.22  E-value: 8.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2442 EMADAQQKQIEREMTVLQQtflteKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDA 2521
Cdd:TIGR02794   58 QKKPAAKKEQERQKKLEQQ-----AEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEA 132
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2496167637 2522 ALNKQKEAEKDILNKQKEMQELERKRLEQErvlADENQKLREKLQQMEEAQKSTLITEK 2580
Cdd:TIGR02794  133 KAKAEAEAERKAKEEAAKQAEEEAKAKAAA---EAKKKAEEAKKKAEAEAKAKAEAEAK 188
PLEC smart00250
Plectin repeat;
2766-2802 9.18e-04

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.39  E-value: 9.18e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2496167637  2766 IRVLEAQLATGGIIDPLNSHRVPNEIAYKQGQYDAEM 2802
Cdd:smart00250    1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
2334-2567 9.34e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.40  E-value: 9.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2334 DSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYI---------------DIIK---DYELQLVAYKAQVEPLTSPLK 2395
Cdd:TIGR04523  111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIkkkekeleklnnkynDLKKqkeELENELNLLEKEKLNIQKNID 190
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2396 KTKLDSASDNI--------IQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEmadAQQKQIEREMTVLQQTFLTEKE 2467
Cdd:TIGR04523  191 KIKNKLLKLELllsnlkkkIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKT---TEISNTQTQLNQLKDEQNKIKK 267
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2468 MLLKKEKLIEDEKKKLeSQFEEEIKKakaLKDEQDRQRQQMEEEKLK-LKATMDAALNKQKEAEKDILNKQKEMQELERK 2546
Cdd:TIGR04523  268 QLSEKQKELEQNNKKI-KELEKQLNQ---LKSEISDLNNQKEQDWNKeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
                          250       260
                   ....*....|....*....|....
gi 2496167637 2547 --RLEQERV-LADENQKLREKLQQ 2567
Cdd:TIGR04523  344 isQLKKELTnSESENSEKQRELEE 367
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2047-2553 9.34e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 9.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2047 KST-QHF--DSLLRSMEKGLVVRHKGQQDETlcKNYISEVKDLRLRIEDCEARTVARIRKPVEKEplkeciQKTAEQAKV 2123
Cdd:COG4717     36 KSTlLAFirAMLLERLEKEADELFKPQGRKP--ELNLKELKELEEELKEAEEKEEEYAELQEELE------ELEEELEEL 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2124 QVELEGLKKDLDKVSTKTQDILNSPQPSAtapvLRSELELTVQKMDHAymlssvyLEKLKTVEMVIRNTQGAEGVLKQYE 2203
Cdd:COG4717    108 EAELEELREELEKLEKLLQLLPLYQELEA----LEAELAELPERLEEL-------EERLEELRELEEELEELEAELAELQ 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2204 NCLREVHTVPN--DVKEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAVSDKMsrvhsERDAELDQHRQHLSSLQDR 2281
Cdd:COG4717    177 EELEELLEQLSlaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL-----ENELEAAALEERLKEARLL 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2282 WKAVFTQIDLRQRELDQLGR----------QLGYYRESYDWLIRWIADAKQRQENIQAVPITDS---KTLKEQLAK---- 2344
Cdd:COG4717    252 LLIAAALLALLGLGGSLLSLiltiagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEEleeEELEELLAAlglp 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2345 EKKLLEEIEKNKDKVDECQKYAKAYIDIIKdyELQLVAYKAQVEPLtspLKKTKLDSASD-----NIIQEYVTLRTRYSE 2419
Cdd:COG4717    332 PDLSPEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIAAL---LAEAGVEDEEElraalEQAEEYQELKEELEE 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2420 LMTLTSQYIKFITDTQRRLEDEEMADAQQkQIEREMTVLQQtfltEKEMLLKKEKLIEDEKKKLESqfEEEIKKAKALKD 2499
Cdd:COG4717    407 LEEQLEELLGELEELLEALDEEELEEELE-ELEEELEELEE----ELEELREELAELEAELEQLEE--DGELAELLQELE 479
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2496167637 2500 EQDRQRQQMEEEKLKLKATmdaalnkqkeaeKDILNKqkemqelERKRLEQERV 2553
Cdd:COG4717    480 ELKAELRELAEEWAALKLA------------LELLEE-------AREEYREERL 514
PTZ00121 PTZ00121
MAEBL; Provisional
2436-2573 1.04e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2436 RRLEDEEMADAQQKQIE----REMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAK-ALKDEQDRQR----- 2505
Cdd:PTZ00121  1170 RKAEDAKKAEAARKAEEvrkaEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEeAKKDAEEAKKaeeer 1249
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2496167637 2506 -----QQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQK 2573
Cdd:PTZ00121  1250 nneeiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK 1322
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
2429-2584 1.26e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 45.07  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2429 KFITDTQRRLEDEEMADAQQKQIEREMTVLQQTflteKEMLLKKEKLIEDEKKKLES----------------------- 2485
Cdd:pfam05622   94 KEVLELQHRNEELTSLAEEAQALKDEMDILRES----SDKVKKLEATVETYKKKLEDlgdlrrqvklleernaeymqrtl 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2486 QFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALN-----KQKEAEKDILNKQKEmqelerkRLEQER-VLADENQ 2559
Cdd:pfam05622  170 QLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKlefeyKKLEEKLEALQKEKE-------RLIIERdTLRETNE 242
                          170       180
                   ....*....|....*....|....*.
gi 2496167637 2560 KLR-EKLQQMEEAQKSTLITEKHVTV 2584
Cdd:pfam05622  243 ELRcAQLQQAELSQADALLSPSSDPG 268
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2217-2580 1.35e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2217 KEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAVSDKMSRVHSERDAELDQHRQHLSSLQDrwkavfTQIDLRQREL 2296
Cdd:COG1196    421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE------ELAEAAARLL 494
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2297 DQLGRQLGYYRESYDWLIRWIADAKQR-----------------------QENIQAVPITDSKTLKE--QLAKEKKL--- 2348
Cdd:COG1196    495 LLLEAEADYEGFLEGVKAALLLAGLRGlagavavligveaayeaaleaalAAALQNIVVEDDEVAAAaiEYLKAAKAgra 574
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2349 ----LEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEPLTSpLKKTKLDSASDNIIQEYVTLRTRYSElmtlT 2424
Cdd:COG1196    575 tflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL-LGRTLVAARLEAALRRAVTLAGRLRE----V 649
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2425 SQYIKFITDTQRRLEDEEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQ 2504
Cdd:COG1196    650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2505 RQQMEEEKLKLKATMDAALNKQKEAEKDILNK----QKEMQELERKRLEQERV--LA-DENQKLREKLQQMEEaQKSTLI 2577
Cdd:COG1196    730 LEAEREELLEELLEEEELLEEEALEELPEPPDleelERELERLEREIEALGPVnlLAiEEYEELEERYDFLSE-QREDLE 808

                   ...
gi 2496167637 2578 TEK 2580
Cdd:COG1196    809 EAR 811
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
2481-2575 1.45e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2481 KKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQK 2560
Cdd:COG3883    125 SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
                           90
                   ....*....|....*
gi 2496167637 2561 LREKLQQMEEAQKST 2575
Cdd:COG3883    205 LAAAEAAAAAAAAAA 219
Filament pfam00038
Intermediate filament protein;
2340-2571 1.48e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 44.14  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2340 EQLAKEK-KLLEEIEKNKDKVDEC-QKYAKAyIDIIKDYELQLVAYKAQVEPLTspLKKTKLDSASDNIIQEYVTLRTRY 2417
Cdd:pfam00038   64 DTLTVERaRLQLELDNLRLAAEDFrQKYEDE-LNLRTSAENDLVGLRKDLDEAT--LARVDLEAKIESLKEELAFLKKNH 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2418 SELMTltsqyikfitDTQRRLEDEemadaqqkQIEREMTVLQQTFLTE--KEMLLKKEKLIEDEKKKLESQFEEEIKKAK 2495
Cdd:pfam00038  141 EEEVR----------ELQAQVSDT--------QVNVEMDAARKLDLTSalAEIRAQYEEIAAKNREEAEEWYQSKLEELQ 202
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2496167637 2496 ALKDEQDRQRQQMEEEKLKLKATMDAalnkqKEAEKDILNKQKEmqELERKRLEQERVLADENQKLREKLQQMEEA 2571
Cdd:pfam00038  203 QAAARNGDALRSAKEEITELRRTIQS-----LEIELQSLKKQKA--SLERQLAETEERYELQLADYQELISELEAE 271
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
2476-2567 1.56e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 41.80  E-value: 1.56e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  2476 IEDEKKKLESQFEEEIKKAKALKDEQDRQRqqmeeeklklkATMDAALNKQKeaEKDILNKQKEMQELERK---RLEQER 2552
Cdd:smart00935   23 LEKEFKKRQAELEKLEKELQKLKEKLQKDA-----------ATLSEAAREKK--EKELQKKVQEFQRKQQKlqqDLQKRQ 89
                            90
                    ....*....|....*
gi 2496167637  2553 vlADENQKLREKLQQ 2567
Cdd:smart00935   90 --QEELQKILDKINK 102
PTZ00121 PTZ00121
MAEBL; Provisional
2081-2556 1.56e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2081 SEVKDLRLRIEDCEARTVARIRKPVEKEPLKECIQKTAEQAKvqvELEGLKKDLDKVSTKTQDILNSPQPSATAPVLRSE 2160
Cdd:PTZ00121  1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK---KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2161 LElTVQKMDHAYMLSSvylEKLKTVEMVIR--NTQGAEGVLKQYEnclrEVHTVPNDVKEVETYRT--NLKKMRAEAEAE 2236
Cdd:PTZ00121  1427 AE-EKKKADEAKKKAE---EAKKADEAKKKaeEAKKAEEAKKKAE----EAKKADEAKKKAEEAKKadEAKKKAEEAKKK 1498
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2237 QPVFDSLEEELKKASAV--SDKMSRVHSERDAELDQHRQHLSSLQDRWKA--VFTQIDLRQRELDQLGRQLGYYRESYDW 2312
Cdd:PTZ00121  1499 ADEAKKAAEAKKKADEAkkAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdeLKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2313 LIRWIADAKQ----RQENIQAVPITDSKTLKEQLAKEkklleeiEKNKDKVDECQKYAKayidiIKDYELQLVAYKAQVE 2388
Cdd:PTZ00121  1579 ALRKAEEAKKaeeaRIEEVMKLYEEEKKMKAEEAKKA-------EEAKIKAEELKKAEE-----EKKKVEQLKKKEAEEK 1646
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2389 PLTSPLKKTKLDSasdniiqeyvtlRTRYSELMTLTSQYIKFITDTQRRLEDEEMADAQQKQIEREMTVLQQTFLTEKEM 2468
Cdd:PTZ00121  1647 KKAEELKKAEEEN------------KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2469 LLKKEKLIEDEK------KKLESQFEEEIKKAKALKDEqdrqrqqmEEEKLKLKATMDAALNKQKE--AEKDILNKQKEM 2540
Cdd:PTZ00121  1715 KKKAEELKKAEEenkikaEEAKKEAEEDKKKAEEAKKD--------EEEKKKIAHLKKEEEKKAEEirKEKEAVIEEELD 1786
                          490
                   ....*....|....*.
gi 2496167637 2541 QELERKRLEQERVLAD 2556
Cdd:PTZ00121  1787 EEDEKRRMEVDKKIKD 1802
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2200-2586 1.65e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2200 KQYENCLREVHTVPNDVKEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAVSDKMSRVHSERDAELDQHRQHLSSLQ 2279
Cdd:PRK03918   200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2280 DRWKAVfTQIDLRQRELDQLGRQLGYYRESYDWLIRWIADAKQRQENIQAVpITDSKTLKEQLAKEKKLLEEIEKnkdKV 2359
Cdd:PRK03918   280 EKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER-IKELEEKEERLEELKKKLKELEK---RL 354
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2360 DECQKYAKAYIDIikdyelqlvayKAQVEPLTSpLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLE 2439
Cdd:PRK03918   355 EELEERHELYEEA-----------KAKKEELER-LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2440 DEEMADAQQKQIEREMTVLQQTfLTE---KEMLLKKEKLIEDEKKKLEsQFEEEIKKAKALKDEQDRQRQQmEEEKLKLK 2516
Cdd:PRK03918   423 ELKKAIEELKKAKGKCPVCGRE-LTEehrKELLEEYTAELKRIEKELK-EIEEKERKLRKELRELEKVLKK-ESELIKLK 499
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2517 ATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQKSTLITEKHVTVVE 2586
Cdd:PRK03918   500 ELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELE 569
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
2241-2571 1.87e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.56  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2241 DSLEEELKKASAVSdkmsrvhSERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESydwlIRWIADA 2320
Cdd:COG3096    357 EELTERLEEQEEVV-------EEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQA----VQALEKA 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2321 KQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQ----KYAKAYidiikdyelQLVaykaqvEPLTSPLKK 2396
Cdd:COG3096    426 RALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADaarrQFEKAY---------ELV------CKIAGEVER 490
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2397 TKLDSASDNIIQEYVTLRTRYSELMTLTSQYikfiTDTQRRLEDEEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLI 2476
Cdd:COG3096    491 SQAWQTARELLRRYRSQQALAQRLQQLRAQL----AELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQL 566
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2477 EDekkkLESQFEEEIKKAKALKDEQDRQRQQMEEekLKLKA----TMDAALNKQKEAEKDILNKQKEMQELERKRLEQER 2552
Cdd:COG3096    567 EE----LEEQAAEAVEQRSELRQQLEQLRARIKE--LAARApawlAAQDALERLREQSGEALADSQEVTAAMQQLLERER 640
                          330
                   ....*....|....*....
gi 2496167637 2553 VLADENQKLREKLQQMEEA 2571
Cdd:COG3096    641 EATVERDELAARKQALESQ 659
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
2432-2544 1.88e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.72  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2432 TDTQRRLEDEEmadAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKakaLKDEQDRQRQQMEEE 2511
Cdd:cd16269    194 TEKEKEIEAER---AKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEEREN---LLKEQERALESKLKE 267
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2496167637 2512 KLKLkatmdaalnKQKEAEKDILNKQKEMQELE 2544
Cdd:cd16269    268 QEAL---------LEEGFKEQAELLQEEIRSLK 291
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2081-2570 1.88e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2081 SEVKDLRLRIEDCEARtvaRIRKPVEKEPLKECIQKTAEQakvQVELEGLKKDLDKV-STKTQDILNSPQPSATAPVLRS 2159
Cdd:PRK02224   213 SELAELDEEIERYEEQ---REQARETRDEADEVLEEHEER---REELETLEAEIEDLrETIAETEREREELAEEVRDLRE 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2160 ELELTVQKMDHAymLSSVYLEKL--KTVEMVIRNTQGAEgvlKQYENCLREVHTVPNDV-KEVETYRTNLKKMRAEAEAE 2236
Cdd:PRK02224   287 RLEELEEERDDL--LAEAGLDDAdaEAVEARREELEDRD---EELRDRLEECRVAAQAHnEEAESLREDADDLEERAEEL 361
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2237 QPVFDSLEEELKKA-SAVSDKMSRVhSERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDqlgrqlgyyresydwlir 2315
Cdd:PRK02224   362 REEAAELESELEEArEAVEDRREEI-EELEEEIEELRERFGDAPVDLGNAEDFLEELREERD------------------ 422
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2316 wiaDAKQRQENIQAvpitDSKTLKEQLAKEKKLLEEieknkDKVDECQKYAK--AYIDIIKDYElqlvaykAQVEPLTSP 2393
Cdd:PRK02224   423 ---ELREREAELEA----TLRTARERVEEAEALLEA-----GKCPECGQPVEgsPHVETIEEDR-------ERVEELEAE 483
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2394 LKKTKLDSAS-DNIIQEYVTLRTRYSELMTLTSQyikfITDTQRRLED-EEMADAQQKQIERemtvlqqtfltekemllk 2471
Cdd:PRK02224   484 LEDLEEEVEEvEERLERAEDLVEAEDRIERLEER----REDLEELIAErRETIEEKRERAEE------------------ 541
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2472 keklIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQ---MEEEKLKLKATMDaALNKQKEAEKDILNKQKEMQELeRKRL 2548
Cdd:PRK02224   542 ----LRERAAELEAEAEEKREAAAEAEEEAEEAREEvaeLNSKLAELKERIE-SLERIRTLLAAIADAEDEIERL-REKR 615
                          490       500
                   ....*....|....*....|..
gi 2496167637 2549 EQervLADENQKLREKLQQMEE 2570
Cdd:PRK02224   616 EA---LAELNDERRERLAEKRE 634
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
2230-2574 1.93e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.78  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2230 RAEAEA--EQPVFDSLEEELKKASAVSDKMSRVHSERDAELDQHrqhLSSLQDRWKAVFtQIDLRQRELDQLGRQLGYYR 2307
Cdd:pfam01576  626 RAEAEAreKETRALSLARALEEALEAKEELERTNKQLRAEMEDL---VSSKDDVGKNVH-ELERSKRALEQQVEEMKTQL 701
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2308 ESYDWLIRWIADAKQRQE-NIQAVPITDSKTL--KEQLAKEKK--LLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVA 2382
Cdd:pfam01576  702 EELEDELQATEDAKLRLEvNMQALKAQFERDLqaRDEQGEEKRrqLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKE 781
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2383 YKAQVEPLT----SPLKK-TKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFI----TDTQRRLEDEEMADAQQKQIER 2453
Cdd:pfam01576  782 LEAQIDAANkgreEAVKQlKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLknleAELLQLQEDLAASERARRQAQQ 861
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2454 EMTVLQQTF---LTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEeklklkatmdaaLNKQKEAE 2530
Cdd:pfam01576  862 ERDELADEIasgASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQ------------LTTELAAE 929
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2496167637 2531 KDILNKQKEM-QELERKrleqervladeNQKLREKLQQMEEAQKS 2574
Cdd:pfam01576  930 RSTSQKSESArQQLERQ-----------NKELKAKLQEMEGTVKS 963
PLEC smart00250
Plectin repeat;
3426-3461 2.20e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 38.62  E-value: 2.20e-03
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 2496167637  3426 LLEAQMVSGGIIDPVNSHRVPNDTAYQKNILSKEVA 3461
Cdd:smart00250    3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
PLEC smart00250
Plectin repeat;
3643-3679 2.25e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 38.23  E-value: 2.25e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 2496167637  3643 KQYLYGTGCVAGFT-TDSGSKMSIYQAMKRGFIQPDVA 3679
Cdd:smart00250    1 QRLLEAQSAIGGIIdPETGQKLSVEEALRRGLIDPETG 38
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
2227-2569 2.25e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 44.35  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2227 KKMRAEAEAEQPVFDSLEEELKKASavsdkmsrvhsERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYY 2306
Cdd:pfam05557   69 EALREQAELNRLKKKYLEALNKKLN-----------EKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEEL 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2307 RESYDWLIRWIADAKQRQENIQAvpitDSKTLKEQLAKEKKLLEEIEK-NKDKVdecqkyakayidIIKDYELQLvaykA 2385
Cdd:pfam05557  138 QERLDLLKAKASEAEQLRQNLEK----QQSSLAEAEQRIKELEFEIQSqEQDSE------------IVKNSKSEL----A 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2386 QVEPLTSPLKKTKLDSASDNIIQEYVTLrtryselmtLTSQyikfITDTQRRLEDEEMADAQQKQIEREMTVLQQ----- 2460
Cdd:pfam05557  198 RIPELEKELERLREHNKHLNENIENKLL---------LKEE----VEDLKRKLEREEKYREEAATLELEKEKLEQelqsw 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2461 ------TFLT---------EKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAA--- 2522
Cdd:pfam05557  265 vklaqdTGLNlrspedlsrRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVrrl 344
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2496167637 2523 ------LNKQKEAEKDIL---NKQKEMQELERKRLEQERVLADENQKLREKLQQME 2569
Cdd:pfam05557  345 qrrvllLTKERDGYRAILesyDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEME 400
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
2347-2585 2.46e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 43.84  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2347 KLLEEIEKNKDKvdecqkyAKAYIDIiKDYELQLVAYKAQVEPLTSPLK-------KTKLDSASDNIIQEYVTLRTRYSE 2419
Cdd:pfam05262  185 ALREDNEKGVNF-------RRDMTDL-KERESQEDAKRAQQLKEELDKKqidadkaQQKADFAQDNADKQRDEVRQKQQE 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2420 LMTLTSQyikfiTDTQRRLEDEEMADAQQKQIEREMTVLQQtflTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKalkd 2499
Cdd:pfam05262  257 AKNLPKP-----ADTSSPKEDKQVAENQKREIEKAQIEIKK---NDEEALKAKDHKAFDLKQESKASEKEAEDKEL---- 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2500 EQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQKSTLITE 2579
Cdd:pfam05262  325 EAQKKREPVAEDLQKTKPQVEAQPTSLNEDAIDSSNPVYGLKVVDPITNLSELVLIDLKTEVRLRESAQQTIRRRGLYER 404

                   ....*.
gi 2496167637 2580 KHVTVV 2585
Cdd:pfam05262  405 EKDLVA 410
PLEC smart00250
Plectin repeat;
3311-3347 2.48e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 38.23  E-value: 2.48e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2496167637  3311 KYLQGSESIAGIYLEPTKENISIYQAMKKKLLRHNTG 3347
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
1111-1231 3.05e-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: 40.74  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1111 ERDRVQKKTFTKWVNKHLIKSQrhVTDLYEDLRDGHNLISLLEVLSGDTllserDVARSVRLPREKGRMRFHKLQNVQIA 1190
Cdd:cd21330      9 EGETREERTFRNWMNSLGVNPR--VNHLYSDLSDALVIFQLYEKIKVPV-----DWNRVNKPPYPKLGENMKKLENCNYA 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2496167637 1191 LDFLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQVS 1231
Cdd:cd21330     82 VELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
COG5022 COG5022
Myosin heavy chain [General function prediction only];
2379-2575 3.06e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.91  E-value: 3.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2379 QLVAYKAQVEPLTSPLKKTKLDSASDNIIQEYV--TLRTRYSELMTLTSQYIKFITDTQRRLEDEEMADAQQKQIE---- 2452
Cdd:COG5022    811 EYRSYLACIIKLQKTIKREKKLRETEEVEFSLKaeVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQElkid 890
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2453 -REMTVLQQTFLT-EKEMLLKKEKLIEDEKKKLESQfEEEIKKAKALKDEQDRQRQQ-MEEEKLKLKATMDAALNKQKEA 2529
Cdd:COG5022    891 vKSISSLKLVNLElESEIIELKKSLSSDLIENLEFK-TELIARLKKLLNNIDLEEGPsIEYVKLPELNKLHEVESKLKET 969
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2496167637 2530 EKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQKST 2575
Cdd:COG5022    970 SEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQEST 1015
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2435-2563 3.15e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.98  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2435 QRRLEDEEMADAQQKQIEREMtvLQQTFltEKEMLLKKEKLIEDekKKLESQFEEEIKKAKALKDEQDRQ-----RQQME 2509
Cdd:pfam13868  216 ERKERQKEREEAEKKARQRQE--LQQAR--EEQIELKERRLAEE--AEREEEEFERMLRKQAEDEEIEQEeaekrRMKRL 289
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2496167637 2510 EEKLKLKATMDAALNK---QKEAEKDILNKQKEMQELERKRLEQERvladeNQKLRE 2563
Cdd:pfam13868  290 EHRRELEKQIEEREEQraaEREEELEEGERLREEEAERRERIEEER-----QKKLKE 341
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
2436-2575 3.59e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 41.18  E-value: 3.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2436 RRLEDEEMADAQQKQIEREmtvlqqtfltEKEMLLKKE--KLIEDEKKKLE---SQFEEEIKKAKalkDEQDRQRQQMEE 2510
Cdd:pfam05672   20 RRQAREQREREEQERLEKE----------EEERLRKEElrRRAEEERARREeeaRRLEEERRREE---EERQRKAEEEAE 86
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2496167637 2511 EKLKLKATMDAALNKQKEAEkdilnKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQKST 2575
Cdd:pfam05672   87 EREQREQEEQERLQKQKEEA-----EAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIMKRT 146
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
2231-2403 3.78e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2231 AEAEAEQpvfDSLEEELKKASAVSDKMSRVHSERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLgyYRE-- 2308
Cdd:COG3883     26 SELQAEL---EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL--YRSgg 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2309 SYDWLIRW-----IADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAY 2383
Cdd:COG3883    101 SVSYLDVLlgsesFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
                          170       180
                   ....*....|....*....|
gi 2496167637 2384 KAQVEPLTSPLKKTKLDSAS 2403
Cdd:COG3883    181 EALLAQLSAEEAAAEAQLAE 200
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
2131-2551 3.81e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.50  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2131 KKDLDKVSTKTQDILNSpqpsatAPVLRSELELTVQKMDHAYMlssvylEKLKTVEMVIRNTQGAEGVLKQYENCLREVH 2210
Cdd:TIGR00606  690 EAELQEFISDLQSKLRL------APDKLKSTESELKKKEKRRD------EMLGLAPGRQSIIDLKEKEIPELRNKLQKVN 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2211 T----VPNDVKEVETYRTNLKKMRAEAEAEQP---VFDSLEEELKKasaVSDKMSRVHSERDA-----ELDQHRQHLSSL 2278
Cdd:TIGR00606  758 RdiqrLKNDIEEQETLLGTIMPEEESAKVCLTdvtIMERFQMELKD---VERKIAQQAAKLQGsdldrTVQQVNQEKQEK 834
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2279 QDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWLIR---WIADAKQRQENIQAVPITDSKTLKE-----QLAKE----- 2345
Cdd:TIGR00606  835 QHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEEQLVELSTEVQSlireiKDAKEqdspl 914
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2346 ----KKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEpltsplkktkldsasdNIIQEYVT--LRTRYSE 2419
Cdd:TIGR00606  915 etflEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIE----------------NKIQDGKDdyLKQKETE 978
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2420 LMTLTSQyikfITDTQRRledeemadaqQKQIEREMTVLQQTFLTEK--EMLLKKE---KLIEDEKKKLE---SQFEEEI 2491
Cdd:TIGR00606  979 LNTVNAQ----LEECEKH----------QEKINEDMRLMRQDIDTQKiqERWLQDNltlRKRENELKEVEeelKQHLKEM 1044
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2492 KKAKALkdEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQE 2551
Cdd:TIGR00606 1045 GQMQVL--QMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2217-2555 3.88e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2217 KEVETYRTNLKKMRAEAEAeqpvfdsLEEELKKAsavsdkmsrvhserDAELDQHRQHLSSLQDRWKAVFTQIDLRQREL 2296
Cdd:COG4372     45 EELEQLREELEQAREELEQ-------LEEELEQA--------------RSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2297 DQLGRQLGYYRESYDWLIRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDY 2376
Cdd:COG4372    104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2377 ELQLVAYKAQvepLTSPLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEMADAQ-QKQIEREM 2455
Cdd:COG4372    184 ALDELLKEAN---RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELlEEVILKEI 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2456 TVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILN 2535
Cdd:COG4372    261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
                          330       340
                   ....*....|....*....|
gi 2496167637 2536 KQKEMQELERKRLEQERVLA 2555
Cdd:COG4372    341 DLLQLLLVGLLDNDVLELLS 360
rplD PRK14907
50S ribosomal protein L4; Provisional
389-545 3.96e-03

50S ribosomal protein L4; Provisional


Pssm-ID: 184900 [Multi-domain]  Cd Length: 295  Bit Score: 42.63  E-value: 3.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  389 EVKSTELKSTVE--TPAKMKPQAVATVASVQEsydTNDTSTPVITKPvkEEKAKKKKATEESVKLAEVKIpgqEKATKTD 466
Cdd:PRK14907     3 ETKKTTKKKTTEekKPAAKKATTSKETAKTKK---TAKTTSTKAAKK--AAKVKKTKSVKTTTKKVTVKF---EKTESVK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637  467 KVSVPTKakpgsTTGKPVVSDNVETPKVVQEPSDAT-PTSVNISEKPKSEvlskAAESSILEVTTSVRTGLTSSRTNAEV 545
Cdd:PRK14907    75 KESVAKK-----TVKKEAVSAEVFEASNKLFKNTSKlPKKLFASEKIYSQ----AIFDTILSERASRRQGTHKVKTRAEV 145
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
2237-2578 4.94e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 43.14  E-value: 4.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2237 QPVFDSLEEELKKASAVSDKMsRVHSErdaELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLgrqlgyyRESYDWLIRW 2316
Cdd:pfam05622   65 QKQLEQLQEENFRLETARDDY-RIKCE---ELEKEVLELQHRNEELTSLAEEAQALKDEMDIL-------RESSDKVKKL 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2317 ---IADAKQRQEniqavpitDSKTLKEQLakekKLLEE-----IEKNKDKVDECQKYAKAyidiikdyELQLVAYKAQVE 2388
Cdd:pfam05622  134 eatVETYKKKLE--------DLGDLRRQV----KLLEErnaeyMQRTLQLEEELKKANAL--------RGQLETYKRQVQ 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2389 PLtsplkKTKLDSAS---DNIIQEYVTLRTRYSELM----TLTSQyikfiTDTQRRLEDE-EMADAQQKQIEREMTVLQQ 2460
Cdd:pfam05622  194 EL-----HGKLSEESkkaDKLEFEYKKLEEKLEALQkekeRLIIE-----RDTLRETNEElRCAQLQQAELSQADALLSP 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2461 TFLTE----KEMLLK--KEKLI--EDEKKKL----ESQFEEEIKKAKALKDEQDRQRQQMEEEK-------LKLKATMDA 2521
Cdd:pfam05622  264 SSDPGdnlaAEIMPAeiREKLIrlQHENKMLrlgqEGSYRERLTELQQLLEDANRRKNELETQNrlanqriLELQQQVEE 343
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2496167637 2522 ALNKQKE----AEKDILNKQKemqeLErKRLEQERVLADENQKLREKLQQMEEAQKSTLIT 2578
Cdd:pfam05622  344 LQKALQEqgskAEDSSLLKQK----LE-EHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQ 399
SH3_Tec_like cd11768
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ...
1896-1940 5.02e-03

Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212702 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 5.02e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2496167637 1896 VQAVCDFKQVE---ITVHKGDECALLNNSQPSKWKVMNRSGSEAVVPS 1940
Cdd:cd11768      2 VVALYDFQPIEpgdLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPS 49
PLEC smart00250
Plectin repeat;
3759-3792 5.09e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 37.46  E-value: 5.09e-03
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2496167637  3759 LEAQTSTGGIIDPEFQFHLPADVAIQRGYINKET 3792
Cdd:smart00250    4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
2118-2574 5.34e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 42.81  E-value: 5.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2118 AEQAKVQVELEGLKKDLDKVSTKTQDILNSPQPSATApvLRSELELTVQKMDHAYMLSSVYLEKL--------KTVEMVI 2189
Cdd:pfam05557    2 AELIESKARLSQLQNEKKQMELEHKRARIELEKKASA--LKRQLDRESDRNQELQKRIRLLEKREaeaeealrEQAELNR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2190 RNTQGAEGVLK------QYENCLREVHTVPNDvkEVETYRTNLKKMRAEAEAE----QPVFDSLEEELKKASAVSDKM-- 2257
Cdd:pfam05557   80 LKKKYLEALNKklnekeSQLADAREVISCLKN--ELSELRRQIQRAELELQSTnselEELQERLDLLKAKASEAEQLRqn 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2258 -------SRVHSERDAELDQHRQhlssLQDRWKAVFTQIDLRQRELDQLGRQLGYYREsydwlirwiaDAKQRQENIQAV 2330
Cdd:pfam05557  158 lekqqssLAEAEQRIKELEFEIQ----SQEQDSEIVKNSKSELARIPELEKELERLRE----------HNKHLNENIENK 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2331 PItdsktLKEQLAKEKKLLEEIEKNKDKV-------DECQKYAKAYIDIIKDYELQLVAYKA--------QVEPLTSPLK 2395
Cdd:pfam05557  224 LL-----LKEEVEDLKRKLEREEKYREEAatlelekEKLEQELQSWVKLAQDTGLNLRSPEDlsrrieqlQQREIVLKEE 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2396 KTKLDSASDNiiqeyvtLRTRYSELMTLTSQYIKFITDTQRRLED-EEMADAQQKQI-----ERE-MTVLQQTF---LTE 2465
Cdd:pfam05557  299 NSSLTSSARQ-------LEKARRELEQELAQYLKKIEDLNKKLKRhKALVRRLQRRVllltkERDgYRAILESYdkeLTM 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2466 KEMLLKKEKLIE------DEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKE 2539
Cdd:pfam05557  372 SNYSPQLLERIEeaedmtQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLE 451
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 2496167637 2540 MQELERKRL-EQERVLadENQKLREKLQQMEEAQKS 2574
Cdd:pfam05557  452 TLELERQRLrEQKNEL--EMELERRCLQGDYDPKKT 485
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
2440-2588 5.62e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.55  E-value: 5.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2440 DEEMADAQQKQIEREMTVLQQTFLTEKEMLLK-KEKLIEDEKKKLESQfEEEIKKAKALKDEQDRQRQQMEEEKLKLKAT 2518
Cdd:COG2268    211 ETEIAIAQANREAEEAELEQEREIETARIAEAeAELAKKKAEERREAE-TARAEAEAAYEIAEANAEREVQRQLEIAERE 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2519 MDAALnKQKEAEKDILNKQKEMQ---ELERKRLEQE------------RVLADENQKLREKLQQMEEAQKSTLITEKHVT 2583
Cdd:COG2268    290 REIEL-QEKEAEREEAELEADVRkpaEAEKQAAEAEaeaeaeairakgLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE 368

                   ....*
gi 2496167637 2584 VVETV 2588
Cdd:COG2268    369 IAEAA 373
DUF4795 pfam16043
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ...
2436-2571 5.63e-03

Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 285 and 978 amino acids in length.


Pssm-ID: 464990 [Multi-domain]  Cd Length: 181  Bit Score: 41.14  E-value: 5.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2436 RRLEDEEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIED-----------EKKKLESQFEEEIKKAKALKDEQDR- 2503
Cdd:pfam16043    1 KKVEDAELLDQLQALILDLQEELEKLSETTSELSERLQQRQKHlealyqqieklEKVKADKEVVEEELDEKADKEALASk 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2496167637 2504 -QRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERV------LADENQKLREKLQQMEEA 2571
Cdd:pfam16043   81 vSRDQFDETLEELNQMLQELLDKLEGQEDAWKKALETLSEELDTKLDRLELdplkelLERRIKALQKLLQEGSEE 155
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
2200-2571 5.68e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.90  E-value: 5.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2200 KQYENCLREVHTVPNDVKEVETYRTNLKKMRAEAEAE-QPVFDSLEEELKKasaVSDKMSRVHSERDAELDQHRQHLSSL 2278
Cdd:pfam12128  251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAElNQLLRTLDDQWKE---KRDELNGELSAADAAVAKDRSELEAL 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2279 QDRWKAvFTQIDLRQRELDQlgRQLGYYRESYDWLIRWIADAKQRQENIQAvpitdsKTLKEQLAKEKKLLEEIEKNKDK 2358
Cdd:pfam12128  328 EDQHGA-FLDADIETAAADQ--EQLPSWQSELENLEERLKALTGKHQDVTA------KYNRRRSKIKEQNNRDIAGIKDK 398
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2359 VDEcQKYAKayidiikdyELQLVAYKAQVEPLTSPLKKtKLDSASDNIIQEYVTLRTRYSEL-MTLTSQYIKFITDTQRR 2437
Cdd:pfam12128  399 LAK-IREAR---------DRQLAVAEDDLQALESELRE-QLEAGKLEFNEEEYRLKSRLGELkLRLNQATATPELLLQLE 467
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2438 LEDEEMADAQQKQIEREMTVLQqtfLTEKEMLLKKEKLIEDEKKKLESQFEEEikkakalkdeqdrQRQQMEEEKLKLKA 2517
Cdd:pfam12128  468 NFDERIERAREEQEAANAEVER---LQSELRQARKRRDQASEALRQASRRLEE-------------RQSALDELELQLFP 531
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2518 ---TMDAALNKQKEAEKDILNKQKEMQELERK--------------------RLEQERV----LADENQKLREKLQQMEE 2570
Cdd:pfam12128  532 qagTLLHFLRKEAPDWEQSIGKVISPELLHRTdldpevwdgsvggelnlygvKLDLKRIdvpeWAASEEELRERLDKAEE 611

                   .
gi 2496167637 2571 A 2571
Cdd:pfam12128  612 A 612
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2437-2579 5.80e-03

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: 43.13  E-value: 5.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2437 RLEDEEMADAQQKQIEREMTVL---QQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIK----KAKALKDEQDRQRQQME 2509
Cdd:TIGR02169  207 REKAERYQALLKEKREYEGYELlkeKEALERQKEAIERQLASLEEELEKLTEEISELEKrleeIEQLLEELNKKIKDLGE 286
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2496167637 2510 EEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKR----LEQERVLAdENQKLREKLQQmEEAQKSTLITE 2579
Cdd:TIGR02169  287 EEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLakleAEIDKLLA-EIEELEREIEE-ERKRRDKLTEE 358
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
2447-2580 6.19e-03

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 41.29  E-value: 6.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2447 QQKQIEREMTVLQQTFLTEKE----MLLKKEKLIEDEKKKLESQfeEEIKKakaLKDEQDRQRQQMEEEKLKLKATMD-- 2520
Cdd:pfam14988   30 ECEEIERRRQELASRYTQQTAelqtQLLQKEKEQASLKKELQAL--RPFAK---LKESQEREIQDLEEEKEKVRAETAek 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2521 ------------AALNKQKEAEKDILNKQKEMQELERK----RLEQERVLAD-------ENQKLREKLQQM-EEAQKSTL 2576
Cdd:pfam14988  105 dreahlqflkekALLEKQLQELRILELGERATRELKRKaqalKLAAKQALSEfcrsikrENRQLQKELLQLiQETQALEA 184

                   ....
gi 2496167637 2577 ITEK 2580
Cdd:pfam14988  185 IKSK 188
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
2338-2575 6.88e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 6.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2338 LKEQLAKEKKLLEEIEKnkdkvdecqkyakayidiikdyelQLVAYKAQvEPLTSplkktkLDSASDNIIQEYVTLRTRY 2417
Cdd:COG3206    180 LEEQLPELRKELEEAEA------------------------ALEEFRQK-NGLVD------LSEEAKLLLQQLSELESQL 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2418 SELmtltsqyikfitdTQRRLEDEEMADAQQKQIEREMTVLQQTFL-TEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKA 2496
Cdd:COG3206    229 AEA-------------RAELAEAEARLAALRAQLGSGPDALPELLQsPVIQQLRAQLAELEAELAELSARYTPNHPDVIA 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2497 LKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQ---------ELERKRLEQERVLADEN-QKLREKLQ 2566
Cdd:COG3206    296 LRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEarlaelpelEAELRRLEREVEVARELyESLLQRLE 375

                   ....*....
gi 2496167637 2567 QMEEAQKST 2575
Cdd:COG3206    376 EARLAEALT 384
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
1122-1224 7.73e-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: 39.20  E-value: 7.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 1122 KWVNKHLIKSQR---HVTDLYEDLRDGHNLISLL---------EVLSGDTLLSERDVARSVRLprekgrmrfhkLQNVQi 1189
Cdd:cd21218     17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLhslapelcdKELVLEVLSEEDLEKRAEKV-----------LQAAE- 84
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2496167637 1190 ALDFLRHrqvklvnIRNDDIADGNPKLTLGLIWTI 1224
Cdd:cd21218     85 KLGCKYF-------LTPEDIVSGNPRLNLAFVATL 112
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2110-2454 8.48e-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: 42.35  E-value: 8.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2110 LKECIQKTAEQakvQVELEGLKKDLDKVSTKTQDILNSpqpsatAPVLRSELELTVQKMDHAYMLSSVYLEKLKTVEMVI 2189
Cdd:TIGR02168  679 IEELEEKIEEL---EEKIAELEKALAELRKELEELEEE------LEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2190 RNTQGAEGVLKQYENCLREvhtvpndvkEVETYRTNLKkmRAEAEAEQpvfdsLEEELKKASAVSDKMSRVHSERDAELD 2269
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEE---------RLEEAEEELA--EAEAEIEE-----LEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2270 QHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWLIRWIADAKQRQENIQAvpitDSKTLKEQLAKEKKLL 2349
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES----ELEALLNERASLEEAL 889
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2350 EEIEKNKDKVDEcqkyakayidIIKDYELQLVAYKAQVEPLTSPLKKTKLDSASdnIIQEYVTLRTRYSELMTLTSQYIk 2429
Cdd:TIGR02168  890 ALLRSELEELSE----------ELRELESKRSELRRELEELREKLAQLELRLEG--LEVRIDNLQERLSEEYSLTLEEA- 956
                          330       340
                   ....*....|....*....|....*
gi 2496167637 2430 fITDTQRRLEDEEMADAQQKQIERE 2454
Cdd:TIGR02168  957 -EALENKIEDDEEEARRRLKRLENK 980
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
2438-2572 8.52e-03

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 39.60  E-value: 8.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2438 LEDEEMADAQQKQIEREMTVLQQtfltEKEMLLKKEKLIEDEKKKLESQFE------EEIKKAKALKDEQDRQRQQMEEE 2511
Cdd:pfam12718   13 QERAEELEEKVKELEQENLEKEQ----EIKSLTHKNQQLEEEVEKLEEQLKeakekaEESEKLKTNNENLTRKIQLLEEE 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2496167637 2512 KLKLKATMDAALNKQKEAEkdilnkqKEMQELERKR--LEQERvLADEnQKLREKLQQMEEAQ 2572
Cdd:pfam12718   89 LEESDKRLKETTEKLRETD-------VKAEHLERKVqaLEQER-DEWE-KKYEELEEKYKEAK 142
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
2338-2572 9.22e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.26  E-value: 9.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2338 LKEQLAKEKKLLEEIEKNKD------KVDECQKYAKAYIDIIKDyELQLVAYKAQVEPLTSPLKKTKLDSASDNIIQEYV 2411
Cdd:TIGR00618  158 LKAKSKEKKELLMNLFPLDQytqlalMEFAKKKSLHGKAELLTL-RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQ 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2412 TLR------TRYSELMTLTSQYIKFITDTQRRLEDEEMADA----QQKQIEREMTVLQqtFLTEKEMLLKKEKLIEDEKK 2481
Cdd:TIGR00618  237 QTQqshaylTQKREAQEEQLKKQQLLKQLRARIEELRAQEAvleeTQERINRARKAAP--LAAHIKAVTQIEQQAQRIHT 314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496167637 2482 KLESQFEEEIK----KAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADE 2557
Cdd:TIGR00618  315 ELQSKMRSRAKllmkRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQK 394
                          250
                   ....*....|....*
gi 2496167637 2558 NQKLREKLQQMEEAQ 2572
Cdd:TIGR00618  395 LQSLCKELDILQREQ 409
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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