NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1761000869|ref|NP_001361658|]
View 

dystonin isoform 7 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
20-147 1.80e-85

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: 276.48  E-value: 1.80e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   20 QAYEDVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIA 99
Cdd:cd21236      1 QAYENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIA 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1761000869  100 LDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 147
Cdd:cd21236     81 LDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
152-255 5.65e-73

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: 239.89  E-value: 5.65e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLDPE 231
Cdd:cd21239      1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLGVTRLLDPE 80
                           90       100
                   ....*....|....*....|....
gi 1761000869  232 DVDVSSPDEKSVITYVSSLYDAFP 255
Cdd:cd21239     81 DVDVSSPDEKSVITYVSSLYDVFP 104
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6270-6485 1.63e-38

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: 145.67  E-value: 1.63e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6270 LGQFQHALDELLAWLTHTEGLLSEQKPvGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSAgEEASNLQN 6349
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6350 KLEVLNQRWQNVLEKTEQRKQQLDGALRQAKGFHgEIEDLQQWLTDTERhLLASKPLGGLPETAKEQLNVHMEVCAAFEA 6429
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEA-ALASEDLGKDLESVEELLKKHKELEEELEA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1761000869 6430 KEETYKSLMQKGQQMLARCPKSAETNIDQDINNLKEKWESVETKLNERKTKLEEAL 6485
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
7167-7242 2.54e-36

Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain


:

Pssm-ID: 128539  Cd Length: 73  Bit Score: 133.73  E-value: 2.54e-36
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1761000869  7167 DKIEDEVTRQVAKCKCAKRFQVEQIGDNKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCR 7242
Cdd:smart00243    1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRF------GDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCR 70
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
977-1054 2.43e-34

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: 128.49  E-value: 2.43e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1761000869  977 VSWHYLINEIDRIRASNVASIKTMLPGEHQQVLSNLQSRFEDFLEDSQESQVFSGSDITQLEKEVNVCKQYYQELLKS 1054
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6709-6921 8.26e-34

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: 132.18  E-value: 8.26e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6709 QFTDALQALIDWLYRVEPQLAEDQPVHgDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARELIEGSRDDSSWVKVQMQ 6788
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6789 ELSTRWETVCALSISKQTRLEAALRQAEEFHSvVHALLEWLAEAEQTLRfHGVLPDDEDALRTLIDQHKEFMKKLEEKRA 6868
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1761000869 6869 ELNKATTMGDTVLAICHPDSITTIKHWITIIRARFEEVLAWAKQHQQRLASAL 6921
Cdd:cd00176    161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6596-6812 4.74e-29

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: 118.32  E-value: 4.74e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6596 RAKQFHEAWSKLMEWLEESEKSLDSElEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEktSLADDNLKL 6675
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6676 DDMLSELRDKWDTICGKSVERQNKLEEALLFSGQFTDALQaLIDWLYRVEPQLAEDQPVHgDIDLVMNLIDNHKAFQKEL 6755
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1761000869 6756 GKRTSSVQALKRSARELIEGSRDDSS-WVKVQMQELSTRWETVCALSISKQTRLEAAL 6812
Cdd:cd00176    156 EAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6162-6376 4.92e-25

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: 106.76  E-value: 4.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6162 QYQDGLQAVFDWVDIAGGKLASMSPiGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEESDKhtVQDP 6241
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--IQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6242 LMELKLIWDSLEERIINRQHKLEGALLALgQFQHALDELLAWLTHTEGLLSEQkPVGGDPKAIEIELAKHHVLQNDVLAH 6321
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1761000869 6322 QSTVEAVNKAGNDLIESSAGEEASNLQNKLEVLNQRWQNVLEKTEQRKQQLDGAL 6376
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6050-6267 6.64e-23

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: 100.60  E-value: 6.64e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6050 LAEKFWCDHMSLIVTIKDTQDFIRDlEDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAAcGEPDKPIVK 6129
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6130 KSIDELNSAWDSLNKAWKDRIDKLEEAMQAAVQYQDGLQAVfDWVDIAGGKLASMsPIGTDLETVKQQIEELKQFKSEAY 6209
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1761000869 6210 QQQIEMERLNHQAELLLKKVTEESDKHtVQDPLMELKLIWDSLEERIINRQHKLEGAL 6267
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEE-IEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5396-5609 1.31e-22

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: 99.83  E-value: 1.31e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5396 RFQDALESLLSWMVDTEELVANQKPPSAEfKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKIATtAEPADKVKILKQL 5475
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5476 SLLDSRWEALLNKAETRNRQLEGISVVAQQFHETLEpLNEWLTTIEKRLVNcEPIGTQASKLEEQIAQHKVLQEDILLRK 5555
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1761000869 5556 QNVDQALLNGLELLKQTTGDEVLIIQDKLEAIKARYKDITKLSTDVAKTLEQAL 5609
Cdd:cd00176    160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6378-6594 1.51e-22

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: 99.44  E-value: 1.51e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6378 QAKGFHGEIEDLQQWLTDTERhLLASKPLGGLPETAKEQLNVHMEVCAAFEAKEETYKSLMQKGQQMLARCPKSAEtNID 6457
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEE-LLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6458 QDINNLKEKWESVETKLNERKTKLEEALNLaMEFHNSLQDFINWLTQAEQTLNVASRPSLiLDTVLFQIDEHKVFANEVN 6537
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 6538 SHREQIIELDKTGTHLKYFSQKQDVVLIKNLLISVQSRWEKVVQRLVERGRSLDDAR 6594
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
701-883 1.44e-20

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: 94.05  E-value: 1.44e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  701 LHNFVSRATNELIWLNEKEEEEVAYDWSERNTNIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTIEAYR 780
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  781 AAMQTQWSWILQLCQCVEQHIKENTAYFEFFNDAKEATDYLRNLKDAIQrkySCDRSSSIHKLEDLVQESMEEKEELLQY 860
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180
                   ....*....|....*....|...
gi 1761000869  861 KSTIANLMGKAKTIIQLKPRNSD 883
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDAD 181
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
876-942 1.66e-20

SH3 domain; This entry represents an SH3 domain.


:

Pssm-ID: 407754  Cd Length: 65  Bit Score: 88.47  E-value: 1.66e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869  876 QLKPRNSdcPLKTSIPIKAICDYRQIEITIYKDDECVLANNSHRAKWKVISPTGNEAMVPSVCFTVP 942
Cdd:pfam17902    1 PLKQRRS--PVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5282-5497 8.71e-19

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: 88.66  E-value: 8.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5282 RLEEFYSKLKEFSILLQKAEEHEESQGPVGMEtETINQQLNMFKVFQKEeIEPLQGKQQDVNWLGQGLIQSAAKSTSTqg 5361
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAE-LAAHEERVEALNELGEQLIEEGHPDAEE-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5362 LEHDLDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDALEsLLSWMVDTEELVANQKPPSAEFKvVKAQIQEQKLLQRL 5441
Cdd:cd00176     77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEE 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1761000869 5442 LDDRKSTVEVIKREGEKIATTAEPADKVKILKQLSLLDSRWEALLNKAETRNRQLE 5497
Cdd:cd00176    155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5832-6048 1.33e-18

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 88.27  E-value: 1.33e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5832 QFWETYEELWPWLTETQSIISQLPAPALEyETLRQQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPGEGFSIQEKYV 5911
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5912 AADTLYSQIKEDVKKRAVALDEAISQStQFHDKIDQILESLERIVERLRQPPsISAEVEKIKEQISENKNVSVDMEKLQP 5991
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASED-LGKDLESVEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 5992 LYETLKQRGEEMIARSGGTdkdiSAKAVQDKLDQMVFIWENIHTLVEEREAKLLDVM 6048
Cdd:cd00176    161 RLKSLNELAEELLEEGHPD----ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5722-5935 4.51e-18

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


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 86.73  E-value: 4.51e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5722 QQFDQAADAELSWITETEKKLMSLGDIRLEQdQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTACSEEeKQSMKKK 5801
Cdd:cd00176      3 QQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5802 LDKVLKNYDTICQINSERYLQLERAQSLVNQFWETyEELWPWLTETQSIISQLPAPAlEYETLRQQQEEHRQLRELIAEH 5881
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1761000869 5882 KPHIDKMNKTGPQLLELSPGEGF-SIQEKYVAADTLYSQIKEDVKKRAVALDEAI 5935
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4514-4735 1.43e-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: 85.19  E-value: 1.43e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4514 KLQKAQEESSAMMQWLQKMNKTATKWQqtpAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELLEENPdtPEAP 4593
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTD---YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH--PDAE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4594 RWKQMLTEIDSKWQELNQLTIDRQQKLEESSNNLTQFQTVEaQLKQWLVEKELMVSVLGPLSiDPNMLNTQRQQVQILLQ 4673
Cdd:cd00176     76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEE 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1761000869 4674 EFATRKPQYEQLTAAGQGILSRpgEDPSLRGIVKEQLAAVTQKWDSLTGQLSDRCDWIDQAI 4735
Cdd:cd00176    154 ELEAHEPRLKSLNELAEELLEE--GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4740-4954 1.54e-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: 82.11  E-value: 1.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4740 QYQSLLRSLSDKLSDLDNKLS--SSLAVSTHPDAMNQQLETAQKMKQEIQQEKKQIKVAQALCEDLSALVKEEylKAELS 4817
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEEllSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD--AEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4818 RQLEGILKSFKDVEQKAENHVQHLQSAcASSHQFQQMSRDFQAWLDtKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLT 4897
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLE-EKEAALASEDLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 4898 AQSHMYEKTIAEGENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLKESL 4954
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5503-5718 3.19e-15

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: 78.26  E-value: 3.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5503 AQQFHETLEPLNEWLTTIEKRLVNCEPIGTQASkLEEQIAQHKVLQEDILLRKQNVDQALLNGLELLKQTtGDEVLIIQD 5582
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLES-VEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5583 KLEAIKARYKDITKLSTDVAKTLEQALQLARRLHStHEELCTWLDKVEVELLSYEtqVLKGEEASQAQM-RPKELKKEAK 5661
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASED--LGKDLESVEELLkKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 5662 NNKALLDSLNEVSSALLELVPWRAREGLEKMVAEDNERYRLVSDTITQKVEEIDAAI 5718
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3924-4153 5.29e-15

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: 77.87  E-value: 5.29e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3924 ELEKFDADYTEFEHWLQQSEQELENLEAGaDDINGLMTKLKRQKSFSEDVISHKGDLRYITISGNRVLEAAKSCSKrdgg 4003
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE---- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4004 kvdtsathrEVQRKLDHATDRFRSLYSKCNVLGNNLKDLVDKYQHYEDASCgLLAGLQACEATASkhlSEPIAVDPKNLQ 4083
Cdd:cd00176     76 ---------EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA---SEDLGKDLESVE 142
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4084 RQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGSllPAKNDIQKTLDDIVGRYEDLSKSVNERNEKLQ 4153
Cdd:cd00176    143 ELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLE 210
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
7092-7155 1.98e-10

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.12  E-value: 1.98e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1761000869 7092 RVMDFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLEmsAVADIFDRDGDGYIDYYEFVAALHP 7155
Cdd:COG5126     70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEAD--ELFARLDTDGDGKISFEEFVAAVRD 131
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3613-4395 4.35e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 67.39  E-value: 4.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3613 ESVTTQVERLETQLH-LEQDLDD-QKIVAERQQEYkEKLQGICDLLTQTENRLighqeafmigdgTVELKKYQSKQEELQ 3690
Cdd:TIGR02168  249 KEAEEELEELTAELQeLEEKLEElRLEVSELEEEI-EELQKELYALANEISRL------------EQQKQILRERLANLE 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3691 KDMQGSAQALAEVvkntenflkENGEKLSQEDKALIEQKLNEAKIKCEQLNLK---AEQSKKELDKVVTTAIKEETEKVA 3767
Cdd:TIGR02168  316 RQLEELEAQLEEL---------ESKLDELAEELAELEEKLEELKEELESLEAEleeLEAELEELESRLEELEEQLETLRS 386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3768 AVKQLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIEQNGTHFQEGDGKSAIGEEDEVNGNLLETDvdgqvgTTQENLN 3847
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ------EELERLE 460
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3848 QQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGQYLspEEKEKLQKNMKELKvhyetalaESEKKMKLTHSLQEELEK 3927
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQ--ENLEGFSEGVKALL--------KNQSGLSGILGVLSELIS 530
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3928 FDADY-TEFEHWLQQSEQEL--ENLEAGADDINGLMTKLKRQKSFSE-DVISH---KGDLRYITISGNRVLEAAKSCSKR 4000
Cdd:TIGR02168  531 VDEGYeAAIEAALGGRLQAVvvENLNAAKKAIAFLKQNELGRVTFLPlDSIKGteiQGNDREILKNIEGFLGVAKDLVKF 610
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4001 D-----------GGK--VDTSATHREVQRKLDHATdRFRSLYSkcnvlgnnlkDLVdkyqhyedASCGLLAGlqACEATA 4067
Cdd:TIGR02168  611 DpklrkalsyllGGVlvVDDLDNALELAKKLRPGY-RIVTLDG----------DLV--------RPGGVITG--GSAKTN 669
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4068 SKHLSEPIAVdpKNLQRQLEEtkaLQGQISSQQVAVEKLKKTAEVLLDARGSLLPAKNDIQKTLDDIVGRYEDLSKSVN- 4146
Cdd:TIGR02168  670 SSILERRREI--EELEEKIEE---LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEq 744
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4147 --ERNEKLQITLTRSLSVQDGLDEMLDwmgnvesslkeqgqvpLNSTALQDIISKNIMLEQDIAGRQSSINAMNEKVkkf 4224
Cdd:TIGR02168  745 leERIAQLSKELTELEAEIEELEERLE----------------EAEEELAEAEAEIEELEAQIEQLKEELKALREAL--- 805
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4225 mettdpstaSSLQAKMKDLSARFSEASHKHKETLAKMEELKTKVELFENLSEKLQtfletktqaltevdvpgKDVTELSQ 4304
Cdd:TIGR02168  806 ---------DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS-----------------EDIESLAA 859
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4305 YMQESTSEFLEHKKHLEvlhSLLKEISSHGLpsDKALVLEKTNNLSKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSL 4384
Cdd:TIGR02168  860 EIEELEELIEELESELE---ALLNERASLEE--ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
                          810
                   ....*....|.
gi 1761000869 4385 KSWIKETTKKV 4395
Cdd:TIGR02168  935 EVRIDNLQERL 945
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1775-1813 1.19e-09

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 56.95  E-value: 1.19e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1761000869 1775 LLSAQLLSGGLINSNSGQRMTVEEAVREGVIDRDTASSI 1813
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4956-5167 1.31e-07

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: 55.91  E-value: 1.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4956 KALKYKEQVETLWPWIDKCQNNLEEIKFCLDPAEGENSIAKLKSLQKEMDQHFGMVELLNNTANSLLSVCEIDKEVVTDE 5035
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5036 NKSLIQKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRqLQCAKEQLDIHDSLGSQAYSNKYLTMLQTQQKSLQALK 5115
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQW-LEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1761000869 5116 HQVDLAKRLAQDLvVEASDSKGTSDVLLQVETIAQEHSTLSQQVDEKCSFLE 5167
Cdd:cd00176    160 PRLKSLNELAEEL-LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
608-699 3.07e-07

Spectrin repeats;


:

Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.95  E-value: 3.07e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   608 VQDLLNWVDEMQVQLDRTEWGSDLPSVESHLENHKNVHRAIEEFESSLKEAKISEIQMTA---PLKLTYAEKLHRLESQY 684
Cdd:smart00150    7 ADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEeghPDAEEIEERLEELNERW 86
                            90
                    ....*....|....*
gi 1761000869   685 AKLLNTSRNQERHLD 699
Cdd:smart00150   87 EELKELAEERRQKLE 101
SCP-1 super family cl30946
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
1033-1269 4.54e-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.


The actual alignment was detected with superfamily member pfam05483:

Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.49  E-value: 4.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 1033 DITQLEKEVNVCK---QYYQELLKSAEREEQEESVYNLYIS----------------------EVRNIRLRLENC---ED 1084
Cdd:pfam05483  451 EIHDLEIQLTAIKtseEHYLKEVEDLKTELEKEKLKNIELTahcdklllenkeltqeasdmtlELKKHQEDIINCkkqEE 530
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 1085 RLIRQIRTPLERddlhESVFRiTEQEKLKKELERLKDDLGTITNKCEE-FFSQAAASSSVPTLRSELNVVLQNMNQVYSM 1163
Cdd:pfam05483  531 RMLKQIENLEEK----EMNLR-DELESVREEFIQKGDEVKCKLDKSEEnARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 1164 SSTYIDKLKTVNLVLKNTQAAEA-LVKLYETKLCEEEAVIAD-KNNIENLISTlkqWRSEVDEKRQVFHALEDELQKAKA 1241
Cdd:pfam05483  606 KNKNIEELHQENKALKKKGSAENkQLNAYEIKVNKLELELASaKQKFEEIIDN---YQKEIEDKKISEEKLLEEVEKAKA 682
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1761000869 1242 ISDEMFKTYKERDLD-----------FDWHKEKADQLVE 1269
Cdd:pfam05483  683 IADEAVKLQKEIDKRcqhkiaemvalMEKHKHQYDKIIE 721
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1194-1358 3.20e-04

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


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 45.90  E-value: 3.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 1194 KLCEEEAVIADKNNIENLISTLKQWRSEVDEKRQVFHALEdelQKAKAISDEmfktykeRDLDFDWHKEKADQLVERWQN 1273
Cdd:cd00176     21 ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALN---ELGEQLIEE-------GHPDAEEIQERLEELNQRWEE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 1274 VHVQIDNRLRDLEGIGKSLKYYRDTYHpLDDWIQqvETTQRKIQENQPENSKTLATQLNQQKMLVSEIEMKQSKMDECQK 1353
Cdd:cd00176     91 LRELAEERRQRLEEALDLQQFFRDADD-LEQWLE--EKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNE 167

                   ....*
gi 1761000869 1354 YAEQY 1358
Cdd:cd00176    168 LAEEL 172
PLEC smart00250
Plectin repeat;
1552-1583 1.84e-03

Plectin repeat;


:

Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.39  E-value: 1.84e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1761000869  1552 DKVIAGTIDQTTGEVLSVFQAVLRGLIDYDTG 1583
Cdd:smart00250    7 QSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
SCP-1 super family cl30946
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
3234-3899 2.83e-03

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


The actual alignment was detected with superfamily member pfam05483:

Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 44.71  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3234 LLNILKQD-QHSQKITGVFELMRELTHMEY-----DLEKRGITSKVLPLQLEN----IFYKLLADgySEKIEHVGDFNQK 3303
Cdd:pfam05483  156 LCNLLKETcARSAEKTKKYEYEREETRQVYmdlnnNIEKMILAFEELRVQAENarleMHFKLKED--HEKIQHLEEEYKK 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3304 ACSTSEmmEEKPHILGDIKSKEGNYYSPNLeTVKEIGLESSTVWASTLPRDEKLKDLcNDFPSHLECTSGSKEMASGDSS 3383
Cdd:pfam05483  234 EINDKE--KQVSLLLIQITEKENKMKDLTF-LLEESRDKANQLEEKTKLQDENLKEL-IEKKDHLTKELEDIKMSLQRSM 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3384 TEQfsSELQQCLQHTEKmheylTLLQDMKPPLDNQESLDNNLEALKNQLRQLETFELGLAPIAVILRKDMKLAEEFLKSL 3463
Cdd:pfam05483  310 STQ--KALEEDLQIATK-----TICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKII 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3464 PSDFPR--GHVEELSISHQSLKTAFSSLSNVSSErtKQIMLAIDSEMSKLAvshEEFLHKLKSFSDWVSEKSKSVKDIEI 3541
Cdd:pfam05483  383 TMELQKksSELEEMTKFKNNKEVELEELKKILAE--DEKLLDEKKQFEKIA---EELKGKEQELIFLLQAREKEIHDLEI 457
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3542 ---VNVQDSEYVKKRLEFLKNVLKDLGHTKMQLETTAFDVQFFISEYAQ---DLSPNQSKQLLRLLNTTQKcfldvQESV 3615
Cdd:pfam05483  458 qltAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQeasDMTLELKKHQEDIINCKKQ-----EERM 532
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3616 TTQVERL-ETQLHLEQDLDDQKivaerqQEYKEKLQGI-CDLLTQTENRLIGHQEAFmigdgtvelkkyqsKQEELQKDM 3693
Cdd:pfam05483  533 LKQIENLeEKEMNLRDELESVR------EEFIQKGDEVkCKLDKSEENARSIEYEVL--------------KKEKQMKIL 592
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3694 QGSAQALAEVVKNTENFLKEngekLSQEDKALIEQ------KLNEAKIKCEQLNLKAEQSKKELDKVVTTAIKEetekva 3767
Cdd:pfam05483  593 ENKCNNLKKQIENKNKNIEE----LHQENKALKKKgsaenkQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE------ 662
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3768 avkqLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIEQNGTHFQEgdgKSAIGEEDEVNGNLLETDVDGQVGTTQeNLN 3847
Cdd:pfam05483  663 ----IEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAE---MVALMEKHKHQYDKIIEERDSELGLYK-NKE 734
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1761000869 3848 QQYQKVKAQHEKIISQHQAVIIATQSaQVLLEKqgqylspEEKEKLQKNMKE 3899
Cdd:pfam05483  735 QEQSSAKAALEIELSNIKAELLSLKK-QLEIEK-------EEKEKLKMEAKE 778
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1661-1698 3.49e-03

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 38.46  E-value: 3.49e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1761000869 1661 VLEILLSTGSLVIPATGEQLTLQKAFQQNLVSSALFSK 1698
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1851-1889 4.60e-03

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


:

Pssm-ID: 459901  Cd Length: 39  Bit Score: 38.08  E-value: 4.60e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1761000869 1851 VLEAQRGYVGLIWPHSGEIFPTSSSLQQELITNELAYKI 1889
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
 
Name Accession Description Interval E-value
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
20-147 1.80e-85

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: 276.48  E-value: 1.80e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   20 QAYEDVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIA 99
Cdd:cd21236      1 QAYENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIA 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1761000869  100 LDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 147
Cdd:cd21236     81 LDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
152-255 5.65e-73

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: 239.89  E-value: 5.65e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLDPE 231
Cdd:cd21239      1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLGVTRLLDPE 80
                           90       100
                   ....*....|....*....|....
gi 1761000869  232 DVDVSSPDEKSVITYVSSLYDAFP 255
Cdd:cd21239     81 DVDVSSPDEKSVITYVSSLYDVFP 104
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
35-254 4.88e-44

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 173.20  E-value: 4.88e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   35 KVQKKTFTKWINQHLMKV-RKHVNDLYEDLRDGHNLISLLEVLSGDTLPR--EKGRMRFHRLQNVQIALDYLKRRQVKLV 111
Cdd:COG5069      8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  112 NIRNDDITDGNPKLTLGLIWTIILHFQISDIHvtgESEDMSAKERLLLWTQQATEGYA-GIRCENFTTCWRDGKLFNAII 190
Cdd:COG5069     88 NIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALI 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1761000869  191 HKYRPDLIDMNTVAVQSN--LANLEHAFYVAEK-IGVIRLLDPEDV-DVSSPDEKSVITYVSSLYDAF 254
Cdd:COG5069    165 HDSRPDTLDPNVLDLQKKnkALNNFQAFENANKvIGIARLIGVEDIvNVSIPDERSIMTYVSWYIIRF 232
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6270-6485 1.63e-38

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: 145.67  E-value: 1.63e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6270 LGQFQHALDELLAWLTHTEGLLSEQKPvGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSAgEEASNLQN 6349
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6350 KLEVLNQRWQNVLEKTEQRKQQLDGALRQAKGFHgEIEDLQQWLTDTERhLLASKPLGGLPETAKEQLNVHMEVCAAFEA 6429
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEA-ALASEDLGKDLESVEELLKKHKELEEELEA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1761000869 6430 KEETYKSLMQKGQQMLARCPKSAETNIDQDINNLKEKWESVETKLNERKTKLEEAL 6485
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
7167-7242 2.54e-36

Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain


Pssm-ID: 128539  Cd Length: 73  Bit Score: 133.73  E-value: 2.54e-36
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1761000869  7167 DKIEDEVTRQVAKCKCAKRFQVEQIGDNKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCR 7242
Cdd:smart00243    1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRF------GDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCR 70
GAS2 pfam02187
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ...
7169-7243 1.53e-34

Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members and Gas2 family members. The GAR domain comprises around 57 amino acids and has been shown to bind to microtubules.


Pssm-ID: 460480  Cd Length: 69  Bit Score: 128.48  E-value: 1.53e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1761000869 7169 IEDEVTRQVAKCKCAKRFQVEQIGDNKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRV 7243
Cdd:pfam02187    1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRF------GDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
977-1054 2.43e-34

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: 128.49  E-value: 2.43e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1761000869  977 VSWHYLINEIDRIRASNVASIKTMLPGEHQQVLSNLQSRFEDFLEDSQESQVFSGSDITQLEKEVNVCKQYYQELLKS 1054
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6709-6921 8.26e-34

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: 132.18  E-value: 8.26e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6709 QFTDALQALIDWLYRVEPQLAEDQPVHgDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARELIEGSRDDSSWVKVQMQ 6788
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6789 ELSTRWETVCALSISKQTRLEAALRQAEEFHSvVHALLEWLAEAEQTLRfHGVLPDDEDALRTLIDQHKEFMKKLEEKRA 6868
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1761000869 6869 ELNKATTMGDTVLAICHPDSITTIKHWITIIRARFEEVLAWAKQHQQRLASAL 6921
Cdd:cd00176    161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6596-6812 4.74e-29

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: 118.32  E-value: 4.74e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6596 RAKQFHEAWSKLMEWLEESEKSLDSElEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEktSLADDNLKL 6675
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6676 DDMLSELRDKWDTICGKSVERQNKLEEALLFSGQFTDALQaLIDWLYRVEPQLAEDQPVHgDIDLVMNLIDNHKAFQKEL 6755
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1761000869 6756 GKRTSSVQALKRSARELIEGSRDDSS-WVKVQMQELSTRWETVCALSISKQTRLEAAL 6812
Cdd:cd00176    156 EAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6162-6376 4.92e-25

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: 106.76  E-value: 4.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6162 QYQDGLQAVFDWVDIAGGKLASMSPiGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEESDKhtVQDP 6241
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--IQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6242 LMELKLIWDSLEERIINRQHKLEGALLALgQFQHALDELLAWLTHTEGLLSEQkPVGGDPKAIEIELAKHHVLQNDVLAH 6321
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1761000869 6322 QSTVEAVNKAGNDLIESSAGEEASNLQNKLEVLNQRWQNVLEKTEQRKQQLDGAL 6376
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6050-6267 6.64e-23

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: 100.60  E-value: 6.64e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6050 LAEKFWCDHMSLIVTIKDTQDFIRDlEDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAAcGEPDKPIVK 6129
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6130 KSIDELNSAWDSLNKAWKDRIDKLEEAMQAAVQYQDGLQAVfDWVDIAGGKLASMsPIGTDLETVKQQIEELKQFKSEAY 6209
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1761000869 6210 QQQIEMERLNHQAELLLKKVTEESDKHtVQDPLMELKLIWDSLEERIINRQHKLEGAL 6267
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEE-IEEKLEELNERWEELLELAEERQKKLEEAL 213
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
39-136 8.01e-23

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 96.23  E-value: 8.01e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869    39 KTFTKWINQHLMK-VRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREK---GRMRFHRLQNVQIALDYLKRRQVKLVNIR 114
Cdd:smart00033    1 KTLLRWVNSLLAEyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 1761000869   115 NDDITDGnPKLTLGLIWTIILH 136
Cdd:smart00033   81 PEDLVEG-PKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5396-5609 1.31e-22

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: 99.83  E-value: 1.31e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5396 RFQDALESLLSWMVDTEELVANQKPPSAEfKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKIATtAEPADKVKILKQL 5475
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5476 SLLDSRWEALLNKAETRNRQLEGISVVAQQFHETLEpLNEWLTTIEKRLVNcEPIGTQASKLEEQIAQHKVLQEDILLRK 5555
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1761000869 5556 QNVDQALLNGLELLKQTTGDEVLIIQDKLEAIKARYKDITKLSTDVAKTLEQAL 5609
Cdd:cd00176    160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6378-6594 1.51e-22

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: 99.44  E-value: 1.51e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6378 QAKGFHGEIEDLQQWLTDTERhLLASKPLGGLPETAKEQLNVHMEVCAAFEAKEETYKSLMQKGQQMLARCPKSAEtNID 6457
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEE-LLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6458 QDINNLKEKWESVETKLNERKTKLEEALNLaMEFHNSLQDFINWLTQAEQTLNVASRPSLiLDTVLFQIDEHKVFANEVN 6537
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 6538 SHREQIIELDKTGTHLKYFSQKQDVVLIKNLLISVQSRWEKVVQRLVERGRSLDDAR 6594
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
35-139 4.93e-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: 94.28  E-value: 4.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   35 KVQKKTFTKWINQHL--MKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLP-REKGRMRFHRLQNVQIALDYLKRRQ-VKL 110
Cdd:pfam00307    1 LELEKELLRWINSHLaeYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPK 80
                           90       100
                   ....*....|....*....|....*....
gi 1761000869  111 VNIRNDDITDGNPKLTLGLIWTIILHFQI 139
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
701-883 1.44e-20

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: 94.05  E-value: 1.44e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  701 LHNFVSRATNELIWLNEKEEEEVAYDWSERNTNIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTIEAYR 780
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  781 AAMQTQWSWILQLCQCVEQHIKENTAYFEFFNDAKEATDYLRNLKDAIQrkySCDRSSSIHKLEDLVQESMEEKEELLQY 860
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180
                   ....*....|....*....|...
gi 1761000869  861 KSTIANLMGKAKTIIQLKPRNSD 883
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDAD 181
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
876-942 1.66e-20

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 88.47  E-value: 1.66e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869  876 QLKPRNSdcPLKTSIPIKAICDYRQIEITIYKDDECVLANNSHRAKWKVISPTGNEAMVPSVCFTVP 942
Cdd:pfam17902    1 PLKQRRS--PVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
151-256 2.16e-19

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: 86.96  E-value: 2.16e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  151 MSAKERLLLWTQQATEGY-AGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQ--SNLANLEHAFYVAE-KIGViR 226
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEkKLGV-P 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 1761000869  227 LLDPEDVDVSSPDEKSVITYVSSLYDAFPK 256
Cdd:pfam00307   80 KVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5282-5497 8.71e-19

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: 88.66  E-value: 8.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5282 RLEEFYSKLKEFSILLQKAEEHEESQGPVGMEtETINQQLNMFKVFQKEeIEPLQGKQQDVNWLGQGLIQSAAKSTSTqg 5361
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAE-LAAHEERVEALNELGEQLIEEGHPDAEE-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5362 LEHDLDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDALEsLLSWMVDTEELVANQKPPSAEFKvVKAQIQEQKLLQRL 5441
Cdd:cd00176     77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEE 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1761000869 5442 LDDRKSTVEVIKREGEKIATTAEPADKVKILKQLSLLDSRWEALLNKAETRNRQLE 5497
Cdd:cd00176    155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5832-6048 1.33e-18

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 88.27  E-value: 1.33e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5832 QFWETYEELWPWLTETQSIISQLPAPALEyETLRQQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPGEGFSIQEKYV 5911
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5912 AADTLYSQIKEDVKKRAVALDEAISQStQFHDKIDQILESLERIVERLRQPPsISAEVEKIKEQISENKNVSVDMEKLQP 5991
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASED-LGKDLESVEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 5992 LYETLKQRGEEMIARSGGTdkdiSAKAVQDKLDQMVFIWENIHTLVEEREAKLLDVM 6048
Cdd:cd00176    161 RLKSLNELAEELLEEGHPD----ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
6272-6373 1.52e-18

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 84.30  E-value: 1.52e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  6272 QFQHALDELLAWLTHTEGLLSeQKPVGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSaGEEASNLQNKL 6351
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-HPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 1761000869  6352 EVLNQRWQNVLEKTEQRKQQLD 6373
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5722-5935 4.51e-18

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 86.73  E-value: 4.51e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5722 QQFDQAADAELSWITETEKKLMSLGDIRLEQdQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTACSEEeKQSMKKK 5801
Cdd:cd00176      3 QQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5802 LDKVLKNYDTICQINSERYLQLERAQSLVNQFWETyEELWPWLTETQSIISQLPAPAlEYETLRQQQEEHRQLRELIAEH 5881
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1761000869 5882 KPHIDKMNKTGPQLLELSPGEGF-SIQEKYVAADTLYSQIKEDVKKRAVALDEAI 5935
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4514-4735 1.43e-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: 85.19  E-value: 1.43e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4514 KLQKAQEESSAMMQWLQKMNKTATKWQqtpAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELLEENPdtPEAP 4593
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTD---YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH--PDAE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4594 RWKQMLTEIDSKWQELNQLTIDRQQKLEESSNNLTQFQTVEaQLKQWLVEKELMVSVLGPLSiDPNMLNTQRQQVQILLQ 4673
Cdd:cd00176     76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEE 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1761000869 4674 EFATRKPQYEQLTAAGQGILSRpgEDPSLRGIVKEQLAAVTQKWDSLTGQLSDRCDWIDQAI 4735
Cdd:cd00176    154 ELEAHEPRLKSLNELAEELLEE--GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
155-250 2.72e-17

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: 80.82  E-value: 2.72e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   155 ERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSN----LANLEHAFYVAEKIGVIR-LLD 229
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVvLFE 80
                            90       100
                    ....*....|....*....|.
gi 1761000869   230 PEDVDVSSPDEKSVITYVSSL 250
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4740-4954 1.54e-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: 82.11  E-value: 1.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4740 QYQSLLRSLSDKLSDLDNKLS--SSLAVSTHPDAMNQQLETAQKMKQEIQQEKKQIKVAQALCEDLSALVKEEylKAELS 4817
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEEllSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD--AEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4818 RQLEGILKSFKDVEQKAENHVQHLQSAcASSHQFQQMSRDFQAWLDtKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLT 4897
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLE-EKEAALASEDLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 4898 AQSHMYEKTIAEGENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLKESL 4954
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5503-5718 3.19e-15

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: 78.26  E-value: 3.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5503 AQQFHETLEPLNEWLTTIEKRLVNCEPIGTQASkLEEQIAQHKVLQEDILLRKQNVDQALLNGLELLKQTtGDEVLIIQD 5582
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLES-VEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5583 KLEAIKARYKDITKLSTDVAKTLEQALQLARRLHStHEELCTWLDKVEVELLSYEtqVLKGEEASQAQM-RPKELKKEAK 5661
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASED--LGKDLESVEELLkKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 5662 NNKALLDSLNEVSSALLELVPWRAREGLEKMVAEDNERYRLVSDTITQKVEEIDAAI 5718
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3924-4153 5.29e-15

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: 77.87  E-value: 5.29e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3924 ELEKFDADYTEFEHWLQQSEQELENLEAGaDDINGLMTKLKRQKSFSEDVISHKGDLRYITISGNRVLEAAKSCSKrdgg 4003
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE---- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4004 kvdtsathrEVQRKLDHATDRFRSLYSKCNVLGNNLKDLVDKYQHYEDASCgLLAGLQACEATASkhlSEPIAVDPKNLQ 4083
Cdd:cd00176     76 ---------EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA---SEDLGKDLESVE 142
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4084 RQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGSllPAKNDIQKTLDDIVGRYEDLSKSVNERNEKLQ 4153
Cdd:cd00176    143 ELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLE 210
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6272-6372 1.70e-14

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: 72.74  E-value: 1.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6272 QFQHALDELLAWLTHTEGLLSEQkPVGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSaGEEASNLQNKL 6351
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEG-HYASEEIQERL 82
                           90       100
                   ....*....|....*....|.
gi 1761000869 6352 EVLNQRWQNVLEKTEQRKQQL 6372
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKL 103
SPEC smart00150
Spectrin repeats;
6709-6809 4.02e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 71.59  E-value: 4.02e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  6709 QFTDALQALIDWLYRVEPQLAeDQPVHGDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARELIEGSRDDSSWVKVQMQ 6788
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 1761000869  6789 ELSTRWETVCALSISKQTRLE 6809
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
6599-6701 1.11e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 64.66  E-value: 1.11e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  6599 QFHEAWSKLMEWLEESEKSLDSElEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEKTSlaDDNLKLDDM 6678
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH--PDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 1761000869  6679 LSELRDKWDTICGKSVERQNKLE 6701
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
702-802 6.61e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 62.35  E-value: 6.61e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   702 HNFVSRATNELIWLNEKEEEEVAYDWSERNTNIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTIEAYRA 781
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 1761000869   782 AMQTQWSWILQLCQCVEQHIK 802
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
7092-7155 1.98e-10

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.12  E-value: 1.98e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1761000869 7092 RVMDFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLEmsAVADIFDRDGDGYIDYYEFVAALHP 7155
Cdd:COG5126     70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEAD--ELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
7092-7154 2.20e-10

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 59.48  E-value: 2.20e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1761000869 7092 RVMDFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAALH 7154
Cdd:cd00051      1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3613-4395 4.35e-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: 67.39  E-value: 4.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3613 ESVTTQVERLETQLH-LEQDLDD-QKIVAERQQEYkEKLQGICDLLTQTENRLighqeafmigdgTVELKKYQSKQEELQ 3690
Cdd:TIGR02168  249 KEAEEELEELTAELQeLEEKLEElRLEVSELEEEI-EELQKELYALANEISRL------------EQQKQILRERLANLE 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3691 KDMQGSAQALAEVvkntenflkENGEKLSQEDKALIEQKLNEAKIKCEQLNLK---AEQSKKELDKVVTTAIKEETEKVA 3767
Cdd:TIGR02168  316 RQLEELEAQLEEL---------ESKLDELAEELAELEEKLEELKEELESLEAEleeLEAELEELESRLEELEEQLETLRS 386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3768 AVKQLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIEQNGTHFQEGDGKSAIGEEDEVNGNLLETDvdgqvgTTQENLN 3847
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ------EELERLE 460
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3848 QQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGQYLspEEKEKLQKNMKELKvhyetalaESEKKMKLTHSLQEELEK 3927
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQ--ENLEGFSEGVKALL--------KNQSGLSGILGVLSELIS 530
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3928 FDADY-TEFEHWLQQSEQEL--ENLEAGADDINGLMTKLKRQKSFSE-DVISH---KGDLRYITISGNRVLEAAKSCSKR 4000
Cdd:TIGR02168  531 VDEGYeAAIEAALGGRLQAVvvENLNAAKKAIAFLKQNELGRVTFLPlDSIKGteiQGNDREILKNIEGFLGVAKDLVKF 610
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4001 D-----------GGK--VDTSATHREVQRKLDHATdRFRSLYSkcnvlgnnlkDLVdkyqhyedASCGLLAGlqACEATA 4067
Cdd:TIGR02168  611 DpklrkalsyllGGVlvVDDLDNALELAKKLRPGY-RIVTLDG----------DLV--------RPGGVITG--GSAKTN 669
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4068 SKHLSEPIAVdpKNLQRQLEEtkaLQGQISSQQVAVEKLKKTAEVLLDARGSLLPAKNDIQKTLDDIVGRYEDLSKSVN- 4146
Cdd:TIGR02168  670 SSILERRREI--EELEEKIEE---LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEq 744
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4147 --ERNEKLQITLTRSLSVQDGLDEMLDwmgnvesslkeqgqvpLNSTALQDIISKNIMLEQDIAGRQSSINAMNEKVkkf 4224
Cdd:TIGR02168  745 leERIAQLSKELTELEAEIEELEERLE----------------EAEEELAEAEAEIEELEAQIEQLKEELKALREAL--- 805
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4225 mettdpstaSSLQAKMKDLSARFSEASHKHKETLAKMEELKTKVELFENLSEKLQtfletktqaltevdvpgKDVTELSQ 4304
Cdd:TIGR02168  806 ---------DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS-----------------EDIESLAA 859
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4305 YMQESTSEFLEHKKHLEvlhSLLKEISSHGLpsDKALVLEKTNNLSKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSL 4384
Cdd:TIGR02168  860 EIEELEELIEELESELE---ALLNERASLEE--ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
                          810
                   ....*....|.
gi 1761000869 4385 KSWIKETTKKV 4395
Cdd:TIGR02168  935 EVRIDNLQERL 945
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1775-1813 1.19e-09

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 56.95  E-value: 1.19e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1761000869 1775 LLSAQLLSGGLINSNSGQRMTVEEAVREGVIDRDTASSI 1813
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC smart00150
Spectrin repeats;
5396-5497 1.43e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 58.50  E-value: 1.43e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  5396 RFQDALESLLSWMVDTEELVAnQKPPSAEFKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKIaTTAEPADKVKILKQL 5475
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQL-IEEGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 1761000869  5476 SLLDSRWEALLNKAETRNRQLE 5497
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
4516-4621 4.18e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 57.34  E-value: 4.18e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  4516 QKAQEESSAMMQWLQKMNKTAtkwQQTPAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELLEENPdtPEAPRW 4595
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL---ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH--PDAEEI 75
                            90       100
                    ....*....|....*....|....*.
gi 1761000869  4596 KQMLTEIDSKWQELNQLTIDRQQKLE 4621
Cdd:smart00150   76 EERLEELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4745-5615 5.43e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.54  E-value: 5.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4745 LRSLSDKLSDLDNKLSSSLAVSTHpDAMNQQLETAQKMKQEIQQEKKQIKVAQalcEDLSALVKEEYLKAELSRQLEGIL 4824
Cdd:TIGR02168  215 YKELKAELRELELALLVLRLEELR-EELEELQEELKEAEEELEELTAELQELE---EKLEELRLEVSELEEEIEELQKEL 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4825 KSFKDVEQKAENHVQHLQSACASSHQFQQMSRDFQAWLDTKKEEQNKS-HPISAKLDVLeslikdhkdfsktltaqshmy 4903
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEElAELEEKLEEL--------------------- 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4904 eKTIAEGENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLkESLEKALKY-KEQVETLWPWIDKCQNNLEEIK 4982
Cdd:TIGR02168  350 -KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI-ASLNNEIERlEARLERLEDRRERLQQEIEELL 427
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4983 FCLDPAEGENSIAKLKSLQKEMDQHFGMVELLNNTANsllsvcEIDKEVvtDENKSLIQKVDMVTEQLHSKKFCLENMTQ 5062
Cdd:TIGR02168  428 KKLEEAELKELQAELEELEEELEELQEELERLEEALE------ELREEL--EEAEQALDAAERELAQLQARLDSLERLQE 499
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5063 KFKEFQevskESKRQLQCAKEQL-DIHDSLGSQaysnkyltmLQTQQKSLQALkhQVDLAKRLaQDLVVEASDSkgtsdV 5141
Cdd:TIGR02168  500 NLEGFS----EGVKALLKNQSGLsGILGVLSEL---------ISVDEGYEAAI--EAALGGRL-QAVVVENLNA-----A 558
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5142 LLQVETIAQEHSTlsqqvdeKCSFLETKLQGIGHFQNTIREM---FSQFAEFDDELDSMAPVGRDA-----------ETL 5207
Cdd:TIGR02168  559 KKAIAFLKQNELG-------RVTFLPLDSIKGTEIQGNDREIlknIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvDDL 631
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5208 QkqkeTIKAFLKKLEALM--------------ASNDNANKTCKMMLAT----EETSPDLVGIKRDLEALSKQCNKLLDRA 5269
Cdd:TIGR02168  632 D----NALELAKKLRPGYrivtldgdlvrpggVITGGSAKTNSSILERrreiEELEEKIEELEEKIAELEKALAELRKEL 707
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5270 QAREEQVEGTIKRLEEFYSKLKEFSILLQKAEEheesqgpvgmETETINQQLNMFKVFQKEEIEPLQGKQQDVNWLGQGL 5349
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEA----------EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5350 IQSAAKSTStqgLEHDLDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDALESLLSWMVDTEElvanqkppsaEFKVVK 5429
Cdd:TIGR02168  778 AEAEAEIEE---LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER----------RLEDLE 844
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5430 AQIQEQKllqrllDDRKSTVEVIKREGEKIATTAEPADKVkiLKQLSLLDSRWEALLNKAETRNRQLEGISVVAQQFHET 5509
Cdd:TIGR02168  845 EQIEELS------EDIESLAAEIEELEELIEELESELEAL--LNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5510 LEPLNEWLTTIEKRLvncEPIGTQASKLEEQIA-QHKVLQEDILLRKQNVD------QALLNGLELLKQTTGDEVLIIQD 5582
Cdd:TIGR02168  917 LEELREKLAQLELRL---EGLEVRIDNLQERLSeEYSLTLEEAEALENKIEddeeeaRRRLKRLENKIKELGPVNLAAIE 993
                          890       900       910
                   ....*....|....*....|....*....|...
gi 1761000869 5583 KLEAIKARYKDITKLSTDVAKTLEQALQLARRL 5615
Cdd:TIGR02168  994 EYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
SPEC smart00150
Spectrin repeats;
4849-4951 1.01e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 56.18  E-value: 1.01e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  4849 HQFQQMSRDFQAWLDtKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLTAQSHMYEKTIAEGENlLLKTQGSEKAALQLQ 4928
Cdd:smart00150    1 QQFLRDADELEAWLE-EKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQ-LIEEGHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 1761000869  4929 LNTIKTNWDTFNKQVKERENKLK 4951
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
6052-6154 1.09e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 56.18  E-value: 1.09e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  6052 EKFWCDHMSLIVTIKDTQDFIRDlEDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAAcGEPDKPIVKKS 6131
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 1761000869  6132 IDELNSAWDSLNKAWKDRIDKLE 6154
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4514-4622 2.41e-08

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: 55.40  E-value: 2.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4514 KLQKAQEESSAMMQWLQKMNKTATkwqQTPAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELLEENPdtPEAP 4593
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLS---SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH--YASE 76
                           90       100
                   ....*....|....*....|....*....
gi 1761000869 4594 RWKQMLTEIDSKWQELNQLTIDRQQKLEE 4622
Cdd:pfam00435   77 EIQERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
6490-6591 2.96e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 55.03  E-value: 2.96e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  6490 EFHNSLQDFINWLTQAEQTLNVASRPSLiLDTVLFQIDEHKVFANEVNSHREQIIELDKTGTHLKyFSQKQDVVLIKNLL 6569
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKD-LESVEALLKKHEAFEAELEAHEERVEALNELGEQLI-EEGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 1761000869  6570 ISVQSRWEKVVQRLVERGRSLD 6591
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
6162-6264 3.63e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 54.64  E-value: 3.63e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  6162 QYQDGLQAVFDWVDIAGGKLASMsPIGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEESDKhtVQDP 6241
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE--IEER 78
                            90       100
                    ....*....|....*....|...
gi 1761000869  6242 LMELKLIWDSLEERIINRQHKLE 6264
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
EF-hand_7 pfam13499
EF-hand domain pair;
7090-7153 7.91e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 52.64  E-value: 7.91e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1761000869 7090 KSRVMDFFRRIDKDQDGKITRQEFIDGI--LSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAAL 7153
Cdd:pfam13499    1 EEKLKEAFKLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6599-6702 9.04e-08

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: 53.48  E-value: 9.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6599 QFHEAWSKLMEWLEESEKSLDSElEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEktSLADDNLKLDDM 6678
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID--EGHYASEEIQER 81
                           90       100
                   ....*....|....*....|....
gi 1761000869 6679 LSELRDKWDTICGKSVERQNKLEE 6702
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6076-6155 9.68e-08

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: 53.48  E-value: 9.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6076 EDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAAcGEPDKPIVKKSIDELNSAWDSLNKAWKDRIDKLEE 6155
Cdd:pfam00435   27 EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6709-6810 1.15e-07

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: 53.48  E-value: 1.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6709 QFTDALQALIDWLYRVEPQLAEDQPVHgDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARELIEGSRDDSSWVKVQMQ 6788
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|..
gi 1761000869 6789 ELSTRWETVCALSISKQTRLEA 6810
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4956-5167 1.31e-07

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: 55.91  E-value: 1.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4956 KALKYKEQVETLWPWIDKCQNNLEEIKFCLDPAEGENSIAKLKSLQKEMDQHFGMVELLNNTANSLLSVCEIDKEVVTDE 5035
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5036 NKSLIQKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRqLQCAKEQLDIHDSLGSQAYSNKYLTMLQTQQKSLQALK 5115
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQW-LEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1761000869 5116 HQVDLAKRLAQDLvVEASDSKGTSDVLLQVETIAQEHSTLSQQVDEKCSFLE 5167
Cdd:cd00176    160 PRLKSLNELAEEL-LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
5722-5824 1.37e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.10  E-value: 1.37e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  5722 QQFDQAADAELSWITETEKKLMSLgDIRLEQDQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTAcSEEEKQSMKKK 5801
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 1761000869  5802 LDKVLKNYDTICQINSERYLQLE 5824
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
5832-5932 1.57e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.72  E-value: 1.57e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  5832 QFWETYEELWPWLTETQSIISQLPAPALEyETLRQQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPGEGFSIQEKYV 5911
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDL-ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 1761000869  5912 AADTLYSQIKEDVKKRAVALD 5932
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
608-699 3.07e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.95  E-value: 3.07e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   608 VQDLLNWVDEMQVQLDRTEWGSDLPSVESHLENHKNVHRAIEEFESSLKEAKISEIQMTA---PLKLTYAEKLHRLESQY 684
Cdd:smart00150    7 ADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEeghPDAEEIEERLEELNERW 86
                            90
                    ....*....|....*
gi 1761000869   685 AKLLNTSRNQERHLD 699
Cdd:smart00150   87 EELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
1774-1810 3.50e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 49.79  E-value: 3.50e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1761000869  1774 RLLSAQLLSGGLINSNSGQRMTVEEAVREGVIDRDTA 1810
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
3611-4401 4.49e-07

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 57.44  E-value: 4.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3611 VQESVTTQVERLETQLHLEQDLDdqkivaERQQEYKEklQGICDLLTQTenrlighQEAFMIGDGTVELKKYQSK-QEEL 3689
Cdd:pfam15921   79 VLEEYSHQVKDLQRRLNESNELH------EKQKFYLR--QSVIDLQTKL-------QEMQMERDAMADIRRRESQsQEDL 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3690 QKDMQGSAQALAEVVKNTENFLKENGEKLSQEDKALIEQKLNEAKIKCEQLNLKAEQSKK-------------ELDKVVT 3756
Cdd:pfam15921  144 RNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmstmhfrSLGSAIS 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3757 TAIKEETEKVAAVK--------QLEESKTKIENLLDWLSNVDKDS-ERAGTKHKqvIEQNGTHFQEGDGKSA-------- 3819
Cdd:pfam15921  224 KILRELDTEISYLKgrifpvedQLEALKSESQNKIELLLQQHQDRiEQLISEHE--VEITGLTEKASSARSQansiqsql 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3820 -IGEEDEVNGNLLETDVDGQVGTTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGQYLSPEE---KEKLQK 3895
Cdd:pfam15921  302 eIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESgnlDDQLQK 381
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3896 NMKELKVHYETALAESEKKMKL----------THSLQEELEKFDADYTEFEHWLQQSEQELE-NLEAGADDINGLMTKLK 3964
Cdd:pfam15921  382 LLADLHKREKELSLEKEQNKRLwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLE 461
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3965 RQKSFSEDVISHKGDLRYITisgnRVLEAAKSCSKRDGGKV-DTSATHREVQRKLDHATDRFRSLYSKCNVLGNNLKDLV 4043
Cdd:pfam15921  462 KVSSLTAQLESTKEMLRKVV----EELTAKKMTLESSERTVsDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLK 537
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4044 DKYQHYEDASCgllaglqACEATASKHLSEPIAVDPknLQRQLEETKALQGQ--ISSQQVAVEKLKKTAEVLlDARGSL- 4120
Cdd:pfam15921  538 NEGDHLRNVQT-------ECEALKLQMAEKDKVIEI--LRQQIENMTQLVGQhgRTAGAMQVEKAQLEKEIN-DRRLELq 607
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4121 ----LPAKNDIQktLDDIVGRYEDLS----KSVNERNEKLQitltrslSVQDGLDEMLDWMGNVESSLKEqgqvplnsta 4192
Cdd:pfam15921  608 efkiLKDKKDAK--IRELEARVSDLElekvKLVNAGSERLR-------AVKDIKQERDQLLNEVKTSRNE---------- 668
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4193 LQDIISKNIMLEQDIAGRQSSINAMNEKVKKFMEttdpSTASSLQAKMKDLSARFSEASHKHKETLAKMEELKTKVELFE 4272
Cdd:pfam15921  669 LNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLK----SAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQID 744
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4273 NLSEKLQTFLETKTQALTEVDVPGKDVTELSQYMQESTSEFLEHKKHLEVLHS----LLKEISSHGLPSDKAlvlektnn 4348
Cdd:pfam15921  745 ALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSqerrLKEKVANMEVALDKA-------- 816
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 4349 lSKKFKEMEDTI-KEKKEAVT-SCQEQLDafqvlVKSLK--SWIKETTKKVPIVQPS 4401
Cdd:pfam15921  817 -SLQFAECQDIIqRQEQESVRlKLQHTLD-----VKELQgpGYTSNSSMKPRLLQPA 867
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4849-4952 5.11e-07

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: 51.55  E-value: 5.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4849 HQFQQMSRDFQAWLDtKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLTAQSHMYEKTIAEGENlLLKTQGSEKAALQLQ 4928
Cdd:pfam00435    4 QQFFRDADDLESWIE-EKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEK-LIDEGHYASEEIQER 81
                           90       100
                   ....*....|....*....|....
gi 1761000869 4929 LNTIKTNWDTFNKQVKERENKLKE 4952
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
4047-4153 7.51e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.79  E-value: 7.51e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  4047 QHYEDASCGLLAGLQACEATASkhlSEPIAVDPKNLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGsllPAKND 4126
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLA---SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH---PDAEE 74
                            90       100
                    ....*....|....*....|....*..
gi 1761000869  4127 IQKTLDDIVGRYEDLSKSVNERNEKLQ 4153
Cdd:smart00150   75 IEERLEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
5719-5825 1.96e-06

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: 50.01  E-value: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5719 LRSQQFDQAADAELSWITETEKKLMSlGDIRLEQDQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTACSEEEKQsM 5798
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE-I 78
                           90       100
                   ....*....|....*....|....*..
gi 1761000869 5799 KKKLDKVLKNYDTICQINSERYLQLER 5825
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
5396-5497 8.58e-06

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: 48.08  E-value: 8.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5396 RFQDALESLLSWMVDTEELVANQKPPSaEFKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKIaTTAEPADKVKILKQL 5475
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKL-IDEGHYASEEIQERL 82
                           90       100
                   ....*....|....*....|..
gi 1761000869 5476 SLLDSRWEALLNKAETRNRQLE 5497
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLE 104
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4072-4153 2.48e-05

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: 46.54  E-value: 2.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4072 SEPIAVDPKNLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGsllPAKNDIQKTLDDIVGRYEDLSKSVNERNEK 4151
Cdd:pfam00435   26 SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH---YASEEIQERLEELNERWEQLLELAAERKQK 102

                   ..
gi 1761000869 4152 LQ 4153
Cdd:pfam00435  103 LE 104
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4163-4370 2.77e-05

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 48.98  E-value: 2.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4163 QDGLDEMLDWMGNVESSLKEQgQVPLNSTALQDIISKNIMLEQDIAGRQSSINAMNEKVKKFMEtTDPSTASSLQAKMKD 4242
Cdd:cd00176      6 LRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQERLEE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4243 LSARFSEASHKhkeTLAKMEELKTKVELFENLSE--KLQTFLETKTQALTEVDVPG--KDVTELSQYMQESTSEFLEHKK 4318
Cdd:cd00176     84 LNQRWEELREL---AEERRQRLEEALDLQQFFRDadDLEQWLEEKEAALASEDLGKdlESVEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1761000869 4319 HLEVLHSLLKEISSHGLPSDKALVLEKTNNLSKKFKEMEDTIKEKKEAVTSC 4370
Cdd:cd00176    161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
5281-5389 3.45e-05

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: 46.16  E-value: 3.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5281 KRLEEFYSKLKEFSILLQKAEEHEESQGPVGMETEtINQQLNMFKVFQKEeIEPLQGKQQDVNWLGQGLIQSAAKSTSTq 5360
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLES-VQALLKKHKALEAE-LAAHQDRVEALNELAEKLIDEGHYASEE- 77
                           90       100
                   ....*....|....*....|....*....
gi 1761000869 5361 gLEHDLDDVNARWKTLNKKVAQRAAQLQE 5389
Cdd:pfam00435   78 -IQERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
701-795 3.95e-05

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: 46.16  E-value: 3.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  701 LHNFVSRATNELIWLNEKEE----EEVAYDWSErntnIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTI 776
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEAllssEDYGKDLES----VQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90
                   ....*....|....*....
gi 1761000869  777 EAYRAAMQTQWSWILQLCQ 795
Cdd:pfam00435   79 QERLEELNERWEQLLELAA 97
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6490-6592 4.36e-05

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: 46.16  E-value: 4.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6490 EFHNSLQDFINWLTQAEQTLNVASRPSLiLDTVLFQIDEHKVFANEVNSHREQIIELDKTGTHLKYfSQKQDVVLIKNLL 6569
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGKD-LESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASEEIQERL 82
                           90       100
                   ....*....|....*....|...
gi 1761000869 6570 ISVQSRWEKVVQRLVERGRSLDD 6592
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
1033-1269 4.54e-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: 50.49  E-value: 4.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 1033 DITQLEKEVNVCK---QYYQELLKSAEREEQEESVYNLYIS----------------------EVRNIRLRLENC---ED 1084
Cdd:pfam05483  451 EIHDLEIQLTAIKtseEHYLKEVEDLKTELEKEKLKNIELTahcdklllenkeltqeasdmtlELKKHQEDIINCkkqEE 530
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 1085 RLIRQIRTPLERddlhESVFRiTEQEKLKKELERLKDDLGTITNKCEE-FFSQAAASSSVPTLRSELNVVLQNMNQVYSM 1163
Cdd:pfam05483  531 RMLKQIENLEEK----EMNLR-DELESVREEFIQKGDEVKCKLDKSEEnARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 1164 SSTYIDKLKTVNLVLKNTQAAEA-LVKLYETKLCEEEAVIAD-KNNIENLISTlkqWRSEVDEKRQVFHALEDELQKAKA 1241
Cdd:pfam05483  606 KNKNIEELHQENKALKKKGSAENkQLNAYEIKVNKLELELASaKQKFEEIIDN---YQKEIEDKKISEEKLLEEVEKAKA 682
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1761000869 1242 ISDEMFKTYKERDLD-----------FDWHKEKADQLVE 1269
Cdd:pfam05483  683 IADEAVKLQKEIDKRcqhkiaemvalMEKHKHQYDKIIE 721
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6162-6264 8.95e-05

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: 45.00  E-value: 8.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6162 QYQDGLQAVFDWVDIAGGKLASMsPIGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEESDKhtVQDP 6241
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQER 81
                           90       100
                   ....*....|....*....|...
gi 1761000869 6242 LMELKLIWDSLEERIINRQHKLE 6264
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLE 104
SPEC smart00150
Spectrin repeats;
5284-5388 3.03e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.47  E-value: 3.03e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  5284 EEFYSKLKEFSILLQKAEEHEESQgPVGMETETINQQLNMFKVFQKEeIEPLQGKQQDVNWLGQGLIQSAAKSTSTqgLE 5363
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAE-LEAHEERVEALNELGEQLIEEGHPDAEE--IE 76
                            90       100
                    ....*....|....*....|....*
gi 1761000869  5364 HDLDDVNARWKTLNKKVAQRAAQLQ 5388
Cdd:smart00150   77 ERLEELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1194-1358 3.20e-04

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 45.90  E-value: 3.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 1194 KLCEEEAVIADKNNIENLISTLKQWRSEVDEKRQVFHALEdelQKAKAISDEmfktykeRDLDFDWHKEKADQLVERWQN 1273
Cdd:cd00176     21 ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALN---ELGEQLIEE-------GHPDAEEIQERLEELNQRWEE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 1274 VHVQIDNRLRDLEGIGKSLKYYRDTYHpLDDWIQqvETTQRKIQENQPENSKTLATQLNQQKMLVSEIEMKQSKMDECQK 1353
Cdd:cd00176     91 LRELAEERRQRLEEALDLQQFFRDADD-LEQWLE--EKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNE 167

                   ....*
gi 1761000869 1354 YAEQY 1358
Cdd:cd00176    168 LAEEL 172
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3886-4434 4.49e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 4.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3886 SPEEKEKLQKNMKELKvHYETALAESEKKMKLTHSLQEELEKFDADYTEFEHWLQQSEQELENLEagaDDINGLMTKLKR 3965
Cdd:PRK03918   143 SDESREKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVL---REINEISSELPE 218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3966 QKSFSEDVISHKGDLRYITisgNRVLEAAKSCSKRDGGKVDTSATHREVQRKLDHATDRFRSLYSKCNVLgNNLKDLVDK 4045
Cdd:PRK03918   219 LREELEKLEKEVKELEELK---EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEE 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4046 YQHYEDASCGLLAGLQACEATASKhLSEPIavdpKNLQRQLEE-------TKALQGQISSQQVAVEKLKKTAEVLLDARg 4118
Cdd:PRK03918   295 YIKLSEFYEEYLDELREIEKRLSR-LEEEI----NGIEERIKEleekeerLEELKKKLKELEKRLEELEERHELYEEAK- 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4119 SLLPAKNDIQKTLDDivgryedlsKSVNERNEKLQITLTRSLSVQDGLDEMLDWMGNVESSLKE-----------QGQVP 4187
Cdd:PRK03918   369 AKKEELERLKKRLTG---------LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElkkaieelkkaKGKCP 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4188 LNSTALQDIISKNIMLE-----QDIAGRQSSINAMNEKVKK-FMETTDPSTASSLQAKMKDLSARFSEASHKHKETlaKM 4261
Cdd:PRK03918   440 VCGRELTEEHRKELLEEytaelKRIEKELKEIEEKERKLRKeLRELEKVLKKESELIKLKELAEQLKELEEKLKKY--NL 517
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4262 EELKTKVELFENLSEKLQTfLETKTQALTevdvpgKDVTELSQYmqESTSEFLEHKKHL--EVLHSLLKEISSHGLPSDK 4339
Cdd:PRK03918   518 EELEKKAEEYEKLKEKLIK-LKGEIKSLK------KELEKLEEL--KKKLAELEKKLDEleEELAELLKELEELGFESVE 588
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4340 AL-----VLEKTNNLSKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSLKSWIKETTKKVPIVQPSFGAEDLGKSLEDT 4414
Cdd:PRK03918   589 ELeerlkELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEY 668
                          570       580
                   ....*....|....*....|
gi 1761000869 4415 KKLQEKWSLKTPEIQKVNNS 4434
Cdd:PRK03918   669 LELSRELAGLRAELEELEKR 688
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
4607-4835 1.74e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4607 QELNQLtidrQQKLEESSNNLTQFQT------VEAQLKQwlVEKELmvsvlgplsidpNMLNTQRQQVQILLQEFATRKP 4680
Cdd:COG3206    182 EQLPEL----RKELEEAEAALEEFRQknglvdLSEEAKL--LLQQL------------SELESQLAEARAELAEAEARLA 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4681 QYEQLTAAGQGILSRPGEDPSLRGIvKEQLAAVTQKWDSLTGQLSDrcdwidqaivKSTQYQSLLRSLSDKLSDLDNKLS 4760
Cdd:COG3206    244 ALRAQLGSGPDALPELLQSPVIQQL-RAQLAELEAELAELSARYTP----------NHPDVIALRAQIAALRAQLQQEAQ 312
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1761000869 4761 SSLAvsthpdAMNQQLETAQKMKQEIQQEKKQIKvaqalcEDLSALVKEEYLKAELSRQLEGILKSFKDVEQKAE 4835
Cdd:COG3206    313 RILA------SLEAELEALQAREASLQAQLAQLE------ARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
5423-5723 1.76e-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: 45.44  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5423 AEFKVVKAQIQEqklLQRLLDDRKSTVEVIKREGEKiattAEPADKVKILKQ---LSLLDSRWEALLNKAETRNRQLEGI 5499
Cdd:TIGR02169  177 EELEEVEENIER---LDLIIDEKRQQLERLRREREK----AERYQALLKEKReyeGYELLKEKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5500 SVVAQQFHETLEPLNEWLTTIEKRL--VNCE----------PIGTQASKLEEQIAQHKVLQEDILLRKQNVDQALLNGLE 5567
Cdd:TIGR02169  250 EEELEKLTEEISELEKRLEEIEQLLeeLNKKikdlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5568 LLKQTTGDevliIQDKLEAIKARYKDITKLSTDVAKTLEQALQLARRLHSTHEELCTWLDKV-----EVELLSYE----- 5637
Cdd:TIGR02169  330 EIDKLLAE----IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELkdyreKLEKLKREinelk 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5638 -TQVLKGEEASQAQMRPKELKKEAknnKALLDSLNEVSSALLEL------VPWRAREGLEKMVAEDNERYRL------VS 5704
Cdd:TIGR02169  406 rELDRLQEELQRLSEELADLNAAI---AGIEAKINELEEEKEDKaleikkQEWKLEQLAADLSKYEQELYDLkeeydrVE 482
                          330
                   ....*....|....*....
gi 1761000869 5705 DTITQKVEEIDAAILRSQQ 5723
Cdd:TIGR02169  483 KELSKLQRELAEAEAQARA 501
PLEC smart00250
Plectin repeat;
1552-1583 1.84e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.39  E-value: 1.84e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1761000869  1552 DKVIAGTIDQTTGEVLSVFQAVLRGLIDYDTG 1583
Cdd:smart00250    7 QSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
6085-6260 2.22e-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: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6085 VKQQQEAAETIREEIDGLQEELDiviNLGSELIAACGEPDKpiVKKSIDELNSAWDSLNKAWKDRIDKLEEamQAAVQYQ 6164
Cdd:COG3883     25 LSELQAELEAAQAELDALQAELE---ELNEEYNELQAELEA--LQAEIDKLQAEIAEAEAEIEERREELGE--RARALYR 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6165 DG-----LQAVFDWVDIAG--GKLASMSPIGTD----LETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTE-- 6231
Cdd:COG3883     98 SGgsvsyLDVLLGSESFSDflDRLSALSKIADAdadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAqq 177
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1761000869 6232 ----------ESDKHTVQDPLMELKLIWDSLEERIINRQ 6260
Cdd:COG3883    178 aeqeallaqlSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
5838-5933 2.51e-03

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 41.15  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5838 EELWPWLTETQSIISQLPAPAlEYETLRQQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPGEGFSIQEKYVAADTLY 5917
Cdd:pfam00435   11 DDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERW 89
                           90
                   ....*....|....*.
gi 1761000869 5918 SQIKEDVKKRAVALDE 5933
Cdd:pfam00435   90 EQLLELAAERKQKLEE 105
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
5360-5594 2.82e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 2.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5360 QGLEHDLDDVNARWKTLnkkvAQRAAQLQEALLHCGRFQDALESLLSWMVDTEELVANQK------PPSAEFKVVKAQIQ 5433
Cdd:COG4913    620 AELEEELAEAEERLEAL----EAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAelerldASSDDLAALEEQLE 695
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5434 E-QKLLQRLLDDRKSTVEVIKREGEKIA----------TTAEPADKVKILKQLSLLDSRWEALLNKAETRNrqlegisvV 5502
Cdd:COG4913    696 ElEAELEELEEELDELKGEIGRLEKELEqaeeeldelqDRLEAAEDLARLELRALLEERFAAALGDAVERE--------L 767
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5503 AQQFHETLEPLNEWLTTIEKRLVNC------------EPIGTQASKLEEQIAQHKVLQEDILLRKQnvDQAllngLELLK 5570
Cdd:COG4913    768 RENLEERIDALRARLNRAEEELERAmrafnrewpaetADLDADLESLPEYLALLDRLEEDGLPEYE--ERF----KELLN 841
                          250       260
                   ....*....|....*....|....*...
gi 1761000869 5571 QTTGDEVLIIQDKLEA----IKARYKDI 5594
Cdd:COG4913    842 ENSIEFVADLLSKLRRaireIKERIDPL 869
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
3234-3899 2.83e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 44.71  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3234 LLNILKQD-QHSQKITGVFELMRELTHMEY-----DLEKRGITSKVLPLQLEN----IFYKLLADgySEKIEHVGDFNQK 3303
Cdd:pfam05483  156 LCNLLKETcARSAEKTKKYEYEREETRQVYmdlnnNIEKMILAFEELRVQAENarleMHFKLKED--HEKIQHLEEEYKK 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3304 ACSTSEmmEEKPHILGDIKSKEGNYYSPNLeTVKEIGLESSTVWASTLPRDEKLKDLcNDFPSHLECTSGSKEMASGDSS 3383
Cdd:pfam05483  234 EINDKE--KQVSLLLIQITEKENKMKDLTF-LLEESRDKANQLEEKTKLQDENLKEL-IEKKDHLTKELEDIKMSLQRSM 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3384 TEQfsSELQQCLQHTEKmheylTLLQDMKPPLDNQESLDNNLEALKNQLRQLETFELGLAPIAVILRKDMKLAEEFLKSL 3463
Cdd:pfam05483  310 STQ--KALEEDLQIATK-----TICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKII 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3464 PSDFPR--GHVEELSISHQSLKTAFSSLSNVSSErtKQIMLAIDSEMSKLAvshEEFLHKLKSFSDWVSEKSKSVKDIEI 3541
Cdd:pfam05483  383 TMELQKksSELEEMTKFKNNKEVELEELKKILAE--DEKLLDEKKQFEKIA---EELKGKEQELIFLLQAREKEIHDLEI 457
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3542 ---VNVQDSEYVKKRLEFLKNVLKDLGHTKMQLETTAFDVQFFISEYAQ---DLSPNQSKQLLRLLNTTQKcfldvQESV 3615
Cdd:pfam05483  458 qltAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQeasDMTLELKKHQEDIINCKKQ-----EERM 532
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3616 TTQVERL-ETQLHLEQDLDDQKivaerqQEYKEKLQGI-CDLLTQTENRLIGHQEAFmigdgtvelkkyqsKQEELQKDM 3693
Cdd:pfam05483  533 LKQIENLeEKEMNLRDELESVR------EEFIQKGDEVkCKLDKSEENARSIEYEVL--------------KKEKQMKIL 592
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3694 QGSAQALAEVVKNTENFLKEngekLSQEDKALIEQ------KLNEAKIKCEQLNLKAEQSKKELDKVVTTAIKEetekva 3767
Cdd:pfam05483  593 ENKCNNLKKQIENKNKNIEE----LHQENKALKKKgsaenkQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE------ 662
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3768 avkqLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIEQNGTHFQEgdgKSAIGEEDEVNGNLLETDVDGQVGTTQeNLN 3847
Cdd:pfam05483  663 ----IEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAE---MVALMEKHKHQYDKIIEERDSELGLYK-NKE 734
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1761000869 3848 QQYQKVKAQHEKIISQHQAVIIATQSaQVLLEKqgqylspEEKEKLQKNMKE 3899
Cdd:pfam05483  735 QEQSSAKAALEIELSNIKAELLSLKK-QLEIEK-------EEKEKLKMEAKE 778
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1661-1698 3.49e-03

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 38.46  E-value: 3.49e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1761000869 1661 VLEILLSTGSLVIPATGEQLTLQKAFQQNLVSSALFSK 1698
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1851-1889 4.60e-03

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 38.08  E-value: 4.60e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1761000869 1851 VLEAQRGYVGLIWPHSGEIFPTSSSLQQELITNELAYKI 1889
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
6085-6483 4.97e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 4.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6085 VKQQQEAAETIREEIDGLQEELDIvinlgseliaacGEPDKPIVKKSIDELNSAWDSLnkawKDRIDKLEEAMQAAVQYQ 6164
Cdd:PRK02224   281 VRDLRERLEELEEERDDLLAEAGL------------DDADAEAVEARREELEDRDEEL----RDRLEECRVAAQAHNEEA 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6165 DGL-QAVFDWVDIAGGKLASMSPIGTDLETVKQQIEElkqfkseayqQQIEMERLNHQAELLLKKVTE-ESDKHTVQDPL 6242
Cdd:PRK02224   345 ESLrEDADDLEERAEELREEAAELESELEEAREAVED----------RREEIEELEEEIEELRERFGDaPVDLGNAEDFL 414
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6243 MELKLIWDSLEERIINRQHKLEGAllalgqfQHALDEllawlthTEGLLSEQK------PVGGDPKAIEIELAKHHV--L 6314
Cdd:PRK02224   415 EELREERDELREREAELEATLRTA-------RERVEE-------AEALLEAGKcpecgqPVEGSPHVETIEEDRERVeeL 480
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6315 QNDVLAHQSTVEAVNKAgndlIESsaGEEASNLQNKLEVLNQRWQNVLEKTEQRKQQLDGALRQAKGFHGEIEDLQqwlT 6394
Cdd:PRK02224   481 EAELEDLEEEVEEVEER----LER--AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE---A 551
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6395 DTERHLLASkplgglpETAKEQLNVHMEVCAAFEAKEETYKSLMQKgqqmLARCPKSAET--NIDQDINNLKEKWESVET 6472
Cdd:PRK02224   552 EAEEKREAA-------AEAEEEAEEAREEVAELNSKLAELKERIES----LERIRTLLAAiaDAEDEIERLREKREALAE 620
                          410
                   ....*....|.
gi 1761000869 6473 KLNERKTKLEE 6483
Cdd:PRK02224   621 LNDERRERLAE 631
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3610-3953 7.73e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 7.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3610 DVQESVTTQVERLEtqlhleqdldDQKIVAERQQEYKEKLQgICDL------LTQTENRLIGHQEAfmIGDGTVELKKYQ 3683
Cdd:COG1196    193 DILGELERQLEPLE----------RQAEKAERYRELKEELK-ELEAellllkLRELEAELEELEAE--LEELEAELEELE 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3684 SKQEELQKDMQGSAQALAEV-----VKNTENFLKENGEKLSQEDKALIEQKLNEAKIKCEQLNLKAEQSKKELDKVVTTA 3758
Cdd:COG1196    260 AELAELEAELEELRLELEELeleleEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3759 IKEETEKVAAVKQLEESKTKIENLLdwlsnvdkdsERAGTKHKQVIEQNGTHFQEGDGKSAIGEEDEVNGNLLEtdvdgQ 3838
Cdd:COG1196    340 EELEEELEEAEEELEEAEAELAEAE----------EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE-----E 404
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3839 VGTTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGqylspEEKEKLQKNMKELKVHYETALAESEKKMKLT 3918
Cdd:COG1196    405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA-----EEEAELEEEEEALLELLAELLEEAALLEAAL 479
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1761000869 3919 HSLQEELEKFDAdytefEHWLQQSEQELENLEAGA 3953
Cdd:COG1196    480 AELLEELAEAAA-----RLLLLLEAEADYEGFLEG 509
 
Name Accession Description Interval E-value
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
20-147 1.80e-85

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: 276.48  E-value: 1.80e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   20 QAYEDVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIA 99
Cdd:cd21236      1 QAYENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIA 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1761000869  100 LDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 147
Cdd:cd21236     81 LDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
34-138 6.28e-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: 242.69  E-value: 6.28e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   34 DKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKLVNI 113
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
                           90       100
                   ....*....|....*....|....*
gi 1761000869  114 RNDDITDGNPKLTLGLIWTIILHFQ 138
Cdd:cd21188     81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
152-255 5.65e-73

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: 239.89  E-value: 5.65e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLDPE 231
Cdd:cd21239      1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLGVTRLLDPE 80
                           90       100
                   ....*....|....*....|....
gi 1761000869  232 DVDVSSPDEKSVITYVSSLYDAFP 255
Cdd:cd21239     81 DVDVSSPDEKSVITYVSSLYDVFP 104
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
31-149 2.44e-67

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: 224.52  E-value: 2.44e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   31 DERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKL 110
Cdd:cd21235      1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1761000869  111 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGESE 149
Cdd:cd21235     81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
31-148 4.80e-65

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: 217.59  E-value: 4.80e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   31 DERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKL 110
Cdd:cd21237      1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1761000869  111 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGES 148
Cdd:cd21237     81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
152-255 7.43e-63

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: 211.10  E-value: 7.43e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-IGVIRLLDP 230
Cdd:cd21189      1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKeFGVTRLLDP 80
                           90       100
                   ....*....|....*....|....*
gi 1761000869  231 EDVDVSSPDEKSVITYVSSLYDAFP 255
Cdd:cd21189     81 EDVDVPEPDEKSIITYVSSLYDVFP 105
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
150-255 8.40e-56

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: 191.02  E-value: 8.40e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  150 DMSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLD 229
Cdd:cd21240      2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLD 81
                           90       100
                   ....*....|....*....|....*.
gi 1761000869  230 PEDVDVSSPDEKSVITYVSSLYDAFP 255
Cdd:cd21240     82 AEDVDVPSPDEKSVITYVSSIYDAFP 107
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
151-255 4.16e-50

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: 174.44  E-value: 4.16e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  151 MSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-IGVIRLLD 229
Cdd:cd21238      1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 1761000869  230 PEDVDVSSPDEKSVITYVSSLYDAFP 255
Cdd:cd21238     81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
31-135 4.64e-49

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


Pssm-ID: 409095  Cd Length: 117  Bit Score: 172.17  E-value: 4.64e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   31 DERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHRLQNVQIALDYLKRRQVK 109
Cdd:cd21246     11 DEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQRVH 90
                           90       100
                   ....*....|....*....|....*.
gi 1761000869  110 LVNIRNDDITDGNPKLTLGLIWTIIL 135
Cdd:cd21246     91 LENMGSHDIVDGNHRLTLGLIWTIIL 116
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
36-139 4.85e-47

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: 165.63  E-value: 4.85e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   36 VQKKTFTKWINQHLMKVRK-HVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKLVNIR 114
Cdd:cd21186      2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
                           90       100
                   ....*....|....*....|....*
gi 1761000869  115 NDDITDGNPKLTLGLIWTIILHFQI 139
Cdd:cd21186     82 SNDIVDGNPKLTLGLVWSIILHWQV 106
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
152-254 1.56e-44

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: 158.73  E-value: 1.56e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAE-KIGVIRLLDP 230
Cdd:cd21194      2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEqELGIAKLLDA 81
                           90       100
                   ....*....|....*....|....
gi 1761000869  231 EDVDVSSPDEKSVITYVSSLYDAF 254
Cdd:cd21194     82 EDVDVARPDEKSIMTYVASYYHYF 105
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
32-139 3.97e-44

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: 157.54  E-value: 3.97e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   32 ERDKVQKKTFTKWINQHLMKVRK--HVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRM--RFHRLQNVQIALDYLKRRQ 107
Cdd:cd21241      1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1761000869  108 VKLVNIRNDDITDGNPKLTLGLIWTIILHFQI 139
Cdd:cd21241     81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
35-254 4.88e-44

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 173.20  E-value: 4.88e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   35 KVQKKTFTKWINQHLMKV-RKHVNDLYEDLRDGHNLISLLEVLSGDTLPR--EKGRMRFHRLQNVQIALDYLKRRQVKLV 111
Cdd:COG5069      8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  112 NIRNDDITDGNPKLTLGLIWTIILHFQISDIHvtgESEDMSAKERLLLWTQQATEGYA-GIRCENFTTCWRDGKLFNAII 190
Cdd:COG5069     88 NIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALI 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1761000869  191 HKYRPDLIDMNTVAVQSN--LANLEHAFYVAEK-IGVIRLLDPEDV-DVSSPDEKSVITYVSSLYDAF 254
Cdd:COG5069    165 HDSRPDTLDPNVLDLQKKnkALNNFQAFENANKvIGIARLIGVEDIvNVSIPDERSIMTYVSWYIIRF 232
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
152-254 7.94e-43

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: 153.71  E-value: 7.94e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAE-KIGVIRLLDP 230
Cdd:cd21248      2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEqKLGLTKLLDP 81
                           90       100
                   ....*....|....*....|....
gi 1761000869  231 EDVDVSSPDEKSVITYVSSLYDAF 254
Cdd:cd21248     82 EDVNVEQPDEKSIITYVVTYYHYF 105
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
23-135 1.36e-42

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: 153.61  E-value: 1.36e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   23 EDVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHRLQNVQIALD 101
Cdd:cd21193      3 KGRIRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALA 82
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1761000869  102 YLKrRQVKLVNIRNDDITDGNPKLTLGLIWTIIL 135
Cdd:cd21193     83 FLK-TKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
31-135 4.70e-42

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


Pssm-ID: 409167  Cd Length: 139  Bit Score: 152.87  E-value: 4.70e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   31 DERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHRLQNVQIALDYLKRRQVK 109
Cdd:cd21318     33 DEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQRVH 112
                           90       100
                   ....*....|....*....|....*.
gi 1761000869  110 LVNIRNDDITDGNPKLTLGLIWTIIL 135
Cdd:cd21318    113 LENVGSHDIVDGNHRLTLGLIWTIIL 138
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
30-135 3.71e-40

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


Pssm-ID: 409166  Cd Length: 132  Bit Score: 147.12  E-value: 3.71e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   30 KDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHRLQNVQIALDYLKRRQV 108
Cdd:cd21317     25 ADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLKEQKV 104
                           90       100
                   ....*....|....*....|....*..
gi 1761000869  109 KLVNIRNDDITDGNPKLTLGLIWTIIL 135
Cdd:cd21317    105 HLENMGSHDIVDGNHRLTLGLIWTIIL 131
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
32-139 4.31e-40

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: 146.18  E-value: 4.31e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   32 ERDKVQKKTFTKWINQHLMKVRK--HVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRM--RFHRLQNVQIALDYLKRRQ 107
Cdd:cd21190      1 EQERVQKKTFTNWINSHLAKLSQpiVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1761000869  108 VKLVNIRNDDITDGNPKLTLGLIWTIILHFQI 139
Cdd:cd21190     81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6270-6485 1.63e-38

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: 145.67  E-value: 1.63e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6270 LGQFQHALDELLAWLTHTEGLLSEQKPvGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSAgEEASNLQN 6349
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6350 KLEVLNQRWQNVLEKTEQRKQQLDGALRQAKGFHgEIEDLQQWLTDTERhLLASKPLGGLPETAKEQLNVHMEVCAAFEA 6429
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEA-ALASEDLGKDLESVEELLKKHKELEEELEA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1761000869 6430 KEETYKSLMQKGQQMLARCPKSAETNIDQDINNLKEKWESVETKLNERKTKLEEAL 6485
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
148-257 3.13e-38

second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409168  Cd Length: 112  Bit Score: 140.91  E-value: 3.13e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  148 SEDMSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAE-KIGVIR 226
Cdd:cd21319      1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAErQLGITK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1761000869  227 LLDPEDVDVSSPDEKSVITYVSSLYDAFPKV 257
Cdd:cd21319     81 LLDPEDVFTENPDEKSIITYVVAFYHYFSKM 111
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
151-255 1.04e-37

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: 139.38  E-value: 1.04e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  151 MSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAE-KIGVIRLLD 229
Cdd:cd21243      4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEkELGIPRLLD 83
                           90       100
                   ....*....|....*....|....*.
gi 1761000869  230 PEDVDVSSPDEKSVITYVSSLYDAFP 255
Cdd:cd21243     84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
35-137 1.16e-37

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409064  Cd Length: 107  Bit Score: 139.07  E-value: 1.16e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   35 KVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR--EKGRMRFHRLQNVQIALDYLKRRQVKLVN 112
Cdd:cd21215      3 DVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTN 82
                           90       100
                   ....*....|....*....|....*
gi 1761000869  113 IRNDDITDGNPKLTLGLIWTIILHF 137
Cdd:cd21215     83 IGAEDIVDGNLKLILGLLWTLILRF 107
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
139-254 3.53e-37

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: 137.88  E-value: 3.53e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  139 ISDIHVtgesEDMSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYV 218
Cdd:cd21216      1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1761000869  219 AEK-IGVIRLLDPED-VDVSSPDEKSVITYVSSLYDAF 254
Cdd:cd21216     77 AEKhLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHAF 114
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
157-255 2.39e-36

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: 135.25  E-value: 2.39e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  157 LLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVA-EKIGVIRLLDPEDVDV 235
Cdd:cd21187      5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAhEHLGIEKLLDPEDVNV 84
                           90       100
                   ....*....|....*....|
gi 1761000869  236 SSPDEKSVITYVSSLYDAFP 255
Cdd:cd21187     85 EQPDKKSILMYVTSLFQVLP 104
GAS2 smart00243
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
7167-7242 2.54e-36

Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain


Pssm-ID: 128539  Cd Length: 73  Bit Score: 133.73  E-value: 2.54e-36
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1761000869  7167 DKIEDEVTRQVAKCKCAKRFQVEQIGDNKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCR 7242
Cdd:smart00243    1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRF------GDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCR 70
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
34-135 2.85e-36

first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409063  Cd Length: 105  Bit Score: 134.82  E-value: 2.85e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   34 DKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHRLQNVQIALDYLKRRQVKLVN 112
Cdd:cd21214      3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
                           90       100
                   ....*....|....*....|...
gi 1761000869  113 IRNDDITDGNPKLTLGLIWTIIL 135
Cdd:cd21214     83 IGAEEIVDGNLKMTLGMIWTIIL 105
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
32-139 3.78e-36

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409091  Cd Length: 111  Bit Score: 134.96  E-value: 3.78e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   32 ERDKVQKKTFTKWINQHLMK--VRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVK 109
Cdd:cd21242      1 EQEQTQKRTFTNWINSQLAKhsPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1761000869  110 LVNIRNDDITDGNPKLTLGLIWTIILHFQI 139
Cdd:cd21242     81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
31-139 9.00e-36

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: 133.89  E-value: 9.00e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   31 DERDKVQKKTFTKWINQHLMKVRK-HVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVK 109
Cdd:cd21231      1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1761000869  110 LVNIRNDDITDGNPKLTLGLIWTIILHFQI 139
Cdd:cd21231     81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
148-257 2.32e-35

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: 132.87  E-value: 2.32e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  148 SEDMSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-IGVIR 226
Cdd:cd21321      1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKeLGLTK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1761000869  227 LLDPEDVDVSSPDEKSVITYVSSLYDAFPKV 257
Cdd:cd21321     81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKM 111
GAS2 pfam02187
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ...
7169-7243 1.53e-34

Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members and Gas2 family members. The GAR domain comprises around 57 amino acids and has been shown to bind to microtubules.


Pssm-ID: 460480  Cd Length: 69  Bit Score: 128.48  E-value: 1.53e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1761000869 7169 IEDEVTRQVAKCKCAKRFQVEQIGDNKYRFflgnqfGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRV 7243
Cdd:pfam02187    1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRF------GDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
Spectrin_like pfam18373
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ...
977-1054 2.43e-34

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: 128.49  E-value: 2.43e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1761000869  977 VSWHYLINEIDRIRASNVASIKTMLPGEHQQVLSNLQSRFEDFLEDSQESQVFSGSDITQLEKEVNVCKQYYQELLKS 1054
Cdd:pfam18373    1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
151-256 5.89e-34

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: 128.44  E-value: 5.89e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  151 MSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAE-KIGVIRLLD 229
Cdd:cd21249      3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEqELGISQLLD 82
                           90       100
                   ....*....|....*....|....*..
gi 1761000869  230 PEDVDVSSPDEKSVITYVSSLYDAFPK 256
Cdd:cd21249     83 PEDVAVPHPDERSIMTYVSLYYHYFSK 109
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6709-6921 8.26e-34

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: 132.18  E-value: 8.26e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6709 QFTDALQALIDWLYRVEPQLAEDQPVHgDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARELIEGSRDDSSWVKVQMQ 6788
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6789 ELSTRWETVCALSISKQTRLEAALRQAEEFHSvVHALLEWLAEAEQTLRfHGVLPDDEDALRTLIDQHKEFMKKLEEKRA 6868
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1761000869 6869 ELNKATTMGDTVLAICHPDSITTIKHWITIIRARFEEVLAWAKQHQQRLASAL 6921
Cdd:cd00176    161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
151-255 1.68e-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: 127.15  E-value: 1.68e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  151 MSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-IGVIRLLD 229
Cdd:cd21192      2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQhLNIPRLLE 81
                           90       100
                   ....*....|....*....|....*.
gi 1761000869  230 PEDVDVSSPDEKSVITYVSSLYDAFP 255
Cdd:cd21192     82 VEDVLVDKPDERSIMTYVSQFLRMFP 107
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
136-257 3.30e-33

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: 127.09  E-value: 3.30e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  136 HFQISDIHVTGESEDMSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHA 215
Cdd:cd21322      1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1761000869  216 FYVAEK-IGVIRLLDPEDVDVSSPDEKSVITYVSSLYDAFPKV 257
Cdd:cd21322     81 FNTAEQhLGLTKLLDPEDVNMEAPDEKSIITYVVSFYHYFSKM 123
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
31-135 2.20e-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: 125.93  E-value: 2.20e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   31 DERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHRLQNVQIALDYLKRRQVK 109
Cdd:cd21316     48 DEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVH 127
                           90       100
                   ....*....|....*....|....*.
gi 1761000869  110 LVNIRNDDITDGNPKLTLGLIWTIIL 135
Cdd:cd21316    128 LENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
139-254 2.60e-31

second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409140  Cd Length: 115  Bit Score: 121.10  E-value: 2.60e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  139 ISDIHvtgeSEDMSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYV 218
Cdd:cd21291      1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1761000869  219 AEK-IGVIRLLDPEDV-DVSSPDEKSVITYVSSLYDAF 254
Cdd:cd21291     77 ASKeIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHAF 114
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
36-139 4.38e-31

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: 120.11  E-value: 4.38e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   36 VQKKTFTKWINQHLMKVRK-HVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKLVNIR 114
Cdd:cd21232      2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
                           90       100
                   ....*....|....*....|....*
gi 1761000869  115 NDDITDGNPKLTLGLIWTIILHFQI 139
Cdd:cd21232     82 GTDIVDGNHKLTLGLLWSIILHWQV 106
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
152-257 8.96e-31

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: 119.43  E-value: 8.96e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-IGVIRLLDP 230
Cdd:cd21320      2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLDP 81
                           90       100
                   ....*....|....*....|....*..
gi 1761000869  231 EDVDVSSPDEKSVITYVSSLYDAFPKV 257
Cdd:cd21320     82 EDISVDHPDEKSIITYVVTYYHYFSKM 108
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
35-139 9.43e-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: 119.31  E-value: 9.43e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   35 KVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR--EKGRMRFHRLQNVQIALDYLKRRQVKLVN 112
Cdd:cd21227      3 EIQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVN 82
                           90       100
                   ....*....|....*....|....*..
gi 1761000869  113 IRNDDITDGNPKLTLGLIWTIILHFQI 139
Cdd:cd21227     83 IGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
35-140 2.43e-30

first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409160  Cd Length: 124  Bit Score: 118.71  E-value: 2.43e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   35 KVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGR--MRFHRLQNVQIALDYLKRRQ-VKLV 111
Cdd:cd21311     14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
                           90       100
                   ....*....|....*....|....*....
gi 1761000869  112 NIRNDDITDGNPKLTLGLIWTIILHFQIS 140
Cdd:cd21311     94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
32-141 8.08e-30

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


Pssm-ID: 409040  Cd Length: 114  Bit Score: 116.91  E-value: 8.08e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   32 ERDKVQKKTFTKWINQHLMKVRK--HVNDLYEDLRDGHNLISLLEVLSGDTLPRE--KGRMRFHRLQNVQIALDYLKRRQ 107
Cdd:cd21191      1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1761000869  108 VKLVNIRNDDITDGNPKLTLGLIWTIILHFQISD 141
Cdd:cd21191     81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
151-248 8.70e-30

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: 116.47  E-value: 8.70e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  151 MSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-IGVIRLLD 229
Cdd:cd21244      4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQeLKIPRLLE 83
                           90
                   ....*....|....*....
gi 1761000869  230 PEDVDVSSPDEKSVITYVS 248
Cdd:cd21244     84 PEDVDVVNPDEKSIMTYVA 102
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
35-137 9.98e-30

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


Pssm-ID: 409032  Cd Length: 108  Bit Score: 116.43  E-value: 9.98e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   35 KVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR---EKGRMRFHRLQNVQIALDYLKRRQVKLV 111
Cdd:cd21183      3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
                           90       100
                   ....*....|....*....|....*.
gi 1761000869  112 NIRNDDITDGNPKLTLGLIWTIILHF 137
Cdd:cd21183     83 NIGSGDIVNGNIKLILGLIWTLILHY 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6596-6812 4.74e-29

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: 118.32  E-value: 4.74e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6596 RAKQFHEAWSKLMEWLEESEKSLDSElEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEktSLADDNLKL 6675
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6676 DDMLSELRDKWDTICGKSVERQNKLEEALLFSGQFTDALQaLIDWLYRVEPQLAEDQPVHgDIDLVMNLIDNHKAFQKEL 6755
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1761000869 6756 GKRTSSVQALKRSARELIEGSRDDSS-WVKVQMQELSTRWETVCALSISKQTRLEAAL 6812
Cdd:cd00176    156 EAHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
157-254 5.31e-29

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: 114.37  E-value: 5.31e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  157 LLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-IGVIRLLDPED-VD 234
Cdd:cd21253      6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKeLGIPALLDAEDmVA 85
                           90       100
                   ....*....|....*....|
gi 1761000869  235 VSSPDEKSVITYVSSLYDAF 254
Cdd:cd21253     86 LKVPDKLSILTYVSQYYNYF 105
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
35-137 3.86e-28

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


Pssm-ID: 409077  Cd Length: 108  Bit Score: 111.81  E-value: 3.86e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   35 KVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR---EKGRMRFHRLQNVQIALDYLKRRQVKLV 111
Cdd:cd21228      3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
                           90       100
                   ....*....|....*....|....*.
gi 1761000869  112 NIRNDDITDGNPKLTLGLIWTIILHF 137
Cdd:cd21228     83 SIDSSAIVDGNLKLILGLIWTLILHY 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6487-6704 5.45e-28

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: 115.24  E-value: 5.45e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6487 LAMEFHNSLQDFINWLTQAEQTLNVASRPSlILDTVLFQIDEHKVFANEVNSHREQIIELDKTGTHLKyFSQKQDVVLIK 6566
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6567 NLLISVQSRWEKVVQRLVERGRSLDDARKRAKQFHEAWsKLMEWLEESEKSLDSElEIANDPDKIKTQLAQHKEFQKSLG 6646
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1761000869 6647 AKHSVYDTTNRTGRSLKEKTSLADDNlKLDDMLSELRDKWDTICGKSVERQNKLEEAL 6704
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADE-EIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
152-254 5.86e-28

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: 111.36  E-value: 5.86e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLDPE 231
Cdd:cd21198      1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDPA 80
                           90       100
                   ....*....|....*....|....
gi 1761000869  232 DVDVSS-PDEKSVITYVSSLYDAF 254
Cdd:cd21198     81 DMVLLSvPDKLSVMTYLHQIRAHF 104
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
155-255 1.65e-27

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: 110.05  E-value: 1.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  155 ERLLL-WTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-IGVIRLLDPED 232
Cdd:cd21234      2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNhLGIEKLLDPED 81
                           90       100
                   ....*....|....*....|...
gi 1761000869  233 VDVSSPDEKSVITYVSSLYDAFP 255
Cdd:cd21234     82 VAVQLPDKKSIIMYLTSLFEVLP 104
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
157-256 2.62e-27

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: 109.63  E-value: 2.62e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  157 LLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSN-LANLEHAFYVAEK-IGVIRLLDPEDVD 234
Cdd:cd21233      5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQhLGIEKLLDPEDVA 84
                           90       100
                   ....*....|....*....|..
gi 1761000869  235 VSSPDEKSVITYVSSLYDAFPK 256
Cdd:cd21233     85 TAHPDKKSILMYVTSLFQVLPQ 106
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
35-140 4.30e-27

first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409159  Cd Length: 125  Bit Score: 109.73  E-value: 4.30e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   35 KVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPRE---KGRMRFHRLQNVQIALDYLKRRQVKLV 111
Cdd:cd21310     15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
                           90       100
                   ....*....|....*....|....*....
gi 1761000869  112 NIRNDDITDGNPKLTLGLIWTIILHFQIS 140
Cdd:cd21310     95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
137-260 1.05e-25

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: 105.55  E-value: 1.05e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  137 FQISDIHVtgesEDMSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAF 216
Cdd:cd21290      2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1761000869  217 YVAEK-IGVIRLLDPED-VDVSSPDEKSVITYVSSLYDAFPKVPEG 260
Cdd:cd21290     78 EVAEKyLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHAFSGAQKA 123
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
155-254 2.05e-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: 103.90  E-value: 2.05e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  155 ERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-IGVIRLLDPED- 232
Cdd:cd22198      3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQeLGIPPVMTGQEm 82
                           90       100
                   ....*....|....*....|..
gi 1761000869  233 VDVSSPDEKSVITYVSSLYDAF 254
Cdd:cd22198     83 ASLAVPDKLSMVSYLSQFYEAF 104
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
30-139 4.16e-25

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


Pssm-ID: 409096  Cd Length: 125  Bit Score: 103.68  E-value: 4.16e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   30 KDERDKVQKKTFTKWINQHLMKVRKHV--NDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHRLQNVQIALDYLKRR 106
Cdd:cd21247     14 QEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLKTK 93
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1761000869  107 -QVKLVNIRNddITDGNPKLTLGLIWTIILHFQI 139
Cdd:cd21247     94 vPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6162-6376 4.92e-25

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: 106.76  E-value: 4.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6162 QYQDGLQAVFDWVDIAGGKLASMSPiGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEESDKhtVQDP 6241
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--IQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6242 LMELKLIWDSLEERIINRQHKLEGALLALgQFQHALDELLAWLTHTEGLLSEQkPVGGDPKAIEIELAKHHVLQNDVLAH 6321
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1761000869 6322 QSTVEAVNKAGNDLIESSAGEEASNLQNKLEVLNQRWQNVLEKTEQRKQQLDGAL 6376
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
139-259 4.34e-24

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: 100.93  E-value: 4.34e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  139 ISDIHVtgesEDMSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYV 218
Cdd:cd21287      1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1761000869  219 AEK-IGVIRLLDPED-VDVSSPDEKSVITYVSSLYDAFPKVPE 259
Cdd:cd21287     77 AEKyLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHAFSGAQK 119
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
157-254 1.55e-23

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: 1.55e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  157 LLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-IGVIRLLDPED-VD 234
Cdd:cd21197      5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETsLGIPALLDAEDmVT 84
                           90       100
                   ....*....|....*....|
gi 1761000869  235 VSSPDEKSVITYVSSLYDAF 254
Cdd:cd21197     85 MHVPDRLSIITYVSQYYNHF 104
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
35-140 1.95e-23

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


Pssm-ID: 409158  Cd Length: 131  Bit Score: 99.38  E-value: 1.95e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   35 KVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR---EKGRMRFHRLQNVQIALDYLKRRQVKLV 111
Cdd:cd21309     16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
                           90       100
                   ....*....|....*....|....*....
gi 1761000869  112 NIRNDDITDGNPKLTLGLIWTIILHFQIS 140
Cdd:cd21309     96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
35-140 6.33e-23

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


Pssm-ID: 409157  Cd Length: 129  Bit Score: 97.85  E-value: 6.33e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   35 KVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR---EKGRMRFHRLQNVQIALDYLKRRQVKLV 111
Cdd:cd21308     19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
                           90       100
                   ....*....|....*....|....*....
gi 1761000869  112 NIRNDDITDGNPKLTLGLIWTIILHFQIS 140
Cdd:cd21308     99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6050-6267 6.64e-23

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: 100.60  E-value: 6.64e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6050 LAEKFWCDHMSLIVTIKDTQDFIRDlEDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAAcGEPDKPIVK 6129
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6130 KSIDELNSAWDSLNKAWKDRIDKLEEAMQAAVQYQDGLQAVfDWVDIAGGKLASMsPIGTDLETVKQQIEELKQFKSEAY 6209
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1761000869 6210 QQQIEMERLNHQAELLLKKVTEESDKHtVQDPLMELKLIWDSLEERIINRQHKLEGAL 6267
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEE-IEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
139-254 7.04e-23

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: 97.49  E-value: 7.04e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  139 ISDIHVtgesEDMSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYV 218
Cdd:cd21289      1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1761000869  219 AEK-IGVIRLLDPED-VDVSSPDEKSVITYVSSLYDAF 254
Cdd:cd21289     77 AEKyLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHAF 114
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
39-136 8.01e-23

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 96.23  E-value: 8.01e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869    39 KTFTKWINQHLMK-VRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREK---GRMRFHRLQNVQIALDYLKRRQVKLVNIR 114
Cdd:smart00033    1 KTLLRWVNSLLAEyDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 1761000869   115 NDDITDGnPKLTLGLIWTIILH 136
Cdd:smart00033   81 PEDLVEG-PKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5396-5609 1.31e-22

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: 99.83  E-value: 1.31e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5396 RFQDALESLLSWMVDTEELVANQKPPSAEfKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKIATtAEPADKVKILKQL 5475
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5476 SLLDSRWEALLNKAETRNRQLEGISVVAQQFHETLEpLNEWLTTIEKRLVNcEPIGTQASKLEEQIAQHKVLQEDILLRK 5555
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1761000869 5556 QNVDQALLNGLELLKQTTGDEVLIIQDKLEAIKARYKDITKLSTDVAKTLEQAL 5609
Cdd:cd00176    160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6378-6594 1.51e-22

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: 99.44  E-value: 1.51e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6378 QAKGFHGEIEDLQQWLTDTERhLLASKPLGGLPETAKEQLNVHMEVCAAFEAKEETYKSLMQKGQQMLARCPKSAEtNID 6457
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEE-LLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE-EIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6458 QDINNLKEKWESVETKLNERKTKLEEALNLaMEFHNSLQDFINWLTQAEQTLNVASRPSLiLDTVLFQIDEHKVFANEVN 6537
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 6538 SHREQIIELDKTGTHLKYFSQKQDVVLIKNLLISVQSRWEKVVQRLVERGRSLDDAR 6594
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
155-254 1.64e-22

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: 95.61  E-value: 1.64e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  155 ERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-IGVIRLLDPEDV 233
Cdd:cd21226      3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKkLGIPKLLEAEDV 82
                           90       100
                   ....*....|....*....|.
gi 1761000869  234 DVSSPDEKSVITYVSSLYDAF 254
Cdd:cd21226     83 MTGNPDERSIVLYTSLFYHAF 103
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
152-254 2.19e-22

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: 95.30  E-value: 2.19e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLDPE 231
Cdd:cd21254      1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGISRLLEPS 80
                           90       100
                   ....*....|....*....|....
gi 1761000869  232 D-VDVSSPDEKSVITYVSSLYDAF 254
Cdd:cd21254     81 DmVLLAVPDKLTVMTYLYQIRAHF 104
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
35-139 4.93e-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: 94.28  E-value: 4.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   35 KVQKKTFTKWINQHL--MKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLP-REKGRMRFHRLQNVQIALDYLKRRQ-VKL 110
Cdd:pfam00307    1 LELEKELLRWINSHLaeYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPK 80
                           90       100
                   ....*....|....*....|....*....
gi 1761000869  111 VNIRNDDITDGNPKLTLGLIWTIILHFQI 139
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
157-255 1.04e-21

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: 93.32  E-value: 1.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  157 LLLWTQQATEGYaGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVA-EKIGVIRLLDPEDVDV 235
Cdd:cd21245      8 LLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAqESLGIPPLLEPEDVMV 86
                           90       100
                   ....*....|....*....|
gi 1761000869  236 SSPDEKSVITYVSSLYDAFP 255
Cdd:cd21245     87 DSPDEQSIMTYVAQFLEHFP 106
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
139-254 5.06e-21

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: 92.06  E-value: 5.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  139 ISDIHVtgesEDMSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYV 218
Cdd:cd21288      1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1761000869  219 AEK-IGVIRLLDPED-VDVSSPDEKSVITYVSSLYDAF 254
Cdd:cd21288     77 AEKhLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHAF 114
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
701-883 1.44e-20

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: 94.05  E-value: 1.44e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  701 LHNFVSRATNELIWLNEKEEEEVAYDWSERNTNIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTIEAYR 780
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  781 AAMQTQWSWILQLCQCVEQHIKENTAYFEFFNDAKEATDYLRNLKDAIQrkySCDRSSSIHKLEDLVQESMEEKEELLQY 860
Cdd:cd00176     82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
                          170       180
                   ....*....|....*....|...
gi 1761000869  861 KSTIANLMGKAKTIIQLKPRNSD 883
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDAD 181
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
152-254 1.61e-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: 89.85  E-value: 1.61e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLDPE 231
Cdd:cd21255      1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80
                           90       100
                   ....*....|....*....|....
gi 1761000869  232 D-VDVSSPDEKSVITYVSSLYDAF 254
Cdd:cd21255     81 DmVLLPIPDKLIVMTYLCQLRAHF 104
SH3_10 pfam17902
SH3 domain; This entry represents an SH3 domain.
876-942 1.66e-20

SH3 domain; This entry represents an SH3 domain.


Pssm-ID: 407754  Cd Length: 65  Bit Score: 88.47  E-value: 1.66e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869  876 QLKPRNSdcPLKTSIPIKAICDYRQIEITIYKDDECVLANNSHRAKWKVISPTGNEAMVPSVCFTVP 942
Cdd:pfam17902    1 PLKQRRS--PVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
152-254 3.15e-20

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


Pssm-ID: 409049  Cd Length: 107  Bit Score: 89.32  E-value: 3.15e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVI-RLLDP 230
Cdd:cd21200      1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIaPLLEV 80
                           90       100
                   ....*....|....*....|....*.
gi 1761000869  231 EDVDV--SSPDEKSVITYVSSLYDAF 254
Cdd:cd21200     81 EDMVRmgNRPDWKCVFTYVQSLYRHL 106
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
153-256 1.17e-19

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: 87.62  E-value: 1.17e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  153 AKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-IGVIRLLDPE 231
Cdd:cd21252      1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAEReLGIPALLDPE 80
                           90       100
                   ....*....|....*....|....*.
gi 1761000869  232 D-VDVSSPDEKSVITYVSSLYDAFPK 256
Cdd:cd21252     81 DmVSMKVPDCLSIMTYVSQYYNHFSN 106
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
151-256 2.16e-19

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: 86.96  E-value: 2.16e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  151 MSAKERLLLWTQQATEGY-AGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQ--SNLANLEHAFYVAE-KIGViR 226
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEkKLGV-P 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 1761000869  227 LLDPEDVDVSSPDEKSVITYVSSLYDAFPK 256
Cdd:pfam00307   80 KVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
152-254 3.09e-19

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: 86.65  E-value: 3.09e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLDPE 231
Cdd:cd21199      8 SKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGIPTTLTID 87
                           90       100
                   ....*....|....*....|....
gi 1761000869  232 D-VDVSSPDEKSVITYVSSLYDAF 254
Cdd:cd21199     88 EmVSMERPDWQSVMSYVTAIYKHF 111
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5282-5497 8.71e-19

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: 88.66  E-value: 8.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5282 RLEEFYSKLKEFSILLQKAEEHEESQGPVGMEtETINQQLNMFKVFQKEeIEPLQGKQQDVNWLGQGLIQSAAKSTSTqg 5361
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAE-LAAHEERVEALNELGEQLIEEGHPDAEE-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5362 LEHDLDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDALEsLLSWMVDTEELVANQKPPSAEFKvVKAQIQEQKLLQRL 5441
Cdd:cd00176     77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEE 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1761000869 5442 LDDRKSTVEVIKREGEKIATTAEPADKVKILKQLSLLDSRWEALLNKAETRNRQLE 5497
Cdd:cd00176    155 LEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
156-254 9.19e-19

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: 85.09  E-value: 9.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  156 RLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-IGVIRLLD-PEDV 233
Cdd:cd21195      8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEReFGIPPVTTgKEMA 87
                           90       100
                   ....*....|....*....|.
gi 1761000869  234 DVSSPDEKSVITYVSSLYDAF 254
Cdd:cd21195     88 SAQEPDKLSMVMYLSKFYELF 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5832-6048 1.33e-18

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 88.27  E-value: 1.33e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5832 QFWETYEELWPWLTETQSIISQLPAPALEyETLRQQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPGEGFSIQEKYV 5911
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5912 AADTLYSQIKEDVKKRAVALDEAISQStQFHDKIDQILESLERIVERLRQPPsISAEVEKIKEQISENKNVSVDMEKLQP 5991
Cdd:cd00176     83 ELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASED-LGKDLESVEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 5992 LYETLKQRGEEMIARSGGTdkdiSAKAVQDKLDQMVFIWENIHTLVEEREAKLLDVM 6048
Cdd:cd00176    161 RLKSLNELAEELLEEGHPD----ADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
6272-6373 1.52e-18

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 84.30  E-value: 1.52e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  6272 QFQHALDELLAWLTHTEGLLSeQKPVGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSaGEEASNLQNKL 6351
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-HPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 1761000869  6352 EVLNQRWQNVLEKTEQRKQQLD 6373
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
608-803 4.17e-18

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 86.73  E-value: 4.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  608 VQDLLNWVDEMQVQLDRTEWGSDLPSVESHLENHKNVHRAIEEFESSLKEAKISE---IQMTAPLKLTYAEKLHRLESQY 684
Cdd:cd00176      9 ADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGeqlIEEGHPDAEEIQERLEELNQRW 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  685 AKLLNTSRNQERHLDT---LHNFVSRATNELIWLNEKEEEEVAYDWSERNTNIARKKDYHAELMRELDQKEENIKSVQEI 761
Cdd:cd00176     89 EELRELAEERRQRLEEaldLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNEL 168
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1761000869  762 AEQLLLENHP-ARLTIEAYRAAMQTQWSWILQLCQCVEQHIKE 803
Cdd:cd00176    169 AEELLEEGHPdADEEIEEKLEELNERWEELLELAEERQKKLEE 211
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5722-5935 4.51e-18

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 86.73  E-value: 4.51e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5722 QQFDQAADAELSWITETEKKLMSLGDIRLEQdQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTACSEEeKQSMKKK 5801
Cdd:cd00176      3 QQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5802 LDKVLKNYDTICQINSERYLQLERAQSLVNQFWETyEELWPWLTETQSIISQLPAPAlEYETLRQQQEEHRQLRELIAEH 5881
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAH 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1761000869 5882 KPHIDKMNKTGPQLLELSPGEGF-SIQEKYVAADTLYSQIKEDVKKRAVALDEAI 5935
Cdd:cd00176    159 EPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
152-249 1.07e-17

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: 81.90  E-value: 1.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYagiRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSN-LANLEHAFYVAE-KIGVIRLLD 229
Cdd:cd21184      1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENpLENATKAMDIAEeELGIPKIIT 77
                           90       100
                   ....*....|....*....|
gi 1761000869  230 PEDVDVSSPDEKSVITYVSS 249
Cdd:cd21184     78 PEDMVSPNVDELSVMTYLSY 97
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
148-254 1.38e-17

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: 81.92  E-value: 1.38e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  148 SEDMSAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-IGVIR 226
Cdd:cd21251      1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKeFGISP 80
                           90       100
                   ....*....|....*....|....*....
gi 1761000869  227 LLDPEDV-DVSSPDEKSVITYVSSLYDAF 254
Cdd:cd21251     81 IMTGKEMaSVGEPDKLSMVMYLTQFYEMF 109
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4514-4735 1.43e-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: 85.19  E-value: 1.43e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4514 KLQKAQEESSAMMQWLQKMNKTATKWQqtpAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELLEENPdtPEAP 4593
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTD---YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH--PDAE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4594 RWKQMLTEIDSKWQELNQLTIDRQQKLEESSNNLTQFQTVEaQLKQWLVEKELMVSVLGPLSiDPNMLNTQRQQVQILLQ 4673
Cdd:cd00176     76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEE 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1761000869 4674 EFATRKPQYEQLTAAGQGILSRpgEDPSLRGIVKEQLAAVTQKWDSLTGQLSDRCDWIDQAI 4735
Cdd:cd00176    154 ELEAHEPRLKSLNELAEELLEE--GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5940-6157 2.47e-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: 84.42  E-value: 2.47e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5940 QFHDKIDQILESLERIVERLRQPpSISAEVEKIKEQISENKNVSVDMEKLQPLYETLKQRGEEMIARSGGtdkdiSAKAV 6019
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-----DAEEI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6020 QDKLDQMVFIWENIHTLVEEREAKLLDVMELAEKFWcDHMSLIVTIKDTQDFIRDlEDPGIDPSVVKQQQEAAETIREEI 6099
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEEL 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1761000869 6100 DGLQEELDIVINLGSELIAACGEPDKPIVKKSIDELNSAWDSLNKAWKDRIDKLEEAM 6157
Cdd:cd00176    156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
155-250 2.72e-17

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: 80.82  E-value: 2.72e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   155 ERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSN----LANLEHAFYVAEKIGVIR-LLD 229
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVvLFE 80
                            90       100
                    ....*....|....*....|.
gi 1761000869   230 PEDVDVSSPDEKSVITYVSSL 250
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
37-137 5.35e-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: 79.93  E-value: 5.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   37 QKKTFTKWINQHL--MKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGR--MRFHRLQNVQIALDYLKRRQVKLVN 112
Cdd:cd21212      1 EIEIYTDWANHYLekGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
                           90       100
                   ....*....|....*....|....*
gi 1761000869  113 IRNDDITDGNPKLTLGLIWTIILHF 137
Cdd:cd21212     81 ITAEDIVDGNLKAILGLFFSLSRYK 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6814-7061 7.12e-17

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 83.26  E-value: 7.12e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6814 QAEEFHSVVHALLEWLAEAEQTLRfHGVLPDDEDALRTLIDQHKEFMKKLEEKRAELNKATTMGDTVLAICHPDSiTTIK 6893
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDA-EEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6894 HWITIIRARFEEVLAWAKQHQQRLASALAgliaKQELLEALLAWLQWAETTLTDKDKEVIPQEIEEVKALIAEHQTFMEE 6973
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEALD----LQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEE 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6974 MTRKQPDVDKVTKTykrraadpsslqshipvldkgragrkrfpASSLYPSGSQTQIETKNPRVNLLVSKWQQVWLLALER 7053
Cdd:cd00176    155 LEAHEPRLKSLNEL-----------------------------AEELLEEGHPDADEEIEEKLEELNERWEELLELAEER 205

                   ....*...
gi 1761000869 7054 RRKLNDAL 7061
Cdd:cd00176    206 QKKLEEAL 213
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
38-135 9.87e-17

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 79.30  E-value: 9.87e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   38 KKTFTKWINQHL-MKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPRE--KGRMRFHRLQNVQIALDYLKRRQV-KLVNI 113
Cdd:cd00014      1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
                           90       100
                   ....*....|....*....|...
gi 1761000869  114 RNDDIT-DGNPKLTLGLIWTIIL 135
Cdd:cd00014     81 EPEDLYeKGNLKKVLGTLWALAL 103
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4740-4954 1.54e-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: 82.11  E-value: 1.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4740 QYQSLLRSLSDKLSDLDNKLS--SSLAVSTHPDAMNQQLETAQKMKQEIQQEKKQIKVAQALCEDLSALVKEEylKAELS 4817
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEEllSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD--AEEIQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4818 RQLEGILKSFKDVEQKAENHVQHLQSAcASSHQFQQMSRDFQAWLDtKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLT 4897
Cdd:cd00176     79 ERLEELNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLE-EKEAALASEDLGKDLESVEELLKKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 4898 AQSHMYEKTIAEGENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLKESL 4954
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
152-252 3.14e-16

calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409110  Cd Length: 107  Bit Score: 77.70  E-value: 3.14e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKI-GVIRLLDP 230
Cdd:cd21261      1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80
                           90       100
                   ....*....|....*....|....
gi 1761000869  231 EDVDV--SSPDEKSVITYVSSLYD 252
Cdd:cd21261     81 EDMMVmgRKPDPMCVFTYVQSLYN 104
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
152-254 3.15e-16

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: 78.15  E-value: 3.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLDPE 231
Cdd:cd21257      8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGIKPSLELS 87
                           90       100
                   ....*....|....*....|....
gi 1761000869  232 D-VDVSSPDEKSVITYVSSLYDAF 254
Cdd:cd21257     88 EmMYTDRPDWQSVMQYVAQIYKYF 111
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
152-251 5.98e-16

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


Pssm-ID: 409108  Cd Length: 112  Bit Score: 77.34  E-value: 5.98e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIG-VIRLLDP 230
Cdd:cd21259      1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHAdCPQLLDV 80
                           90       100
                   ....*....|....*....|..
gi 1761000869  231 ED-VDVSSPDEKSVITYVSSLY 251
Cdd:cd21259     81 EDmVRMREPDWKCVYTYIQEFY 102
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
152-252 6.84e-16

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


Pssm-ID: 409107  Cd Length: 111  Bit Score: 77.01  E-value: 6.84e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIG-VIRLLDP 230
Cdd:cd21258      1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLAdCVPLVEV 80
                           90       100
                   ....*....|....*....|....
gi 1761000869  231 EDVDV--SSPDEKSVITYVSSLYD 252
Cdd:cd21258     81 EDMMImgKKPDSKCVFTYVQSLYN 104
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
152-254 1.72e-15

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: 76.27  E-value: 1.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLDPE 231
Cdd:cd21256     14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAESVGIKSTLDIN 93
                           90       100
                   ....*....|....*....|....
gi 1761000869  232 D-VDVSSPDEKSVITYVSSLYDAF 254
Cdd:cd21256     94 EmVRTERPDWQSVMTYVTAIYKYF 117
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5503-5718 3.19e-15

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: 78.26  E-value: 3.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5503 AQQFHETLEPLNEWLTTIEKRLVNCEPIGTQASkLEEQIAQHKVLQEDILLRKQNVDQALLNGLELLKQTtGDEVLIIQD 5582
Cdd:cd00176      2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLES-VEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5583 KLEAIKARYKDITKLSTDVAKTLEQALQLARRLHStHEELCTWLDKVEVELLSYEtqVLKGEEASQAQM-RPKELKKEAK 5661
Cdd:cd00176     80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASED--LGKDLESVEELLkKHKELEEELE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 5662 NNKALLDSLNEVSSALLELVPWRAREGLEKMVAEDNERYRLVSDTITQKVEEIDAAI 5718
Cdd:cd00176    157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3924-4153 5.29e-15

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: 77.87  E-value: 5.29e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3924 ELEKFDADYTEFEHWLQQSEQELENLEAGaDDINGLMTKLKRQKSFSEDVISHKGDLRYITISGNRVLEAAKSCSKrdgg 4003
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE---- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4004 kvdtsathrEVQRKLDHATDRFRSLYSKCNVLGNNLKDLVDKYQHYEDASCgLLAGLQACEATASkhlSEPIAVDPKNLQ 4083
Cdd:cd00176     76 ---------EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALA---SEDLGKDLESVE 142
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4084 RQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGSllPAKNDIQKTLDDIVGRYEDLSKSVNERNEKLQ 4153
Cdd:cd00176    143 ELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNERWEELLELAEERQKKLE 210
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
154-251 5.69e-15

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: 74.74  E-value: 5.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  154 KERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIG-VIRLLDPED 232
Cdd:cd21260      3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHAdCAPLLEVED 82
                           90       100
                   ....*....|....*....|
gi 1761000869  233 -VDVSSPDEKSVITYVSSLY 251
Cdd:cd21260     83 mVRMSVPDSKCVYTYIQELY 102
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
156-254 6.58e-15

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: 74.15  E-value: 6.58e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  156 RLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLD--PEDV 233
Cdd:cd21250      8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTtgKEMA 87
                           90       100
                   ....*....|....*....|.
gi 1761000869  234 DVSSPDEKSVITYVSSLYDAF 254
Cdd:cd21250     88 SAEEPDKLSMVMYLSKFYELF 108
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
39-140 1.01e-14

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: 73.81  E-value: 1.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   39 KTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEVL-------SGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKLV 111
Cdd:cd21298      9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
                           90       100
                   ....*....|....*....|....*....
gi 1761000869  112 NIRNDDITDGNPKLTLGLIWTIILHFQIS 140
Cdd:cd21298     87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6272-6372 1.70e-14

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: 72.74  E-value: 1.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6272 QFQHALDELLAWLTHTEGLLSEQkPVGGDPKAIEIELAKHHVLQNDVLAHQSTVEAVNKAGNDLIESSaGEEASNLQNKL 6351
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEG-HYASEEIQERL 82
                           90       100
                   ....*....|....*....|.
gi 1761000869 6352 EVLNQRWQNVLEKTEQRKQQL 6372
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKL 103
SPEC smart00150
Spectrin repeats;
6709-6809 4.02e-14

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 71.59  E-value: 4.02e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  6709 QFTDALQALIDWLYRVEPQLAeDQPVHGDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARELIEGSRDDSSWVKVQMQ 6788
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 1761000869  6789 ELSTRWETVCALSISKQTRLE 6809
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5611-5826 4.37e-14

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 75.17  E-value: 4.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5611 LARRLHSTHEELCTWLDKVEVELLSyeTQVLKGEEASQAQMRP-KELKKEAKNNKALLDSLNEVSSALLELVPWRAREgL 5689
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKhEALEAELAAHEERVEALNELGEQLIEEGHPDAEE-I 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5690 EKMVAEDNERYRLVSDTITQKVEEIDAAiLRSQQFDQAADAELSWITETEKKLMSLgDIRLEQDQTSAQLQVQKTFTMEI 5769
Cdd:cd00176     78 QERLEELNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEEL 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 5770 LRHKDIIDDLVKSGHKIMTACSEEEKQSMKKKLDKVLKNYDTICQINSERYLQLERA 5826
Cdd:cd00176    156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4849-5035 5.13e-14

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 74.79  E-value: 5.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4849 HQFQQMSRDFQAWLDtKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLTAQSHMYEKTIAEGENLLlKTQGSEKAALQLQ 4928
Cdd:cd00176      3 QQFLRDADELEAWLS-EKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4929 LNTIKTNWDTFNKQVKERENKLKESLEKALKYkEQVETLWPWIDKCQNNLEEIKFCLDPAEGENSIAKLKSLQKEMDQHF 5008
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180
                   ....*....|....*....|....*..
gi 1761000869 5009 GMVELLNNTANSLLSVCEIDKEVVTDE 5035
Cdd:cd00176    160 PRLKSLNELAEELLEEGHPDADEEIEE 186
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
55-134 7.76e-14

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: 71.08  E-value: 7.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   55 HVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRM----RFHRLQNVQIALDYLKRRQV----KLVNIRNDDITDGNPKLT 126
Cdd:cd21223     25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104

                   ....*...
gi 1761000869  127 LGLIWTII 134
Cdd:cd21223    105 LALLWRII 112
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
31-136 1.73e-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: 70.39  E-value: 1.73e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   31 DERDKvqkKTFTKWINQhlMKVRKHVNDLYEDLRDGhnlISLLEVLsgDTL-P---------REKGRMRFHRLQNVQIAL 100
Cdd:cd21219      2 GSREE---RAFRMWLNS--LGLDPLINNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVENCNYAV 71
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1761000869  101 DYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILH 136
Cdd:cd21219     72 DLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
34-133 1.86e-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: 1.86e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   34 DKVQKKTFTKWINQHLMKVR-KHVNDLYEDLRDGHNLISLLEVLSGDTLPRE---KGRMRFHRLQNVQIALDYL-KRRQV 108
Cdd:cd21225      2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIeEDLKI 81
                           90       100
                   ....*....|....*....|....*
gi 1761000869  109 KLVNIRNDDITDGNPKLTLGLIWTI 133
Cdd:cd21225     82 RVQGIGAEDFVDNNKKLILGLLWTL 106
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
39-145 2.19e-13

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: 70.15  E-value: 2.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   39 KTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEVLSGDT--------LPREKGRMRFHRLQNVQIALDYLKRRQVKL 110
Cdd:cd21300     10 RVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYAVELGKQLGFSL 87
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1761000869  111 VNIRNDDITDGNPKLTLGLIWtiilhfQISDIHVT 145
Cdd:cd21300     88 VGIQGADITDGSRTLTLALVW------QLMRFHIT 116
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
37-137 2.72e-13

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: 69.63  E-value: 2.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   37 QKKTFTKWINQHLMK---VRKhVNDLYEDLRDGHNLISLLEVLSGDTL------PREKGRMRfhrlQNVQIALDYLKRRQ 107
Cdd:cd21213      1 QLQAYVAWVNSQLKKrpgIRP-VQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKR 75
                           90       100       110
                   ....*....|....*....|....*....|
gi 1761000869  108 VKLVNIRNDDITDGNPKLTLGLIWTIILHF 137
Cdd:cd21213     76 IRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
154-252 4.81e-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: 68.52  E-value: 4.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  154 KERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSN---LANLEHAFYVAEKIGVIR--LL 228
Cdd:cd00014      1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLGLPEldLF 80
                           90       100
                   ....*....|....*....|....
gi 1761000869  229 DPEDVdVSSPDEKSVITYVSSLYD 252
Cdd:cd00014     81 EPEDL-YEKGNLKKVLGTLWALAL 103
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
38-134 7.85e-13

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: 68.37  E-value: 7.85e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   38 KKTFTKWINQHLMKVR---------KHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMR-----FHRLQNVQIALDYL 103
Cdd:cd21217      3 KEAFVEHINSLLADDPdlkhllpidPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1761000869  104 KRRQVKLVNIRNDDITDGNPKLTLGLIWTII 134
Cdd:cd21217     83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
SPEC smart00150
Spectrin repeats;
6382-6482 6.65e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 65.43  E-value: 6.65e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  6382 FHGEIEDLQQWLTDTERhLLASKPLGGLPETAKEQLNVHMEVCAAFEAKEETYKSLMQKGQQMLARCPKSAEtNIDQDIN 6461
Cdd:smart00150    3 FLRDADELEAWLEEKEQ-LLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAE-EIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 1761000869  6462 NLKEKWESVETKLNERKTKLE 6482
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
6599-6701 1.11e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 64.66  E-value: 1.11e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  6599 QFHEAWSKLMEWLEESEKSLDSElEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEKTSlaDDNLKLDDM 6678
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH--PDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 1761000869  6679 LSELRDKWDTICGKSVERQNKLE 6701
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
702-802 6.61e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 62.35  E-value: 6.61e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   702 HNFVSRATNELIWLNEKEEEEVAYDWSERNTNIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTIEAYRA 781
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 1761000869   782 AMQTQWSWILQLCQCVEQHIK 802
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4635-4844 9.24e-11

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: 65.16  E-value: 9.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4635 AQLKQWLVEKELMVSVLGPLSiDPNMLNTQRQQVQILLQEFATRKPQYEQLTAAGQGILSrpgEDPSLRGIVKEQLAAVT 4714
Cdd:cd00176     10 DELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE---EGHPDAEEIQERLEELN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4715 QKWDSLTGQLSDRCDWIDQAIvkstQYQSLLRSLSDKLSDLDNKLS--SSLAVSTHPDAMNQQLETAQKMKQEIQQEKKQ 4792
Cdd:cd00176     86 QRWEELRELAEERRQRLEEAL----DLQQFFRDADDLEQWLEEKEAalASEDLGKDLESVEELLKKHKELEEELEAHEPR 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1761000869 4793 IKVAQALCEDLSALvKEEYLKAELSRQLEGILKSFKDVEQKAENHVQHLQSA 4844
Cdd:cd00176    162 LKSLNELAEELLEE-GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
7092-7155 1.98e-10

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.12  E-value: 1.98e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1761000869 7092 RVMDFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLEmsAVADIFDRDGDGYIDYYEFVAALHP 7155
Cdd:COG5126     70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEAD--ELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
7092-7154 2.20e-10

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 59.48  E-value: 2.20e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1761000869 7092 RVMDFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAALH 7154
Cdd:cd00051      1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3613-4395 4.35e-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: 67.39  E-value: 4.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3613 ESVTTQVERLETQLH-LEQDLDD-QKIVAERQQEYkEKLQGICDLLTQTENRLighqeafmigdgTVELKKYQSKQEELQ 3690
Cdd:TIGR02168  249 KEAEEELEELTAELQeLEEKLEElRLEVSELEEEI-EELQKELYALANEISRL------------EQQKQILRERLANLE 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3691 KDMQGSAQALAEVvkntenflkENGEKLSQEDKALIEQKLNEAKIKCEQLNLK---AEQSKKELDKVVTTAIKEETEKVA 3767
Cdd:TIGR02168  316 RQLEELEAQLEEL---------ESKLDELAEELAELEEKLEELKEELESLEAEleeLEAELEELESRLEELEEQLETLRS 386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3768 AVKQLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIEQNGTHFQEGDGKSAIGEEDEVNGNLLETDvdgqvgTTQENLN 3847
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ------EELERLE 460
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3848 QQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGQYLspEEKEKLQKNMKELKvhyetalaESEKKMKLTHSLQEELEK 3927
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQ--ENLEGFSEGVKALL--------KNQSGLSGILGVLSELIS 530
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3928 FDADY-TEFEHWLQQSEQEL--ENLEAGADDINGLMTKLKRQKSFSE-DVISH---KGDLRYITISGNRVLEAAKSCSKR 4000
Cdd:TIGR02168  531 VDEGYeAAIEAALGGRLQAVvvENLNAAKKAIAFLKQNELGRVTFLPlDSIKGteiQGNDREILKNIEGFLGVAKDLVKF 610
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4001 D-----------GGK--VDTSATHREVQRKLDHATdRFRSLYSkcnvlgnnlkDLVdkyqhyedASCGLLAGlqACEATA 4067
Cdd:TIGR02168  611 DpklrkalsyllGGVlvVDDLDNALELAKKLRPGY-RIVTLDG----------DLV--------RPGGVITG--GSAKTN 669
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4068 SKHLSEPIAVdpKNLQRQLEEtkaLQGQISSQQVAVEKLKKTAEVLLDARGSLLPAKNDIQKTLDDIVGRYEDLSKSVN- 4146
Cdd:TIGR02168  670 SSILERRREI--EELEEKIEE---LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEq 744
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4147 --ERNEKLQITLTRSLSVQDGLDEMLDwmgnvesslkeqgqvpLNSTALQDIISKNIMLEQDIAGRQSSINAMNEKVkkf 4224
Cdd:TIGR02168  745 leERIAQLSKELTELEAEIEELEERLE----------------EAEEELAEAEAEIEELEAQIEQLKEELKALREAL--- 805
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4225 mettdpstaSSLQAKMKDLSARFSEASHKHKETLAKMEELKTKVELFENLSEKLQtfletktqaltevdvpgKDVTELSQ 4304
Cdd:TIGR02168  806 ---------DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS-----------------EDIESLAA 859
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4305 YMQESTSEFLEHKKHLEvlhSLLKEISSHGLpsDKALVLEKTNNLSKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSL 4384
Cdd:TIGR02168  860 EIEELEELIEELESELE---ALLNERASLEE--ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
                          810
                   ....*....|.
gi 1761000869 4385 KSWIKETTKKV 4395
Cdd:TIGR02168  935 EVRIDNLQERL 945
SPEC smart00150
Spectrin repeats;
6816-6917 5.36e-10

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 60.04  E-value: 5.36e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  6816 EEFHSVVHALLEWLAEAEQTLRfHGVLPDDEDALRTLIDQHKEFMKKLEEKRAELNKATTMGDTVLAICHPDSiTTIKHW 6895
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDA-EEIEER 78
                            90       100
                    ....*....|....*....|..
gi 1761000869  6896 ITIIRARFEEVLAWAKQHQQRL 6917
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
23-137 5.53e-10

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


Pssm-ID: 409071  Cd Length: 121  Bit Score: 60.29  E-value: 5.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   23 EDVLERYKDERDKVQ--KKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLP----REKGRMRFHRLQNV 96
Cdd:cd21222      1 DAFDDLFDEAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNV 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1761000869   97 QIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHF 137
Cdd:cd21222     81 KLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5175-5391 6.45e-10

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: 62.85  E-value: 6.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5175 HFQNTIREMFSQFAEFDDELDSMAPvGRDAETLQKQKETIKAFLKKLEALMASNDNANKTCKMMLatEETSPDLVGIKRD 5254
Cdd:cd00176      4 QFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI--EEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5255 LEALSKQCNKLLDRAQAREEQVEGTIKRLEeFYSKLKEFSILLQKAEEHEESQgPVGMETETINQQLNMFKVFQkEEIEP 5334
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELE-EELEA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 5335 LQGKQQDVNWLGQGLIQSAAkSTSTQGLEHDLDDVNARWKTLNKKVAQRAAQLQEAL 5391
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGH-PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
152-257 7.83e-10

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: 59.32  E-value: 7.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGyagIRCENFTTCWRDGKLFNAIIHKYRPDLI-DMNTVAVQSNLANLEHAFYVAEK-IGVIRLLD 229
Cdd:cd21230      1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDwLGVPQLIT 77
                           90       100
                   ....*....|....*....|....*...
gi 1761000869  230 PEDVDVSSPDEKSVITYVSSlydaFPKV 257
Cdd:cd21230     78 PEEIINPNVDEMSVMTYLSQ----FPKA 101
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1775-1813 1.19e-09

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 56.95  E-value: 1.19e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1761000869 1775 LLSAQLLSGGLINSNSGQRMTVEEAVREGVIDRDTASSI 1813
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
SPEC smart00150
Spectrin repeats;
5396-5497 1.43e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 58.50  E-value: 1.43e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  5396 RFQDALESLLSWMVDTEELVAnQKPPSAEFKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKIaTTAEPADKVKILKQL 5475
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQL-IEEGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 1761000869  5476 SLLDSRWEALLNKAETRNRQLE 5497
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
7052-7153 1.50e-09

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 59.81  E-value: 1.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 7052 ERRRKLNDALDRLE-------ELREFANFDFDIWRkkymrwmnhkksrvmDFFRRIDKDQDGKITRQEFIDGILSSKFPT 7124
Cdd:COG5126      2 LQRRKLDRRFDLLDadgdgvlERDDFEALFRRLWA---------------TLFSEADTDGDGRISREEFVAGMESLFEAT 66
                           90       100
                   ....*....|....*....|....*....
gi 1761000869 7125 SRLEMSAVADIFDRDGDGYIDYYEFVAAL 7153
Cdd:COG5126     67 VEPFARAAFDLLDTDGDGKISADEFRRLL 95
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
152-254 2.62e-09

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: 58.13  E-value: 2.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  152 SAKERLLLWTQQATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAE-KIGVIRLLDP 230
Cdd:cd21196      3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAEnELGITPVVSA 82
                           90       100
                   ....*....|....*....|....
gi 1761000869  231 EDVdVSSPDEKSVITYVSSLYDAF 254
Cdd:cd21196     83 QAV-VAGSDPLGLIAYLSHFHSAF 105
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
37-136 2.63e-09

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


Pssm-ID: 409148  Cd Length: 114  Bit Score: 58.28  E-value: 2.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   37 QKKTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKG-----RMRFHRLQNVQIALDYLKRRQVKLV 111
Cdd:cd21299      5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
                           90       100
                   ....*....|....*....|....*
gi 1761000869  112 NIRNDDITDGNPKLTLGLIWTIILH 136
Cdd:cd21299     83 NVAGNDIVQGNKKLILALLWQLMRY 107
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6382-6483 3.24e-09

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: 57.71  E-value: 3.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6382 FHGEIEDLQQWLTDTERhLLASKPLGGLPETAKEQLNVHMEVCAAFEAKEETYKSLMQKGQQMLARCPKSAEtNIDQDIN 6461
Cdd:pfam00435    6 FFRDADDLESWIEEKEA-LLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASE-EIQERLE 83
                           90       100
                   ....*....|....*....|..
gi 1761000869 6462 NLKEKWESVETKLNERKTKLEE 6483
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
4516-4621 4.18e-09

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 57.34  E-value: 4.18e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  4516 QKAQEESSAMMQWLQKMNKTAtkwQQTPAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELLEENPdtPEAPRW 4595
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLL---ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH--PDAEEI 75
                            90       100
                    ....*....|....*....|....*.
gi 1761000869  4596 KQMLTEIDSKWQELNQLTIDRQQKLE 4621
Cdd:smart00150   76 EERLEELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4745-5615 5.43e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.54  E-value: 5.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4745 LRSLSDKLSDLDNKLSSSLAVSTHpDAMNQQLETAQKMKQEIQQEKKQIKVAQalcEDLSALVKEEYLKAELSRQLEGIL 4824
Cdd:TIGR02168  215 YKELKAELRELELALLVLRLEELR-EELEELQEELKEAEEELEELTAELQELE---EKLEELRLEVSELEEEIEELQKEL 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4825 KSFKDVEQKAENHVQHLQSACASSHQFQQMSRDFQAWLDTKKEEQNKS-HPISAKLDVLeslikdhkdfsktltaqshmy 4903
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEElAELEEKLEEL--------------------- 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4904 eKTIAEGENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLkESLEKALKY-KEQVETLWPWIDKCQNNLEEIK 4982
Cdd:TIGR02168  350 -KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI-ASLNNEIERlEARLERLEDRRERLQQEIEELL 427
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4983 FCLDPAEGENSIAKLKSLQKEMDQHFGMVELLNNTANsllsvcEIDKEVvtDENKSLIQKVDMVTEQLHSKKFCLENMTQ 5062
Cdd:TIGR02168  428 KKLEEAELKELQAELEELEEELEELQEELERLEEALE------ELREEL--EEAEQALDAAERELAQLQARLDSLERLQE 499
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5063 KFKEFQevskESKRQLQCAKEQL-DIHDSLGSQaysnkyltmLQTQQKSLQALkhQVDLAKRLaQDLVVEASDSkgtsdV 5141
Cdd:TIGR02168  500 NLEGFS----EGVKALLKNQSGLsGILGVLSEL---------ISVDEGYEAAI--EAALGGRL-QAVVVENLNA-----A 558
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5142 LLQVETIAQEHSTlsqqvdeKCSFLETKLQGIGHFQNTIREM---FSQFAEFDDELDSMAPVGRDA-----------ETL 5207
Cdd:TIGR02168  559 KKAIAFLKQNELG-------RVTFLPLDSIKGTEIQGNDREIlknIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvDDL 631
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5208 QkqkeTIKAFLKKLEALM--------------ASNDNANKTCKMMLAT----EETSPDLVGIKRDLEALSKQCNKLLDRA 5269
Cdd:TIGR02168  632 D----NALELAKKLRPGYrivtldgdlvrpggVITGGSAKTNSSILERrreiEELEEKIEELEEKIAELEKALAELRKEL 707
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5270 QAREEQVEGTIKRLEEFYSKLKEFSILLQKAEEheesqgpvgmETETINQQLNMFKVFQKEEIEPLQGKQQDVNWLGQGL 5349
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEA----------EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5350 IQSAAKSTStqgLEHDLDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDALESLLSWMVDTEElvanqkppsaEFKVVK 5429
Cdd:TIGR02168  778 AEAEAEIEE---LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER----------RLEDLE 844
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5430 AQIQEQKllqrllDDRKSTVEVIKREGEKIATTAEPADKVkiLKQLSLLDSRWEALLNKAETRNRQLEGISVVAQQFHET 5509
Cdd:TIGR02168  845 EQIEELS------EDIESLAAEIEELEELIEELESELEAL--LNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5510 LEPLNEWLTTIEKRLvncEPIGTQASKLEEQIA-QHKVLQEDILLRKQNVD------QALLNGLELLKQTTGDEVLIIQD 5582
Cdd:TIGR02168  917 LEELREKLAQLELRL---EGLEVRIDNLQERLSeEYSLTLEEAEALENKIEddeeeaRRRLKRLENKIKELGPVNLAAIE 993
                          890       900       910
                   ....*....|....*....|....*....|...
gi 1761000869 5583 KLEAIKARYKDITKLSTDVAKTLEQALQLARRL 5615
Cdd:TIGR02168  994 EYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
SPEC smart00150
Spectrin repeats;
4849-4951 1.01e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 56.18  E-value: 1.01e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  4849 HQFQQMSRDFQAWLDtKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLTAQSHMYEKTIAEGENlLLKTQGSEKAALQLQ 4928
Cdd:smart00150    1 QQFLRDADELEAWLE-EKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQ-LIEEGHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 1761000869  4929 LNTIKTNWDTFNKQVKERENKLK 4951
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
6052-6154 1.09e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 56.18  E-value: 1.09e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  6052 EKFWCDHMSLIVTIKDTQDFIRDlEDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAAcGEPDKPIVKKS 6131
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 1761000869  6132 IDELNSAWDSLNKAWKDRIDKLE 6154
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4514-4622 2.41e-08

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: 55.40  E-value: 2.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4514 KLQKAQEESSAMMQWLQKMNKTATkwqQTPAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELLEENPdtPEAP 4593
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLS---SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH--YASE 76
                           90       100
                   ....*....|....*....|....*....
gi 1761000869 4594 RWKQMLTEIDSKWQELNQLTIDRQQKLEE 4622
Cdd:pfam00435   77 EIQERLEELNERWEQLLELAAERKQKLEE 105
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
32-139 2.93e-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: 56.16  E-value: 2.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   32 ERDKVQKKTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEVL-------SGDTLPREKGRMRFHRLQNVQIALDYLK 104
Cdd:cd21331     18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVELGK 95
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1761000869  105 RR-QVKLVNIRNDDITDGNPKLTLGLIWTIILHFQI 139
Cdd:cd21331     96 HPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
SPEC smart00150
Spectrin repeats;
6490-6591 2.96e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 55.03  E-value: 2.96e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  6490 EFHNSLQDFINWLTQAEQTLNVASRPSLiLDTVLFQIDEHKVFANEVNSHREQIIELDKTGTHLKyFSQKQDVVLIKNLL 6569
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKD-LESVEALLKKHEAFEAELEAHEERVEALNELGEQLI-EEGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 1761000869  6570 ISVQSRWEKVVQRLVERGRSLD 6591
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
6162-6264 3.63e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 54.64  E-value: 3.63e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  6162 QYQDGLQAVFDWVDIAGGKLASMsPIGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEESDKhtVQDP 6241
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE--IEER 78
                            90       100
                    ....*....|....*....|...
gi 1761000869  6242 LMELKLIWDSLEERIINRQHKLE 6264
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4483-4623 5.09e-08

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: 57.07  E-value: 5.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4483 IKKDMTDISHGYEDLGLLLKDKIAELNTKLsKLQKAQEESSAMMQWLQKMNKTAtkwQQTPAPTDTEAVKTQVEQNKSFE 4562
Cdd:cd00176     77 IQERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAAL---ASEDLGKDLESVEELLKKHKELE 152
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1761000869 4563 AELKQNVNKVQELKDKLTELLEENPDTPEAPRwKQMLTEIDSKWQELNQLTIDRQQKLEES 4623
Cdd:cd00176    153 EELEAHEPRLKSLNELAEELLEEGHPDADEEI-EEKLEELNERWEELLELAEERQKKLEEA 212
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3676-4390 6.24e-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: 60.07  E-value: 6.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3676 TVELKKYQSKQEELQKDMQG-SAQALAEVVKNTENFLKENGEKLSQEDKAL--IEQKLNEAKIKCEQLNLKAEQSKKELD 3752
Cdd:TIGR02168  212 AERYKELKAELRELELALLVlRLEELREELEELQEELKEAEEELEELTAELqeLEEKLEELRLEVSELEEEIEELQKELY 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3753 KVVTTAIKEETEKVAAVKQLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIEQNGTHFQEGDGKSAIGEEDEVNGNLLE 3832
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3833 TdvdgQVGTTQENLNQQYQKVkAQHEKIISQHQAVIIAT----QSAQVLLEKQGQYLSPEEKEKLQKNMKELKVHYETAL 3908
Cdd:TIGR02168  372 S----RLEELEEQLETLRSKV-AQLELQIASLNNEIERLearlERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3909 AESEKKMKLTHSLQEELEKFDADYTEFEHWLQQSEQELENLEAGADDINGLMTKL-------------KRQKSFSEDVIS 3975
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLegfsegvkallknQSGLSGILGVLS 526
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3976 HK----------------GDLRYITISG-NRVLEAAKSCSKRDGGKVDTSATHREVQRKLDhaTDRFRSLYSKCNVLGnN 4038
Cdd:TIGR02168  527 ELisvdegyeaaieaalgGRLQAVVVENlNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQ--GNDREILKNIEGFLG-V 603
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4039 LKDLVDKYQHYEDASCGLLAGL-------QACEATASKHLSEPI----------------AVDPKN---LQRQLE----- 4087
Cdd:TIGR02168  604 AKDLVKFDPKLRKALSYLLGGVlvvddldNALELAKKLRPGYRIvtldgdlvrpggvitgGSAKTNssiLERRREieele 683
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4088 -ETKALQGQISSQQVAVEKLKKTAEVLLDARGSLLPAKNDIQKTLDDIVGRYEDLSKSVN---ERNEKLQITLTRSLSVQ 4163
Cdd:TIGR02168  684 eKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleERIAQLSKELTELEAEI 763
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4164 DGLDEMLDwmgnvesslkeqgqvpLNSTALQDIISKNIMLEQDIAGRQSSINAMNEKVKKFME---------TTDPSTAS 4234
Cdd:TIGR02168  764 EELEERLE----------------EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeltllneeaANLRERLE 827
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4235 SLQAKMKDLSARFSEASHKHKETLAKME----ELKTKVELFENLSEKLQTFLETKTQALTEVDVPGKDVTELSQYMQEST 4310
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIEslaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4311 SEFLEHKKHLEVLHSLLKEISSHgLPSDKALVLEKTNNLSKKFKEMEDTIKEKKEAVTSCQEQLDAFqvlVKSLKSWIKE 4390
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELR-LEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR---LKRLENKIKE 983
EF-hand_7 pfam13499
EF-hand domain pair;
7090-7153 7.91e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 52.64  E-value: 7.91e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1761000869 7090 KSRVMDFFRRIDKDQDGKITRQEFIDGI--LSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAAL 7153
Cdd:pfam13499    1 EEKLKEAFKLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6599-6702 9.04e-08

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: 53.48  E-value: 9.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6599 QFHEAWSKLMEWLEESEKSLDSElEIANDPDKIKTQLAQHKEFQKSLGAKHSVYDTTNRTGRSLKEktSLADDNLKLDDM 6678
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID--EGHYASEEIQER 81
                           90       100
                   ....*....|....*....|....
gi 1761000869 6679 LSELRDKWDTICGKSVERQNKLEE 6702
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6076-6155 9.68e-08

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: 53.48  E-value: 9.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6076 EDPGIDPSVVKQQQEAAETIREEIDGLQEELDIVINLGSELIAAcGEPDKPIVKKSIDELNSAWDSLNKAWKDRIDKLEE 6155
Cdd:pfam00435   27 EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6709-6810 1.15e-07

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: 53.48  E-value: 1.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6709 QFTDALQALIDWLYRVEPQLAEDQPVHgDIDLVMNLIDNHKAFQKELGKRTSSVQALKRSARELIEGSRDDSSWVKVQMQ 6788
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
                           90       100
                   ....*....|....*....|..
gi 1761000869 6789 ELSTRWETVCALSISKQTRLEA 6810
Cdd:pfam00435   84 ELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4956-5167 1.31e-07

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: 55.91  E-value: 1.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4956 KALKYKEQVETLWPWIDKCQNNLEEIKFCLDPAEGENSIAKLKSLQKEMDQHFGMVELLNNTANSLLSVCEIDKEVVTDE 5035
Cdd:cd00176      1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5036 NKSLIQKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRqLQCAKEQLDIHDSLGSQAYSNKYLTMLQTQQKSLQALK 5115
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQW-LEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1761000869 5116 HQVDLAKRLAQDLvVEASDSKGTSDVLLQVETIAQEHSTLSQQVDEKCSFLE 5167
Cdd:cd00176    160 PRLKSLNELAEEL-LEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC smart00150
Spectrin repeats;
5722-5824 1.37e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.10  E-value: 1.37e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  5722 QQFDQAADAELSWITETEKKLMSLgDIRLEQDQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTAcSEEEKQSMKKK 5801
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 1761000869  5802 LDKVLKNYDTICQINSERYLQLE 5824
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
5832-5932 1.57e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 52.72  E-value: 1.57e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  5832 QFWETYEELWPWLTETQSIISQLPAPALEyETLRQQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPGEGFSIQEKYV 5911
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDL-ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 1761000869  5912 AADTLYSQIKEDVKKRAVALD 5932
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4774-5545 2.20e-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: 58.53  E-value: 2.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4774 QQLETAQKMKqEIQQEKKQIKVAqalcedLSALVKEEyLKAELSRQLEgilkSFKDVEQKAENHVQHLQSACASSHQFqq 4853
Cdd:TIGR02168  207 RQAEKAERYK-ELKAELRELELA------LLVLRLEE-LREELEELQE----ELKEAEEELEELTAELQELEEKLEEL-- 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4854 msRDFQAWLDTKKEEQNKS-HPISAKLDVLESLIKDHKDFSKTLTAQSHMYEKTIAEGENLLLKTQgSEKAALQLQLNTI 4932
Cdd:TIGR02168  273 --RLEVSELEEEIEELQKElYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA-EELAELEEKLEEL 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4933 KTNWDTFNKQVKERENKLKESLEKALKYKEQVETLWPWIDKCQNNLEEIKfcldpaegensiAKLKSLQKEMDQHFGMVE 5012
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN------------NEIERLEARLERLEDRRE 417
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5013 LLNNTANSLLsvceidKEVVTDENKSLIQKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRQLQCAKEQLDIHDSLg 5092
Cdd:TIGR02168  418 RLQQEIEELL------KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR- 490
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5093 sqaysnkyLTMLQTQQKSLQ--------ALKHQVDLAK---RLAQDLVVEASDSKGTSDVL---LQ------VETIAQEH 5152
Cdd:TIGR02168  491 --------LDSLERLQENLEgfsegvkaLLKNQSGLSGilgVLSELISVDEGYEAAIEAALggrLQavvvenLNAAKKAI 562
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5153 STLSQQVDEKCSFLETKLQGIGHFQNTIREM---FSQFAEFDDELDSMAP------------------------------ 5199
Cdd:TIGR02168  563 AFLKQNELGRVTFLPLDSIKGTEIQGNDREIlknIEGFLGVAKDLVKFDPklrkalsyllggvlvvddldnalelakklr 642
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5200 ------------------------------VGRDAE------TLQKQKETIKAFLKKLEALMASNDNA-NKTCKMMLATE 5242
Cdd:TIGR02168  643 pgyrivtldgdlvrpggvitggsaktnssiLERRREieeleeKIEELEEKIAELEKALAELRKELEELeEELEQLRKELE 722
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5243 ETSPDLVGIKRDLEALSKQCNKLLDRAQAR-------EEQVEGTIKRLEEFYSKLKEfsillqkAEEHEESQgpvgmeTE 5315
Cdd:TIGR02168  723 ELSRQISALRKDLARLEAEVEQLEERIAQLskeltelEAEIEELEERLEEAEEELAE-------AEAEIEEL------EA 789
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5316 TINQQLNMFKVfQKEEIEPLQGKQQDVNwlgqglIQSAAKSTSTQGLEHDLDDVNARWKTLNKKVAQRAAQLQEALLHCG 5395
Cdd:TIGR02168  790 QIEQLKEELKA-LREALDELRAELTLLN------EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5396 RFQDALESLlswmvdteelvanqkppSAEFKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKiattaepadKVKILKQL 5475
Cdd:TIGR02168  863 ELEELIEEL-----------------ESELEALLNERASLEEALALLRSELEELSEELRELES---------KRSELRRE 916
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5476 SlldsrwEALLNKAETRNRQLEGISVVAQQFHETLepLNEWLTTIEKRLVNCEPIGTQASKLEEQIAQHK 5545
Cdd:TIGR02168  917 L------EELREKLAQLELRLEGLEVRIDNLQERL--SEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
SPEC smart00150
Spectrin repeats;
608-699 3.07e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.95  E-value: 3.07e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   608 VQDLLNWVDEMQVQLDRTEWGSDLPSVESHLENHKNVHRAIEEFESSLKEAKISEIQMTA---PLKLTYAEKLHRLESQY 684
Cdd:smart00150    7 ADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEeghPDAEEIEERLEELNERW 86
                            90
                    ....*....|....*
gi 1761000869   685 AKLLNTSRNQERHLD 699
Cdd:smart00150   87 EELKELAEERRQKLE 101
PLEC smart00250
Plectin repeat;
1774-1810 3.50e-07

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 49.79  E-value: 3.50e-07
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1761000869  1774 RLLSAQLLSGGLINSNSGQRMTVEEAVREGVIDRDTA 1810
Cdd:smart00250    2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
7095-7154 3.62e-07

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 50.68  E-value: 3.62e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 7095 DFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLemSAVADIFDRDGDGYIDYYEFVAALH 7154
Cdd:cd00052      3 QIFRSLDPDGDGLISGDEARPFLGKSGLPRSVL--AQIWDLADTDKDGKLDKEEFAIAMH 60
SPEC smart00150
Spectrin repeats;
5504-5606 4.03e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 51.56  E-value: 4.03e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  5504 QQFHETLEPLNEWLTTIEKRLVNcEPIGTQASKLEEQIAQHKVLQEDILLRKQNVDQALLNGLELLKQtTGDEVLIIQDK 5583
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78
                            90       100
                    ....*....|....*....|...
gi 1761000869  5584 LEAIKARYKDITKLSTDVAKTLE 5606
Cdd:smart00150   79 LEELNERWEELKELAEERRQKLE 101
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
3611-4401 4.49e-07

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 57.44  E-value: 4.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3611 VQESVTTQVERLETQLHLEQDLDdqkivaERQQEYKEklQGICDLLTQTenrlighQEAFMIGDGTVELKKYQSK-QEEL 3689
Cdd:pfam15921   79 VLEEYSHQVKDLQRRLNESNELH------EKQKFYLR--QSVIDLQTKL-------QEMQMERDAMADIRRRESQsQEDL 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3690 QKDMQGSAQALAEVVKNTENFLKENGEKLSQEDKALIEQKLNEAKIKCEQLNLKAEQSKK-------------ELDKVVT 3756
Cdd:pfam15921  144 RNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmstmhfrSLGSAIS 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3757 TAIKEETEKVAAVK--------QLEESKTKIENLLDWLSNVDKDS-ERAGTKHKqvIEQNGTHFQEGDGKSA-------- 3819
Cdd:pfam15921  224 KILRELDTEISYLKgrifpvedQLEALKSESQNKIELLLQQHQDRiEQLISEHE--VEITGLTEKASSARSQansiqsql 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3820 -IGEEDEVNGNLLETDVDGQVGTTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGQYLSPEE---KEKLQK 3895
Cdd:pfam15921  302 eIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESgnlDDQLQK 381
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3896 NMKELKVHYETALAESEKKMKL----------THSLQEELEKFDADYTEFEHWLQQSEQELE-NLEAGADDINGLMTKLK 3964
Cdd:pfam15921  382 LLADLHKREKELSLEKEQNKRLwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLE 461
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3965 RQKSFSEDVISHKGDLRYITisgnRVLEAAKSCSKRDGGKV-DTSATHREVQRKLDHATDRFRSLYSKCNVLGNNLKDLV 4043
Cdd:pfam15921  462 KVSSLTAQLESTKEMLRKVV----EELTAKKMTLESSERTVsDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLK 537
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4044 DKYQHYEDASCgllaglqACEATASKHLSEPIAVDPknLQRQLEETKALQGQ--ISSQQVAVEKLKKTAEVLlDARGSL- 4120
Cdd:pfam15921  538 NEGDHLRNVQT-------ECEALKLQMAEKDKVIEI--LRQQIENMTQLVGQhgRTAGAMQVEKAQLEKEIN-DRRLELq 607
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4121 ----LPAKNDIQktLDDIVGRYEDLS----KSVNERNEKLQitltrslSVQDGLDEMLDWMGNVESSLKEqgqvplnsta 4192
Cdd:pfam15921  608 efkiLKDKKDAK--IRELEARVSDLElekvKLVNAGSERLR-------AVKDIKQERDQLLNEVKTSRNE---------- 668
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4193 LQDIISKNIMLEQDIAGRQSSINAMNEKVKKFMEttdpSTASSLQAKMKDLSARFSEASHKHKETLAKMEELKTKVELFE 4272
Cdd:pfam15921  669 LNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLK----SAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQID 744
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4273 NLSEKLQTFLETKTQALTEVDVPGKDVTELSQYMQESTSEFLEHKKHLEVLHS----LLKEISSHGLPSDKAlvlektnn 4348
Cdd:pfam15921  745 ALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSqerrLKEKVANMEVALDKA-------- 816
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 4349 lSKKFKEMEDTI-KEKKEAVT-SCQEQLDafqvlVKSLK--SWIKETTKKVPIVQPS 4401
Cdd:pfam15921  817 -SLQFAECQDIIqRQEQESVRlKLQHTLD-----VKELQgpGYTSNSSMKPRLLQPA 867
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
32-140 4.63e-07

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: 51.91  E-value: 4.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   32 ERDKVQKKTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEV---------LSGDTLPREKGRMRfhRLQNVQIALDY 102
Cdd:cd21329      2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1761000869  103 LKRR-QVKLVNIRNDDITDGNPKLTLGLIWTIILHFQIS 140
Cdd:cd21329     78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4849-4952 5.11e-07

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: 51.55  E-value: 5.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4849 HQFQQMSRDFQAWLDtKKEEQNKSHPISAKLDVLESLIKDHKDFSKTLTAQSHMYEKTIAEGENlLLKTQGSEKAALQLQ 4928
Cdd:pfam00435    4 QQFFRDADDLESWIE-EKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEK-LIDEGHYASEEIQER 81
                           90       100
                   ....*....|....*....|....
gi 1761000869 4929 LNTIKTNWDTFNKQVKERENKLKE 4952
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
4047-4153 7.51e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.79  E-value: 7.51e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  4047 QHYEDASCGLLAGLQACEATASkhlSEPIAVDPKNLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGsllPAKND 4126
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLA---SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH---PDAEE 74
                            90       100
                    ....*....|....*....|....*..
gi 1761000869  4127 IQKTLDDIVGRYEDLSKSVNERNEKLQ 4153
Cdd:smart00150   75 IEERLEELNERWEELKELAEERRQKLE 101
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
3674-4657 7.68e-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: 56.60  E-value: 7.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3674 DGTVELKKYqsKQEELQKDMQgsaqALAEVVKNTENFLKENGEKLSQEDKALIEQKLNEAKIKC---EQL---NLKAEQS 3747
Cdd:TIGR01612  736 DIIVEIKKH--IHGEINKDLN----KILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNhynDQInidNIKDEDA 809
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3748 KKELDKvvttaiKEETEKVAAVKQLEESKT--KIENLLD-WLSNVDKDSERAgTKHKQVIEQNGTHFQEGDGKSAIGEED 3824
Cdd:TIGR01612  810 KQNYDK------SKEYIKTISIKEDEIFKIinEMKFMKDdFLNKVDKFINFE-NNCKEKIDSEHEQFAELTNKIKAEISD 882
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3825 EvNGNLLETDVDGQ---VGTTQENLNQQYQKVKAQhEKIISQHQAVIIATQSAQVLLEKQGQYlspeeKEKLQKNMKELK 3901
Cdd:TIGR01612  883 D-KLNDYEKKFNDSkslINEINKSIEEEYQNINTL-KKVDEYIKICENTKESIEKFHNKQNIL-----KEILNKNIDTIK 955
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3902 vhyETALAESEKKMKLTHSLQEELEKFDADYTEfehwLQQSEQELENLEAgADDINGLMTKLKRQKsfsEDVISHKGDLR 3981
Cdd:TIGR01612  956 ---ESNLIEKSYKDKFDNTLIDKINELDKAFKD----ASLNDYEAKNNEL-IKYFNDLKANLGKNK---ENMLYHQFDEK 1024
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3982 YITISG--NRVLEAAKSCSKRDGGkVDTSATH--REVQRKLDHATDRF-RSLYSKCNVLGNNLKDLVDKYQHYEDASCGL 4056
Cdd:TIGR01612 1025 EKATNDieQKIEDANKNIPNIEIA-IHTSIYNiiDEIEKEIGKNIELLnKEILEEAEINITNFNEIKEKLKHYNFDDFGK 1103
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4057 LAGLqaceatasKHLSEpiavdpknLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGSLLpakNDIQKTLDDIVg 4136
Cdd:TIGR01612 1104 EENI--------KYADE--------INKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQI---NDLEDVADKAI- 1163
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4137 rYEDLSKSVNERNEKLQITLTRSLSVQDGLDEMLDWMGNVESslkeqgqvplNSTALQDIisKNIMLEQDIAGRQSSINA 4216
Cdd:TIGR01612 1164 -SNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEK----------DKTSLEEV--KGINLSYGKNLGKLFLEK 1230
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4217 MNEKVKKfmettDPSTASSLQAKMKDLSaRFSEASHKHKETLAKMEELKTKVELFENLSEKLQTF-------------LE 4283
Cdd:TIGR01612 1231 IDEEKKK-----SEHMIKAMEAYIEDLD-EIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHhiiskkhdenisdIR 1304
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4284 TKTQALTEVDVPGKDVTELSQYMQEStseFLEHKKHLEVLHSLLKEISShglpSDKALVLEKTNNLSKKFKEMEDTIKEK 4363
Cdd:TIGR01612 1305 EKSLKIIEDFSEESDINDIKKELQKN---LLDAQKHNSDINLYLNEIAN----IYNILKLNKIKKIIDEVKEYTKEIEEN 1377
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4364 KEAVTScqeQLDAFQVLVKSLKSWIKETTKKVPIvQPSFGAEDLGKSLEDTKK-----LQEKWSLKTP-EIQKVNNSGIS 4437
Cdd:TIGR01612 1378 NKNIKD---ELDKSEKLIKKIKDDINLEECKSKI-ESTLDDKDIDECIKKIKElknhiLSEESNIDTYfKNADENNENVL 1453
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4438 LcnLISAVttpakAIAAVKSGGAVLNGEGTATNTEEFWANKgltsiKKDMTDISHGYEDlglllkdkiaelntKLSKLQK 4517
Cdd:TIGR01612 1454 L--LFKNI-----EMADNKSQHILKIKKDNATNDHDFNINE-----LKEHIDKSKGCKD--------------EADKNAK 1507
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4518 AQEESSAMM-QWLQKMNKTATKWQQTpaptdteAVKTQVEQNKSfeaELKQNVNKVQELKDKLTELLEENPDTPEAPRWK 4596
Cdd:TIGR01612 1508 AIEKNKELFeQYKKDVTELLNKYSAL-------AIKNKFAKTKK---DSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKE 1577
                          970       980       990      1000      1010      1020
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1761000869 4597 QMLTEID-SKWQELNQLTIDRQQKLEESSNNLTQFQTVEAQLKQWLVEKELMVSVLGPLSID 4657
Cdd:TIGR01612 1578 KFRIEDDaAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSID 1639
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
4747-5596 8.83e-07

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: 56.59  E-value: 8.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4747 SLSDKLSDLDNKLSSSLAVS---------THPDAMNQQLETAQKMKQ---EIQQEKKQIKvAQALCEDLSALVKEEYLKA 4814
Cdd:TIGR00606  127 SLSSKCAEIDREMISHLGVSkavlnnvifCHQEDSNWPLSEGKALKQkfdEIFSATRYIK-ALETLRQVRQTQGQKVQEH 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4815 ELSRQLegiLKSFKDVEQKAENHVQHLQSACASShqfQQMSRDFQAWLDTKKEEQNKSHPISAKLDVLESLIKDHKDFSK 4894
Cdd:TIGR00606  206 QMELKY---LKQYKEKACEIRDQITSKEAQLESS---REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKK 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4895 TLTAQSHMYE--------------KTIAEGENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLKESLEKALKY 4960
Cdd:TIGR00606  280 QMEKDNSELElkmekvfqgtdeqlNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRH 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4961 KEQVETLWPWIDKCQNNLEEIKFCLDPaEGENSIAKLKSLQKE-MDQHFGMVELLNNTANSLLSVCEIDKEVVTDENKSL 5039
Cdd:TIGR00606  360 QEHIRARDSLIQSLATRLELDGFERGP-FSERQIKNFHTLVIErQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGL 438
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5040 IQKVDMVTEQLHSKKfclENMTQKFKEFQEVSKESKRQLQCAKEQLDIHDSLgSQAYSNKYLTMLQTQQKSLQALKHQVD 5119
Cdd:TIGR00606  439 GRTIELKKEILEKKQ---EELKFVIKELQQLEGSSDRILELDQELRKAEREL-SKAEKNSLTETLKKEVKSLQNEKADLD 514
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5120 LAKRlAQDLVVEASDSKGTSdvLLQVETIAQEHSTLSQQVDEKCSFLETKLQG-IGHFQNTI---REMFSQFAEFDDELD 5195
Cdd:TIGR00606  515 RKLR-KLDQEMEQLNHHTTT--RTQMEMLTKDKMDKDEQIRKIKSRHSDELTSlLGYFPNKKqleDWLHSKSKEINQTRD 591
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5196 SMAPVGRDAETLQKQKETIKAFLKKLEALMAS-NDNANKTCkmmlATEETSPDLVGIKRDLEALSKQ------------- 5261
Cdd:TIGR00606  592 RLAKLNKELASLEQNKNHINNELESKEEQLSSyEDKLFDVC----GSQDEESDLERLKEEIEKSSKQramlagatavysq 667
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5262 -----------CNKLLDRAQAREEQVEGTIKRLEE----FYSKLKEFSILLQKAE-EHEESQGPVGMETETINQqlnmfk 5325
Cdd:TIGR00606  668 fitqltdenqsCCPVCQRVFQTEAELQEFISDLQSklrlAPDKLKSTESELKKKEkRRDEMLGLAPGRQSIIDL------ 741
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5326 vfQKEEIEPLQGKQQDVNwlgqgliqsaaksTSTQGLEHDLDDVNARWKTLNKKVaQRAAQLQEALLHCGRFQDALEsll 5405
Cdd:TIGR00606  742 --KEKEIPELRNKLQKVN-------------RDIQRLKNDIEEQETLLGTIMPEE-ESAKVCLTDVTIMERFQMELK--- 802
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5406 swmvDTEELVANQkppSAEFKVVKAQIQEQKLLQRlLDDRKSTVEVIKREGEKIATTAEPADkvkilKQLSLLDSRweal 5485
Cdd:TIGR00606  803 ----DVERKIAQQ---AAKLQGSDLDRTVQQVNQE-KQEKQHELDTVVSKIELNRKLIQDQQ-----EQIQHLKSK---- 865
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5486 LNKAETRNRQLEGISVVAQQFHETLEPLNEwlttiekrlvNCEPIGTQASKLEEQIAQHKVLQEDILLRKQNvdqaLLNG 5565
Cdd:TIGR00606  866 TNELKSEKLQIGTNLQRRQQFEEQLVELST----------EVQSLIREIKDAKEQDSPLETFLEKDQQEKEE----LISS 931
                          890       900       910
                   ....*....|....*....|....*....|.
gi 1761000869 5566 LELLKQTTGDEVLIIQDKLEAIKARYKDITK 5596
Cdd:TIGR00606  932 KETSNKKAQDKVNDIKEKVKNIHGYMKDIEN 962
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
39-133 1.17e-06

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


Pssm-ID: 409135  Cd Length: 105  Bit Score: 50.41  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   39 KTFTKWINQHLMKV--RKHVNDLYEDLRDGHNLISLLEVLSGDTL------PREKGRMrfhrLQNVQIALDYLKRRQVKL 110
Cdd:cd21286      3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 78
                           90       100
                   ....*....|....*....|...
gi 1761000869  111 VNIRNDDITDGNPKLTLGLIWTI 133
Cdd:cd21286     79 QGLSAEEIRNGNLKAILGLFFSL 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
5719-5825 1.96e-06

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: 50.01  E-value: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5719 LRSQQFDQAADAELSWITETEKKLMSlGDIRLEQDQTSAQLQVQKTFTMEILRHKDIIDDLVKSGHKIMTACSEEEKQsM 5798
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE-I 78
                           90       100
                   ....*....|....*....|....*..
gi 1761000869 5799 KKKLDKVLKNYDTICQINSERYLQLER 5825
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4865-5814 2.31e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 2.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4865 KKEEQNKSHPISAKLDVLESLIKDHKDFSKTLTAQSHMYEKTIAegenllLKTQGSEkaaLQLQLNTiktnwdtfnKQVK 4944
Cdd:TIGR02168  174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE------LKAELRE---LELALLV---------LRLE 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4945 ERENKLKESLEKALKYKEQVETLWPWIDKCQNNLEEIKfcLDPAEGENSI----AKLKSLQKEMDQHFGMVELLNNTANS 5020
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELR--LEVSELEEEIeelqKELYALANEISRLEQQKQILRERLAN 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5021 LL-SVCEIDKEVVTDENKSLIQK--VDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRQLQCAKEQLDIHDSLGSQAYS 5097
Cdd:TIGR02168  314 LErQLEELEAQLEELESKLDELAeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5098 NKYLTM--LQTQQKSLQALKHQVDLAKRLAQDLVVEASDSKgTSDVLLQVETIAQEHSTLSQQVDEKCSFLETKLQGIGH 5175
Cdd:TIGR02168  394 QIASLNneIERLEARLERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEELEEELEELQEELERLEEALEELREELEE 472
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5176 FQNTIREMFSQFAEFDDELDSMAPVGRDAETLQKQKETIKAFLKKLEALMASndnanktckmmLAteetspDLVGIKRDL 5255
Cdd:TIGR02168  473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV-----------LS------ELISVDEGY 535
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5256 E-----ALSKQCNKLLDRaqaREEQVEGTIKRLEEFYSKLKEFSILLQKAEEHEESQGPVGMETETINQQLNMFKVFQKE 5330
Cdd:TIGR02168  536 EaaieaALGGRLQAVVVE---NLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5331 EIEPLQGkqqdvNWLGQGLI----QSA---AKSTSTQGLEHDLDD--VNARWkTLNKKVAQRAAQLQEallhcgrfqdal 5401
Cdd:TIGR02168  613 KLRKALS-----YLLGGVLVvddlDNAlelAKKLRPGYRIVTLDGdlVRPGG-VITGGSAKTNSSILE------------ 674
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5402 esllswmvdteelvanqkpPSAEFKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKIATTAEpADKVKILKQLSLLDSR 5481
Cdd:TIGR02168  675 -------------------RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLR-KELEELSRQISALRKD 734
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5482 WEALLNKAETRNRQLEGISVVAQQFHETLEPLNEWLTTIEKRLVNCEpigTQASKLEEQIAQHKvlQEDILLRKQnvdqa 5561
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE---AEIEELEAQIEQLK--EELKALREA----- 804
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5562 lLNGLELLKQTTGDEVLIIQDKLEAIKARYKDITKLSTDVAKTLEQALQLARRLHSTHEELCTWLDKVEVELLSYETQVL 5641
Cdd:TIGR02168  805 -LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5642 KGEEA-----SQAQMRPKELKKEAKNNKALLDSLNEVSSALLELVpwRAREGLEKMVAED----NERYRLVSDTITQKVE 5712
Cdd:TIGR02168  884 SLEEAlallrSELEELSEELRELESKRSELRRELEELREKLAQLE--LRLEGLEVRIDNLqerlSEEYSLTLEEAEALEN 961
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5713 EIDAAILRSQQFdqaadaelswITETEKKLMSLGDIRLEQDQTSAQLQVQKTFtmeILRHKDIIDDLVKSGHKIMTACSE 5792
Cdd:TIGR02168  962 KIEDDEEEARRR----------LKRLENKIKELGPVNLAAIEEYEELKERYDF---LTAQKEDLTEAKETLEEAIEEIDR 1028
                          970       980
                   ....*....|....*....|..
gi 1761000869 5793 EEKQSMKKKLDKVLKNYDTICQ 5814
Cdd:TIGR02168 1029 EARERFKDTFDQVNENFQRVFP 1050
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4501-5322 2.37e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 2.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4501 LKDKIAELNTKLSKLQKaQEESSAMMQWLQKMNKTATKWQQTpapTDTEAVKTQVEQnksFEAELKQNVNKVQELKDKLT 4580
Cdd:TIGR02168  191 LEDILNELERQLKSLER-QAEKAERYKELKAELRELELALLV---LRLEELREELEE---LQEELKEAEEELEELTAELQ 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4581 ELLEEnpdtpeaprwkqmLTEIDSKWQELNQLTIDRQQKLEESSNNLtqfQTVEAQlKQWLVEKelmvsvLGPLSIDPNM 4660
Cdd:TIGR02168  264 ELEEK-------------LEELRLEVSELEEEIEELQKELYALANEI---SRLEQQ-KQILRER------LANLERQLEE 320
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4661 LNTQRQQVQ----ILLQEFATRKPQYEQLtaagqgilsrpgedpslrgivKEQLAAVTQKWDSLTGQLSDRCDWIDQAIV 4736
Cdd:TIGR02168  321 LEAQLEELEskldELAEELAELEEKLEEL---------------------KEELESLEAELEELEAELEELESRLEELEE 379
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4737 KSTQYQSLLRSLSDKLSDLDNKLSSSLAVSTHPDAMNQQLETAQKMKQEIQQEKKQIKVAQALCEDLSALVKEEYLKAEL 4816
Cdd:TIGR02168  380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4817 SRQLEGILKSFKDVEQK---AENHVQHLQSACASshqFQQMSRDFQAWLDTKKEEQNKSHPISAKLDVLESLIKDHKDFS 4893
Cdd:TIGR02168  460 EEALEELREELEEAEQAldaAERELAQLQARLDS---LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4894 KTLtaqshmyEKTIAEG-ENLLLKTQGSEKAALQLQLNTIKTNWdTFNKQVKERENKLKESLEKALKYKEQVETLWPWID 4972
Cdd:TIGR02168  537 AAI-------EAALGGRlQAVVVENLNAAKKAIAFLKQNELGRV-TFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4973 KCQNNLEE-IKFCLDPAEGENSIAKLKSLQKEMDQHFGMV----ELLN----------NTANSLLSV------CEIDKEV 5031
Cdd:TIGR02168  609 KFDPKLRKaLSYLLGGVLVVDDLDNALELAKKLRPGYRIVtldgDLVRpggvitggsaKTNSSILERrreieeLEEKIEE 688
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5032 VTDENKSLIQKVDMVTEQlhskkfcLENMTQKFKEFQEVSKESKRQLQCAKEQLDIHdslgsQAYSNKYLTMLQTQQKSL 5111
Cdd:TIGR02168  689 LEEKIAELEKALAELRKE-------LEELEEELEQLRKELEELSRQISALRKDLARL-----EAEVEQLEERIAQLSKEL 756
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5112 QALKHQvdlAKRLAQDLVVEASDSKGTSDVLLQVETIAQEHSTLSQQVDEKCSFLETKLqgighfQNTIREMFSQFAEFD 5191
Cdd:TIGR02168  757 TELEAE---IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL------TLLNEEAANLRERLE 827
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5192 DELDSMAPVGRDAETLQKQKETIKAFLKKLEALMASndnanktckmmlatEETSPDlvGIKRDLEALSKQCNKL---LDR 5268
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE--------------LEELIE--ELESELEALLNERASLeeaLAL 891
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1761000869 5269 AQAREEQVEGTIKRLEefysklKEFSILLQKAEEHEESQGPVGMETETINQQLN 5322
Cdd:TIGR02168  892 LRSELEELSEELRELE------SKRSELRRELEELREKLAQLELRLEGLEVRID 939
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
147-256 3.08e-06

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: 49.68  E-value: 3.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  147 ESEDMSAKERLLLWTQQATegyAGIRCENFTTCWRDGKLFNAIIHKYRPDLI-DMNTVAVQSNLANLEHAFYVAEK-IGV 224
Cdd:cd21314      6 DARKQTPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDwLGV 82
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1761000869  225 IRLLDPEDVDVSSPDEKSVITYVSSlydaFPK 256
Cdd:cd21314     83 PQVIAPEEIVDPNVDEHSVMTYLSQ----FPK 110
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6813-6917 4.34e-06

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: 48.85  E-value: 4.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6813 RQAEEFHSVVHALLEWLAEAEQTLRfHGVLPDDEDALRTLIDQHKEFMKKLEEKRAELNKATTMGDTVLAICHPDSiTTI 6892
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLS-SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYAS-EEI 78
                           90       100
                   ....*....|....*....|....*
gi 1761000869 6893 KHWITIIRARFEEVLAWAKQHQQRL 6917
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKL 103
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
145-256 4.81e-06

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: 48.94  E-value: 4.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  145 TGESEDMSAKERLLLWTQQATEgYAGIrcENFTTCWRDGKLFNAIIHKYRPDLI-DMNTVAVQSNLANLEHAFYVAEK-I 222
Cdd:cd21313      1 DDDAKKQTPKQRLLGWIQNKIP-YLPI--TNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDwL 77
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1761000869  223 GVIRLLDPEDVDVSSPDEKSVITYVSSlydaFPK 256
Cdd:cd21313     78 GVPQVITPEEIIHPDVDEHSVMTYLSQ----FPK 107
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
23-144 5.13e-06

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


Pssm-ID: 409172  Cd Length: 145  Bit Score: 50.04  E-value: 5.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   23 EDVLERYKDErdkvQKKTFTKWINQ---------HLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMR 89
Cdd:cd21323     15 EGTQHSYSEE----EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTP 90
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1761000869   90 FHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHV 144
Cdd:cd21323     91 FTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
4702-5494 5.80e-06

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: 53.58  E-value: 5.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4702 LRGIVKEQLAAVTQKWDsltgQLSDRCDWIDQAIVKSTQYQSLLRSLSDKLSDLDNklSSSLAVSTHpDAMN----QQLE 4777
Cdd:pfam15921  147 LQNTVHELEAAKCLKED----MLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEE--ASGKKIYEH-DSMStmhfRSLG 219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4778 TA-QKMKQEIQQEKKQIKVAQALCEDlsalvKEEYLKAELSRQLEGILKSFKD-VEQKAENHVQHLQSACASSHQFQQMS 4855
Cdd:pfam15921  220 SAiSKILRELDTEISYLKGRIFPVED-----QLEALKSESQNKIELLLQQHQDrIEQLISEHEVEITGLTEKASSARSQA 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4856 RDFQAWLDTKKEE-QNKSHPISAKLDVLESLIKDhkdFSKTLTAQSHMYEKTIAEGENLLLKTQGsekaalqlQLNTIKT 4934
Cdd:pfam15921  295 NSIQSQLEIIQEQaRNQNSMYMRQLSDLESTVSQ---LRSELREAKRMYEDKIEELEKQLVLANS--------ELTEART 363
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4935 NWDTFNKQVKERENKLKESL------EKALKY-KEQVETLWpwiDKCQNN---LEEIKFCLDP--AEGENSIAKLKSLQK 5002
Cdd:pfam15921  364 ERDQFSQESGNLDDQLQKLLadlhkrEKELSLeKEQNKRLW---DRDTGNsitIDHLRRELDDrnMEVQRLEALLKAMKS 440
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5003 E----MDQHFGMVELLNNtanSLLSVCEIDKEVvtDENKSLIQKVdmvTEQLHSKKFCLENMTQKFKEFQEVSKESKRQL 5078
Cdd:pfam15921  441 EcqgqMERQMAAIQGKNE---SLEKVSSLTAQL--ESTKEMLRKV---VEELTAKKMTLESSERTVSDLTASLQEKERAI 512
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5079 QCAKEQLdihdslgsqaysNKYLTMLQTQQKSLQALKHQVDLAKRLAQD---LVVEASDSKGTSDVL-LQVETIAQ---- 5150
Cdd:pfam15921  513 EATNAEI------------TKLRSRVDLKLQELQHLKNEGDHLRNVQTEceaLKLQMAEKDKVIEILrQQIENMTQlvgq 580
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5151 ----------EHSTLSQQVDEKcsflETKLQGIGHFQN----TIREMFSQFAefDDELDSMAPVGRDAETLQkqkeTIKA 5216
Cdd:pfam15921  581 hgrtagamqvEKAQLEKEINDR----RLELQEFKILKDkkdaKIRELEARVS--DLELEKVKLVNAGSERLR----AVKD 650
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5217 FLKKLEALMasndNANKTCKMMLatEETSPDLVGIKRDL----EALSKQCNKL---LDRAQAREEQVEGTIKRLEEFYSK 5289
Cdd:pfam15921  651 IKQERDQLL----NEVKTSRNEL--NSLSEDYEVLKRNFrnksEEMETTTNKLkmqLKSAQSELEQTRNTLKSMEGSDGH 724
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5290 LKEFSILLQKAEEHEESQ-GPVGMETETINQQL---NMFKVFQKEEieplqgkqqdVNWLGQGLIQSAAKSTSTQGlehD 5365
Cdd:pfam15921  725 AMKVAMGMQKQITAKRGQiDALQSKIQFLEEAMtnaNKEKHFLKEE----------KNKLSQELSTVATEKNKMAG---E 791
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5366 LDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDAL-----ESL---LSWMVDTEELvanQKPPSAEFKVVKAQIQEQKL 5437
Cdd:pfam15921  792 LEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIqrqeqESVrlkLQHTLDVKEL---QGPGYTSNSSMKPRLLQPAS 868
                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1761000869 5438 LQRL---LDDRKSTVEVIKREGEKiaTTAEPADKVKILKQL-----SLLDSRWEALLNKAETRNR 5494
Cdd:pfam15921  869 FTRThsnVPSSQSTASFLSHHSRK--TNALKEDPTRDLKQLlqelrSVINEEPTVQLSKAEDKGR 931
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
5396-5497 8.58e-06

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: 48.08  E-value: 8.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5396 RFQDALESLLSWMVDTEELVANQKPPSaEFKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEKIaTTAEPADKVKILKQL 5475
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKL-IDEGHYASEEIQERL 82
                           90       100
                   ....*....|....*....|..
gi 1761000869 5476 SLLDSRWEALLNKAETRNRQLE 5497
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLE 104
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
154-248 9.85e-06

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: 47.77  E-value: 9.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  154 KERLLLWTQQAtegYAGIRCENFTTCWRDGKLFNAIIHKYRPDLI-DMNTVAVQSNLANLEHAFYVAEKI-GVIRLLDPE 231
Cdd:cd21229      5 KKLMLAWLQAV---LPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREfNIPMVLSPE 81
                           90
                   ....*....|....*....
gi 1761000869  232 DVdvSSP--DEKSVITYVS 248
Cdd:cd21229     82 DL--SSPhlDELSGMTYLS 98
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
3533-5094 1.02e-05

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: 53.13  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3533 SKSVKDIEIV------NVQDS--EYVKKRLEFL-KNVLK-------DLGHTKMQLETTAFDVqfFISE----YAQDLSP- 3591
Cdd:TIGR01612 1039 NKNIPNIEIAihtsiyNIIDEieKEIGKNIELLnKEILEeaeinitNFNEIKEKLKHYNFDD--FGKEenikYADEINKi 1116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3592 -NQSKQLLRLLNTTQKCFLDVQESVTTQVERLETQLHLEQDLDDQKIVAERQQEYKEKLQGICDLLTQTENrlighqeaf 3670
Cdd:TIGR01612 1117 kDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKN--------- 1187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3671 mIGDgtvELKKYQSKQEELQKDmqgsaQALAEVVKNTENFLKENGEKLSQEdkalieqKLNEAKIKCEQLNLKAEQSKKE 3750
Cdd:TIGR01612 1188 -IYD---EIKKLLNEIAEIEKD-----KTSLEEVKGINLSYGKNLGKLFLE-------KIDEEKKKSEHMIKAMEAYIED 1251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3751 LDKvvttaIKEETEKVAAVKQLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIeqngthfqegdgkSAIGEEDE--VNG 3828
Cdd:TIGR01612 1252 LDE-----IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENI-------------SDIREKSLkiIED 1313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3829 NLLETDVDGQVGTTQENLNQQyQKVKAQHEKIISQHQAV--IIATQSAQVLLEKQGQYlsPEEKEKLQKNMKELKVHYET 3906
Cdd:TIGR01612 1314 FSEESDINDIKKELQKNLLDA-QKHNSDINLYLNEIANIynILKLNKIKKIIDEVKEY--TKEIEENNKNIKDELDKSEK 1390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3907 ALaeseKKMKLTHSLQEELEKFDA--DYTEFEHWLQQSEQELENLEAGADDINglmTKLKRQKSFSEDVIShkgDLRYIT 3984
Cdd:TIGR01612 1391 LI----KKIKDDINLEECKSKIEStlDDKDIDECIKKIKELKNHILSEESNID---TYFKNADENNENVLL---LFKNIE 1460
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3985 ISGNRVLEAAKScsKRDGGKVDTSATHREVQRKLDHAtdrfrslySKCNVLGNNLKDLVDK----YQHYEDASCGLLAGL 4060
Cdd:TIGR01612 1461 MADNKSQHILKI--KKDNATNDHDFNINELKEHIDKS--------KGCKDEADKNAKAIEKnkelFEQYKKDVTELLNKY 1530
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4061 QACEA----TASKHLSEPIAVDPKNLQRQ--LEETKALQ--GQISSQQVAVE----KLKKTAEVLLDARGSLLPAKN--- 4125
Cdd:TIGR01612 1531 SALAIknkfAKTKKDSEIIIKEIKDAHKKfiLEAEKSEQkiKEIKKEKFRIEddaaKNDKSNKAAIDIQLSLENFENkfl 1610
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4126 ---DIQKTLDDIVGRYEDLSK-----SVNERNEKLQITLTRSLSVQDGLDEMLDWMGNVESSLKEqgqvplnstaLQDII 4197
Cdd:TIGR01612 1611 kisDIKKKINDCLKETESIEKkissfSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKE----------LDELD 1680
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4198 SKNIMLEQDIAGRQSSIN-AMNEKVKKFMETTD---PSTASSLQAKMKDLSARFSEASHKHKETLAKMEELKTKV----E 4269
Cdd:TIGR01612 1681 SEIEKIEIDVDQHKKNYEiGIIEKIKEIAIANKeeiESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIgdiyE 1760
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4270 LFENLSEKLQTFLET-KTQALTEVDVPGKDVTELSQYMQESTSEflehKKHLEVLHSL----LKEISSHgLPSDKALVLE 4344
Cdd:TIGR01612 1761 EFIELYNIIAGCLETvSKEPITYDEIKNTRINAQNEFLKIIEIE----KKSKSYLDDIeakeFDRIINH-FKKKLDHVND 1835
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4345 KTNNLSKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSLKSWIKETTKKVpiVQPSFGAEDLGKSLedtKKLqeKWSLK 4424
Cdd:TIGR01612 1836 KFTKEYSKINEGFDDISKSIENVKNSTDENLLFDILNKTKDAYAGIIGKKY--YSYKDEAEKIFINI---SKL--ANSIN 1908
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4425 tpeIQKVNNSGISLCNLISavttpakaIAAVKSggavLNGEgtATNTEEFWANKGLTSikKDMTDISHGYedlglllkdk 4504
Cdd:TIGR01612 1909 ---IQIQNNSGIDLFDNIN--------IAILSS----LDSE--KEDTLKFIPSPEKEP--EIYTKIRDSY---------- 1959
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4505 iaelNTKLSKLQKAQEESSAMMQWLQKMNKTATKWQQTPAPTDTEAVKTQVEQNKsfeaelKQNVNKVQELKDKLTELLE 4584
Cdd:TIGR01612 1960 ----DTLLDIFKKSQDLHKKEQDTLNIIFENQQLYEKIQASNELKDTLSDLKYKK------EKILNDVKLLLHKFDELNK 2029
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4585 -----ENPDTP-EAPRWKQMLTEIDSKWQELNQLTIDRQQKLEES--SNNLTQFQTVEAQLKQWLVEKElmvsvlgPLSI 4656
Cdd:TIGR01612 2030 lscdsQNYDTIlELSKQDKIKEKIDNYEKEKEKFGIDFDVKAMEEkfDNDIKDIEKFENNYKHSEKDNH-------DFSE 2102
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4657 DPNMLNTQRQQVQILLQEFATRKPQYEQLTAAGQGILSRpgedpsLRGIVKE-QLAAVTQKWDSLTGQLSDRCDWIDQAI 4735
Cdd:TIGR01612 2103 EKDNIIQSKKKLKELTEAFNTEIKIIEDKIIEKNDLIDK------LIEMRKEcLLFSYATLVETLKSKVINHSEFITSAA 2176
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4736 VKSTQYQSLLRSLSDKLSDLDNKLSSSLAVSTHPDAMNQQLETAQKMKQE-IQQEKKQIKVAQALCE---------DLSA 4805
Cdd:TIGR01612 2177 KFSKDFFEFIEDISDSLNDDIDALQIKYNLNQTKKHMISILADATKDHNNlIEKEKEATKIINNLTElftidfnnaDADI 2256
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4806 L----VKEEYLKAELSRQLEGILKSFKDVEQKAENHVQHLQSacasshQFQQMSRDFQAWLDTKKeeqNKSHPISAKLDV 4881
Cdd:TIGR01612 2257 LhnnkIQIIYFNSELHKSIESIKKLYKKINAFKLLNISHINE------KYFDISKEFDNIIQLQK---HKLTENLNDLKE 2327
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4882 LESLIKDHKD-FSKTLTAQSHMYEKTIAEGENLLLKTQGsekaalqlQLNTIKtnwdtfNKQVKERENkLKESLEKALKY 4960
Cdd:TIGR01612 2328 IDQYISDKKNiFLHALNENTNFNFNALKEIYDDIINREN--------KADEIE------NINNKENEN-IMQYIDTITKL 2392
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4961 KEQVETLWPWIDKCQNNLEEIKFCLDPAEgENSIAKLKSLQKEMDQHFGmvELLNNtansllsVCEIDKEVVTDENKSLI 5040
Cdd:TIGR01612 2393 TEKIQDILIFVTTYENDNNIIKQHIQDND-ENDVSKIKDNLKKTIQSFQ--EILNK-------IDEIKAQFYGGNNINNI 2462
                         1610      1620      1630      1640      1650      1660
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1761000869 5041 -----QKVDMVtEQLHSKKFCLEN-MTQKFKEFQEV--SKESKRQLQCAKEQLDIHDSLGSQ 5094
Cdd:TIGR01612 2463 iitisQNANDV-KNHFSKDLTIENeLIQIQKRLEDIknAAHEIRSEQITKYTNAIHNHIEEQ 2523
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
5613-6499 1.08e-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: 52.75  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5613 RRLHSTHEELctwlDKVEVELLSYETQVLK-GEEASQAQmRPKELKKEAKNNKALLdSLNEVSSALLELvpwRAREGLEK 5691
Cdd:TIGR02168  179 RKLERTRENL----DRLEDILNELERQLKSlERQAEKAE-RYKELKAELRELELAL-LVLRLEELREEL---EELQEELK 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5692 MVAEDNERYRLVSDTITQKVEEIDAAIL-RSQQFDQAADAELSWITETEKKLMSLGDIRLEQDQTSAQLQVQKTFTMEIL 5770
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSeLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5771 RHKDI-IDDLVKSGHKIMTAcsEEEKQSMKKKLDKVLKNYDTICQINSERYLQLERAQSLVNQFWETYEELwpwLTETQS 5849
Cdd:TIGR02168  330 SKLDElAEELAELEEKLEEL--KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIER 404
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5850 IISQLPAPALEYETLRQQQEEHRQlreliaehKPHIDKMNKTGPQLLELSPGEgFSIQEKYVAADTLYSQIKEDVKKRAV 5929
Cdd:TIGR02168  405 LEARLERLEDRRERLQQEIEELLK--------KLEEAELKELQAELEELEEEL-EELQEELERLEEALEELREELEEAEQ 475
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5930 ALDEAISQstqfHDKIDQILESLERIVERLRQPPSISAEVEKIKEQISENKNVSVDMEKLQPLYETlkqrgeEMIARSGG 6009
Cdd:TIGR02168  476 ALDAAERE----LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEA------AIEAALGG 545
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6010 TDKDIsakaVQDKLDQmvfIWENIHTLVEEREAKLLdVMEL----AEKFWCDHMSLIVTIKDTQDFIRDLE--DPGIDPS 6083
Cdd:TIGR02168  546 RLQAV----VVENLNA---AKKAIAFLKQNELGRVT-FLPLdsikGTEIQGNDREILKNIEGFLGVAKDLVkfDPKLRKA 617
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6084 ---------VVKQQQEAAETIREeidgLQEELDIVInLGSELIAACGEpdkpIVKKSIDELNSAwdsLNKawKDRIDKLE 6154
Cdd:TIGR02168  618 lsyllggvlVVDDLDNALELAKK----LRPGYRIVT-LDGDLVRPGGV----ITGGSAKTNSSI---LER--RREIEELE 683
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6155 EAM-QAAVQYQDGLQAvfdwvdiaggklasmspigtdLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEES 6233
Cdd:TIGR02168  684 EKIeELEEKIAELEKA---------------------LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6234 DKHTVQdplmelkliWDSLEERIINRQHKLEGALLALGQFQHALDELLawlthtEGLLSEQKPVGGdpkaieielakhhv 6313
Cdd:TIGR02168  743 EQLEER---------IAQLSKELTELEAEIEELEERLEEAEEELAEAE------AEIEELEAQIEQ-------------- 793
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6314 LQNDVLAHQSTVEAVNKAGNDLiessaGEEASNLQNKLEVLNQRWQNVLEKTEQRKQQLDGALRQAKGFHGEIEDLQQWL 6393
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLL-----NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6394 TDTER---HLLASKplgglpETAKEQLNVHMEVCAAFEAKEETYKSLMQKGQQMLARCpksaetniDQDINNLKEKWESV 6470
Cdd:TIGR02168  869 EELESeleALLNER------ASLEEALALLRSELEELSEELRELESKRSELRRELEEL--------REKLAQLELRLEGL 934
                          890       900
                   ....*....|....*....|....*....
gi 1761000869 6471 ETKLNERKTKLEEALNLAMEFHNSLQDFI 6499
Cdd:TIGR02168  935 EVRIDNLQERLSEEYSLTLEEAEALENKI 963
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
4494-5069 1.32e-05

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: 52.43  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4494 YEDLGLLLKDKIAELNTKLS-----------KLQKAQEESSAMMQWLQKMNK--------------TATKWQQTPAPTDT 4548
Cdd:pfam15921  215 FRSLGSAISKILRELDTEISylkgrifpvedQLEALKSESQNKIELLLQQHQdrieqliseheveiTGLTEKASSARSQA 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4549 EAVKTQVE--------QNKSFEAELKQNVNKVQELKDKLTELLEENPDTPEAPRWKQMLTEidskwQELNQLTIDRQQKL 4620
Cdd:pfam15921  295 NSIQSQLEiiqeqarnQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN-----SELTEARTERDQFS 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4621 EESSNNLTQFQTVEAQLKQwlVEKELMVSVLGPLSI-DPNMLNTQrqQVQILLQEFATRKPQYEQLTAAGQGILSRpged 4699
Cdd:pfam15921  370 QESGNLDDQLQKLLADLHK--REKELSLEKEQNKRLwDRDTGNSI--TIDHLRRELDDRNMEVQRLEALLKAMKSE---- 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4700 psLRGIVKEQLAAVT------QKWDSLTGQLSDRCDW----IDQAIVKSTQYQSLLRSLSDKLSDLDNKLSSSLAVSTHP 4769
Cdd:pfam15921  442 --CQGQMERQMAAIQgkneslEKVSSLTAQLESTKEMlrkvVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEI 519
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4770 DAMNQQLETAQKMKQEIQQEKKQIKVAQALCEDLSALVKEEYLKAELSRQlegilksfkDVEQKAENHVQHLQSACASSH 4849
Cdd:pfam15921  520 TKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQ---------QIENMTQLVGQHGRTAGAMQV 590
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4850 QFQQMSRDFQAWLDTKKEEQNKSHPISAKLDVLESLIKDHK-DFSKTLTAQSHMYE--KTIAEGENLLL---KTQGSEKA 4923
Cdd:pfam15921  591 EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElEKVKLVNAGSERLRavKDIKQERDQLLnevKTSRNELN 670
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4924 ALQLQLNTIKTNWDTFNKQVKERENKLKESLEKAlkykeqvetlwpwidkcQNNLEEIKFCLDPAEGEN--SIAKLKSLQ 5001
Cdd:pfam15921  671 SLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSA-----------------QSELEQTRNTLKSMEGSDghAMKVAMGMQ 733
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1761000869 5002 KEMDQHFGMVELLNNTANSL---LSVCEIDKEVVTDENKSLIQKVDMVTEQLHSKKFCLENMTQKFKEFQE 5069
Cdd:pfam15921  734 KQITAKRGQIDALQSKIQFLeeaMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
149-256 1.98e-05

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: 47.47  E-value: 1.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  149 EDMSAKERLLLWTQQATegyAGIRCENFTTCWRDGKLFNAIIHKYRPDLI-DMNTVAVQSNLANLEHAFYVAEK-IGVIR 226
Cdd:cd21315     13 KGPTPKQRLLGWIQSKV---PDLPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDwLDVPQ 89
                           90       100       110
                   ....*....|....*....|....*....|
gi 1761000869  227 LLDPEDVDVSSPDEKSVITYVSslydAFPK 256
Cdd:cd21315     90 LIKPEEMVNPKVDELSMMTYLS----QFPN 115
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
29-134 2.16e-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: 48.04  E-value: 2.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   29 YKDErdkvQKKTFTKWIN---------QHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFHRLQN 95
Cdd:cd21292     21 YSEE----EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHEN 96
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1761000869   96 VQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTII 134
Cdd:cd21292     97 LTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
37-145 2.20e-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: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   37 QKKTFTKWINQ---------HLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFHRLQNVQIALDYL 103
Cdd:cd21325     25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1761000869  104 KRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVT 145
Cdd:cd21325    105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
5067-5959 2.26e-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: 51.60  E-value: 2.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5067 FQEVSKESKRQLQCAKEQL----DIHDSLGSQaysnkyLTMLQTQQKS---LQALKHQV-DLAKRLAQDLVVEASDSKGT 5138
Cdd:TIGR02168  170 YKERRKETERKLERTRENLdrleDILNELERQ------LKSLERQAEKaerYKELKAELrELELALLVLRLEELREELEE 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5139 SDVLL-QVETIAQEHSTLSQQVDEKCSFLETKlqgighfqntIREMFSQFAEFDDELDSmapVGRDAETLQKQKETIKAF 5217
Cdd:TIGR02168  244 LQEELkEAEEELEELTAELQELEEKLEELRLE----------VSELEEEIEELQKELYA---LANEISRLEQQKQILRER 310
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5218 LKKLEAlmasndnanktckmmlateetspDLVGIKRDLEALSKQCNKLLDRAQAREEQVEGTIKRLEEFYSKLKEFSILL 5297
Cdd:TIGR02168  311 LANLER-----------------------QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5298 QKAEEHEESQgpvgmeTETINQQLNmfKVFQ-KEEIEPLQGKQQDVNWLGQGLiQSAAKSTSTQGLEHDLDDVNARWKTL 5376
Cdd:TIGR02168  368 EELESRLEEL------EEQLETLRS--KVAQlELQIASLNNEIERLEARLERL-EDRRERLQQEIEELLKKLEEAELKEL 438
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5377 NKKVAQRAAQLQEALLHCGRFQDALESLlswmvDTEELVANQKPPSAEFKVVKAQiQEQKLLQRLLDDRKSTVEVIKreg 5456
Cdd:TIGR02168  439 QAELEELEEELEELQEELERLEEALEEL-----REELEEAEQALDAAERELAQLQ-ARLDSLERLQENLEGFSEGVK--- 509
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5457 EKIATTAEPADKVKILKQLSLLDSRWEALLNKA----------ETRNRQLEGISVVAQ--QFHETLEPLNEWL-TTIEK- 5522
Cdd:TIGR02168  510 ALLKNQSGLSGILGVLSELISVDEGYEAAIEAAlggrlqavvvENLNAAKKAIAFLKQneLGRVTFLPLDSIKgTEIQGn 589
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5523 ---RLVNCEPIGTQASKLEEQIAQHKVLQEDILLRKQNVDQaLLNGLELLKQTTGDEVLIIQD----------------- 5582
Cdd:TIGR02168  590 dreILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDD-LDNALELAKKLRPGYRIVTLDgdlvrpggvitggsakt 668
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5583 ----------------KLEAIKARYKDITKLSTDVAKTLEQALQLARRLHSTHEELCTWLDKVEVELLSYETQVLKGEEa 5646
Cdd:TIGR02168  669 nssilerrreieeleeKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE- 747
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5647 sQAQMRPKELKKEAKNNKALLDSLNEVSSALLELVpwRAREGLEKMVAEDNERYRLVSDTITQKVEEIDAAILRSQQFDQ 5726
Cdd:TIGR02168  748 -RIAQLSKELTELEAEIEELEERLEEAEEELAEAE--AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5727 AADAELSWITETEKKLMSLGDI--RLEQDQTSAQLQVqktFTMEILRHKdIIDDLVKsgHKIMTACSEEEKQSMKKKLDK 5804
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQieELSEDIESLAAEI---EELEELIEE-LESELEA--LLNERASLEEALALLRSELEE 898
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5805 VLKNYDTICQINSERYLQLERAQSLVNQFWETYEELwpwLTETQSIISQLPApalEYETLRQQQEEH--------RQLRE 5876
Cdd:TIGR02168  899 LSEELRELESKRSELRRELEELREKLAQLELRLEGL---EVRIDNLQERLSE---EYSLTLEEAEALenkieddeEEARR 972
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5877 LIAEHKPHIDKMnktGPQLLElSPGEGFSIQEKYvaaDTLYSQiKEDVKKRAVALDEAISQ-----STQFHDKIDQILES 5951
Cdd:TIGR02168  973 RLKRLENKIKEL---GPVNLA-AIEEYEELKERY---DFLTAQ-KEDLTEAKETLEEAIEEidreaRERFKDTFDQVNEN 1044

                   ....*...
gi 1761000869 5952 LERIVERL 5959
Cdd:TIGR02168 1045 FQRVFPKL 1052
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
3599-4433 2.41e-05

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: 51.51  E-value: 2.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3599 RLLNTTQKCFLDVQESVTTQVERLETQLHLEQDLDDQKIVAERQQEYKEKLqgicDLLTQTENRLIGHQEAFMIGDGTVE 3678
Cdd:pfam02463  174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE----YLLYLDYLKLNEERIDLLQELLRDE 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3679 LKKYQSKQEELQKDMQGSAQALAE------VVKNTENFLKENGEKLSQEDKALIEQKLNEAKIKCEQLNLKAEQSK--KE 3750
Cdd:pfam02463  250 QEEIESSKQEIEKEEEKLAQVLKEnkeeekEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKaeKE 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3751 LDKVVTTAIKEETEKVAAVKQLEESKTKIENLLDWLSNVDKDSERAGTKHKqvieqngthfQEGDGKSAIGEEDEVNGNL 3830
Cdd:pfam02463  330 LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK----------LESERLSSAAKLKEEELEL 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3831 LETDVDgQVGTTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGQYlspEEKEKLQKNMKELKVHYETALAE 3910
Cdd:pfam02463  400 KSEEEK-EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE---LEKQELKLLKDELELKKSEDLLK 475
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3911 SEKKMKLTHSLQEELEKFDADytEFEHWLQQSEQELENLEAGADDINGLMTKLKRQKSFSEDVISHKGDLRYITISGNRV 3990
Cdd:pfam02463  476 ETQLVKLQEQLELLLSRQKLE--ERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEV 553
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3991 LEAAKSCSKRDGGKVDTSATHREVQRKLDHATDRFRSLYSKCNVLGNNLKDLVDKYQHYEDASCGLLAGLQACeataskh 4070
Cdd:pfam02463  554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVE------- 626
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4071 lsepiaVDPKNLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGSLLPAKNDIQKTLDDIVGRYEDLSKSVNERNE 4150
Cdd:pfam02463  627 ------GILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4151 KLQITLTRSLSVQDGLDEMLdwmgnvesslkeqgqvpLNSTALQDIISKNIMLEQDIAGRQSSINAMNEKVKKFMETTDP 4230
Cdd:pfam02463  701 IKKKEQREKEELKKLKLEAE-----------------ELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKE 763
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4231 STASSLQAKMKDLSARFSEASHKHKETLAKMEELKTKVELFENLSEKLQTFLETKTQALTEVDVPGKDVTELSQYMQEST 4310
Cdd:pfam02463  764 EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELK 843
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4311 SEFLEHKKHLEVLHSLLKEISSHGLPSDKALVLEKtnnlSKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSLKSWIKE 4390
Cdd:pfam02463  844 EEQKLEKLAEEELERLEEEITKEELLQELLLKEEE----LEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEI 919
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|...
gi 1761000869 4391 TTKKVPIVQPSFGAEDLGKSLEDTKKLQEKWSLKTPEIQKVNN 4433
Cdd:pfam02463  920 EERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERN 962
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4072-4153 2.48e-05

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: 46.54  E-value: 2.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4072 SEPIAVDPKNLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDARGsllPAKNDIQKTLDDIVGRYEDLSKSVNERNEK 4151
Cdd:pfam00435   26 SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH---YASEEIQERLEELNERWEQLLELAAERKQK 102

                   ..
gi 1761000869 4152 LQ 4153
Cdd:pfam00435  103 LE 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4344-5085 2.49e-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: 51.60  E-value: 2.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4344 EKTNNLSKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSLKSWIKETTKKVpivqpsFGAEDLGKSLEDTKKLQEKwSL 4423
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL------YALANEISRLEQQKQILRE-RL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4424 KTPEIQKVNNSGiSLCNLISAVTTPAKAIAAVKSGGAVLNGEGTATNTEefwaNKGLTSIKKDMTDISHGYEDLGLLLKD 4503
Cdd:TIGR02168  312 ANLERQLEELEA-QLEELESKLDELAEELAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELEEQLETLRS 386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4504 KIAELNTKLSKLQKAQEESSAMMQWLQKMNKtatKWQQTPAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLTELL 4583
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRE---RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4584 EEnpdtpEAPRWKQMLTEIDSKWQELNQLTiDRQQKLEESSNNLTQFQTVEAQLKQWLVEKELMVSVLGPL-SIDP---- 4658
Cdd:TIGR02168  464 EE-----LREELEEAEQALDAAERELAQLQ-ARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELiSVDEgyea 537
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4659 ---------------NMLNTQRQQVQILLQEFATRKPQYEQLTAAGQGILSRPGEDPSLRGIVKEQLAAVTQKWDSLTGQ 4723
Cdd:TIGR02168  538 aieaalggrlqavvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKA 617
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4724 LSDR------CDWIDQAIVKSTQYQSLLRSLSdklsdLDNKLSSSLAVST--HPDAMNQQLETaqkmKQEIQQEKKQIKV 4795
Cdd:TIGR02168  618 LSYLlggvlvVDDLDNALELAKKLRPGYRIVT-----LDGDLVRPGGVITggSAKTNSSILER----RREIEELEEKIEE 688
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4796 AQALCEDLSALVkeeylkAELSRQLEGILKSFKDVEQKAEnhvqhlqsacasshqfqQMSRDFQAWLDTKKEEQNKSHPI 4875
Cdd:TIGR02168  689 LEEKIAELEKAL------AELRKELEELEEELEQLRKELE-----------------ELSRQISALRKDLARLEAEVEQL 745
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4876 SAKLDVLESLIKDhkdfsktLTAQSHMYEKTIAEgENLLLKTQGSEKAALQLQLNTIKTNWDTFNKQVKERENKLKESLE 4955
Cdd:TIGR02168  746 EERIAQLSKELTE-------LEAEIEELEERLEE-AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4956 KALKYKEQVETLWPWIDKCQNNLEEIKfcldpAEGENSIAKLKSLQKEMDQhfgmvellnntansllsvCEIDKEVVTDE 5035
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLE-----EQIEELSEDIESLAAEIEE------------------LEELIEELESE 874
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5036 NKSLIQKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRQLQCAKEQL 5085
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4163-4370 2.77e-05

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 48.98  E-value: 2.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4163 QDGLDEMLDWMGNVESSLKEQgQVPLNSTALQDIISKNIMLEQDIAGRQSSINAMNEKVKKFMEtTDPSTASSLQAKMKD 4242
Cdd:cd00176      6 LRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQERLEE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4243 LSARFSEASHKhkeTLAKMEELKTKVELFENLSE--KLQTFLETKTQALTEVDVPG--KDVTELSQYMQESTSEFLEHKK 4318
Cdd:cd00176     84 LNQRWEELREL---AEERRQRLEEALDLQQFFRDadDLEQWLEEKEAALASEDLGKdlESVEELLKKHKELEEELEAHEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1761000869 4319 HLEVLHSLLKEISSHGLPSDKALVLEKTNNLSKKFKEMEDTIKEKKEAVTSC 4370
Cdd:cd00176    161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
4552-5140 3.01e-05

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: 51.17  E-value: 3.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4552 KTQVEQNKSFEAELKQNVNKVQELKDK-LTELLEEnpdtpeaprwKQMLTEIDSKWQELNQLTIDRQQKLEESSNNLTQF 4630
Cdd:TIGR04523  116 KEQKNKLEVELNKLEKQKKENKKNIDKfLTEIKKK----------EKELEKLNNKYNDLKKQKEELENELNLLEKEKLNI 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4631 QTVEAQLKQWLVEKELMVSVLGPLSIDPNMLNTQ----RQQVQILLQEFATRKPQYEQLTAagqgILSRpgedpslrgiV 4706
Cdd:TIGR04523  186 QKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQiselKKQNNQLKDNIEKKQQEINEKTT----EISN----------T 251
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4707 KEQLAAVTQKWDSLTGQLSDRCDWIDQAIVKSTQYQSLLRSLSDKLSDLDNKLSSSLAVSTHPDAMNQ--QLETAQ---- 4780
Cdd:TIGR04523  252 QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQekKLEEIQnqis 331
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4781 -------KMKQEIQQEKKQIKVAQALCEDLSALVKEEYLKAE-LSRQLEGILKSFKDVEQKAENHVQHLQSACASSHQFQ 4852
Cdd:TIGR04523  332 qnnkiisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEkLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4853 QMSRDFQAWLDTKKEEQNKshpisakldvLESLIKDHKDFSKTLTAQSHMYEKTIAEGENLLlKTQGSEKAALQLQLNTI 4932
Cdd:TIGR04523  412 EQIKKLQQEKELLEKEIER----------LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR-ESLETQLKVLSRSINKI 480
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4933 KTNWDTFNKQVKERENKLKESLEKALKYKEQVETLWPWIDKCQNNLEEIKfcLDPAEGENSIAKLKSLQKEMDQhfgmve 5012
Cdd:TIGR04523  481 KQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE--SEKKEKESKISDLEDELNKDDF------ 552
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5013 llNNTANSL-LSVCEIDKEVVT--DENKSLIQKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRQLQCAKEQldiHD 5089
Cdd:TIGR04523  553 --ELKKENLeKEIDEKNKEIEElkQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE---NE 627
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1761000869 5090 SLGSQAysNKYLTMLQTQQKSLQALKHQVDLAKRLAQDLVVEASDSKGTSD 5140
Cdd:TIGR04523  628 KLSSII--KNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKID 676
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
5281-5389 3.45e-05

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: 46.16  E-value: 3.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5281 KRLEEFYSKLKEFSILLQKAEEHEESQGPVGMETEtINQQLNMFKVFQKEeIEPLQGKQQDVNWLGQGLIQSAAKSTSTq 5360
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGKDLES-VQALLKKHKALEAE-LAAHQDRVEALNELAEKLIDEGHYASEE- 77
                           90       100
                   ....*....|....*....|....*....
gi 1761000869 5361 gLEHDLDDVNARWKTLNKKVAQRAAQLQE 5389
Cdd:pfam00435   78 -IQERLEELNERWEQLLELAAERKQKLEE 105
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
701-795 3.95e-05

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: 46.16  E-value: 3.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  701 LHNFVSRATNELIWLNEKEE----EEVAYDWSErntnIARKKDYHAELMRELDQKEENIKSVQEIAEQLLLENHPARLTI 776
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEAllssEDYGKDLES----VQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90
                   ....*....|....*....
gi 1761000869  777 EAYRAAMQTQWSWILQLCQ 795
Cdd:pfam00435   79 QERLEELNERWEQLLELAA 97
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6490-6592 4.36e-05

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: 46.16  E-value: 4.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6490 EFHNSLQDFINWLTQAEQTLNVASRPSLiLDTVLFQIDEHKVFANEVNSHREQIIELDKTGTHLKYfSQKQDVVLIKNLL 6569
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSEDYGKD-LESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASEEIQERL 82
                           90       100
                   ....*....|....*....|...
gi 1761000869 6570 ISVQSRWEKVVQRLVERGRSLDD 6592
Cdd:pfam00435   83 EELNERWEQLLELAAERKQKLEE 105
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
1033-1269 4.54e-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: 50.49  E-value: 4.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 1033 DITQLEKEVNVCK---QYYQELLKSAEREEQEESVYNLYIS----------------------EVRNIRLRLENC---ED 1084
Cdd:pfam05483  451 EIHDLEIQLTAIKtseEHYLKEVEDLKTELEKEKLKNIELTahcdklllenkeltqeasdmtlELKKHQEDIINCkkqEE 530
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 1085 RLIRQIRTPLERddlhESVFRiTEQEKLKKELERLKDDLGTITNKCEE-FFSQAAASSSVPTLRSELNVVLQNMNQVYSM 1163
Cdd:pfam05483  531 RMLKQIENLEEK----EMNLR-DELESVREEFIQKGDEVKCKLDKSEEnARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 1164 SSTYIDKLKTVNLVLKNTQAAEA-LVKLYETKLCEEEAVIAD-KNNIENLISTlkqWRSEVDEKRQVFHALEDELQKAKA 1241
Cdd:pfam05483  606 KNKNIEELHQENKALKKKGSAENkQLNAYEIKVNKLELELASaKQKFEEIIDN---YQKEIEDKKISEEKLLEEVEKAKA 682
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1761000869 1242 ISDEMFKTYKERDLD-----------FDWHKEKADQLVE 1269
Cdd:pfam05483  683 IADEAVKLQKEIDKRcqhkiaemvalMEKHKHQYDKIIE 721
CH_AtFIM_like_rpt1 cd21293
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
37-134 5.29e-05

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


Pssm-ID: 409142  Cd Length: 116  Bit Score: 45.98  E-value: 5.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   37 QKKTFTKWINQHL---------MKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMR-----FHRLQNVQIALDY 102
Cdd:cd21293      2 EKGSYVDHINRYLgddpflkqfLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1761000869  103 LKRRQVKLVNIRNDDITDGNPKLTLGLIWTII 134
Cdd:cd21293     82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
SPEC smart00150
Spectrin repeats;
5940-6044 5.73e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.40  E-value: 5.73e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  5940 QFHDKIDQILESLERiVERLRQPPSISAEVEKIKEQISENKNVSVDMEKLQPLYETLKQRGEEMIARSGGtdkdiSAKAV 6019
Cdd:smart00150    2 QFLRDADELEAWLEE-KEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-----DAEEI 75
                            90       100
                    ....*....|....*....|....*
gi 1761000869  6020 QDKLDQMVFIWENIHTLVEEREAKL 6044
Cdd:smart00150   76 EERLEELNERWEELKELAEERRQKL 100
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
20-144 7.11e-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: 7.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   20 QAYEDVLERYKDErdkvQKKTFTKWINQ---------HLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPR----EKG 86
Cdd:cd21324     12 QSSAGTQHSYSEE----EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKK 87
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1761000869   87 RMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHV 144
Cdd:cd21324     88 LTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
32-140 8.32e-05

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


Pssm-ID: 409179  Cd Length: 125  Bit Score: 45.75  E-value: 8.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   32 ERDKVQKKTFTKWINQhlMKVRKHVNDLYEDLRDGHNLISLLEVL---------SGDTLPREKGRMRfhRLQNVQIALDY 102
Cdd:cd21330      9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1761000869  103 LKRR-QVKLVNIRNDDITDGNPKLTLGLIWTIILHFQIS 140
Cdd:cd21330     85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6162-6264 8.95e-05

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: 45.00  E-value: 8.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6162 QYQDGLQAVFDWVDIAGGKLASMsPIGTDLETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTEESDKhtVQDP 6241
Cdd:pfam00435    5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--IQER 81
                           90       100
                   ....*....|....*....|...
gi 1761000869 6242 LMELKLIWDSLEERIINRQHKLE 6264
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLE 104
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
5230-5871 9.24e-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: 49.72  E-value: 9.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5230 NANKTCKMMLATEETSPDLVGIKRDLEALSKQCNKLldRAQAREEQVE---------GTIKRLEEFY-----SKLKEFSI 5295
Cdd:pfam05483  167 SAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL--RVQAENARLEmhfklkedhEKIQHLEEEYkkeinDKEKQVSL 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5296 LLQKAEEHEESQGPVGMETETINQQLNMFK---VFQKEEIEPLQGKQQDVNWLGQGLIQSAAKSTSTQ-GLEHDLDDVNa 5371
Cdd:pfam05483  245 LLIQITEKENKMKDLTFLLEESRDKANQLEektKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQkALEEDLQIAT- 323
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5372 rwKTLNKKVAQRAAQLQEAllhcgrfqDALESLLSWMVdteelvanqkppsAEFKVVKAQIQEQ-KLLQRLLDDRKSTVE 5450
Cdd:pfam05483  324 --KTICQLTEEKEAQMEEL--------NKAKAAHSFVV-------------TEFEATTCSLEELlRTEQQRLEKNEDQLK 380
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5451 VIKREGEKIATTAEPADKVKILKQLSLldSRWEALLNKAET---RNRQLEGIsvvAQQFHETLEPLNEWLTTIEKRLVNC 5527
Cdd:pfam05483  381 IITMELQKKSSELEEMTKFKNNKEVEL--EELKKILAEDEKlldEKKQFEKI---AEELKGKEQELIFLLQAREKEIHDL 455
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5528 EpIGTQASKLEEQIAQHKVLQEDILLRKQ---------NVDQALLNGLELLkQTTGDEVLIIQDKLEAIKARYKDITKLS 5598
Cdd:pfam05483  456 E-IQLTAIKTSEEHYLKEVEDLKTELEKEklknieltaHCDKLLLENKELT-QEASDMTLELKKHQEDIINCKKQEERML 533
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5599 TDVAKTLEQALQLARRLHSTHEEL--------CTwLDKVEVELLSYETQVLKGEEASQA-QMRPKELKKEAKNNKALLDS 5669
Cdd:pfam05483  534 KQIENLEEKEMNLRDELESVREEFiqkgdevkCK-LDKSEENARSIEYEVLKKEKQMKIlENKCNNLKKQIENKNKNIEE 612
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5670 LNEVSSAllelvpwraregLEKMVAEDNERYRLVSDTITQKVEEIDAAilrSQQFDQaadaelswITETEKKlmSLGDIR 5749
Cdd:pfam05483  613 LHQENKA------------LKKKGSAENKQLNAYEIKVNKLELELASA---KQKFEE--------IIDNYQK--EIEDKK 667
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5750 LEQDQTSAQLQVQKTFTMEILRHKDIIDdlVKSGHKIMTACSEEEKQsmKKKLDKVLKNYDTICQInserYLQLERAQSL 5829
Cdd:pfam05483  668 ISEEKLLEEVEKAKAIADEAVKLQKEID--KRCQHKIAEMVALMEKH--KHQYDKIIEERDSELGL----YKNKEQEQSS 739
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1761000869 5830 VNQFWETyeELWPWLTETQSIISQLPAPALEYETLRQQQEEH 5871
Cdd:pfam05483  740 AKAALEI--ELSNIKAELLSLKKQLEIEKEEKEKLKMEAKEN 779
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
38-96 1.08e-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: 44.96  E-value: 1.08e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1761000869   38 KKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREK----GRMRFHRLQNV 96
Cdd:cd21221      3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVV 65
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
4497-5169 1.36e-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: 49.28  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4497 LGLLLKDKIAELNTKLSKLQKAQEessammqwLQKMNKTATKWQQTPAPTDTEAVKTQVEQNKSFEAELKQNVNKVQE-- 4574
Cdd:TIGR01612  601 LKLELKEKIKNISDKNEYIKKAID--------LKKIIENNNAYIDELAKISPYQVPEHLKNKDKIYSTIKSELSKIYEdd 672
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4575 ---LKDKLTELLEENP--DTPEAPRWKQMLTEIDSKWQELNQLtidrqqKLEESSNNLTQFQTVEAQLKQWLVEkeLMVS 4649
Cdd:TIGR01612  673 idaLYNELSSIVKENAidNTEDKAKLDDLKSKIDKEYDKIQNM------ETATVELHLSNIENKKNELLDIIVE--IKKH 744
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4650 VLGPLSIDPNML----NTQRQQVQILLQEFATRKPQYEQLTAAGQGILSRPGEDPSLRGIVKEQLAAVTQKWDSLTGQLS 4725
Cdd:TIGR01612  745 IHGEINKDLNKIledfKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTIS 824
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4726 DRCDWIDQAIVKSTQYQSLLRSLSDKLSDLDNKLSSSLAvSTHpdamNQQLETAQKMKQEIQQEK-----KQIKVAQALC 4800
Cdd:TIGR01612  825 IKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKID-SEH----EQFAELTNKIKAEISDDKlndyeKKFNDSKSLI 899
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4801 EDLSALVKEEYLKAELSRQLEGILKSFKDVEQKAENHV-----------QHLQSACASSHQFQQMSRDFQAWLDTKKEEQ 4869
Cdd:TIGR01612  900 NEINKSIEEEYQNINTLKKVDEYIKICENTKESIEKFHnkqnilkeilnKNIDTIKESNLIEKSYKDKFDNTLIDKINEL 979
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4870 NKSHPiSAKLDVLES----LIKDHKDFSKTL-TAQSHMYEKTIAEGE----NLLLKTQGSEKAALQLQL----------- 4929
Cdd:TIGR01612  980 DKAFK-DASLNDYEAknneLIKYFNDLKANLgKNKENMLYHQFDEKEkatnDIEQKIEDANKNIPNIEIaihtsiyniid 1058
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4930 ---NTIKTNWDTFNKQVKERE-------NKLKESL----------EKALKY-------KEQVETLWPWIDKCQNNLEEIK 4982
Cdd:TIGR01612 1059 eieKEIGKNIELLNKEILEEAeinitnfNEIKEKLkhynfddfgkEENIKYadeinkiKDDIKNLDQKIDHHIKALEEIK 1138
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4983 fcldpAEGENSIAKLKSlqkemdqhfgmvellnnTANSLLSVCeiDKEVVTDENKSLIQKVDMVTEQLHSKKFCLENMTQ 5062
Cdd:TIGR01612 1139 -----KKSENYIDEIKA-----------------QINDLEDVA--DKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKK 1194
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5063 KFKEFQEVSKEsKRQLQCAKeqlDIHDSLGsQAYSNKYLTMLQTQQ-------KSLQALKHQVDLAKRLAQDLVVEAS-- 5133
Cdd:TIGR01612 1195 LLNEIAEIEKD-KTSLEEVK---GINLSYG-KNLGKLFLEKIDEEKkksehmiKAMEAYIEDLDEIKEKSPEIENEMGie 1269
                          730       740       750
                   ....*....|....*....|....*....|....*..
gi 1761000869 5134 -DSKGTSDVLLQVETIAQEHSTLSQQVDEKCSFLETK 5169
Cdd:TIGR01612 1270 mDIKAEMETFNISHDDDKDHHIISKKHDENISDIREK 1306
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
150-252 1.59e-04

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: 44.60  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  150 DMSAKERLLLWTQQ--ATEGYAGIRCENFTTCWRDGKLFNAIIHKYRPDLID----MNTVAVQSNLANLEHAFYVAEKIG 223
Cdd:cd21218      8 YLPPEEILLRWVNYhlKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelvLEVLSEEDLEKRAEKVLQAAEKLG 87
                           90       100
                   ....*....|....*....|....*....
gi 1761000869  224 VIRLLDPEdvDVSSPDEKSVITYVSSLYD 252
Cdd:cd21218     88 CKYFLTPE--DIVSGNPRLNLAFVATLFN 114
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
34-133 2.55e-04

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


Pssm-ID: 409134  Cd Length: 121  Bit Score: 44.18  E-value: 2.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   34 DKVQKKTFTKWINQHLMKV--RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKG--RMRFHRLQNVQIALDYLKRRQVK 109
Cdd:cd21285      8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
                           90       100
                   ....*....|....*....|....
gi 1761000869  110 LVNIRNDDITDGNPKLTLGLIWTI 133
Cdd:cd21285     88 IQGLSAEEIRNGNLKAILGLFFSL 111
SPEC smart00150
Spectrin repeats;
5284-5388 3.03e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 43.47  E-value: 3.03e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  5284 EEFYSKLKEFSILLQKAEEHEESQgPVGMETETINQQLNMFKVFQKEeIEPLQGKQQDVNWLGQGLIQSAAKSTSTqgLE 5363
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAE-LEAHEERVEALNELGEQLIEEGHPDAEE--IE 76
                            90       100
                    ....*....|....*....|....*
gi 1761000869  5364 HDLDDVNARWKTLNKKVAQRAAQLQ 5388
Cdd:smart00150   77 ERLEELNERWEELKELAEERRQKLE 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1194-1358 3.20e-04

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 45.90  E-value: 3.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 1194 KLCEEEAVIADKNNIENLISTLKQWRSEVDEKRQVFHALEdelQKAKAISDEmfktykeRDLDFDWHKEKADQLVERWQN 1273
Cdd:cd00176     21 ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALN---ELGEQLIEE-------GHPDAEEIQERLEELNQRWEE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 1274 VHVQIDNRLRDLEGIGKSLKYYRDTYHpLDDWIQqvETTQRKIQENQPENSKTLATQLNQQKMLVSEIEMKQSKMDECQK 1353
Cdd:cd00176     91 LRELAEERRQRLEEALDLQQFFRDADD-LEQWLE--EKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNE 167

                   ....*
gi 1761000869 1354 YAEQY 1358
Cdd:cd00176    168 LAEEL 172
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3611-4365 4.10e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.76  E-value: 4.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3611 VQESVTTQVERLETQ-LHLEQDLDDQKIVAERqqEYKEKLQGICDLLTQ---TENRLIGHQEafmigdgtvELKKYQSKQ 3686
Cdd:TIGR02169  192 IIDEKRQQLERLRRErEKAERYQALLKEKREY--EGYELLKEKEALERQkeaIERQLASLEE---------ELEKLTEEI 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3687 EELQKDMQGSAQALAEVVK-------NTENFLKENGEKLSQEdKALIEQKLNEAKIKCEQLNLKAEQSKKELDKV----- 3754
Cdd:TIGR02169  261 SELEKRLEEIEQLLEELNKkikdlgeEEQLRVKEKIGELEAE-IASLERSIAEKERELEDAEERLAKLEAEIDKLlaeie 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3755 -VTTAIKEETEKVAAVK-QLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIEQngthfqegdgKSAIGEE-DEVNGNLl 3831
Cdd:TIGR02169  340 eLEREIEEERKRRDKLTeEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK----------LEKLKREiNELKREL- 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3832 etdvdGQVGTTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQgqylspeeKEKLQKNMKELKvhyetalaes 3911
Cdd:TIGR02169  409 -----DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ--------EWKLEQLAADLS---------- 465
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3912 ekkmklthSLQEELEKFDADYTEFEHWLQQSEQELENLEAGADDINglmtklKRQKSFS--EDVISHKGDLRYITISG-N 3988
Cdd:TIGR02169  466 --------KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE------ERVRGGRavEEVLKASIQGVHGTVAQlG 531
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3989 RVLEA-AKSCSKRDGGK-----VDTSATHREV-----QRKLDHAT----------DRFRSLYSKCNVLGNNLkDLVDKYQ 4047
Cdd:TIGR02169  532 SVGERyATAIEVAAGNRlnnvvVEDDAVAKEAiellkRRKAGRATflplnkmrdeRRDLSILSEDGVIGFAV-DLVEFDP 610
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4048 HYEDA------SCGLLAGLQACE-------------------------ATASKHLSEPIAVDPKNLQRQLEETKALQGQI 4096
Cdd:TIGR02169  611 KYEPAfkyvfgDTLVVEDIEAARrlmgkyrmvtlegelfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKREL 690
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4097 SSQQVAVEKLKKTAEVLLDARgsllpakNDIQKTLDDIVGRYEDLSKSVNERNEKLQITLTRSLSVQDGLDEMLDWMGNV 4176
Cdd:TIGR02169  691 SSLQSELRRIENRLDELSQEL-------SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4177 ESSLKEQgQVPLNstALQDIISKnimLEQDIAGRQ-SSINAMNEKVKKFMETTDpSTASSLQAKMKDLSARFSEASHKHK 4255
Cdd:TIGR02169  764 EARIEEL-EEDLH--KLEEALND---LEARLSHSRiPEIQAELSKLEEEVSRIE-ARLREIEQKLNRLTLEKEYLEKEIQ 836
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4256 ETLAKMEELKTKVELFENLSEKLQTFLETKTQALTEVDvpgKDVTELSQYMQESTSEFLEHKKHLEVLHSLLKEISS--H 4333
Cdd:TIGR02169  837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE---AALRDLESRLGDLKKERDELEAQLRELERKIEELEAqiE 913
                          810       820       830
                   ....*....|....*....|....*....|..
gi 1761000869 4334 GLPSDKALVLEKTNNLSKKFKEMEDTIKEKKE 4365
Cdd:TIGR02169  914 KKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3886-4434 4.49e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 4.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3886 SPEEKEKLQKNMKELKvHYETALAESEKKMKLTHSLQEELEKFDADYTEFEHWLQQSEQELENLEagaDDINGLMTKLKR 3965
Cdd:PRK03918   143 SDESREKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVL---REINEISSELPE 218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3966 QKSFSEDVISHKGDLRYITisgNRVLEAAKSCSKRDGGKVDTSATHREVQRKLDHATDRFRSLYSKCNVLgNNLKDLVDK 4045
Cdd:PRK03918   219 LREELEKLEKEVKELEELK---EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEE 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4046 YQHYEDASCGLLAGLQACEATASKhLSEPIavdpKNLQRQLEE-------TKALQGQISSQQVAVEKLKKTAEVLLDARg 4118
Cdd:PRK03918   295 YIKLSEFYEEYLDELREIEKRLSR-LEEEI----NGIEERIKEleekeerLEELKKKLKELEKRLEELEERHELYEEAK- 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4119 SLLPAKNDIQKTLDDivgryedlsKSVNERNEKLQITLTRSLSVQDGLDEMLDWMGNVESSLKE-----------QGQVP 4187
Cdd:PRK03918   369 AKKEELERLKKRLTG---------LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElkkaieelkkaKGKCP 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4188 LNSTALQDIISKNIMLE-----QDIAGRQSSINAMNEKVKK-FMETTDPSTASSLQAKMKDLSARFSEASHKHKETlaKM 4261
Cdd:PRK03918   440 VCGRELTEEHRKELLEEytaelKRIEKELKEIEEKERKLRKeLRELEKVLKKESELIKLKELAEQLKELEEKLKKY--NL 517
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4262 EELKTKVELFENLSEKLQTfLETKTQALTevdvpgKDVTELSQYmqESTSEFLEHKKHL--EVLHSLLKEISSHGLPSDK 4339
Cdd:PRK03918   518 EELEKKAEEYEKLKEKLIK-LKGEIKSLK------KELEKLEEL--KKKLAELEKKLDEleEELAELLKELEELGFESVE 588
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4340 AL-----VLEKTNNLSKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSLKSWIKETTKKVPIVQPSFGAEDLGKSLEDT 4414
Cdd:PRK03918   589 ELeerlkELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEY 668
                          570       580
                   ....*....|....*....|
gi 1761000869 4415 KKLQEKWSLKTPEIQKVNNS 4434
Cdd:PRK03918   669 LELSRELAGLRAELEELEKR 688
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
4625-4733 5.68e-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: 42.69  E-value: 5.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4625 NNLTQFQTVEAQLKQWLVEKELMVSVlGPLSIDPNMLNTQRQQVQILLQEFATRKPQYEQLTAAGQGILSRPGEDPSLrg 4704
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE-- 77
                           90       100
                   ....*....|....*....|....*....
gi 1761000869 4705 iVKEQLAAVTQKWDSLTGQLSDRCDWIDQ 4733
Cdd:pfam00435   78 -IQERLEELNERWEQLLELAAERKQKLEE 105
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
7093-7165 5.88e-04

EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins; ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination.


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 44.17  E-value: 5.88e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1761000869 7093 VMDFFRRIDKDQDGKIT----RQEFIDGILSSKFP-TSRLEMSavadIFDRDGDGYIDYYEFvAALhpnkdaYKPITD 7165
Cdd:cd16183      2 LWNVFQRVDKDRSGQISatelQQALSNGTWTPFNPeTVRLMIG----MFDRDNSGTINFQEF-AAL------WKYITD 68
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
7096-7154 7.92e-04

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 43.74  E-value: 7.92e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1761000869 7096 FFRRIDKDQDGKITRQEfIDGILSSkfptSRLEMS-AVAD----IFDRDGDGYIDYYEFvAALH 7154
Cdd:cd16185      5 WFRAVDRDRSGSIDVNE-LQKALAG----GGLLFSlATAEklirMFDRDGNGTIDFEEF-AALH 62
SPEC smart00150
Spectrin repeats;
4629-4727 8.01e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 42.32  E-value: 8.01e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  4629 QFQTVEAQLKQWLVEKELMVSVLgPLSIDPNMLNTQRQQVQILLQEFATRKPQYEQLTAAGQGILSRPGEDPSlrgIVKE 4708
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAE---EIEE 77
                            90
                    ....*....|....*....
gi 1761000869  4709 QLAAVTQKWDSLTGQLSDR 4727
Cdd:smart00150   78 RLEELNERWEELKELAEER 96
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
34-134 8.09e-04

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: 42.82  E-value: 8.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   34 DKVQKKTFTKWINQ---------HLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTL-------PREKGRM--RFHRLQN 95
Cdd:cd21294      4 NEDERREFTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIdervlnkPPRKNKPlnNFQMIEN 83
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1761000869   96 VQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTII 134
Cdd:cd21294     84 NNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3381-4152 1.06e-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: 46.20  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3381 DSSTEQFSSELQQCLQHTEKMHEY---LTLLQDMKPPLDNQ-ESLDNNLEALKNQLRQLETFELGLAPIAVILRKDMKLA 3456
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELeekLEELRLEVSELEEEiEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3457 EEFLKSLPSdfprgHVEELSISHQSLKTAFSSLsnvssertKQIMLAIDSEMSKLAVSHEEFLHKLKSFSDWVSEKSKSV 3536
Cdd:TIGR02168  322 EAQLEELES-----KLDELAEELAELEEKLEEL--------KEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3537 KDIEivnvQDSEYVKKRLEFLKNVLKDLGHTKMQLETTafdvqffISEYAQDLSPNQSKQLLRLLNTTQKcfldVQESVT 3616
Cdd:TIGR02168  389 AQLE----LQIASLNNEIERLEARLERLEDRRERLQQE-------IEELLKKLEEAELKELQAELEELEE----ELEELQ 453
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3617 TQVERLETQLHLEQDLDDQKIVAERQQEYKEK-LQGICDLLTQTENRLIG----------HQEAFMIGDGTV-ELKKYQS 3684
Cdd:TIGR02168  454 EELERLEEALEELREELEEAEQALDAAERELAqLQARLDSLERLQENLEGfsegvkallkNQSGLSGILGVLsELISVDE 533
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3685 KQE-ELQKDMQGSAQALaeVVKNTE------NFLKENgeklsqedkalieqklneAKIKCEQLNLKAeQSKKELDKVVTT 3757
Cdd:TIGR02168  534 GYEaAIEAALGGRLQAV--VVENLNaakkaiAFLKQN------------------ELGRVTFLPLDS-IKGTEIQGNDRE 592
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3758 AIKEETEKVAAVKQLEESKTKIENLLD-WLSNVD-KDSERAGTKHKQVIEQNGTHF-QEGD----GKSAIGEEDEVNGNL 3830
Cdd:TIGR02168  593 ILKNIEGFLGVAKDLVKFDPKLRKALSyLLGGVLvVDDLDNALELAKKLRPGYRIVtLDGDlvrpGGVITGGSAKTNSSI 672
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3831 LETDVdgqvgttqeNLNQQYQKVKAQHEKIISQHQAVIiATQSAQVLLEKQGQYLSPEEKEKLQKnMKELKVHYETALAE 3910
Cdd:TIGR02168  673 LERRR---------EIEELEEKIEELEEKIAELEKALA-ELRKELEELEEELEQLRKELEELSRQ-ISALRKDLARLEAE 741
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3911 SEKKMKLTHSLQEELEKFDA-------DYTEFEHWLQQSEQELENLEAGADDINGLMTKLKRQ-KSFSEDVISHKGDLRY 3982
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAeieeleeRLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAlDELRAELTLLNEEAAN 821
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3983 ITISGNRVLEAAKSCSKRdggKVDTSATHREVQRKLDHATDRFRSLYSKCNVLGNNLKDLVDKYQHYEDASCGLLAGLQA 4062
Cdd:TIGR02168  822 LRERLESLERRIAATERR---LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4063 ceataskhLSEPIAVDPKNLQRQLEETKALQGQISSQQVAVEKLKKTAEVLLDArgsllpAKNDIQKTLDDIVGRYEDLS 4142
Cdd:TIGR02168  899 --------LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER------LSEEYSLTLEEAEALENKIE 964
                          810
                   ....*....|
gi 1761000869 4143 KSVNERNEKL 4152
Cdd:TIGR02168  965 DDEEEARRRL 974
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
5076-5659 1.08e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5076 RQLQCAKEQLDIhdslgsQAYSNKYltmlQTQQKSLQALKHQVDLAKRLAQDLVVEASDSKGtsdvllQVETIAQEHSTL 5155
Cdd:COG1196    216 RELKEELKELEA------ELLLLKL----RELEAELEELEAELEELEAELEELEAELAELEA------ELEELRLELEEL 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5156 SQQVDEKCSFLETKLQGIGHFQNTIREMFSQFAEFDDELDSMApvgRDAETLQKQKETIKAFLKKLEALMASNDNANKTC 5235
Cdd:COG1196    280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE---EELAELEEELEELEEELEELEEELEEAEEELEEA 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5236 KMMLAT-EETSPDLVGIKRDLEALSKQCNKLLDRAQAREEQVEGTIKRLEEFYSKLKEFSILLQKAEEHEESQgpvgmET 5314
Cdd:COG1196    357 EAELAEaEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA-----LA 431
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5315 ETINQQLNMFKVFQKEEIEPLQGKQQDVnwlgQGLIQSAAKSTSTQGLEHDLDDVNArwkTLNKKVAQRAAQLQEALLHC 5394
Cdd:COG1196    432 ELEEEEEEEEEALEEAAEEEAELEEEEE----ALLELLAELLEEAALLEAALAELLE---ELAEAAARLLLLLEAEADYE 504
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5395 GRFQDALESLL--SWMVDTEELVANQKPPSAEFKVVKAQIQEQkLLQRLLDDRKSTVEVIKREGEKIAT--TAEPADKVK 5470
Cdd:COG1196    505 GFLEGVKAALLlaGLRGLAGAVAVLIGVEAAYEAALEAALAAA-LQNIVVEDDEVAAAAIEYLKAAKAGraTFLPLDKIR 583
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5471 ILKQLSLLDSRW---------EALLNKAETRNRQLEGISVVAQQFHETLEPLNEWLTTIEKRLVNCEPIGTQASKLEEQI 5541
Cdd:COG1196    584 ARAALAAALARGaigaavdlvASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5542 AQHKVLQEDILLRKQNVDQALLNGLELLKQTTGDEVLIIQDKLEAIKARYKDITKLSTDVAKTLEQALQLARRLHSTHEE 5621
Cdd:COG1196    664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 1761000869 5622 LctwlDKVEVELLSYETQVLKGEEASQAQMRpkELKKE 5659
Cdd:COG1196    744 E----EELLEEEALEELPEPPDLEELERELE--RLERE 775
EF-hand_8 pfam13833
EF-hand domain pair;
7104-7153 1.13e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 40.38  E-value: 1.13e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1761000869 7104 QDGKITRQEFIDGI-LSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAAL 7153
Cdd:pfam13833    1 EKGVITREELKRALaLLGLKDLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
147-256 1.14e-03

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: 42.49  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  147 ESEDMSAKERLLLWTQQAtegYAGIRCENFTTCWRDGKLFNAIIHKYRPDLI-DMNTVAVQSNLANLEHAFYVAEK-IGV 224
Cdd:cd21312      7 EAKKQTPKQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDwLGI 83
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1761000869  225 IRLLDPEDVDVSSPDEKSVITYVSSlydaFPK 256
Cdd:cd21312     84 PQVITPEEIVDPNVDEHSVMTYLSQ----FPK 111
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
43-133 1.16e-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: 42.29  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   43 KWINQHLMKV---RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRM------RFHRLQNVQIALDYLKRRQVklvnI 113
Cdd:cd21218     17 RWVNYHLKKAgptKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlseedLEKRAEKVLQAAEKLGCKYF----L 92
                           90       100
                   ....*....|....*....|
gi 1761000869  114 RNDDITDGNPKLTLGLIWTI 133
Cdd:cd21218     93 TPEDIVSGNPRLNLAFVATL 112
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
7097-7154 1.20e-03

EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand calcium-binding protein RLP49, is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal His-Asp-Glu-Leu (HDEL) tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320028 [Multi-domain]  Cd Length: 268  Bit Score: 44.96  E-value: 1.20e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1761000869 7097 FRRIDKDQDGKITRQEFIDGILSSKFPTSR-LEMSAVADIFDRDGDGYIDYYEFVAALH 7154
Cdd:cd16230    129 FRVADQDGDSMATREELTAFLHPEEFPHMRdIVVAETLEDLDKNKDGYVQVEEYIADLY 187
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4501-5305 1.24e-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: 45.82  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4501 LKDKIAELNTKLSKLQKAQEESSAMMQWLqKMNKTATKWQQTPAPTDTEAVKTQVEQNKSFEAELKQNVNKVQELKDKLT 4580
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISRL-EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4581 ELLEEnpdtpeaprWKQMLTEIDSKWQELNQLTIDRQQKLEESSNNLTQfqtVEAQLKQwlvekelmvsvlgplsidpnm 4660
Cdd:TIGR02168  351 EELES---------LEAELEELEAELEELESRLEELEEQLETLRSKVAQ---LELQIAS--------------------- 397
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4661 LNTQRQQVQILLQEFATRKpqyEQLTAAGQGILSRPgeDPSLRGIVKEQLAAVTQKWDSLTGQLSDRCDWIDQAIVKSTQ 4740
Cdd:TIGR02168  398 LNNEIERLEARLERLEDRR---ERLQQEIEELLKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4741 YQSLLRSLSDKLSDLDNKLSSSlavsthpDAMNQQLETAQKMKQEIQQEKKQIKVAQALcedLSALVK-EEYLKAELSRQ 4819
Cdd:TIGR02168  473 AEQALDAAERELAQLQARLDSL-------ERLQENLEGFSEGVKALLKNQSGLSGILGV---LSELISvDEGYEAAIEAA 542
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4820 LEGILKSF-KDVEQKAENHVQHLQSACASSHQFQQMSRDFQAWLDTKKEEQNKSHPisAKLDVLESLIKDHKDFSKTLT- 4897
Cdd:TIGR02168  543 LGGRLQAVvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIE--GFLGVAKDLVKFDPKLRKALSy 620
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4898 --AQSHMYEkTIAEGENLLLKTQGSEKAAlQLQLNTIKTNWdTFNKQVKERENKLkesLEKALKykeqvetlwpwIDKCQ 4975
Cdd:TIGR02168  621 llGGVLVVD-DLDNALELAKKLRPGYRIV-TLDGDLVRPGG-VITGGSAKTNSSI---LERRRE-----------IEELE 683
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4976 NNLEEIKfcLDPAEGENSIAKLKSLQKEMDQHFGMVELLNNTANSLLSVCEIDKEVVTDENKSLIQKVDMVTEQLHSKKF 5055
Cdd:TIGR02168  684 EKIEELE--EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5056 CLENMTQKFKEFQEVSKESKRQLQCAKEQLdihdslgsqaysNKYLTMLQTQQKSLQALKHQVDLAKRLAQDLVVEASDS 5135
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQI------------EQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5136 -KGTSDVLLQVETIAQEHSTLSQQVdekcsfleTKLQG-IGHFQNTIREMFSQFAEFDDELDSmapvgrdaetlqkQKET 5213
Cdd:TIGR02168  830 eRRIAATERRLEDLEEQIEELSEDI--------ESLAAeIEELEELIEELESELEALLNERAS-------------LEEA 888
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5214 IKAFLKKLEALMASNDNANKTckmmlateetspdlvgiKRDLEALSKQCNKLLDRAQAREEQVEGTIKRLEEFYSklKEF 5293
Cdd:TIGR02168  889 LALLRSELEELSEELRELESK-----------------RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS--EEY 949
                          810
                   ....*....|..
gi 1761000869 5294 SILLQKAEEHEE 5305
Cdd:TIGR02168  950 SLTLEEAEALEN 961
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
4607-4835 1.74e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4607 QELNQLtidrQQKLEESSNNLTQFQT------VEAQLKQwlVEKELmvsvlgplsidpNMLNTQRQQVQILLQEFATRKP 4680
Cdd:COG3206    182 EQLPEL----RKELEEAEAALEEFRQknglvdLSEEAKL--LLQQL------------SELESQLAEARAELAEAEARLA 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4681 QYEQLTAAGQGILSRPGEDPSLRGIvKEQLAAVTQKWDSLTGQLSDrcdwidqaivKSTQYQSLLRSLSDKLSDLDNKLS 4760
Cdd:COG3206    244 ALRAQLGSGPDALPELLQSPVIQQL-RAQLAELEAELAELSARYTP----------NHPDVIALRAQIAALRAQLQQEAQ 312
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1761000869 4761 SSLAvsthpdAMNQQLETAQKMKQEIQQEKKQIKvaqalcEDLSALVKEEYLKAELSRQLEGILKSFKDVEQKAE 4835
Cdd:COG3206    313 RILA------SLEAELEALQAREASLQAQLAQLE------ARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
5423-5723 1.76e-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: 45.44  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5423 AEFKVVKAQIQEqklLQRLLDDRKSTVEVIKREGEKiattAEPADKVKILKQ---LSLLDSRWEALLNKAETRNRQLEGI 5499
Cdd:TIGR02169  177 EELEEVEENIER---LDLIIDEKRQQLERLRREREK----AERYQALLKEKReyeGYELLKEKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5500 SVVAQQFHETLEPLNEWLTTIEKRL--VNCE----------PIGTQASKLEEQIAQHKVLQEDILLRKQNVDQALLNGLE 5567
Cdd:TIGR02169  250 EEELEKLTEEISELEKRLEEIEQLLeeLNKKikdlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5568 LLKQTTGDevliIQDKLEAIKARYKDITKLSTDVAKTLEQALQLARRLHSTHEELCTWLDKV-----EVELLSYE----- 5637
Cdd:TIGR02169  330 EIDKLLAE----IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELkdyreKLEKLKREinelk 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5638 -TQVLKGEEASQAQMRPKELKKEAknnKALLDSLNEVSSALLEL------VPWRAREGLEKMVAEDNERYRL------VS 5704
Cdd:TIGR02169  406 rELDRLQEELQRLSEELADLNAAI---AGIEAKINELEEEKEDKaleikkQEWKLEQLAADLSKYEQELYDLkeeydrVE 482
                          330
                   ....*....|....*....
gi 1761000869 5705 DTITQKVEEIDAAILRSQQ 5723
Cdd:TIGR02169  483 KELSKLQRELAEAEAQARA 501
PLEC smart00250
Plectin repeat;
1552-1583 1.84e-03

Plectin repeat;


Pssm-ID: 197605  Cd Length: 38  Bit Score: 39.39  E-value: 1.84e-03
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1761000869  1552 DKVIAGTIDQTTGEVLSVFQAVLRGLIDYDTG 1583
Cdd:smart00250    7 QSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
7092-7154 1.91e-03

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 42.90  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 7092 RVMDFFRRIDKDQDGKITRQEF-------------IDGI--LSSKFPTSR----------------LEMSAVADIFDRDG 7140
Cdd:cd16180      1 ELRRIFQAVDRDRSGRISAKELqralsngdwtpfsIETVrlMINMFDRDRsgtinfdefvglwkyiQDWRRLFRRFDRDR 80
                           90
                   ....*....|....
gi 1761000869 7141 DGYIDYYEFVAALH 7154
Cdd:cd16180     81 SGSIDFNELQNALS 94
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
5251-5718 2.09e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5251 IKRDLEALSKQCNKLLDRAQAREEQVEGTIKRLEEFYSKLKEFSILLQKAEEHEESqgpvgmETETINQQLNMFKVFQKE 5330
Cdd:COG1196    314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------AEAELAEAEEELEELAEE 387
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5331 EIEPLQgkqqdvnwlgqgliQSAAKSTSTQGLEHDLDDVNARWKTLNKKVAQRAAQLQEALLHCGRFQDALESLLSWMVD 5410
Cdd:COG1196    388 LLEALR--------------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5411 TEELVANQKPPSAEFKVVKAQIQEQKLLQRLLDDRKSTVEVIKREGEkiATTAEPADKVKILKQLSLLDSRWEALL---- 5486
Cdd:COG1196    454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE--ADYEGFLEGVKAALLLAGLRGLAGAVAvlig 531
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5487 -------------------NKAETRNRQLEGISVVAQQFHE--TLEPLN-----EWLTTIEKRLVNCEPIGTQASKLEEQ 5540
Cdd:COG1196    532 veaayeaaleaalaaalqnIVVEDDEVAAAAIEYLKAAKAGraTFLPLDkirarAALAAALARGAIGAAVDLVASDLREA 611
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5541 IAQHKVLQEDILLRkqNVDQALLNGLELLKQTTGDEVLIIQDKLEAIKARYKDITKLSTDVAKTLEQALQLARRLhsthe 5620
Cdd:COG1196    612 DARYYVLGDTLLGR--TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL----- 684
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5621 elctwLDKVEVELLSYETQVLKGEEASQAQMRPKELKKEAKNNKALLDSLNEVSSALLELVPWRAREGLEKMVAEDNERY 5700
Cdd:COG1196    685 -----AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
                          490
                   ....*....|....*...
gi 1761000869 5701 rLVSDTITQKVEEIDAAI 5718
Cdd:COG1196    760 -PDLEELERELERLEREI 776
CH_PARVA_B_rpt2 cd21306
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
24-137 2.13e-03

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


Pssm-ID: 409155  Cd Length: 121  Bit Score: 41.63  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   24 DVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRF----HRLQNVQIA 99
Cdd:cd21306      4 DTLFDHAPDKLNVVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFA 83
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1761000869  100 LDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHF 137
Cdd:cd21306     84 FELMQDAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
6085-6260 2.22e-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: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6085 VKQQQEAAETIREEIDGLQEELDiviNLGSELIAACGEPDKpiVKKSIDELNSAWDSLNKAWKDRIDKLEEamQAAVQYQ 6164
Cdd:COG3883     25 LSELQAELEAAQAELDALQAELE---ELNEEYNELQAELEA--LQAEIDKLQAEIAEAEAEIEERREELGE--RARALYR 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6165 DG-----LQAVFDWVDIAG--GKLASMSPIGTD----LETVKQQIEELKQFKSEAYQQQIEMERLNHQAELLLKKVTE-- 6231
Cdd:COG3883     98 SGgsvsyLDVLLGSESFSDflDRLSALSKIADAdadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAqq 177
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1761000869 6232 ----------ESDKHTVQDPLMELKLIWDSLEERIINRQ 6260
Cdd:COG3883    178 aeqeallaqlSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
7066-7117 2.31e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 39.84  E-value: 2.31e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1761000869 7066 ELRE-FANFDFD----IWRKKYMRWMNH-----KKSRVMDFFRRIDKDQDGKITRQEFIDGI 7117
Cdd:cd00051      1 ELREaFRLFDKDgdgtISADELKAALKSlgeglSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3888-4420 2.40e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3888 EEKEKLQKNMKELKVHYETALAESEKKMKLTHSLQEELEKFDADYTEFEHW---LQQSEQELENLEAGA----------- 3953
Cdd:PRK03918   186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEELEKELESLEGSKrkleekirele 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3954 DDINGLMTKLKRQKSFSEDVISHKGD-LRYITISGNRVlEAAKSCSKRDGGKVDTSATHREVQRKLDHATD---RFRSLY 4029
Cdd:PRK03918   266 ERIEELKKEIEELEEKVKELKELKEKaEEYIKLSEFYE-EYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELK 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4030 SKCNVLGNNLKDLVDKYQHYEDAScGLLAGLQACEATASKHLSEPIAVDPKNLQRQLEETK-----------ALQGQISS 4098
Cdd:PRK03918   345 KKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEeeiskitarigELKKEIKE 423
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4099 QQVAVEKLKKT--------AEVLLDARGSLLPAK----NDIQKTLDDIVGRYEDLSKsvneRNEKLQITLTRSLSVQDgL 4166
Cdd:PRK03918   424 LKKAIEELKKAkgkcpvcgRELTEEHRKELLEEYtaelKRIEKELKEIEEKERKLRK----ELRELEKVLKKESELIK-L 498
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4167 DEMLDWMGNVESSLKEQGQVPL--NSTALQDIISKNIMLEQDIAGRQSSINAMNEkvkkfmettdpstassLQAKMKDLS 4244
Cdd:PRK03918   499 KELAEQLKELEEKLKKYNLEELekKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE----------------LKKKLAELE 562
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4245 ARFSEASHKHKETLAKMEELktKVELFENLSEKLQTFLETKTQALTEVDVPgKDVTELSQYMQESTSEFLEHKKHLEVLH 4324
Cdd:PRK03918   563 KKLDELEEELAELLKELEEL--GFESVEELEERLKELEPFYNEYLELKDAE-KELEREEKELKKLEEELDKAFEELAETE 639
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4325 SLLKEISSHGLPSDKALVLEKTNNLSKKFKEMEDTIKEKKEAVTSCQEQLDAFQVLVKSLKSWIKETTKKVPIVqpsfga 4404
Cdd:PRK03918   640 KRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL------ 713
                          570
                   ....*....|....*.
gi 1761000869 4405 EDLGKSLEDTKKLQEK 4420
Cdd:PRK03918   714 EKLEKALERVEELREK 729
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
3671-3815 2.46e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.82  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3671 MIGDGTVELKKYQSKQEELQKDMQGSAQALAEVVKNTENfLKENGEKLSQEDKALIEQKLNEAKIKCEQlnlKAEQSKKE 3750
Cdd:PRK00409   510 LIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEK-LKEELEEKKEKLQEEEDKLLEEAEKEAQQ---AIKEAKKE 585
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 3751 LDKVVTTAIKEETEKVAAVK--QLEESKTKIenlldwlsnvdKDSERAGTKHKQVIEQNGTHFQEGD 3815
Cdd:PRK00409   586 ADEIIKELRQLQKGGYASVKahELIEARKRL-----------NKANEKKEKKKKKQKEKQEELKVGD 641
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
5838-5933 2.51e-03

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 41.15  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5838 EELWPWLTETQSIISQLPAPAlEYETLRQQQEEHRQLRELIAEHKPHIDKMNKTGPQLLELSPGEGFSIQEKYVAADTLY 5917
Cdd:pfam00435   11 DDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERW 89
                           90
                   ....*....|....*.
gi 1761000869 5918 SQIKEDVKKRAVALDE 5933
Cdd:pfam00435   90 EQLLELAAERKQKLEE 105
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
5360-5594 2.82e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 2.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5360 QGLEHDLDDVNARWKTLnkkvAQRAAQLQEALLHCGRFQDALESLLSWMVDTEELVANQK------PPSAEFKVVKAQIQ 5433
Cdd:COG4913    620 AELEEELAEAEERLEAL----EAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAelerldASSDDLAALEEQLE 695
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5434 E-QKLLQRLLDDRKSTVEVIKREGEKIA----------TTAEPADKVKILKQLSLLDSRWEALLNKAETRNrqlegisvV 5502
Cdd:COG4913    696 ElEAELEELEEELDELKGEIGRLEKELEqaeeeldelqDRLEAAEDLARLELRALLEERFAAALGDAVERE--------L 767
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5503 AQQFHETLEPLNEWLTTIEKRLVNC------------EPIGTQASKLEEQIAQHKVLQEDILLRKQnvDQAllngLELLK 5570
Cdd:COG4913    768 RENLEERIDALRARLNRAEEELERAmrafnrewpaetADLDADLESLPEYLALLDRLEEDGLPEYE--ERF----KELLN 841
                          250       260
                   ....*....|....*....|....*...
gi 1761000869 5571 QTTGDEVLIIQDKLEA----IKARYKDI 5594
Cdd:COG4913    842 ENSIEFVADLLSKLRRaireIKERIDPL 869
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
3234-3899 2.83e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 44.71  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3234 LLNILKQD-QHSQKITGVFELMRELTHMEY-----DLEKRGITSKVLPLQLEN----IFYKLLADgySEKIEHVGDFNQK 3303
Cdd:pfam05483  156 LCNLLKETcARSAEKTKKYEYEREETRQVYmdlnnNIEKMILAFEELRVQAENarleMHFKLKED--HEKIQHLEEEYKK 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3304 ACSTSEmmEEKPHILGDIKSKEGNYYSPNLeTVKEIGLESSTVWASTLPRDEKLKDLcNDFPSHLECTSGSKEMASGDSS 3383
Cdd:pfam05483  234 EINDKE--KQVSLLLIQITEKENKMKDLTF-LLEESRDKANQLEEKTKLQDENLKEL-IEKKDHLTKELEDIKMSLQRSM 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3384 TEQfsSELQQCLQHTEKmheylTLLQDMKPPLDNQESLDNNLEALKNQLRQLETFELGLAPIAVILRKDMKLAEEFLKSL 3463
Cdd:pfam05483  310 STQ--KALEEDLQIATK-----TICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKII 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3464 PSDFPR--GHVEELSISHQSLKTAFSSLSNVSSErtKQIMLAIDSEMSKLAvshEEFLHKLKSFSDWVSEKSKSVKDIEI 3541
Cdd:pfam05483  383 TMELQKksSELEEMTKFKNNKEVELEELKKILAE--DEKLLDEKKQFEKIA---EELKGKEQELIFLLQAREKEIHDLEI 457
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3542 ---VNVQDSEYVKKRLEFLKNVLKDLGHTKMQLETTAFDVQFFISEYAQ---DLSPNQSKQLLRLLNTTQKcfldvQESV 3615
Cdd:pfam05483  458 qltAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQeasDMTLELKKHQEDIINCKKQ-----EERM 532
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3616 TTQVERL-ETQLHLEQDLDDQKivaerqQEYKEKLQGI-CDLLTQTENRLIGHQEAFmigdgtvelkkyqsKQEELQKDM 3693
Cdd:pfam05483  533 LKQIENLeEKEMNLRDELESVR------EEFIQKGDEVkCKLDKSEENARSIEYEVL--------------KKEKQMKIL 592
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3694 QGSAQALAEVVKNTENFLKEngekLSQEDKALIEQ------KLNEAKIKCEQLNLKAEQSKKELDKVVTTAIKEetekva 3767
Cdd:pfam05483  593 ENKCNNLKKQIENKNKNIEE----LHQENKALKKKgsaenkQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE------ 662
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3768 avkqLEESKTKIENLLDWLSNVDKDSERAGTKHKQVIEQNGTHFQEgdgKSAIGEEDEVNGNLLETDVDGQVGTTQeNLN 3847
Cdd:pfam05483  663 ----IEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAE---MVALMEKHKHQYDKIIEERDSELGLYK-NKE 734
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1761000869 3848 QQYQKVKAQHEKIISQHQAVIIATQSaQVLLEKqgqylspEEKEKLQKNMKE 3899
Cdd:pfam05483  735 QEQSSAKAALEIELSNIKAELLSLKK-QLEIEK-------EEKEKLKMEAKE 778
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
5504-5607 3.05e-03

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 40.76  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5504 QQFHETLEPLNEWLTTIEKRLVNcEPIGTQASKLEEQIAQHKVLQEDILLRKQNVDQALLNGLELLkQTTGDEVLIIQDK 5583
Cdd:pfam00435    4 QQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI-DEGHYASEEIQER 81
                           90       100
                   ....*....|....*....|....
gi 1761000869 5584 LEAIKARYKDITKLSTDVAKTLEQ 5607
Cdd:pfam00435   82 LEELNERWEQLLELAAERKQKLEE 105
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
4494-5224 3.11e-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: 44.57  E-value: 3.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4494 YEDLGLLLKDKIAELNTKLSKLQkaqEESSAMMQWLQKMNKTATKWQQTpaptdteavktqveqnksFEAELKQNVNKVQ 4573
Cdd:TIGR00618  178 YTQLALMEFAKKKSLHGKAELLT---LRSQLLTLCTPCMPDTYHERKQV------------------LEKELKHLREALQ 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4574 ELKDKLTELLEENPDTPEAPRWKQMLTEIDSKWQELNQLtIDRQQKLEESSNNLTQFQTVEAQLKQWLVEKELMVSVLGP 4653
Cdd:TIGR00618  237 QTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQ-EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTE 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4654 LSIDPNMLNTQRQQVQILLQEFATRKPQY--EQLTAAGQGILSRPGEDPSLRGIVKEQLAAVTQKWDSLTGQLsdrcdwi 4731
Cdd:TIGR00618  316 LQSKMRSRAKLLMKRAAHVKQQSSIEEQRrlLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQK------- 388
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4732 dqaivksTQYQSLLRSLSDKLSDLDNKLSSSLAVSTHPDAMNQQLETAQKmKQEIQQEKKQIKvAQALCEDLSALVKEEY 4811
Cdd:TIGR00618  389 -------TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKK-QQELQQRYAELC-AAAITCTAQCEKLEKI 459
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4812 LKAELSRQLEGILKSFKDVEQKAENHVQHLQSACASSHQFQQMSRDFqawldtkkeEQNKSHPISAKLDVLEslikdhkd 4891
Cdd:TIGR00618  460 HLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL---------CGSCIHPNPARQDIDN-------- 522
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4892 fSKTLTAQSHMYEKTIAEGENLLLKTQG---SEKAALQLQLNTIKTNWDTFNKQVKEReNKLKESLEKALKykeQVETLW 4968
Cdd:TIGR00618  523 -PGPLTRRMQRGEQTYAQLETSEEDVYHqltSERKQRASLKEQMQEIQQSFSILTQCD-NRSKEDIPNLQN---ITVRLQ 597
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4969 PWIDKcQNNLEEIKFCLDPAEGENSIAKLKSLQKEM-DQHFGMVELLNNTA--------------NSLLSVCEiDKEVVT 5033
Cdd:TIGR00618  598 DLTEK-LSEAEDMLACEQHALLRKLQPEQDLQDVRLhLQQCSQELALKLTAlhalqltltqervrEHALSIRV-LPKELL 675
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5034 DENKSLIQKVDMVTEQLHSKKFCLENMTQKFKEFQEVSKESKRQLQcakEQLDIHDSLGSQAYSNkyLTMLQTQQKSLQ- 5112
Cdd:TIGR00618  676 ASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFN---EIENASSSLGSDLAAR--EDALNQSLKELMh 750
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5113 ----ALKHQVDLAKRLAQDLVVEASDSKGTSDVLLQVETIAQEHSTLSQQVDEKCSFLETKL---------------QGI 5173
Cdd:TIGR00618  751 qartVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIpsdedilnlqcetlvQEE 830
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1761000869 5174 GHFQNTIREMFSQFAEFDDELDSMAPVGRDAETLQKQKETIKAFLKKLEAL 5224
Cdd:TIGR00618  831 EQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGI 881
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1661-1698 3.49e-03

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 38.46  E-value: 3.49e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1761000869 1661 VLEILLSTGSLVIPATGEQLTLQKAFQQNLVSSALFSK 1698
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3888-4390 3.92e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 3.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3888 EEKEKLQKNMKELKVHYEtalaESEKKMKLTHSLQEELEKFDADYTEFEHWLQQSEQELENLEagaddinglmTKLKRQK 3967
Cdd:PRK03918   221 EELEKLEKEVKELEELKE----EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE----------EKVKELK 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3968 SFSEDVishkgdLRYITISGNRVlEAAKSCSKRDGGKVDTSATHREVQRKLDHATD---RFRSLYSKCNVLGNNLKDLVD 4044
Cdd:PRK03918   287 ELKEKA------EEYIKLSEFYE-EYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEE 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4045 KYQHYEDAScGLLAGLQACEATASKHLSEPIAVDPKNLQRQLEETK-----------ALQGQISSQQVAVEKLKKT---- 4109
Cdd:PRK03918   360 RHELYEEAK-AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEeeiskitarigELKKEIKELKKAIEELKKAkgkc 438
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4110 ----AEVLLDARGSLLPAK----NDIQKTLDDIVGRYEDLSKsvneRNEKLQITLTRSLSVQDgLDEMLDWMGNVESSLK 4181
Cdd:PRK03918   439 pvcgRELTEEHRKELLEEYtaelKRIEKELKEIEEKERKLRK----ELRELEKVLKKESELIK-LKELAEQLKELEEKLK 513
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4182 EQGQVPL--NSTALQDIISKNIMLEQDIAGRQSSINAMNEKVKKFMETTdpSTASSLQAKMKDLSARFSEASHKH----K 4255
Cdd:PRK03918   514 KYNLEELekKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELE--KKLDELEEELAELLKELEELGFESveelE 591
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4256 ETLAKME-------ELKTKVELFENLSEKLQTFLETKTQALTEVDVPGKDVTELSQYMQESTSEFL--EHKKHLEVLHSL 4326
Cdd:PRK03918   592 ERLKELEpfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeEYEELREEYLEL 671
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1761000869 4327 LKEISS--HGLPSDKALVLEKTNNLsKKFKEMEDTIKEKKEAVTSCQEQLDAFQVL---VKSLKSWIKE 4390
Cdd:PRK03918   672 SRELAGlrAELEELEKRREEIKKTL-EKLKEELEEREKAKKELEKLEKALERVEELrekVKKYKALLKE 739
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
5068-5311 4.09e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 4.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5068 QEVSKESKRQLQCAKEQLDIHDSLGSQAYSNKyltmlQTQQKSLQALKHQVDLAKRLAQDLVVEASDSKGtsdvllQVET 5147
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEE-----KALLKQLAALERRIAALARRIRALEQELAALEA------ELAE 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5148 IAQEHSTLSQQVDEKCSFLET---KLQGIGHfQNTIREMFSQfAEFDDELDSMAPVGRDAETLQKQKETIKAFLKKLEAL 5224
Cdd:COG4942     88 LEKEIAELRAELEAQKEELAEllrALYRLGR-QPPLALLLSP-EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 5225 MASNDNANKTCKMMLATEETSpdlvgiKRDLEALSKQCNKLLDRAQAREEQVEGTIKRLEEFYSKLKEFSILLQKAEEHE 5304
Cdd:COG4942    166 RAELEAERAELEALLAELEEE------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239

                   ....*..
gi 1761000869 5305 ESQGPVG 5311
Cdd:COG4942    240 AERTPAA 246
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3677-3967 4.16e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 4.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3677 VELKKYQSKQEELQKDMQgsaqaLAEVVKNTENFLKE-NGEKLSQEDKALIEQKLNEAKIKCEQLNLKAEQSKKELDKVV 3755
Cdd:PRK03918   483 RELEKVLKKESELIKLKE-----LAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK 557
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3756 TTAIKEETEKVAavKQLEESKTKIENLldWLSNVDKDSERAGT---KHKQVIEQNgthfqegDGKSAIgEEDEVNGNLLE 3832
Cdd:PRK03918   558 LAELEKKLDELE--EELAELLKELEEL--GFESVEELEERLKElepFYNEYLELK-------DAEKEL-EREEKELKKLE 625
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3833 TDVDgqvgTTQENLNqqyqKVKAQHEKIISQhqaviiatqsaqvlLEKQGQYLSPEEKEKLQKNMKELKVHYETALAESE 3912
Cdd:PRK03918   626 EELD----KAFEELA----ETEKRLEELRKE--------------LEELEKKYSEEEYEELREEYLELSRELAGLRAELE 683
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1761000869 3913 KKMKLTHSLQEELEKFDADYTEFEhwlqQSEQELENLEAGADDINGLMTKLKRQK 3967
Cdd:PRK03918   684 ELEKRREEIKKTLEKLKEELEERE----KAKKELEKLEKALERVEELREKVKKYK 734
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
3494-3950 4.32e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.94  E-value: 4.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3494 SERTKQIMLAIDSEMSKLAvsheeflHKLKSFSDWVSEKSKSVKDIEIVNVQDSEYVKKRLEFLKNVLKDLGHTK----M 3569
Cdd:pfam05483   87 AEKIKKWKVSIEAELKQKE-------NKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnL 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3570 QLETTAFDVQFfISEYaqDLSPNQSKQLLRLLNTTQKCFLDVQESVTTQVERLETQLHLEQDLDDQKIV---AERQQEYK 3646
Cdd:pfam05483  160 LKETCARSAEK-TKKY--EYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQhleEEYKKEIN 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3647 EKLQGICDLL---TQTENRLighqeafmiGDGTVELKKYQSKQEELQKDMQGSAQALAEVVKNTENFLKENGE-----KL 3718
Cdd:pfam05483  237 DKEKQVSLLLiqiTEKENKM---------KDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmslQR 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3719 SQEDKALIEQKLNEAKIKCEQLNLKAEQSKKELDKVVTTAIKEETEKVAAVKQLEE----SKTKIENLLDWLSNVDKDSE 3794
Cdd:pfam05483  308 SMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEllrtEQQRLEKNEDQLKIITMELQ 387
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3795 RAGTKHKQVIE-QNGTHFQEGDGKSAIGEEDEVngnlleTDVDGQVGTTQENLNQQYQKVKA---QHEKIISQHQAVIIA 3870
Cdd:pfam05483  388 KKSSELEEMTKfKNNKEVELEELKKILAEDEKL------LDEKKQFEKIAEELKGKEQELIFllqAREKEIHDLEIQLTA 461
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3871 TQSAQVLLEKQGQYLSPE-EKEKLqKNMkELKVHYETALAESEKKMKLTHSLQEELEKFDADYTEFEHWLQQSEQELENL 3949
Cdd:pfam05483  462 IKTSEEHYLKEVEDLKTElEKEKL-KNI-ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENL 539

                   .
gi 1761000869 3950 E 3950
Cdd:pfam05483  540 E 540
PTZ00121 PTZ00121
MAEBL; Provisional
3678-4004 4.58e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3678 ELKK----YQSKQEELQKdmQGSAQALAEVVKNTENFLKENGEKLSQEDKALIEQKLNEAKIKCEQLNLKAEQSKKELDK 3753
Cdd:PTZ00121  1487 EAKKkaeeAKKKADEAKK--AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK 1564
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3754 VVTTAIKEETEKVAAVKQLEESK----TKIENLLDWLSNVD-------KDSERAGTKHKQVIEQNGTHFQEGDGKSAIGE 3822
Cdd:PTZ00121  1565 KAEEAKKAEEDKNMALRKAEEAKkaeeARIEEVMKLYEEEKkmkaeeaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3823 EDEVNGNLLETDVDGQVGTTQENLNQQYQKVKAQH------------EKIISQHQAVIIATQSAQVLLE--KQGQYLSPE 3888
Cdd:PTZ00121  1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEakkaeedekkaaEALKKEAEEAKKAEELKKKEAEekKKAEELKKA 1724
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3889 EK------EKLQKNMKELKVHYETALAESEKKMKLTHSLQEELEKFDADYTEFEHWLQQSEQELENLEAGADDinglmTK 3962
Cdd:PTZ00121  1725 EEenkikaEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD-----KK 1799
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761000869 3963 LKRQKSFSEDVI--SHKGDL-------------RYITISGNRVLEAAKSCSKRDGGK 4004
Cdd:PTZ00121  1800 IKDIFDNFANIIegGKEGNLvindskemedsaiKEVADSKNMQLEEADAFEKHKFNK 1856
Plectin pfam00681
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ...
1851-1889 4.60e-03

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


Pssm-ID: 459901  Cd Length: 39  Bit Score: 38.08  E-value: 4.60e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1761000869 1851 VLEAQRGYVGLIWPHSGEIFPTSSSLQQELITNELAYKI 1889
Cdd:pfam00681    1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
6085-6483 4.97e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 4.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6085 VKQQQEAAETIREEIDGLQEELDIvinlgseliaacGEPDKPIVKKSIDELNSAWDSLnkawKDRIDKLEEAMQAAVQYQ 6164
Cdd:PRK02224   281 VRDLRERLEELEEERDDLLAEAGL------------DDADAEAVEARREELEDRDEEL----RDRLEECRVAAQAHNEEA 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6165 DGL-QAVFDWVDIAGGKLASMSPIGTDLETVKQQIEElkqfkseayqQQIEMERLNHQAELLLKKVTE-ESDKHTVQDPL 6242
Cdd:PRK02224   345 ESLrEDADDLEERAEELREEAAELESELEEAREAVED----------RREEIEELEEEIEELRERFGDaPVDLGNAEDFL 414
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6243 MELKLIWDSLEERIINRQHKLEGAllalgqfQHALDEllawlthTEGLLSEQK------PVGGDPKAIEIELAKHHV--L 6314
Cdd:PRK02224   415 EELREERDELREREAELEATLRTA-------RERVEE-------AEALLEAGKcpecgqPVEGSPHVETIEEDRERVeeL 480
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6315 QNDVLAHQSTVEAVNKAgndlIESsaGEEASNLQNKLEVLNQRWQNVLEKTEQRKQQLDGALRQAKGFHGEIEDLQqwlT 6394
Cdd:PRK02224   481 EAELEDLEEEVEEVEER----LER--AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE---A 551
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 6395 DTERHLLASkplgglpETAKEQLNVHMEVCAAFEAKEETYKSLMQKgqqmLARCPKSAET--NIDQDINNLKEKWESVET 6472
Cdd:PRK02224   552 EAEEKREAA-------AEAEEEAEEAREEVAELNSKLAELKERIES----LERIRTLLAAiaDAEDEIERLREKREALAE 620
                          410
                   ....*....|.
gi 1761000869 6473 KLNERKTKLEE 6483
Cdd:PRK02224   621 LNDERRERLAE 631
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
7090-7207 5.05e-03

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 42.81  E-value: 5.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 7090 KSRVMDFFRRIDKDQDGKITRQEFIDGILSSKFPTSRLEMSAVADIFDRDGDGYIDYYEFVAALHPNKDAYKPITDADKI 7169
Cdd:cd15899     34 KRRLGVIVSKMDVDKDGFISAKELHSWILESFKRHAMEESKEQFRAVDPDEDGHVSWDEYKNDTYGSVGDDEENVADNIK 113
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1761000869 7170 EDEVTRQVakckcakrfqveqIGDNKYRFFLGNQFGDS 7207
Cdd:cd15899    114 EDEEYKKL-------------LLKDKKRFEAADQDGDL 138
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
31-250 5.29e-03

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 43.78  E-value: 5.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869   31 DERDKVQKKTFTKWINQHLmkVRKHVNDLYEDLRDGHNLISLLEVLSGD---TLPREKGR-------MRFHRLQNVQIAL 100
Cdd:COG5069    374 DAEGEFEARVFTFWLNSLD--VSPEITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAV 451
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  101 DYLKRRQVKLVNIRNDDITDGNpKLTLGLIWTIILHFQISDIHVTGESEDMSAKERLLLWTQQATEGY---AGIRCENFT 177
Cdd:COG5069    452 DLGITEGFSLVGIKGLEILDGI-RLKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWLGSLGLKGdkeEGIRSFGDP 530
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869  178 TCWRDGKLFNAIIHKYRPDLIDMNTVAVQS-------NLANLEHAFYVAEKIGVIRLLDPEDVDVSSPdEKSVITYVSSL 250
Cdd:COG5069    531 AGSVSGVFYLDVLKGIHSELVDYDLVTRGFtefddiaDARSLAISSKILRSLGAIIKFLPEDINGVRP-RLDVLTFIESL 609
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
7088-7160 6.31e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 6.31e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1761000869 7088 HKKSRVMDFFRRIDKDQDGKITRQEFIDGilsskfptSRLEMSAVADIFDRDGDGYIDYYEFVAALHPNKDAY 7160
Cdd:COG5126      2 LQRRKLDRRFDLLDADGDGVLERDDFEAL--------FRRLWATLFSEADTDGDGRISREEFVAGMESLFEAT 66
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
4476-4981 7.67e-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: 7.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4476 ANKGLTSIKKDMTDISHGYEDLGLLLKDKIAELNTKLSKLQKAQEESSAMMQWLQKMNKTatkwqqtpaptdtEAVKTQV 4555
Cdd:TIGR00606  424 KQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKA-------------ERELSKA 490
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4556 EQNKSFEAELKQNVNKVQELKDKLTELLEENPDTPEAPRWKQMLTEIDSkwqelnqLTIDRQQKLEESSNNLTQFQTVEA 4635
Cdd:TIGR00606  491 EKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEM-------LTKDKMDKDEQIRKIKSRHSDELT 563
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4636 QLKQWLVEKELMVSVLGPLSIDPNMLNTQRQQVQILLQEFATRKPQY--------EQLTAAGQGILSRPG---EDPSLRG 4704
Cdd:TIGR00606  564 SLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHInneleskeEQLSSYEDKLFDVCGsqdEESDLER 643
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4705 IVKE---------QLAAVTQKWDSLTGQLSDR-------CDWIDQAIVK----STQYQSLLRSLSDKLSDLDNKLSSsla 4764
Cdd:TIGR00606  644 LKEEieksskqraMLAGATAVYSQFITQLTDEnqsccpvCQRVFQTEAElqefISDLQSKLRLAPDKLKSTESELKK--- 720
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4765 VSTHPDAMNQQLETAQKMKQEIQQEKKQI-----KVAQALCEDLSALVKEEYLKAELSRQLE---------GILKSF--- 4827
Cdd:TIGR00606  721 KEKRRDEMLGLAPGRQSIIDLKEKEIPELrnklqKVNRDIQRLKNDIEEQETLLGTIMPEEEsakvcltdvTIMERFqme 800
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4828 -KDVEQKAENHVQHLQSA--CASSHQFQQMSRDFQAWLDT-----------KKEEQNKSHPISAKLDVL----------- 4882
Cdd:TIGR00606  801 lKDVERKIAQQAAKLQGSdlDRTVQQVNQEKQEKQHELDTvvskielnrklIQDQQEQIQHLKSKTNELkseklqigtnl 880
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 4883 -----------------ESLIKDHKDFSKTLTAQSHMYEKTIAEGENLLLKTQGSEKAAlQLQLNTIKTNWDTFNKQVKE 4945
Cdd:TIGR00606  881 qrrqqfeeqlvelstevQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKA-QDKVNDIKEKVKNIHGYMKD 959
                          570       580       590
                   ....*....|....*....|....*....|....*..
gi 1761000869 4946 RENKLKESLEKALKYKE-QVETLWPWIDKCQNNLEEI 4981
Cdd:TIGR00606  960 IENKIQDGKDDYLKQKEtELNTVNAQLEECEKHQEKI 996
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3610-3953 7.73e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 7.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3610 DVQESVTTQVERLEtqlhleqdldDQKIVAERQQEYKEKLQgICDL------LTQTENRLIGHQEAfmIGDGTVELKKYQ 3683
Cdd:COG1196    193 DILGELERQLEPLE----------RQAEKAERYRELKEELK-ELEAellllkLRELEAELEELEAE--LEELEAELEELE 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3684 SKQEELQKDMQGSAQALAEV-----VKNTENFLKENGEKLSQEDKALIEQKLNEAKIKCEQLNLKAEQSKKELDKVVTTA 3758
Cdd:COG1196    260 AELAELEAELEELRLELEELeleleEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3759 IKEETEKVAAVKQLEESKTKIENLLdwlsnvdkdsERAGTKHKQVIEQNGTHFQEGDGKSAIGEEDEVNGNLLEtdvdgQ 3838
Cdd:COG1196    340 EELEEELEEAEEELEEAEAELAEAE----------EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE-----E 404
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3839 VGTTQENLNQQYQKVKAQHEKIISQHQAVIIATQSAQVLLEKQGqylspEEKEKLQKNMKELKVHYETALAESEKKMKLT 3918
Cdd:COG1196    405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA-----EEEAELEEEEEALLELLAELLEEAALLEAAL 479
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1761000869 3919 HSLQEELEKFDAdytefEHWLQQSEQELENLEAGA 3953
Cdd:COG1196    480 AELLEELAEAAA-----RLLLLLEAEADYEGFLEG 509
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
3676-3756 8.11e-03

Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.


Pssm-ID: 394970 [Multi-domain]  Cd Length: 598  Bit Score: 43.02  E-value: 8.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761000869 3676 TVELKKYQSKQEE--LQKDMQGSAQA-------------LAEVVKNTENFLKENGEKLSQEDKALIEQKLNEAKIKCEQL 3740
Cdd:pfam00012  494 TIEASEGLSDDEIerMVKDAEEYAEEdkkrkerieakneAEEYVYSLEKSLEEEGDKVPEAEKSKVESAIEWLKDELEGD 573
                           90
                   ....*....|....*..
gi 1761000869 3741 NLKAEQSK-KELDKVVT 3756
Cdd:pfam00012  574 DKEEIEAKtEELAQVSQ 590
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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