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Conserved domains on  [gi|272506000|gb|AAF46171|]
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uncharacterized protein Dmel_CG34417, isoform I [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
3433-3538 7.19e-68

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: 224.53  E-value: 7.19e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 3512
Cdd:cd21200     1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
                          90       100
                  ....*....|....*....|....*..
gi 272506000 3513 EDMVEMS-RPDWKCVFVYVQSIYRRFR 3538
Cdd:cd21200    81 EDMVRMGnRPDWKCVFTYVQSLYRHLR 107
Smoothelin pfam12510
Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is ...
3169-3218 5.87e-16

Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00307. Smoothelin is a cytoskeletal protein specifically expressed in differentiated smooth muscle cells and has been shown to co-localize with smooth muscle alpha actin.


:

Pssm-ID: 463614 [Multi-domain]  Cd Length: 50  Bit Score: 74.27  E-value: 5.87e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 272506000  3169 SSSSAPVTRTTCDIEEIWDEQVLKQLLEQASTYEERRKIRARLRELMAER 3218
Cdd:pfam12510    1 EETSAASKLTAEELEAIEDEEVLDKLLETATDYEERRLIRAAIRELRKRK 50
Smoothelin pfam12510
Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is ...
2594-2636 5.17e-14

Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00307. Smoothelin is a cytoskeletal protein specifically expressed in differentiated smooth muscle cells and has been shown to co-localize with smooth muscle alpha actin.


:

Pssm-ID: 463614 [Multi-domain]  Cd Length: 50  Bit Score: 68.49  E-value: 5.17e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 272506000  2594 SDLELEIEEIFDLQRLEKLLETVASYEMRRRIRAQMRLIRKNM 2636
Cdd:pfam12510    8 KLTAEELEAIEDEEVLDKLLETATDYEERRLIRAAIRELRKRK 50
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
1394-1702 8.28e-11

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 68.56  E-value: 8.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1394 PKEEDSPKYPKGPETPKSPRNDQR--------IPSIPKKGQSPVQFKTEETPRYPQEQER--YPKEPETSQYPK--ESPR 1461
Cdd:PTZ00449  582 PKDPKHPKDPEEPKKPKRPRSAQRptrpkspkLPELLDIPKSPKRPESPKSPKRPPPPQRpsSPERPEGPKIIKspKPPK 661
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1462 NPK----------------------EDAETININEETTIVITKEGSKSPSPRWSPSPERRVPK-------SQQPPSPTAS 1512
Cdd:PTZ00449  662 SPKppfdpkfkekfyddyldaaaksKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKlprdeefPFEPIGDPDA 741
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1513 PSVSPVSGRKIPNEvESNFVTEKIIDCRGKTVVEKISQRP----RTPSPTTPKKNTK-PSQKIPERVPETESEPEKDSES 1587
Cdd:PTZ00449  742 EQPDDIEFFTPPEE-ERTFFHETPADTPLPDILAEEFKEEdihaETGEPDEAMKRPDsPSEHEDKPPGDHPSLPKKRHRL 820
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1588 EtkkttSVSVTKTETERRNSRTTKTKQPLPLKEPQSKvpagksPRKDSLTGRKRDSLVEETRittTTTTTRQGRKPSDTN 1667
Cdd:PTZ00449  821 D-----GLALSTTDLESDAGRIAKDASGKIVKLKRSK------SFDDLTTVEEAEEMGAEAR---KIVVDDDGTEADDED 886
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 272506000 1668 GSPSiKDRLRSSPRKQKTSPQQTRTPTPAQTRNPE 1702
Cdd:PTZ00449  887 THPP-EEKHKSEVRRRRPPKKPSKPKKPSKPKKPK 920
PHA03247 super family cl33720
large tegument protein UL36; Provisional
566-1191 5.50e-08

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.57  E-value: 5.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  566 YQEP--QRSPQKLREAPTPSWEQPATRRQPveedfsthgfPSVRTTTTSTRPDQPDGEVLHtsktvSRNQSANRktNTER 643
Cdd:PHA03247 2480 YRRPaeARFPFAAGAAPDPGGGGPPDPDAP----------PAPSRLAPAILPDEPVGEPVH-----PRMLTWIR--GLEE 2542
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  644 IIETQVEHPNAPSHSTPRSGSPRRSQPRDDYASSPRGPAGKPSQSRPSNTGGSTTTKTTTTSEPLTRRQLQKerevdaah 723
Cdd:PHA03247 2543 LASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPP-------- 2614
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  724 rafaaslrSSSPADSTTsvgshhqtPRSSVSSNRTFRREMREGSHDSQAPSESSRissttvtRHTTGGNVTSNTIKTKTT 803
Cdd:PHA03247 2615 --------SPLPPDTHA--------PDPPPPSPSPAANEPDPHPPPTVPPPERPR-------DDPAPGRVSRPRRARRLG 2671
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  804 KPVKTASEPRSPTPKAGGSvttttttittksspspapaspttaapptsapassappdnklsqytytTTKPGDIFSLPPTT 883
Cdd:PHA03247 2672 RAAQASSPPQRPRRRAARP-----------------------------------------------TVGSLTSLADPPPP 2704
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  884 PPTINNEPTLTTTRNTTTTTTTTTTATSDNLQNHPKKSAIEPATDTDSQPIRKVKLSANEAKVVEEAPCVRRQyyqlgne 963
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA------- 2777
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  964 GENPETPESSGTPANKKPHQMRRPHDEPEPQLRRSSKSPSVEPRQVQRETtfegrrvsqdreisideliLIEETSGAPGS 1043
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP-------------------LPPPTSAQPTA 2838
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1044 PKIPSPRAQS---------PGKPATRSQSPEKPQPR-ATPRQSPEKE--QPAFKQTHEVYtpSQPEKQFPRARSPE-KTP 1110
Cdd:PHA03247 2839 PPPPPGPPPPslplggsvaPGGDVRRRPPSRSPAAKpAAPARPPVRRlaRPAVSRSTESF--ALPPDQPERPPQPQaPPP 2916
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1111 GWTQPQVSPRQSPEKQLPRAQSPEKvPAVRQPSVSPRQSPEKQIPDPKTRDQGPGLPRISPRQSPEKQLPKDVPQKSRQS 1190
Cdd:PHA03247 2917 PQPQPQPPPPPQPQPPPPPPPRPQP-PLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPP 2995

                  .
gi 272506000 1191 P 1191
Cdd:PHA03247 2996 L 2996
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
1035-1421 3.59e-06

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 53.15  E-value: 3.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1035 EETSGAPGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFKQTHEVYTPSQPEKQfpraRSPEKTPGWTQ 1114
Cdd:PTZ00449  502 EDSDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKE----HKPSKIPTLSK 577
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1115 PQVSPRQSPEKQLPRAQSPEKVPAVRQPSVSPRqSPEK----QIPDPKTRDQGPGLPR--------ISPRQSPEKQLPKD 1182
Cdd:PTZ00449  578 KPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPK-SPKLpellDIPKSPKRPESPKSPKrppppqrpSSPERPEGPKIIKS 656
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1183 VPQKSRQSPEKDLTNQQRREEEIFRSTITTTQKRTTNNLNEEFITNERDNQNQ----PISEKKPQIPANAEPNTKPSETI 1258
Cdd:PTZ00449  657 PKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPEtpgtPFTTPRPLPPKLPRDEEFPFEPI 736
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1259 ESPDGGFPSK----TTEVEAQPEVKESPTYRK-KGLTRRETFEDRCRQILGMEEDG----DTQGTYTERPNNEQEDVNVS 1329
Cdd:PTZ00449  737 GDPDAEQPDDieffTPPEEERTFFHETPADTPlPDILAEEFKEEDIHAETGEPDEAmkrpDSPSEHEDKPPGDHPSLPKK 816
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1330 HTTIETIQVKIEDCPND------DEDDKPRRVTET------YVVRTQPKIKVEEELFV---DVTEAEDVEilVNPSK--- 1391
Cdd:PTZ00449  817 RHRLDGLALSTTDLESDagriakDASGKIVKLKRSksfddlTTVEEAEEMGAEARKIVvddDGTEADDED--THPPEekh 894
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 272506000 1392 -------KSPKEEDSPKYPKGPETPKSPrNDQRIPSI 1421
Cdd:PTZ00449  895 ksevrrrRPPKKPSKPKKPSKPKKPKKP-DSAFIPSI 930
PTZ00121 super family cl31754
MAEBL; Provisional
2080-2248 4.09e-04

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 2080 RQSEPERELDEESEPELDRDTDVEDDDQTSQLETEEEITQTVTKKETLKEFKQQTKETRETRRDSKAEPEKLQKKSPQTK 2159
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 2160 VKEES----ARVPKYQAKVSQKVSQWEPKKQPQREPKVTQKETPLEPKKQPLSKVKdEPEKVNKREPKVPQKESQTKLKE 2235
Cdd:PTZ00121 1661 IKAAEeakkAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK-KAEELKKAEEENKIKAEEAKKEA 1739
                         170
                  ....*....|...
gi 272506000 2236 EPERVTKKTPQKE 2248
Cdd:PTZ00121 1740 EEDKKKAEEAKKD 1752
 
Name Accession Description Interval E-value
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
3433-3538 7.19e-68

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: 224.53  E-value: 7.19e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 3512
Cdd:cd21200     1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
                          90       100
                  ....*....|....*....|....*..
gi 272506000 3513 EDMVEMS-RPDWKCVFVYVQSIYRRFR 3538
Cdd:cd21200    81 EDMVRMGnRPDWKCVFTYVQSLYRHLR 107
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
3432-3538 6.20e-25

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 101.98  E-value: 6.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  3432 ATVKDQLLQWCKHKTQEY-ENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQT--RRHNFELAFSVADEKAGIAP 3508
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEfdKLENINLALDVAEKKLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 272506000  3509 -LLDVEDMVEmsrPDWKCVFVYVQSIYRRFR 3538
Cdd:pfam00307   81 vLIEPEDLVE---GDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
3436-3533 1.99e-22

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: 94.30  E-value: 1.99e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000   3436 DQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQT----RRHNFELAFSVADEKAGIAPLLD 3511
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLsrfkKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 272506000   3512 VEDMVEMsRPDWKCVFVYVQSI 3533
Cdd:smart00033   81 PEDLVEG-PKLILGVIWTLISL 101
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
3433-3538 1.25e-19

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 96.55  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYEN-VQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRH--NFELAFSVADEKAGIAPL 3509
Cdd:COG5069   125 TKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARL 204
                          90       100
                  ....*....|....*....|....*....
gi 272506000 3510 LDVEDMVEMSRPDWKCVFVYVQSIYRRFR 3538
Cdd:COG5069   205 IGVEDIVNVSIPDERSIMTYVSWYIIRFG 233
Smoothelin pfam12510
Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is ...
3169-3218 5.87e-16

Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00307. Smoothelin is a cytoskeletal protein specifically expressed in differentiated smooth muscle cells and has been shown to co-localize with smooth muscle alpha actin.


Pssm-ID: 463614 [Multi-domain]  Cd Length: 50  Bit Score: 74.27  E-value: 5.87e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 272506000  3169 SSSSAPVTRTTCDIEEIWDEQVLKQLLEQASTYEERRKIRARLRELMAER 3218
Cdd:pfam12510    1 EETSAASKLTAEELEAIEDEEVLDKLLETATDYEERRLIRAAIRELRKRK 50
Smoothelin pfam12510
Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is ...
2594-2636 5.17e-14

Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00307. Smoothelin is a cytoskeletal protein specifically expressed in differentiated smooth muscle cells and has been shown to co-localize with smooth muscle alpha actin.


Pssm-ID: 463614 [Multi-domain]  Cd Length: 50  Bit Score: 68.49  E-value: 5.17e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 272506000  2594 SDLELEIEEIFDLQRLEKLLETVASYEMRRRIRAQMRLIRKNM 2636
Cdd:pfam12510    8 KLTAEELEAIEDEEVLDKLLETATDYEERRLIRAAIRELRKRK 50
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1394-1702 8.28e-11

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 68.56  E-value: 8.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1394 PKEEDSPKYPKGPETPKSPRNDQR--------IPSIPKKGQSPVQFKTEETPRYPQEQER--YPKEPETSQYPK--ESPR 1461
Cdd:PTZ00449  582 PKDPKHPKDPEEPKKPKRPRSAQRptrpkspkLPELLDIPKSPKRPESPKSPKRPPPPQRpsSPERPEGPKIIKspKPPK 661
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1462 NPK----------------------EDAETININEETTIVITKEGSKSPSPRWSPSPERRVPK-------SQQPPSPTAS 1512
Cdd:PTZ00449  662 SPKppfdpkfkekfyddyldaaaksKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKlprdeefPFEPIGDPDA 741
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1513 PSVSPVSGRKIPNEvESNFVTEKIIDCRGKTVVEKISQRP----RTPSPTTPKKNTK-PSQKIPERVPETESEPEKDSES 1587
Cdd:PTZ00449  742 EQPDDIEFFTPPEE-ERTFFHETPADTPLPDILAEEFKEEdihaETGEPDEAMKRPDsPSEHEDKPPGDHPSLPKKRHRL 820
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1588 EtkkttSVSVTKTETERRNSRTTKTKQPLPLKEPQSKvpagksPRKDSLTGRKRDSLVEETRittTTTTTRQGRKPSDTN 1667
Cdd:PTZ00449  821 D-----GLALSTTDLESDAGRIAKDASGKIVKLKRSK------SFDDLTTVEEAEEMGAEAR---KIVVDDDGTEADDED 886
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 272506000 1668 GSPSiKDRLRSSPRKQKTSPQQTRTPTPAQTRNPE 1702
Cdd:PTZ00449  887 THPP-EEKHKSEVRRRRPPKKPSKPKKPSKPKKPK 920
PHA03247 PHA03247
large tegument protein UL36; Provisional
566-1191 5.50e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.57  E-value: 5.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  566 YQEP--QRSPQKLREAPTPSWEQPATRRQPveedfsthgfPSVRTTTTSTRPDQPDGEVLHtsktvSRNQSANRktNTER 643
Cdd:PHA03247 2480 YRRPaeARFPFAAGAAPDPGGGGPPDPDAP----------PAPSRLAPAILPDEPVGEPVH-----PRMLTWIR--GLEE 2542
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  644 IIETQVEHPNAPSHSTPRSGSPRRSQPRDDYASSPRGPAGKPSQSRPSNTGGSTTTKTTTTSEPLTRRQLQKerevdaah 723
Cdd:PHA03247 2543 LASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPP-------- 2614
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  724 rafaaslrSSSPADSTTsvgshhqtPRSSVSSNRTFRREMREGSHDSQAPSESSRissttvtRHTTGGNVTSNTIKTKTT 803
Cdd:PHA03247 2615 --------SPLPPDTHA--------PDPPPPSPSPAANEPDPHPPPTVPPPERPR-------DDPAPGRVSRPRRARRLG 2671
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  804 KPVKTASEPRSPTPKAGGSvttttttittksspspapaspttaapptsapassappdnklsqytytTTKPGDIFSLPPTT 883
Cdd:PHA03247 2672 RAAQASSPPQRPRRRAARP-----------------------------------------------TVGSLTSLADPPPP 2704
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  884 PPTINNEPTLTTTRNTTTTTTTTTTATSDNLQNHPKKSAIEPATDTDSQPIRKVKLSANEAKVVEEAPCVRRQyyqlgne 963
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA------- 2777
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  964 GENPETPESSGTPANKKPHQMRRPHDEPEPQLRRSSKSPSVEPRQVQRETtfegrrvsqdreisideliLIEETSGAPGS 1043
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP-------------------LPPPTSAQPTA 2838
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1044 PKIPSPRAQS---------PGKPATRSQSPEKPQPR-ATPRQSPEKE--QPAFKQTHEVYtpSQPEKQFPRARSPE-KTP 1110
Cdd:PHA03247 2839 PPPPPGPPPPslplggsvaPGGDVRRRPPSRSPAAKpAAPARPPVRRlaRPAVSRSTESF--ALPPDQPERPPQPQaPPP 2916
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1111 GWTQPQVSPRQSPEKQLPRAQSPEKvPAVRQPSVSPRQSPEKQIPDPKTRDQGPGLPRISPRQSPEKQLPKDVPQKSRQS 1190
Cdd:PHA03247 2917 PQPQPQPPPPPQPQPPPPPPPRPQP-PLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPP 2995

                  .
gi 272506000 1191 P 1191
Cdd:PHA03247 2996 L 2996
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1035-1421 3.59e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 53.15  E-value: 3.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1035 EETSGAPGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFKQTHEVYTPSQPEKQfpraRSPEKTPGWTQ 1114
Cdd:PTZ00449  502 EDSDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKE----HKPSKIPTLSK 577
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1115 PQVSPRQSPEKQLPRAQSPEKVPAVRQPSVSPRqSPEK----QIPDPKTRDQGPGLPR--------ISPRQSPEKQLPKD 1182
Cdd:PTZ00449  578 KPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPK-SPKLpellDIPKSPKRPESPKSPKrppppqrpSSPERPEGPKIIKS 656
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1183 VPQKSRQSPEKDLTNQQRREEEIFRSTITTTQKRTTNNLNEEFITNERDNQNQ----PISEKKPQIPANAEPNTKPSETI 1258
Cdd:PTZ00449  657 PKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPEtpgtPFTTPRPLPPKLPRDEEFPFEPI 736
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1259 ESPDGGFPSK----TTEVEAQPEVKESPTYRK-KGLTRRETFEDRCRQILGMEEDG----DTQGTYTERPNNEQEDVNVS 1329
Cdd:PTZ00449  737 GDPDAEQPDDieffTPPEEERTFFHETPADTPlPDILAEEFKEEDIHAETGEPDEAmkrpDSPSEHEDKPPGDHPSLPKK 816
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1330 HTTIETIQVKIEDCPND------DEDDKPRRVTET------YVVRTQPKIKVEEELFV---DVTEAEDVEilVNPSK--- 1391
Cdd:PTZ00449  817 RHRLDGLALSTTDLESDagriakDASGKIVKLKRSksfddlTTVEEAEEMGAEARKIVvddDGTEADDED--THPPEekh 894
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 272506000 1392 -------KSPKEEDSPKYPKGPETPKSPrNDQRIPSI 1421
Cdd:PTZ00449  895 ksevrrrRPPKKPSKPKKPSKPKKPKKP-DSAFIPSI 930
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
926-1184 2.28e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.45  E-value: 2.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000   926 ATDTDSQPIRKVKLSANEAKVVEEAPC----VRRQYYQLGNEGENPETPESSGTpankKPHQMRRPHDEPEpqlrrsSKS 1001
Cdd:pfam03154   49 AASTSSNDSKAESMKKSSKKIKEEAPSplksAKRQREKGASDTEEPERATAKKS----KTQEISRPNSPSE------GEG 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  1002 PSVEPRQVQRETTFEGRRVSQDREISidelilieetsgapgSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQ 1081
Cdd:pfam03154  119 ESSDGRSVNDEGSSDPKDIDQDNRST---------------SPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASP 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  1082 PAFKQTHEVYTPSQPEKQFPRARSPEKTPGWTQPQVSP----------RQSPEKQLPRAQSPEKVPAVRQPSVSPRQSPE 1151
Cdd:pfam03154  184 PSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTqstaaphtliQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSP 263
                          250       260       270
                   ....*....|....*....|....*....|...
gi 272506000  1152 KQIPDPKTRDQGPGLPRisPRQSPEKQLPKDVP 1184
Cdd:pfam03154  264 QPLPQPSLHGQMPPMPH--SLQTGPSHMQHPVP 294
PTZ00121 PTZ00121
MAEBL; Provisional
2080-2248 4.09e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 2080 RQSEPERELDEESEPELDRDTDVEDDDQTSQLETEEEITQTVTKKETLKEFKQQTKETRETRRDSKAEPEKLQKKSPQTK 2159
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 2160 VKEES----ARVPKYQAKVSQKVSQWEPKKQPQREPKVTQKETPLEPKKQPLSKVKdEPEKVNKREPKVPQKESQTKLKE 2235
Cdd:PTZ00121 1661 IKAAEeakkAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK-KAEELKKAEEENKIKAEEAKKEA 1739
                         170
                  ....*....|...
gi 272506000 2236 EPERVTKKTPQKE 2248
Cdd:PTZ00121 1740 EEDKKKAEEAKKD 1752
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1008-1255 3.95e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1008 QVQRETTFEGRRVSQDREISIDELILIEETSGAPGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFKQT 1087
Cdd:NF033839  254 KVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVK 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1088 HEVYTPS-----QPEKQFPRAR-SPEKTPGWTQPQVSPRQSPEKQLPRAQSPEKVPAVRQPSVSPRQSPEKQIPDPKTRD 1161
Cdd:NF033839  334 PQPEKPKpevkpQLETPKPEVKpQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQP 413
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1162 QGPGlPRISPrqSPEKQLPKDVPQKSRQSPEKDLTNQQRREE-----EIFRSTITTTQKRTTNNLNEEFITNERDNQNQP 1236
Cdd:NF033839  414 EKPK-PEVKP--QPEKPKPEVKPQPEKPKPEVKPQPEKPKPEvkpqpETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQ 490
                         250
                  ....*....|....*....
gi 272506000 1237 ISEKKPQIPANAEPNTKPS 1255
Cdd:NF033839  491 ADDKKPSTPNNLSKDKQPS 509
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1000-1192 4.77e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1000 KSPSVEPRQVQRETTFEGRRVSQDREISIDELILIEETSGAPGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEK 1079
Cdd:NF033839  290 KKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQP 369
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1080 EQPAFKQTHEVYTPSQPEKQFPRARSPEKTPGWTQPQVSPRQSPEKqlpraQSPEKVPAVRQPSVSPRQSPEKQIPDPKT 1159
Cdd:NF033839  370 EKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEK-----PKPEVKPQPEKPKPEVKPQPEKPKPEVKP 444
                         170       180       190
                  ....*....|....*....|....*....|...
gi 272506000 1160 RDQGPGlPRISPRqsPEKQLPKDVPQKSRQSPE 1192
Cdd:NF033839  445 QPEKPK-PEVKPQ--PETPKPEVKPQPEKPKPE 474
 
Name Accession Description Interval E-value
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
3433-3538 7.19e-68

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: 224.53  E-value: 7.19e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 3512
Cdd:cd21200     1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
                          90       100
                  ....*....|....*....|....*..
gi 272506000 3513 EDMVEMS-RPDWKCVFVYVQSIYRRFR 3538
Cdd:cd21200    81 EDMVRMGnRPDWKCVFTYVQSLYRHLR 107
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
3433-3535 7.83e-49

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: 170.17  E-value: 7.83e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 3512
Cdd:cd21259     1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80
                          90       100
                  ....*....|....*....|...
gi 272506000 3513 EDMVEMSRPDWKCVFVYVQSIYR 3535
Cdd:cd21259    81 EDMVRMREPDWKCVYTYIQEFYR 103
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
3434-3535 1.52e-47

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: 166.80  E-value: 1.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3434 VKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVE 3513
Cdd:cd21260     2 VKNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVE 81
                          90       100
                  ....*....|....*....|..
gi 272506000 3514 DMVEMSRPDWKCVFVYVQSIYR 3535
Cdd:cd21260    82 DMVRMSVPDSKCVYTYIQELYR 103
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
3433-3538 8.32e-46

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: 161.37  E-value: 8.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 3512
Cdd:cd21258     1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEV 80
                          90       100
                  ....*....|....*....|....*..
gi 272506000 3513 EDMVEM-SRPDWKCVFVYVQSIYRRFR 3538
Cdd:cd21258    81 EDMMIMgKKPDSKCVFTYVQSLYNHLR 107
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
3438-3537 3.52e-43

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: 154.06  E-value: 3.52e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3438 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVAdEKAGIAPLLDVEDMVE 3517
Cdd:cd21199    13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAA-ESVGIPTTLTIDEMVS 91
                          90       100
                  ....*....|....*....|
gi 272506000 3518 MSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21199    92 MERPDWQSVMSYVTAIYKHF 111
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
3433-3538 9.28e-42

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: 149.73  E-value: 9.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 3512
Cdd:cd21261     1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEV 80
                          90       100
                  ....*....|....*....|....*..
gi 272506000 3513 EDMVEMSR-PDWKCVFVYVQSIYRRFR 3538
Cdd:cd21261    81 EDMMVMGRkPDPMCVFTYVQSLYNHLR 107
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
3433-3537 5.90e-39

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: 142.12  E-value: 5.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 3512
Cdd:cd21216    10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKMLDA 89
                          90       100
                  ....*....|....*....|....*
gi 272506000 3513 EDMVEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21216    90 EDIVNTPRPDERSVMTYVSCYYHAF 114
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
3438-3538 1.40e-35

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: 132.09  E-value: 1.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3438 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDMVE 3517
Cdd:cd21253     6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDMVA 85
                          90       100
                  ....*....|....*....|.
gi 272506000 3518 MSRPDWKCVFVYVQSIYRRFR 3538
Cdd:cd21253    86 LKVPDKLSILTYVSQYYNYFH 106
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
3435-3537 1.62e-34

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: 129.05  E-value: 1.62e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3435 KDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVED 3514
Cdd:cd21248     4 KDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDPED 83
                          90       100
                  ....*....|....*....|...
gi 272506000 3515 mVEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21248    84 -VNVEQPDEKSIITYVVTYYHYF 105
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
3435-3537 1.82e-34

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: 129.38  E-value: 1.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3435 KDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVAdEKAGIAPLLDVED 3514
Cdd:cd21257    10 RNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAA-ESVGIKPSLELSE 88
                          90       100
                  ....*....|....*....|...
gi 272506000 3515 MVEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21257    89 MMYTDRPDWQSVMQYVAQIYKYF 111
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
3435-3537 8.75e-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: 126.76  E-value: 8.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3435 KDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVED 3514
Cdd:cd21194     4 KDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDAED 83
                          90       100
                  ....*....|....*....|...
gi 272506000 3515 mVEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21194    84 -VDVARPDEKSIMTYVASYYHYF 105
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
3435-3537 2.77e-33

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: 125.96  E-value: 2.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3435 KDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVAdEKAGIAPLLDVED 3514
Cdd:cd21256    16 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAA-ESVGIKSTLDINE 94
                          90       100
                  ....*....|....*....|...
gi 272506000 3515 MVEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21256    95 MVRTERPDWQSVMTYVTAIYKYF 117
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
3427-3537 5.90e-32

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: 122.25  E-value: 5.90e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3427 LNARAATVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGI 3506
Cdd:cd21291     4 INEEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGI 83
                          90       100       110
                  ....*....|....*....|....*....|.
gi 272506000 3507 APLLDVEDMVEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21291    84 PQLLDVEDVCDVAKPDERSIMTYVAYYFHAF 114
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
3433-3537 1.10e-31

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: 121.27  E-value: 1.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 3512
Cdd:cd21319     5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
                          90       100
                  ....*....|....*....|....*
gi 272506000 3513 EDmVEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21319    85 ED-VFTENPDEKSIITYVVAFYHYF 108
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
3433-3537 1.18e-31

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: 120.96  E-value: 1.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 3512
Cdd:cd21189     1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                          90       100
                  ....*....|....*....|....*
gi 272506000 3513 EDmVEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21189    81 ED-VDVPEPDEKSIITYVSSLYDVF 104
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
3436-3538 4.01e-31

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: 119.31  E-value: 4.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3436 DQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDM 3515
Cdd:cd22198     3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEM 82
                          90       100
                  ....*....|....*....|...
gi 272506000 3516 VEMSRPDWKCVFVYVQSIYRRFR 3538
Cdd:cd22198    83 ASLAVPDKLSMVSYLSQFYEAFK 105
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
3438-3538 6.07e-29

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: 113.02  E-value: 6.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3438 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDMVE 3517
Cdd:cd21197     5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDMVT 84
                          90       100
                  ....*....|....*....|.
gi 272506000 3518 MSRPDWKCVFVYVQSIYRRFR 3538
Cdd:cd21197    85 MHVPDRLSIITYVSQYYNHFR 105
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
3438-3537 7.02e-29

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: 112.90  E-value: 7.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3438 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVAdEKAGIAPLLDVEDMVE 3517
Cdd:cd21198     6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAA-AKLGIPRLLDPADMVL 84
                          90       100
                  ....*....|....*....|
gi 272506000 3518 MSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21198    85 LSVPDKLSVMTYLHQIRAHF 104
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
3433-3537 1.43e-28

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: 112.26  E-value: 1.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 3512
Cdd:cd21249     4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLDP 83
                          90       100
                  ....*....|....*....|....*
gi 272506000 3513 EDmVEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21249    84 ED-VAVPHPDERSIMTYVSLYYHYF 107
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
3438-3535 2.31e-28

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: 111.37  E-value: 2.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3438 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDmVE 3517
Cdd:cd21187     5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED-VN 83
                          90
                  ....*....|....*...
gi 272506000 3518 MSRPDWKCVFVYVQSIYR 3535
Cdd:cd21187    84 VEQPDKKSILMYVTSLFQ 101
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
3433-3537 2.29e-26

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: 106.29  E-value: 2.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 3512
Cdd:cd21321     5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTKLLDP 84
                          90       100
                  ....*....|....*....|....*
gi 272506000 3513 EDmVEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21321    85 ED-VNVDQPDEKSIITYVATYYHYF 108
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
3438-3539 6.91e-26

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: 104.57  E-value: 6.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3438 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDMVE 3517
Cdd:cd21252     5 LQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPEDMVS 84
                          90       100
                  ....*....|....*....|..
gi 272506000 3518 MSRPDWKCVFVYVQSIYRRFRN 3539
Cdd:cd21252    85 MKVPDCLSIMTYVSQYYNHFSN 106
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
3428-3537 1.44e-25

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: 104.37  E-value: 1.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3428 NARAATVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIA 3507
Cdd:cd21322    12 NRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHLGLT 91
                          90       100       110
                  ....*....|....*....|....*....|
gi 272506000 3508 PLLDVEDmVEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21322    92 KLLDPED-VNMEAPDEKSIITYVVSFYHYF 120
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
3432-3538 6.20e-25

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 101.98  E-value: 6.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  3432 ATVKDQLLQWCKHKTQEY-ENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQT--RRHNFELAFSVADEKAGIAP 3508
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEfdKLENINLALDVAEKKLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 272506000  3509 -LLDVEDMVEmsrPDWKCVFVYVQSIYRRFR 3538
Cdd:pfam00307   81 vLIEPEDLVE---GDNKSVLTYLASLFRRFQ 108
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
3427-3541 6.24e-25

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: 102.47  E-value: 6.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3427 LNARAATVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGI 3506
Cdd:cd21287     4 ISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDI 83
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 272506000 3507 APLLDVEDMVEMSRPDWKCVFVYVQSIYRRFRNCQ 3541
Cdd:cd21287    84 PKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQ 118
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
3436-3537 4.78e-24

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: 99.16  E-value: 4.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3436 DQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADeKAGIAPLLDVEDM 3515
Cdd:cd21254     4 QSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFA-SLGISRLLEPSDM 82
                          90       100
                  ....*....|....*....|..
gi 272506000 3516 VEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21254    83 VLLAVPDKLTVMTYLYQIRAHF 104
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
3433-3537 1.24e-23

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: 98.14  E-value: 1.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVAdEKAGIAPLLDV 3512
Cdd:cd21239     1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVA-EKLGVTRLLDP 79
                          90       100
                  ....*....|....*....|....*
gi 272506000 3513 EDmVEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21239    80 ED-VDVSSPDEKSVITYVSSLYDVF 103
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
3438-3537 1.28e-23

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: 97.88  E-value: 1.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3438 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDMVe 3517
Cdd:cd21192     8 LLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLEVEDVL- 86
                          90       100
                  ....*....|....*....|
gi 272506000 3518 MSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21192    87 VDKPDERSIMTYVSQFLRMF 106
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
3433-3537 2.63e-23

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: 97.00  E-value: 2.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 3512
Cdd:cd21243     5 GAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLDP 84
                          90       100
                  ....*....|....*....|....*
gi 272506000 3513 EDmVEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21243    85 ED-VDVDKPDEKSIMTYVAQFLKKY 108
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
3436-3538 3.83e-23

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: 96.87  E-value: 3.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3436 DQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDM 3515
Cdd:cd21250     7 NKLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEM 86
                          90       100
                  ....*....|....*....|...
gi 272506000 3516 VEMSRPDWKCVFVYVQSIYRRFR 3538
Cdd:cd21250    87 ASAEEPDKLSMVMYLSKFYELFR 109
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
3433-3537 5.45e-23

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: 96.32  E-value: 5.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 3512
Cdd:cd21320     2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
                          90       100
                  ....*....|....*....|....*
gi 272506000 3513 EDmVEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21320    82 ED-ISVDHPDEKSIITYVVTYYHYF 105
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
3427-3537 6.04e-23

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


Pssm-ID: 409138  Cd Length: 124  Bit Score: 96.72  E-value: 6.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3427 LNARAATVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGI 3506
Cdd:cd21289     4 ISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDI 83
                          90       100       110
                  ....*....|....*....|....*....|.
gi 272506000 3507 APLLDVEDMVEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21289    84 PKMLDAEDIVNTPKPDEKAIMTYVSCFYHAF 114
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
3427-3537 1.23e-22

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: 95.91  E-value: 1.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3427 LNARAATVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGI 3506
Cdd:cd21288     4 ISVEETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDI 83
                          90       100       110
                  ....*....|....*....|....*....|.
gi 272506000 3507 APLLDVEDMVEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21288    84 PKMLDAEDIVNTPKPDERAIMTYVSCFYHAF 114
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
3421-3541 1.84e-22

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: 95.54  E-value: 1.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3421 KFTDPALNARAATVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVA 3500
Cdd:cd21290     1 RFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 272506000 3501 DEKAGIAPLLDVEDMVEMSRPDWKCVFVYVQSIYRRFRNCQ 3541
Cdd:cd21290    81 EKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQ 121
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
3436-3533 1.99e-22

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: 94.30  E-value: 1.99e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000   3436 DQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQT----RRHNFELAFSVADEKAGIAPLLD 3511
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLsrfkKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 272506000   3512 VEDMVEMsRPDWKCVFVYVQSI 3533
Cdd:smart00033   81 PEDLVEG-PKLILGVIWTLISL 101
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
3437-3539 2.82e-22

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: 94.24  E-value: 2.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3437 QLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDMV 3516
Cdd:cd21251     9 KLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPIMTGKEMA 88
                          90       100
                  ....*....|....*....|...
gi 272506000 3517 EMSRPDWKCVFVYVQSIYRRFRN 3539
Cdd:cd21251    89 SVGEPDKLSMVMYLTQFYEMFKD 111
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
3437-3539 3.97e-22

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: 93.95  E-value: 3.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3437 QLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDMV 3516
Cdd:cd21195     8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEMA 87
                          90       100
                  ....*....|....*....|...
gi 272506000 3517 EMSRPDWKCVFVYVQSIYRRFRN 3539
Cdd:cd21195    88 SAQEPDKLSMVMYLSKFYELFRG 110
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
3434-3537 5.94e-22

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


Pssm-ID: 409075  Cd Length: 103  Bit Score: 92.91  E-value: 5.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3434 VKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVE 3513
Cdd:cd21226     1 SEDGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAE 80
                          90       100
                  ....*....|....*....|....
gi 272506000 3514 DMVEmSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21226    81 DVMT-GNPDERSIVLYTSLFYHAF 103
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
3436-3537 6.42e-22

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: 92.93  E-value: 6.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3436 DQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSvADEKAGIAPLLDVEDM 3515
Cdd:cd21255     4 QSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFE-AFASLGVPRLLEPADM 82
                          90       100
                  ....*....|....*....|..
gi 272506000 3516 VEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21255    83 VLLPIPDKLIVMTYLCQLRAHF 104
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
3433-3537 9.57e-22

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: 92.80  E-value: 9.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVAdEKAGIAPLLDV 3512
Cdd:cd21240     4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVA-ERLGVTRLLDA 82
                          90       100
                  ....*....|....*....|....*
gi 272506000 3513 EDmVEMSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21240    83 ED-VDVPSPDEKSVITYVSSIYDAF 106
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
3438-3535 3.56e-20

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: 88.45  E-value: 3.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3438 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTT-LTKQTRRHNFELAFSVADEKAGIAPLLDVEDmV 3516
Cdd:cd21233     5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSvVSQQSATERLDHAFNIARQHLGIEKLLDPED-V 83
                          90
                  ....*....|....*....
gi 272506000 3517 EMSRPDWKCVFVYVQSIYR 3535
Cdd:cd21233    84 ATAHPDKKSILMYVTSLFQ 102
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
3438-3534 4.57e-20

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: 87.71  E-value: 4.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3438 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDmVE 3517
Cdd:cd21234     5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED-VA 83
                          90
                  ....*....|....*..
gi 272506000 3518 MSRPDWKCVFVYVQSIY 3534
Cdd:cd21234    84 VQLPDKKSIIMYLTSLF 100
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
3433-3538 1.25e-19

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 96.55  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYEN-VQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRH--NFELAFSVADEKAGIAPL 3509
Cdd:COG5069   125 TKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARL 204
                          90       100
                  ....*....|....*....|....*....
gi 272506000 3510 LDVEDMVEMSRPDWKCVFVYVQSIYRRFR 3538
Cdd:COG5069   205 IGVEDIVNVSIPDERSIMTYVSWYIIRFG 233
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
3433-3534 6.99e-19

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: 84.30  E-value: 6.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 3512
Cdd:cd21238     2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 81
                          90       100
                  ....*....|....*....|..
gi 272506000 3513 EDmVEMSRPDWKCVFVYVQSIY 3534
Cdd:cd21238    82 ED-VDVPQPDEKSIITYVSSLY 102
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
3433-3530 6.19e-17

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: 79.11  E-value: 6.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 3512
Cdd:cd21244     5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLEP 84
                          90
                  ....*....|....*...
gi 272506000 3513 EDmVEMSRPDWKCVFVYV 3530
Cdd:cd21244    85 ED-VDVVNPDEKSIMTYV 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
3435-3535 7.42e-17

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 78.53  E-value: 7.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3435 KDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDY---TTLTKQTRRHNFELAFSVA-DEKAGIAPLL 3510
Cdd:cd00014     1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKinkKPKSPFKKRENINLFLNACkKLGLPELDLF 80
                          90       100
                  ....*....|....*....|....*
gi 272506000 3511 DVEDMVEmsRPDWKCVFVYVQSIYR 3535
Cdd:cd00014    81 EPEDLYE--KGNLKKVLGTLWALAL 103
Smoothelin pfam12510
Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is ...
3169-3218 5.87e-16

Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00307. Smoothelin is a cytoskeletal protein specifically expressed in differentiated smooth muscle cells and has been shown to co-localize with smooth muscle alpha actin.


Pssm-ID: 463614 [Multi-domain]  Cd Length: 50  Bit Score: 74.27  E-value: 5.87e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 272506000  3169 SSSSAPVTRTTCDIEEIWDEQVLKQLLEQASTYEERRKIRARLRELMAER 3218
Cdd:pfam12510    1 EETSAASKLTAEELEAIEDEEVLDKLLETATDYEERRLIRAAIRELRKRK 50
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
3435-3541 1.17e-15

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: 74.97  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3435 KDQLLQWCKHKTQEYenvQINNFSSSWSDGLAFCALIHHFLPDAF-DYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVE 3513
Cdd:cd21184     3 KSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLENATKAMDIAEEELGIPKIITPE 79
                          90       100
                  ....*....|....*....|....*...
gi 272506000 3514 DMVEmSRPDWKCVFVYVQSiyrrFRNCQ 3541
Cdd:cd21184    80 DMVS-PNVDELSVMTYLSY----FRNAK 102
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
3438-3537 2.35e-15

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: 74.44  E-value: 2.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3438 LLQWCKHKTQEYeNVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDmVE 3517
Cdd:cd21245     8 LLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPED-VM 85
                          90       100
                  ....*....|....*....|
gi 272506000 3518 MSRPDWKCVFVYVQSIYRRF 3537
Cdd:cd21245    86 VDSPDEQSIMTYVAQFLEHF 105
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
3431-3521 2.67e-15

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: 74.31  E-value: 2.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3431 AATVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLL 3510
Cdd:cd21196     1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVV 80
                          90
                  ....*....|.
gi 272506000 3511 DVEDMVEMSRP 3521
Cdd:cd21196    81 SAQAVVAGSDP 91
Smoothelin pfam12510
Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is ...
2594-2636 5.17e-14

Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00307. Smoothelin is a cytoskeletal protein specifically expressed in differentiated smooth muscle cells and has been shown to co-localize with smooth muscle alpha actin.


Pssm-ID: 463614 [Multi-domain]  Cd Length: 50  Bit Score: 68.49  E-value: 5.17e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 272506000  2594 SDLELEIEEIFDLQRLEKLLETVASYEMRRRIRAQMRLIRKNM 2636
Cdd:pfam12510    8 KLTAEELEAIEDEEVLDKLLETATDYEERRLIRAAIRELRKRK 50
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
3434-3530 6.60e-11

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: 62.70  E-value: 6.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3434 VKDQLLQWCKHKTQEYeNVQINNFSSSWSDGLAFCALIHHFLPD----------------------------AFDYTTLT 3485
Cdd:cd21224     1 VLSLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSllpldairqpttqtvdraqdeaedfwvaEFSPSTGD 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 272506000 3486 KQTR-------RHNFELAFSVADEKAGIAPLLDVEDMVEmSRPDWKCVFVYV 3530
Cdd:cd21224    80 SGLSsellaneKRNFKLVQQAVAELGGVPALLRASDMSN-TIPDEKVVILFL 130
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1394-1702 8.28e-11

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 68.56  E-value: 8.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1394 PKEEDSPKYPKGPETPKSPRNDQR--------IPSIPKKGQSPVQFKTEETPRYPQEQER--YPKEPETSQYPK--ESPR 1461
Cdd:PTZ00449  582 PKDPKHPKDPEEPKKPKRPRSAQRptrpkspkLPELLDIPKSPKRPESPKSPKRPPPPQRpsSPERPEGPKIIKspKPPK 661
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1462 NPK----------------------EDAETININEETTIVITKEGSKSPSPRWSPSPERRVPK-------SQQPPSPTAS 1512
Cdd:PTZ00449  662 SPKppfdpkfkekfyddyldaaaksKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKlprdeefPFEPIGDPDA 741
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1513 PSVSPVSGRKIPNEvESNFVTEKIIDCRGKTVVEKISQRP----RTPSPTTPKKNTK-PSQKIPERVPETESEPEKDSES 1587
Cdd:PTZ00449  742 EQPDDIEFFTPPEE-ERTFFHETPADTPLPDILAEEFKEEdihaETGEPDEAMKRPDsPSEHEDKPPGDHPSLPKKRHRL 820
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1588 EtkkttSVSVTKTETERRNSRTTKTKQPLPLKEPQSKvpagksPRKDSLTGRKRDSLVEETRittTTTTTRQGRKPSDTN 1667
Cdd:PTZ00449  821 D-----GLALSTTDLESDAGRIAKDASGKIVKLKRSK------SFDDLTTVEEAEEMGAEAR---KIVVDDDGTEADDED 886
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 272506000 1668 GSPSiKDRLRSSPRKQKTSPQQTRTPTPAQTRNPE 1702
Cdd:PTZ00449  887 THPP-EEKHKSEVRRRRPPKKPSKPKKPSKPKKPK 920
PHA03247 PHA03247
large tegument protein UL36; Provisional
566-1191 5.50e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.57  E-value: 5.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  566 YQEP--QRSPQKLREAPTPSWEQPATRRQPveedfsthgfPSVRTTTTSTRPDQPDGEVLHtsktvSRNQSANRktNTER 643
Cdd:PHA03247 2480 YRRPaeARFPFAAGAAPDPGGGGPPDPDAP----------PAPSRLAPAILPDEPVGEPVH-----PRMLTWIR--GLEE 2542
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  644 IIETQVEHPNAPSHSTPRSGSPRRSQPRDDYASSPRGPAGKPSQSRPSNTGGSTTTKTTTTSEPLTRRQLQKerevdaah 723
Cdd:PHA03247 2543 LASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPP-------- 2614
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  724 rafaaslrSSSPADSTTsvgshhqtPRSSVSSNRTFRREMREGSHDSQAPSESSRissttvtRHTTGGNVTSNTIKTKTT 803
Cdd:PHA03247 2615 --------SPLPPDTHA--------PDPPPPSPSPAANEPDPHPPPTVPPPERPR-------DDPAPGRVSRPRRARRLG 2671
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  804 KPVKTASEPRSPTPKAGGSvttttttittksspspapaspttaapptsapassappdnklsqytytTTKPGDIFSLPPTT 883
Cdd:PHA03247 2672 RAAQASSPPQRPRRRAARP-----------------------------------------------TVGSLTSLADPPPP 2704
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  884 PPTINNEPTLTTTRNTTTTTTTTTTATSDNLQNHPKKSAIEPATDTDSQPIRKVKLSANEAKVVEEAPCVRRQyyqlgne 963
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA------- 2777
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  964 GENPETPESSGTPANKKPHQMRRPHDEPEPQLRRSSKSPSVEPRQVQRETtfegrrvsqdreisideliLIEETSGAPGS 1043
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP-------------------LPPPTSAQPTA 2838
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1044 PKIPSPRAQS---------PGKPATRSQSPEKPQPR-ATPRQSPEKE--QPAFKQTHEVYtpSQPEKQFPRARSPE-KTP 1110
Cdd:PHA03247 2839 PPPPPGPPPPslplggsvaPGGDVRRRPPSRSPAAKpAAPARPPVRRlaRPAVSRSTESF--ALPPDQPERPPQPQaPPP 2916
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1111 GWTQPQVSPRQSPEKQLPRAQSPEKvPAVRQPSVSPRQSPEKQIPDPKTRDQGPGLPRISPRQSPEKQLPKDVPQKSRQS 1190
Cdd:PHA03247 2917 PQPQPQPPPPPQPQPPPPPPPRPQP-PLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPP 2995

                  .
gi 272506000 1191 P 1191
Cdd:PHA03247 2996 L 2996
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
3433-3519 4.32e-07

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: 50.84  E-value: 4.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3433 TVKDQLLQWCKHKTQEyenVQINNFSSSWSDGLAFCALIHHFLPDAF-DYTTLTKQTRRHNFELAFSVADEKAGIAPLLD 3511
Cdd:cd21230     1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
                          90
                  ....*....|...
gi 272506000 3512 VEDMV-----EMS 3519
Cdd:cd21230    78 PEEIInpnvdEMS 90
PHA03378 PHA03378
EBNA-3B; Provisional
970-1207 8.22e-07

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 55.46  E-value: 8.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  970 PESSGTPaNKKPHqmrrPHDEPEPQLRRSSKSPSVEPRQVQRETTFEGRRVSQDREISIDELIL--------IEETSGAP 1041
Cdd:PHA03378  590 PSYAQTP-WPVPH----PSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFptphqppqVEITPYKP 664
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1042 GSPKIPSPRAQ-SPGKPAT---RSQSPE--KPQPRATPRQSPEKEQPAFKQthevytpsQPEKQFPRARSPEKTPGWTQP 1115
Cdd:PHA03378  665 TWTQIGHIPYQpSPTGANTmlpIQWAPGtmQPPPRAPTPMRPPAAPPGRAQ--------RPAAATGRARPPAAAPGRARP 736
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1116 qvsPRQSPEKQLPRAQSPekvPAVRQPSVSPRQSPEKQI----PDPKTRDQGPGLPRISPRQSPEKQLPKDVPQKSRQSP 1191
Cdd:PHA03378  737 ---PAAAPGRARPPAAAP---GRARPPAAAPGRARPPAAapgaPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQLM 810
                         250
                  ....*....|....*.
gi 272506000 1192 EKDLTNQQRREEEIFR 1207
Cdd:PHA03378  811 PRAAPGQQGPTKQILR 826
PHA03247 PHA03247
large tegument protein UL36; Provisional
967-1283 8.31e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.71  E-value: 8.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  967 PETPESSGTPANKKPHQMRRPHDEPEPQLRRSSKSPSVE-PRQVQRETTFEG---------RRVSQDREISIDELilieE 1036
Cdd:PHA03247 2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSrPRRARRLGRAAQassppqrprRRAARPTVGSLTSL----A 2699
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1037 TSGAPGSPKIPSPRAQSPGKP---ATRSQSPEKPQPRATPRQSPEKEQPAFKQTHEVY----TPSQPEKQF-PRARSPEK 1108
Cdd:PHA03247 2700 DPPPPPPTPEPAPHALVSATPlppGPAAARQASPALPAAPAPPAVPAGPATPGGPARParppTTAGPPAPApPAAPAAGP 2779
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1109 TPGWTQPQVSPRQSPEKQLPRAQSPEKVPAV---RQPSVSPRQSPEKQIPDPKTRDQGPGLPRISPRQSPEKQLPKDVP- 1184
Cdd:PHA03247 2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAvlaPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPg 2859
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1185 ------QKSRQSPEKDLTNQQRREEEIFRSTITttqkrttnnlneefitneRDNQNQPISEKKPQIPANAEPNTKPSETI 1258
Cdd:PHA03247 2860 gdvrrrPPSRSPAAKPAAPARPPVRRLARPAVS------------------RSTESFALPPDQPERPPQPQAPPPPQPQP 2921
                         330       340
                  ....*....|....*....|....*
gi 272506000 1259 ESPDGGFPSKTTEVEAQPEVKESPT 1283
Cdd:PHA03247 2922 QPPPPPQPQPPPPPPPRPQPPLAPT 2946
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1381-1768 1.47e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 54.31  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1381 EDVEILVNPSKK---SPKEEDSPKY---PKGPET----PKSP---------RNDQRIPSIPKKGQSPVQFKTEETPRYP- 1440
Cdd:PTZ00449  483 QEIKKLIKKSKKklaPIEEEDSDKHdepPEGPEAsglpPKAPgdkegeegeHEDSKESDEPKEGGKPGETKEGEVGKKPg 562
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1441 -------------QEQERYPKEPETSQYPKE-----SPRNPKEDAETININEETTIVITKegskSPSPRWSPSPERRVPK 1502
Cdd:PTZ00449  563 pakehkpskiptlSKKPEFPKDPKHPKDPEEpkkpkRPRSAQRPTRPKSPKLPELLDIPK----SPKRPESPKSPKRPPP 638
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1503 SQQPPSPTASPSVSPVSGRKIPNEVESNF---VTEKIID------CRGKTVV------EKISQRPRTPSPTTPKKNTKPS 1567
Cdd:PTZ00449  639 PQRPSSPERPEGPKIIKSPKPPKSPKPPFdpkFKEKFYDdyldaaAKSKETKttvvldESFESILKETLPETPGTPFTTP 718
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1568 QKIPERVPETESEP-----EKDSES------------------ETKKTTSVSVTKTETERRNSRTTKTKQP-LPLKEPQS 1623
Cdd:PTZ00449  719 RPLPPKLPRDEEFPfepigDPDAEQpddiefftppeeertffhETPADTPLPDILAEEFKEEDIHAETGEPdEAMKRPDS 798
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1624 KVPAGKSPRKDSLTGRKRDSLVEETRITTTTTTTRQGRKPSDTNGSPSIKDRLRSSprKQKTSPQQTRTPTPAQTRNPED 1703
Cdd:PTZ00449  799 PSEHEDKPPGDHPSLPKKRHRLDGLALSTTDLESDAGRIAKDASGKIVKLKRSKSF--DDLTTVEEAEEMGAEARKIVVD 876
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 272506000 1704 DVDGDSSSPDASPTrvgnERRRSSNISVHTEIIIDHMAPKSPKTERRSQGGTGNVPSPIRKLPVT 1768
Cdd:PTZ00449  877 DDGTEADDEDTHPP----EEKHKSEVRRRRPPKKPSKPKKPSKPKKPKKPDSAFIPSIIAIFLVS 937
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1035-1421 3.59e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 53.15  E-value: 3.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1035 EETSGAPGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFKQTHEVYTPSQPEKQfpraRSPEKTPGWTQ 1114
Cdd:PTZ00449  502 EDSDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKE----HKPSKIPTLSK 577
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1115 PQVSPRQSPEKQLPRAQSPEKVPAVRQPSVSPRqSPEK----QIPDPKTRDQGPGLPR--------ISPRQSPEKQLPKD 1182
Cdd:PTZ00449  578 KPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPK-SPKLpellDIPKSPKRPESPKSPKrppppqrpSSPERPEGPKIIKS 656
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1183 VPQKSRQSPEKDLTNQQRREEEIFRSTITTTQKRTTNNLNEEFITNERDNQNQ----PISEKKPQIPANAEPNTKPSETI 1258
Cdd:PTZ00449  657 PKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPEtpgtPFTTPRPLPPKLPRDEEFPFEPI 736
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1259 ESPDGGFPSK----TTEVEAQPEVKESPTYRK-KGLTRRETFEDRCRQILGMEEDG----DTQGTYTERPNNEQEDVNVS 1329
Cdd:PTZ00449  737 GDPDAEQPDDieffTPPEEERTFFHETPADTPlPDILAEEFKEEDIHAETGEPDEAmkrpDSPSEHEDKPPGDHPSLPKK 816
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1330 HTTIETIQVKIEDCPND------DEDDKPRRVTET------YVVRTQPKIKVEEELFV---DVTEAEDVEilVNPSK--- 1391
Cdd:PTZ00449  817 RHRLDGLALSTTDLESDagriakDASGKIVKLKRSksfddlTTVEEAEEMGAEARKIVvddDGTEADDED--THPPEekh 894
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 272506000 1392 -------KSPKEEDSPKYPKGPETPKSPrNDQRIPSI 1421
Cdd:PTZ00449  895 ksevrrrRPPKKPSKPKKPSKPKKPKKP-DSAFIPSI 930
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
3439-3516 4.25e-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: 47.68  E-value: 4.25e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 272506000 3439 LQWCKHKTQEyenVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSvADEKAGIAPLLDVEDMV 3516
Cdd:cd21185     7 LRWVRQLLPD---VDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMA 80
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
3435-3515 5.32e-06

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


Pssm-ID: 409078  Cd Length: 105  Bit Score: 47.77  E-value: 5.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3435 KDQLLQWCKHKTQEyenVQINNFSSSWSDGLAFCALIHHFLPDAF-DYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVE 3513
Cdd:cd21229     5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81

                  ..
gi 272506000 3514 DM 3515
Cdd:cd21229    82 DL 83
PRK10263 PRK10263
DNA translocase FtsK; Provisional
921-1463 9.31e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 52.01  E-value: 9.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  921 SAIEPATDTDSQPIRKVKLSAN--EAKVVEEAPCVRRQYYQLGNEGENPETPESSGTPANKKPHQMRRPHDE----PEPQ 994
Cdd:PRK10263  324 AAATTATQSWAAPVEPVTQTPPvaSVDVPPAQPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEplqqPVQP 403
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  995 LRRSSKSPSVEPRQVQRETTFEGRRVSQDREISIDELILIEETSGA--PGSPKIPSPRAQSPGK-PATRSQSPEKPQPRA 1071
Cdd:PRK10263  404 QQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAeeQQSTFAPQSTYQTEQTyQQPAAQEPLYQQPQP 483
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1072 TPRQSPEKEQPAFKQTHevytPSQP------EKQFPRARSPEKTPGWTQPQVSPRQSPEKQLP--RAQSPEKVPAVRQ-P 1142
Cdd:PRK10263  484 VEQQPVVEPEPVVEETK----PARPplyyfeEVEEKRAREREQLAAWYQPIPEPVKEPEPIKSslKAPSVAAVPPVEAaA 559
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1143 SVSPRQSPEKQ----------IPDPKTRDQGPGLPRISPRQSPEKQLPKdvPQKSRQSPEKDLTN------QQRREEEIF 1206
Cdd:PRK10263  560 AVSPLASGVKKatlatgaaatVAAPVFSLANSGGPRPQVKEGIGPQLPR--PKRIRVPTRRELASygiklpSQRAAEEKA 637
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1207 RSTITTTQKRTTNNLNEEFITNERDNQNQPISEKKPQIPANAEPNTKPSETIESPDGGfpskttEVEAQPEVKESPTYRK 1286
Cdd:PRK10263  638 REAQRNQYDSGDQYNDDEIDAMQQDELARQFAQTQQQRYGEQYQHDVPVNAEDADAAA------EAELARQFAQTQQQRY 711
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1287 KGltrretfedrcrqilgmeedgdtqgtytERPNNEQEdVNVSHTTIETIQVKIEDCPNddeddkprrvtetyvvrtqpk 1366
Cdd:PRK10263  712 SG----------------------------EQPAGANP-FSLDDFEFSPMKALLDDGPH--------------------- 741
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1367 ikveEELFVDVTEAEDVEILVNPSKKSPKEEDSPKYPKG----PETPKSPRNDQRIPSIPKKGQSpvQFKTEETPRYPQE 1442
Cdd:PRK10263  742 ----EPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPqyqqPQQPVAPQPQYQQPQQPVAPQP--QYQQPQQPVAPQP 815
                         570       580
                  ....*....|....*....|.
gi 272506000 1443 QERYPKEPETSQYPKESPRNP 1463
Cdd:PRK10263  816 QYQQPQQPVAPQPQYQQPQQP 836
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
3452-3515 8.12e-05

CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.


Pssm-ID: 432229  Cd Length: 85  Bit Score: 43.83  E-value: 8.12e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 272506000  3452 VQINNFSSSWSDGLAFCALIHHFLPDAFDYT------TLTKQTRRHNFELAFSVADEKAGIAPL-LDVEDM 3515
Cdd:pfam11971   11 PPVEDLLRDLSDGCALAALIHFYCPQLIDLEdiclkeSMSLADSLYNIQLLQEFCQRHLGNRCChLTLEDL 81
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
3438-3517 1.14e-04

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 44.21  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 3438 LLQWCKH--KTQEYENVQINNFSSSWSDGLAFCALIHHFLP----DAFDYTTLTKQTRRHNFELAFSVAdEKAGIAPLLD 3511
Cdd:cd21218    15 LLRWVNYhlKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPelcdKELVLEVLSEEDLEKRAEKVLQAA-EKLGCKYFLT 93

                  ....*.
gi 272506000 3512 VEDMVE 3517
Cdd:cd21218    94 PEDIVS 99
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
926-1184 2.28e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.45  E-value: 2.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000   926 ATDTDSQPIRKVKLSANEAKVVEEAPC----VRRQYYQLGNEGENPETPESSGTpankKPHQMRRPHDEPEpqlrrsSKS 1001
Cdd:pfam03154   49 AASTSSNDSKAESMKKSSKKIKEEAPSplksAKRQREKGASDTEEPERATAKKS----KTQEISRPNSPSE------GEG 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  1002 PSVEPRQVQRETTFEGRRVSQDREISidelilieetsgapgSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQ 1081
Cdd:pfam03154  119 ESSDGRSVNDEGSSDPKDIDQDNRST---------------SPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASP 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  1082 PAFKQTHEVYTPSQPEKQFPRARSPEKTPGWTQPQVSP----------RQSPEKQLPRAQSPEKVPAVRQPSVSPRQSPE 1151
Cdd:pfam03154  184 PSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTqstaaphtliQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSP 263
                          250       260       270
                   ....*....|....*....|....*....|...
gi 272506000  1152 KQIPDPKTRDQGPGLPRisPRQSPEKQLPKDVP 1184
Cdd:pfam03154  264 QPLPQPSLHGQMPPMPH--SLQTGPSHMQHPVP 294
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
961-1157 2.85e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.09  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  961 GNEGENPETPESSGTPANKKPHQMRRPHDEPEPQLRRSSKSPSVEPRQVQRETTFEGRRVSQDREISIDELILIEETSGA 1040
Cdd:PHA03307  250 GPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSST 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1041 PGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFKQTHEVYTPSQPEKqfPRARSPEKTPGWTQ--PQVS 1118
Cdd:PHA03307  330 SSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTR--RRARAAVAGRARRRdaTGRF 407
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 272506000 1119 PRQSPEKQLPRAQSPEKVPAVRQPSVSPRQSPEKQIPDP 1157
Cdd:PHA03307  408 PAGRPRPSPLDAGAASGAFYARYPLLTPSGEPWPGSPPP 446
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
940-1190 3.15e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.79  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  940 SANEAKVVEEAPCVRRQYYQLGNEGENPETPESSGTPANKKPHQMRRPhdepepqlrrSSKSPSVEPRQVQRETTFEGRR 1019
Cdd:PRK12323  376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAP----------ARRSPAPEALAAARQASARGPG 445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1020 VSQdreisideliliEETSGAPGSP--KIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFKQTHEVYTPSqpe 1097
Cdd:PRK12323  446 GAP------------APAPAPAAAPaaAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPA--- 510
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1098 kqfPRARSPEKTPGWTQPQVSPRQSPEKQLPRAQSPEKVPAvrqPSVSPRQSPEKQIPDPKTRDQGPGLPRISPRQSPE- 1176
Cdd:PRK12323  511 ---PAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAA---PAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPAl 584
                         250
                  ....*....|....*..
gi 272506000 1177 -KQLP-KDVPQK-SRQS 1190
Cdd:PRK12323  585 aARLPvRGLAQQlARQS 601
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1041-1127 3.93e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 46.62  E-value: 3.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1041 PGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFKQTHEVYTPSQPEKQFPRARSPEKT----PGWTQPQ 1116
Cdd:PRK10263  755 PQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPvapqPQYQQPQ 834
                          90
                  ....*....|.
gi 272506000 1117 VSPRQSPEKQL 1127
Cdd:PRK10263  835 QPVAPQPQDTL 845
PTZ00121 PTZ00121
MAEBL; Provisional
2080-2248 4.09e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 2080 RQSEPERELDEESEPELDRDTDVEDDDQTSQLETEEEITQTVTKKETLKEFKQQTKETRETRRDSKAEPEKLQKKSPQTK 2159
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 2160 VKEES----ARVPKYQAKVSQKVSQWEPKKQPQREPKVTQKETPLEPKKQPLSKVKdEPEKVNKREPKVPQKESQTKLKE 2235
Cdd:PTZ00121 1661 IKAAEeakkAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK-KAEELKKAEEENKIKAEEAKKEA 1739
                         170
                  ....*....|...
gi 272506000 2236 EPERVTKKTPQKE 2248
Cdd:PTZ00121 1740 EEDKKKAEEAKKD 1752
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1034-1146 5.04e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 5.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1034 IEETSGAPGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAfkQTHEVYTPSQPEKQFPRARSPEKTPG-W 1112
Cdd:PRK07764  392 GAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAP--PSPAGNAPAGGAPSPPPAAAPSAQPApA 469
                          90       100       110
                  ....*....|....*....|....*....|....
gi 272506000 1113 TQPQVSPRQSPEKQLPRAQSPEKVPAVRQPSVSP 1146
Cdd:PRK07764  470 PAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAP 503
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1047-1180 6.74e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.85  E-value: 6.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1047 PSPRAQSPG-KPATRSQSPEKPQPRATPRQSPEKEQPAFKQTHEVYTPSQPEKQFPRARSPEktPGWTQPQVSPRQSPEK 1125
Cdd:PRK10263  740 PHEPLFTPIvEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQ--PQYQQPQQPVAPQPQY 817
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 272506000 1126 QLPRaQSPEKVPAVRQPSVSPRQSPEKQIPDPKTRDQGPGlpriSPRQSPEKQLP 1180
Cdd:PRK10263  818 QQPQ-QPVAPQPQYQQPQQPVAPQPQDTLLHPLLMRNGDS----RPLHKPTTPLP 867
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1040-1193 8.20e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.25  E-value: 8.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1040 APGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAfkqthevytpsQPEKQFPRARSPEKTPGWTQPQVSP 1119
Cdd:PRK12323  373 GPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAA-----------RAVAAAPARRSPAPEALAAARQASA 441
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 272506000 1120 RQS-PEKQLPRAQSPEKVPAVRQPSVSPRQSPEKQIPDPKTRDQGPGLPRISPRQSPEKQLPKDVPQKSRQSPEK 1193
Cdd:PRK12323  442 RGPgGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDA 516
PHA03247 PHA03247
large tegument protein UL36; Provisional
1033-1200 8.73e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 8.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1033 LIEETSGAPGSPKIPSPRAQSPGKPaTRSQSPEKPQPRatprqspekeqpafkqthevytPSQPEKQfPRARSPEKTPGW 1112
Cdd:PHA03247 2540 LEELASDDAGDPPPPLPPAAPPAAP-DRSVPPPRPAPR----------------------PSEPAVT-SRARRPDAPPQS 2595
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1113 TQPQ--VSPRQSPEKQLPRAQSPEKVPAVRQPSVSPRQSPEKqipdpktrdqgpgLPRISPRQSPEKQLPKDVPQKSRQS 1190
Cdd:PHA03247 2596 ARPRapVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANE-------------PDPHPPPTVPPPERPRDDPAPGRVS 2662
                         170
                  ....*....|
gi 272506000 1191 PEKDLTNQQR 1200
Cdd:PHA03247 2663 RPRRARRLGR 2672
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
967-1194 9.40e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 9.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  967 PETPESSGTPANKKPHQMRRPHDEPEPQLRRSSKSPSVEPRQVQRETTfegrrvsQDREISiDELILIEETSGAPGSPKI 1046
Cdd:PHA03307  120 TPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAA-------SSRQAA-LPLSSPEETARAPSSPPA 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1047 PSPRAQSPGKPATRSQSPEKP--QPRATPRQSPEKEQ---PAFKQTHEVYTPSQPEKQFPRARSPEKTPGwtqPQVSPRQ 1121
Cdd:PHA03307  192 EPPPSTPPAAASPRPPRRSSPisASASSPAPAPGRSAaddAGASSSDSSSSESSGCGWGPENECPLPRPA---PITLPTR 268
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 272506000 1122 spekqlPRAQSPEKVPAVRQPSVSPRQSPekQIPDPKTRDQGPGLPRISPRQSPEKQL---PKDVPQKSRQSPEKD 1194
Cdd:PHA03307  269 ------IWEASGWNGPSSRPGPASSSSSP--RERSPSPSPSSPGSGPAPSSPRASSSSsssRESSSSSTSSSSESS 336
PTZ00121 PTZ00121
MAEBL; Provisional
2080-2254 1.38e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 2080 RQSEPERELDEESEPELDRDTDVEDDDQTSQLETEEEitQTVTKKETLKefKQQTKETRETRRDSKAEPEKLQKKSPQTK 2159
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIKAAEEA--KKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 2160 VKEESARVPKYQAKVSQKVSQWEP--KKQPQREPKVTQ-KETPLEPKKQPLSKVKDEPEKVNKREPKVPQKESQTKLKEE 2236
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEElkKAEEENKIKAEEaKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
                         170
                  ....*....|....*...
gi 272506000 2237 PERVTKKTPQKEPRKEPL 2254
Cdd:PTZ00121 1777 KEAVIEEELDEEDEKRRM 1794
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
479-750 1.57e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  479 PTSRVVQKAPTPSYAPPSHSPRQSPAkdfSTHGFPSVRPNKATQEYPSQRPGIAGEEVVVVRSEKSRQVKQQTSSQRTIE 558
Cdd:PHA03307  175 PLSSPEETARAPSSPPAEPPPSTPPA---AASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGP 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  559 TEVVGDDYQEPQRSPQKLREAPTpsWEQPATRRQPVEEDfsthgfPSVRTTTTSTRPDQPDGEVLHTSKTVSRNQSANRK 638
Cdd:PHA03307  252 ENECPLPRPAPITLPTRIWEASG--WNGPSSRPGPASSS------SSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRE 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  639 TNTERIIETqvehPNAPSHSTPRSGSPRRSQPRDDYASSPRGPAGKPSQSRPSNTGGSTTTKTTTTSEPLTRRQLQKERE 718
Cdd:PHA03307  324 SSSSSTSSS----SESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRAR 399
                         250       260       270
                  ....*....|....*....|....*....|..
gi 272506000  719 VDAAHRAFAASLRSSSPADSTTSVGSHHQTPR 750
Cdd:PHA03307  400 RRDATGRFPAGRPRPSPLDAGAASGAFYARYP 431
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1037-1204 3.21e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1037 TSGAPGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFK--QTHEVYTPSQPEKQFPRARSPEKTPGWTQ 1114
Cdd:PRK07764  617 APAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGgdGWPAKAGGAAPAAPPPAPAPAAPAAPAGA 696
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1115 PQVSPRQSPEKQLPRAQSPEKV---PAVRQPSVSPRQSPEKQIPDPKTRDQGPGlPRISPRQSPEKQLPKDVPQKSRQSP 1191
Cdd:PRK07764  697 APAQPAPAPAATPPAGQADDPAaqpPQAAQGASAPSPAADDPVPLPPEPDDPPD-PAGAPAQPPPPPAPAPAAAPAAAPP 775
                         170
                  ....*....|...
gi 272506000 1192 EKDLTNQQRREEE 1204
Cdd:PRK07764  776 PSPPSEEEEMAED 788
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1008-1255 3.95e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1008 QVQRETTFEGRRVSQDREISIDELILIEETSGAPGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFKQT 1087
Cdd:NF033839  254 KVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVK 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1088 HEVYTPS-----QPEKQFPRAR-SPEKTPGWTQPQVSPRQSPEKQLPRAQSPEKVPAVRQPSVSPRQSPEKQIPDPKTRD 1161
Cdd:NF033839  334 PQPEKPKpevkpQLETPKPEVKpQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQP 413
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1162 QGPGlPRISPrqSPEKQLPKDVPQKSRQSPEKDLTNQQRREE-----EIFRSTITTTQKRTTNNLNEEFITNERDNQNQP 1236
Cdd:NF033839  414 EKPK-PEVKP--QPEKPKPEVKPQPEKPKPEVKPQPEKPKPEvkpqpETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQ 490
                         250
                  ....*....|....*....
gi 272506000 1237 ISEKKPQIPANAEPNTKPS 1255
Cdd:NF033839  491 ADDKKPSTPNNLSKDKQPS 509
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1000-1192 4.77e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1000 KSPSVEPRQVQRETTFEGRRVSQDREISIDELILIEETSGAPGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEK 1079
Cdd:NF033839  290 KKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQP 369
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1080 EQPAFKQTHEVYTPSQPEKQFPRARSPEKTPGWTQPQVSPRQSPEKqlpraQSPEKVPAVRQPSVSPRQSPEKQIPDPKT 1159
Cdd:NF033839  370 EKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEK-----PKPEVKPQPEKPKPEVKPQPEKPKPEVKP 444
                         170       180       190
                  ....*....|....*....|....*....|...
gi 272506000 1160 RDQGPGlPRISPRqsPEKQLPKDVPQKSRQSPE 1192
Cdd:NF033839  445 QPEKPK-PEVKPQ--PETPKPEVKPQPEKPKPE 474
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
998-1208 6.56e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 6.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  998 SSKSPSVEPRQVQRETTFEGRRVSQDREISIDELILIEETSGAPGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSP 1077
Cdd:PHA03307   57 AGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSE 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1078 EKEqpafkqthevytPSQPEKQFPRARSPEKTPGWTQPQVSPRQSPEKQLPRAQSPEKVPAVRQPSVSPRqsPEKQIPDP 1157
Cdd:PHA03307  137 MLR------------PVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPP--PSTPPAAA 202
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 272506000 1158 KTRDQGPGLPRISPRQSPEKQLPKDVPQKSRQSPEKDLTNQQRREEEIFRS 1208
Cdd:PHA03307  203 SPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPEN 253
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
935-1204 7.26e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 42.33  E-value: 7.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000   935 RKVKLSANEAKVVEEAPCVRRQYYQLGNEGENPETPESSGTPANKKPhqmrrphdEPEPQLRRSS------KSPSVEPRQ 1008
Cdd:pfam09770  104 RQQPAARAAQSSAQPPASSLPQYQYASQQSQQPSKPVRTGYEKYKEP--------EPIPDLQVDAslwgvaPKKAAAPAP 175
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  1009 VQRETTFEGRRVSQDREI-SIDELiliEE----TSGAPGSPKIPSPrAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPA 1083
Cdd:pfam09770  176 APQPAAQPASLPAPSRKMmSLEEV---EAamraQAKKPAQQPAPAP-AQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQ 251
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000  1084 FKQTHEvyTPSQPEKQFPRARSPEKTPgwTQPQVSPRQSPEKQLPRaqspekvpavrQPSVSPRQ---------SPEKQI 1154
Cdd:pfam09770  252 QPQQHP--GQGHPVTILQRPQSPQPDP--AQPSIQPQAQQFHQQPP-----------PVPVQPTQilqnpnrlsAARVGY 316
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 272506000  1155 PDPKTRDQGPGLPRISPRQSPekQLPKDVPQKSRQSPEKDLTNQQRR---EEE 1204
Cdd:pfam09770  317 PQNPQPGVQPAPAHQAHRQQG--SFGRQAPIITHPQQLAQLSEEEKAaylDEE 367
PHA03247 PHA03247
large tegument protein UL36; Provisional
1394-1722 8.46e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 8.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1394 PKEEDSPKYPKGPETPKSPRNDQRIPSIPKKGQSPVQFKTEETPRYPQEQERYPKEPETSQYPKESPRN-------PKED 1466
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAapaagppRRLT 2784
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1467 AETININEETTIVITKEGSKSPSPRWSPSPERRVPKSQQPPSPTASP-SVSPVSGRKIPNEVESNFVTEKIIdCRGKTVV 1545
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPtSAQPTAPPPPPGPPPPSLPLGGSV-APGGDVR 2863
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1546 EKISQRPRTPSPTTPKKNTKPSQKIPERVPETESEPEKDSESETKKTTSVSVTKTETERRNSRTTKTKQPLPLKEPQSKV 1625
Cdd:PHA03247 2864 RRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPL 2943
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 272506000 1626 PAGKSPRKDS----LTGRKRDSLVEETRITTTTTTTRQGRKPSDTNGSPSIKDRLRSSPR----KQKTSPQQTRTPTPA- 1696
Cdd:PHA03247 2944 APTTDPAGAGepsgAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRvsswASSLALHEETDPPPVs 3023
                         330       340       350
                  ....*....|....*....|....*....|
gi 272506000 1697 --QTRNPEDDVDG--DSSSPDASPTRVGNE 1722
Cdd:PHA03247 3024 lkQTLWPPDDTEDsdADSLFDSDSERSDLE 3053
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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