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Conserved domains on  [gi|440216479|gb|AGB95125|]
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uncharacterized protein Dmel_CG34417, isoform R [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 ...
5020-5125 1.05e-67

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: 1.05e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 5099
Cdd:cd21200     1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
                          90       100
                  ....*....|....*....|....*..
gi 440216479 5100 EDMVEMS-RPDWKCVFVYVQSIYRRFR 5125
Cdd:cd21200    81 EDMVRMGnRPDWKCVFTYVQSLYRHLR 107
Smoothelin pfam12510
Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is ...
3127-3176 1.79e-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: 76.20  E-value: 1.79e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 440216479  3127 SSSSAPVTRTTCDIEEIWDEQVLKQLLEQASTYEERRKIRARLRELMAER 3176
Cdd:pfam12510    1 EETSAASKLTAEELEAIEDEEVLDKLLETATDYEERRLIRAAIRELRKRK 50
Smoothelin pfam12510
Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is ...
2594-2636 1.78e-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: 70.42  E-value: 1.78e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 440216479  2594 SDLELEIEEIFDLQRLEKLLETVASYEMRRRIRAQMRLIRKNM 2636
Cdd:pfam12510    8 KLTAEELEAIEDEEVLDKLLETATDYEERRLIRAAIRELRKRK 50
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
1394-1702 2.78e-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: 70.49  E-value: 2.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1394 PKEEDSPKYPKGPETPKSPRNDQR--------IPSIPKKGQSPVQFKTEETPRYPQEQER--YPKEPETSQYPK--ESPR 1461
Cdd:PTZ00449  582 PKDPKHPKDPEEPKKPKRPRSAQRptrpkspkLPELLDIPKSPKRPESPKSPKRPPPPQRpsSPERPEGPKIIKspKPPK 661
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1462 NPK----------------------EDAETININEETTIVITKEGSKSPSPRWSPSPERRVPK-------SQQPPSPTAS 1512
Cdd:PTZ00449  662 SPKppfdpkfkekfyddyldaaaksKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKlprdeefPFEPIGDPDA 741
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1513 PSVSPVSGRKIPNEvESNFVTEKIIDCRGKTVVEKISQRP----RTPSPTTPKKNTK-PSQKIPERVPETESEPEKDSES 1587
Cdd:PTZ00449  742 EQPDDIEFFTPPEE-ERTFFHETPADTPLPDILAEEFKEEdihaETGEPDEAMKRPDsPSEHEDKPPGDHPSLPKKRHRL 820
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1588 EtkkttSVSVTKTETERRNSRTTKTKQPLPLKEPQSKvpagksPRKDSLTGRKRDSLVEETRittTTTTTRQGRKPSDTN 1667
Cdd:PTZ00449  821 D-----GLALSTTDLESDAGRIAKDASGKIVKLKRSK------SFDDLTTVEEAEEMGAEAR---KIVVDDDGTEADDED 886
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 440216479 1668 GSPSiKDRLRSSPRKQKTSPQQTRTPTPAQTRNPE 1702
Cdd:PTZ00449  887 THPP-EEKHKSEVRRRRPPKKPSKPKKPSKPKKPK 920
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3810-3916 8.45e-08

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 8.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 3810 QREQSQRDQNQRELSKREQFQREQLQREQLQREQLQREKLQREQLQREQLQREQLQREQLQREQLQREQLQREQLQRDQL 3889
Cdd:COG1196   671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
                          90       100
                  ....*....|....*....|....*..
gi 440216479 3890 QLQQQQQAAAAVQIERQRRQELERQLR 3916
Cdd:COG1196   751 EALEELPEPPDLEELERELERLEREIE 777
PHA03247 super family cl33720
large tegument protein UL36; Provisional
566-1191 2.03e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 2.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  566 YQEP--QRSPQKLREAPTPSWEQPATRRQPveedfsthgfPSVRTTTTSTRPDQPDGEVLHtsktvSRNQSANRktNTER 643
Cdd:PHA03247 2480 YRRPaeARFPFAAGAAPDPGGGGPPDPDAP----------PAPSRLAPAILPDEPVGEPVH-----PRMLTWIR--GLEE 2542
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  644 IIETQVEHPNAPSHSTPRSGSPRRSQPRDDYASSPRGPAGKPSQSRPSNTGGSTTTKTTTTSEPLTRRQLQKerevdaah 723
Cdd:PHA03247 2543 LASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPP-------- 2614
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  724 rafaaslrSSSPADSTTsvgshhqtPRSSVSSNRTFRREMREGSHDSQAPSESSRissttvtRHTTGGNVTSNTIKTKTT 803
Cdd:PHA03247 2615 --------SPLPPDTHA--------PDPPPPSPSPAANEPDPHPPPTVPPPERPR-------DDPAPGRVSRPRRARRLG 2671
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  804 KPVKTASEPRSPTPKAGGSvttttttittksspspapaspttaapptsapassappdnklsqytytTTKPGDIFSLPPTT 883
Cdd:PHA03247 2672 RAAQASSPPQRPRRRAARP-----------------------------------------------TVGSLTSLADPPPP 2704
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  884 PPTINNEPTLTTTRNTTTTTTTTTTATSDNLQNHPKKSAIEPATDTDSQPIRKVKLSANEAKVVEEAPCVRRQyyqlgne 963
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA------- 2777
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  964 GENPETPESSGTPANKKPHQMRRPHDEPEPQLRRSSKSPSVEPRQVQRETtfegrrvsqdreisideliLIEETSGAPGS 1043
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP-------------------LPPPTSAQPTA 2838
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1044 PKIPSPRAQS---------PGKPATRSQSPEKPQPR-ATPRQSPEKE--QPAFKQTHEVYtpSQPEKQFPRARSPE-KTP 1110
Cdd:PHA03247 2839 PPPPPGPPPPslplggsvaPGGDVRRRPPSRSPAAKpAAPARPPVRRlaRPAVSRSTESF--ALPPDQPERPPQPQaPPP 2916
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1111 GWTQPQVSPRQSPEKQLPRAQSPEKvPAVRQPSVSPRQSPEKQIPDPKTRDQGPGLPRISPRQSPEKQLPKDVPQKSRQS 1190
Cdd:PHA03247 2917 PQPQPQPPPPPQPQPPPPPPPRPQP-PLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPP 2995

                  .
gi 440216479 1191 P 1191
Cdd:PHA03247 2996 L 2996
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
1035-1421 1.51e-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: 55.08  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1035 EETSGAPGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFKQTHEVYTPSQPEKQfpraRSPEKTPGWTQ 1114
Cdd:PTZ00449  502 EDSDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKE----HKPSKIPTLSK 577
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1115 PQVSPRQSPEKQLPRAQSPEKVPAVRQPSVSPRqSPEK----QIPDPKTRDQGPGLPR--------ISPRQSPEKQLPKD 1182
Cdd:PTZ00449  578 KPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPK-SPKLpellDIPKSPKRPESPKSPKrppppqrpSSPERPEGPKIIKS 656
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1183 VPQKSRQSPEKDLTNQQRREEEIFRSTITTTQKRTTNNLNEEFITNERDNQNQ----PISEKKPQIPANAEPNTKPSETI 1258
Cdd:PTZ00449  657 PKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPEtpgtPFTTPRPLPPKLPRDEEFPFEPI 736
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1259 ESPDGGFPSK----TTEVEAQPEVKESPTYRK-KGLTRRETFEDRCRQILGMEEDG----DTQGTYTERPNNEQEDVNVS 1329
Cdd:PTZ00449  737 GDPDAEQPDDieffTPPEEERTFFHETPADTPlPDILAEEFKEEDIHAETGEPDEAmkrpDSPSEHEDKPPGDHPSLPKK 816
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1330 HTTIETIQVKIEDCPND------DEDDKP------RRVTETYVVRTQPKIKVEEELFV---DVTEAEDVEilVNPSK--- 1391
Cdd:PTZ00449  817 RHRLDGLALSTTDLESDagriakDASGKIvklkrsKSFDDLTTVEEAEEMGAEARKIVvddDGTEADDED--THPPEekh 894
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 440216479 1392 -------KSPKEEDSPKYPKGPETPKSPrNDQRIPSI 1421
Cdd:PTZ00449  895 ksevrrrRPPKKPSKPKKPSKPKKPKKP-DSAFIPSI 930
PTZ00121 super family cl31754
MAEBL; Provisional
2080-2248 2.09e-04

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 2080 RQSEPERELDEESEPELDRDTDVEDDDQTSQLETEEEITQTVTKKETLKEFKQQTKETRETRRDSKAEPEKLQKKSPQTK 2159
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 2160 VKEES----ARVPKYQAKVSQKVSQWEPKKQPQREPKVTQKETPLEPKKQPLSKVKdEPEKVNKREPKVPQKESQTKLKE 2235
Cdd:PTZ00121 1661 IKAAEeakkAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK-KAEELKKAEEENKIKAEEAKKEA 1739
                         170
                  ....*....|...
gi 440216479 2236 EPERVTKKTPQKE 2248
Cdd:PTZ00121 1740 EEDKKKAEEAKKD 1752
PHA03247 super family cl33720
large tegument protein UL36; Provisional
4126-4601 1.08e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4126 KRPSLPNAMDPGTAAPPrqvyqaPPPPTNIS-------FTYADFPPVRRPQGASAHNYRSQPCLTSAVDQVEALTNPLGA 4198
Cdd:PHA03247 2609 RGPAPPSPLPPDTHAPD------PPPPSPSPaanepdpHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQR 2682
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4199 PlvltssNPTYLPPPgsrrfdyiSSPVDVDADSPPNSPTSfmtMPNPTLMTDNTDDDLDLDSDNNMLEYRAETKVMRKPR 4278
Cdd:PHA03247 2683 P------RRRAARPT--------VGSLTSLADPPPPPPTP---EPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVP 2745
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4279 SQTAVRVADRRNAhmsddevygknSRAAKSllytmkqlggGPGNAsvgnsgqrrqplTAPSSPKSGCLSPDGRPYQAPLV 4358
Cdd:PHA03247 2746 AGPATPGGPARPA-----------RPPTTA----------GPPAP------------APPAAPAAGPPRRLTRPAVASLS 2792
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4359 EPLFPQLSTFEPKRQPQFANSPMSTPPAVSMPSinyqanPTYTPPrsnqnsnsylgetnTSYVVTYPLDDSGDEPEPESM 4438
Cdd:PHA03247 2793 ESRESLPSPWDPADPPAAVLAPAAALPPAASPA------GPLPPP--------------TSAQPTAPPPPPGPPPPSLPL 2852
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4439 ATSVSQ----RLRRTSEhsnassslslgstswTANPVHNTVPSVPLDSAMGPPVDRSTKPQVSQPVGPKMPQHVAQKQIP 4514
Cdd:PHA03247 2853 GGSVAPggdvRRRPPSR---------------SPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPP 2917
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4515 QQLPNQLPQQIPQQLPKQLPQQIPQQLPQQLPQQLPKQLPQQIPPQLPKQLPQQIPQP--ELPQQLPnnlPRHAPKLSSR 4592
Cdd:PHA03247 2918 QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPrfRVPQPAP---SREAPASSTP 2994

                  ....*....
gi 440216479 4593 SHTIQGDSG 4601
Cdd:PHA03247 2995 PLTGHSLSR 3003
 
Name Accession Description Interval E-value
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
5020-5125 1.05e-67

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: 1.05e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 5099
Cdd:cd21200     1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
                          90       100
                  ....*....|....*....|....*..
gi 440216479 5100 EDMVEMS-RPDWKCVFVYVQSIYRRFR 5125
Cdd:cd21200    81 EDMVRMGnRPDWKCVFTYVQSLYRHLR 107
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
5019-5125 9.01e-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: 9.01e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  5019 ATVKDQLLQWCKHKTQEY-ENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQT--RRHNFELAFSVADEKAGIAP 5095
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEfdKLENINLALDVAEKKLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 440216479  5096 -LLDVEDMVEmsrPDWKCVFVYVQSIYRRFR 5125
Cdd:pfam00307   81 vLIEPEDLVE---GDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
5023-5120 2.89e-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: 2.89e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479   5023 DQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQT----RRHNFELAFSVADEKAGIAPLLD 5098
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLsrfkKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 440216479   5099 VEDMVEMsRPDWKCVFVYVQSI 5120
Cdd:smart00033   81 PEDLVEG-PKLILGVIWTLISL 101
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
5020-5125 8.38e-20

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 97.70  E-value: 8.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYEN-VQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRH--NFELAFSVADEKAGIAPL 5096
Cdd:COG5069   125 TKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARL 204
                          90       100
                  ....*....|....*....|....*....
gi 440216479 5097 LDVEDMVEMSRPDWKCVFVYVQSIYRRFR 5125
Cdd:COG5069   205 IGVEDIVNVSIPDERSIMTYVSWYIIRFG 233
Smoothelin pfam12510
Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is ...
3127-3176 1.79e-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: 76.20  E-value: 1.79e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 440216479  3127 SSSSAPVTRTTCDIEEIWDEQVLKQLLEQASTYEERRKIRARLRELMAER 3176
Cdd:pfam12510    1 EETSAASKLTAEELEAIEDEEVLDKLLETATDYEERRLIRAAIRELRKRK 50
Smoothelin pfam12510
Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is ...
2594-2636 1.78e-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: 70.42  E-value: 1.78e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 440216479  2594 SDLELEIEEIFDLQRLEKLLETVASYEMRRRIRAQMRLIRKNM 2636
Cdd:pfam12510    8 KLTAEELEAIEDEEVLDKLLETATDYEERRLIRAAIRELRKRK 50
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1394-1702 2.78e-11

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 70.49  E-value: 2.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1394 PKEEDSPKYPKGPETPKSPRNDQR--------IPSIPKKGQSPVQFKTEETPRYPQEQER--YPKEPETSQYPK--ESPR 1461
Cdd:PTZ00449  582 PKDPKHPKDPEEPKKPKRPRSAQRptrpkspkLPELLDIPKSPKRPESPKSPKRPPPPQRpsSPERPEGPKIIKspKPPK 661
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1462 NPK----------------------EDAETININEETTIVITKEGSKSPSPRWSPSPERRVPK-------SQQPPSPTAS 1512
Cdd:PTZ00449  662 SPKppfdpkfkekfyddyldaaaksKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKlprdeefPFEPIGDPDA 741
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1513 PSVSPVSGRKIPNEvESNFVTEKIIDCRGKTVVEKISQRP----RTPSPTTPKKNTK-PSQKIPERVPETESEPEKDSES 1587
Cdd:PTZ00449  742 EQPDDIEFFTPPEE-ERTFFHETPADTPLPDILAEEFKEEdihaETGEPDEAMKRPDsPSEHEDKPPGDHPSLPKKRHRL 820
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1588 EtkkttSVSVTKTETERRNSRTTKTKQPLPLKEPQSKvpagksPRKDSLTGRKRDSLVEETRittTTTTTRQGRKPSDTN 1667
Cdd:PTZ00449  821 D-----GLALSTTDLESDAGRIAKDASGKIVKLKRSK------SFDDLTTVEEAEEMGAEAR---KIVVDDDGTEADDED 886
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 440216479 1668 GSPSiKDRLRSSPRKQKTSPQQTRTPTPAQTRNPE 1702
Cdd:PTZ00449  887 THPP-EEKHKSEVRRRRPPKKPSKPKKPSKPKKPK 920
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3810-3916 8.45e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 8.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 3810 QREQSQRDQNQRELSKREQFQREQLQREQLQREQLQREKLQREQLQREQLQREQLQREQLQREQLQREQLQREQLQRDQL 3889
Cdd:COG1196   671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
                          90       100
                  ....*....|....*....|....*..
gi 440216479 3890 QLQQQQQAAAAVQIERQRRQELERQLR 3916
Cdd:COG1196   751 EALEELPEPPDLEELERELERLEREIE 777
PHA03247 PHA03247
large tegument protein UL36; Provisional
566-1191 2.03e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 2.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  566 YQEP--QRSPQKLREAPTPSWEQPATRRQPveedfsthgfPSVRTTTTSTRPDQPDGEVLHtsktvSRNQSANRktNTER 643
Cdd:PHA03247 2480 YRRPaeARFPFAAGAAPDPGGGGPPDPDAP----------PAPSRLAPAILPDEPVGEPVH-----PRMLTWIR--GLEE 2542
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  644 IIETQVEHPNAPSHSTPRSGSPRRSQPRDDYASSPRGPAGKPSQSRPSNTGGSTTTKTTTTSEPLTRRQLQKerevdaah 723
Cdd:PHA03247 2543 LASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPP-------- 2614
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  724 rafaaslrSSSPADSTTsvgshhqtPRSSVSSNRTFRREMREGSHDSQAPSESSRissttvtRHTTGGNVTSNTIKTKTT 803
Cdd:PHA03247 2615 --------SPLPPDTHA--------PDPPPPSPSPAANEPDPHPPPTVPPPERPR-------DDPAPGRVSRPRRARRLG 2671
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  804 KPVKTASEPRSPTPKAGGSvttttttittksspspapaspttaapptsapassappdnklsqytytTTKPGDIFSLPPTT 883
Cdd:PHA03247 2672 RAAQASSPPQRPRRRAARP-----------------------------------------------TVGSLTSLADPPPP 2704
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  884 PPTINNEPTLTTTRNTTTTTTTTTTATSDNLQNHPKKSAIEPATDTDSQPIRKVKLSANEAKVVEEAPCVRRQyyqlgne 963
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA------- 2777
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  964 GENPETPESSGTPANKKPHQMRRPHDEPEPQLRRSSKSPSVEPRQVQRETtfegrrvsqdreisideliLIEETSGAPGS 1043
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP-------------------LPPPTSAQPTA 2838
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1044 PKIPSPRAQS---------PGKPATRSQSPEKPQPR-ATPRQSPEKE--QPAFKQTHEVYtpSQPEKQFPRARSPE-KTP 1110
Cdd:PHA03247 2839 PPPPPGPPPPslplggsvaPGGDVRRRPPSRSPAAKpAAPARPPVRRlaRPAVSRSTESF--ALPPDQPERPPQPQaPPP 2916
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1111 GWTQPQVSPRQSPEKQLPRAQSPEKvPAVRQPSVSPRQSPEKQIPDPKTRDQGPGLPRISPRQSPEKQLPKDVPQKSRQS 1190
Cdd:PHA03247 2917 PQPQPQPPPPPQPQPPPPPPPRPQP-PLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPP 2995

                  .
gi 440216479 1191 P 1191
Cdd:PHA03247 2996 L 2996
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1035-1421 1.51e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 55.08  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1035 EETSGAPGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFKQTHEVYTPSQPEKQfpraRSPEKTPGWTQ 1114
Cdd:PTZ00449  502 EDSDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKE----HKPSKIPTLSK 577
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1115 PQVSPRQSPEKQLPRAQSPEKVPAVRQPSVSPRqSPEK----QIPDPKTRDQGPGLPR--------ISPRQSPEKQLPKD 1182
Cdd:PTZ00449  578 KPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPK-SPKLpellDIPKSPKRPESPKSPKrppppqrpSSPERPEGPKIIKS 656
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1183 VPQKSRQSPEKDLTNQQRREEEIFRSTITTTQKRTTNNLNEEFITNERDNQNQ----PISEKKPQIPANAEPNTKPSETI 1258
Cdd:PTZ00449  657 PKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPEtpgtPFTTPRPLPPKLPRDEEFPFEPI 736
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1259 ESPDGGFPSK----TTEVEAQPEVKESPTYRK-KGLTRRETFEDRCRQILGMEEDG----DTQGTYTERPNNEQEDVNVS 1329
Cdd:PTZ00449  737 GDPDAEQPDDieffTPPEEERTFFHETPADTPlPDILAEEFKEEDIHAETGEPDEAmkrpDSPSEHEDKPPGDHPSLPKK 816
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1330 HTTIETIQVKIEDCPND------DEDDKP------RRVTETYVVRTQPKIKVEEELFV---DVTEAEDVEilVNPSK--- 1391
Cdd:PTZ00449  817 RHRLDGLALSTTDLESDagriakDASGKIvklkrsKSFDDLTTVEEAEEMGAEARKIVvddDGTEADDED--THPPEekh 894
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 440216479 1392 -------KSPKEEDSPKYPKGPETPKSPrNDQRIPSI 1421
Cdd:PTZ00449  895 ksevrrrRPPKKPSKPKKPSKPKKPKKP-DSAFIPSI 930
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
3810-3882 1.52e-06

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 55.13  E-value: 1.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 440216479 3810 QREQSQRDQNQRELSKREQFQR-EQLQREQLQREQLQRekLQREQLQREQLQREQLQREQLQREQLQReqLQRE 3882
Cdd:PTZ00266  441 EKENAHRKALEMKILEKKRIERlEREERERLERERMER--IERERLERERLERERLERDRLERDRLDR--LERE 510
PTZ00121 PTZ00121
MAEBL; Provisional
2080-2248 2.09e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 2080 RQSEPERELDEESEPELDRDTDVEDDDQTSQLETEEEITQTVTKKETLKEFKQQTKETRETRRDSKAEPEKLQKKSPQTK 2159
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 2160 VKEES----ARVPKYQAKVSQKVSQWEPKKQPQREPKVTQKETPLEPKKQPLSKVKdEPEKVNKREPKVPQKESQTKLKE 2235
Cdd:PTZ00121 1661 IKAAEeakkAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK-KAEELKKAEEENKIKAEEAKKEA 1739
                         170
                  ....*....|...
gi 440216479 2236 EPERVTKKTPQKE 2248
Cdd:PTZ00121 1740 EEDKKKAEEAKKD 1752
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
926-1184 4.37e-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: 47.07  E-value: 4.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479   926 ATDTDSQPIRKVKLSANEAKVVEEAPC----VRRQYYQLGNEGENPETPESSGTpankKPHQMRRPHDEPEpqlrrsSKS 1001
Cdd:pfam03154   49 AASTSSNDSKAESMKKSSKKIKEEAPSplksAKRQREKGASDTEEPERATAKKS----KTQEISRPNSPSE------GEG 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  1002 PSVEPRQVQRETTFEGRRVSQDREISidelilieetsgapgSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQ 1081
Cdd:pfam03154  119 ESSDGRSVNDEGSSDPKDIDQDNRST---------------SPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASP 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  1082 PAFKQTHEVYTPSQPEKQFPRARSPEKTPGWTQPQVSP----------RQSPEKQLPRAQSPEKVPAVRQPSVSPRQSPE 1151
Cdd:pfam03154  184 PSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTqstaaphtliQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSP 263
                          250       260       270
                   ....*....|....*....|....*....|...
gi 440216479  1152 KQIPDPKTRDQGPGLPRisPRQSPEKQLPKDVP 1184
Cdd:pfam03154  264 QPLPQPSLHGQMPPMPH--SLQTGPSHMQHPVP 294
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
3815-3913 7.82e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 45.41  E-value: 7.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  3815 QRDQNQRELSKREQFQREQLQR-EQLQREQLQREKLQREQLQREQLQREQLQReqlqREQLQREQLQREQLQRDQLQLQQ 3893
Cdd:pfam15558   18 KEEQRMRELQQQAALAWEELRRrDQKRQETLERERRLLLQQSQEQWQAEKEQR----KARLGREERRRADRREKQVIEKE 93
                           90       100
                   ....*....|....*....|
gi 440216479  3894 QQQAAAAVQIERQRRQELER 3913
Cdd:pfam15558   94 SRWREQAEDQENQRQEKLER 113
PHA03247 PHA03247
large tegument protein UL36; Provisional
4126-4601 1.08e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4126 KRPSLPNAMDPGTAAPPrqvyqaPPPPTNIS-------FTYADFPPVRRPQGASAHNYRSQPCLTSAVDQVEALTNPLGA 4198
Cdd:PHA03247 2609 RGPAPPSPLPPDTHAPD------PPPPSPSPaanepdpHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQR 2682
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4199 PlvltssNPTYLPPPgsrrfdyiSSPVDVDADSPPNSPTSfmtMPNPTLMTDNTDDDLDLDSDNNMLEYRAETKVMRKPR 4278
Cdd:PHA03247 2683 P------RRRAARPT--------VGSLTSLADPPPPPPTP---EPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVP 2745
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4279 SQTAVRVADRRNAhmsddevygknSRAAKSllytmkqlggGPGNAsvgnsgqrrqplTAPSSPKSGCLSPDGRPYQAPLV 4358
Cdd:PHA03247 2746 AGPATPGGPARPA-----------RPPTTA----------GPPAP------------APPAAPAAGPPRRLTRPAVASLS 2792
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4359 EPLFPQLSTFEPKRQPQFANSPMSTPPAVSMPSinyqanPTYTPPrsnqnsnsylgetnTSYVVTYPLDDSGDEPEPESM 4438
Cdd:PHA03247 2793 ESRESLPSPWDPADPPAAVLAPAAALPPAASPA------GPLPPP--------------TSAQPTAPPPPPGPPPPSLPL 2852
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4439 ATSVSQ----RLRRTSEhsnassslslgstswTANPVHNTVPSVPLDSAMGPPVDRSTKPQVSQPVGPKMPQHVAQKQIP 4514
Cdd:PHA03247 2853 GGSVAPggdvRRRPPSR---------------SPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPP 2917
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4515 QQLPNQLPQQIPQQLPKQLPQQIPQQLPQQLPQQLPKQLPQQIPPQLPKQLPQQIPQP--ELPQQLPnnlPRHAPKLSSR 4592
Cdd:PHA03247 2918 QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPrfRVPQPAP---SREAPASSTP 2994

                  ....*....
gi 440216479 4593 SHTIQGDSG 4601
Cdd:PHA03247 2995 PLTGHSLSR 3003
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1008-1255 1.25e-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: 45.14  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1008 QVQRETTFEGRRVSQDREISIDELILIEETSGAPGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFKQT 1087
Cdd:NF033839  254 KVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVK 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1088 HEVYTP-----SQPEKQFPRAR-SPEKTPGWTQPQVSPRQSPEKQLPRAQSPEKVPAVRQPSVSPRQSPEKQIPDPKTRD 1161
Cdd:NF033839  334 PQPEKPkpevkPQLETPKPEVKpQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQP 413
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1162 QGPGlPRISPrqSPEKQLPKDVPQKSRQSPEKDLTNQQRREE-----EIFRSTITTTQKRTTNNLNEEFITNERDNQNQP 1236
Cdd:NF033839  414 EKPK-PEVKP--QPEKPKPEVKPQPEKPKPEVKPQPEKPKPEvkpqpETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQ 490
                         250
                  ....*....|....*....
gi 440216479 1237 ISEKKPQIPANAEPNTKPS 1255
Cdd:NF033839  491 ADDKKPSTPNNLSKDKQPS 509
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
969-1192 1.80e-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: 44.76  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  969 TPESSGTPANKKPhQMRRPHDEPEPQLRRSSKSPSVEPRQVQRETTFEGRRVsqdreisidelilieETSGAPGSPKIPS 1048
Cdd:NF033839  280 TQDTPKEPGNKKP-SAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKP---------------EVKPQPEKPKPEV 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1049 PRAQSPGKPATRSQsPEKPQPRAtprqSPEKEQPAFKQTHEVYTPSQPEKQFPRARSPEKTPGWTQPQVSPRQSPEKqlp 1128
Cdd:NF033839  344 KPQLETPKPEVKPQ-PEKPKPEV----KPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEK--- 415
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 440216479 1129 raQSPEKVPAVRQPSVSPRQSPEKQIPDPKTRDQGPGlPRISPRqsPEKQLPKDVPQKSRQSPE 1192
Cdd:NF033839  416 --PKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPK-PEVKPQ--PETPKPEVKPQPEKPKPE 474
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
3810-3882 4.41e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.56  E-value: 4.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 440216479 3810 QREQSQRDQNQRELSKREQFQREQLQREQLQREQlQREKLQREQlQREQLQREQLQREQLQRE-QLQREQLQRE 3882
Cdd:cd16269   215 KLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEE-ERENLLKEQ-ERALESKLKEQEALLEEGfKEQAELLQEE 286
 
Name Accession Description Interval E-value
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
5020-5125 1.05e-67

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: 1.05e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 5099
Cdd:cd21200     1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
                          90       100
                  ....*....|....*....|....*..
gi 440216479 5100 EDMVEMS-RPDWKCVFVYVQSIYRRFR 5125
Cdd:cd21200    81 EDMVRMGnRPDWKCVFTYVQSLYRHLR 107
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
5020-5122 1.14e-48

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: 1.14e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 5099
Cdd:cd21259     1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80
                          90       100
                  ....*....|....*....|...
gi 440216479 5100 EDMVEMSRPDWKCVFVYVQSIYR 5122
Cdd:cd21259    81 EDMVRMREPDWKCVYTYIQEFYR 103
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
5021-5122 2.21e-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: 2.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5021 VKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVE 5100
Cdd:cd21260     2 VKNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVE 81
                          90       100
                  ....*....|....*....|..
gi 440216479 5101 DMVEMSRPDWKCVFVYVQSIYR 5122
Cdd:cd21260    82 DMVRMSVPDSKCVYTYIQELYR 103
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
5020-5125 1.21e-45

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: 1.21e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 5099
Cdd:cd21258     1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEV 80
                          90       100
                  ....*....|....*....|....*..
gi 440216479 5100 EDMVEM-SRPDWKCVFVYVQSIYRRFR 5125
Cdd:cd21258    81 EDMMIMgKKPDSKCVFTYVQSLYNHLR 107
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
5025-5124 5.12e-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: 5.12e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5025 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVAdEKAGIAPLLDVEDMVE 5104
Cdd:cd21199    13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAA-ESVGIPTTLTIDEMVS 91
                          90       100
                  ....*....|....*....|
gi 440216479 5105 MSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21199    92 MERPDWQSVMSYVTAIYKHF 111
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
5020-5125 1.35e-41

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: 1.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 5099
Cdd:cd21261     1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEV 80
                          90       100
                  ....*....|....*....|....*..
gi 440216479 5100 EDMVEMSR-PDWKCVFVYVQSIYRRFR 5125
Cdd:cd21261    81 EDMMVMGRkPDPMCVFTYVQSLYNHLR 107
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
5020-5124 8.59e-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: 8.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 5099
Cdd:cd21216    10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKMLDA 89
                          90       100
                  ....*....|....*....|....*
gi 440216479 5100 EDMVEMSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21216    90 EDIVNTPRPDERSVMTYVSCYYHAF 114
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
5025-5125 2.03e-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: 2.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5025 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDMVE 5104
Cdd:cd21253     6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDMVA 85
                          90       100
                  ....*....|....*....|.
gi 440216479 5105 MSRPDWKCVFVYVQSIYRRFR 5125
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 ...
5022-5124 2.35e-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: 2.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5022 KDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVED 5101
Cdd:cd21248     4 KDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDPED 83
                          90       100
                  ....*....|....*....|...
gi 440216479 5102 mVEMSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21248    84 -VNVEQPDEKSIITYVVTYYHYF 105
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
5022-5124 4.57e-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: 128.61  E-value: 4.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5022 KDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVAdEKAGIAPLLDVED 5101
Cdd:cd21257    10 RNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAA-ESVGIKPSLELSE 88
                          90       100
                  ....*....|....*....|...
gi 440216479 5102 MVEMSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21257    89 MMYTDRPDWQSVMQYVAQIYKYF 111
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
5022-5124 1.27e-33

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: 1.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5022 KDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVED 5101
Cdd:cd21194     4 KDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDAED 83
                          90       100
                  ....*....|....*....|...
gi 440216479 5102 mVEMSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21194    84 -VDVARPDEKSIMTYVASYYHYF 105
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
5022-5124 3.85e-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: 126.34  E-value: 3.85e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5022 KDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVAdEKAGIAPLLDVED 5101
Cdd:cd21256    16 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAA-ESVGIKSTLDINE 94
                          90       100
                  ....*....|....*....|...
gi 440216479 5102 MVEMSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21256    95 MVRTERPDWQSVMTYVTAIYKYF 117
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
5020-5124 8.07e-32

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: 121.73  E-value: 8.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 5099
Cdd:cd21189     1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                          90       100
                  ....*....|....*....|....*
gi 440216479 5100 EDmVEMSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21189    81 ED-VDVPEPDEKSIITYVSSLYDVF 104
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
5014-5124 8.59e-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: 8.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5014 LNARAATVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGI 5093
Cdd:cd21291     4 INEEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGI 83
                          90       100       110
                  ....*....|....*....|....*....|.
gi 440216479 5094 APLLDVEDMVEMSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21291    84 PQLLDVEDVCDVAKPDERSIMTYVAYYFHAF 114
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
5020-5124 1.60e-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: 1.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 5099
Cdd:cd21319     5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
                          90       100
                  ....*....|....*....|....*
gi 440216479 5100 EDmVEMSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21319    85 ED-VFTENPDEKSIITYVVAFYHYF 108
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
5023-5125 5.82e-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: 5.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5023 DQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDM 5102
Cdd:cd22198     3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEM 82
                          90       100
                  ....*....|....*....|...
gi 440216479 5103 VEMSRPDWKCVFVYVQSIYRRFR 5125
Cdd:cd22198    83 ASLAVPDKLSMVSYLSQFYEAFK 105
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
5025-5125 8.82e-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: 8.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5025 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDMVE 5104
Cdd:cd21197     5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDMVT 84
                          90       100
                  ....*....|....*....|.
gi 440216479 5105 MSRPDWKCVFVYVQSIYRRFR 5125
Cdd:cd21197    85 MHVPDRLSIITYVSQYYNHFR 105
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
5025-5124 1.02e-28

calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409047  Cd Length: 105  Bit Score: 112.90  E-value: 1.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5025 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVAdEKAGIAPLLDVEDMVE 5104
Cdd:cd21198     6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAA-AKLGIPRLLDPADMVL 84
                          90       100
                  ....*....|....*....|
gi 440216479 5105 MSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21198    85 LSVPDKLSVMTYLHQIRAHF 104
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
5020-5124 2.08e-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: 2.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 5099
Cdd:cd21249     4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLDP 83
                          90       100
                  ....*....|....*....|....*
gi 440216479 5100 EDmVEMSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21249    84 ED-VAVPHPDERSIMTYVSLYYHYF 107
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
5025-5122 2.37e-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: 111.75  E-value: 2.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5025 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDmVE 5104
Cdd:cd21187     5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED-VN 83
                          90
                  ....*....|....*...
gi 440216479 5105 MSRPDWKCVFVYVQSIYR 5122
Cdd:cd21187    84 VEQPDKKSILMYVTSLFQ 101
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
5020-5124 2.91e-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: 106.68  E-value: 2.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 5099
Cdd:cd21321     5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTKLLDP 84
                          90       100
                  ....*....|....*....|....*
gi 440216479 5100 EDmVEMSRPDWKCVFVYVQSIYRRF 5124
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), ...
5025-5126 1.05e-25

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: 1.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5025 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDMVE 5104
Cdd:cd21252     5 LQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPEDMVS 84
                          90       100
                  ....*....|....*....|..
gi 440216479 5105 MSRPDWKCVFVYVQSIYRRFRN 5126
Cdd:cd21252    85 MKVPDCLSIMTYVSQYYNHFSN 106
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
5015-5124 1.40e-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: 105.14  E-value: 1.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5015 NARAATVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIA 5094
Cdd:cd21322    12 NRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHLGLT 91
                          90       100       110
                  ....*....|....*....|....*....|
gi 440216479 5095 PLLDVEDmVEMSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21322    92 KLLDPED-VNMEAPDEKSIITYVVSFYHYF 120
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
5014-5128 6.28e-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: 102.86  E-value: 6.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5014 LNARAATVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGI 5093
Cdd:cd21287     4 ISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDI 83
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 440216479 5094 APLLDVEDMVEMSRPDWKCVFVYVQSIYRRFRNCQ 5128
Cdd:cd21287    84 PKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQ 118
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
5019-5125 9.01e-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: 9.01e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  5019 ATVKDQLLQWCKHKTQEY-ENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQT--RRHNFELAFSVADEKAGIAP 5095
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEfdKLENINLALDVAEKKLGVPK 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 440216479  5096 -LLDVEDMVEmsrPDWKCVFVYVQSIYRRFR 5125
Cdd:pfam00307   81 vLIEPEDLVE---GDNKSVLTYLASLFRRFQ 108
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
5023-5124 6.95e-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: 6.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5023 DQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADeKAGIAPLLDVEDM 5102
Cdd:cd21254     4 QSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFA-SLGISRLLEPSDM 82
                          90       100
                  ....*....|....*....|..
gi 440216479 5103 VEMSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21254    83 VLLAVPDKLTVMTYLYQIRAHF 104
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
5025-5124 1.01e-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: 98.65  E-value: 1.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5025 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDMVe 5104
Cdd:cd21192     8 LLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLEVEDVL- 86
                          90       100
                  ....*....|....*....|
gi 440216479 5105 MSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21192    87 VDKPDERSIMTYVSQFLRMF 106
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
5020-5124 1.09e-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: 98.52  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVAdEKAGIAPLLDV 5099
Cdd:cd21239     1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVA-EKLGVTRLLDP 79
                          90       100
                  ....*....|....*....|....*
gi 440216479 5100 EDmVEMSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21239    80 ED-VDVSSPDEKSVITYVSSLYDVF 103
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
5020-5124 2.28e-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: 97.77  E-value: 2.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 5099
Cdd:cd21243     5 GAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLDP 84
                          90       100
                  ....*....|....*....|....*
gi 440216479 5100 EDmVEMSRPDWKCVFVYVQSIYRRF 5124
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 ...
5023-5125 3.46e-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: 97.26  E-value: 3.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5023 DQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDM 5102
Cdd:cd21250     7 NKLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEM 86
                          90       100
                  ....*....|....*....|...
gi 440216479 5103 VEMSRPDWKCVFVYVQSIYRRFR 5125
Cdd:cd21250    87 ASAEEPDKLSMVMYLSKFYELFR 109
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
5014-5124 5.79e-23

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


Pssm-ID: 409138  Cd Length: 124  Bit Score: 97.10  E-value: 5.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5014 LNARAATVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGI 5093
Cdd:cd21289     4 ISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDI 83
                          90       100       110
                  ....*....|....*....|....*....|.
gi 440216479 5094 APLLDVEDMVEMSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21289    84 PKMLDAEDIVNTPKPDEKAIMTYVSCFYHAF 114
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
5020-5124 7.92e-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: 7.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 5099
Cdd:cd21320     2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
                          90       100
                  ....*....|....*....|....*
gi 440216479 5100 EDmVEMSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21320    82 ED-ISVDHPDEKSIITYVVTYYHYF 105
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
5014-5124 1.16e-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: 96.30  E-value: 1.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5014 LNARAATVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGI 5093
Cdd:cd21288     4 ISVEETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDI 83
                          90       100       110
                  ....*....|....*....|....*....|.
gi 440216479 5094 APLLDVEDMVEMSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21288    84 PKMLDAEDIVNTPKPDERAIMTYVSCFYHAF 114
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
5008-5128 1.75e-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: 95.92  E-value: 1.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5008 KFTDPALNARAATVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVA 5087
Cdd:cd21290     1 RFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 440216479 5088 DEKAGIAPLLDVEDMVEMSRPDWKCVFVYVQSIYRRFRNCQ 5128
Cdd:cd21290    81 EKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQ 121
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
5023-5120 2.89e-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: 2.89e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479   5023 DQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQT----RRHNFELAFSVADEKAGIAPLLD 5098
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLsrfkKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|..
gi 440216479   5099 VEDMVEMsRPDWKCVFVYVQSI 5120
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 ...
5024-5126 3.03e-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: 94.63  E-value: 3.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5024 QLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDMV 5103
Cdd:cd21251     9 KLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPIMTGKEMA 88
                          90       100
                  ....*....|....*....|...
gi 440216479 5104 EMSRPDWKCVFVYVQSIYRRFRN 5126
Cdd:cd21251    89 SVGEPDKLSMVMYLTQFYEMFKD 111
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
5024-5126 4.23e-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: 94.34  E-value: 4.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5024 QLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDMV 5103
Cdd:cd21195     8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEMA 87
                          90       100
                  ....*....|....*....|...
gi 440216479 5104 EMSRPDWKCVFVYVQSIYRRFRN 5126
Cdd:cd21195    88 SAQEPDKLSMVMYLSKFYELFRG 110
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
5020-5124 8.08e-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: 93.18  E-value: 8.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVAdEKAGIAPLLDV 5099
Cdd:cd21240     4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVA-ERLGVTRLLDA 82
                          90       100
                  ....*....|....*....|....*
gi 440216479 5100 EDmVEMSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21240    83 ED-VDVPSPDEKSVITYVSSIYDAF 106
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
5021-5124 8.64e-22

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


Pssm-ID: 409075  Cd Length: 103  Bit Score: 92.91  E-value: 8.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5021 VKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVE 5100
Cdd:cd21226     1 SEDGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAE 80
                          90       100
                  ....*....|....*....|....
gi 440216479 5101 DMVEmSRPDWKCVFVYVQSIYRRF 5124
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 ...
5023-5124 9.34e-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: 9.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5023 DQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSvADEKAGIAPLLDVEDM 5102
Cdd:cd21255     4 QSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFE-AFASLGVPRLLEPADM 82
                          90       100
                  ....*....|....*....|..
gi 440216479 5103 VEMSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21255    83 VLLPIPDKLIVMTYLCQLRAHF 104
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
5025-5121 4.46e-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: 88.09  E-value: 4.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5025 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDmVE 5104
Cdd:cd21234     5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED-VA 83
                          90
                  ....*....|....*..
gi 440216479 5105 MSRPDWKCVFVYVQSIY 5121
Cdd:cd21234    84 VQLPDKKSIIMYLTSLF 100
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
5025-5122 5.39e-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: 5.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5025 LLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTT-LTKQTRRHNFELAFSVADEKAGIAPLLDVEDmV 5103
Cdd:cd21233     5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSvVSQQSATERLDHAFNIARQHLGIEKLLDPED-V 83
                          90
                  ....*....|....*....
gi 440216479 5104 EMSRPDWKCVFVYVQSIYR 5122
Cdd:cd21233    84 ATAHPDKKSILMYVTSLFQ 102
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
5020-5125 8.38e-20

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 97.70  E-value: 8.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYEN-VQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRH--NFELAFSVADEKAGIAPL 5096
Cdd:COG5069   125 TKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARL 204
                          90       100
                  ....*....|....*....|....*....
gi 440216479 5097 LDVEDMVEMSRPDWKCVFVYVQSIYRRFR 5125
Cdd:COG5069   205 IGVEDIVNVSIPDERSIMTYVSWYIIRFG 233
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
5020-5121 7.17e-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: 85.07  E-value: 7.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 5099
Cdd:cd21238     2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 81
                          90       100
                  ....*....|....*....|..
gi 440216479 5100 EDmVEMSRPDWKCVFVYVQSIY 5121
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 ...
5020-5117 6.86e-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: 79.49  E-value: 6.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDV 5099
Cdd:cd21244     5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLEP 84
                          90
                  ....*....|....*...
gi 440216479 5100 EDmVEMSRPDWKCVFVYV 5117
Cdd:cd21244    85 ED-VDVVNPDEKSIMTYV 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
5022-5122 1.08e-16

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


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 78.53  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5022 KDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDY---TTLTKQTRRHNFELAFSVA-DEKAGIAPLL 5097
Cdd:cd00014     1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKinkKPKSPFKKRENINLFLNACkKLGLPELDLF 80
                          90       100
                  ....*....|....*....|....*
gi 440216479 5098 DVEDMVEmsRPDWKCVFVYVQSIYR 5122
Cdd:cd00014    81 EPEDLYE--KGNLKKVLGTLWALAL 103
Smoothelin pfam12510
Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is ...
3127-3176 1.79e-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: 76.20  E-value: 1.79e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 440216479  3127 SSSSAPVTRTTCDIEEIWDEQVLKQLLEQASTYEERRKIRARLRELMAER 3176
Cdd:pfam12510    1 EETSAASKLTAEELEAIEDEEVLDKLLETATDYEERRLIRAAIRELRKRK 50
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
5022-5128 1.06e-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: 75.74  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5022 KDQLLQWCKHKTQEYenvQINNFSSSWSDGLAFCALIHHFLPDAF-DYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVE 5100
Cdd:cd21184     3 KSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLENATKAMDIAEEELGIPKIITPE 79
                          90       100
                  ....*....|....*....|....*...
gi 440216479 5101 DMVEmSRPDWKCVFVYVQSiyrrFRNCQ 5128
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 ...
5025-5124 2.87e-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: 2.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5025 LLQWCKHKTQEYeNVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVEDmVE 5104
Cdd:cd21245     8 LLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPED-VM 85
                          90       100
                  ....*....|....*....|
gi 440216479 5105 MSRPDWKCVFVYVQSIYRRF 5124
Cdd:cd21245    86 VDSPDEQSIMTYVAQFLEHF 105
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
5018-5108 3.88e-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: 3.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5018 AATVKDQLLQWCKHKTQEYENVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSVADEKAGIAPLL 5097
Cdd:cd21196     1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVV 80
                          90
                  ....*....|.
gi 440216479 5098 DVEDMVEMSRP 5108
Cdd:cd21196    81 SAQAVVAGSDP 91
Smoothelin pfam12510
Smoothelin cytoskeleton protein; This domain family is found in eukaryotes, and is ...
2594-2636 1.78e-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: 70.42  E-value: 1.78e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 440216479  2594 SDLELEIEEIFDLQRLEKLLETVASYEMRRRIRAQMRLIRKNM 2636
Cdd:pfam12510    8 KLTAEELEAIEDEEVLDKLLETATDYEERRLIRAAIRELRKRK 50
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1394-1702 2.78e-11

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 70.49  E-value: 2.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1394 PKEEDSPKYPKGPETPKSPRNDQR--------IPSIPKKGQSPVQFKTEETPRYPQEQER--YPKEPETSQYPK--ESPR 1461
Cdd:PTZ00449  582 PKDPKHPKDPEEPKKPKRPRSAQRptrpkspkLPELLDIPKSPKRPESPKSPKRPPPPQRpsSPERPEGPKIIKspKPPK 661
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1462 NPK----------------------EDAETININEETTIVITKEGSKSPSPRWSPSPERRVPK-------SQQPPSPTAS 1512
Cdd:PTZ00449  662 SPKppfdpkfkekfyddyldaaaksKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKlprdeefPFEPIGDPDA 741
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1513 PSVSPVSGRKIPNEvESNFVTEKIIDCRGKTVVEKISQRP----RTPSPTTPKKNTK-PSQKIPERVPETESEPEKDSES 1587
Cdd:PTZ00449  742 EQPDDIEFFTPPEE-ERTFFHETPADTPLPDILAEEFKEEdihaETGEPDEAMKRPDsPSEHEDKPPGDHPSLPKKRHRL 820
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1588 EtkkttSVSVTKTETERRNSRTTKTKQPLPLKEPQSKvpagksPRKDSLTGRKRDSLVEETRittTTTTTRQGRKPSDTN 1667
Cdd:PTZ00449  821 D-----GLALSTTDLESDAGRIAKDASGKIVKLKRSK------SFDDLTTVEEAEEMGAEAR---KIVVDDDGTEADDED 886
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 440216479 1668 GSPSiKDRLRSSPRKQKTSPQQTRTPTPAQTRNPE 1702
Cdd:PTZ00449  887 THPP-EEKHKSEVRRRRPPKKPSKPKKPSKPKKPK 920
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
5021-5117 9.63e-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: 9.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5021 VKDQLLQWCKHKTQEYeNVQINNFSSSWSDGLAFCALIHHFLPD----------------------------AFDYTTLT 5072
Cdd:cd21224     1 VLSLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSllpldairqpttqtvdraqdeaedfwvaEFSPSTGD 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 440216479 5073 KQTR-------RHNFELAFSVADEKAGIAPLLDVEDMVEmSRPDWKCVFVYV 5117
Cdd:cd21224    80 SGLSsellaneKRNFKLVQQAVAELGGVPALLRASDMSN-TIPDEKVVILFL 130
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3810-3916 8.45e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 8.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 3810 QREQSQRDQNQRELSKREQFQREQLQREQLQREQLQREKLQREQLQREQLQREQLQREQLQREQLQREQLQREQLQRDQL 3889
Cdd:COG1196   671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
                          90       100
                  ....*....|....*....|....*..
gi 440216479 3890 QLQQQQQAAAAVQIERQRRQELERQLR 3916
Cdd:COG1196   751 EALEELPEPPDLEELERELERLEREIE 777
PHA03247 PHA03247
large tegument protein UL36; Provisional
566-1191 2.03e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 2.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  566 YQEP--QRSPQKLREAPTPSWEQPATRRQPveedfsthgfPSVRTTTTSTRPDQPDGEVLHtsktvSRNQSANRktNTER 643
Cdd:PHA03247 2480 YRRPaeARFPFAAGAAPDPGGGGPPDPDAP----------PAPSRLAPAILPDEPVGEPVH-----PRMLTWIR--GLEE 2542
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  644 IIETQVEHPNAPSHSTPRSGSPRRSQPRDDYASSPRGPAGKPSQSRPSNTGGSTTTKTTTTSEPLTRRQLQKerevdaah 723
Cdd:PHA03247 2543 LASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPP-------- 2614
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  724 rafaaslrSSSPADSTTsvgshhqtPRSSVSSNRTFRREMREGSHDSQAPSESSRissttvtRHTTGGNVTSNTIKTKTT 803
Cdd:PHA03247 2615 --------SPLPPDTHA--------PDPPPPSPSPAANEPDPHPPPTVPPPERPR-------DDPAPGRVSRPRRARRLG 2671
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  804 KPVKTASEPRSPTPKAGGSvttttttittksspspapaspttaapptsapassappdnklsqytytTTKPGDIFSLPPTT 883
Cdd:PHA03247 2672 RAAQASSPPQRPRRRAARP-----------------------------------------------TVGSLTSLADPPPP 2704
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  884 PPTINNEPTLTTTRNTTTTTTTTTTATSDNLQNHPKKSAIEPATDTDSQPIRKVKLSANEAKVVEEAPCVRRQyyqlgne 963
Cdd:PHA03247 2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA------- 2777
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  964 GENPETPESSGTPANKKPHQMRRPHDEPEPQLRRSSKSPSVEPRQVQRETtfegrrvsqdreisideliLIEETSGAPGS 1043
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP-------------------LPPPTSAQPTA 2838
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1044 PKIPSPRAQS---------PGKPATRSQSPEKPQPR-ATPRQSPEKE--QPAFKQTHEVYtpSQPEKQFPRARSPE-KTP 1110
Cdd:PHA03247 2839 PPPPPGPPPPslplggsvaPGGDVRRRPPSRSPAAKpAAPARPPVRRlaRPAVSRSTESF--ALPPDQPERPPQPQaPPP 2916
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1111 GWTQPQVSPRQSPEKQLPRAQSPEKvPAVRQPSVSPRQSPEKQIPDPKTRDQGPGLPRISPRQSPEKQLPKDVPQKSRQS 1190
Cdd:PHA03247 2917 PQPQPQPPPPPQPQPPPPPPPRPQP-PLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPP 2995

                  .
gi 440216479 1191 P 1191
Cdd:PHA03247 2996 L 2996
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1381-1768 5.29e-07

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 56.62  E-value: 5.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1381 EDVEILVNPSKK---SPKEEDSPKY---PKGPET----PKSP---------RNDQRIPSIPKKGQSPVQFKTEETPRYP- 1440
Cdd:PTZ00449  483 QEIKKLIKKSKKklaPIEEEDSDKHdepPEGPEAsglpPKAPgdkegeegeHEDSKESDEPKEGGKPGETKEGEVGKKPg 562
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1441 -------------QEQERYPKEPETSQYPKE-----SPRNPKEDAETININEETTIVITKegskSPSPRWSPSPERRVPK 1502
Cdd:PTZ00449  563 pakehkpskiptlSKKPEFPKDPKHPKDPEEpkkpkRPRSAQRPTRPKSPKLPELLDIPK----SPKRPESPKSPKRPPP 638
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1503 SQQPPSPTASPSVSPVSGRKIPNEVESNF---VTEKIID------CRGKTVV------EKISQRPRTPSPTTPKKNTKPS 1567
Cdd:PTZ00449  639 PQRPSSPERPEGPKIIKSPKPPKSPKPPFdpkFKEKFYDdyldaaAKSKETKttvvldESFESILKETLPETPGTPFTTP 718
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1568 QKIPERVPETESEP-----EKDSES------------------ETKKTTSVSVTKTETERRNSRTTKTKQP-LPLKEPQS 1623
Cdd:PTZ00449  719 RPLPPKLPRDEEFPfepigDPDAEQpddiefftppeeertffhETPADTPLPDILAEEFKEEDIHAETGEPdEAMKRPDS 798
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1624 KVPAGKSPRKDSLTGRKRDSLVEETRITTTTTTTRQGRKPSDTNGSPSIKDRLRSSprKQKTSPQQTRTPTPAQTRNPED 1703
Cdd:PTZ00449  799 PSEHEDKPPGDHPSLPKKRHRLDGLALSTTDLESDAGRIAKDASGKIVKLKRSKSF--DDLTTVEEAEEMGAEARKIVVD 876
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 440216479 1704 DVDGDSSSPDASPTrvgnERRRSSNISVHTEIIIDHMAPKSPKTERRSQGGTGNVPSPIRKLPVT 1768
Cdd:PTZ00449  877 DDGTEADDEDTHPP----EEKHKSEVRRRRPPKKPSKPKKPSKPKKPKKPDSAFIPSIIAIFLVS 937
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
5020-5106 6.05e-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: 6.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5020 TVKDQLLQWCKHKTQEyenVQINNFSSSWSDGLAFCALIHHFLPDAF-DYTTLTKQTRRHNFELAFSVADEKAGIAPLLD 5098
Cdd:cd21230     1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
                          90
                  ....*....|...
gi 440216479 5099 VEDMV-----EMS 5106
Cdd:cd21230    78 PEEIInpnvdEMS 90
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1035-1421 1.51e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 55.08  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1035 EETSGAPGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFKQTHEVYTPSQPEKQfpraRSPEKTPGWTQ 1114
Cdd:PTZ00449  502 EDSDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKE----HKPSKIPTLSK 577
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1115 PQVSPRQSPEKQLPRAQSPEKVPAVRQPSVSPRqSPEK----QIPDPKTRDQGPGLPR--------ISPRQSPEKQLPKD 1182
Cdd:PTZ00449  578 KPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPK-SPKLpellDIPKSPKRPESPKSPKrppppqrpSSPERPEGPKIIKS 656
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1183 VPQKSRQSPEKDLTNQQRREEEIFRSTITTTQKRTTNNLNEEFITNERDNQNQ----PISEKKPQIPANAEPNTKPSETI 1258
Cdd:PTZ00449  657 PKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPEtpgtPFTTPRPLPPKLPRDEEFPFEPI 736
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1259 ESPDGGFPSK----TTEVEAQPEVKESPTYRK-KGLTRRETFEDRCRQILGMEEDG----DTQGTYTERPNNEQEDVNVS 1329
Cdd:PTZ00449  737 GDPDAEQPDDieffTPPEEERTFFHETPADTPlPDILAEEFKEEDIHAETGEPDEAmkrpDSPSEHEDKPPGDHPSLPKK 816
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1330 HTTIETIQVKIEDCPND------DEDDKP------RRVTETYVVRTQPKIKVEEELFV---DVTEAEDVEilVNPSK--- 1391
Cdd:PTZ00449  817 RHRLDGLALSTTDLESDagriakDASGKIvklkrsKSFDDLTTVEEAEEMGAEARKIVvddDGTEADDED--THPPEekh 894
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 440216479 1392 -------KSPKEEDSPKYPKGPETPKSPrNDQRIPSI 1421
Cdd:PTZ00449  895 ksevrrrRPPKKPSKPKKPSKPKKPKKP-DSAFIPSI 930
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
3810-3882 1.52e-06

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 55.13  E-value: 1.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 440216479 3810 QREQSQRDQNQRELSKREQFQR-EQLQREQLQREQLQRekLQREQLQREQLQREQLQREQLQREQLQReqLQRE 3882
Cdd:PTZ00266  441 EKENAHRKALEMKILEKKRIERlEREERERLERERMER--IERERLERERLERERLERDRLERDRLDR--LERE 510
PHA03378 PHA03378
EBNA-3B; Provisional
970-1207 1.55e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 55.07  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  970 PESSGTPaNKKPHqmrrPHDEPEPQLRRSSKSPSVEPRQVQRETTFEGRRVSQDREISIDELIL--------IEETSGAP 1041
Cdd:PHA03378  590 PSYAQTP-WPVPH----PSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFptphqppqVEITPYKP 664
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1042 GSPKIPSPRAQ-SPGKPAT---RSQSPE--KPQPRATPRQSPEKEQPAFKQthevytpsQPEKQFPRARSPEKTPGWTQP 1115
Cdd:PHA03378  665 TWTQIGHIPYQpSPTGANTmlpIQWAPGtmQPPPRAPTPMRPPAAPPGRAQ--------RPAAATGRARPPAAAPGRARP 736
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1116 qvsPRQSPEKQLPRAQSPekvPAVRQPSVSPRQSPEKQI----PDPKTRDQGPGLPRISPRQSPEKQLPKDVPQKSRQSP 1191
Cdd:PHA03378  737 ---PAAAPGRARPPAAAP---GRARPPAAAPGRARPPAAapgaPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQLM 810
                         250
                  ....*....|....*.
gi 440216479 1192 EKDLTNQQRREEEIFR 1207
Cdd:PHA03378  811 PRAAPGQQGPTKQILR 826
PHA03247 PHA03247
large tegument protein UL36; Provisional
967-1283 2.32e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  967 PETPESSGTPANKKPHQMRRPHDEPEPQLRRSSKSPSVEP--------RQVQRETTFEG--RRVSQDREISIDELilieE 1036
Cdd:PHA03247 2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRprrarrlgRAAQASSPPQRprRRAARPTVGSLTSL----A 2699
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1037 TSGAPGSPKIPSPRAQSPGKP---ATRSQSPEKPQPRATPRQSPEKEQPAFKQTHEVY----TPSQPEKQF-PRARSPEK 1108
Cdd:PHA03247 2700 DPPPPPPTPEPAPHALVSATPlppGPAAARQASPALPAAPAPPAVPAGPATPGGPARParppTTAGPPAPApPAAPAAGP 2779
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1109 TPGWTQPQVSPRQSPEKQLPRAQSPEKVPAV---RQPSVSPRQSPEKQIPDPKTRDQGPGLPRISPRQSPEKQLPKDVP- 1184
Cdd:PHA03247 2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAvlaPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPg 2859
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1185 ------QKSRQSPEKDLTNQQRREEEIFRSTITttqkrttnnlneefitneRDNQNQPISEKKPQIPANAEPNTKPSETI 1258
Cdd:PHA03247 2860 gdvrrrPPSRSPAAKPAAPARPPVRRLARPAVS------------------RSTESFALPPDQPERPPQPQAPPPPQPQP 2921
                         330       340
                  ....*....|....*....|....*
gi 440216479 1259 ESPDGGFPSKTTEVEAQPEVKESPT 1283
Cdd:PHA03247 2922 QPPPPPQPQPPPPPPPRPQPPLAPT 2946
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
5026-5103 6.18e-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: 6.18e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 440216479 5026 LQWCKHKTQEyenVQINNFSSSWSDGLAFCALIHHFLPDAFDYTTLTKQTRRHNFELAFSvADEKAGIAPLLDVEDMV 5103
Cdd:cd21185     7 LRWVRQLLPD---VDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMA 80
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
5022-5102 7.74e-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: 7.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5022 KDQLLQWCKHKTQEyenVQINNFSSSWSDGLAFCALIHHFLPDAF-DYTTLTKQTRRHNFELAFSVADEKAGIAPLLDVE 5100
Cdd:cd21229     5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81

                  ..
gi 440216479 5101 DM 5102
Cdd:cd21229    82 DL 83
PRK10263 PRK10263
DNA translocase FtsK; Provisional
921-1463 2.24e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 51.24  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  921 SAIEPATDTDSQPIRKVKLSAN--EAKVVEEAPCVRRQYYQLGNEGENPETPESSGTPANKKPHQMRRPHDE----PEPQ 994
Cdd:PRK10263  324 AAATTATQSWAAPVEPVTQTPPvaSVDVPPAQPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEplqqPVQP 403
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  995 LRRSSKSPSVEPRQVQRETTFEGRRVSQDREISIDELILIEETSGA--PGSPKIPSPRAQSPGK-PATRSQSPEKPQPRA 1071
Cdd:PRK10263  404 QQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAeeQQSTFAPQSTYQTEQTyQQPAAQEPLYQQPQP 483
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1072 TPRQSPEKEQPAFKQTHevytPSQP------EKQFPRARSPEKTPGWTQPQVSPRQSPEKQLP--RAQSPEKVPAVRQ-P 1142
Cdd:PRK10263  484 VEQQPVVEPEPVVEETK----PARPplyyfeEVEEKRAREREQLAAWYQPIPEPVKEPEPIKSslKAPSVAAVPPVEAaA 559
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1143 SVSPRQSPEKQ----------IPDPKTRDQGPGLPRISPRQSPEKQLPKdvPQKSRQSPEKDLTN------QQRREEEIF 1206
Cdd:PRK10263  560 AVSPLASGVKKatlatgaaatVAAPVFSLANSGGPRPQVKEGIGPQLPR--PKRIRVPTRRELASygiklpSQRAAEEKA 637
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1207 RSTITTTQKRTTNNLNEEFITNERDNQNQPISEKKPQIPANAEPNTKPSETIESPDGGfpskttEVEAQPEVKESPTYRK 1286
Cdd:PRK10263  638 REAQRNQYDSGDQYNDDEIDAMQQDELARQFAQTQQQRYGEQYQHDVPVNAEDADAAA------EAELARQFAQTQQQRY 711
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1287 KGltrretfedrcrqilgmeedgdtqgtytERPNNEQEdVNVSHTTIETIQVKIEDCPNddeddkprrvtetyvvrtqpk 1366
Cdd:PRK10263  712 SG----------------------------EQPAGANP-FSLDDFEFSPMKALLDDGPH--------------------- 741
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1367 ikveEELFVDVTEAEDVEILVNPSKKSPKEEDSPKYPKG----PETPKSPRNDQRIPSIPKKGQSpvQFKTEETPRYPQE 1442
Cdd:PRK10263  742 ----EPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPqyqqPQQPVAPQPQYQQPQQPVAPQP--QYQQPQQPVAPQP 815
                         570       580
                  ....*....|....*....|.
gi 440216479 1443 QERYPKEPETSQYPKESPRNP 1463
Cdd:PRK10263  816 QYQQPQQPVAPQPQYQQPQQP 836
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
3809-3882 3.21e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 49.80  E-value: 3.21e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 440216479 3809 YQREQSQRDQNQRElSKREQFQREQLQREQLQREQLQREKLQREQLQREQLQREQLQREQLQREQLQREQLQRE 3882
Cdd:PRK09510   64 YNRQQQQQKSAKRA-EEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEE 136
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
3812-3876 3.64e-05

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 50.51  E-value: 3.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 440216479 3812 EQSQRDQNQR-ELSKREQFQREQLQREQLQREQLQREKLQREQLQReqLQREQLQReqLQREQLQR 3876
Cdd:PTZ00266  461 ERLEREERERlERERMERIERERLERERLERERLERDRLERDRLDR--LERERVDR--LERDRLEK 522
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3810-3918 4.64e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 4.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 3810 QREQSQRDQNQRELSKREQFQREQLQREQLQREQLQREKLQREQLQRE----QLQREQLQREQLQREQLQREQLQREQLQ 3885
Cdd:COG1196   305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEleeaEAELAEAEEALLEAEAELAEAEEELEEL 384
                          90       100       110
                  ....*....|....*....|....*....|...
gi 440216479 3886 RDQLQLQQQQQAAAAVQIERQRRQELERQLRLE 3918
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEALLERLE 417
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3810-3917 7.26e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 7.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 3810 QREQSQRDQNQRELSKREQfQREQLQREQLQREQLQREKLQREQLQREQLQREQLQREQLQREQLQREQLQREQLQRDQL 3889
Cdd:COG1196   368 LEAEAELAEAEEELEELAE-ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
                          90       100
                  ....*....|....*....|....*...
gi 440216479 3890 QLQQQQQAAAAVQIERQRRQELERQLRL 3917
Cdd:COG1196   447 AAEEEAELEEEEEALLELLAELLEEAAL 474
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3810-3917 9.11e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 9.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 3810 QREQSQRDQNQRELSKREQFQREQLQREQLQREQLQREKLQ-REQLQREQLQREQLQREQLQREQLQREQLQREQLQRDQ 3888
Cdd:COG1196   322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEaEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
                          90       100
                  ....*....|....*....|....*....
gi 440216479 3889 LQLQQQQQAAAAVQIERQRRQELERQLRL 3917
Cdd:COG1196   402 LEELEEAEEALLERLERLEEELEELEEAL 430
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
5039-5102 1.18e-04

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: 1.18e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 440216479  5039 VQINNFSSSWSDGLAFCALIHHFLPDAFDYT------TLTKQTRRHNFELAFSVADEKAGIAPL-LDVEDM 5102
Cdd:pfam11971   11 PPVEDLLRDLSDGCALAALIHFYCPQLIDLEdiclkeSMSLADSLYNIQLLQEFCQRHLGNRCChLTLEDL 81
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
5025-5104 1.65e-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: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 5025 LLQWCKH--KTQEYENVQINNFSSSWSDGLAFCALIHHFLP----DAFDYTTLTKQTRRHNFELAFSVAdEKAGIAPLLD 5098
Cdd:cd21218    15 LLRWVNYhlKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPelcdKELVLEVLSEEDLEKRAEKVLQAA-EKLGCKYFLT 93

                  ....*.
gi 440216479 5099 VEDMVE 5104
Cdd:cd21218    94 PEDIVS 99
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3810-3917 1.93e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 3810 QREQSQRDQNQRELSKREQFQREQLQREQLQREQLQREKLQREQLQREQLQREQLQREQLQREQL--QREQLQREQLQRD 3887
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLeeELEELEEALAELE 434
                          90       100       110
                  ....*....|....*....|....*....|
gi 440216479 3888 QLQLQQQQQAAAAVQIERQRRQELERQLRL 3917
Cdd:COG1196   435 EEEEEEEEALEEAAEEEAELEEEEEALLEL 464
PTZ00121 PTZ00121
MAEBL; Provisional
2080-2248 2.09e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 2080 RQSEPERELDEESEPELDRDTDVEDDDQTSQLETEEEITQTVTKKETLKEFKQQTKETRETRRDSKAEPEKLQKKSPQTK 2159
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 2160 VKEES----ARVPKYQAKVSQKVSQWEPKKQPQREPKVTQKETPLEPKKQPLSKVKdEPEKVNKREPKVPQKESQTKLKE 2235
Cdd:PTZ00121 1661 IKAAEeakkAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK-KAEELKKAEEENKIKAEEAKKEA 1739
                         170
                  ....*....|...
gi 440216479 2236 EPERVTKKTPQKE 2248
Cdd:PTZ00121 1740 EEDKKKAEEAKKD 1752
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
926-1184 4.37e-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: 47.07  E-value: 4.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479   926 ATDTDSQPIRKVKLSANEAKVVEEAPC----VRRQYYQLGNEGENPETPESSGTpankKPHQMRRPHDEPEpqlrrsSKS 1001
Cdd:pfam03154   49 AASTSSNDSKAESMKKSSKKIKEEAPSplksAKRQREKGASDTEEPERATAKKS----KTQEISRPNSPSE------GEG 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  1002 PSVEPRQVQRETTFEGRRVSQDREISidelilieetsgapgSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQ 1081
Cdd:pfam03154  119 ESSDGRSVNDEGSSDPKDIDQDNRST---------------SPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASP 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  1082 PAFKQTHEVYTPSQPEKQFPRARSPEKTPGWTQPQVSP----------RQSPEKQLPRAQSPEKVPAVRQPSVSPRQSPE 1151
Cdd:pfam03154  184 PSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTqstaaphtliQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSP 263
                          250       260       270
                   ....*....|....*....|....*....|...
gi 440216479  1152 KQIPDPKTRDQGPGLPRisPRQSPEKQLPKDVP 1184
Cdd:pfam03154  264 QPLPQPSLHGQMPPMPH--SLQTGPSHMQHPVP 294
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3810-3917 5.13e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 5.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 3810 QREQSQRDQNQRELSKREQFQREQLQREQLQREQLQREKLQREQLQREQLQREQLQREQLQREQLQREQLQREQLQRDQL 3889
Cdd:COG1196   277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
                          90       100
                  ....*....|....*....|....*...
gi 440216479 3890 QLQQQQQAAAAVQIERQRRQELERQLRL 3917
Cdd:COG1196   357 EAELAEAEEALLEAEAELAEAEEELEEL 384
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
961-1157 6.38e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 6.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  961 GNEGENPETPESSGTPANKKPHQMRRPHDEPEPQLRRSSKSPSVEPRQVQRETTFEGRRVSQDREISIDELILIEETSGA 1040
Cdd:PHA03307  250 GPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSST 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1041 PGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFKQTHEVYTPSQPEKqfPRARSPEKTPGWTQ--PQVS 1118
Cdd:PHA03307  330 SSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTR--RRARAAVAGRARRRdaTGRF 407
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 440216479 1119 PRQSPEKQLPRAQSPEKVPAVRQPSVSPRQSPEKQIPDP 1157
Cdd:PHA03307  408 PAGRPRPSPLDAGAASGAFYARYPLLTPSGEPWPGSPPP 446
PTZ00121 PTZ00121
MAEBL; Provisional
2080-2254 6.66e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 6.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 2080 RQSEPERELDEESEPELDRDTDVEDDDQTSQLETEEEitQTVTKKETLKefKQQTKETRETRRDSKAEPEKLQKKSPQTK 2159
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIKAAEEA--KKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 2160 VKEESARVPKYQAKVSQKVSQWEP--KKQPQREPKVTQ-KETPLEPKKQPLSKVKDEPEKVNKREPKVPQKESQTKLKEE 2236
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEElkKAEEENKIKAEEaKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
                         170
                  ....*....|....*...
gi 440216479 2237 PERVTKKTPQKEPRKEPL 2254
Cdd:PTZ00121 1777 KEAVIEEELDEEDEKRRM 1794
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1041-1127 6.85e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 46.23  E-value: 6.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1041 PGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFKQTHEVYTPSQPEKQFPRARSPEKT----PGWTQPQ 1116
Cdd:PRK10263  755 PQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPvapqPQYQQPQ 834
                          90
                  ....*....|.
gi 440216479 1117 VSPRQSPEKQL 1127
Cdd:PRK10263  835 QPVAPQPQDTL 845
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
3815-3913 7.82e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 45.41  E-value: 7.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  3815 QRDQNQRELSKREQFQREQLQR-EQLQREQLQREKLQREQLQREQLQREQLQReqlqREQLQREQLQREQLQRDQLQLQQ 3893
Cdd:pfam15558   18 KEEQRMRELQQQAALAWEELRRrDQKRQETLERERRLLLQQSQEQWQAEKEQR----KARLGREERRRADRREKQVIEKE 93
                           90       100
                   ....*....|....*....|
gi 440216479  3894 QQQAAAAVQIERQRRQELER 3913
Cdd:pfam15558   94 SRWREQAEDQENQRQEKLER 113
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
3810-3916 7.90e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 7.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 3810 QREQSQRDQNQRELSKREQFQREQLQREQLqREQLQREKLQREQLQREQLQREQLQREQLQREQlQREQLQREQLQRDQL 3889
Cdd:COG4717   108 EAELEELREELEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEERLEELRELEEELEELEA-ELAELQEELEELLEQ 185
                          90       100       110
                  ....*....|....*....|....*....|.
gi 440216479 3890 QLQQQQQAAAAVQIE----RQRRQELERQLR 3916
Cdd:COG4717   186 LSLATEEELQDLAEEleelQQRLAELEEELE 216
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
3810-3910 8.91e-04

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 45.71  E-value: 8.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  3810 QREQSQRDQNQRELSKR-----EQFQREQLQREQLQREQLQREKLQREQLQREQ--------LQREQLQREQLQREQLQR 3876
Cdd:pfam15709  329 EQEKASRDRLRAERAEMrrlevERKRREQEEQRRLQQEQLERAEKMREELELEQqrrfeeirLRKQRLEEERQRQEEEER 408
                           90       100       110
                   ....*....|....*....|....*....|....
gi 440216479  3877 EQLQREQLQRDQLQLQQQQQAAAAVQIERQRRQE 3910
Cdd:pfam15709  409 KQRLQLQAAQERARQQQEEFRRKLQELQRKKQQE 442
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1034-1146 9.72e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 9.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1034 IEETSGAPGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAfkQTHEVYTPSQPEKQFPRARSPEKTPG-W 1112
Cdd:PRK07764  392 GAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAP--PSPAGNAPAGGAPSPPPAAAPSAQPApA 469
                          90       100       110
                  ....*....|....*....|....*....|....
gi 440216479 1113 TQPQVSPRQSPEKQLPRAQSPEKVPAVRQPSVSP 1146
Cdd:PRK07764  470 PAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAP 503
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
940-1190 1.00e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.64  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  940 SANEAKVVEEAPCVRRQYYQLGNEGENPETPESSGTPANKKPHQMRRPhdepepqlrrSSKSPSVEPRQVQRETTFEGRR 1019
Cdd:PRK12323  376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAP----------ARRSPAPEALAAARQASARGPG 445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1020 VSQdreisideliliEETSGAPGSP--KIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFKQTHEVYTPSqpe 1097
Cdd:PRK12323  446 GAP------------APAPAPAAAPaaAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPA--- 510
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1098 kqfPRARSPEKTPGWTQPQVSPRQSPEKQLPRAQSPEKVPAvrqPSVSPRQSPEKQIPDPKTRDQGPGLPRISPRQSPE- 1176
Cdd:PRK12323  511 ---PAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAA---PAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPAl 584
                         250
                  ....*....|....*..
gi 440216479 1177 -KQLP-KDVPQK-SRQS 1190
Cdd:PRK12323  585 aARLPvRGLAQQlARQS 601
PHA03247 PHA03247
large tegument protein UL36; Provisional
4126-4601 1.08e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4126 KRPSLPNAMDPGTAAPPrqvyqaPPPPTNIS-------FTYADFPPVRRPQGASAHNYRSQPCLTSAVDQVEALTNPLGA 4198
Cdd:PHA03247 2609 RGPAPPSPLPPDTHAPD------PPPPSPSPaanepdpHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQR 2682
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4199 PlvltssNPTYLPPPgsrrfdyiSSPVDVDADSPPNSPTSfmtMPNPTLMTDNTDDDLDLDSDNNMLEYRAETKVMRKPR 4278
Cdd:PHA03247 2683 P------RRRAARPT--------VGSLTSLADPPPPPPTP---EPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVP 2745
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4279 SQTAVRVADRRNAhmsddevygknSRAAKSllytmkqlggGPGNAsvgnsgqrrqplTAPSSPKSGCLSPDGRPYQAPLV 4358
Cdd:PHA03247 2746 AGPATPGGPARPA-----------RPPTTA----------GPPAP------------APPAAPAAGPPRRLTRPAVASLS 2792
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4359 EPLFPQLSTFEPKRQPQFANSPMSTPPAVSMPSinyqanPTYTPPrsnqnsnsylgetnTSYVVTYPLDDSGDEPEPESM 4438
Cdd:PHA03247 2793 ESRESLPSPWDPADPPAAVLAPAAALPPAASPA------GPLPPP--------------TSAQPTAPPPPPGPPPPSLPL 2852
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4439 ATSVSQ----RLRRTSEhsnassslslgstswTANPVHNTVPSVPLDSAMGPPVDRSTKPQVSQPVGPKMPQHVAQKQIP 4514
Cdd:PHA03247 2853 GGSVAPggdvRRRPPSR---------------SPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPP 2917
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 4515 QQLPNQLPQQIPQQLPKQLPQQIPQQLPQQLPQQLPKQLPQQIPPQLPKQLPQQIPQP--ELPQQLPnnlPRHAPKLSSR 4592
Cdd:PHA03247 2918 QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPrfRVPQPAP---SREAPASSTP 2994

                  ....*....
gi 440216479 4593 SHTIQGDSG 4601
Cdd:PHA03247 2995 PLTGHSLSR 3003
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1047-1180 1.20e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.46  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1047 PSPRAQSPG-KPATRSQSPEKPQPRATPRQSPEKEQPAFKQTHEVYTPSQPEKQFPRARSPEktPGWTQPQVSPRQSPEK 1125
Cdd:PRK10263  740 PHEPLFTPIvEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQ--PQYQQPQQPVAPQPQY 817
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 440216479 1126 QLPRaQSPEKVPAVRQPSVSPRQSPEKQIPDPKTRDQGPGlpriSPRQSPEKQLP 1180
Cdd:PRK10263  818 QQPQ-QPVAPQPQYQQPQQPVAPQPQDTLLHPLLMRNGDS----RPLHKPTTPLP 867
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1008-1255 1.25e-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: 45.14  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1008 QVQRETTFEGRRVSQDREISIDELILIEETSGAPGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFKQT 1087
Cdd:NF033839  254 KVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVK 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1088 HEVYTP-----SQPEKQFPRAR-SPEKTPGWTQPQVSPRQSPEKQLPRAQSPEKVPAVRQPSVSPRQSPEKQIPDPKTRD 1161
Cdd:NF033839  334 PQPEKPkpevkPQLETPKPEVKpQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQP 413
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1162 QGPGlPRISPrqSPEKQLPKDVPQKSRQSPEKDLTNQQRREE-----EIFRSTITTTQKRTTNNLNEEFITNERDNQNQP 1236
Cdd:NF033839  414 EKPK-PEVKP--QPEKPKPEVKPQPEKPKPEVKPQPEKPKPEvkpqpETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQ 490
                         250
                  ....*....|....*....
gi 440216479 1237 ISEKKPQIPANAEPNTKPS 1255
Cdd:NF033839  491 ADDKKPSTPNNLSKDKQPS 509
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3810-3917 1.39e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 3810 QREQSQRDQNQRELSKREQFQREQLQREQLQREQLQREKLQREQLQREQLQREQLQREQLQREQLQREQ--LQREQLQRD 3887
Cdd:COG1196   342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEalLERLERLEE 421
                          90       100       110
                  ....*....|....*....|....*....|
gi 440216479 3888 QLQLQQQQQAAAAVQIERQRRQELERQLRL 3917
Cdd:COG1196   422 ELEELEEALAELEEEEEEEEEALEEAAEEE 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3810-3882 1.56e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.56e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 440216479 3810 QREQSQRDQNQRELSKREQFQREQLQREQLQREQLQ---REKLQREQLQREQLQREQLQREQLQREQLQREQLQRE 3882
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQaeeYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
969-1192 1.80e-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: 44.76  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  969 TPESSGTPANKKPhQMRRPHDEPEPQLRRSSKSPSVEPRQVQRETTFEGRRVsqdreisidelilieETSGAPGSPKIPS 1048
Cdd:NF033839  280 TQDTPKEPGNKKP-SAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKP---------------EVKPQPEKPKPEV 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1049 PRAQSPGKPATRSQsPEKPQPRAtprqSPEKEQPAFKQTHEVYTPSQPEKQFPRARSPEKTPGWTQPQVSPRQSPEKqlp 1128
Cdd:NF033839  344 KPQLETPKPEVKPQ-PEKPKPEV----KPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEK--- 415
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 440216479 1129 raQSPEKVPAVRQPSVSPRQSPEKQIPDPKTRDQGPGlPRISPRqsPEKQLPKDVPQKSRQSPE 1192
Cdd:NF033839  416 --PKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPK-PEVKPQ--PETPKPEVKPQPEKPKPE 474
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1040-1193 1.91e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.48  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1040 APGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAfkqthevytpsQPEKQFPRARSPEKTPGWTQPQVSP 1119
Cdd:PRK12323  373 GPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAA-----------RAVAAAPARRSPAPEALAAARQASA 441
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 440216479 1120 RQS-PEKQLPRAQSPEKVPAVRQPSVSPRQSPEKQIPDPKTRDQGPGLPRISPRQSPEKQLPKDVPQKSRQSPEK 1193
Cdd:PRK12323  442 RGPgGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDA 516
PHA03247 PHA03247
large tegument protein UL36; Provisional
1033-1200 2.05e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1033 LIEETSGAPGSPKIPSPRAQSPGKPaTRSQSPEKPQPRatprqspekeqpafkqthevytPSQPEKQfPRARSPEKTPGW 1112
Cdd:PHA03247 2540 LEELASDDAGDPPPPLPPAAPPAAP-DRSVPPPRPAPR----------------------PSEPAVT-SRARRPDAPPQS 2595
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1113 TQPQ--VSPRQSPEKQLPRAQSPEKVPAVRQPSVSPRQSPEKqipdpktrdqgpgLPRISPRQSPEKQLPKDVPQKSRQS 1190
Cdd:PHA03247 2596 ARPRapVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANE-------------PDPHPPPTVPPPERPRDDPAPGRVS 2662
                         170
                  ....*....|
gi 440216479 1191 PEKDLTNQQR 1200
Cdd:PHA03247 2663 RPRRARRLGR 2672
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
967-1194 2.62e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.39  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  967 PETPESSGTPANKKPHQMRRPHDEPEPQLRRSSKSPSVEPRQVQRETTfegrrvsQDREISiDELILIEETSGAPGSPKI 1046
Cdd:PHA03307  120 TPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAA-------SSRQAA-LPLSSPEETARAPSSPPA 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1047 PSPRAQSPGKPATRSQSPEKP--QPRATPRQSPEKEQ---PAFKQTHEVYTPSQPEKQFPRARSPEKTPGwtqPQVSPRQ 1121
Cdd:PHA03307  192 EPPPSTPPAAASPRPPRRSSPisASASSPAPAPGRSAaddAGASSSDSSSSESSGCGWGPENECPLPRPA---PITLPTR 268
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 440216479 1122 spekqlPRAQSPEKVPAVRQPSVSPRQSPekQIPDPKTRDQGPGLPRISPRQSPEKQL---PKDVPQKSRQSPEKD 1194
Cdd:PHA03307  269 ------IWEASGWNGPSSRPGPASSSSSP--RERSPSPSPSSPGSGPAPSSPRASSSSsssRESSSSSTSSSSESS 336
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
3810-3882 2.72e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 43.87  E-value: 2.72e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 440216479  3810 QREQSQR--DQNQRELSKREQFQREQLQREQLQREQLQR-EKLQREQLQREQLQREQLQREQLQREQLQREQLQRE 3882
Cdd:pfam15558   64 QAEKEQRkaRLGREERRRADRREKQVIEKESRWREQAEDqENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQAL 139
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
479-750 3.92e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  479 PTSRVVQKAPTPSYAPPSHSPRQSPAkdfSTHGFPSVRPNKATQEYPSQRPGIAGEEVVVVRSEKSRQVKQQTSSQRTIE 558
Cdd:PHA03307  175 PLSSPEETARAPSSPPAEPPPSTPPA---AASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGP 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  559 TEVVGDDYQEPQRSPQKLREAPTpsWEQPATRRQPVEEDfsthgfPSVRTTTTSTRPDQPDGEVLHTSKTVSRNQSANRK 638
Cdd:PHA03307  252 ENECPLPRPAPITLPTRIWEASG--WNGPSSRPGPASSS------SSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRE 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  639 TNTERIIETqvehPNAPSHSTPRSGSPRRSQPRDDYASSPRGPAGKPSQSRPSNTGGSTTTKTTTTSEPLTRRQLQKERE 718
Cdd:PHA03307  324 SSSSSTSSS----SESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRAR 399
                         250       260       270
                  ....*....|....*....|....*....|..
gi 440216479  719 VDAAHRAFAASLRSSSPADSTTSVGSHHQTPR 750
Cdd:PHA03307  400 RRDATGRFPAGRPRPSPLDAGAASGAFYARYP 431
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
3824-3913 3.94e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 43.57  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 3824 SKREQFQREQLQREQLQREQLQREKLQR-EQLQREQLQREQLQReqLQREQLQREQLQREqlqrdqlqlqqqqqaaaavq 3902
Cdd:PTZ00266  435 AERARIEKENAHRKALEMKILEKKRIERlEREERERLERERMER--IERERLERERLERE-------------------- 492
                          90
                  ....*....|.
gi 440216479 3903 ieRQRRQELER 3913
Cdd:PTZ00266  493 --RLERDRLER 501
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3810-3917 3.95e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 3810 QREQSQRDQNQRELSKREQFQREQLQREQLQREQLQ--REKLQREQLQREQLQREQLQREQLQREQLQREQLQREQLQRD 3887
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
                          90       100       110
                  ....*....|....*....|....*....|
gi 440216479 3888 QLQlqqqqQAAAAVQIERQRRQELERQLRL 3917
Cdd:COG1196   395 AAE-----LAAQLEELEEAEEALLERLERL 419
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
3810-3882 4.41e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.56  E-value: 4.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 440216479 3810 QREQSQRDQNQRELSKREQFQREQLQREQLQREQlQREKLQREQlQREQLQREQLQREQLQRE-QLQREQLQRE 3882
Cdd:cd16269   215 KLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEE-ERENLLKEQ-ERALESKLKEQEALLEEGfKEQAELLQEE 286
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3804-3916 5.30e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 5.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 3804 LqreqyQREQSQRDQNQRELSKREQfQREQLQREQLQREQLQREKLQREQLQREQLQREQLQREQLQREQLQREQLQREQ 3883
Cdd:COG1196   318 L-----EELEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
                          90       100       110
                  ....*....|....*....|....*....|...
gi 440216479 3884 LQRDQLQLQQQQQAAAAVQIERQRRQELERQLR 3916
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERLEEELE 424
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3795-3913 5.39e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 5.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 3795 REQRELREqlqreqyQREQSQRDQNQRELSKREQFQREQLQREQLQREQLQREKLQREQLQREQLQREQLQREQLQREQL 3874
Cdd:COG1196   377 AEEELEEL-------AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 440216479 3875 QREQLQREQLQRDQLQLQQQQQAAAAVQIERQRRQELER 3913
Cdd:COG1196   450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1037-1204 6.67e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 6.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1037 TSGAPGSPKIPSPRAQSPGKPATRSQSPEKPQPRATPRQSPEKEQPAFK--QTHEVYTPSQPEKQFPRARSPEKTPGWTQ 1114
Cdd:PRK07764  617 APAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGgdGWPAKAGGAAPAAPPPAPAPAAPAAPAGA 696
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 1115 PQVSPRQSPEKQLPRAQSPEKV---PAVRQPSVSPRQSPEKQIPDPKTRDQGPGlPRISPRQSPEKQLPKDVPQKSRQSP 1191
Cdd:PRK07764  697 APAQPAPAPAATPPAGQADDPAaqpPQAAQGASAPSPAADDPVPLPPEPDDPPD-PAGAPAQPPPPPAPAPAAAPAAAPP 775
                         170
                  ....*....|...
gi 440216479 1192 EKDLTNQQRREEE 1204
Cdd:PRK07764  776 PSPPSEEEEMAED 788
PTZ00121 PTZ00121
MAEBL; Provisional
2079-2309 7.51e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 2079 SRQSEPERELDEESEPELDRDTDVEDDDQTSQLETE---EEI--TQTVTKKETLKEFKQQTK-ETRETRRDSKAEPEKLQ 2152
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEArkaDELkkAEEKKKADEAKKAEEKKKaDEAKKKAEEAKKADEAK 1321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 2153 KKSPQTKVKEESARVPKYQAKVSQKVSQWEPKKQPQREPKVTQKETPLEPKKQPLSKVKDEPEKvnkrepKVPQKESQTK 2232
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK------KAEEKKKADE 1395
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 440216479 2233 LKEEPERVTKKTPQKEPRKEPLRQSEDEPEFSPEEEFDDEPLPMTKTHTTAIEMKRQKDILNRPSVFGQRTPERKSS 2309
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
3810-3882 7.90e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 7.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479  3810 QREQSQRDQNQRELSK-REQFQREQLQREQLQREQLQREKL-----QREQLQREQLQREQLQREQLQREQLQ---REQLQ 3880
Cdd:pfam13868  115 QAEAEEKLEKQRQLREeIDEFNEEQAEWKELEKEEEREEDErileyLKEKAEREEEREAEREEIEEEKEREIarlRAQQE 194

                   ..
gi 440216479  3881 RE 3882
Cdd:pfam13868  195 KA 196
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3816-3917 8.50e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 8.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216479 3816 RDQNQRELSKREQFQREQLQREQLQREQLQREKlQREQLqREQLQREQLQREQLQ-REQLQREQLQREQLQRDQLQLQQQ 3894
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEA-ELEEL-RLELEELELELEEAQaEEYELLAELARLEQDIARLEERRR 312
                          90       100
                  ....*....|....*....|...
gi 440216479 3895 QQAAAAVQIERQRRQELERQLRL 3917
Cdd:COG1196   313 ELEERLEELEEELAELEEELEEL 335
 
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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