NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|672033739|ref|XP_008756816|]
View 

utrophin isoform X2 [Rattus norvegicus]

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
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
2869-3030 1.03e-107

EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. 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.


:

Pssm-ID: 320005  Cd Length: 162  Bit Score: 340.72  E-value: 1.03e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2869 ELNTTNEVFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLM 2948
Cdd:cd16247     1 DLNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2949 SLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDW 3028
Cdd:cd16247    81 SLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDW 160

                  ..
gi 672033739 3029 MR 3030
Cdd:cd16247   161 MR 162
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
152-255 1.74e-67

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: 223.30  E-value: 1.74e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  152 SEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPE 231
Cdd:cd21234     1 SEKILLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPE 80
                          90       100
                  ....*....|....*....|....
gi 672033739  232 DVAVQLPDKKSIIMYLTSLFEVLP 255
Cdd:cd21234    81 DVAVQLPDKKSIIMYLTSLFEVLP 104
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
31-137 7.13e-67

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: 221.42  E-value: 7.13e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   31 DVQKKTFTKWINARFSKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNI 110
Cdd:cd21232     1 DVQKKTFTKWINARFSKSGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNI 80
                          90       100
                  ....*....|....*....|....*..
gi 672033739  111 GGTDIVDGNPKLTLGLLWSIILHWQVK 137
Cdd:cd21232    81 GGTDIVDGNHKLTLGLLWSIILHWQVK 107
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
310-528 6.14e-31

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: 122.94  E-value: 6.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  310 DLDSYQIALEEVLTWLLSAEDTFQeQDDISDDVEDVKEQFATHETFMMELTAHQSSVGSVLQAGNQLMTQGTLSDEEefe 389
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  390 IQEQMTLLNARWEALRVESMERQSRLHDALMELQK-KQLQQLSGWLtltEERIQKMESLPVGDDLPSLQNLLEEHKSLQS 468
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFfRDADDLEQWL---EEKEAALASEDLGKDLESVEELLKKHKELEE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  469 DLEAEQVKVNSLTHMVVIVDENSGESATAVLEDQLQKLGERWTAVCRWTEERWNRLQEIN 528
Cdd:cd00176   154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
3055-3103 8.85e-30

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


:

Pssm-ID: 239074  Cd Length: 49  Bit Score: 113.60  E-value: 8.85e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 672033739 3055 AKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVEY 3103
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2437-2677 2.31e-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: 86.35  E-value: 2.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2437 RDLENFVKWLQEAETTAnvladasQRENALQDSVLARQLRQQMLDIQAEIDAHNDIFKSIDGNRQKMVKAlgNSEEATML 2516
Cdd:cd00176     7 RDADELEAWLSEKEELL-------SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2517 QHRLDDMNQRWNDLKAKSASIRAHLEASAEKWnRLLASLEELIKWLNMKDEELkKQMPIGGDVPALQLQYDHCKVLRREL 2596
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2597 KEKEYSVLNAVDQARVFLADQPIEAPEEprrnpqskteltpeeraqkiakaMRKQSSEVREKWESLNAVTSTWQKQVGKA 2676
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEE-----------------------IEEKLEELNERWEELLELAEERQKKLEEA 212

                  .
gi 672033739 2677 L 2677
Cdd:cd00176   213 L 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1967-2169 1.01e-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: 78.64  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1967 EWKQFHCDLDDLTQWLSEAEDLLVGTCAPDGSLDLEKARTHQLELEDGLSSHQPCLIDVNQKGEDIVQRLRPsDASFLKD 2046
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2047 KLASLNQRWSALVAEVKDLQPRLKGESKQVSGYRKrLDEVVCWLTKVENAVQKRSTPDPEENPWEL----TDLAQEMDAQ 2122
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLESVEELlkkhKELEEELEAH 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 672033739 2123 AENIKWLNRAELEMLSDKNLSlcERDNLSESLRNVNTMWTKICREVP 2169
Cdd:cd00176   159 EPRLKSLNELAEELLEEGHPD--ADEEIEEKLEELNERWEELLELAE 203
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
691-904 7.63e-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: 76.33  E-value: 7.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  691 KFDATSAELQSWILRSKAALQNTEMNeyKKSQETSGVRKKWKGLEKEQKEKIPQLDELNQTGQILQEQMGKEgllAEEIN 770
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD---AEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  771 DVLERVLLEWKMISQQLEDLGRKIQLQEDINAYFRQLDALEKTIRAKEEWLRDASFSESPQrSLPSLKDSCQRELTDLLG 850
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLE-SVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 672033739  851 LHPRIEILCASCSAL--RSQPSVPGFVQQGFDDLRRHYQAVQKALEEYQQQLENEL 904
Cdd:cd00176   158 HEPRLKSLNELAEELleEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
803-1015 5.96e-12

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: 67.86  E-value: 5.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  803 YFRQLDALEKTIRAKEEWLRDASFSESPQrSLPSLKDSCQRELTDLLGLHPRIEILCASCSAL-RSQPSVPGFVQQGFDD 881
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLiEEGHPDAEEIQERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  882 LRRHYQAVQKALEEYQQQLENELKSQPepaYLDTLNTLKKMLSESEKAAQaSLSALNDPSAVEQALQEKKALDETLENQK 961
Cdd:cd00176    84 LNQRWEELRELAEERRQRLEEALDLQQ---FFRDADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 672033739  962 PTLHKLSEETKALEKNMLPDVGKTYRQEFDDAQGKWNKVKTKVSRDLRSLEEII 1015
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1235-1446 1.93e-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: 66.32  E-value: 1.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1235 WVELLHYLDLETSWLNTLEERMQSTE--ALPERAEAVHDALESLESVLRHPADNRTQIRELGQTLIDGGILD-DIISEKL 1311
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDygDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDaEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1312 EAFNSRYEELSHLAESKQISLEKQLQVLRETDHMLQVLKESLGELDKQLTTYLTDRIDAFQLPQEAQK-IQAEISAHELT 1390
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKeLEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 672033739 1391 LEELKKNVRPQPPTSPEGRTtrggsqmDLLQRKLREVSTKFQLFQKPANFEQRMLD 1446
Cdd:cd00176   162 LKSLNELAEELLEEGHPDAD-------EEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1132-1336 2.12e-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: 63.23  E-value: 2.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1132 KDLAEMQEWMAQAEEDYLERDFEyKSPEELESAVEEMKRAKEDVLQKEVRVKILKDSIKLVAARVPSGGQELTSEFNEVL 1211
Cdd:cd00176     7 RDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1212 ESYQLLCNRIRGKCHTLEEVWSCWVELLHYLDLEtSWLNTLEERMQSTE--ALPERAEAVHDALESLESVLRHPADNRTQ 1289
Cdd:cd00176    86 QRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDlgKDLESVEELLKKHKELEEELEAHEPRLKS 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 672033739 1290 IRELGQTLIDGGILD--DIISEKLEAFNSRYEELSHLAESKQISLEKQL 1336
Cdd:cd00176   165 LNELAEELLEEGHPDadEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2217-2429 6.38e-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: 61.69  E-value: 6.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2217 DLDKTITELADWLVLIDQMLKSNiVTVGDVKEINKTVSRMKITKADLEQRHPQLDFVFTLAQNLKNkaSSSDLRTAITEK 2296
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2297 LEKLKTQWESTQHGVELRRQQLEDMVVDSLQWDDHREETEELmrkHEARFYMLQQARRDPLS---KQVSDNQLLLQELGS 2373
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWL---EEKEAALASEDLGKDLEsveELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 672033739 2374 GDGVIMAFDNVLQKLLEEYSSDDTRNVEETTEYLKTSWINLKQSIADRQSALEAEL 2429
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2679-2795 2.78e-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: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2679 KLRDLQGAVDDLDADMKEVEAVRNGWKPVGDLliDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLDLHPSPKMS 2758
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 672033739 2759 RQLDDLNMRWKLLQVSVEDRLKQLQEAHRDFGPSSQH 2795
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA 115
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
880-1827 5.81e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.91  E-value: 5.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   880 DDLRRHYQAVQKALEEYQQQLENeLKSQPEPA--YLDtlntlkkmLSESEKAAQASLSALNDPSAV---EQALQEKKALD 954
Cdd:TIGR02168  182 ERTRENLDRLEDILNELERQLKS-LERQAEKAerYKE--------LKAELRELELALLVLRLEELReelEELQEELKEAE 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   955 ETLENQKPTLHKLSEETKALEKNMLPDvgktyRQEFDDAQGKWNKVKTKVSRDLRSLEEIIPRLRDFKADSEVIEkwTNG 1034
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSEL-----EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE--AQL 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1035 VKDFLMKEQAAQgDTTALQRQLDQ----CTTFANEIETIESSLKNLRDIETSLQRcpvtgVKTWVQTRLADYQSQLEKFS 1110
Cdd:TIGR02168  326 EELESKLDELAE-ELAELEEKLEElkeeLESLEAELEELEAELEELESRLEELEE-----QLETLRSKVAQLELQIASLN 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1111 QEIDIQKSRLSDSQEKAMNLKKDLAEMQEWMAQAEEDYLERDFEYKSPE------ELESAVEEMKRAKEDVLQKEVRVKI 1184
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelqeELERLEEALEELREELEEAEQALDA 479
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1185 LKDSIKLVAARvpsggqeltsefnevLESYQLLCNRIRGKCHTLEEVWscwvellhyldLETSWLNTLEERMQSTEALPE 1264
Cdd:TIGR02168  480 AERELAQLQAR---------------LDSLERLQENLEGFSEGVKALL-----------KNQSGLSGILGVLSELISVDE 533
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1265 RAEAvhdaleSLESVLrhpadnrtqirelgqtlidGGILDDIISEKLEAFNsryEELSHLAESKQisleKQLQVLRETDH 1344
Cdd:TIGR02168  534 GYEA------AIEAAL-------------------GGRLQAVVVENLNAAK---KAIAFLKQNEL----GRVTFLPLDSI 581
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1345 MLQVLKESLGELDKQLTTYLTDRIDAFQLPQEAQKIQAEISAHELTLEELKKNVRPQPPTSPEGR-TTRGGSQmdllqrk 1423
Cdd:TIGR02168  582 KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRiVTLDGDL------- 654
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1424 lreVSTKFQLFQKPANFEQRMLDCKRVLDGVKAELHVLsvkdvdpdviqthLDKCMKLYKTLSEVKLEVETviktgrhiV 1503
Cdd:TIGR02168  655 ---VRPGGVITGGSAKTNSSILERRREIEELEEKIEEL-------------EEKIAELEKALAELRKELEE--------L 710
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1504 QKQQTDNPKGMDEQLTSLKVLYNDLGAQVTEGKQDLERASQLSRKLKKEAAILSEWLSTTEAELVQKSTSEGVIGDLDTE 1583
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1584 ISWAKNILKDLERRKVDLNAI-TESSAALQHLVVGSESVLEDtlcvlnagwsrvrtwTEDWRNTLLNHQNQLEVFDGHVA 1662
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAElTLLNEEAANLRERLESLERR---------------IAATERRLEDLEEQIEELSEDIE 855
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1663 HISTWLYQAEALLDEIEKKPASKQEEI------VKRLLSELSDASIQVENVREQAivlvnargsssRELvEPKLAELSKN 1736
Cdd:TIGR02168  856 SLAAEIEELEELIEELESELEALLNERasleeaLALLRSELEELSEELRELESKR-----------SEL-RRELEELREK 923
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1737 FEKVSQHINSAQMLI----------GQDPAGTVEAVGPFSDLESLESDIEnmLKVVEKHLD---PSNDEKMDEeraqIEE 1803
Cdd:TIGR02168  924 LAQLELRLEGLEVRIdnlqerlseeYSLTLEEAEALENKIEDDEEEARRR--LKRLENKIKelgPVNLAAIEE----YEE 997
                          970       980
                   ....*....|....*....|....
gi 672033739  1804 VLQRGEHLLHEpMEDSKKEKIRLQ 1827
Cdd:TIGR02168  998 LKERYDFLTAQ-KEDLTEAKETLE 1020
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
2804-2832 1.85e-06

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


:

Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 46.75  E-value: 1.85e-06
                          10        20
                  ....*....|....*....|....*....
gi 672033739 2804 PWQRSISHNKVPYYINHQTQTTCWDHPKM 2832
Cdd:cd00201     3 GWEERWDPDGRVYYYNHNTKETQWEDPRE 31
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
543-646 2.47e-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


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 48.21  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  543 AWLTEKEEALNKVQTGnfKDQKELGVSVRRLAILKEDMEMKRQTLDQLSEIGQDVGQllSNPKASEKMNSDSEELTQRWD 622
Cdd:cd00176    14 AWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQERLEELNQRWE 89
                          90       100
                  ....*....|....*....|....
gi 672033739  623 SLVQRLEDSSNQVTQAVAKLGMSQ 646
Cdd:cd00176    90 ELRELAEERRQRLEEALDLQQFFR 113
 
Name Accession Description Interval E-value
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
2869-3030 1.03e-107

EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. 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.


Pssm-ID: 320005  Cd Length: 162  Bit Score: 340.72  E-value: 1.03e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2869 ELNTTNEVFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLM 2948
Cdd:cd16247     1 DLNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2949 SLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDW 3028
Cdd:cd16247    81 SLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDW 160

                  ..
gi 672033739 3029 MR 3030
Cdd:cd16247   161 MR 162
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
152-255 1.74e-67

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: 223.30  E-value: 1.74e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  152 SEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPE 231
Cdd:cd21234     1 SEKILLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPE 80
                          90       100
                  ....*....|....*....|....
gi 672033739  232 DVAVQLPDKKSIIMYLTSLFEVLP 255
Cdd:cd21234    81 DVAVQLPDKKSIIMYLTSLFEVLP 104
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
31-137 7.13e-67

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: 221.42  E-value: 7.13e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   31 DVQKKTFTKWINARFSKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNI 110
Cdd:cd21232     1 DVQKKTFTKWINARFSKSGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNI 80
                          90       100
                  ....*....|....*....|....*..
gi 672033739  111 GGTDIVDGNPKLTLGLLWSIILHWQVK 137
Cdd:cd21232    81 GGTDIVDGNHKLTLGLLWSIILHWQVK 107
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
2833-2951 4.95e-52

EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 462668  Cd Length: 123  Bit Score: 179.66  E-value: 4.95e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2833 TELFQSLGDLNNVRFSAYRTAIKIRRLQKALCLDLLELNTTNEVFKQHKLN--QNDQLLSVPDVINCLTTTYDGLEQLHK 2910
Cdd:pfam09068    1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 672033739  2911 D--LVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLS 2951
Cdd:pfam09068   81 TthQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
32-269 3.03e-33

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 139.31  E-value: 3.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   32 VQKKTFTKWINARFSKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPK--ERGSTRVHALNNVNRVLQVLHQNNVELVN 109
Cdd:COG5069     9 VQKKTFTKWTNEKLISGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLFN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  110 IGGTDIVDGNPKLTLGLLWSIILhwqvKDVMKDIMSDLQQTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVL 189
Cdd:COG5069    89 IGPQDIVDGNPKLILGLIWSLIS----RLTIATINEEGELTKHINLLLWCDEDTGGYKPEVDTFDFFRSWRDGLAFSALI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  190 HRHKPDLFSWDRVVKMSPTERLE--HAFSKAHTYLGIEKLLDPEDVA-VQLPDKKSIIMYLTSLFEVLPQQVTID-AIRE 265
Cdd:COG5069   165 HDSRPDTLDPNVLDLQKKNKALNnfQAFENANKVIGIARLIGVEDIVnVSIPDERSIMTYVSWYIIRFGLLEKIDiALHR 244

                  ....
gi 672033739  266 VETL 269
Cdd:COG5069   245 VYRL 248
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
310-528 6.14e-31

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: 122.94  E-value: 6.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  310 DLDSYQIALEEVLTWLLSAEDTFQeQDDISDDVEDVKEQFATHETFMMELTAHQSSVGSVLQAGNQLMTQGTLSDEEefe 389
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  390 IQEQMTLLNARWEALRVESMERQSRLHDALMELQK-KQLQQLSGWLtltEERIQKMESLPVGDDLPSLQNLLEEHKSLQS 468
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFfRDADDLEQWL---EEKEAALASEDLGKDLESVEELLKKHKELEE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  469 DLEAEQVKVNSLTHMVVIVDENSGESATAVLEDQLQKLGERWTAVCRWTEERWNRLQEIN 528
Cdd:cd00176   154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
3055-3103 8.85e-30

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 113.60  E-value: 8.85e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 672033739 3055 AKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVEY 3103
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
31-135 2.44e-20

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: 88.50  E-value: 2.44e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739    31 DVQKKTFTKWINARFSKSG-KPPINDMFSDLKDGRKLLDLLEGLTGTSLP-KERGSTRVHALNNVNRVLQVLHQN-NVEL 107
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGpGVRVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKlGVPK 80
                           90       100
                   ....*....|....*....|....*...
gi 672033739   108 VNIGGTDIVDGNPKLTLGLLWSIILHWQ 135
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
35-133 4.94e-20

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: 87.37  E-value: 4.94e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739     35 KTFTKWINARFSKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPK---ERGSTRVHALNNVNRVLQVLHQNNVELVNIG 111
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvAASLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 672033739    112 GTDIVDGnPKLTLGLLWSIILH 133
Cdd:smart00033   81 PEDLVEG-PKLILGVIWTLISL 101
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
152-255 1.46e-18

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: 83.49  E-value: 1.46e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   152 SEKILLSWVRQTTRPYSQ-VNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVK--MSPTERLEHAFSKAHTYLGIEK-L 227
Cdd:pfam00307    3 LEKELLRWINSHLAEYGPgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKseFDKLENINLALDVAEKKLGVPKvL 82
                           90       100
                   ....*....|....*....|....*...
gi 672033739   228 LDPEDVAvqLPDKKSIIMYLTSLFEVLP 255
Cdd:pfam00307   83 IEPEDLV--EGDNKSVLTYLASLFRRFQ 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2437-2677 2.31e-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: 86.35  E-value: 2.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2437 RDLENFVKWLQEAETTAnvladasQRENALQDSVLARQLRQQMLDIQAEIDAHNDIFKSIDGNRQKMVKAlgNSEEATML 2516
Cdd:cd00176     7 RDADELEAWLSEKEELL-------SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2517 QHRLDDMNQRWNDLKAKSASIRAHLEASAEKWnRLLASLEELIKWLNMKDEELkKQMPIGGDVPALQLQYDHCKVLRREL 2596
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2597 KEKEYSVLNAVDQARVFLADQPIEAPEEprrnpqskteltpeeraqkiakaMRKQSSEVREKWESLNAVTSTWQKQVGKA 2676
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEE-----------------------IEEKLEELNERWEELLELAEERQKKLEEA 212

                  .
gi 672033739 2677 L 2677
Cdd:cd00176   213 L 213
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
154-250 3.58e-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: 79.28  E-value: 3.58e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739    154 KILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVK----MSPTERLEHAFSKAHTYLGIEKLLD 229
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslsrFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 672033739    230 PEDVAVQLPDKKSIIMYLTSL 250
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1967-2169 1.01e-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: 78.64  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1967 EWKQFHCDLDDLTQWLSEAEDLLVGTCAPDGSLDLEKARTHQLELEDGLSSHQPCLIDVNQKGEDIVQRLRPsDASFLKD 2046
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2047 KLASLNQRWSALVAEVKDLQPRLKGESKQVSGYRKrLDEVVCWLTKVENAVQKRSTPDPEENPWEL----TDLAQEMDAQ 2122
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLESVEELlkkhKELEEELEAH 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 672033739 2123 AENIKWLNRAELEMLSDKNLSlcERDNLSESLRNVNTMWTKICREVP 2169
Cdd:cd00176   159 EPRLKSLNELAEELLEEGHPD--ADEEIEEKLEELNERWEELLELAE 203
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
3051-3095 5.11e-15

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 71.36  E-value: 5.11e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 672033739  3051 AKHQAKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSgRTAKGHK 3095
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQ 44
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
691-904 7.63e-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: 76.33  E-value: 7.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  691 KFDATSAELQSWILRSKAALQNTEMNeyKKSQETSGVRKKWKGLEKEQKEKIPQLDELNQTGQILQEQMGKEgllAEEIN 770
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD---AEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  771 DVLERVLLEWKMISQQLEDLGRKIQLQEDINAYFRQLDALEKTIRAKEEWLRDASFSESPQrSLPSLKDSCQRELTDLLG 850
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLE-SVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 672033739  851 LHPRIEILCASCSAL--RSQPSVPGFVQQGFDDLRRHYQAVQKALEEYQQQLENEL 904
Cdd:cd00176   158 HEPRLKSLNELAEELleEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
3052-3095 2.43e-14

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 69.39  E-value: 2.43e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 672033739   3052 KHQAKCNICKEcPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHK 3095
Cdd:smart00291    2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
SPEC smart00150
Spectrin repeats;
314-415 2.07e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 65.81  E-value: 2.07e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739    314 YQIALEEVLTWLLSAEDTFQeQDDISDDVEDVKEQFATHETFMMELTAHQSSVGSVLQAGNQLMTQGtlsDEEEFEIQEQ 393
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG---HPDAEEIEER 78
                            90       100
                    ....*....|....*....|..
gi 672033739    394 MTLLNARWEALRVESMERQSRL 415
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
803-1015 5.96e-12

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: 67.86  E-value: 5.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  803 YFRQLDALEKTIRAKEEWLRDASFSESPQrSLPSLKDSCQRELTDLLGLHPRIEILCASCSAL-RSQPSVPGFVQQGFDD 881
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLiEEGHPDAEEIQERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  882 LRRHYQAVQKALEEYQQQLENELKSQPepaYLDTLNTLKKMLSESEKAAQaSLSALNDPSAVEQALQEKKALDETLENQK 961
Cdd:cd00176    84 LNQRWEELRELAEERRQRLEEALDLQQ---FFRDADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 672033739  962 PTLHKLSEETKALEKNMLPDVGKTYRQEFDDAQGKWNKVKTKVSRDLRSLEEII 1015
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
419-526 1.25e-11

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: 63.49  E-value: 1.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   419 LMELQKKQLQQLSGWLtltEERIQKMESLPVGDDLPSLQNLLEEHKSLQSDLEAEQVKVNSLTHMVVIVdENSGESATAV 498
Cdd:pfam00435    2 LLQQFFRDADDLESWI---EEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKL-IDEGHYASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 672033739   499 LEDQLQKLGERWTAVCRWTEERWNRLQE 526
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1235-1446 1.93e-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: 66.32  E-value: 1.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1235 WVELLHYLDLETSWLNTLEERMQSTE--ALPERAEAVHDALESLESVLRHPADNRTQIRELGQTLIDGGILD-DIISEKL 1311
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDygDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDaEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1312 EAFNSRYEELSHLAESKQISLEKQLQVLRETDHMLQVLKESLGELDKQLTTYLTDRIDAFQLPQEAQK-IQAEISAHELT 1390
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKeLEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 672033739 1391 LEELKKNVRPQPPTSPEGRTtrggsqmDLLQRKLREVSTKFQLFQKPANFEQRMLD 1446
Cdd:cd00176   162 LKSLNELAEELLEEGHPDAD-------EEIEEKLEELNERWEELLELAEERQKKLE 210
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1132-1336 2.12e-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: 63.23  E-value: 2.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1132 KDLAEMQEWMAQAEEDYLERDFEyKSPEELESAVEEMKRAKEDVLQKEVRVKILKDSIKLVAARVPSGGQELTSEFNEVL 1211
Cdd:cd00176     7 RDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1212 ESYQLLCNRIRGKCHTLEEVWSCWVELLHYLDLEtSWLNTLEERMQSTE--ALPERAEAVHDALESLESVLRHPADNRTQ 1289
Cdd:cd00176    86 QRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDlgKDLESVEELLKKHKELEEELEAHEPRLKS 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 672033739 1290 IRELGQTLIDGGILD--DIISEKLEAFNSRYEELSHLAESKQISLEKQL 1336
Cdd:cd00176   165 LNELAEELLEEGHPDadEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
561-1343 2.45e-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: 67.00  E-value: 2.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   561 KDQKELGVSVRRLAILKEDMEMKRQTLDQL--------SEIGQDVGQLLSNPKASEKMNSDSEELTQRWDSLVQRLEDSS 632
Cdd:TIGR02168  222 LRELELALLVLRLEELREELEELQEELKEAeeeleeltAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   633 NQVTQAVAKLgmsqipqkDLLETVHVREQGMIKKPKQELPPPPPPKKRQIHVDVEAKKKFDATSAELQswilRSKAALQN 712
Cdd:TIGR02168  302 QQKQILRERL--------ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----ELEAELEE 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   713 TEMNEYKKSQETSGVRKKWKGLEKEQKEKIPQLDELNQTGQILQEQMGKeglLAEEINDVLER-VLLEWKMISQQLEDLG 791
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER---LQQEIEELLKKlEEAELKELQAELEELE 446
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   792 RKI-QLQEDINAYFRQLDALEKTIRAKEEWLRDAsfsESPQRSLPSLKDSCQRELTDLLGLHPRIEILCASCSALrsqPS 870
Cdd:TIGR02168  447 EELeELQEELERLEEALEELREELEEAEQALDAA---ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL---SG 520
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   871 VPGFVQQGFD-----------DLRRHYQAV-----QKALEEYQQQLENELK------------SQPEPAYLDTLNTLKKM 922
Cdd:TIGR02168  521 ILGVLSELISvdegyeaaieaALGGRLQAVvvenlNAAKKAIAFLKQNELGrvtflpldsikgTEIQGNDREILKNIEGF 600
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   923 LS------ESEKAAQASLSALNDPSAV----EQALQEKKALDE-----TLENQ------------KPTLHKLSEETKALE 975
Cdd:TIGR02168  601 LGvakdlvKFDPKLRKALSYLLGGVLVvddlDNALELAKKLRPgyrivTLDGDlvrpggvitggsAKTNSSILERRREIE 680
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   976 KNmlpdvgktyRQEFDDAQGKWNKVKTKVSRDLRSLEEIIPRLRDFKADSEVIEKWTNGVKDFLMKEQAAQGDTTALQRQ 1055
Cdd:TIGR02168  681 EL---------EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1056 LDQctTFANEIETIESSLKNLRDIETSLQRCPVTGVKtwVQTRLADYQSQLEKFSQEIDIQKSRLSDSQEKAMNLKKDLA 1135
Cdd:TIGR02168  752 LSK--ELTELEAEIEELEERLEEAEEELAEAEAEIEE--LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1136 EMQEWMAQAEE--DYLERDFEYKSP--EELESAVEEMKRAKEDVLQKEVRVKILKDSIKLVAARVPSGGQELTSEFNEVL 1211
Cdd:TIGR02168  828 SLERRIAATERrlEDLEEQIEELSEdiESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1212 ESYQllcnRIRGKCHTLEEvwscwveLLHYLDLEtswLNTLE-ERMQSTEALPERAEAVHDALESLES-VLRHPADNRTQ 1289
Cdd:TIGR02168  908 SKRS----ELRRELEELRE-------KLAQLELR---LEGLEvRIDNLQERLSEEYSLTLEEAEALENkIEDDEEEARRR 973
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 672033739  1290 IRELGQTLID-GGI-LDDIisEKLEAFNSRYEELSHLAESKQISLEKQLQVLRETD 1343
Cdd:TIGR02168  974 LKRLENKIKElGPVnLAAI--EEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2217-2429 6.38e-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: 61.69  E-value: 6.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2217 DLDKTITELADWLVLIDQMLKSNiVTVGDVKEINKTVSRMKITKADLEQRHPQLDFVFTLAQNLKNkaSSSDLRTAITEK 2296
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2297 LEKLKTQWESTQHGVELRRQQLEDMVVDSLQWDDHREETEELmrkHEARFYMLQQARRDPLS---KQVSDNQLLLQELGS 2373
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWL---EEKEAALASEDLGKDLEsveELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 672033739 2374 GDGVIMAFDNVLQKLLEEYSSDDTRNVEETTEYLKTSWINLKQSIADRQSALEAEL 2429
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2679-2795 2.78e-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: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2679 KLRDLQGAVDDLDADMKEVEAVRNGWKPVGDLliDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLDLHPSPKMS 2758
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 672033739 2759 RQLDDLNMRWKLLQVSVEDRLKQLQEAHRDFGPSSQH 2795
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA 115
SPEC smart00150
Spectrin repeats;
1970-2070 3.50e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.87  E-value: 3.50e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   1970 QFHCDLDDLTQWLSEAEDLLVGTCAPDGSLDLEKARTHQLELEDGLSSHQPCLIDVNQKGEDIVQRlRPSDASFLKDKLA 2049
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 672033739   2050 SLNQRWSALVAEVKDLQPRLK 2070
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
880-1827 5.81e-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: 58.91  E-value: 5.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   880 DDLRRHYQAVQKALEEYQQQLENeLKSQPEPA--YLDtlntlkkmLSESEKAAQASLSALNDPSAV---EQALQEKKALD 954
Cdd:TIGR02168  182 ERTRENLDRLEDILNELERQLKS-LERQAEKAerYKE--------LKAELRELELALLVLRLEELReelEELQEELKEAE 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   955 ETLENQKPTLHKLSEETKALEKNMLPDvgktyRQEFDDAQGKWNKVKTKVSRDLRSLEEIIPRLRDFKADSEVIEkwTNG 1034
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSEL-----EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE--AQL 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1035 VKDFLMKEQAAQgDTTALQRQLDQ----CTTFANEIETIESSLKNLRDIETSLQRcpvtgVKTWVQTRLADYQSQLEKFS 1110
Cdd:TIGR02168  326 EELESKLDELAE-ELAELEEKLEElkeeLESLEAELEELEAELEELESRLEELEE-----QLETLRSKVAQLELQIASLN 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1111 QEIDIQKSRLSDSQEKAMNLKKDLAEMQEWMAQAEEDYLERDFEYKSPE------ELESAVEEMKRAKEDVLQKEVRVKI 1184
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelqeELERLEEALEELREELEEAEQALDA 479
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1185 LKDSIKLVAARvpsggqeltsefnevLESYQLLCNRIRGKCHTLEEVWscwvellhyldLETSWLNTLEERMQSTEALPE 1264
Cdd:TIGR02168  480 AERELAQLQAR---------------LDSLERLQENLEGFSEGVKALL-----------KNQSGLSGILGVLSELISVDE 533
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1265 RAEAvhdaleSLESVLrhpadnrtqirelgqtlidGGILDDIISEKLEAFNsryEELSHLAESKQisleKQLQVLRETDH 1344
Cdd:TIGR02168  534 GYEA------AIEAAL-------------------GGRLQAVVVENLNAAK---KAIAFLKQNEL----GRVTFLPLDSI 581
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1345 MLQVLKESLGELDKQLTTYLTDRIDAFQLPQEAQKIQAEISAHELTLEELKKNVRPQPPTSPEGR-TTRGGSQmdllqrk 1423
Cdd:TIGR02168  582 KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRiVTLDGDL------- 654
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1424 lreVSTKFQLFQKPANFEQRMLDCKRVLDGVKAELHVLsvkdvdpdviqthLDKCMKLYKTLSEVKLEVETviktgrhiV 1503
Cdd:TIGR02168  655 ---VRPGGVITGGSAKTNSSILERRREIEELEEKIEEL-------------EEKIAELEKALAELRKELEE--------L 710
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1504 QKQQTDNPKGMDEQLTSLKVLYNDLGAQVTEGKQDLERASQLSRKLKKEAAILSEWLSTTEAELVQKSTSEGVIGDLDTE 1583
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1584 ISWAKNILKDLERRKVDLNAI-TESSAALQHLVVGSESVLEDtlcvlnagwsrvrtwTEDWRNTLLNHQNQLEVFDGHVA 1662
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAElTLLNEEAANLRERLESLERR---------------IAATERRLEDLEEQIEELSEDIE 855
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1663 HISTWLYQAEALLDEIEKKPASKQEEI------VKRLLSELSDASIQVENVREQAivlvnargsssRELvEPKLAELSKN 1736
Cdd:TIGR02168  856 SLAAEIEELEELIEELESELEALLNERasleeaLALLRSELEELSEELRELESKR-----------SEL-RRELEELREK 923
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1737 FEKVSQHINSAQMLI----------GQDPAGTVEAVGPFSDLESLESDIEnmLKVVEKHLD---PSNDEKMDEeraqIEE 1803
Cdd:TIGR02168  924 LAQLELRLEGLEVRIdnlqerlseeYSLTLEEAEALENKIEDDEEEARRR--LKRLENKIKelgPVNLAAIEE----YEE 997
                          970       980
                   ....*....|....*....|....
gi 672033739  1804 VLQRGEHLLHEpMEDSKKEKIRLQ 1827
Cdd:TIGR02168  998 LKERYDFLTAQ-KEDLTEAKETLE 1020
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
878-1493 6.96e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.54  E-value: 6.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  878 GFDDLRRHY---QAVQKALEEYQQQLENELKSQPEpayldtlntLKKMLSESEKAAQASLSALNDPSAVEQALQEK---- 950
Cdd:PRK03918  156 GLDDYENAYknlGEVIKEIKRRIERLEKFIKRTEN---------IEELIKEKEKELEEVLREINEISSELPELREElekl 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  951 KALDETLENQKPTLHKLSEETKALEKNMlpdvgktyRQEFDDAQGKWNKVKTKVSRdLRSLEEIIPRLRDFKADSEVIEK 1030
Cdd:PRK03918  227 EKEVKELEELKEEIEELEKELESLEGSK--------RKLEEKIRELEERIEELKKE-IEELEEKVKELKELKEKAEEYIK 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1031 wtngvkdflmkeqaaqgdttaLQRQLDQCTTFANEIETIESSLKNLRDIetslqrcpvtgvktwVQTRLADyqsqLEKFS 1110
Cdd:PRK03918  298 ---------------------LSEFYEEYLDELREIEKRLSRLEEEING---------------IEERIKE----LEEKE 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1111 QEIDIQKSRLSDSQEKAMNLKKDLAEMQEWMA-QAEEDYLERDFEYKSPEELESAVEEMKRAKEDVLQK----------- 1178
Cdd:PRK03918  338 ERLEELKKKLKELEKRLEELEERHELYEEAKAkKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEiskitarigel 417
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1179 EVRVKILKDSI---KLVAARVPSGGQELTSEFN-EVLESYQLLCNRIRGKCHTLEEVWSCWVELLHYLD---LETSWLNT 1251
Cdd:PRK03918  418 KKEIKELKKAIeelKKAKGKCPVCGRELTEEHRkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvlKKESELIK 497
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1252 LEERMQSTEALPERAEAVHdaLESLESVLRHPADNRTQIRELGQTLIdgGILDDIisEKLEAFNSRYEELS---HLAESK 1328
Cdd:PRK03918  498 LKELAEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKLIKLKGEIK--SLKKEL--EKLEELKKKLAELEkklDELEEE 571
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1329 QISLEKQLQVLRETDhmLQVLKESLGELDKQLTTYLTdridAFQLPQEAQKIQAEISAHELTLEELKKNVrpqppTSPEG 1408
Cdd:PRK03918  572 LAELLKELEELGFES--VEELEERLKELEPFYNEYLE----LKDAEKELEREEKELKKLEEELDKAFEEL-----AETEK 640
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1409 RTTRGGSQMDLLQRKLREvstkfqlfQKPANFEQRMLDCKRVLDGVKAELHVLSVKDvdpDVIQTHLDKCMKLYKTLSEV 1488
Cdd:PRK03918  641 RLEELRKELEELEKKYSE--------EEYEELREEYLELSRELAGLRAELEELEKRR---EEIKKTLEKLKEELEEREKA 709

                  ....*
gi 672033739 1489 KLEVE 1493
Cdd:PRK03918  710 KKELE 714
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
912-1123 2.93e-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: 53.99  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  912 YLDTLNTLKKMLSESEKAAQaSLSALNDPSAVEQALQEKKALDETLENQKPTLHKLSEETKALEKNMLPDVGKTyRQEFD 991
Cdd:cd00176     5 FLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI-QERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  992 DAQGKWNKVKTKVSRDLRSLEEIIpRLRDFKADSEVIEKWTNGVKDFLMKEQAAqGDTTALQRQLDQCTTFANEIETIES 1071
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASEDLG-KDLESVEELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 672033739 1072 SLKNLRDIETSLQRCPVTGVKTWVQTRLADYQSQLEKFSQEIDIQKSRLSDS 1123
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC smart00150
Spectrin repeats;
2437-2542 3.66e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.79  E-value: 3.66e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   2437 RDLENFVKWLQEAETTAnvladasQRENALQDSVLARQLRQQMLDIQAEIDAHNDIFKSIDGNRQKMVKAlgNSEEATML 2516
Cdd:smart00150    5 RDADELEAWLEEKEQLL-------ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE--GHPDAEEI 75
                            90       100
                    ....*....|....*....|....*.
gi 672033739   2517 QHRLDDMNQRWNDLKAKSASIRAHLE 2542
Cdd:smart00150   76 EERLEELNERWEELKELAEERRQKLE 101
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
2213-2598 9.81e-07

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 55.12  E-value: 9.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2213 SVPADLDKT---ITELADWLVLIDQMLKSNIVTVGDVKEINKTVSR-MKITKADLEQRHPQLDFVFTLAQNLKNKASSsd 2288
Cdd:pfam15921  465 SLTAQLESTkemLRKVVEELTAKKMTLESSERTVSDLTASLQEKERaIEATNAEITKLRSRVDLKLQELQHLKNEGDH-- 542
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2289 LRTAITEkLEKLKTQWESTQHGVELRRQQLEDMVvdslqwddhreeteELMRKHeARFYMLQQARRDPLSKQVSDNQLLL 2368
Cdd:pfam15921  543 LRNVQTE-CEALKLQMAEKDKVIEILRQQIENMT--------------QLVGQH-GRTAGAMQVEKAQLEKEINDRRLEL 606
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2369 QELgsgdgvimafdnvlqKLLEEYSSDDTRNVEETTEYLKTSWINLKQSIADRQSAL-------EAELRTVQTSRRDL-- 2439
Cdd:pfam15921  607 QEF---------------KILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVkdikqerDQLLNEVKTSRNELns 671
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2440 ---------ENFVKWLQEAETTANvladasqrenalqdsvlarQLRQQMLDIQAEIDAHNDIFKSIDGNRQKMVK-ALGN 2509
Cdd:pfam15921  672 lsedyevlkRNFRNKSEEMETTTN-------------------KLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKvAMGM 732
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2510 SEEAT--------------MLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWNRLLASLEElikwLNMKDEELKKQ--- 2572
Cdd:pfam15921  733 QKQITakrgqidalqskiqFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV----LRSQERRLKEKvan 808
                          410       420
                   ....*....|....*....|....*..
gi 672033739  2573 MPIGGDVPAlqLQYDHCK-VLRRELKE 2598
Cdd:pfam15921  809 MEVALDKAS--LQFAECQdIIQRQEQE 833
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
729-1035 1.45e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.30  E-value: 1.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   729 KKWKGLEKEQKEKIPQLDELNQTGQILQEQMGKEGLLAEEINDVLERvllewkmISQQLEDLG--RKIQLQEDINAYFRQ 806
Cdd:TIGR02169  230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE-------LNKKIKDLGeeEQLRVKEKIGELEAE 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   807 LDALEKTIRAKEEWLRDAsfsESPQRSLPSLKDSCQRELTDLLG-----------LHPRIEILCASCSALRSQpsvPGFV 875
Cdd:TIGR02169  303 IASLERSIAEKERELEDA---EERLAKLEAEIDKLLAEIEELEReieeerkrrdkLTEEYAELKEELEDLRAE---LEEV 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   876 QQGFDDLRRHYQAVQKALEEYQQQLeNELKSQpepayLDTLNTLKKMLSEsekaAQASLSAlndpsAVEQALQEKKALDE 955
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEKLKREI-NELKRE-----LDRLQEELQRLSE----ELADLNA-----AIAGIEAKINELEE 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   956 TLENQKPTLHKLSEETKALEKNMlpdvgKTYRQEFDDAQGKWNKVKTKVSRDLRSLEE-------IIPRLRDFKADSEVI 1028
Cdd:TIGR02169  442 EKEDKALEIKKQEWKLEQLAADL-----SKYEQELYDLKEEYDRVEKELSKLQRELAEaeaqaraSEERVRGGRAVEEVL 516

                   ....*..
gi 672033739  1029 EKWTNGV 1035
Cdd:TIGR02169  517 KASIQGV 523
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1130-1230 1.49e-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: 49.24  E-value: 1.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1130 LKKDLAEMQEWMAQAEEDYLERDFEyKSPEELESAVEEMKRAKEDVLQKEVRVKILKDSIKLVAARVPSGGQELTSEFNE 1209
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSEDYG-KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEE 84
                           90       100
                   ....*....|....*....|.
gi 672033739  1210 VLESYQLLCNRIRGKCHTLEE 1230
Cdd:pfam00435   85 LNERWEQLLELAAERKQKLEE 105
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
2804-2832 1.85e-06

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 46.75  E-value: 1.85e-06
                          10        20
                  ....*....|....*....|....*....
gi 672033739 2804 PWQRSISHNKVPYYINHQTQTTCWDHPKM 2832
Cdd:cd00201     3 GWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
2800-2832 1.42e-05

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 44.13  E-value: 1.42e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 672033739   2800 SVQLPWQRSISHNKVPYYINHQTQTTCWDHPKM 2832
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
SPEC smart00150
Spectrin repeats;
1237-1333 1.70e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.17  E-value: 1.70e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   1237 ELLHYLDLETSWLNTLEERMQSTE--ALPERAEAVHDALESLESVLRHPADNRTQIRELGQTLIDGGILD-DIISEKLEA 1313
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDlgKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDaEEIEERLEE 81
                            90       100
                    ....*....|....*....|
gi 672033739   1314 FNSRYEELSHLAESKQISLE 1333
Cdd:smart00150   82 LNERWEELKELAEERRQKLE 101
SPEC smart00150
Spectrin repeats;
2683-2783 1.91e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.78  E-value: 1.91e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   2683 LQGAVDDLDADMKEVEAVRNGWKPVGDLliDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLDLHPSPKMSRQLD 2762
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 672033739   2763 DLNMRWKLLQVSVEDRLKQLQ 2783
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1966-2058 2.02e-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: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1966 EEWKQFHCDLDDLTQWLSEAEDLLVgtcAPDGSLDLEKA----RTHQlELEDGLSSHQPCLIDVNQKGEDIVQRlRPSDA 2041
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLS---SEDYGKDLESVqallKKHK-ALEAELAAHQDRVEALNELAEKLIDE-GHYAS 75
                           90
                   ....*....|....*..
gi 672033739  2042 SFLKDKLASLNQRWSAL 2058
Cdd:pfam00435   76 EEIQERLEELNERWEQL 92
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
543-646 2.47e-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: 48.21  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  543 AWLTEKEEALNKVQTGnfKDQKELGVSVRRLAILKEDMEMKRQTLDQLSEIGQDVGQllSNPKASEKMNSDSEELTQRWD 622
Cdd:cd00176    14 AWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQERLEELNQRWE 89
                          90       100
                  ....*....|....*....|....
gi 672033739  623 SLVQRLEDSSNQVTQAVAKLGMSQ 646
Cdd:cd00176    90 ELRELAEERRQRLEEALDLQQFFR 113
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2293-2696 2.91e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 2.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2293 ITEKLEKLKTQWESTQHGVELRRQQLEDMvvdSLQWDDHREETEELMRKHEARFYMLQQARR--DPLSKQVSDNQLLLQE 2370
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEEL---EEELEQLRKELEELSRQISALRKDLARLEAevEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2371 LgsgDGVIMAFDNVLQKLLEEYSSDDTR--NVEETTEYLKTSWINLKQSIADRQSALEAELRTVQTSRRDLENFVKWLQE 2448
Cdd:TIGR02168  759 L---EAEIEELEERLEEAEEELAEAEAEieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2449 AETTANVLADASQRENALQDSVLA--RQLRQQMLDIQAEIDAHNDIFKSIDGNRQKMVKALGNseeatmLQHRLDDMNQR 2526
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEE------LSEELRELESK 909
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2527 WNDLKAKSASIRAHLEASAEKWNRLLASLEELIKWLN----MKDEELKKQMPigGDVPALQLQYDHCKVLRRELKEkeys 2602
Cdd:TIGR02168  910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeeysLTLEEAEALEN--KIEDDEEEARRRLKRLENKIKE---- 983
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2603 vLNAVDqarvfladqpIEAPEEPRrnpqskteltpeeraqkiakamrkqssEVREKWESLNavtstwqKQVGKALEKLRD 2682
Cdd:TIGR02168  984 -LGPVN----------LAAIEEYE---------------------------ELKERYDFLT-------AQKEDLTEAKET 1018
                          410
                   ....*....|....
gi 672033739  2683 LQGAVDDLDADMKE 2696
Cdd:TIGR02168 1019 LEEAIEEIDREARE 1032
SPEC smart00150
Spectrin repeats;
2218-2319 3.56e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.01  E-value: 3.56e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   2218 LDKTITELADWLVLIDQMLKSNIVTvGDVKEINKTVSRMKITKADLEQRHPQLDFVFTLAQNLKNkaSSSDLRTAITEKL 2297
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASEDLG-KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 672033739   2298 EKLKTQWESTQHGVELRRQQLE 2319
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
2804-2830 4.06e-05

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 42.88  E-value: 4.06e-05
                           10        20
                   ....*....|....*....|....*..
gi 672033739  2804 PWQRSISHNKVPYYINHQTQTTCWDHP 2830
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
889-1566 6.75e-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: 48.96  E-value: 6.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   889 VQKALEEYQQQLE---------NELKSQPEPAYLDTLNTLKKMLSEsekaAQASLSALNDPSAVEQALQEKkaLDETLEN 959
Cdd:pfam15921   76 IERVLEEYSHQVKdlqrrlnesNELHEKQKFYLRQSVIDLQTKLQE----MQMERDAMADIRRRESQSQED--LRNQLQN 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   960 qkpTLHKLsEETKALEKNMLPDVGKTYRQ--------------------EFDDAQGK------------WNKVKTKVSRD 1007
Cdd:pfam15921  150 ---TVHEL-EAAKCLKEDMLEDSNTQIEQlrkmmlshegvlqeirsilvDFEEASGKkiyehdsmstmhFRSLGSAISKI 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1008 LRSLE--------EIIP---RLRDFKADSE-----VIEKWTNGVKDFLMK-EQAAQGDTTALQRQLDQCTTFANEIETIE 1070
Cdd:pfam15921  226 LRELDteisylkgRIFPvedQLEALKSESQnkielLLQQHQDRIEQLISEhEVEITGLTEKASSARSQANSIQSQLEIIQ 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1071 SSLKN--------LRDIETSlqrcpVTGVKTWVQTRLADYQSQLEKFSQEIDIQKSRLSDSQEKAMNLKKDLAEMQEWMA 1142
Cdd:pfam15921  306 EQARNqnsmymrqLSDLEST-----VSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQ 380
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1143 QAEEDYLERDfeykspEELESAVEEMKRAKEDVLQKEVRVKILK---DSIKLVAARVPSGGQELTSEFNEVLESyQLLCn 1219
Cdd:pfam15921  381 KLLADLHKRE------KELSLEKEQNKRLWDRDTGNSITIDHLRrelDDRNMEVQRLEALLKAMKSECQGQMER-QMAA- 452
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1220 rIRGKCHTLEEVWScwveLLHYLDLETSWLNTLEERMQSTEALPERAE-AVHDALESLESVLRHPADNRTQIRELGQTLi 1298
Cdd:pfam15921  453 -IQGKNESLEKVSS----LTAQLESTKEMLRKVVEELTAKKMTLESSErTVSDLTASLQEKERAIEATNAEITKLRSRV- 526
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1299 dggildDIISEKLEAFNSRYEELSHL-AESKQISLEkqlqvLRETDHMLQVLKESLGELdKQLTTYLTDRIDAFQLpqEA 1377
Cdd:pfam15921  527 ------DLKLQELQHLKNEGDHLRNVqTECEALKLQ-----MAEKDKVIEILRQQIENM-TQLVGQHGRTAGAMQV--EK 592
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1378 QKIQAEISAHELTLEELK--KNVRPQPPTSPEGRTTrggsqmDLLQRKLREVSTKFQLFQKPANFEQRMldcKRVLDGVK 1455
Cdd:pfam15921  593 AQLEKEINDRRLELQEFKilKDKKDAKIRELEARVS------DLELEKVKLVNAGSERLRAVKDIKQER---DQLLNEVK 663
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1456 AELHVLSVKDVDPDVIQTHL-DKCMKLYKTLSEVKLEVETV---IKTGRHIVQKQQTDN------PKGMDEQLTSLKVLY 1525
Cdd:pfam15921  664 TSRNELNSLSEDYEVLKRNFrNKSEEMETTTNKLKMQLKSAqseLEQTRNTLKSMEGSDghamkvAMGMQKQITAKRGQI 743
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|.
gi 672033739  1526 NDLGAQVTEGKQDLERASQLSRKLKKEAAILSEWLSTTEAE 1566
Cdd:pfam15921  744 DALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE 784
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2678-2784 2.10e-04

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 43.08  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2678 EKLRDLQGAVDDLDADMKEVEAVrNGWKPVGDLLiDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLDLHPSPKM 2757
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEAL-LSSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 672033739  2758 SRQLDDLNMRWKLLQVSVEDRLKQLQE 2784
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
SPEC smart00150
Spectrin repeats;
543-630 3.47e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 42.32  E-value: 3.47e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739    543 AWLTEKEEALNKVQTGnfKDQKELGVSVRRLAILKEDMEMKRQTLDQLSEIGQDVGQllSNPKASEKMNSDSEELTQRWD 622
Cdd:smart00150   12 AWLEEKEQLLASEDLG--KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERLEELNERWE 87

                    ....*...
gi 672033739    623 SLVQRLED 630
Cdd:smart00150   88 ELKELAEE 95
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1094-1360 7.81e-04

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: 7.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1094 WVQTRLADYQSQLEKFSQEIDIQKSRLSDSQEKAMNLKKDLAEMQEWMAQAEEDYLERDFEYKSPE-ELESAVEEMKRAK 1172
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqDIARLEERRRELE 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1173 EDVLQKEVRVKILKDSIKLVAARVpsggQELTSEFNEVLESYQLLCNRIRGKCHTLEEvwscwvELLHYLDLETSWLNTL 1252
Cdd:COG1196   316 ERLEELEEELAELEEELEELEEEL----EELEEELEEAEEELEEAEAELAEAEEALLE------AEAELAEAEEELEELA 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1253 EERMQSTEALPERAEAVHDALESLESVLRHPADNRTQIRELGQTLIDGGILDDIISEKLEAFNSRYEELSHLAESKQISL 1332
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
                         250       260
                  ....*....|....*....|....*...
gi 672033739 1333 EKQLQVLRETDHMLQVLKESLGELDKQL 1360
Cdd:COG1196   466 AELLEEAALLEAALAELLEELAEAAARL 493
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
767-997 1.11e-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: 44.37  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  767 EEINDVLERVLLEWKMISQQLEDLGRKIQLQEdinayfRQLDALEKTIRAKEEWLRDASFSESP-QRSLPSLKDSCQREL 845
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALA------RRIRALEQELAALEAELAELEKEIAElRAELEAQKEELAELL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  846 TDL--LGLHPRIEILCASCSALRSQPSVP--GFVQQGFDDLRRHYQAVQKALEEYQQQLENELKSQpePAYLDTLNTLKK 921
Cdd:COG4942   111 RALyrLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAEL--EALLAELEEERA 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672033739  922 MLSESEKAAQASLSALN-DPSAVEQALQEKKALDETLENQkptLHKLSEETKALEKnmlpdvgKTYRQEFDDAQGKW 997
Cdd:COG4942   189 ALEALKAERQKLLARLEkELAELAAELAELQQEAEELEAL---IARLEAEAAAAAE-------RTPAAGFAALKGKL 255
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2437-2543 1.87e-03

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 40.38  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2437 RDLENFVKWLQEAETTAnvladASQRENALQDSVlaRQLRQQMLDIQAEIDAHNDIFKSIDGNRQKMVKALGNSEEAtmL 2516
Cdd:pfam00435    8 RDADDLESWIEEKEALL-----SSEDYGKDLESV--QALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--I 78
                           90       100
                   ....*....|....*....|....*..
gi 672033739  2517 QHRLDDMNQRWNDLKAKSASIRAHLEA 2543
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
2416-2627 2.14e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2416 QSIADRQSALEAELRTVQTSRRDLENFVKWLQEAettanvLADASQRENALQDSVLARQLRQQMLDIQAEIDahndifks 2495
Cdd:COG3206   215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQ------LGSGPDALPELLQSPVIQQLRAQLAELEAELA-------- 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2496 idgnrQKMVKALGNSEEATMLQHRLDDMNQRwndLKAKSASIRAHLEASAEKWNRLLASLEELIkwlnmkdEELKKQMpi 2575
Cdd:COG3206   281 -----ELSARYTPNHPDVIALRAQIAALRAQ---LQQEAQRILASLEAELEALQAREASLQAQL-------AQLEARL-- 343
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2576 gGDVPALQLQYdhcKVLRREL--KEKEY-SVLNAVDQARVFLADQP-----IEAPEEPRR 2627
Cdd:COG3206   344 -AELPELEAEL---RRLEREVevARELYeSLLQRLEEARLAEALTVgnvrvIDPAVVPLK 399
DUF4175 pfam13779
Domain of unknown function (DUF4175);
737-954 2.26e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 43.82  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   737 EQKEKIPQLDELNQ-TGQILQ------EQMGKEGLLAE------EINDVLERvllewkMISQQLEDlgrkiQLQEDINAY 803
Cdd:pfam13779  537 PQDLQQPDDPNAQEmTQQDLQrmldriEELARSGRRAEaqqmlsQLQQMLEN------LQAGQPQQ-----QQQQGQSEM 605
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   804 FRQLDALEKTIRAKEEwLRDASFSESPQRSLPSLKDSCQRELTDLLGLHPrieilcaSCSALRSQPSVPGFVQQGFDDLR 883
Cdd:pfam13779  606 QQAMDELGDLLREQQQ-LLDETFRQLQQQGGQQQGQPGQQGQQGQGQQPG-------QGGQQPGAQMPPQGGAEALGDLA 677
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672033739   884 RHYQAVQKALEEYQQQLENELKSQPEPAyldtlntlkkmLSESEKA---AQASLSALNDPSAVEqalQEKKALD 954
Cdd:pfam13779  678 ERQQALRRRLEELQDELKELGGKEPGQA-----------LGDAGRAmrdAEEALGQGDLAGAVD---AQGRALE 737
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
884-1217 3.33e-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: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  884 RHYQAVQKALEEYQQQLenelksqpepaYLDTLNTLKKMLSESEKAAQASLSALndpsavEQALQEKKALDETLENQKPT 963
Cdd:COG1196   213 ERYRELKEELKELEAEL-----------LLLKLRELEAELEELEAELEELEAEL------EELEAELAELEAELEELRLE 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  964 LHKLseetkaleknmlpdvgktyRQEFDDAQGKWNKVKTKVSRDLRSLEEIIPRLRDFKADSEVIEkwtngvKDFLMKEQ 1043
Cdd:COG1196   276 LEEL-------------------ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE------EELAELEE 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1044 AAQGDTTALQRQLDQCTTFANEIETIESSLKNLRDIETSLQRcpvtGVKTWVQTRLADYQSQLEKFSQEIDIQKsRLSDS 1123
Cdd:COG1196   331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA----ELAEAEEELEELAEELLEALRAAAELAA-QLEEL 405
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1124 QEKAMNLKKDLAEMQEWMAQAEEDYLERDfeyKSPEELESAVEEMKRAKEDVLQKEVRVKILKDSIKLVAARVPSGGQEL 1203
Cdd:COG1196   406 EEAEEALLERLERLEEELEELEEALAELE---EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
                         330
                  ....*....|....
gi 672033739 1204 TSEFNEVLESYQLL 1217
Cdd:COG1196   483 LEELAEAAARLLLL 496
SPEC smart00150
Spectrin repeats;
803-901 4.28e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 39.24  E-value: 4.28e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739    803 YFRQLDALEKTIRAKEEWLRDASFSESPQrSLPSLKDSCQRELTDLLGLHPRIEILCASCSAL-RSQPSVPGFVQQGFDD 881
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASEDLGKDLE-SVEALLKKHEAFEAELEAHEERVEALNELGEQLiEEGHPDAEEIEERLEE 81
                            90       100
                    ....*....|....*....|
gi 672033739    882 LRRHYQAVQKALEEYQQQLE 901
Cdd:smart00150   82 LNERWEELKELAEERRQKLE 101
 
Name Accession Description Interval E-value
EFh_UTRO cd16247
EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 ...
2869-3030 1.03e-107

EF-hand-like motif found in utrophin; Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. 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.


Pssm-ID: 320005  Cd Length: 162  Bit Score: 340.72  E-value: 1.03e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2869 ELNTTNEVFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLM 2948
Cdd:cd16247     1 DLNTTHSVFKQHKLTQNDQLLSVPDVINCLTTIYDGLEQKHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVLSLKIGLM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2949 SLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDW 3028
Cdd:cd16247    81 SLSKGLLEEKYRYLFKEVAGPGDTCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQHANNKPEIDVKQFIDW 160

                  ..
gi 672033739 3029 MR 3030
Cdd:cd16247   161 MR 162
EFh_DMD_like cd16242
EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes ...
2869-3030 1.13e-93

EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes dystrophin and its two paralogs, utrophin and DRP-2. Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. 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 also involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. 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. DRP-2 is mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. The dystrophins subfamily has been characterized by a compact cluster of domains comprising a WW domain, four EF-hand-like motifs and a ZZ-domain, followed by two syntrophin binding sites (SBSs) and a looser region with two coiled-coils.


Pssm-ID: 320000  Cd Length: 163  Bit Score: 300.69  E-value: 1.13e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2869 ELNTTNEVFKQHKLN-QNDQLLSVPDVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 2947
Cdd:cd16242     1 SLSTAIEAFDQHGLRaQNDKLIDVPDMITCLTTIYEALEEEHPTLVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSFKVGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2948 MSLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFID 3027
Cdd:cd16242    81 VLLCNAHLEEKYRYLFSLIADPNGCVDQRRLGLLLHDCIQIPRQLGEVAAFGGSNIEPSVRSCFEKAGEKPEISAAHFLD 160

                  ...
gi 672033739 3028 WMR 3030
Cdd:cd16242   161 WLK 163
EFh_DMD cd16246
EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal ...
2875-3030 1.81e-81

EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. 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 involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). 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. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.


Pssm-ID: 320004  Cd Length: 162  Bit Score: 265.74  E-value: 1.81e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2875 EVFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLSKGL 2954
Cdd:cd16246     7 EALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAH 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672033739 2955 LEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDWMR 3030
Cdd:cd16246    87 LEDKYRYLFKQVASSTGFCDQRRLGLLLHDAIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWMR 162
EFh_DRP-2 cd16248
EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin ...
2869-3029 5.42e-69

EF-hand-like motif found in dystrophin-related protein 2 (DRP-2); DRP-2 is a dystrophin homologue mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. Like dystrophin, DRP-2 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 only two spectrin repeats (SRs) and a WW domain.


Pssm-ID: 320006  Cd Length: 162  Bit Score: 230.07  E-value: 5.42e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2869 ELNTTNEVFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLM 2948
Cdd:cd16248     1 TLSSATEIFTEHELQMSERVMDVVEVIHCLTALYERLEEERGILVNVPLCVDMCLNWLLNVYDSGRNGKIRVLSFKTGIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2949 SLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFIDW 3028
Cdd:cd16248    81 CLCNADVKEKYQYLFSQVAGPGGQCDQRHLSLLLHEAIQIPRQLGEVAAFGGSNVEPSVRSCFRFAPGKPVIELSQFLEW 160

                  .
gi 672033739 3029 M 3029
Cdd:cd16248   161 M 161
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
152-255 1.74e-67

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: 223.30  E-value: 1.74e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  152 SEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPE 231
Cdd:cd21234     1 SEKILLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPE 80
                          90       100
                  ....*....|....*....|....
gi 672033739  232 DVAVQLPDKKSIIMYLTSLFEVLP 255
Cdd:cd21234    81 DVAVQLPDKKSIIMYLTSLFEVLP 104
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
31-137 7.13e-67

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: 221.42  E-value: 7.13e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   31 DVQKKTFTKWINARFSKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNI 110
Cdd:cd21232     1 DVQKKTFTKWINARFSKSGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNI 80
                          90       100
                  ....*....|....*....|....*..
gi 672033739  111 GGTDIVDGNPKLTLGLLWSIILHWQVK 137
Cdd:cd21232    81 GGTDIVDGNHKLTLGLLWSIILHWQVK 107
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
31-137 2.04e-65

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: 217.25  E-value: 2.04e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   31 DVQKKTFTKWINARFSKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNI 110
Cdd:cd21186     1 DVQKKTFTKWINSQLSKANKPPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNI 80
                          90       100
                  ....*....|....*....|....*..
gi 672033739  111 GGTDIVDGNPKLTLGLLWSIILHWQVK 137
Cdd:cd21186    81 SSNDIVDGNPKLTLGLVWSIILHWQVK 107
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
152-255 1.00e-60

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: 203.81  E-value: 1.00e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  152 SEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPE 231
Cdd:cd21187     1 LEKTLLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPE 80
                          90       100
                  ....*....|....*....|....
gi 672033739  232 DVAVQLPDKKSIIMYLTSLFEVLP 255
Cdd:cd21187    81 DVNVEQPDKKSILMYVTSLFQVLP 104
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
27-137 2.81e-58

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: 197.07  E-value: 2.81e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   27 DEHNDVQKKTFTKWINARFSKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPKERGSTRVHALNNVNRVLQVLHQNNVE 106
Cdd:cd21231     1 YEREDVQKKTFTKWINAQFAKFGKPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 672033739  107 LVNIGGTDIVDGNPKLTLGLLWSIILHWQVK 137
Cdd:cd21231    81 LVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
2869-3029 2.33e-54

EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family 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. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 319999  Cd Length: 163  Bit Score: 187.86  E-value: 2.33e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2869 ELNTTNEVFKQHKLNQ-NDQLLSVPDVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 2947
Cdd:cd15901     1 DLSTVLSVFDRHGLSGsQDSVLDCEELETILTELYIKLNKRRPDLIDVPRASDLLLNWLLNLYDRNRTGCIRLLSVKIAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2948 MSLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFID 3027
Cdd:cd15901    81 ITLCAASLLDKYRYLFGQLADSSGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVEAAVESCFQLARSRVGVSEDTFLS 160

                  ..
gi 672033739 3028 WM 3029
Cdd:cd15901   161 WL 162
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
152-261 1.57e-53

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: 183.59  E-value: 1.57e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  152 SEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKM-SPTERLEHAFSKAHTYLGIEKLLDP 230
Cdd:cd21233     1 SEKILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQqSATERLDHAFNIARQHLGIEKLLDP 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 672033739  231 EDVAVQLPDKKSIIMYLTSLFEVLPQQVTID 261
Cdd:cd21233    81 EDVATAHPDKKSILMYVTSLFQVLPQQVSIE 111
EF-hand_2 pfam09068
EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
2833-2951 4.95e-52

EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 462668  Cd Length: 123  Bit Score: 179.66  E-value: 4.95e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2833 TELFQSLGDLNNVRFSAYRTAIKIRRLQKALCLDLLELNTTNEVFKQHKLN--QNDQLLSVPDVINCLTTTYDGLEQLHK 2910
Cdd:pfam09068    1 TELMQELQDFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNslENDLLLSVSELEALLSSIYFALNKRKP 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 672033739  2911 D--LVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLMSLS 2951
Cdd:pfam09068   81 TthQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123
EF-hand_3 pfam09069
EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. ...
2955-3046 1.84e-45

EF-hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.


Pssm-ID: 462669  Cd Length: 90  Bit Score: 159.77  E-value: 1.84e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2955 LEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGsnIEPSVRSCFQQNNNKPEISVKEFIDWMRLEPQ 3034
Cdd:pfam09069    1 LVDKYRYLFSQISDSNGLLDQSKLGLLLHELLQLPRQVGEVPAFGG--IEPSVRSCFEQVGGKPKITLNHFLDWLMSEPQ 78
                           90
                   ....*....|..
gi 672033739  3035 SMVWLPVLHRVA 3046
Cdd:pfam09069   79 SLVWLPVLHRLA 90
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
32-135 1.10e-41

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: 149.47  E-value: 1.10e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   32 VQKKTFTKWINARFSKSGKPpINDMFSDLKDGRKLLDLLEGLTGTSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 111
Cdd:cd21188     3 VQKKTFTKWVNKHLIKARRR-VVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNIR 81
                          90       100
                  ....*....|....*....|....
gi 672033739  112 GTDIVDGNPKLTLGLLWSIILHWQ 135
Cdd:cd21188    82 AEDIVDGNPKLTLGLIWTIILHFQ 105
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
151-255 3.92e-40

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: 144.84  E-value: 3.92e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  151 NSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDP 230
Cdd:cd21189     1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                          90       100
                  ....*....|....*....|....*
gi 672033739  231 EDVAVQLPDKKSIIMYLTSLFEVLP 255
Cdd:cd21189    81 EDVDVPEPDEKSIITYVSSLYDVFP 105
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
18-139 5.50e-37

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: 137.04  E-value: 5.50e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   18 FSDIIKSRSDEHNDVQKKTFTKWINARFSKSGKPpINDMFSDLKDGRKLLDLLEGLTGTSLPKERGSTRVHALNNVNRVL 97
Cdd:cd21236     3 YENVLERYKDERDKVQKKTFTKWINQHLMKVRKH-VNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIAL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 672033739   98 QVLHQNNVELVNIGGTDIVDGNPKLTLGLLWSIILHWQVKDV 139
Cdd:cd21236    82 DYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 123
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
22-132 6.89e-37

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: 136.34  E-value: 6.89e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   22 IKSRSDEHNDVQKKTFTKWINARFSKSGKPpINDMFSDLKDGRKLLDLLEGLTGTSLPK-ERGSTRVHALNNVNRVLQVL 100
Cdd:cd21246     6 IKALADEREAVQKKTFTKWVNSHLARVGCR-INDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFL 84
                          90       100       110
                  ....*....|....*....|....*....|..
gi 672033739  101 HQNNVELVNIGGTDIVDGNPKLTLGLLWSIIL 132
Cdd:cd21246    85 KEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
22-132 2.38e-36

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: 134.73  E-value: 2.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   22 IKSRSDEHNDVQKKTFTKWINARFSKsGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPK-ERGSTRVHALNNVNRVLQVL 100
Cdd:cd21193     6 IRALQEERINIQKKTFTKWINSFLEK-ANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL 84
                          90       100       110
                  ....*....|....*....|....*....|..
gi 672033739  101 HQNnVELVNIGGTDIVDGNPKLTLGLLWSIIL 132
Cdd:cd21193    85 KTK-VRLENIGAEDIVDGNPRLILGLIWTIIL 115
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
28-137 8.37e-36

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: 132.88  E-value: 8.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   28 EHNDVQKKTFTKWINARFSKSgKPP--INDMFSDLKDGRKLLDLLEGLTGTSLPKERGST--RVHALNNVNRVLQVLHQN 103
Cdd:cd21241     1 EQERVQKKTFTNWINSYLAKR-KPPmkVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESK 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 672033739  104 NVELVNIGGTDIVDGNPKLTLGLLWSIILHWQVK 137
Cdd:cd21241    80 KIKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
156-251 1.13e-35

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: 132.13  E-value: 1.13e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  156 LLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPEDVAV 235
Cdd:cd21248     7 LLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDPEDVNV 86
                          90
                  ....*....|....*.
gi 672033739  236 QLPDKKSIIMYLTSLF 251
Cdd:cd21248    87 EQPDEKSIITYVVTYY 102
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
28-137 1.85e-34

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: 129.18  E-value: 1.85e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   28 EHNDVQKKTFTKWINARFSKSGKPP-INDMFSDLKDGRKLLDLLEGLTGTSLPKERGSTRVHALNNVNRVLQVLHQNNVE 106
Cdd:cd21242     1 EQEQTQKRTFTNWINSQLAKHSPPSvVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 672033739  107 LVNIGGTDIVDGNPKLTLGLLWSIILHWQVK 137
Cdd:cd21242    81 LINIHVPDIIEGKPSIILGLIWTIILHFHIE 111
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
156-251 2.23e-34

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: 128.68  E-value: 2.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  156 LLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPEDVAV 235
Cdd:cd21194     7 LLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDAEDVDV 86
                          90
                  ....*....|....*.
gi 672033739  236 QLPDKKSIIMYLTSLF 251
Cdd:cd21194    87 ARPDEKSIMTYVASYY 102
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
148-251 8.88e-34

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: 127.04  E-value: 8.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  148 QQTNSEK-ILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEK 226
Cdd:cd21319     1 RETRSAKdALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
                          90       100
                  ....*....|....*....|....*
gi 672033739  227 LLDPEDVAVQLPDKKSIIMYLTSLF 251
Cdd:cd21319    81 LLDPEDVFTENPDEKSIITYVVAFY 105
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
32-269 3.03e-33

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 139.31  E-value: 3.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   32 VQKKTFTKWINARFSKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPK--ERGSTRVHALNNVNRVLQVLHQNNVELVN 109
Cdd:COG5069     9 VQKKTFTKWTNEKLISGGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLFN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  110 IGGTDIVDGNPKLTLGLLWSIILhwqvKDVMKDIMSDLQQTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVL 189
Cdd:COG5069    89 IGPQDIVDGNPKLILGLIWSLIS----RLTIATINEEGELTKHINLLLWCDEDTGGYKPEVDTFDFFRSWRDGLAFSALI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  190 HRHKPDLFSWDRVVKMSPTERLE--HAFSKAHTYLGIEKLLDPEDVA-VQLPDKKSIIMYLTSLFEVLPQQVTID-AIRE 265
Cdd:COG5069   165 HDSRPDTLDPNVLDLQKKNKALNnfQAFENANKVIGIARLIGVEDIVnVSIPDERSIMTYVSWYIIRFGLLEKIDiALHR 244

                  ....
gi 672033739  266 VETL 269
Cdd:COG5069   245 VYRL 248
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
27-140 4.91e-33

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: 125.52  E-value: 4.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   27 DEHNDVQKKTFTKWINARFSKSGKPpINDMFSDLKDGRKLLDLLEGLTGTSLPKERGSTRVHALNNVNRVLQVLHQNNVE 106
Cdd:cd21235     1 DERDRVQKKTFTKWVNKHLIKAQRH-ISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 672033739  107 LVNIGGTDIVDGNPKLTLGLLWSIILHWQVKDVM 140
Cdd:cd21235    80 LVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQ 113
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
22-132 5.87e-33

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: 125.91  E-value: 5.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   22 IKSRSDEHNDVQKKTFTKWINARFSKSGKPpINDMFSDLKDGRKLLDLLEGLTGTSLPK-ERGSTRVHALNNVNRVLQVL 100
Cdd:cd21318    28 IKALADEREAVQKKTFTKWVNSHLARVPCR-INDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFL 106
                          90       100       110
                  ....*....|....*....|....*....|..
gi 672033739  101 HQNNVELVNIGGTDIVDGNPKLTLGLLWSIIL 132
Cdd:cd21318   107 KEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
28-137 1.84e-32

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: 123.45  E-value: 1.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   28 EHNDVQKKTFTKWINARFSKSGKP-PINDMFSDLKDGRKLLDLLEGLTGTSLPKERG--STRVHALNNVNRVLQVLHQNN 104
Cdd:cd21190     1 EQERVQKKTFTNWINSHLAKLSQPiVINDLFVDIKDGTALLRLLEVLSGQKLPIESGrvLQRAHKLSNIRNALDFLTKRC 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 672033739  105 VELVNIGGTDIVDGNPKLTLGLLWSIILHWQVK 137
Cdd:cd21190    81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
22-132 1.82e-31

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: 121.31  E-value: 1.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   22 IKSRSDEHNDVQKKTFTKWINARFSKSgKPPINDMFSDLKDGRKLLDLLEGLTGTSLPK-ERGSTRVHALNNVNRVLQVL 100
Cdd:cd21317    21 IKALADEREAVQKKTFTKWVNSHLARV-TCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFL 99
                          90       100       110
                  ....*....|....*....|....*....|..
gi 672033739  101 HQNNVELVNIGGTDIVDGNPKLTLGLLWSIIL 132
Cdd:cd21317   100 KEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
27-139 1.93e-31

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: 120.91  E-value: 1.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   27 DEHNDVQKKTFTKWINARFSKSGKPpINDMFSDLKDGRKLLDLLEGLTGTSLPKERGSTRVHALNNVNRVLQVLHQNNVE 106
Cdd:cd21237     1 DERDRVQKKTFTKWVNKHLMKVRKH-INDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVK 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 672033739  107 LVNIGGTDIVDGNPKLTLGLLWSIILHWQVKDV 139
Cdd:cd21237    80 LVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 112
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
310-528 6.14e-31

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: 122.94  E-value: 6.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  310 DLDSYQIALEEVLTWLLSAEDTFQeQDDISDDVEDVKEQFATHETFMMELTAHQSSVGSVLQAGNQLMTQGTLSDEEefe 389
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  390 IQEQMTLLNARWEALRVESMERQSRLHDALMELQK-KQLQQLSGWLtltEERIQKMESLPVGDDLPSLQNLLEEHKSLQS 468
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALDLQQFfRDADDLEQWL---EEKEAALASEDLGKDLESVEELLKKHKELEE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  469 DLEAEQVKVNSLTHMVVIVDENSGESATAVLEDQLQKLGERWTAVCRWTEERWNRLQEIN 528
Cdd:cd00176   154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
149-255 2.41e-30

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: 117.14  E-value: 2.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  149 QTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLL 228
Cdd:cd21192     1 QGSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLL 80
                          90       100
                  ....*....|....*....|....*..
gi 672033739  229 DPEDVAVQLPDKKSIIMYLTSLFEVLP 255
Cdd:cd21192    81 EVEDVLVDKPDERSIMTYVSQFLRMFP 107
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
139-251 5.46e-30

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: 117.08  E-value: 5.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  139 VMKDIMSDLQQTNSEK-ILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSK 217
Cdd:cd21322     4 VIKIETEDNRETRSAKdALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNT 83
                          90       100       110
                  ....*....|....*....|....*....|....
gi 672033739  218 AHTYLGIEKLLDPEDVAVQLPDKKSIIMYLTSLF 251
Cdd:cd21322    84 AEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
31-132 7.86e-30

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: 115.58  E-value: 7.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   31 DVQKKTFTKWINARFSKSGKPpINDMFSDLKDGRKLLDLLEGLTGTSLPK--ERGSTRVHALNNVNRVLQVLHQNNVELV 108
Cdd:cd21215     3 DVQKKTFTKWLNTKLSSRGLS-ITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLT 81
                          90       100
                  ....*....|....*....|....
gi 672033739  109 NIGGTDIVDGNPKLTLGLLWSIIL 132
Cdd:cd21215    82 NIGAEDIVDGNLKLILGLLWTLIL 105
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
3055-3103 8.85e-30

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 113.60  E-value: 8.85e-30
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 672033739 3055 AKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVEY 3103
Cdd:cd02334     1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
33-132 1.23e-29

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: 115.18  E-value: 1.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   33 QKKTFTKWINARFSKSGkPPINDMFSDLKDGRKLLDLLEGLTGTSLPK-ERGSTRVHALNNVNRVLQVLHQNNVELVNIG 111
Cdd:cd21214     6 QRKTFTAWCNSHLRKAG-TQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVSIG 84
                          90       100
                  ....*....|....*....|.
gi 672033739  112 GTDIVDGNPKLTLGLLWSIIL 132
Cdd:cd21214    85 AEEIVDGNLKMTLGMIWTIIL 105
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
150-255 1.57e-29

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: 114.70  E-value: 1.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  150 TNSEKILLsWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTyLGIEKLLD 229
Cdd:cd21239     1 SAKERLLL-WSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLD 78
                          90       100
                  ....*....|....*....|....*.
gi 672033739  230 PEDVAVQLPDKKSIIMYLTSLFEVLP 255
Cdd:cd21239    79 PEDVDVSSPDEKSVITYVSSLYDVFP 104
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
148-251 2.65e-29

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: 114.38  E-value: 2.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  148 QQTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKL 227
Cdd:cd21216     7 EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKM 86
                          90       100
                  ....*....|....*....|....*
gi 672033739  228 LDPED-VAVQLPDKKSIIMYLTSLF 251
Cdd:cd21216    87 LDAEDiVNTPRPDERSVMTYVSCYY 111
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
149-251 4.44e-29

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: 113.80  E-value: 4.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  149 QTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLL 228
Cdd:cd21249     2 LRSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLL 81
                          90       100
                  ....*....|....*....|...
gi 672033739  229 DPEDVAVQLPDKKSIIMYLtSLF 251
Cdd:cd21249    82 DPEDVAVPHPDERSIMTYV-SLY 103
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
152-251 3.20e-28

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: 111.02  E-value: 3.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  152 SEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPE 231
Cdd:cd21226     1 SEDGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAE 80
                          90       100
                  ....*....|....*....|
gi 672033739  232 DVAVQLPDKKSIIMYlTSLF 251
Cdd:cd21226    81 DVMTGNPDERSIVLY-TSLF 99
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
148-251 3.71e-28

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: 111.30  E-value: 3.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  148 QQTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKL 227
Cdd:cd21321     2 EKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTKL 81
                          90       100
                  ....*....|....*....|....
gi 672033739  228 LDPEDVAVQLPDKKSIIMYLTSLF 251
Cdd:cd21321    82 LDPEDVNVDQPDEKSIITYVATYY 105
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
28-138 6.11e-28

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: 110.75  E-value: 6.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   28 EHNDVQKKTFTKWINARFSKSGKP-PINDMFSDLKDGRKLLDLLEGLTGTSLPKER--GSTRVHALNNVNRVLQVLHQNN 104
Cdd:cd21191     1 ERENVQKRTFTRWINLHLEKCNPPlEVKDLFVDIQDGKILMALLEVLSGQNLLQEYkpSSHRIFRLNNIAKALKFLEDSN 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 672033739  105 VELVNIGGTDIVDGNPKLTLGLLWSIILHWQVKD 138
Cdd:cd21191    81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
150-255 1.37e-27

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: 109.34  E-value: 1.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  150 TNSEKILLsWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLD 229
Cdd:cd21238     2 TAKEKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                          90       100
                  ....*....|....*....|....*.
gi 672033739  230 PEDVAVQLPDKKSIIMYLTSLFEVLP 255
Cdd:cd21238    81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
151-251 3.34e-27

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: 108.26  E-value: 3.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  151 NSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDP 230
Cdd:cd21320     2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
                          90       100
                  ....*....|....*....|.
gi 672033739  231 EDVAVQLPDKKSIIMYLTSLF 251
Cdd:cd21320    82 EDISVDHPDEKSIITYVVTYY 102
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
149-255 3.79e-27

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: 108.17  E-value: 3.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  149 QTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLL 228
Cdd:cd21243     3 KGGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLL 82
                          90       100
                  ....*....|....*....|....*..
gi 672033739  229 DPEDVAVQLPDKKSIIMYLTSLFEVLP 255
Cdd:cd21243    83 DPEDVDVDKPDEKSIMTYVAQFLKKYP 109
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
154-254 3.99e-27

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: 107.82  E-value: 3.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  154 KILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPED- 232
Cdd:cd21253     4 KALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDm 83
                          90       100
                  ....*....|....*....|..
gi 672033739  233 VAVQLPDKKSIIMYLTSLFEVL 254
Cdd:cd21253    84 VALKVPDKLSILTYVSQYYNYF 105
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
31-136 5.38e-26

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: 104.68  E-value: 5.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   31 DVQKKTFTKWINARFSKSGKPpINDMFSDLKDGRKLLDLLEGLTGTSLPK--ERGSTRVHALNNVNRVLQVLHQNNVELV 108
Cdd:cd21227     3 EIQKNTFTNWVNEQLKPTGMS-VEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLV 81
                          90       100
                  ....*....|....*....|....*...
gi 672033739  109 NIGGTDIVDGNPKLTLGLLWSIILHWQV 136
Cdd:cd21227    82 NIGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
22-132 6.13e-26

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: 106.28  E-value: 6.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   22 IKSRSDEHNDVQKKTFTKWINARFSKSgKPPINDMFSDLKDGRKLLDLLEGLTGTSLPK-ERGSTRVHALNNVNRVLQVL 100
Cdd:cd21316    43 IKALADEREAVQKKTFTKWVNSHLARV-SCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFL 121
                          90       100       110
                  ....*....|....*....|....*....|..
gi 672033739  101 HQNNVELVNIGGTDIVDGNPKLTLGLLWSIIL 132
Cdd:cd21316   122 KEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
153-255 4.29e-25

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: 102.04  E-value: 4.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  153 EKILLsWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTyLGIEKLLDPED 232
Cdd:cd21240     7 EKLLL-WTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAED 84
                          90       100
                  ....*....|....*....|...
gi 672033739  233 VAVQLPDKKSIIMYLTSLFEVLP 255
Cdd:cd21240    85 VDVPSPDEKSVITYVSSIYDAFP 107
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
156-251 1.85e-24

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: 100.68  E-value: 1.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  156 LLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPEDVA- 234
Cdd:cd21291    15 LLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGIPQLLDVEDVCd 94
                          90
                  ....*....|....*..
gi 672033739  235 VQLPDKKSIIMYLTSLF 251
Cdd:cd21291    95 VAKPDERSIMTYVAYYF 111
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
147-251 3.59e-24

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: 100.16  E-value: 3.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  147 LQQTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEK 226
Cdd:cd21290     9 VEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPK 88
                          90       100
                  ....*....|....*....|....*.
gi 672033739  227 LLDPED-VAVQLPDKKSIIMYLTSLF 251
Cdd:cd21290    89 MLDAEDiVNTARPDEKAIMTYVSSFY 114
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
154-255 2.21e-23

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


Pssm-ID: 409094  Cd Length: 106  Bit Score: 97.17  E-value: 2.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  154 KILLSWVRQTTRPYSqVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPEDV 233
Cdd:cd21245     6 KALLNWVQRRTRKYG-VAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPEDV 84
                          90       100
                  ....*....|....*....|..
gi 672033739  234 AVQLPDKKSIIMYLTSLFEVLP 255
Cdd:cd21245    85 MVDSPDEQSIMTYVAQFLEHFP 106
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
22-136 8.60e-23

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


Pssm-ID: 409096  Cd Length: 125  Bit Score: 96.37  E-value: 8.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   22 IKSRSDEHNDVQKKTFTKWINARFSKSG-KPPINDMFSDLKDGRKLLDLLEGLTGTSLPK-ERGSTRVHALNNVNRVLQV 99
Cdd:cd21247    10 IRKLQEQRMTMQKKTFTKWMNNVFSKNGaKIEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITF 89
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 672033739  100 LhQNNVELVNIGGTDIVDGNPKLTLGLLWSIILHWQV 136
Cdd:cd21247    90 L-KTKVPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
147-254 2.49e-22

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: 94.77  E-value: 2.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  147 LQQTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEK 226
Cdd:cd21287     6 VEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPK 85
                          90       100
                  ....*....|....*....|....*....
gi 672033739  227 LLDPED-VAVQLPDKKSIIMYLTSLFEVL 254
Cdd:cd21287    86 MLDAEDiVGTARPDEKAIMTYVSSFYHAF 114
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
154-251 1.08e-21

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: 92.22  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  154 KILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPED- 232
Cdd:cd21197     3 QALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDm 82
                          90
                  ....*....|....*....
gi 672033739  233 VAVQLPDKKSIIMYLTSLF 251
Cdd:cd21197    83 VTMHVPDRLSIITYVSQYY 101
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
147-254 2.91e-21

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: 92.10  E-value: 2.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  147 LQQTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEK 226
Cdd:cd21289     6 VEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPK 85
                          90       100
                  ....*....|....*....|....*....
gi 672033739  227 LLDPEDVA-VQLPDKKSIIMYLTSLFEVL 254
Cdd:cd21289    86 MLDAEDIVnTPKPDEKAIMTYVSCFYHAF 114
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
156-254 7.68e-21

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: 90.04  E-value: 7.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  156 LLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDrvvKMSPTERLEH---AFSKAHTYLGIEKLLDPED 232
Cdd:cd22198     5 LLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFS---SLDPENIAENnqlAFDVAEQELGIPPVMTGQE 81
                          90       100
                  ....*....|....*....|...
gi 672033739  233 VA-VQLPDKKSIIMYLTSLFEVL 254
Cdd:cd22198    82 MAsLAVPDKLSMVSYLSQFYEAF 104
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
32-136 1.27e-20

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: 90.20  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   32 VQKKTFTKWINARFSKSGKPpINDMFSDLKDGRKLLDLLEGLTGTSLPK--ERGSTRVHALNNVNRVLQVL-HQNNVELV 108
Cdd:cd21311    15 IQQNTFTRWANEHLKTANKH-IADLETDLSDGLRLIALVEVLSGKKFPKfnKRPTFRSQKLENVSVALKFLeEDEGIKIV 93
                          90       100
                  ....*....|....*....|....*...
gi 672033739  109 NIGGTDIVDGNPKLTLGLLWSIILHWQV 136
Cdd:cd21311    94 NIDSSDIVDGKLKLILGLIWTLILHYSI 121
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
31-135 2.44e-20

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: 88.50  E-value: 2.44e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739    31 DVQKKTFTKWINARFSKSG-KPPINDMFSDLKDGRKLLDLLEGLTGTSLP-KERGSTRVHALNNVNRVLQVLHQN-NVEL 107
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGpGVRVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKlGVPK 80
                           90       100
                   ....*....|....*....|....*...
gi 672033739   108 VNIGGTDIVDGNPKLTLGLLWSIILHWQ 135
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
149-252 4.08e-20

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: 87.97  E-value: 4.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  149 QTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLL 228
Cdd:cd21244     3 KMSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLL 82
                          90       100
                  ....*....|....*....|....
gi 672033739  229 DPEDVAVQLPDKKSIIMYLTSLFE 252
Cdd:cd21244    83 EPEDVDVVNPDEKSIMTYVAQFLQ 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
35-133 4.94e-20

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: 87.37  E-value: 4.94e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739     35 KTFTKWINARFSKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPK---ERGSTRVHALNNVNRVLQVLHQNNVELVNIG 111
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvAASLSRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 672033739    112 GTDIVDGnPKLTLGLLWSIILH 133
Cdd:smart00033   81 PEDLVEG-PKLILGVIWTLISL 101
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
151-250 6.71e-20

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: 87.10  E-value: 6.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  151 NSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTyLGIEKLLDP 230
Cdd:cd21198     1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
                          90       100
                  ....*....|....*....|.
gi 672033739  231 EDVAV-QLPDKKSIIMYLTSL 250
Cdd:cd21198    80 ADMVLlSVPDKLSVMTYLHQI 100
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
156-251 9.74e-20

calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409101  Cd Length: 107  Bit Score: 86.85  E-value: 9.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  156 LLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPED-VA 234
Cdd:cd21252     5 LQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPEDmVS 84
                          90
                  ....*....|....*..
gi 672033739  235 VQLPDKKSIIMYLTSLF 251
Cdd:cd21252    85 MKVPDCLSIMTYVSQYY 101
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
32-134 1.99e-19

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: 86.00  E-value: 1.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   32 VQKKTFTKWINARFSKSGKPpINDMFSDLKDGRKLLDLLEGLTGTSLPK---ERGSTRVHALNNVNRVLQVLHQNNVELV 108
Cdd:cd21183     4 IQANTFTRWCNEHLKERGMQ-IHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
                          90       100
                  ....*....|....*....|....*.
gi 672033739  109 NIGGTDIVDGNPKLTLGLLWSIILHW 134
Cdd:cd21183    83 NIGSGDIVNGNIKLILGLIWTLILHY 108
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
156-254 3.72e-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: 85.48  E-value: 3.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  156 LLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPEDVA- 234
Cdd:cd21195     9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEMAs 88
                          90       100
                  ....*....|....*....|
gi 672033739  235 VQLPDKKSIIMYLTSLFEVL 254
Cdd:cd21195    89 AQEPDKLSMVMYLSKFYELF 108
EFh_DAH cd16245
EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and ...
2870-3029 4.96e-19

EF-hand-like motif found in Drosophila melanogaster discontinuous actin hexagon (DAH) and similar proteins; DAH, the product of the dah (discontinuous actin hexagon) gene, is a Drosophila homolog to vertebrate dystrotelin. It is tightly membrane-associated and highly phosphorylated in a time-dependent fashion. DAH plays an essential role in the process of cellularization, and is associated with vesicles that convene at the cleavage furrow. The absence of DAH leads the severe disruption of the cleavage furrows around the nuclei and development stalls. DAH contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils.


Pssm-ID: 320003 [Multi-domain]  Cd Length: 164  Bit Score: 86.97  E-value: 4.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2870 LNTTNEVFKQHKLNQNDQLLSVP--DVINCLTTTYDGLEQLHKDLVNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 2947
Cdd:cd16245     2 LKLIMGVFDRHQLSNSENNLCLPpdELEAVLHDIYFAAEKLGNFNIDVDLATELLANLFLNVFDPERKKSISVLELKVFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2948 MSLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSNIEPSVRSCFQQNNNKPEISVKEFID 3027
Cdd:cd16245    82 TLLCGSSLQEKYLYLFQLLADHNNCVSRKRLEALLKSLAKLLSYLGEDVAFGSHLIELAVEQCFENSPGLVGLTEYQFIG 161

                  ..
gi 672033739 3028 WM 3029
Cdd:cd16245   162 WW 163
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
155-251 6.58e-19

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: 84.32  E-value: 6.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  155 ILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDrvvKMSPTER---LEHAFSKAHTYLGIEKLLDPE 231
Cdd:cd21200     5 MLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYS---SLDPKNRrknFELAFSTAEELADIAPLLEVE 81
                          90       100
                  ....*....|....*....|..
gi 672033739  232 DVAV--QLPDKKSIIMYLTSLF 251
Cdd:cd21200    82 DMVRmgNRPDWKCVFTYVQSLY 103
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
152-255 1.46e-18

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: 83.49  E-value: 1.46e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   152 SEKILLSWVRQTTRPYSQ-VNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVK--MSPTERLEHAFSKAHTYLGIEK-L 227
Cdd:pfam00307    3 LEKELLRWINSHLAEYGPgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKseFDKLENINLALDVAEKKLGVPKvL 82
                           90       100
                   ....*....|....*....|....*...
gi 672033739   228 LDPEDVAvqLPDKKSIIMYLTSLFEVLP 255
Cdd:pfam00307   83 IEPEDLV--EGDNKSVLTYLASLFRRFQ 108
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
151-250 1.54e-18

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


Pssm-ID: 409103  Cd Length: 107  Bit Score: 83.36  E-value: 1.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  151 NSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAhTYLGIEKLLDP 230
Cdd:cd21254     1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGF-ASLGISRLLEP 79
                          90       100
                  ....*....|....*....|.
gi 672033739  231 ED-VAVQLPDKKSIIMYLTSL 250
Cdd:cd21254    80 SDmVLLAVPDKLTVMTYLYQI 100
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2437-2677 2.31e-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: 86.35  E-value: 2.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2437 RDLENFVKWLQEAETTAnvladasQRENALQDSVLARQLRQQMLDIQAEIDAHNDIFKSIDGNRQKMVKAlgNSEEATML 2516
Cdd:cd00176     7 RDADELEAWLSEKEELL-------SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE--GHPDAEEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2517 QHRLDDMNQRWNDLKAKSASIRAHLEASAEKWnRLLASLEELIKWLNMKDEELkKQMPIGGDVPALQLQYDHCKVLRREL 2596
Cdd:cd00176    78 QERLEELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEEL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2597 KEKEYSVLNAVDQARVFLADQPIEAPEEprrnpqskteltpeeraqkiakaMRKQSSEVREKWESLNAVTSTWQKQVGKA 2676
Cdd:cd00176   156 EAHEPRLKSLNELAEELLEEGHPDADEE-----------------------IEEKLEELNERWEELLELAEERQKKLEEA 212

                  .
gi 672033739 2677 L 2677
Cdd:cd00176   213 L 213
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
32-134 2.79e-18

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: 82.92  E-value: 2.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   32 VQKKTFTKWINARFSKSGKPpINDMFSDLKDGRKLLDLLEGLTGTSLPK---ERGSTRVHALNNVNRVLQVLHQNNVELV 108
Cdd:cd21228     4 IQQNTFTRWCNEHLKCVNKR-IYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
                          90       100
                  ....*....|....*....|....*.
gi 672033739  109 NIGGTDIVDGNPKLTLGLLWSIILHW 134
Cdd:cd21228    83 SIDSSAIVDGNLKLILGLIWTLILHY 108
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
147-251 2.98e-18

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: 83.20  E-value: 2.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  147 LQQTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEK 226
Cdd:cd21288     6 VEETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPK 85
                          90       100
                  ....*....|....*....|....*.
gi 672033739  227 LLDPED-VAVQLPDKKSIIMYLTSLF 251
Cdd:cd21288    86 MLDAEDiVNTPKPDERAIMTYVSCFY 111
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
153-257 3.85e-18

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: 82.73  E-value: 3.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  153 EKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDrvvKMSPTER---LEHAFSKAHTYLGIEKLLD 229
Cdd:cd21259     3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYS---QLSPQNRrhnFEVAFSSAEKHADCPQLLD 79
                          90       100
                  ....*....|....*....|....*....
gi 672033739  230 PED-VAVQLPDKKSIIMYLTSLFEVLPQQ 257
Cdd:cd21259    80 VEDmVRMREPDWKCVYTYIQEFYRCLVQK 108
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
153-254 1.08e-17

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


Pssm-ID: 409107  Cd Length: 111  Bit Score: 81.25  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  153 EKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPED 232
Cdd:cd21258     3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
                          90       100
                  ....*....|....*....|....
gi 672033739  233 VAV--QLPDKKSIIMYLTSLFEVL 254
Cdd:cd21258    83 MMImgKKPDSKCVFTYVQSLYNHL 106
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
152-249 1.37e-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: 80.74  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  152 SEKILLSWVRQTTRPYsqvNVLNFTTSWTDGLAFNAVLHRHKPDLFS-WDRVVKMSPTERLEHAFSKAHTYLGIEKLLDP 230
Cdd:cd21184     2 GKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPdNESLDKENPLENATKAMDIAEEELGIPKIITP 78
                          90
                  ....*....|....*....
gi 672033739  231 EDVAVQLPDKKSIIMYLTS 249
Cdd:cd21184    79 EDMVSPNVDELSVMTYLSY 97
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
156-250 2.10e-17

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: 80.22  E-value: 2.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  156 LLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTyLGIEKLLDPED-VA 234
Cdd:cd21255     6 LLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEPADmVL 84
                          90
                  ....*....|....*.
gi 672033739  235 VQLPDKKSIIMYLTSL 250
Cdd:cd21255    85 LPIPDKLIVMTYLCQL 100
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
152-257 2.88e-17

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: 80.13  E-value: 2.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  152 SEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPE 231
Cdd:cd21260     2 VKNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVE 81
                          90       100
                  ....*....|....*....|....*..
gi 672033739  232 D-VAVQLPDKKSIIMYLTSLFEVLPQQ 257
Cdd:cd21260    82 DmVRMSVPDSKCVYTYIQELYRSLVQK 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
154-250 3.58e-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: 79.28  E-value: 3.58e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739    154 KILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVK----MSPTERLEHAFSKAHTYLGIEKLLD 229
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslsrFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 672033739    230 PEDVAVQLPDKKSIIMYLTSL 250
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
156-254 4.77e-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: 79.22  E-value: 4.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  156 LLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPEDVA- 234
Cdd:cd21251    10 LLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPIMTGKEMAs 89
                          90       100
                  ....*....|....*....|
gi 672033739  235 VQLPDKKSIIMYLTSLFEVL 254
Cdd:cd21251    90 VGEPDKLSMVMYLTQFYEMF 109
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
425-630 2.11e-16

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 80.95  E-value: 2.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  425 KQLQQLSGWLTLTEERIQKMEslpVGDDLPSLQNLLEEHKSLQSDLEAEQVKVNSLTHMVVIVDEnSGESATAVLEDQLQ 504
Cdd:cd00176     7 RDADELEAWLSEKEELLSSTD---YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  505 KLGERWTAVCRWTEERWNRLQEINILWqELLEEQCLLEAWLTEKEEALNKVQTGnfKDQKELGVSVRRLAILKEDMEMKR 584
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLG--KDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 672033739  585 QTLDQLSEIGQDVGQlLSNPKASEKMNSDSEELTQRWDSLVQRLED 630
Cdd:cd00176   160 PRLKSLNELAEELLE-EGHPDADEEIEEKLEELNERWEELLELAEE 204
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
32-130 2.13e-16

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: 77.57  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   32 VQKKTFTKWINARFSKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPKE---RGSTRVHALNNVNRVLQVLHQN-NVEL 107
Cdd:cd21225     4 VQIKAFTAWVNSVLEKRGIPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKIRV 83
                          90       100
                  ....*....|....*....|...
gi 672033739  108 VNIGGTDIVDGNPKLTLGLLWSI 130
Cdd:cd21225    84 QGIGAEDFVDNNKKLILGLLWTL 106
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
32-136 5.30e-16

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: 76.99  E-value: 5.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   32 VQKKTFTKWINARFSKSGKPpINDMFSDLKDGRKLLDLLEGLTGTSLPKE---RGSTRVHALNNVNRVLQVLHQNNVELV 108
Cdd:cd21310    16 IQQNTFTRWCNEHLKCVQKR-LNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
                          90       100
                  ....*....|....*....|....*...
gi 672033739  109 NIGGTDIVDGNPKLTLGLLWSIILHWQV 136
Cdd:cd21310    95 SIDSKAIVDGNLKLILGLIWTLILHYSI 122
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
153-254 6.84e-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: 75.77  E-value: 6.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  153 EKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDrvvKMSPTER---LEHAFSKAHTYLGIEKLLD 229
Cdd:cd21261     3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYD---SLSPSNRkhnFELAFSMAEKLANCDRLIE 79
                          90       100
                  ....*....|....*....|....*..
gi 672033739  230 PEDVAV--QLPDKKSIIMYLTSLFEVL 254
Cdd:cd21261    80 VEDMMVmgRKPDPMCVFTYVQSLYNHL 106
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
33-133 8.55e-16

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


Pssm-ID: 409061  Cd Length: 105  Bit Score: 75.70  E-value: 8.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   33 QKKTFTKWINARFSKSG-KPPINDMFSDLKDGRKLLDLLEGLTGTSLPK--ERGSTRVHALNNVNRVLQVLHQNNVELVN 109
Cdd:cd21212     1 EIEIYTDWANHYLEKGGhKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGihSRPKTRAQKLENIQACLQFLAALGVDVQG 80
                          90       100
                  ....*....|....*....|....
gi 672033739  110 IGGTDIVDGNPKLTLGLLWSIILH 133
Cdd:cd21212    81 ITAEDIVDGNLKAILGLFFSLSRY 104
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1967-2169 1.01e-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: 78.64  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1967 EWKQFHCDLDDLTQWLSEAEDLLVGTCAPDGSLDLEKARTHQLELEDGLSSHQPCLIDVNQKGEDIVQRLRPsDASFLKD 2046
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2047 KLASLNQRWSALVAEVKDLQPRLKGESKQVSGYRKrLDEVVCWLTKVENAVQKRSTPDPEENPWEL----TDLAQEMDAQ 2122
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDLESVEELlkkhKELEEELEAH 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 672033739 2123 AENIKWLNRAELEMLSDKNLSlcERDNLSESLRNVNTMWTKICREVP 2169
Cdd:cd00176   159 EPRLKSLNELAEELLEEGHPD--ADEEIEEKLEELNERWEELLELAE 203
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
156-251 1.88e-15

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


Pssm-ID: 409048  Cd Length: 112  Bit Score: 74.70  E-value: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  156 LLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYlGIEKLLDPED-VA 234
Cdd:cd21199    13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESV-GIPTTLTIDEmVS 91
                          90
                  ....*....|....*..
gi 672033739  235 VQLPDKKSIIMYLTSLF 251
Cdd:cd21199    92 MERPDWQSVMSYVTAIY 108
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
156-253 3.93e-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: 73.76  E-value: 3.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  156 LLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLD-PEDVA 234
Cdd:cd21250     9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMAS 88
                          90
                  ....*....|....*....
gi 672033739  235 VQLPDKKSIIMYLTSLFEV 253
Cdd:cd21250    89 AEEPDKLSMVMYLSKFYEL 107
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
3051-3095 5.11e-15

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 71.36  E-value: 5.11e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 672033739  3051 AKHQAKCNICKECPIVGFRYRSLKHFNYDVCQSCFFSgRTAKGHK 3095
Cdd:pfam00569    1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQ 44
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
691-904 7.63e-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: 76.33  E-value: 7.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  691 KFDATSAELQSWILRSKAALQNTEMNeyKKSQETSGVRKKWKGLEKEQKEKIPQLDELNQTGQILQEQMGKEgllAEEIN 770
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD---AEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  771 DVLERVLLEWKMISQQLEDLGRKIQLQEDINAYFRQLDALEKTIRAKEEWLRDASFSESPQrSLPSLKDSCQRELTDLLG 850
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLE-SVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 672033739  851 LHPRIEILCASCSAL--RSQPSVPGFVQQGFDDLRRHYQAVQKALEEYQQQLENEL 904
Cdd:cd00176   158 HEPRLKSLNELAEELleEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
EFh_DTN cd16244
EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the ...
2875-3029 8.83e-15

EF-hand-like motif found in dystrobrevins and similar proteins; Dystrobrevins are part of the dystrophin-glycoprotein complex (DGC). They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. The family includes two paralogs dystrobrevins, alpha- and beta-dystrobrevin, both of which are cytoplasmic components of the dystrophin-associated protein complex that function as scaffold proteins in signal transduction and intracellular transport. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. The dystrobrevins 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, dystrobrevins contain one or two syntrophin binding sites (SBSs).


Pssm-ID: 320002 [Multi-domain]  Cd Length: 161  Bit Score: 74.58  E-value: 8.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2875 EVFKQHKLNQND--QLLSVPDVINCLTTTYdglEQLHKDL-----VNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 2947
Cdd:cd16244     7 EAFRENGLNTLDptTELSVSRLETLLSSIY---YQLNKRLptthqIDVDQSISLLLNWLLAAYDPEATGRLTVFSVKVAL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2948 MSLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQQNNnkpEISVKEFID 3027
Cdd:cd16244    84 STLCAGKLVDKLRYIFSQISDSNGVLVFSKFEDFLREALKLPTAVFEGPSFGYN--ESAARSCFPGQS---KVTVNDFLD 158

                  ..
gi 672033739 3028 WM 3029
Cdd:cd16244   159 VM 160
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
34-132 1.10e-14

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: 72.37  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   34 KKTFTKWINARFSKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPKE--RGSTRVHALNNVNRVLQVLHQNNV-ELVNI 110
Cdd:cd00014     1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
                          90       100
                  ....*....|....*....|...
gi 672033739  111 GGTDIV-DGNPKLTLGLLWSIIL 132
Cdd:cd00014    81 EPEDLYeKGNLKKVLGTLWALAL 103
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
34-133 1.48e-14

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 72.31  E-value: 1.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   34 KKTFTKWINarfSKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSL-------PKERGstRVHALNNVNRVLQVLHQNNVE 106
Cdd:cd21219     6 ERAFRMWLN---SLGLDPLINNLYEDLRDGLVLLQVLDKIQPGCVnwkkvnkPKPLN--KFKKVENCNYAVDLAKKLGFS 80
                          90       100
                  ....*....|....*....|....*..
gi 672033739  107 LVNIGGTDIVDGNPKLTLGLLWSIILH 133
Cdd:cd21219    81 LVGIGGKDIADGNRKLTLALVWQLMRY 107
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
3052-3095 2.43e-14

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 69.39  E-value: 2.43e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 672033739   3052 KHQAKCNICKEcPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHK 3095
Cdd:smart00291    2 HHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
27-128 3.62e-14

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: 71.30  E-value: 3.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   27 DEHNDVQKKTFTKWINarfSKSGKPPINDMFSDLKDGRKLLDLLEGLTGTS--------LPKERGSTRVHALNNVNRVLQ 98
Cdd:cd21300     2 DAEGEREARVFTLWLN---SLDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYAVE 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 672033739   99 VLHQNNVELVNIGGTDIVDGNPKLTLGLLW 128
Cdd:cd21300    79 LGKQLGFSLVGIQGADITDGSRTLTLALVW 108
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
32-136 3.22e-13

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: 69.34  E-value: 3.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   32 VQKKTFTKWINARFsKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPK---ERGSTRVHALNNVNRVLQVLHQNNVELV 108
Cdd:cd21309    17 IQQNTFTRWCNEHL-KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
                          90       100
                  ....*....|....*....|....*...
gi 672033739  109 NIGGTDIVDGNPKLTLGLLWSIILHWQV 136
Cdd:cd21309    96 SIDSKAIVDGNLKLILGLVWTLILHYSI 123
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
32-136 1.34e-12

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: 67.42  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   32 VQKKTFTKWINARFsKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPK---ERGSTRVHALNNVNRVLQVLHQNNVELV 108
Cdd:cd21308    20 IQQNTFTRWCNEHL-KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
                          90       100
                  ....*....|....*....|....*...
gi 672033739  109 NIGGTDIVDGNPKLTLGLLWSIILHWQV 136
Cdd:cd21308    99 SIDSKAIVDGNLKLILGLIWTLILHYSI 126
SPEC smart00150
Spectrin repeats;
314-415 2.07e-12

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 65.81  E-value: 2.07e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739    314 YQIALEEVLTWLLSAEDTFQeQDDISDDVEDVKEQFATHETFMMELTAHQSSVGSVLQAGNQLMTQGtlsDEEEFEIQEQ 393
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG---HPDAEEIEER 78
                            90       100
                    ....*....|....*....|..
gi 672033739    394 MTLLNARWEALRVESMERQSRL 415
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
803-1015 5.96e-12

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: 67.86  E-value: 5.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  803 YFRQLDALEKTIRAKEEWLRDASFSESPQrSLPSLKDSCQRELTDLLGLHPRIEILCASCSAL-RSQPSVPGFVQQGFDD 881
Cdd:cd00176     5 FLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLiEEGHPDAEEIQERLEE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  882 LRRHYQAVQKALEEYQQQLENELKSQPepaYLDTLNTLKKMLSESEKAAQaSLSALNDPSAVEQALQEKKALDETLENQK 961
Cdd:cd00176    84 LNQRWEELRELAEERRQRLEEALDLQQ---FFRDADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 672033739  962 PTLHKLSEETKALEKNMLPDVGKTYRQEFDDAQGKWNKVKTKVSRDLRSLEEII 1015
Cdd:cd00176   160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1900-2069 6.55e-12

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: 67.86  E-value: 6.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1900 LKRIKDQLDRLGEQLAAVHEKQPDVIlEASGPEAIQIRDMLSQLNAKWDRVNRLYSDRRGSFARAVEEWKQFHcDLDDLT 1979
Cdd:cd00176    42 HEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1980 QWLSEAEDLLVGTCAPDGSLDLEKARTHQLELEDGLSSHQPCLIDVNQKGEDIVQRLRPSDASFLKDKLASLNQRWSALV 2059
Cdd:cd00176   120 QWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELL 199
                         170
                  ....*....|
gi 672033739 2060 AEVKDLQPRL 2069
Cdd:cd00176   200 ELAEERQKKL 209
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
156-252 1.23e-11

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: 64.32  E-value: 1.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  156 LLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTyLGIEKLLDPED-VA 234
Cdd:cd21256    19 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGIKSTLDINEmVR 97
                          90
                  ....*....|....*...
gi 672033739  235 VQLPDKKSIIMYLTSLFE 252
Cdd:cd21256    98 TERPDWQSVMTYVTAIYK 115
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
419-526 1.25e-11

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: 63.49  E-value: 1.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   419 LMELQKKQLQQLSGWLtltEERIQKMESLPVGDDLPSLQNLLEEHKSLQSDLEAEQVKVNSLTHMVVIVdENSGESATAV 498
Cdd:pfam00435    2 LLQQFFRDADDLESWI---EEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKL-IDEGHYASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 672033739   499 LEDQLQKLGERWTAVCRWTEERWNRLQE 526
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
35-128 1.35e-11

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: 63.79  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   35 KTFTKWINarfSKSGKPPINDMFSDLKDGRKLLDLLEGLTgtslPKERGSTRVH-----------ALNNVNRVLQVLHQN 103
Cdd:cd21298     9 KTYRNWMN---SLGVNPFVNHLYSDLRDGLVLLQLYDKIK----PGVVDWSRVNkpfkklganmkKIENCNYAVELGKKL 81
                          90       100
                  ....*....|....*....|....*
gi 672033739  104 NVELVNIGGTDIVDGNPKLTLGLLW 128
Cdd:cd21298    82 KFSLVGIGGKDIYDGNRTLTLALVW 106
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1235-1446 1.93e-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: 66.32  E-value: 1.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1235 WVELLHYLDLETSWLNTLEERMQSTE--ALPERAEAVHDALESLESVLRHPADNRTQIRELGQTLIDGGILD-DIISEKL 1311
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDygDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDaEEIQERL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1312 EAFNSRYEELSHLAESKQISLEKQLQVLRETDHMLQVLKESLGELDKQLTTYLTDRIDAFQLPQEAQK-IQAEISAHELT 1390
Cdd:cd00176    82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKeLEEELEAHEPR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 672033739 1391 LEELKKNVRPQPPTSPEGRTtrggsqmDLLQRKLREVSTKFQLFQKPANFEQRMLD 1446
Cdd:cd00176   162 LKSLNELAEELLEEGHPDAD-------EEIEEKLEELNERWEELLELAEERQKKLE 210
EFh_DYTN cd16243
EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate ...
2926-3030 2.67e-11

EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate orthologue of Drosophila DAH, which is involved in the synchronised cellularization of thousands of nuclei in the syncytial early fly embryo (a specialised form of cytokinesis). Dystrotelin is mainly expressed in the developing central nervous system (CNS) and adult nervous and muscular tissues. Heterologously expressed dystrotelin protein localizes spontaneously to the cytoplasmic membrane, and possibly to the endoplasmic reticulum (ER). Dystrotelin is not critical for mammalian development. It may be involved in other forms of cytokinesis. Its N-terminal region contains 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. The C-terminal region is extremely divergent. Unlike other superfamily members, dystrophin or dystrobrevin, the residues directly involved in beta-dystroglycan binding are not conserved in dystrotelin, which makes it unlikely that dystrotelin interacts with this ligand. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 320001  Cd Length: 163  Bit Score: 64.72  E-value: 2.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2926 LLNVYDTGRTGKIRVQSLKIGLMSLSKGLLEEKYRCLFK----EVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGgs 3001
Cdd:cd16243    58 LFRLYDREQTGFVSLRSVEAALIALSGDTLSAKYRALFQlyesGQGGSSGSITRSGLRVLLQDLSQIPAVVQESHVFG-- 135
                          90       100
                  ....*....|....*....|....*....
gi 672033739 3002 NIEPSVRSCFQQNNNkPEISVKEFIDWMR 3030
Cdd:cd16243   136 NVETAVRSCFSGVLT-ASISEEHFLSWLQ 163
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
156-252 4.83e-11

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: 62.35  E-value: 4.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  156 LLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTyLGIEKLLDPED-VA 234
Cdd:cd21257    13 LLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VGIKPSLELSEmMY 91
                          90
                  ....*....|....*...
gi 672033739  235 VQLPDKKSIIMYLTSLFE 252
Cdd:cd21257    92 TDRPDWQSVMQYVAQIYK 109
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2547-2786 4.86e-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: 4.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2547 KWNRLLASLEELIKWLNMKDEELKkQMPIGGDVPALQLQYDHCKVLRRELKEKEYSVLNAVDQARVFLADQPIEAPEepr 2626
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2627 rnpqskteltpeeraqkiakaMRKQSSEVREKWESLNAVTSTWQKQVGKALEKLRDLQgAVDDLDADMKEVEAVRNGWKP 2706
Cdd:cd00176    77 ---------------------IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASEDL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2707 VGDLliDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQL-SPLDLHPSPKMSRQLDDLNMRWKLLQVSVEDRLKQLQEA 2785
Cdd:cd00176   135 GKDL--ESVEELLKKHKELEEELEAHEPRLKSLNELAEELlEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212

                  .
gi 672033739 2786 H 2786
Cdd:cd00176   213 L 213
SPEC smart00150
Spectrin repeats;
425-525 6.36e-11

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 61.58  E-value: 6.36e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739    425 KQLQQLSGWLtltEERIQKMESLPVGDDLPSLQNLLEEHKSLQSDLEAEQVKVNSLTHMVVIVdENSGESATAVLEDQLQ 504
Cdd:smart00150    5 RDADELEAWL---EEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQL-IEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 672033739    505 KLGERWTAVCRWTEERWNRLQ 525
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
153-250 7.96e-11

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: 61.20  E-value: 7.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  153 EKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSP---TERLEHAFSKAHTY-LGIEKLL 228
Cdd:cd00014     1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLgLPELDLF 80
                          90       100
                  ....*....|....*....|..
gi 672033739  229 DPEDVaVQLPDKKSIIMYLTSL 250
Cdd:cd00014    81 EPEDL-YEKGNLKKVLGTLWAL 101
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
34-131 1.53e-10

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


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 61.05  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   34 KKTFTKWINARFSK----SGKPPIN----DMFSDLKDGRKLLDLLEGLTGTSLPkERGSTRVHALN------NVNRVLQV 99
Cdd:cd21217     3 KEAFVEHINSLLADdpdlKHLLPIDpdgdDLFEALRDGVLLCKLINKIVPGTID-ERKLNKKKPKNifeateNLNLALNA 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 672033739  100 LHQNNVELVNIGGTDIVDGNPKLTLGLLWSII 131
Cdd:cd21217    82 AKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1132-1336 2.12e-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: 63.23  E-value: 2.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1132 KDLAEMQEWMAQAEEDYLERDFEyKSPEELESAVEEMKRAKEDVLQKEVRVKILKDSIKLVAARVPSGGQELTSEFNEVL 1211
Cdd:cd00176     7 RDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1212 ESYQLLCNRIRGKCHTLEEVWSCWVELLHYLDLEtSWLNTLEERMQSTE--ALPERAEAVHDALESLESVLRHPADNRTQ 1289
Cdd:cd00176    86 QRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDlgKDLESVEELLKKHKELEEELEAHEPRLKS 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 672033739 1290 IRELGQTLIDGGILD--DIISEKLEAFNSRYEELSHLAESKQISLEKQL 1336
Cdd:cd00176   165 LNELAEELLEEGHPDadEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
33-133 2.29e-10

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: 60.59  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   33 QKKTFTKWINarfSKSGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPKERGST-----RVHALNNVNRVLQVLHQNNVEL 107
Cdd:cd21299     5 EERCFRLWIN---SLGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANKppikmPFKKVENCNQVVKIGKQLKFSL 81
                          90       100
                  ....*....|....*....|....*.
gi 672033739  108 VNIGGTDIVDGNPKLTLGLLWSIILH 133
Cdd:cd21299    82 VNVAGNDIVQGNKKLILALLWQLMRY 107
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
561-1343 2.45e-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: 67.00  E-value: 2.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   561 KDQKELGVSVRRLAILKEDMEMKRQTLDQL--------SEIGQDVGQLLSNPKASEKMNSDSEELTQRWDSLVQRLEDSS 632
Cdd:TIGR02168  222 LRELELALLVLRLEELREELEELQEELKEAeeeleeltAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   633 NQVTQAVAKLgmsqipqkDLLETVHVREQGMIKKPKQELPPPPPPKKRQIHVDVEAKKKFDATSAELQswilRSKAALQN 712
Cdd:TIGR02168  302 QQKQILRERL--------ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----ELEAELEE 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   713 TEMNEYKKSQETSGVRKKWKGLEKEQKEKIPQLDELNQTGQILQEQMGKeglLAEEINDVLER-VLLEWKMISQQLEDLG 791
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER---LQQEIEELLKKlEEAELKELQAELEELE 446
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   792 RKI-QLQEDINAYFRQLDALEKTIRAKEEWLRDAsfsESPQRSLPSLKDSCQRELTDLLGLHPRIEILCASCSALrsqPS 870
Cdd:TIGR02168  447 EELeELQEELERLEEALEELREELEEAEQALDAA---ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL---SG 520
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   871 VPGFVQQGFD-----------DLRRHYQAV-----QKALEEYQQQLENELK------------SQPEPAYLDTLNTLKKM 922
Cdd:TIGR02168  521 ILGVLSELISvdegyeaaieaALGGRLQAVvvenlNAAKKAIAFLKQNELGrvtflpldsikgTEIQGNDREILKNIEGF 600
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   923 LS------ESEKAAQASLSALNDPSAV----EQALQEKKALDE-----TLENQ------------KPTLHKLSEETKALE 975
Cdd:TIGR02168  601 LGvakdlvKFDPKLRKALSYLLGGVLVvddlDNALELAKKLRPgyrivTLDGDlvrpggvitggsAKTNSSILERRREIE 680
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   976 KNmlpdvgktyRQEFDDAQGKWNKVKTKVSRDLRSLEEIIPRLRDFKADSEVIEKWTNGVKDFLMKEQAAQGDTTALQRQ 1055
Cdd:TIGR02168  681 EL---------EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1056 LDQctTFANEIETIESSLKNLRDIETSLQRCPVTGVKtwVQTRLADYQSQLEKFSQEIDIQKSRLSDSQEKAMNLKKDLA 1135
Cdd:TIGR02168  752 LSK--ELTELEAEIEELEERLEEAEEELAEAEAEIEE--LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1136 EMQEWMAQAEE--DYLERDFEYKSP--EELESAVEEMKRAKEDVLQKEVRVKILKDSIKLVAARVPSGGQELTSEFNEVL 1211
Cdd:TIGR02168  828 SLERRIAATERrlEDLEEQIEELSEdiESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1212 ESYQllcnRIRGKCHTLEEvwscwveLLHYLDLEtswLNTLE-ERMQSTEALPERAEAVHDALESLES-VLRHPADNRTQ 1289
Cdd:TIGR02168  908 SKRS----ELRRELEELRE-------KLAQLELR---LEGLEvRIDNLQERLSEEYSLTLEEAEALENkIEDDEEEARRR 973
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 672033739  1290 IRELGQTLID-GGI-LDDIisEKLEAFNSRYEELSHLAESKQISLEKQLQVLRETD 1343
Cdd:TIGR02168  974 LKRLENKIKElGPVnLAAI--EEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
152-248 4.05e-10

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: 59.32  E-value: 4.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  152 SEKILLSWVrQTTRPysQVNVLNFTTSWTDGLAFNAVLHRHKPDLFS-WDrvvKMSPTERLEH---AFSKAHTYLGIEKL 227
Cdd:cd21229     4 PKKLMLAWL-QAVLP--ELKITNFSTDWNDGIALSALLDYCKPGLCPnWR---KLDPSNSLENcrrAMDLAKREFNIPMV 77
                          90       100
                  ....*....|....*....|.
gi 672033739  228 LDPEDVAVQLPDKKSIIMYLT 248
Cdd:cd21229    78 LSPEDLSSPHLDELSGMTYLS 98
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2217-2429 6.38e-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: 61.69  E-value: 6.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2217 DLDKTITELADWLVLIDQMLKSNiVTVGDVKEINKTVSRMKITKADLEQRHPQLDFVFTLAQNLKNkaSSSDLRTAITEK 2296
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2297 LEKLKTQWESTQHGVELRRQQLEDMVVDSLQWDDHREETEELmrkHEARFYMLQQARRDPLS---KQVSDNQLLLQELGS 2373
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWL---EEKEAALASEDLGKDLEsveELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 672033739 2374 GDGVIMAFDNVLQKLLEEYSSDDTRNVEETTEYLKTSWINLKQSIADRQSALEAEL 2429
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_PLS3_rpt3 cd21331
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
33-131 4.05e-09

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: 57.32  E-value: 4.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   33 QKKTFTKWINarfSKSGKPPINDMFSDLKDGRKLLDLLEGL-------TGTSLPKERGSTRVHALNNVNRVLQV-LHQNN 104
Cdd:cd21331    23 EERTFRNWMN---SLGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVELgKHPAK 99
                          90       100
                  ....*....|....*....|....*..
gi 672033739  105 VELVNIGGTDIVDGNPKLTLGLLWSII 131
Cdd:cd21331   100 FSLVGIGGQDLNDGNPTLTLALVWQLM 126
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
156-248 6.53e-09

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: 55.85  E-value: 6.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  156 LLSWVrQTTRPYSQVNvlNFTTSWTDGLAFNAVLHRHKPDLF-SWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPEDVA 234
Cdd:cd21230     6 LLGWI-QNKIPQLPIT--NFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLITPEEII 82
                          90
                  ....*....|....
gi 672033739  235 VQLPDKKSIIMYLT 248
Cdd:cd21230    83 NPNVDEMSVMTYLS 96
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
310-417 1.05e-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: 1.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   310 DLDSYQIALEEVLTWLLSAEDTFQEQDdISDDVEDVKEQFATHETFMMELTAHQSSVGSVLQAGNQLMTQGTLSDEeefE 389
Cdd:pfam00435    2 LLQQFFRDADDLESWIEEKEALLSSED-YGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASE---E 77
                           90       100
                   ....*....|....*....|....*...
gi 672033739   390 IQEQMTLLNARWEALRVESMERQSRLHD 417
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
33-133 1.33e-08

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: 55.00  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   33 QKKTFTKWINARFSK-SGKPPINDMFSDLKDGRKLLDLLEGLTGTSLPKERGSTRVHAL--NNVNRVLQVLHQNNVELVN 109
Cdd:cd21213     1 QLQAYVAWVNSQLKKrPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAErkENVEKVLQFMASKRIRMHQ 80
                          90       100
                  ....*....|....*....|....
gi 672033739  110 IGGTDIVDGNPKLTLGLLWSIILH 133
Cdd:cd21213    81 TSAKDIVDGNLKAIMRLILALAAH 104
EFh_DTNA cd16249
EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin ...
2875-3027 2.21e-08

EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin alpha (DTN-A), or dystrophin-related protein 3 (DRP-3), is the mammalian ortholog of the Torpedo 87 kDa postsynaptic protein that tightly associates with dystrophin. It is a cytoplasmic protein expressed predominantly in skeletal muscle, heart, lung, and brain. Alpha-dystrobrevin has been implicated in the regulation of acetylcholine receptor (AChR) aggregate density and patterning. It is also essential in the pathogenesis of dystrophin-dependent muscular dystrophies. It plays a critical role in the full functionality of dystrophin through increasing dystrophin's binding to the dystrophin-glycoprotein complex (DGC), and provides protection during cardiac stress. Alpha-dystrobrevin binds to the intermediate filament proteins syncoilin and beta-synemin, thereby linking the dystrophin-associated protein complex (DAPC) to the intermediate filament network. Moreover, alpha-dystrobrevin involves in cell signaling via interaction with other proteins such as syntrophin, a modular adaptor protein that coordinates the assembly of the signaling proteins nitric oxide synthase, stress-activated protein kinase-3, and Grb2 to the DAPC. Furthermore, alpha-dystrobrevin plays an important role in muscle function, as well as in nuclear morphology maintenance through specific interaction with the nuclear lamina component lamin B1. In addition, alpha-dystrobrevin is required in dystrophin-associated protein scaffolding in brain. Absence of glial alpha-dystrobrevin causes abnormalities of the blood-brain barrier and progressive brain edema. Alpha-dystrobrevin 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, alpha-dystrobrevin contain two syntrophin binding sites (SBSs).


Pssm-ID: 320007  Cd Length: 161  Bit Score: 56.06  E-value: 2.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2875 EVFKQHKLNQND--QLLSVPDVINCLTTTYdglEQLHKDL-----VNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 2947
Cdd:cd16249     7 EALRENALNNLDpnTELNVARLEAVLSTIF---YQLNKRMptthqINVEQSISLLLNFLLAAFDPEGHGKISVFAVKMAL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2948 MSLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQQnnnKPEISVKEFID 3027
Cdd:cd16249    84 ATLCGGKIMDKLRYIFSMISDSNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYT--EQSARSCFSQ---QKKVTLNGFLD 158
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
2679-2795 2.78e-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: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2679 KLRDLQGAVDDLDADMKEVEAVRNGWKPVGDLliDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLDLHPSPKMS 2758
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL--ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 672033739 2759 RQLDDLNMRWKLLQVSVEDRLKQLQEAHRDFGPSSQH 2795
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA 115
SPEC smart00150
Spectrin repeats;
1970-2070 3.50e-08

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 53.87  E-value: 3.50e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   1970 QFHCDLDDLTQWLSEAEDLLVGTCAPDGSLDLEKARTHQLELEDGLSSHQPCLIDVNQKGEDIVQRlRPSDASFLKDKLA 2049
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 672033739   2050 SLNQRWSALVAEVKDLQPRLK 2070
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
156-248 5.18e-08

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: 53.51  E-value: 5.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  156 LLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTYLGIEKLLDPEDVaV 235
Cdd:cd21196     8 LLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQAV-V 86
                          90
                  ....*....|...
gi 672033739  236 QLPDKKSIIMYLT 248
Cdd:cd21196    87 AGSDPLGLIAYLS 99
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
880-1827 5.81e-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: 58.91  E-value: 5.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   880 DDLRRHYQAVQKALEEYQQQLENeLKSQPEPA--YLDtlntlkkmLSESEKAAQASLSALNDPSAV---EQALQEKKALD 954
Cdd:TIGR02168  182 ERTRENLDRLEDILNELERQLKS-LERQAEKAerYKE--------LKAELRELELALLVLRLEELReelEELQEELKEAE 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   955 ETLENQKPTLHKLSEETKALEKNMLPDvgktyRQEFDDAQGKWNKVKTKVSRDLRSLEEIIPRLRDFKADSEVIEkwTNG 1034
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSEL-----EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE--AQL 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1035 VKDFLMKEQAAQgDTTALQRQLDQ----CTTFANEIETIESSLKNLRDIETSLQRcpvtgVKTWVQTRLADYQSQLEKFS 1110
Cdd:TIGR02168  326 EELESKLDELAE-ELAELEEKLEElkeeLESLEAELEELEAELEELESRLEELEE-----QLETLRSKVAQLELQIASLN 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1111 QEIDIQKSRLSDSQEKAMNLKKDLAEMQEWMAQAEEDYLERDFEYKSPE------ELESAVEEMKRAKEDVLQKEVRVKI 1184
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelqeELERLEEALEELREELEEAEQALDA 479
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1185 LKDSIKLVAARvpsggqeltsefnevLESYQLLCNRIRGKCHTLEEVWscwvellhyldLETSWLNTLEERMQSTEALPE 1264
Cdd:TIGR02168  480 AERELAQLQAR---------------LDSLERLQENLEGFSEGVKALL-----------KNQSGLSGILGVLSELISVDE 533
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1265 RAEAvhdaleSLESVLrhpadnrtqirelgqtlidGGILDDIISEKLEAFNsryEELSHLAESKQisleKQLQVLRETDH 1344
Cdd:TIGR02168  534 GYEA------AIEAAL-------------------GGRLQAVVVENLNAAK---KAIAFLKQNEL----GRVTFLPLDSI 581
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1345 MLQVLKESLGELDKQLTTYLTDRIDAFQLPQEAQKIQAEISAHELTLEELKKNVRPQPPTSPEGR-TTRGGSQmdllqrk 1423
Cdd:TIGR02168  582 KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRiVTLDGDL------- 654
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1424 lreVSTKFQLFQKPANFEQRMLDCKRVLDGVKAELHVLsvkdvdpdviqthLDKCMKLYKTLSEVKLEVETviktgrhiV 1503
Cdd:TIGR02168  655 ---VRPGGVITGGSAKTNSSILERRREIEELEEKIEEL-------------EEKIAELEKALAELRKELEE--------L 710
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1504 QKQQTDNPKGMDEQLTSLKVLYNDLGAQVTEGKQDLERASQLSRKLKKEAAILSEWLSTTEAELVQKSTSEGVIGDLDTE 1583
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1584 ISWAKNILKDLERRKVDLNAI-TESSAALQHLVVGSESVLEDtlcvlnagwsrvrtwTEDWRNTLLNHQNQLEVFDGHVA 1662
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAElTLLNEEAANLRERLESLERR---------------IAATERRLEDLEEQIEELSEDIE 855
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1663 HISTWLYQAEALLDEIEKKPASKQEEI------VKRLLSELSDASIQVENVREQAivlvnargsssRELvEPKLAELSKN 1736
Cdd:TIGR02168  856 SLAAEIEELEELIEELESELEALLNERasleeaLALLRSELEELSEELRELESKR-----------SEL-RRELEELREK 923
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1737 FEKVSQHINSAQMLI----------GQDPAGTVEAVGPFSDLESLESDIEnmLKVVEKHLD---PSNDEKMDEeraqIEE 1803
Cdd:TIGR02168  924 LAQLELRLEGLEVRIdnlqerlseeYSLTLEEAEALENKIEDDEEEARRR--LKRLENKIKelgPVNLAAIEE----YEE 997
                          970       980
                   ....*....|....*....|....
gi 672033739  1804 VLQRGEHLLHEpMEDSKKEKIRLQ 1827
Cdd:TIGR02168  998 LKERYDFLTAQ-KEDLTEAKETLE 1020
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
878-1493 6.96e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.54  E-value: 6.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  878 GFDDLRRHY---QAVQKALEEYQQQLENELKSQPEpayldtlntLKKMLSESEKAAQASLSALNDPSAVEQALQEK---- 950
Cdd:PRK03918  156 GLDDYENAYknlGEVIKEIKRRIERLEKFIKRTEN---------IEELIKEKEKELEEVLREINEISSELPELREElekl 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  951 KALDETLENQKPTLHKLSEETKALEKNMlpdvgktyRQEFDDAQGKWNKVKTKVSRdLRSLEEIIPRLRDFKADSEVIEK 1030
Cdd:PRK03918  227 EKEVKELEELKEEIEELEKELESLEGSK--------RKLEEKIRELEERIEELKKE-IEELEEKVKELKELKEKAEEYIK 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1031 wtngvkdflmkeqaaqgdttaLQRQLDQCTTFANEIETIESSLKNLRDIetslqrcpvtgvktwVQTRLADyqsqLEKFS 1110
Cdd:PRK03918  298 ---------------------LSEFYEEYLDELREIEKRLSRLEEEING---------------IEERIKE----LEEKE 337
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1111 QEIDIQKSRLSDSQEKAMNLKKDLAEMQEWMA-QAEEDYLERDFEYKSPEELESAVEEMKRAKEDVLQK----------- 1178
Cdd:PRK03918  338 ERLEELKKKLKELEKRLEELEERHELYEEAKAkKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEiskitarigel 417
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1179 EVRVKILKDSI---KLVAARVPSGGQELTSEFN-EVLESYQLLCNRIRGKCHTLEEVWSCWVELLHYLD---LETSWLNT 1251
Cdd:PRK03918  418 KKEIKELKKAIeelKKAKGKCPVCGRELTEEHRkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvlKKESELIK 497
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1252 LEERMQSTEALPERAEAVHdaLESLESVLRHPADNRTQIRELGQTLIdgGILDDIisEKLEAFNSRYEELS---HLAESK 1328
Cdd:PRK03918  498 LKELAEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKLIKLKGEIK--SLKKEL--EKLEELKKKLAELEkklDELEEE 571
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1329 QISLEKQLQVLRETDhmLQVLKESLGELDKQLTTYLTdridAFQLPQEAQKIQAEISAHELTLEELKKNVrpqppTSPEG 1408
Cdd:PRK03918  572 LAELLKELEELGFES--VEELEERLKELEPFYNEYLE----LKDAEKELEREEKELKKLEEELDKAFEEL-----AETEK 640
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1409 RTTRGGSQMDLLQRKLREvstkfqlfQKPANFEQRMLDCKRVLDGVKAELHVLSVKDvdpDVIQTHLDKCMKLYKTLSEV 1488
Cdd:PRK03918  641 RLEELRKELEELEKKYSE--------EEYEELREEYLELSRELAGLRAELEELEKRR---EEIKKTLEKLKEELEEREKA 709

                  ....*
gi 672033739 1489 KLEVE 1493
Cdd:PRK03918  710 KKELE 714
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
146-250 1.90e-07

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: 52.00  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  146 DLQQTNSEKILLSWVrQTTRPysQVNVLNFTTSWTDGLAFNAVLHRHKP----DLFSWDrvvKMSPTERLEHAFSKAHTY 221
Cdd:cd21314     6 DARKQTPKQRLLGWI-QNKVP--QLPITNFNRDWQDGKALGALVDNCAPglcpDWESWD---PNQPVQNAREAMQQADDW 79
                          90       100
                  ....*....|....*....|....*....
gi 672033739  222 LGIEKLLDPEDVAVQLPDKKSIIMYLTSL 250
Cdd:cd21314    80 LGVPQVIAPEEIVDPNVDEHSVMTYLSQF 108
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
3057-3103 1.93e-07

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 49.74  E-value: 1.93e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 672033739 3057 CNICKEcPIVGFRYRSLKHFNYDVCQSCFFSGRtaKGHKLHYPMVEY 3103
Cdd:cd02249     3 CDGCLK-PIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
247-419 2.14e-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: 54.37  E-value: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  247 LTSLFEVLPQQVTIDAIREVETLPRKYK--------KECEGEEINIQSAVLTEEGQSPRAETPSTVTEVDMDLDSYQIAL 318
Cdd:cd00176    16 LSEKEELLSSTDYGDDLESVEALLKKHEaleaelaaHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  319 EEVLTWLLSAEDTFQ-------------------EQDDISDDVEDVKEQFATHETFMMELTAHQSSVGSVLQAGNQLMTQ 379
Cdd:cd00176    96 EERRQRLEEALDLQQffrdaddleqwleekeaalASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEE 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 672033739  380 GTLSDEEefEIQEQMTLLNARWEALRVESMERQSRLHDAL 419
Cdd:cd00176   176 GHPDADE--EIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
912-1123 2.93e-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: 53.99  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  912 YLDTLNTLKKMLSESEKAAQaSLSALNDPSAVEQALQEKKALDETLENQKPTLHKLSEETKALEKNMLPDVGKTyRQEFD 991
Cdd:cd00176     5 FLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI-QERLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  992 DAQGKWNKVKTKVSRDLRSLEEIIpRLRDFKADSEVIEKWTNGVKDFLMKEQAAqGDTTALQRQLDQCTTFANEIETIES 1071
Cdd:cd00176    83 ELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALASEDLG-KDLESVEELLKKHKELEEELEAHEP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 672033739 1072 SLKNLRDIETSLQRCPVTGVKTWVQTRLADYQSQLEKFSQEIDIQKSRLSDS 1123
Cdd:cd00176   161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
53-131 3.29e-07

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: 51.44  E-value: 3.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   53 INDMFSDLKDG-R--KLLDLLEG----LTGTSLPKERGSTRVHalnNVNRVLQVLHQNNVELVNIGGT----DIVDGNPK 121
Cdd:cd21223    26 VTNLAVDLRDGvRlcRLVELLTGdwslLSKLRVPAISRLQKLH---NVEVALKALKEAGVLRGGDGGGitakDIVDGHRE 102
                          90
                  ....*....|
gi 672033739  122 LTLGLLWSII 131
Cdd:cd21223   103 KTLALLWRII 112
SPEC smart00150
Spectrin repeats;
2437-2542 3.66e-07

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.79  E-value: 3.66e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   2437 RDLENFVKWLQEAETTAnvladasQRENALQDSVLARQLRQQMLDIQAEIDAHNDIFKSIDGNRQKMVKAlgNSEEATML 2516
Cdd:smart00150    5 RDADELEAWLEEKEQLL-------ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE--GHPDAEEI 75
                            90       100
                    ....*....|....*....|....*.
gi 672033739   2517 QHRLDDMNQRWNDLKAKSASIRAHLE 2542
Cdd:smart00150   76 EERLEELNERWEELKELAEERRQKLE 101
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
2213-2598 9.81e-07

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 55.12  E-value: 9.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2213 SVPADLDKT---ITELADWLVLIDQMLKSNIVTVGDVKEINKTVSR-MKITKADLEQRHPQLDFVFTLAQNLKNKASSsd 2288
Cdd:pfam15921  465 SLTAQLESTkemLRKVVEELTAKKMTLESSERTVSDLTASLQEKERaIEATNAEITKLRSRVDLKLQELQHLKNEGDH-- 542
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2289 LRTAITEkLEKLKTQWESTQHGVELRRQQLEDMVvdslqwddhreeteELMRKHeARFYMLQQARRDPLSKQVSDNQLLL 2368
Cdd:pfam15921  543 LRNVQTE-CEALKLQMAEKDKVIEILRQQIENMT--------------QLVGQH-GRTAGAMQVEKAQLEKEINDRRLEL 606
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2369 QELgsgdgvimafdnvlqKLLEEYSSDDTRNVEETTEYLKTSWINLKQSIADRQSAL-------EAELRTVQTSRRDL-- 2439
Cdd:pfam15921  607 QEF---------------KILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVkdikqerDQLLNEVKTSRNELns 671
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2440 ---------ENFVKWLQEAETTANvladasqrenalqdsvlarQLRQQMLDIQAEIDAHNDIFKSIDGNRQKMVK-ALGN 2509
Cdd:pfam15921  672 lsedyevlkRNFRNKSEEMETTTN-------------------KLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKvAMGM 732
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2510 SEEAT--------------MLQHRLDDMNQRWNDLKAKSASIRAHLEASAEKWNRLLASLEElikwLNMKDEELKKQ--- 2572
Cdd:pfam15921  733 QKQITakrgqidalqskiqFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV----LRSQERRLKEKvan 808
                          410       420
                   ....*....|....*....|....*..
gi 672033739  2573 MPIGGDVPAlqLQYDHCK-VLRRELKE 2598
Cdd:pfam15921  809 MEVALDKAS--LQFAECQdIIQRQEQE 833
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
1547-1745 1.14e-06

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: 52.06  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1547 RKLKKEAAILSEWLSTTEAELvqksTSEGVIGDLDT-EISWAK--NILKDLERRKVDLNAITESSAALQHLVVGSESVLE 1623
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELL----SSTDYGDDLESvEALLKKheALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1624 DTLCVLNAGWSRVRTWTEDWRNtLLNHQNQLEVFDGHVAHISTWLYQAEALL--DEIEKKPASKQEEI--VKRLLSELSD 1699
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQ-RLEEALDLQQFFRDADDLEQWLEEKEAALasEDLGKDLESVEELLkkHKELEEELEA 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 672033739 1700 ASIQVENVREQAIVLVNARGSSSRELVEPKLAELSKNFEKVSQHIN 1745
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAE 203
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
729-1035 1.45e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.30  E-value: 1.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   729 KKWKGLEKEQKEKIPQLDELNQTGQILQEQMGKEGLLAEEINDVLERvllewkmISQQLEDLG--RKIQLQEDINAYFRQ 806
Cdd:TIGR02169  230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE-------LNKKIKDLGeeEQLRVKEKIGELEAE 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   807 LDALEKTIRAKEEWLRDAsfsESPQRSLPSLKDSCQRELTDLLG-----------LHPRIEILCASCSALRSQpsvPGFV 875
Cdd:TIGR02169  303 IASLERSIAEKERELEDA---EERLAKLEAEIDKLLAEIEELEReieeerkrrdkLTEEYAELKEELEDLRAE---LEEV 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   876 QQGFDDLRRHYQAVQKALEEYQQQLeNELKSQpepayLDTLNTLKKMLSEsekaAQASLSAlndpsAVEQALQEKKALDE 955
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEKLKREI-NELKRE-----LDRLQEELQRLSE----ELADLNA-----AIAGIEAKINELEE 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   956 TLENQKPTLHKLSEETKALEKNMlpdvgKTYRQEFDDAQGKWNKVKTKVSRDLRSLEE-------IIPRLRDFKADSEVI 1028
Cdd:TIGR02169  442 EKEDKALEIKKQEWKLEQLAADL-----SKYEQELYDLKEEYDRVEKELSKLQRELAEaeaqaraSEERVRGGRAVEEVL 516

                   ....*..
gi 672033739  1029 EKWTNGV 1035
Cdd:TIGR02169  517 KASIQGV 523
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1130-1230 1.49e-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: 49.24  E-value: 1.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1130 LKKDLAEMQEWMAQAEEDYLERDFEyKSPEELESAVEEMKRAKEDVLQKEVRVKILKDSIKLVAARVPSGGQELTSEFNE 1209
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSEDYG-KDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEE 84
                           90       100
                   ....*....|....*....|.
gi 672033739  1210 VLESYQLLCNRIRGKCHTLEE 1230
Cdd:pfam00435   85 LNERWEQLLELAAERKQKLEE 105
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
778-1395 1.50e-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: 54.29  E-value: 1.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   778 LEWKMISQQLEDLGRKI-QLQEDINAYFRQLDALEKTIRAKEEWLrdaSFSESPQRSLPSLKDSCQRELTDLLG----LH 852
Cdd:TIGR02168  225 LELALLVLRLEELREELeELQEELKEAEEELEELTAELQELEEKL---EELRLEVSELEEEIEELQKELYALANeisrLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   853 PRIEILCASCSALRSQPSVPGFVQQGFDDLRRHYQAVQKALEEYQQQLENELKSQPEPayLDTLNTLKKMLSESEKAAQA 932
Cdd:TIGR02168  302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE--LEELEAELEELESRLEELEE 379
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   933 SLSALNdpSAVEQALQEKKALDETLENQKPTLHKLSEETKALEKNMLPDVGKTYRQEFDDAQGKWNKVKTKVSRDLRSLE 1012
Cdd:TIGR02168  380 QLETLR--SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1013 EIIPRLrdfKADSEVIEKWTNGVKDFLMKEQAAQGDTTALQRQLDQCTTFANEIETIESSLKNLRD-------------- 1078
Cdd:TIGR02168  458 RLEEAL---EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGilgvlselisvdeg 534
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1079 ----IET----SLQRCPVTGVKTWVQ------------------TRLADYQSQ-------------------LEKFSQEI 1113
Cdd:TIGR02168  535 yeaaIEAalggRLQAVVVENLNAAKKaiaflkqnelgrvtflplDSIKGTEIQgndreilkniegflgvakdLVKFDPKL 614
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1114 DI------QKSRLSDSQEKAMNLKKDLAEMQEWM-----------------AQAEEDYLERDFEYkspEELESAVEEMKr 1170
Cdd:TIGR02168  615 RKalsyllGGVLVVDDLDNALELAKKLRPGYRIVtldgdlvrpggvitggsAKTNSSILERRREI---EELEEKIEELE- 690
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1171 AKEDVLQKEV-RVKILKDSIKLVAARVPSGGQELTSEFNEVLESY-------QLLCNRIRGKCHTLEEVWSCWVELLHYL 1242
Cdd:TIGR02168  691 EKIAELEKALaELRKELEELEEELEQLRKELEELSRQISALRKDLarleaevEQLEERIAQLSKELTELEAEIEELEERL 770
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1243 DLETSWLNTLEERMQSTEALPERA----------------------EAVHDALESLESVLRHPADNRTQIRELGQTLIDg 1300
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLkeelkalrealdelraeltllnEEAANLRERLESLERRIAATERRLEDLEEQIEE- 849
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1301 gilddiISEKLEAFNSRYEELSHLAESKQISLEKQLQVLRETDHMLQVLKESLGELDKQLTTYLTDRIDafqLPQEAQKI 1380
Cdd:TIGR02168  850 ------LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE---LRRELEEL 920
                          730
                   ....*....|....*
gi 672033739  1381 QAEISAHELTLEELK 1395
Cdd:TIGR02168  921 REKLAQLELRLEGLE 935
EFh_DTNB cd16250
EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin ...
2875-3029 1.54e-06

EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin beta (DTN-B), is a dystrophin-related protein that is restricted to non-muscle tissues and is abundantly expressed in brain, lung, kidney, and liver. It may be involved in regulating chromatin dynamics, possibly playing a role in neuronal differentiation, through the interactions with the high mobility group HMG20 proteins iBRAF/HMG20a and BRAF35 /HMG20b. It also binds to and represses the promoter of synapsin I, a neuronal differentiation gene. Moreover, beta-dystrobrevin functions as a kinesin-binding receptor involved in brain development via the association with the extracellular matrix components pancortins. Furthermore, beta-dystrobrevin binds directly to dystrophin and is a cytoplasmic component of the dystrophin-associated glycoprotein complex, a multimeric protein complex that links the extracellular matrix to the cortical actin cytoskeleton and acts as a scaffold for signaling proteins such as protein kinase A. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. Beta-dystrobrevin 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, beta-dystrobrevin contain two syntrophin binding sites (SBSs).


Pssm-ID: 320008  Cd Length: 161  Bit Score: 50.79  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2875 EVFKQHKLNQNDQL--LSVPDVINCLTTTYdglEQLHKDL-----VNVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGL 2947
Cdd:cd16250     7 EAFRDNGLNTLDHSteISVSRLETIISSIY---YQLNKRLpsthqISVEQSISLLLNFMIAAYDSEGHGKLTVFSVKAML 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2948 MSLSKGLLEEKYRCLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQLGEVAAFGGSniEPSVRSCFQQnnnKPEISVKEFID 3027
Cdd:cd16250    84 ATMCGGKILDKLRYTFSQMSDSNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYT--EHSVRTCFPQ---QKKIMLNMFLD 158

                  ..
gi 672033739 3028 WM 3029
Cdd:cd16250   159 TM 160
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
157-252 1.77e-06

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


Pssm-ID: 409034  Cd Length: 98  Bit Score: 48.84  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  157 LSWVRQTTrPYSQVNvlNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPTERLEHAFSKAHTyLGIEKLLDPEDVAVQ 236
Cdd:cd21185     7 LRWVRQLL-PDVDVN--NFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADP 82
                          90
                  ....*....|....*.
gi 672033739  237 LPDKKSIIMYLTSLFE 252
Cdd:cd21185    83 EVEHLGIMAYAAQLQK 98
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
2804-2832 1.85e-06

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 46.75  E-value: 1.85e-06
                          10        20
                  ....*....|....*....|....*....
gi 672033739 2804 PWQRSISHNKVPYYINHQTQTTCWDHPKM 2832
Cdd:cd00201     3 GWEERWDPDGRVYYYNHNTKETQWEDPRE 31
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1159-2012 6.67e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 6.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1159 EELESAVEEMKRAKEDVLQ-KEVRVKILKDSIKLVAARVPSGGQELtSEFNEVLESYQLLCNRIRGKCHTLEEVWSCWVE 1237
Cdd:TIGR02168  196 NELERQLKSLERQAEKAERyKELKAELRELELALLVLRLEELREEL-EELQEELKEAEEELEELTAELQELEEKLEELRL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1238 LLHYLDLEtswLNTLEERMQSTEALPERAEA-VHDALESLESVLRHPADNRTQIRELGQTLIdggilddiisEKLEAFNS 1316
Cdd:TIGR02168  275 EVSELEEE---IEELQKELYALANEISRLEQqKQILRERLANLERQLEELEAQLEELESKLD----------ELAEELAE 341
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1317 RYEELSHLAESKQiSLEKQLQVLRETdhmLQVLKESLGELDKQLTTYltdRIDAFQLPQEAQKIQAEISAHELTLEELKK 1396
Cdd:TIGR02168  342 LEEKLEELKEELE-SLEAELEELEAE---LEELESRLEELEEQLETL---RSKVAQLELQIASLNNEIERLEARLERLED 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1397 NVRPQPPTSPEGRTTRGGSQMDLLQRKLREV--------STKFQLFQKPANFEQRMLDCKRVLDGVKAELHVLSVKdvdP 1468
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAELKELQAELEELeeeleelqEELERLEEALEELREELEEAEQALDAAERELAQLQAR---L 491
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1469 DVIQTHLDKCMKLYKTLSEVKLEVETviKTGRHIVQKQQTDNPKGMdeQLTSLKVLYNDLGAQVTEGKQDLERASQLsrk 1548
Cdd:TIGR02168  492 DSLERLQENLEGFSEGVKALLKNQSG--LSGILGVLSELISVDEGY--EAAIEAALGGRLQAVVVENLNAAKKAIAF--- 564
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1549 LKKEAAILSEWLsttEAELVQKSTSEGVIGDLDTEISWAKNILKDLERRKVDLN----------AITESSA---ALQHLV 1615
Cdd:TIGR02168  565 LKQNELGRVTFL---PLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvLVVDDLDnalELAKKL 641
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1616 VGSESVLEDTLCVLNAGWSRVRTwTEDWRNTLLNHQNQLEVFDGHVAHISTWLYQAEALLDEIEKKPASKQEEIVKrLLS 1695
Cdd:TIGR02168  642 RPGYRIVTLDGDLVRPGGVITGG-SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ-LRK 719
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1696 ELSDASIQVENVREQAivlvnARGSSSRELVEPKLAELSKNFEKVSQHINSAQMLIGQDPAGTVEAVgpfSDLESLESDI 1775
Cdd:TIGR02168  720 ELEELSRQISALRKDL-----ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE---AEIEELEAQI 791
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1776 ENMLKVVEkhldpSNDEKMDEERAQIEEvLQRGEHLLHEPMEDSKKEKIRLQLLLLHTRYNKIKaipqrktiplssgims 1855
Cdd:TIGR02168  792 EQLKEELK-----ALREALDELRAELTL-LNEEAANLRERLESLERRIAATERRLEDLEEQIEE---------------- 849
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1856 salpadylveinkilLTLDDIELSLNIPELNTTVYEdfsfQEDSLKRIKDQLDRLGEQLAAVHEKQPDVILEasgpeaiq 1935
Cdd:TIGR02168  850 ---------------LSEDIESLAAEIEELEELIEE----LESELEALLNERASLEEALALLRSELEELSEE-------- 902
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1936 IRDMLSQLNAKwdrvNRLYSDRRGSFARAVEEWKQFHCDLDDLTQWLSEAEDLL---VGTCAPDGSLDLEKARTHQLELE 2012
Cdd:TIGR02168  903 LRELESKRSEL----RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeAEALENKIEDDEEEARRRLKRLE 978
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
405-1213 7.82e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 7.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   405 RVESMERQSRLHDALMELqKKQLQQLSGWLTLT--EERIQKMESLPVgddlpSLQNLLEEHKSLQSDLEAEQVKVNSLth 482
Cdd:TIGR02168  201 QLKSLERQAEKAERYKEL-KAELRELELALLVLrlEELREELEELQE-----ELKEAEEELEELTAELQELEEKLEEL-- 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   483 mvvivdensgESATAVLEDQLQKLGERWTAVCRWTEERWNRLQEINilwqellEEQCLLEAWLTEKEEALNKVQTGNFKD 562
Cdd:TIGR02168  273 ----------RLEVSELEEEIEELQKELYALANEISRLEQQKQILR-------ERLANLERQLEELEAQLEELESKLDEL 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   563 QKELGVSVRRLAILKEDMEMKRqtlDQLSEIGQDVGQLLSNPKASEKmnsDSEELTQRWDSLVQRLEDSSNQVTQAVAKL 642
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLE---AELEELEAELEELESRLEELEE---QLETLRSKVAQLELQIASLNNEIERLEARL 409
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   643 GMSQIPQKDLLETVHVREQGMIKKPKQELPPPPPPKKRQIHVDVEAKKKFDATSAELQSWILRSKAALQNTEMNEYKKSQ 722
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   723 ETSGVRKKWKGLEKEQKEKIPQLDELNQTGQILqeqmgkeGLLAEEINdvlerVLLEWkmiSQQLE-DLGRKIQ--LQED 799
Cdd:TIGR02168  490 RLDSLERLQENLEGFSEGVKALLKNQSGLSGIL-------GVLSELIS-----VDEGY---EAAIEaALGGRLQavVVEN 554
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   800 INAYFRQLDALEKTIRAKEEWL----RDASFSESPQRSLPSLKDSCQRELTDLLGLHPRIEILCASC-----------SA 864
Cdd:TIGR02168  555 LNAAKKAIAFLKQNELGRVTFLpldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddldNA 634
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   865 LRSQPSV---------------PGFVQQGFDDLRRH----------------------YQAVQKALEEYQQQLEnELKSQ 907
Cdd:TIGR02168  635 LELAKKLrpgyrivtldgdlvrPGGVITGGSAKTNSsilerrreieeleekieeleekIAELEKALAELRKELE-ELEEE 713
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   908 PEPAYLDTLNTLKKMLSESEKAAQASLSALNDPSAVEQALQEKKALDETLENQKPTLHKLSEETKALEKNMlpdvgKTYR 987
Cdd:TIGR02168  714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI-----EELE 788
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   988 QEFDDAQGKWNKVKtkvsRDLRSLEEIIPRLRDFKADSEviEKWTNGVKDFLMKEQAA----------QGDTTALQRQLD 1057
Cdd:TIGR02168  789 AQIEQLKEELKALR----EALDELRAELTLLNEEAANLR--ERLESLERRIAATERRLedleeqieelSEDIESLAAEIE 862
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1058 QCTTFANEIE-----------------------------TIESSLKNLRDIETSLQRCpvtgvktwvQTRLADYQSQLEK 1108
Cdd:TIGR02168  863 ELEELIEELEseleallnerasleealallrseleelseELRELESKRSELRRELEEL---------REKLAQLELRLEG 933
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1109 FSQEIDIQKSRLS----DSQEKAMNLKKDLaEMQEWMAQAEEDYLERDF------------EYKSPEE----LESAVEEM 1168
Cdd:TIGR02168  934 LEVRIDNLQERLSeeysLTLEEAEALENKI-EDDEEEARRRLKRLENKIkelgpvnlaaieEYEELKErydfLTAQKEDL 1012
                          890       900       910       920       930       940
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672033739  1169 KRAKEDVLQ------KEVRVKiLKDSIKLVAARVPS-------GGQ---ELTSEfNEVLES 1213
Cdd:TIGR02168 1013 TEAKETLEEaieeidREARER-FKDTFDQVNENFQRvfpklfgGGEaelRLTDP-EDLLEA 1071
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
148-250 9.26e-06

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


Pssm-ID: 409161  Cd Length: 114  Bit Score: 47.49  E-value: 9.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  148 QQTNSEKiLLSWVrQTTRPysQVNVLNFTTSWTDGLAFNAVLHRHKPDLF-SWDRVVKMSPTERLEHAFSKAHTYLGIEK 226
Cdd:cd21312    10 KQTPKQR-LLGWI-QNKLP--QLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQ 85
                          90       100
                  ....*....|....*....|....
gi 672033739  227 LLDPEDVAVQLPDKKSIIMYLTSL 250
Cdd:cd21312    86 VITPEEIVDPNVDEHSVMTYLSQF 109
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
2800-2832 1.42e-05

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 44.13  E-value: 1.42e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 672033739   2800 SVQLPWQRSISHNKVPYYINHQTQTTCWDHPKM 2832
Cdd:smart00456    1 PLPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
SPEC smart00150
Spectrin repeats;
1237-1333 1.70e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.17  E-value: 1.70e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   1237 ELLHYLDLETSWLNTLEERMQSTE--ALPERAEAVHDALESLESVLRHPADNRTQIRELGQTLIDGGILD-DIISEKLEA 1313
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDlgKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDaEEIEERLEE 81
                            90       100
                    ....*....|....*....|
gi 672033739   1314 FNSRYEELSHLAESKQISLE 1333
Cdd:smart00150   82 LNERWEELKELAEERRQKLE 101
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
146-250 1.91e-05

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: 46.24  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  146 DLQQTNSEKILLSWVrQTTRPYsqVNVLNFTTSWTDGLAFNAVLHRHKP----DLFSWDrvvKMSPTERLEHAFSKAHTY 221
Cdd:cd21313     3 DAKKQTPKQRLLGWI-QNKIPY--LPITNFNQNWQDGKALGALVDSCAPglcpDWESWD---PQKPVDNAREAMQQADDW 76
                          90       100
                  ....*....|....*....|....*....
gi 672033739  222 LGIEKLLDPEDVAVQLPDKKSIIMYLTSL 250
Cdd:cd21313    77 LGVPQVITPEEIIHPDVDEHSVMTYLSQF 105
SPEC smart00150
Spectrin repeats;
2683-2783 1.91e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.78  E-value: 1.91e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   2683 LQGAVDDLDADMKEVEAVRNGWKPVGDLliDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLDLHPSPKMSRQLD 2762
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASEDLGKDL--ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
                            90       100
                    ....*....|....*....|.
gi 672033739   2763 DLNMRWKLLQVSVEDRLKQLQ 2783
Cdd:smart00150   81 ELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
1966-2058 2.02e-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: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1966 EEWKQFHCDLDDLTQWLSEAEDLLVgtcAPDGSLDLEKA----RTHQlELEDGLSSHQPCLIDVNQKGEDIVQRlRPSDA 2041
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLS---SEDYGKDLESVqallKKHK-ALEAELAAHQDRVEALNELAEKLIDE-GHYAS 75
                           90
                   ....*....|....*..
gi 672033739  2042 SFLKDKLASLNQRWSAL 2058
Cdd:pfam00435   76 EEIQERLEELNERWEQL 92
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
543-646 2.47e-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: 48.21  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  543 AWLTEKEEALNKVQTGnfKDQKELGVSVRRLAILKEDMEMKRQTLDQLSEIGQDVGQllSNPKASEKMNSDSEELTQRWD 622
Cdd:cd00176    14 AWLSEKEELLSSTDYG--DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQERLEELNQRWE 89
                          90       100
                  ....*....|....*....|....
gi 672033739  623 SLVQRLEDSSNQVTQAVAKLGMSQ 646
Cdd:cd00176    90 ELRELAEERRQRLEEALDLQQFFR 113
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1004-1919 2.57e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1004 VSRDLRSLE---EIIPRLRDFKADSEVIEKW--TNGVKDFLMKEQAAQGDTTALQRQLDQCTTfanEIETIESSLKNLRD 1078
Cdd:TIGR02168  198 LERQLKSLErqaEKAERYKELKAELRELELAllVLRLEELREELEELQEELKEAEEELEELTA---ELQELEEKLEELRL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1079 IETSLQRcpvtgvktwvqtRLADYQSQLEKFSQEIDIQKSRLSDSQEKAMNLKKDLAEMQEWMAQAEedylerdfeyKSP 1158
Cdd:TIGR02168  275 EVSELEE------------EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE----------SKL 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1159 EELESAVEEMKrAKEDVLQKEVrvkilkdsiklvaarvpsggQELTSEFNEVLESYQLLCNRIRGKCHTLEEVWSCWVEL 1238
Cdd:TIGR02168  333 DELAEELAELE-EKLEELKEEL--------------------ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1239 LHYLDLETSWLNTLEERMQSTEalpERAEAVHDALESLESVLrhpadNRTQIRELGQTLIDGGILDDIISEKLEAFNSRY 1318
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLE---DRRERLQQEIEELLKKL-----EEAELKELQAELEELEEELEELQEELERLEEAL 463
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1319 EELSHL---AESKQISLEKQLQVLRETDHMLQVLKESLGELDKQLTTYLTDRID-AFQLPQEAQKIQAEiSAHELTLEel 1394
Cdd:TIGR02168  464 EELREEleeAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlSGILGVLSELISVD-EGYEAAIE-- 540
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1395 kknvrpqpptspegrTTRGGSQMDLLQRKLREVSTKFQlFQKPANFEQRMLdckRVLDGVKAelhvlSVKDVDPDVIQTH 1474
Cdd:TIGR02168  541 ---------------AALGGRLQAVVVENLNAAKKAIA-FLKQNELGRVTF---LPLDSIKG-----TEIQGNDREILKN 596
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1475 LDKCMKLYKTLSEVKLEVETVIKT--GRHIVqkqqTDNPKGMDEQLTSLKVLYN------DL----GAQVteGKQDLERA 1542
Cdd:TIGR02168  597 IEGFLGVAKDLVKFDPKLRKALSYllGGVLV----VDDLDNALELAKKLRPGYRivtldgDLvrpgGVIT--GGSAKTNS 670
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1543 SQLSRKlkKEAAILSEWLSTTEAElvqkstsegvIGDLDTEISWAKNILKDLERRKVDLNAITESSAALQHLVVGSESVL 1622
Cdd:TIGR02168  671 SILERR--REIEELEEKIEELEEK----------IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1623 EdtlcvlnagwSRVRTWTEDWRN---TLLNHQNQLEVFDGHVAHISTWLYQAEALLDEIEKKPASKQEEIVKrLLSELSD 1699
Cdd:TIGR02168  739 E----------AEVEQLEERIAQlskELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-LREALDE 807
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1700 ASIQVENVREQAIVLVNARGSSSRELVEPK--LAELSKNFEKVSQHINSAQmligqdpagtveavgpfSDLESLESDIEN 1777
Cdd:TIGR02168  808 LRAELTLLNEEAANLRERLESLERRIAATErrLEDLEEQIEELSEDIESLA-----------------AEIEELEELIEE 870
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1778 MLKVVEKHLdpsndekmdEERAQIEEVLQRGEHLLHEPME-----DSKKEKIRLQLLLLHTRYNKIKAIPQRKTIPLSSG 1852
Cdd:TIGR02168  871 LESELEALL---------NERASLEEALALLRSELEELSEelrelESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
                          890       900       910       920       930       940
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672033739  1853 ImsSALPADYLveinkilLTLDDIElslnipELNTTVYEDFSFQEDSLKRIKDQLDRLGE-QLAAVHE 1919
Cdd:TIGR02168  942 Q--ERLSEEYS-------LTLEEAE------ALENKIEDDEEEARRRLKRLENKIKELGPvNLAAIEE 994
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2293-2696 2.91e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 2.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2293 ITEKLEKLKTQWESTQHGVELRRQQLEDMvvdSLQWDDHREETEELMRKHEARFYMLQQARR--DPLSKQVSDNQLLLQE 2370
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEEL---EEELEQLRKELEELSRQISALRKDLARLEAevEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2371 LgsgDGVIMAFDNVLQKLLEEYSSDDTR--NVEETTEYLKTSWINLKQSIADRQSALEAELRTVQTSRRDLENFVKWLQE 2448
Cdd:TIGR02168  759 L---EAEIEELEERLEEAEEELAEAEAEieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2449 AETTANVLADASQRENALQDSVLA--RQLRQQMLDIQAEIDAHNDIFKSIDGNRQKMVKALGNseeatmLQHRLDDMNQR 2526
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEE------LSEELRELESK 909
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2527 WNDLKAKSASIRAHLEASAEKWNRLLASLEELIKWLN----MKDEELKKQMPigGDVPALQLQYDHCKVLRRELKEkeys 2602
Cdd:TIGR02168  910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeeysLTLEEAEALEN--KIEDDEEEARRRLKRLENKIKE---- 983
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2603 vLNAVDqarvfladqpIEAPEEPRrnpqskteltpeeraqkiakamrkqssEVREKWESLNavtstwqKQVGKALEKLRD 2682
Cdd:TIGR02168  984 -LGPVN----------LAAIEEYE---------------------------ELKERYDFLT-------AQKEDLTEAKET 1018
                          410
                   ....*....|....
gi 672033739  2683 LQGAVDDLDADMKE 2696
Cdd:TIGR02168 1019 LEEAIEEIDREARE 1032
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
30-131 3.39e-05

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


Pssm-ID: 409143  Cd Length: 125  Bit Score: 45.90  E-value: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   30 NDVQKKTFTKWINARFSksGKPPIND----------MFSDLKDGRKLLDLLEGLTGTSLPKERG---STRVHALNNvnrv 96
Cdd:cd21294     4 NEDERREFTKHINAVLA--GDPDVGSrlpfptdtfqLFDECKDGLVLSKLINDSVPDTIDERVLnkpPRKNKPLNN---- 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 672033739   97 LQVLHQNNV----------ELVNIGGTDIVDGNPKLTLGLLWSII 131
Cdd:cd21294    78 FQMIENNNIvinsakaigcSVVNIGAGDIIEGREHLILGLIWQII 122
SPEC smart00150
Spectrin repeats;
2218-2319 3.56e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 45.01  E-value: 3.56e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   2218 LDKTITELADWLVLIDQMLKSNIVTvGDVKEINKTVSRMKITKADLEQRHPQLDFVFTLAQNLKNkaSSSDLRTAITEKL 2297
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASEDLG-KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERL 79
                            90       100
                    ....*....|....*....|..
gi 672033739   2298 EKLKTQWESTQHGVELRRQQLE 2319
Cdd:smart00150   80 EELNERWEELKELAEERRQKLE 101
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
2804-2830 4.06e-05

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 42.88  E-value: 4.06e-05
                           10        20
                   ....*....|....*....|....*..
gi 672033739  2804 PWQRSISHNKVPYYINHQTQTTCWDHP 2830
Cdd:pfam00397    4 GWEERWDPDGRVYYYNHETGETQWEKP 30
CH_PLS2_rpt3 cd21330
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
33-131 4.11e-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: 4.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   33 QKKTFTKWINarfSKSGKPPINDMFSDLKDGRKLLDLLEGLTG-------TSLPKERGSTRVHALNNVNRVLQV-LHQNN 104
Cdd:cd21330    14 EERTFRNWMN---SLGVNPRVNHLYSDLSDALVIFQLYEKIKVpvdwnrvNKPPYPKLGENMKKLENCNYAVELgKNKAK 90
                          90       100
                  ....*....|....*....|....*..
gi 672033739  105 VELVNIGGTDIVDGNPKLTLGLLWSII 131
Cdd:cd21330    91 FSLVGIAGQDLNEGNRTLTLALIWQLM 117
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
3057-3100 4.25e-05

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 43.49  E-value: 4.25e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 672033739 3057 CNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPM 3100
Cdd:cd02338     3 CDGCGKSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPM 46
CH_PLS1_rpt3 cd21329
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
33-131 4.77e-05

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


Pssm-ID: 409178  Cd Length: 118  Bit Score: 45.36  E-value: 4.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   33 QKKTFTKWINarfSKSGKPPINDMFSDLKDGRKLLDLLEGltgTSLPKERGST----------RVHALNNVNRVLQV-LH 101
Cdd:cd21329     7 EERTFRNWMN---SLGVNPYVNHLYSDLCDALVIFQLYEM---TRVPVDWGHVnkppypalggNMKKIENCNYAVELgKN 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 672033739  102 QNNVELVNIGGTDIVDGNPKLTLGLLWSII 131
Cdd:cd21329    81 KAKFSLVGIAGSDLNEGNKTLTLALIWQLM 110
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
35-130 5.67e-05

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: 44.64  E-value: 5.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   35 KTFTKWINARFSKSGKPP-INDMFSDLKDGRKLLDLLEGLTGTSLPKERGSTRVHA--LNNVNRVLQVLHQNNVELVNIG 111
Cdd:cd21286     3 KIYTDWANHYLAKSGHKRlIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSqmIENVDVCLSFLAARGVNVQGLS 82
                          90
                  ....*....|....*....
gi 672033739  112 GTDIVDGNPKLTLGLLWSI 130
Cdd:cd21286    83 AEEIRNGNLKAILGLFFSL 101
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
142-251 5.95e-05

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: 44.98  E-value: 5.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  142 DIMSDLQQTNSEKILLSWV----RQTTRPYSQVNvlNFTTSWTDGLAFNAVLHRHKPDLFswDRVVKMS------PTERL 211
Cdd:cd21218     1 ETLESLLYLPPEEILLRWVnyhlKKAGPTKKRVT--NFSSDLKDGEVYALLLHSLAPELC--DKELVLEvlseedLEKRA 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 672033739  212 EHAFSKAHTyLGIEKLLDPEDVAvqLPDKKSIIMYLTSLF 251
Cdd:cd21218    77 EKVLQAAEK-LGCKYFLTPEDIV--SGNPRLNLAFVATLF 113
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
889-1566 6.75e-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: 48.96  E-value: 6.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   889 VQKALEEYQQQLE---------NELKSQPEPAYLDTLNTLKKMLSEsekaAQASLSALNDPSAVEQALQEKkaLDETLEN 959
Cdd:pfam15921   76 IERVLEEYSHQVKdlqrrlnesNELHEKQKFYLRQSVIDLQTKLQE----MQMERDAMADIRRRESQSQED--LRNQLQN 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   960 qkpTLHKLsEETKALEKNMLPDVGKTYRQ--------------------EFDDAQGK------------WNKVKTKVSRD 1007
Cdd:pfam15921  150 ---TVHEL-EAAKCLKEDMLEDSNTQIEQlrkmmlshegvlqeirsilvDFEEASGKkiyehdsmstmhFRSLGSAISKI 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1008 LRSLE--------EIIP---RLRDFKADSE-----VIEKWTNGVKDFLMK-EQAAQGDTTALQRQLDQCTTFANEIETIE 1070
Cdd:pfam15921  226 LRELDteisylkgRIFPvedQLEALKSESQnkielLLQQHQDRIEQLISEhEVEITGLTEKASSARSQANSIQSQLEIIQ 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1071 SSLKN--------LRDIETSlqrcpVTGVKTWVQTRLADYQSQLEKFSQEIDIQKSRLSDSQEKAMNLKKDLAEMQEWMA 1142
Cdd:pfam15921  306 EQARNqnsmymrqLSDLEST-----VSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQ 380
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1143 QAEEDYLERDfeykspEELESAVEEMKRAKEDVLQKEVRVKILK---DSIKLVAARVPSGGQELTSEFNEVLESyQLLCn 1219
Cdd:pfam15921  381 KLLADLHKRE------KELSLEKEQNKRLWDRDTGNSITIDHLRrelDDRNMEVQRLEALLKAMKSECQGQMER-QMAA- 452
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1220 rIRGKCHTLEEVWScwveLLHYLDLETSWLNTLEERMQSTEALPERAE-AVHDALESLESVLRHPADNRTQIRELGQTLi 1298
Cdd:pfam15921  453 -IQGKNESLEKVSS----LTAQLESTKEMLRKVVEELTAKKMTLESSErTVSDLTASLQEKERAIEATNAEITKLRSRV- 526
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1299 dggildDIISEKLEAFNSRYEELSHL-AESKQISLEkqlqvLRETDHMLQVLKESLGELdKQLTTYLTDRIDAFQLpqEA 1377
Cdd:pfam15921  527 ------DLKLQELQHLKNEGDHLRNVqTECEALKLQ-----MAEKDKVIEILRQQIENM-TQLVGQHGRTAGAMQV--EK 592
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1378 QKIQAEISAHELTLEELK--KNVRPQPPTSPEGRTTrggsqmDLLQRKLREVSTKFQLFQKPANFEQRMldcKRVLDGVK 1455
Cdd:pfam15921  593 AQLEKEINDRRLELQEFKilKDKKDAKIRELEARVS------DLELEKVKLVNAGSERLRAVKDIKQER---DQLLNEVK 663
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1456 AELHVLSVKDVDPDVIQTHL-DKCMKLYKTLSEVKLEVETV---IKTGRHIVQKQQTDN------PKGMDEQLTSLKVLY 1525
Cdd:pfam15921  664 TSRNELNSLSEDYEVLKRNFrNKSEEMETTTNKLKMQLKSAqseLEQTRNTLKSMEGSDghamkvAMGMQKQITAKRGQI 743
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|.
gi 672033739  1526 NDLGAQVTEGKQDLERASQLSRKLKKEAAILSEWLSTTEAE 1566
Cdd:pfam15921  744 DALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE 784
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
24-131 1.00e-04

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: 44.96  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   24 SRSDEhndvQKKTFTKWINARFSKSG--------KPPINDMFSDLKDGRklldLLEGLTGTSLPK---ERgstrvhALNN 92
Cdd:cd21292    20 SYSEE----EKVAFVNWINKNLGDDPdckhllpmDPNTDDLFEKVKDGI----LLCKMINLSVPDtidER------AINK 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 672033739   93 VNRVLQVLHQN-NVEL----------VNIGGTDIVDGNPKLTLGLLWSII 131
Cdd:cd21292    86 KKLTVFTIHENlTLALnsasaigcnvVNIGAEDLKEGKPHLVLGLLWQII 135
CH_PLS1_rpt1 cd21323
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ...
22-131 1.22e-04

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: 45.03  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   22 IKSRSDEHN--DVQKKTFTKWINARFSksGKP------PIN----DMFSDLKDGRKLLDLLEgLTGTSLPKERGS----- 84
Cdd:cd21323    12 ISSEGTQHSysEEEKVAFVNWINKALE--GDPdckhvvPMNptdeSLFKSLADGILLCKMIN-LSQPDTIDERAInkkkl 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 672033739   85 TRVHALNNVNRVLQVLHQNNVELVNIGGTDIVDGNPKLTLGLLWSII 131
Cdd:cd21323    89 TPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQII 135
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2678-2784 2.10e-04

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 43.08  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2678 EKLRDLQGAVDDLDADMKEVEAVrNGWKPVGDLLiDSLQDHIEKTLAFREEIAPINLKVKTMNDLSSQLSPLDLHPSPKM 2757
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEAL-LSSEDYGKDL-ESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEI 78
                           90       100
                   ....*....|....*....|....*..
gi 672033739  2758 SRQLDDLNMRWKLLQVSVEDRLKQLQE 2784
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
39-130 3.21e-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: 42.67  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   39 KWINARFSKSG--KPPINDMFSDLKDGRKLLDLLEGLTGTSLPKE---RGSTRVHALNNVNRVLQVLHQNNVELVnIGGT 113
Cdd:cd21218    17 RWVNYHLKKAGptKKRVTNFSSDLKDGEVYALLLHSLAPELCDKElvlEVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPE 95
                          90
                  ....*....|....*..
gi 672033739  114 DIVDGNPKLTLGLLWSI 130
Cdd:cd21218    96 DIVSGNPRLNLAFVATL 112
SPEC smart00150
Spectrin repeats;
543-630 3.47e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 42.32  E-value: 3.47e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739    543 AWLTEKEEALNKVQTGnfKDQKELGVSVRRLAILKEDMEMKRQTLDQLSEIGQDVGQllSNPKASEKMNSDSEELTQRWD 622
Cdd:smart00150   12 AWLEEKEQLLASEDLG--KDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE--EGHPDAEEIEERLEELNERWE 87

                    ....*...
gi 672033739    623 SLVQRLED 630
Cdd:smart00150   88 ELKELAEE 95
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
3057-3103 4.16e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 40.52  E-value: 4.16e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 672033739 3057 CNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRtakgHKLHYPMVEY 3103
Cdd:cd02339     3 CDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDK----HDLEHRFYRY 45
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
680-1190 4.30e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 4.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  680 RQIHVDVEAKKKFDATSAELQSWILRSKAALQNTEMNEYKKSQETSGVRKKWKGLEKEQKEKIPQLDELNQTGQILQEQM 759
Cdd:PRK03918  172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  760 GKEGLLAEEINDvLERVLLEWKMISQQLEDLGRKI-QLQEDINAYfrqldalEKTIRAKEEWLRDASFSESPQRSLPSLK 838
Cdd:PRK03918  252 GSKRKLEEKIRE-LEERIEELKKEIEELEEKVKELkELKEKAEEY-------IKLSEFYEEYLDELREIEKRLSRLEEEI 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  839 DSCQRELTDLLGLHPRIEILcascsalrsqpsvpgfvQQGFDDLRRHYQAVQKALEEYQQ--QLENELKSQPEPAYLDTL 916
Cdd:PRK03918  324 NGIEERIKELEEKEERLEEL-----------------KKKLKELEKRLEELEERHELYEEakAKKEELERLKKRLTGLTP 386
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  917 NTLKKMLSESEKAA---QASLSALNDP-SAVEQALQE-KKALDE---------------TLENQKPTLHKLSEETKALEK 976
Cdd:PRK03918  387 EKLEKELEELEKAKeeiEEEISKITARiGELKKEIKElKKAIEElkkakgkcpvcgrelTEEHRKELLEEYTAELKRIEK 466
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  977 NMlpdvgktyrQEFDDAQGKWNKVKTKV------SRDLRSLEEIIPRLRDFKADSEVI--EKWTNGVKDF-LMKEQAA-- 1045
Cdd:PRK03918  467 EL---------KEIEEKERKLRKELRELekvlkkESELIKLKELAEQLKELEEKLKKYnlEELEKKAEEYeKLKEKLIkl 537
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1046 QGDTTALQRQLDQCTTFANEIETIESSLKN----LRDIETSLQRCPVTGVKTWVQT------------RLADYQSQLEKF 1109
Cdd:PRK03918  538 KGEIKSLKKELEKLEELKKKLAELEKKLDEleeeLAELLKELEELGFESVEELEERlkelepfyneylELKDAEKELERE 617
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1110 SQEIDIQKSRLSDSQEKAMNLKKDLAEMQEWMAQAEEDYLERDFEYKSpEELESAVEEMKRAKEDVLQKEVRVKILKDSI 1189
Cdd:PRK03918  618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR-EEYLELSRELAGLRAELEELEKRREEIKKTL 696

                  .
gi 672033739 1190 K 1190
Cdd:PRK03918  697 E 697
SPEC smart00150
Spectrin repeats;
2550-2623 4.83e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 41.93  E-value: 4.83e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672033739   2550 RLLASLEELIKWLNMKdEELKKQMPIGGDVPALQLQYDHCKVLRRELKEKEYSVLNAVDQARVFLADQPIEAPE 2623
Cdd:smart00150    2 QFLRDADELEAWLEEK-EQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE 74
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2288-2613 5.74e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 5.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2288 DLRTAITEKLEKLKTQWESTQHGVELrRQQLEDMVVDSL--QWDDHREETEELMRKHEArfymlQQARRDPLSKQVSDNQ 2365
Cdd:TIGR02168  193 DILNELERQLKSLERQAEKAERYKEL-KAELRELELALLvlRLEELREELEELQEELKE-----AEEELEELTAELQELE 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2366 LLLQELGSGDGVIMAFDNVLQKLLEEYSSdDTRNVEETTEYLKTSWINLKQSIADRQSALEAELRTVQTSRRDL------ 2439
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALAN-EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELaeleek 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2440 -----ENFVKWLQEAETTANVLADASQRENALQDSVLAR-----QLRQQMLDIQAEIDAHNDIFKSIDGNRQKmvkalgN 2509
Cdd:TIGR02168  346 leelkEELESLEAELEELEAELEELESRLEELEEQLETLrskvaQLELQIASLNNEIERLEARLERLEDRRER------L 419
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2510 SEEATMLQHRLDdmNQRWNDLKAKSASIRAHLEASAEKWNRLLASLEELIKWLNMKDEELKKqmpIGGDVPALQLQYDHC 2589
Cdd:TIGR02168  420 QQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA---AERELAQLQARLDSL 494
                          330       340
                   ....*....|....*....|....
gi 672033739  2590 KVLRRELKEKEYSVLNAVDQARVF 2613
Cdd:TIGR02168  495 ERLQENLEGFSEGVKALLKNQSGL 518
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1094-1360 7.81e-04

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: 7.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1094 WVQTRLADYQSQLEKFSQEIDIQKSRLSDSQEKAMNLKKDLAEMQEWMAQAEEDYLERDFEYKSPE-ELESAVEEMKRAK 1172
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqDIARLEERRRELE 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1173 EDVLQKEVRVKILKDSIKLVAARVpsggQELTSEFNEVLESYQLLCNRIRGKCHTLEEvwscwvELLHYLDLETSWLNTL 1252
Cdd:COG1196   316 ERLEELEEELAELEEELEELEEEL----EELEEELEEAEEELEEAEAELAEAEEALLE------AEAELAEAEEELEELA 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1253 EERMQSTEALPERAEAVHDALESLESVLRHPADNRTQIRELGQTLIDGGILDDIISEKLEAFNSRYEELSHLAESKQISL 1332
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
                         250       260
                  ....*....|....*....|....*...
gi 672033739 1333 EKQLQVLRETDHMLQVLKESLGELDKQL 1360
Cdd:COG1196   466 AELLEEAALLEAALAELLEELAEAAARL 493
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
3057-3102 8.86e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.


Pssm-ID: 239085  Cd Length: 49  Bit Score: 39.50  E-value: 8.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 672033739 3057 CNICKECPIVGFRYRSLKHFNYDVCQSCFFSGRTAKGHKLHYPMVE 3102
Cdd:cd02345     3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYE 48
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
156-254 1.01e-03

second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409073 [Multi-domain]  Cd Length: 138  Bit Score: 41.90  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  156 LLSWVRQTTRPYSqVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRvVKMSPT--------------------------- 208
Cdd:cd21224     5 LLKWCQAVCAHYG-VKVENFTVSFADGRALCYLIHHYLPSLLPLDA-IRQPTTqtvdraqdeaedfwvaefspstgdsgl 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 672033739  209 --ERLEHA---FSKAHT---YLG-IEKLLDPEDVAVQLPDKKSIIMYLTSLFEVL 254
Cdd:cd21224    83 ssELLANEkrnFKLVQQavaELGgVPALLRASDMSNTIPDEKVVILFLSYLCARL 137
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
29-131 1.09e-03

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: 42.35  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   29 HNDVQKKTFTKWIN--------ARFSKSGKPPINDMFSDLKDGRKLLDLLEgLTGTSLPKERGSTRVHAL-----NNVNR 95
Cdd:cd21325    21 YSEEEKYAFVNWINkalendpdCRHVIPMNPNTDDLFKAVGDGIVLCKMIN-LSVPDTIDERAINKKKLTpfiiqENLNL 99
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 672033739   96 VLQVLHQNNVELVNIGGTDIVDGNPKLTLGLLWSII 131
Cdd:cd21325   100 ALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 135
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
767-997 1.11e-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: 44.37  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  767 EEINDVLERVLLEWKMISQQLEDLGRKIQLQEdinayfRQLDALEKTIRAKEEWLRDASFSESP-QRSLPSLKDSCQREL 845
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALA------RRIRALEQELAALEAELAELEKEIAElRAELEAQKEELAELL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  846 TDL--LGLHPRIEILCASCSALRSQPSVP--GFVQQGFDDLRRHYQAVQKALEEYQQQLENELKSQpePAYLDTLNTLKK 921
Cdd:COG4942   111 RALyrLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAEL--EALLAELEEERA 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672033739  922 MLSESEKAAQASLSALN-DPSAVEQALQEKKALDETLENQkptLHKLSEETKALEKnmlpdvgKTYRQEFDDAQGKW 997
Cdd:COG4942   189 ALEALKAERQKLLARLEkELAELAAELAELQQEAEELEAL---IARLEAEAAAAAE-------RTPAAGFAALKGKL 255
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
29-131 1.16e-03

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: 41.92  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   29 HNDVQKKTFTKWINARFSKSG--------KPPINDMFSDLKDGRKLLDLLEGLTGTSLPK----ERGSTRVHALNNVNRV 96
Cdd:cd21324    21 YSEEEKYAFVNWINKALENDPdckhvipmNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLA 100
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 672033739   97 LQVLHQNNVELVNIGGTDIVDGNPKLTLGLLWSII 131
Cdd:cd21324   101 LNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 135
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
704-1179 1.62e-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: 44.65  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   704 LRSKAALQNTEMNEY--KKSQETSGVRKKWKGLEKEQKE---KIPQLDELN-QTGQILQEQMGKEGLLAE----EINDVL 773
Cdd:TIGR00606  417 LQSKERLKQEQADEIrdEKKGLGRTIELKKEILEKKQEElkfVIKELQQLEgSSDRILELDQELRKAERElskaEKNSLT 496
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   774 ERVLLEWKMISQQLEDLGRKIQLQEDINAyfrQLDALEKTIRAKEEWLRDASFSESPQRSLpslKDSCQRELTDLLGLHP 853
Cdd:TIGR00606  497 ETLKKEVKSLQNEKADLDRKLRKLDQEME---QLNHHTTTRTQMEMLTKDKMDKDEQIRKI---KSRHSDELTSLLGYFP 570
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   854 RIEILCASCSALRSQpsvpgfVQQGFDDLRRHYQAVQKaLEEYQQQLENELKSQPE---------------PAYLDTLNT 918
Cdd:TIGR00606  571 NKKQLEDWLHSKSKE------INQTRDRLAKLNKELAS-LEQNKNHINNELESKEEqlssyedklfdvcgsQDEESDLER 643
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   919 LKKMLSESEK--AAQASLSALNDpSAVEQALQEKKALDETLENQKPTLHKLSEETKALEKNML--PDVGKTYRQEFDDAQ 994
Cdd:TIGR00606  644 LKEEIEKSSKqrAMLAGATAVYS-QFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRlaPDKLKSTESELKKKE 722
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   995 GKWNKVKTKVSRDLRSLEEIIPRLRDFKADSEVIEKWTNGVKDFLMKEQAAQGDTTALQRQLDQCTTFANEIETIESSLK 1074
Cdd:TIGR00606  723 KRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELK 802
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1075 -NLRDIE---TSLQRCPVTGVKTWVQTRLADYQSQLEKFSQEIDIQKSRLSDSQEKAMNLKKDLAEMQEWMAQAEEDYLE 1150
Cdd:TIGR00606  803 dVERKIAqqaAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR 882
                          490       500       510
                   ....*....|....*....|....*....|...
gi 672033739  1151 RD-FEYKSPE---ELESAVEEMKRAKEDVLQKE 1179
Cdd:TIGR00606  883 RQqFEEQLVElstEVQSLIREIKDAKEQDSPLE 915
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
30-130 1.74e-03

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: 41.10  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   30 NDVQKKTFTKWINARFSKSG-KPPINDMFSDLKDGRKLLDLLEGLTGTSLPKERG--STRVHALNNVNRVLQVLHQNNVE 106
Cdd:cd21285     8 NGFDKQIYTDWANHYLAKSGhKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
                          90       100
                  ....*....|....*....|....
gi 672033739  107 LVNIGGTDIVDGNPKLTLGLLWSI 130
Cdd:cd21285    88 IQGLSAEEIRNGNLKAILGLFFSL 111
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
2437-2543 1.87e-03

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 40.38  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2437 RDLENFVKWLQEAETTAnvladASQRENALQDSVlaRQLRQQMLDIQAEIDAHNDIFKSIDGNRQKMVKALGNSEEAtmL 2516
Cdd:pfam00435    8 RDADDLESWIEEKEALL-----SSEDYGKDLESV--QALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE--I 78
                           90       100
                   ....*....|....*....|....*..
gi 672033739  2517 QHRLDDMNQRWNDLKAKSASIRAHLEA 2543
Cdd:pfam00435   79 QERLEELNERWEQLLELAAERKQKLEE 105
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
2416-2627 2.14e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2416 QSIADRQSALEAELRTVQTSRRDLENFVKWLQEAettanvLADASQRENALQDSVLARQLRQQMLDIQAEIDahndifks 2495
Cdd:COG3206   215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQ------LGSGPDALPELLQSPVIQQLRAQLAELEAELA-------- 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2496 idgnrQKMVKALGNSEEATMLQHRLDDMNQRwndLKAKSASIRAHLEASAEKWNRLLASLEELIkwlnmkdEELKKQMpi 2575
Cdd:COG3206   281 -----ELSARYTPNHPDVIALRAQIAALRAQ---LQQEAQRILASLEAELEALQAREASLQAQL-------AQLEARL-- 343
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2576 gGDVPALQLQYdhcKVLRREL--KEKEY-SVLNAVDQARVFLADQP-----IEAPEEPRR 2627
Cdd:COG3206   344 -AELPELEAEL---RRLEREVevARELYeSLLQRLEEARLAEALTVgnvrvIDPAVVPLK 399
DUF4175 pfam13779
Domain of unknown function (DUF4175);
737-954 2.26e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 43.82  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   737 EQKEKIPQLDELNQ-TGQILQ------EQMGKEGLLAE------EINDVLERvllewkMISQQLEDlgrkiQLQEDINAY 803
Cdd:pfam13779  537 PQDLQQPDDPNAQEmTQQDLQrmldriEELARSGRRAEaqqmlsQLQQMLEN------LQAGQPQQ-----QQQQGQSEM 605
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   804 FRQLDALEKTIRAKEEwLRDASFSESPQRSLPSLKDSCQRELTDLLGLHPrieilcaSCSALRSQPSVPGFVQQGFDDLR 883
Cdd:pfam13779  606 QQAMDELGDLLREQQQ-LLDETFRQLQQQGGQQQGQPGQQGQQGQGQQPG-------QGGQQPGAQMPPQGGAEALGDLA 677
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672033739   884 RHYQAVQKALEEYQQQLENELKSQPEPAyldtlntlkkmLSESEKA---AQASLSALNDPSAVEqalQEKKALD 954
Cdd:pfam13779  678 ERQQALRRRLEELQDELKELGGKEPGQA-----------LGDAGRAmrdAEEALGQGDLAGAVD---AQGRALE 737
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
884-1217 3.33e-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: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  884 RHYQAVQKALEEYQQQLenelksqpepaYLDTLNTLKKMLSESEKAAQASLSALndpsavEQALQEKKALDETLENQKPT 963
Cdd:COG1196   213 ERYRELKEELKELEAEL-----------LLLKLRELEAELEELEAELEELEAEL------EELEAELAELEAELEELRLE 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  964 LHKLseetkaleknmlpdvgktyRQEFDDAQGKWNKVKTKVSRDLRSLEEIIPRLRDFKADSEVIEkwtngvKDFLMKEQ 1043
Cdd:COG1196   276 LEEL-------------------ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE------EELAELEE 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1044 AAQGDTTALQRQLDQCTTFANEIETIESSLKNLRDIETSLQRcpvtGVKTWVQTRLADYQSQLEKFSQEIDIQKsRLSDS 1123
Cdd:COG1196   331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA----ELAEAEEELEELAEELLEALRAAAELAA-QLEEL 405
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 1124 QEKAMNLKKDLAEMQEWMAQAEEDYLERDfeyKSPEELESAVEEMKRAKEDVLQKEVRVKILKDSIKLVAARVPSGGQEL 1203
Cdd:COG1196   406 EEAEEALLERLERLEEELEELEEALAELE---EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
                         330
                  ....*....|....
gi 672033739 1204 TSEFNEVLESYQLL 1217
Cdd:COG1196   483 LEELAEAAARLLLL 496
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
382-1178 4.08e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 4.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   382 LSDEEEFEIQEQMTLLNArwealRVESMERQsrlhdalMELQKKQLQQLsgwltltEERIQKMESLpvgddlpsLQNLLE 461
Cdd:TIGR02169  284 LGEEEQLRVKEKIGELEA-----EIASLERS-------IAEKERELEDA-------EERLAKLEAE--------IDKLLA 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   462 EHKSLQSDLEAEQVKVNSLTHMVvivdensgESATAVLEDQLQKLGERWTAVCRWTEERWNRLQEINILwqelleeqcll 541
Cdd:TIGR02169  337 EIEELEREIEEERKRRDKLTEEY--------AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL----------- 397
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   542 eawlteKEEaLNKVQTGNFKDQKELGVSVRRLAILKEDMEMKRQTLDQLS--------EIGQDVGQLLSNPKASEKMNSD 613
Cdd:TIGR02169  398 ------KRE-INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEeekedkalEIKKQEWKLEQLAADLSKYEQE 470
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   614 SEELTQRWDSLVQRLEDSSNQVTQAVAKLGMSQIPQKDLLETVHVREQGMikkpkqelppppppkkRQIHvdveakkkfd 693
Cdd:TIGR02169  471 LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASI----------------QGVH---------- 524
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   694 ATSAELQSWILRSKAALQNTEMNEYKK-SQETSGVRKKWKGLEKEQKEKIPQLDELN--QTGQILQEQMGKEGLLAEEIN 770
Cdd:TIGR02169  525 GTVAQLGSVGERYATAIEVAAGNRLNNvVVEDDAVAKEAIELLKRRKAGRATFLPLNkmRDERRDLSILSEDGVIGFAVD 604
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   771 dvlervLLEW-----KMISQQLEDLGrkiqLQEDINAYFRQLD-----ALEKTIRAKEEWLRDASFSESPQRSLPSlkds 840
Cdd:TIGR02169  605 ------LVEFdpkyePAFKYVFGDTL----VVEDIEAARRLMGkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSR---- 670
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   841 cqRELTDLLGLHPRIEILCASCSALRSQPSVpgfVQQGFDDLRRHYQAVQKALEEYQQQLEnelksqpepAYLDTLNTLK 920
Cdd:TIGR02169  671 --SEPAELQRLRERLEGLKRELSSLQSELRR---IENRLDELSQELSDASRKIGEIEKEIE---------QLEQEEEKLK 736
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   921 KMLSESEkaaqASLSALNDpsAVEQALQEKKALDETLENQKPTLHKLSEETKALEKNMLPdvgktyrQEFDDAQGKWNKV 1000
Cdd:TIGR02169  737 ERLEELE----EDLSSLEQ--EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH-------SRIPEIQAELSKL 803
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1001 KTKVSRDLRSLEEIIPRLRDFKADSEVIEK-----------WTNGVKDFLMKEQAAQGDTTALQRQLDQcttFANEIETI 1069
Cdd:TIGR02169  804 EEEVSRIEARLREIEQKLNRLTLEKEYLEKeiqelqeqridLKEQIKSIEKEIENLNGKKEELEEELEE---LEAALRDL 880
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1070 ESSLKNL-RDIETslqrcpvtgvktwVQTRLADYQSQLEKFSQEIDIQKSRLSDSQEKAMNLKKDLAEMqewmaqaeEDY 1148
Cdd:TIGR02169  881 ESRLGDLkKERDE-------------LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI--------EDP 939
                          810       820       830
                   ....*....|....*....|....*....|
gi 672033739  1149 LERDFEYKSPEELESAVEEMKRAKEDVLQK 1178
Cdd:TIGR02169  940 KGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1298-2159 4.15e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 4.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1298 IDGGILDDIISEKLEAFNSRYEE---LSHLAESKQISLEKqlqvLRETDHMLQVLKESLGELDKQLTTYltdRIDAfQLP 1374
Cdd:TIGR02168  141 IEQGKISEIIEAKPEERRAIFEEaagISKYKERRKETERK----LERTRENLDRLEDILNELERQLKSL---ERQA-EKA 212
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1375 QEAQKIQAEISAHELTL-----EELKKNVRPQpptspEGRTTRGGSQMDLLQRKLREVSTKFQLFQ-KPANFEQRMLDCK 1448
Cdd:TIGR02168  213 ERYKELKAELRELELALlvlrlEELREELEEL-----QEELKEAEEELEELTAELQELEEKLEELRlEVSELEEEIEELQ 287
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1449 RVLDGVKAELHVLSVKdvdpdvIQTHLDKCMKLYKTLSEVKLEVETViktGRHIVQKQqtDNPKGMDEQLTSLKVLYNDL 1528
Cdd:TIGR02168  288 KELYALANEISRLEQQ------KQILRERLANLERQLEELEAQLEEL---ESKLDELA--EELAELEEKLEELKEELESL 356
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1529 GAQVTEGKQDLERASQLSRKLKKEAailsEWLSTTEAELVQKstsegvIGDLDTEISWAKNILKDLERRKVdlNAITESS 1608
Cdd:TIGR02168  357 EAELEELEAELEELESRLEELEEQL----ETLRSKVAQLELQ------IASLNNEIERLEARLERLEDRRE--RLQQEIE 424
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1609 AALQHLVVGSESVLEDTLCVLNAGwsrvrtwTEDWRNTLLNHQNQLEVFDGHVAHISTWLYQAEALLDEiekkpASKQEE 1688
Cdd:TIGR02168  425 ELLKKLEEAELKELQAELEELEEE-------LEELQEELERLEEALEELREELEEAEQALDAAERELAQ-----LQARLD 492
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1689 IVKRLLSELSDASIQVENVREQAIVLVNARGSSSrELVEPKlAELSKNFEKVSQhiNSAQMLIGQDPAGTVEAVgpfsdl 1768
Cdd:TIGR02168  493 SLERLQENLEGFSEGVKALLKNQSGLSGILGVLS-ELISVD-EGYEAAIEAALG--GRLQAVVVENLNAAKKAI------ 562
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1769 ESLESdiENMLKVVEKHLDPSNDEKMDEERAQIEEVLQRGEHLLHEPMEDSKKEKIRLQLLLLHTRY--NKIKAIPQRKT 1846
Cdd:TIGR02168  563 AFLKQ--NELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVvdDLDNALELAKK 640
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1847 IPLSSGIMSsalPADYLVEINKILL------TLDDIELSLNIPELNttvyEDFSFQEDSLKRIKDQLDRLGEQLAavhek 1920
Cdd:TIGR02168  641 LRPGYRIVT---LDGDLVRPGGVITggsaktNSSILERRREIEELE----EKIEELEEKIAELEKALAELRKELE----- 708
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1921 qpdvileasgpeaiQIRDMLSQLNAKWDRVNRLYSDRRGSFARAVEEWKQFHCDLDDLTQWLSEAEDLLVGTcapdgSLD 2000
Cdd:TIGR02168  709 --------------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL-----EER 769
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2001 LEKARTHQLELEDGLSSHQPcliDVNQKGEDIVQrlrpsdasfLKDKLASLNQRWSALVAEVKDLQPRLKGESKQVSGYR 2080
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELEA---QIEQLKEELKA---------LREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  2081 KRLDEVvcwltkVENAVQKRStpDPEENPWELTDLAQEMD-AQAENIKWLN-RAELEMLSDKNLSlcERDNLSESLRNVN 2158
Cdd:TIGR02168  838 RRLEDL------EEQIEELSE--DIESLAAEIEELEELIEeLESELEALLNeRASLEEALALLRS--ELEELSEELRELE 907

                   .
gi 672033739  2159 T 2159
Cdd:TIGR02168  908 S 908
SPEC smart00150
Spectrin repeats;
803-901 4.28e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 39.24  E-value: 4.28e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739    803 YFRQLDALEKTIRAKEEWLRDASFSESPQrSLPSLKDSCQRELTDLLGLHPRIEILCASCSAL-RSQPSVPGFVQQGFDD 881
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASEDLGKDLE-SVEALLKKHEAFEAELEAHEERVEALNELGEQLiEEGHPDAEEIEERLEE 81
                            90       100
                    ....*....|....*....|
gi 672033739    882 LRRHYQAVQKALEEYQQQLE 901
Cdd:smart00150   82 LNERWEELKELAEERRQKLE 101
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
943-1328 5.55e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 42.36  E-value: 5.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   943 VEQALQEKKALDETLENQKPTLHKLSEETKALEKNML----PDVGKTYRQEFDDAQGKWNKVKTKVSRDLRSLEEII--- 1015
Cdd:pfam13166   98 IAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLdecwKKIKRKKNSALSEALNGFKYEANFKSRLLREIEKDNfna 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1016 -PRLRDFKADSEV----------IEKWTNGVKDFLMKEQAAqgdttALQRQLdqcTTFANEIETIESSLKN-------LR 1077
Cdd:pfam13166  178 gVLLSDEDRKAALatvfsdnkpeIAPLTFNVIDFDALEKAE-----ILIQKV---IGKSSAIEELIKNPDLadwveqgLE 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1078 DIETSLQRCPVTGvktwvQTRLADYQSQLEK-FSQEIDIQKSRLSdsqekamnlkkdlaEMQEWMAQAEEDYLERdfeYK 1156
Cdd:pfam13166  250 LHKAHLDTCPFCG-----QPLPAERKAALEAhFDDEFTEFQNRLQ--------------KLIEKVESAISSLLAQ---LP 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1157 SPEELESAVEEMKRAKEDVLQ-KEVRVKILKDSIKLVAARV--PSGGQELTS------EFNEVLESYQLLCNRIRGKCHT 1227
Cdd:pfam13166  308 AVSDLASLLSAFELDVEDIESeAEVLNSQLDGLRRALEAKRkdPFKSIELDSvdakieSINDLVASINELIAKHNEITDN 387
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1228 LEE-VWSCWVEL-LHYLDLETSWLNTLEERMQSTEALPERAEAVHDALESLESVLRhpadnrTQIRELGQTLIDGGILDD 1305
Cdd:pfam13166  388 FEEeKNKAKKKLrLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLR------EEIKELEAQLRDHKPGAD 461
                          410       420
                   ....*....|....*....|...
gi 672033739  1306 IISEKLEAFNSRYEELSHLAESK 1328
Cdd:pfam13166  462 EINKLLKAFGFGELELSFNEEGK 484
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
803-902 6.69e-03

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


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 38.84  E-value: 6.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   803 YFRQLDALEKTIRAKEEWLRDASFSESPQrSLPSLKDSCQRELTDLLGLHPRIEILCASCSALR-SQPSVPGFVQQGFDD 881
Cdd:pfam00435    6 FFRDADDLESWIEEKEALLSSEDYGKDLE-SVQALLKKHKALEAELAAHQDRVEALNELAEKLIdEGHYASEEIQERLEE 84
                           90       100
                   ....*....|....*....|.
gi 672033739   882 LRRHYQAVQKALEEYQQQLEN 902
Cdd:pfam00435   85 LNERWEQLLELAAERKQKLEE 105
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
687-1149 7.01e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 7.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  687 EAKKKFDATSAELQSwiLRSKAALQNTEMNEYKKSQETSGVRKKWKGLEKEQKEKIPQLDELNQTGQILQEQMGKEGLLA 766
Cdd:COG4717    92 ELQEELEELEEELEE--LEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELE 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  767 EEINDVLERVLLEWKMIS----QQLEDLGRKIQ-LQEDINAYFRQLDALE---KTIRAKEEWLRDASFSESPQRSLpslk 838
Cdd:COG4717   170 AELAELQEELEELLEQLSlateEELQDLAEELEeLQQRLAELEEELEEAQeelEELEEELEQLENELEAAALEERL---- 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  839 dscQRELTDLLGLHPRIEILCASCSALRSQPSVPG--FVQQGFDDLRRHYQAVQKALEEYQQQLENELKSQPEPAYLDTL 916
Cdd:COG4717   246 ---KEARLLLLIAAALLALLGLGGSLLSLILTIAGvlFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELE 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  917 NTLKKMLSESEKAAQASLSALNDPSAVEQALQEKKALDETLEnqkptLHKLSEETKALeknmLPDVGKTYRQEFDDAQGK 996
Cdd:COG4717   323 ELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-----LEELEQEIAAL----LAEAGVEDEEELRAALEQ 393
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  997 WNKVKTKVSRdLRSLEEIIPRLRDFkadseviekwtngvkdflMKEQAAQGDTTALQRQLDQCTTfanEIETIESSLKNL 1076
Cdd:COG4717   394 AEEYQELKEE-LEELEEQLEELLGE------------------LEELLEALDEEELEEELEELEE---ELEELEEELEEL 451
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672033739 1077 RDIETSLQRcpvtgvktwvQTRLADYQSQLEKFSQEIDIQKSRLSDSQEKAMNLKKDLAEMQEWMAQAEEDYL 1149
Cdd:COG4717   452 REELAELEA----------ELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2465-2699 9.18e-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: 41.29  E-value: 9.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2465 ALQDSVLARQLRQQMLDIQAEIDAHNDIFKSIDGNRQKMVKALGNSEEatmlqhRLDDMNQRWNDLKAKSASIRAHLEAS 2544
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER------RIAALARRIRALEQELAALEAELAEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2545 AEKWNRLLASLEELIKWLnmkdEELKKQMPIGGDVPALQL---QYDHCKVLRRelkekeYSVLNAVDQARVFLADQPIEA 2621
Cdd:COG4942    89 EKEIAELRAELEAQKEEL----AELLRALYRLGRQPPLALllsPEDFLDAVRR------LQYLKYLAPARREQAEELRAD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739 2622 PEEPRRNPQS----KTELTPEERAQKIAKA-MRKQSSEVREKWESLNAVTSTWQKQVGKALEKLRDLQGAVDDLDADMKE 2696
Cdd:COG4942   159 LAELAALRAEleaeRAELEALLAELEEERAaLEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238

                  ...
gi 672033739 2697 VEA 2699
Cdd:COG4942   239 AAE 241
SPEC smart00150
Spectrin repeats;
691-797 9.23e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 38.46  E-value: 9.23e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739    691 KFDATSAELQSWILRSKAALQNTEMneYKKSQETSGVRKKWKGLEKEQKEKIPQLDELNQTGQILQEQMGKEgllAEEIN 770
Cdd:smart00150    2 QFLRDADELEAWLEEKEQLLASEDL--GKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD---AEEIE 76
                            90       100
                    ....*....|....*....|....*..
gi 672033739    771 DVLERVLLEWKMISQQLEDlgRKIQLQ 797
Cdd:smart00150   77 ERLEELNERWEELKELAEE--RRQKLE 101
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
736-1558 9.48e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.88  E-value: 9.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   736 KEQKEKIPQLDELNQTGQILQEQMGKEGLLAEEINDVLERVLLEWKMISQQLEDLGRKIQLQEDINAYFRqlDALEKTiR 815
Cdd:TIGR00618  163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLR--EALQQT-Q 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   816 AKEEWLRDasfsespQRSLPSLKDSCQRELTDLLglhprieilcASCSALRSQPSVPGFVQQGFdDLRRH---YQAVQKA 892
Cdd:TIGR00618  240 QSHAYLTQ-------KREAQEEQLKKQQLLKQLR----------ARIEELRAQEAVLEETQERI-NRARKaapLAAHIKA 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   893 LEEYQQQLEN---ELKSQpepayldtLNTLKKMLSESEKAAQASLSALNDPSAVEQALQEKKALDETLENQKPTLHKLSE 969
Cdd:TIGR00618  302 VTQIEQQAQRihtELQSK--------MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ 373
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739   970 ETKALEKNmlpdvgKTYRQEFDDAQGKWNKVKTKVSRDLRSLEEIIPRLRDFKAdseviekwTNGVKDFLMKEQAAQGDT 1049
Cdd:TIGR00618  374 QHTLTQHI------HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD--------LQGQLAHAKKQQELQQRY 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1050 TALQRQLDQCTTFANEIETIEsslknLRDIETSLQRcpvtgvktwVQTRLADYQSQLEKFSQEIDIQKSRLSDSQEKAMN 1129
Cdd:TIGR00618  440 AELCAAAITCTAQCEKLEKIH-----LQESAQSLKE---------REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCP 505
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1130 LKKDLAEMQEWMAQAEEdylerdfeyksPEELESAVEemkrakedvlQKEVRVKILKDSIKLVAARVPS---GGQELTSE 1206
Cdd:TIGR00618  506 LCGSCIHPNPARQDIDN-----------PGPLTRRMQ----------RGEQTYAQLETSEEDVYHQLTSerkQRASLKEQ 564
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1207 FNEVLESYQLLCNRIRGKCHTLEEVWSCWVELLHYLDLEtswlntLEERMQSTEALPERAEAVHDALESLESVL-RHPAD 1285
Cdd:TIGR00618  565 MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL------SEAEDMLACEQHALLRKLQPEQDLQDVRLhLQQCS 638
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1286 NRTQIRELGQTLIDGGILDDIISEKLEA---FNSRYEELSHLAESKQISLEKQLQVLRET----DHMLQVLKESLGELDK 1358
Cdd:TIGR00618  639 QELALKLTALHALQLTLTQERVREHALSirvLPKELLASRQLALQKMQSEKEQLTYWKEMlaqcQTLLRELETHIEEYDR 718
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1359 QLTtyltdridafQLPQEAQKIQAEISAHELTLEELKKNVRPQPPTSPEGRTtrggsqmDLLQRKLREVSTKFQLFQKPA 1438
Cdd:TIGR00618  719 EFN----------EIENASSSLGSDLAAREDALNQSLKELMHQARTVLKART-------EAHFNNNEEVTAALQTGAELS 781
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672033739  1439 NFEQRMLDCKRVLDgvkaelhvlsvkdvdpdviqthldkcmKLYKTLSEVKLEVETVIKTGRHIVQKQQTDNPKGMDEQL 1518
Cdd:TIGR00618  782 HLAAEIQFFNRLRE---------------------------EDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFL 834
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|
gi 672033739  1519 TSLKVLYNDLGAQVTEGKQDLERASQLSRKLKKEAAILSE 1558
Cdd:TIGR00618  835 SRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
 
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