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Conserved domains on  [gi|33667117|ref|NP_891554|]
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MICAL-like protein 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
2-107 6.73e-79

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: 250.73  E-value: 6.73e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   2 AAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDA 81
Cdd:cd21253   1 AGIKALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80
                        90       100
                ....*....|....*....|....*.
gi 33667117  82 EDMVALKVPDRLSILTYVSQYYNYFH 107
Cdd:cd21253  81 EDMVALKVPDKLSILTYVSQYYNYFH 106
bMERB_dom pfam12130
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
743-872 3.91e-62

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.


:

Pssm-ID: 463467 [Multi-domain]  Cd Length: 131  Bit Score: 206.21  E-value: 3.91e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   743 QLQDIERRLDALELRGVELEKRLR-AAEGDDAEDSLMVDWFWLIHEKQLLLRQESELMYKSKAQRLEEQQLDIEGELRRL 821
Cdd:pfam12130   1 ELEEIEERQRELEERGVELEKALRgEMSGDEEEEQLLQEWFKLVNEKNALVRRESELMYLAKEQDLEERQARLEQELREL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 33667117   822 MAKPEALKSLQERRREQELLEQYVSTVNDRSDIVDSLDEDRLREQEEDQML 872
Cdd:pfam12130  81 MSKPDWLKTEEDKQREEELLEELVEIVEQRDALVDSLEEDRLREEEEDEEL 131
LIM_Mical_like_1 cd09444
This domain belongs to the LIM domain family which are found on Mical (molecule interacting ...
188-241 6.38e-37

This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins; The LIM domain on proteins of unknown function: This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins. Known members of the Mical-like family includes single LIM domain containing proteins, Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2), and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth, and mobility. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


:

Pssm-ID: 188828 [Multi-domain]  Cd Length: 55  Bit Score: 132.53  E-value: 6.38e-37
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKATGEPGTFVCTSH 241
Cdd:cd09444   1 CAACGQHVHLVQRHLVDGKLYHRNCFRCKECSSTLLPGSYKAGPEPGTFVCTHH 54
PHA03247 super family cl33720
large tegument protein UL36; Provisional
243-649 4.91e-11

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 67.27  E-value: 4.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   243 PAAASASPKLTGLVPRQPGAMGVDSRTSCSPQKAQEANKARPSAWEPAAGNSPARASVPAAPNPAATSATSVHVRSPARP 322
Cdd:PHA03247 2628 PPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPT 2707
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   323 SESRLAPTPTEGKVRPRVTNSSPMGWSSAAPCTAAAASHPAVPPSAPDPRPATPQGGGAPRVAAPQTTLSSSSTSAATVD 402
Cdd:PHA03247 2708 PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPA 2787
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   403 PPAWTPSASRTQQARNKFFQTSAVPPGTSLSGRGPTPSLVLSKDSSKEQARNFLKQALSALEEA--GAPAPG------RP 474
Cdd:PHA03247 2788 VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPlgGSVAPGgdvrrrPP 2867
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   475 SPATAAVPSSQPKteaPQASPLAKPLQSSSPRVLGLP--SRMEPPAPLSTSSTSQASALPPAGRRNLAESsgvgrvgagS 552
Cdd:PHA03247 2868 SRSPAAKPAAPAR---PPVRRLARPAVSRSTESFALPpdQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP---------P 2935
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   553 RPKPEAPMAKGKSTtltqdmsTSLQEGQEDGPAGWRANLKPVDRRSPAERTLKPKEPRALAEP-----RAGEAPRKVSGS 627
Cdd:PHA03247 2936 PPRPQPPLAPTTDP-------AGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASstpplTGHSLSRVSSWA 3008
                         410       420
                  ....*....|....*....|..
gi 33667117   628 FAGSVHItltpvrpDRTPRPAS 649
Cdd:PHA03247 3009 SSLALHE-------ETDPPPVS 3023
 
Name Accession Description Interval E-value
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
2-107 6.73e-79

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: 250.73  E-value: 6.73e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   2 AAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDA 81
Cdd:cd21253   1 AGIKALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80
                        90       100
                ....*....|....*....|....*.
gi 33667117  82 EDMVALKVPDRLSILTYVSQYYNYFH 107
Cdd:cd21253  81 EDMVALKVPDKLSILTYVSQYYNYFH 106
bMERB_dom pfam12130
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
743-872 3.91e-62

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.


Pssm-ID: 463467 [Multi-domain]  Cd Length: 131  Bit Score: 206.21  E-value: 3.91e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   743 QLQDIERRLDALELRGVELEKRLR-AAEGDDAEDSLMVDWFWLIHEKQLLLRQESELMYKSKAQRLEEQQLDIEGELRRL 821
Cdd:pfam12130   1 ELEEIEERQRELEERGVELEKALRgEMSGDEEEEQLLQEWFKLVNEKNALVRRESELMYLAKEQDLEERQARLEQELREL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 33667117   822 MAKPEALKSLQERRREQELLEQYVSTVNDRSDIVDSLDEDRLREQEEDQML 872
Cdd:pfam12130  81 MSKPDWLKTEEDKQREEELLEELVEIVEQRDALVDSLEEDRLREEEEDEEL 131
LIM_Mical_like_1 cd09444
This domain belongs to the LIM domain family which are found on Mical (molecule interacting ...
188-241 6.38e-37

This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins; The LIM domain on proteins of unknown function: This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins. Known members of the Mical-like family includes single LIM domain containing proteins, Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2), and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth, and mobility. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188828 [Multi-domain]  Cd Length: 55  Bit Score: 132.53  E-value: 6.38e-37
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKATGEPGTFVCTSH 241
Cdd:cd09444   1 CAACGQHVHLVQRHLVDGKLYHRNCFRCKECSSTLLPGSYKAGPEPGTFVCTHH 54
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
1-108 2.28e-27

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: 106.99  E-value: 2.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117     1 MAAIRALQQWCRQQCEGYRD-VNICNMTTSFRDGLAFCAILHRHRPDLINFSALKK--ENIYENNKLAFRVAEEHLGIP- 76
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKseFDKLENINLALDVAEKKLGVPk 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 33667117    77 ALLDAEDMVAlkvPDRLSILTYVSQYYNYFHG 108
Cdd:pfam00307  81 VLIEPEDLVE---GDNKSVLTYLASLFRRFQA 109
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
10-106 6.17e-20

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 95.01  E-value: 6.17e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  10 WCRQQCEGYR-DVNICNMTTSFRDGLAFCAILHRHRPDLI--NFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDMVA 86
Cdd:COG5069 133 WCDEDTGGYKpEVDTFDFFRSWRDGLAFSALIHDSRPDTLdpNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVN 212
                        90       100
                ....*....|....*....|
gi 33667117  87 LKVPDRLSILTYVSQYYNYF 106
Cdd:COG5069 213 VSIPDERSIMTYVSWYIIRF 232
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
5-102 1.54e-17

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 78.51  E-value: 1.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117      5 RALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKK----ENIYENNKLAFRVAEEHLGIPALLD 80
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslsrFKKIENINLALSFAEKLGGKVVLFE 80
                           90       100
                   ....*....|....*....|..
gi 33667117     81 AEDMVALKvPDRLSILTYVSQY 102
Cdd:smart00033  81 PEDLVEGP-KLILGVIWTLISL 101
PHA03247 PHA03247
large tegument protein UL36; Provisional
243-649 4.91e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 67.27  E-value: 4.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   243 PAAASASPKLTGLVPRQPGAMGVDSRTSCSPQKAQEANKARPSAWEPAAGNSPARASVPAAPNPAATSATSVHVRSPARP 322
Cdd:PHA03247 2628 PPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPT 2707
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   323 SESRLAPTPTEGKVRPRVTNSSPMGWSSAAPCTAAAASHPAVPPSAPDPRPATPQGGGAPRVAAPQTTLSSSSTSAATVD 402
Cdd:PHA03247 2708 PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPA 2787
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   403 PPAWTPSASRTQQARNKFFQTSAVPPGTSLSGRGPTPSLVLSKDSSKEQARNFLKQALSALEEA--GAPAPG------RP 474
Cdd:PHA03247 2788 VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPlgGSVAPGgdvrrrPP 2867
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   475 SPATAAVPSSQPKteaPQASPLAKPLQSSSPRVLGLP--SRMEPPAPLSTSSTSQASALPPAGRRNLAESsgvgrvgagS 552
Cdd:PHA03247 2868 SRSPAAKPAAPAR---PPVRRLARPAVSRSTESFALPpdQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP---------P 2935
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   553 RPKPEAPMAKGKSTtltqdmsTSLQEGQEDGPAGWRANLKPVDRRSPAERTLKPKEPRALAEP-----RAGEAPRKVSGS 627
Cdd:PHA03247 2936 PPRPQPPLAPTTDP-------AGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASstpplTGHSLSRVSSWA 3008
                         410       420
                  ....*....|....*....|..
gi 33667117   628 FAGSVHItltpvrpDRTPRPAS 649
Cdd:PHA03247 3009 SSLALHE-------ETDPPPVS 3023
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
188-241 7.75e-08

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 49.69  E-value: 7.75e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 33667117    188 CGVCGKHVHLVQRHL-ADGRLYHRSCFRCKQCSCTLHSGAYKATGepGTFVCTSH 241
Cdd:smart00132   2 CAGCGKPIYGTERVLrALGKVWHPECFKCATCGKPLSGDTFFEKD--GKLYCKDC 54
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
240-580 4.15e-06

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 50.34  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   240 SHLPAAASASPKLTGLVPRQPGAMGVDSRTSCSPQKAQEANKARPSAWEPAAGNSPARASVPAAPNPAATSA-TSVHVRS 318
Cdd:pfam17823 128 QSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAAsSAPATLT 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   319 PARPSESRLAPT--PTEGKVRPRVTNSSPMgwsSAAPCTAAAASHPAVPPSAPDPRPATPQGGGAPRVAAPQTTLSSSST 396
Cdd:pfam17823 208 PARGISTAATATghPAAGTALAAVGNSSPA---AGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDPHARRLSPAK 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   397 SAATvDPPAWTPSASRTQQARNKFFQTSAVPPGTSLSGRgPTPSLvlskdsskeqarnflkqalSALEEAGAPAPGRPSP 476
Cdd:pfam17823 285 HMPS-DTMARNPAAPMGAQAQGPIIQVSTDQPVHNTAGE-PTPSP-------------------SNTTLEPNTPKSVAST 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   477 ATAAVPSSQPKTEAPQASPLAKPLQSSSPRVLGlPSRMEPPAPLSTSSTSQASALPPAGRRNLAESSgvgrvgAGSRPKP 556
Cdd:pfam17823 344 NLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEA-TSPTTQPSPLLPTQGAAGPGILLAPEQVATEAT------AGTASAG 416
                         330       340
                  ....*....|....*....|....
gi 33667117   557 EAPMAKGKSTTLTQDMSTSLQEGQ 580
Cdd:pfam17823 417 PTPRSSGDPKTLAMASCQLSTQGQ 440
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
738-885 2.04e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117    738 EEIQRQLQDIERRLDALELRGVELEKRLRAAEGDDAEDSLMVDwfWLIHEKQLLLRQE-------------SELMYKSKA 804
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK--DLGEEEQLRVKEKigeleaeiaslerSIAEKEREL 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117    805 QRLEEQQLDIEGELRRLMAKPEAL-KSLQERRREQELLEQYVSTVNDRsdivdsLDEDRLREQEEDQMLRDMIEKLGLQR 883
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIEELeREIEEERKRRDKLTEEYAELKEE------LEDLRAELEEVDKEFAETRDELKDYR 391

                   ..
gi 33667117    884 KK 885
Cdd:TIGR02169  392 EK 393
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
738-893 1.27e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 1.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117 738 EEIQRQLQDIERRLDALELRGVELEKRLRAAEgddaedslmvdwfwliHEKQLLLRQESELMYKSKAQRLEEQQLDIEGE 817
Cdd:COG4717  84 EEKEEEYAELQEELEELEEELEELEAELEELR----------------EELEKLEKLLQLLPLYQELEALEAELAELPER 147
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33667117 818 LRRLMAKPEALKSLQERRREqelLEQYVSTVndRSDIVDSLDEDRLREQEEDQMLRDMIEKLGLQRKKSKFRLSKI 893
Cdd:COG4717 148 LEELEERLEELRELEEELEE---LEAELAEL--QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
188-227 2.77e-04

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 39.62  E-value: 2.77e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 33667117   188 CGVCGKHV---HLVQrhlADGRLYHRSCFRCKQCSCTLHSGAY 227
Cdd:pfam00412   1 CAGCNRPIydrELVR---ALGKVWHPECFRCAVCGKPLTTGDF 40
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
738-879 8.00e-04

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 41.66  E-value: 8.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117 738 EEIQRQLQDIERRLDAL----ELRGVELEKRLRAAEGDDAEDSLMvDWfwlIHEKQLLLRQESelmYKSKAQRLEEQQLD 813
Cdd:cd00176  75 EEIQERLEELNQRWEELrelaEERRQRLEEALDLQQFFRDADDLE-QW---LEEKEAALASED---LGKDLESVEELLKK 147
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33667117 814 IEGELRRLMAKPEALKSLQERRreQELLEQyvSTVNDRSDIVDSLDEDRLREQEEDQMLRDMIEKL 879
Cdd:cd00176 148 HKELEEELEAHEPRLKSLNELA--EELLEE--GHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
738-887 8.02e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 8.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  738 EEIQRQLQDIERRLDALELRGVELEKRLRAAEGDDAEDSLMVDWFWLIHEKQLLLRQESELM--YKSKAQRLE------E 809
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYeeYLDELREIEkrlsrlE 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  810 QQLD-IEGELRRLMAKPEALKSLQER----RREQELLEQYVSTVNDRSDIVDSLdeDRLREQEEDQMLRDMIEKLGLQRK 884
Cdd:PRK03918 321 EEINgIEERIKELEEKEERLEELKKKlkelEKRLEELEERHELYEEAKAKKEEL--ERLKKRLTGLTPEKLEKELEELEK 398

                 ...
gi 33667117  885 KSK 887
Cdd:PRK03918 399 AKE 401
COG5373 COG5373
Uncharacterized membrane protein [Function unknown];
450-519 7.22e-03

Uncharacterized membrane protein [Function unknown];


Pssm-ID: 444140 [Multi-domain]  Cd Length: 854  Bit Score: 39.98  E-value: 7.22e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117 450 EQARNFLKQALSALEEAGAPAPGRPSPATAAVPSSQPKTEAPQASPLAKPLQSSSPRVLGLPSRMEPPAP 519
Cdd:COG5373  31 EELEAELAEAAEAASAPAEPEPEAAAAATAAAPEAAPAPVPEAPAAPPAAAEAPAPAAAAPPAEAEPAAA 100
 
Name Accession Description Interval E-value
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
2-107 6.73e-79

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: 250.73  E-value: 6.73e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   2 AAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDA 81
Cdd:cd21253   1 AGIKALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80
                        90       100
                ....*....|....*....|....*.
gi 33667117  82 EDMVALKVPDRLSILTYVSQYYNYFH 107
Cdd:cd21253  81 EDMVALKVPDKLSILTYVSQYYNYFH 106
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
3-107 2.88e-69

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: 224.72  E-value: 2.88e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   3 AIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAE 82
Cdd:cd21197   1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAE 80
                        90       100
                ....*....|....*....|....*
gi 33667117  83 DMVALKVPDRLSILTYVSQYYNYFH 107
Cdd:cd21197  81 DMVTMHVPDRLSIITYVSQYYNHFR 105
bMERB_dom pfam12130
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
743-872 3.91e-62

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.


Pssm-ID: 463467 [Multi-domain]  Cd Length: 131  Bit Score: 206.21  E-value: 3.91e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   743 QLQDIERRLDALELRGVELEKRLR-AAEGDDAEDSLMVDWFWLIHEKQLLLRQESELMYKSKAQRLEEQQLDIEGELRRL 821
Cdd:pfam12130   1 ELEEIEERQRELEERGVELEKALRgEMSGDEEEEQLLQEWFKLVNEKNALVRRESELMYLAKEQDLEERQARLEQELREL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 33667117   822 MAKPEALKSLQERRREQELLEQYVSTVNDRSDIVDSLDEDRLREQEEDQML 872
Cdd:pfam12130  81 MSKPDWLKTEEDKQREEELLEELVEIVEQRDALVDSLEEDRLREEEEDEEL 131
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
5-106 3.65e-59

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: 197.01  E-value: 3.65e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   5 RALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDM 84
Cdd:cd21252   3 RALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPEDM 82
                        90       100
                ....*....|....*....|..
gi 33667117  85 VALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21252  83 VSMKVPDCLSIMTYVSQYYNHF 104
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
3-107 4.40e-58

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: 194.04  E-value: 4.40e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   3 AIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAE 82
Cdd:cd22198   1 RPEELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQ 80
                        90       100
                ....*....|....*....|....*
gi 33667117  83 DMVALKVPDRLSILTYVSQYYNYFH 107
Cdd:cd22198  81 EMASLAVPDKLSMVSYLSQFYEAFK 105
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
1-107 3.36e-45

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: 157.91  E-value: 3.36e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   1 MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLD 80
Cdd:cd21216   9 LSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKMLD 88
                        90       100
                ....*....|....*....|....*..
gi 33667117  81 AEDMVALKVPDRLSILTYVSQYYNYFH 107
Cdd:cd21216  89 AEDIVNTPRPDERSVMTYVSCYYHAFA 115
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
7-106 1.01e-40

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: 144.88  E-value: 1.01e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   7 LQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEhLGIPALLDAEDMVA 86
Cdd:cd21198   6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDPADMVL 84
                        90       100
                ....*....|....*....|
gi 33667117  87 LKVPDRLSILTYVSQYYNYF 106
Cdd:cd21198  85 LSVPDKLSVMTYLHQIRAHF 104
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
6-106 1.01e-40

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: 144.85  E-value: 1.01e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   6 ALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDmV 85
Cdd:cd21248   6 ALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDPED-V 84
                        90       100
                ....*....|....*....|.
gi 33667117  86 ALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21248  85 NVEQPDEKSIITYVVTYYHYF 105
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
6-106 1.13e-39

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: 142.17  E-value: 1.13e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   6 ALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDmV 85
Cdd:cd21194   6 ALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDAED-V 84
                        90       100
                ....*....|....*....|.
gi 33667117  86 ALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21194  85 DVARPDEKSIMTYVASYYHYF 105
LIM_Mical_like_1 cd09444
This domain belongs to the LIM domain family which are found on Mical (molecule interacting ...
188-241 6.38e-37

This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins; The LIM domain on proteins of unknown function: This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins. Known members of the Mical-like family includes single LIM domain containing proteins, Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2), and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth, and mobility. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188828 [Multi-domain]  Cd Length: 55  Bit Score: 132.53  E-value: 6.38e-37
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKATGEPGTFVCTSH 241
Cdd:cd09444   1 CAACGQHVHLVQRHLVDGKLYHRNCFRCKECSSTLLPGSYKAGPEPGTFVCTHH 54
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
7-108 8.88e-37

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: 134.01  E-value: 8.88e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   7 LQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDMVA 86
Cdd:cd21195   9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEMAS 88
                        90       100
                ....*....|....*....|..
gi 33667117  87 LKVPDRLSILTYVSQYYNYFHG 108
Cdd:cd21195  89 AQEPDKLSMVMYLSKFYELFRG 110
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
7-109 1.30e-36

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: 133.44  E-value: 1.30e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   7 LQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAeEHLGIPALLDAEDMVA 86
Cdd:cd21254   6 LLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGF-ASLGISRLLEPSDMVL 84
                        90       100
                ....*....|....*....|...
gi 33667117  87 LKVPDRLSILTYVSQYYNYFHGR 109
Cdd:cd21254  85 LAVPDKLTVMTYLYQIRAHFSGQ 107
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
1-106 3.37e-36

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: 132.65  E-value: 3.37e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   1 MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLD 80
Cdd:cd21291   9 LTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGIPQLLD 88
                        90       100
                ....*....|....*....|....*.
gi 33667117  81 AEDMVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21291  89 VEDVCDVAKPDERSIMTYVAYYFHAF 114
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
7-108 1.33e-35

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: 130.77  E-value: 1.33e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   7 LQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDMVA 86
Cdd:cd21250   9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMAS 88
                        90       100
                ....*....|....*....|..
gi 33667117  87 LKVPDRLSILTYVSQYYNYFHG 108
Cdd:cd21250  89 AEEPDKLSMVMYLSKFYELFRG 110
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
2-106 1.66e-35

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: 130.29  E-value: 1.66e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   2 AAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRvAEEHLGIPALLDA 81
Cdd:cd21255   1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFE-AFASLGVPRLLEP 79
                        90       100
                ....*....|....*....|....*
gi 33667117  82 EDMVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21255  80 ADMVLLPIPDKLIVMTYLCQLRAHF 104
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
3-106 1.83e-34

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: 127.12  E-value: 1.83e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   3 AIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAE 82
Cdd:cd21189   2 AKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDPE 81
                        90       100
                ....*....|....*....|....
gi 33667117  83 DmVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21189  82 D-VDVPEPDEKSIITYVSSLYDVF 104
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
1-106 1.06e-33

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: 125.06  E-value: 1.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   1 MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLD 80
Cdd:cd21251   4 VARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPIMT 83
                        90       100
                ....*....|....*....|....*.
gi 33667117  81 AEDMVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21251  84 GKEMASVGEPDKLSMVMYLTQFYEMF 109
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
2-106 1.38e-33

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: 125.12  E-value: 1.38e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   2 AAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDA 81
Cdd:cd21319   5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
                        90       100
                ....*....|....*....|....*
gi 33667117  82 EDmVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21319  85 ED-VFTENPDEKSIITYVVAFYHYF 108
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
2-106 2.70e-33

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: 124.40  E-value: 2.70e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   2 AAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDA 81
Cdd:cd21321   5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTKLLDP 84
                        90       100
                ....*....|....*....|....*
gi 33667117  82 EDmVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21321  85 ED-VNVDQPDEKSIITYVATYYHYF 108
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
2-106 2.91e-33

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


Pssm-ID: 409171  Cd Length: 130  Bit Score: 124.78  E-value: 2.91e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   2 AAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDA 81
Cdd:cd21322  17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHLGLTKLLDP 96
                        90       100
                ....*....|....*....|....*
gi 33667117  82 EDmVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21322  97 ED-VNMEAPDEKSIITYVVSFYHYF 120
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
5-103 5.59e-33

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: 122.92  E-value: 5.59e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   5 RALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDm 84
Cdd:cd21187   3 KTLLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED- 81
                        90
                ....*....|....*....
gi 33667117  85 VALKVPDRLSILTYVSQYY 103
Cdd:cd21187  82 VNVEQPDKKSILMYVTSLF 100
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
2-106 7.36e-32

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409169  Cd Length: 108  Bit Score: 119.82  E-value: 7.36e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   2 AAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDA 81
Cdd:cd21320   2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
                        90       100
                ....*....|....*....|....*
gi 33667117  82 EDmVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21320  82 ED-ISVDHPDEKSIITYVVTYYHYF 105
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
1-106 8.60e-32

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: 119.58  E-value: 8.60e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   1 MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLD 80
Cdd:cd21249   3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
                        90       100
                ....*....|....*....|....*.
gi 33667117  81 AEDmVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21249  83 PED-VAVPHPDERSIMTYVSLYYHYF 107
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
1-106 9.10e-30

second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409041  Cd Length: 107  Bit Score: 113.67  E-value: 9.10e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   1 MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLD 80
Cdd:cd21192   2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
                        90       100
                ....*....|....*....|....*.
gi 33667117  81 AEDMVALKvPDRLSILTYVSQYYNYF 106
Cdd:cd21192  82 VEDVLVDK-PDERSIMTYVSQFLRMF 106
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
6-106 1.35e-29

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: 113.61  E-value: 1.35e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   6 ALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEhLGIPALLDAEDMV 85
Cdd:cd21199  12 ALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAES-VGIPTTLTIDEMV 90
                        90       100
                ....*....|....*....|.
gi 33667117  86 ALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21199  91 SMERPDWQSVMSYVTAIYKHF 111
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
2-108 4.57e-29

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: 112.49  E-value: 4.57e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   2 AAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDA 81
Cdd:cd21287  10 SAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDA 89
                        90       100
                ....*....|....*....|....*..
gi 33667117  82 EDMVALKVPDRLSILTYVSQYYNYFHG 108
Cdd:cd21287  90 EDIVGTARPDEKAIMTYVSSFYHAFSG 116
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
2-108 6.99e-29

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: 112.09  E-value: 6.99e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   2 AAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDA 81
Cdd:cd21288  10 SAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDA 89
                        90       100
                ....*....|....*....|....*..
gi 33667117  82 EDMVALKVPDRLSILTYVSQYYNYFHG 108
Cdd:cd21288  90 EDIVNTPKPDERAIMTYVSCFYHAFAG 116
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
2-108 1.02e-28

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: 111.36  E-value: 1.02e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   2 AAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDA 81
Cdd:cd21289  10 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDA 89
                        90       100
                ....*....|....*....|....*..
gi 33667117  82 EDMVALKVPDRLSILTYVSQYYNYFHG 108
Cdd:cd21289  90 EDIVNTPKPDEKAIMTYVSCFYHAFAG 116
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
7-107 2.28e-28

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: 109.74  E-value: 2.28e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   7 LQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDMVA 86
Cdd:cd21200   6 LLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEVEDMVR 85
                        90       100
                ....*....|....*....|..
gi 33667117  87 LK-VPDRLSILTYVSQYYNYFH 107
Cdd:cd21200  86 MGnRPDWKCVFTYVQSLYRHLR 107
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
1-108 2.28e-27

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: 106.99  E-value: 2.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117     1 MAAIRALQQWCRQQCEGYRD-VNICNMTTSFRDGLAFCAILHRHRPDLINFSALKK--ENIYENNKLAFRVAEEHLGIP- 76
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKseFDKLENINLALDVAEKKLGVPk 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 33667117    77 ALLDAEDMVAlkvPDRLSILTYVSQYYNYFHG 108
Cdd:pfam00307  81 VLIEPEDLVE---GDNKSVLTYLASLFRRFQA 109
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
2-108 5.05e-27

second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409139  Cd Length: 125  Bit Score: 106.71  E-value: 5.05e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   2 AAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDA 81
Cdd:cd21290  13 SAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDA 92
                        90       100
                ....*....|....*....|....*..
gi 33667117  82 EDMVALKVPDRLSILTYVSQYYNYFHG 108
Cdd:cd21290  93 EDIVNTARPDEKAIMTYVSSFYHAFSG 119
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
1-106 9.22e-27

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: 105.30  E-value: 9.22e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   1 MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLD 80
Cdd:cd21244   4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
                        90       100
                ....*....|....*....|....*.
gi 33667117  81 AEDmVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21244  84 PED-VDVVNPDEKSIMTYVAQFLQYS 108
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
7-103 8.77e-26

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: 102.76  E-value: 8.77e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   7 LQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDMVA 86
Cdd:cd21259   6 LLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVEDMVR 85
                        90
                ....*....|....*..
gi 33667117  87 LKVPDRLSILTYVSQYY 103
Cdd:cd21259  86 MREPDWKCVYTYIQEFY 102
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
1-106 3.58e-25

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: 100.86  E-value: 3.58e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   1 MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLD 80
Cdd:cd21243   4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
                        90       100
                ....*....|....*....|....*.
gi 33667117  81 AEDmVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21243  84 PED-VDVDKPDEKSIMTYVAQFLKKY 108
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
5-103 3.16e-24

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: 97.72  E-value: 3.16e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   5 RALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDm 84
Cdd:cd21234   3 KILLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED- 81
                        90
                ....*....|....*....
gi 33667117  85 VALKVPDRLSILTYVSQYY 103
Cdd:cd21234  82 VAVQLPDKKSIIMYLTSLF 100
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
7-103 3.17e-24

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: 98.23  E-value: 3.17e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   7 LQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDMVA 86
Cdd:cd21260   6 LLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVEDMVR 85
                        90
                ....*....|....*..
gi 33667117  87 LKVPDRLSILTYVSQYY 103
Cdd:cd21260  86 MSVPDSKCVYTYIQELY 102
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
6-106 2.68e-23

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: 95.48  E-value: 2.68e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   6 ALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEhLGIPALLDAEDMV 85
Cdd:cd21257  12 ALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VGIKPSLELSEMM 90
                        90       100
                ....*....|....*....|.
gi 33667117  86 ALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21257  91 YTDRPDWQSVMQYVAQIYKYF 111
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
5-103 3.70e-23

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: 95.00  E-value: 3.70e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   5 RALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSA-LKKENIYENNKLAFRVAEEHLGIPALLDAED 83
Cdd:cd21233   3 KILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSvVSQQSATERLDHAFNIARQHLGIEKLLDPED 82
                        90       100
                ....*....|....*....|
gi 33667117  84 mVALKVPDRLSILTYVSQYY 103
Cdd:cd21233  83 -VATAHPDKKSILMYVTSLF 101
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
6-106 3.81e-23

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: 94.84  E-value: 3.81e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   6 ALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDMV 85
Cdd:cd21226   4 GLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDVM 83
                        90       100
                ....*....|....*....|.
gi 33667117  86 ALKvPDRLSILTYVSQYYNYF 106
Cdd:cd21226  84 TGN-PDERSIVLYTSLFYHAF 103
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
6-106 1.04e-22

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: 93.98  E-value: 1.04e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   6 ALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEhLGIPALLDAEDMV 85
Cdd:cd21256  18 ALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGIKSTLDINEMV 96
                        90       100
                ....*....|....*....|.
gi 33667117  86 ALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21256  97 RTERPDWQSVMTYVTAIYKYF 117
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
1-104 7.62e-22

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: 91.24  E-value: 7.62e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   1 MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLD 80
Cdd:cd21238   1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                        90       100
                ....*....|....*....|....
gi 33667117  81 AEDmVALKVPDRLSILTYVSQYYN 104
Cdd:cd21238  81 PED-VDVPQPDEKSIITYVSSLYD 103
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
5-105 2.70e-21

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: 89.60  E-value: 2.70e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   5 RALQQWCRQQCEGYrdvNICNMTTSFRDGLAFCAILHRHRPDLI-NFSALKKENIYENNKLAFRVAEEHLGIPALLDAED 83
Cdd:cd21184   4 SLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLENATKAMDIAEEELGIPKIITPED 80
                        90       100
                ....*....|....*....|..
gi 33667117  84 MVALKVpDRLSILTYVSQYYNY 105
Cdd:cd21184  81 MVSPNV-DELSVMTYLSYFRNA 101
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
10-106 4.07e-21

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: 88.89  E-value: 4.07e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  10 WCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEhLGIPALLDAEDmVALKV 89
Cdd:cd21239   9 WSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDPED-VDVSS 86
                        90
                ....*....|....*..
gi 33667117  90 PDRLSILTYVSQYYNYF 106
Cdd:cd21239  87 PDEKSVITYVSSLYDVF 103
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
7-106 2.22e-20

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: 87.03  E-value: 2.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   7 LQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDMVA 86
Cdd:cd21258   6 LLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVEDMMI 85
                        90       100
                ....*....|....*....|.
gi 33667117  87 L-KVPDRLSILTYVSQYYNYF 106
Cdd:cd21258  86 MgKKPDSKCVFTYVQSLYNHL 106
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
7-106 3.86e-20

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: 86.17  E-value: 3.86e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   7 LQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDMVA 86
Cdd:cd21261   6 LLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVEDMMV 85
                        90       100
                ....*....|....*....|.
gi 33667117  87 L-KVPDRLSILTYVSQYYNYF 106
Cdd:cd21261  86 MgRKPDPMCVFTYVQSLYNHL 106
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
1-106 5.40e-20

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: 85.86  E-value: 5.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   1 MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEhLGIPALLD 80
Cdd:cd21240   3 MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLD 81
                        90       100
                ....*....|....*....|....*.
gi 33667117  81 AEDmVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21240  82 AED-VDVPSPDEKSVITYVSSIYDAF 106
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
10-106 6.17e-20

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 95.01  E-value: 6.17e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  10 WCRQQCEGYR-DVNICNMTTSFRDGLAFCAILHRHRPDLI--NFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDMVA 86
Cdd:COG5069 133 WCDEDTGGYKpEVDTFDFFRSWRDGLAFSALIHDSRPDTLdpNVLDLQKKNKALNNFQAFENANKVIGIARLIGVEDIVN 212
                        90       100
                ....*....|....*....|
gi 33667117  87 LKVPDRLSILTYVSQYYNYF 106
Cdd:COG5069 213 VSIPDERSIMTYVSWYIIRF 232
LIM_Mical_like cd09358
The LIM domain of Mical (molecule interacting with CasL) like family; The LIM domain of Mical ...
188-241 1.09e-19

The LIM domain of Mical (molecule interacting with CasL) like family; The LIM domain of Mical (molecule interacting with CasL) like family: Known members of this family includes LIM domain containing proteins; Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2) and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth and mobility. Eplin has also found to be tumor suppressor. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs.. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188744 [Multi-domain]  Cd Length: 53  Bit Score: 83.09  E-value: 1.09e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKATgePGTFVCTSH 241
Cdd:cd09358   1 CAVCGKTVYPMERLVADGKLFHKSCFRCSHCNKTLRLGNYASL--EGKLYCKPH 52
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
5-102 1.54e-17

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 78.51  E-value: 1.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117      5 RALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKK----ENIYENNKLAFRVAEEHLGIPALLD 80
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslsrFKKIENINLALSFAEKLGGKVVLFE 80
                           90       100
                   ....*....|....*....|..
gi 33667117     81 AEDMVALKvPDRLSILTYVSQY 102
Cdd:smart00033  81 PEDLVEGP-KLILGVIWTLISL 101
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
3-106 3.89e-17

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: 77.91  E-value: 3.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   3 AIRALQQWCrQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAE 82
Cdd:cd21245   4 AIKALLNWV-QRRTRKYGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPE 82
                        90       100
                ....*....|....*....|....
gi 33667117  83 DmVALKVPDRLSILTYVSQYYNYF 106
Cdd:cd21245  83 D-VMVDSPDEQSIMTYVAQFLEHF 105
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
7-106 4.55e-16

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: 74.70  E-value: 4.55e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   7 LQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDMVA 86
Cdd:cd21196   8 LLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQAVVA 87
                        90       100
                ....*....|....*....|
gi 33667117  87 LKVPdrLSILTYVSQYYNYF 106
Cdd:cd21196  88 GSDP--LGLIAYLSHFHSAF 105
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
4-104 9.24e-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: 73.53  E-value: 9.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   4 IRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIY---ENNKLAFRVAEEH-LGIPALL 79
Cdd:cd00014   1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFkkrENINLFLNACKKLgLPELDLF 80
                        90       100
                ....*....|....*....|....*
gi 33667117  80 DAEDMVALKvpDRLSILTYVSQYYN 104
Cdd:cd00014  81 EPEDLYEKG--NLKKVLGTLWALAL 103
LIM_Mical cd09439
The LIM domain of Mical (molecule interacting with CasL); The LIM domain of Mical (molecule ...
188-241 6.04e-15

The LIM domain of Mical (molecule interacting with CasL); The LIM domain of Mical (molecule interacting with CasL): MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semapho-rin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM domain and calporin homology domain are known for interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein monooxygenase (MO) is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL was characterized to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL was also named junctional Rab13-binding protein (JRAB). As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188823 [Multi-domain]  Cd Length: 55  Bit Score: 69.63  E-value: 6.04e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKATGEPGTFVCTSH 241
Cdd:cd09439   1 CYFCKKRVYVMERLSAEGLFFHRSCFKCSYCGTTLRLGAYAFDRDDGKFYCKPH 54
LIM_like_1 cd09400
LIM domain in proteins of unknown function; LIM domain in proteins of unknown function: LIM ...
186-238 4.65e-12

LIM domain in proteins of unknown function; LIM domain in proteins of unknown function: LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation, and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. The LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


Pssm-ID: 188784  Cd Length: 61  Bit Score: 61.68  E-value: 4.65e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 33667117 186 STCGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKATgEPGTFVC 238
Cdd:cd09400   3 EPCASCGLPVFLAERLLIEGKVYHRTCFKCARCGVQLTPGSFYET-EYGSYCC 54
PHA03247 PHA03247
large tegument protein UL36; Provisional
243-649 4.91e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 67.27  E-value: 4.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   243 PAAASASPKLTGLVPRQPGAMGVDSRTSCSPQKAQEANKARPSAWEPAAGNSPARASVPAAPNPAATSATSVHVRSPARP 322
Cdd:PHA03247 2628 PPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPT 2707
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   323 SESRLAPTPTEGKVRPRVTNSSPMGWSSAAPCTAAAASHPAVPPSAPDPRPATPQGGGAPRVAAPQTTLSSSSTSAATVD 402
Cdd:PHA03247 2708 PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPA 2787
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   403 PPAWTPSASRTQQARNKFFQTSAVPPGTSLSGRGPTPSLVLSKDSSKEQARNFLKQALSALEEA--GAPAPG------RP 474
Cdd:PHA03247 2788 VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPlgGSVAPGgdvrrrPP 2867
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   475 SPATAAVPSSQPKteaPQASPLAKPLQSSSPRVLGLP--SRMEPPAPLSTSSTSQASALPPAGRRNLAESsgvgrvgagS 552
Cdd:PHA03247 2868 SRSPAAKPAAPAR---PPVRRLARPAVSRSTESFALPpdQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP---------P 2935
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   553 RPKPEAPMAKGKSTtltqdmsTSLQEGQEDGPAGWRANLKPVDRRSPAERTLKPKEPRALAEP-----RAGEAPRKVSGS 627
Cdd:PHA03247 2936 PPRPQPPLAPTTDP-------AGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASstpplTGHSLSRVSSWA 3008
                         410       420
                  ....*....|....*....|..
gi 33667117   628 FAGSVHItltpvrpDRTPRPAS 649
Cdd:PHA03247 3009 SSLALHE-------ETDPPPVS 3023
LIM1_SF3 cd09440
The first Lim domain of pollen specific protein SF3; The first Lim domain of pollen specific ...
188-242 7.44e-11

The first Lim domain of pollen specific protein SF3; The first Lim domain of pollen specific protein SF3: SF3 is a Lim protein that is found exclusively in mature plant pollen grains. It contains two LIM domains. The exact function of SF3 is unknown. It may be a transcription factor required for the expression of late pollen genes. It is possible that SF3 protein is involved in controlling pollen-specific processes such as male gamete maturation, pollen tube formation, or even fertilization. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188824 [Multi-domain]  Cd Length: 63  Bit Score: 58.25  E-value: 7.44e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKATgePGTFVCTSHL 242
Cdd:cd09440   5 CKACDKTVYLVDQLSADGVVYHKSCFRCSHCKGTLKLSNYSSM--EGVLYCKPHF 57
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
4-100 1.68e-10

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: 59.62  E-value: 1.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   4 IRALQQWCRQQCEGYrDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALK----------------------------- 54
Cdd:cd21224   2 LSLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRqpttqtvdraqdeaedfwvaefspstgds 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 33667117  55 ------KENIYENNKLAFRVAEEHLGIPALLDAEDMVAlKVPDRLSILTYVS 100
Cdd:cd21224  81 glsselLANEKRNFKLVQQAVAELGGVPALLRASDMSN-TIPDEKVVILFLS 131
PHA03247 PHA03247
large tegument protein UL36; Provisional
243-722 2.09e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.96  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   243 PAAASASPKLTGLVPRQPGAMGVDSR---TSCSPQKAQEANKARPSAW---------EPAAGNSPArasVPAAPNPAATS 310
Cdd:PHA03247 2489 PFAAGAAPDPGGGGPPDPDAPPAPSRlapAILPDEPVGEPVHPRMLTWirgleelasDDAGDPPPP---LPPAAPPAAPD 2565
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   311 ATSVHVRSPARPSE----SRLA-PTPTEGKVRPRVTNSSPMGWSSAAPCTAAAASHPAVPPSAPDPRPATPQGGGAPRVA 385
Cdd:PHA03247 2566 RSVPPPRPAPRPSEpavtSRARrPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPT 2645
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   386 APQTTLSSSSTSAATVDPPAWTPSASRTQQARN---KFFQTSAVPPGTSL--SGRGPTPSLVLSKDSSKEQARNFLKQAL 460
Cdd:PHA03247 2646 VPPPERPRDDPAPGRVSRPRRARRLGRAAQASSppqRPRRRAARPTVGSLtsLADPPPPPPTPEPAPHALVSATPLPPGP 2725
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   461 SALEEAGAPAPGRPSPATAAVPSSQPKTEAPQASP--LAKPLQSSSPR--VLGLPSRMEPPAPLSTSSTSQASALPPAGR 536
Cdd:PHA03247 2726 AAARQASPALPAAPAPPAVPAGPATPGGPARPARPptTAGPPAPAPPAapAAGPPRRLTRPAVASLSESRESLPSPWDPA 2805
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   537 RNLAESSGVGRVGAGSRpKPEAPMAKGKSTTLTQDMSTSLQEGQEDGPAGWRANLKPVDRRSPAERTlkPKEPRALAEPR 616
Cdd:PHA03247 2806 DPPAAVLAPAAALPPAA-SPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSP--AAKPAAPARPP 2882
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   617 AGEAPRKvsgsfagsvhitltPVRPDRTPRPASPGPSLPARSPSPprrrrlavpasldvcdnwlrPEPPGQEARVQSWKE 696
Cdd:PHA03247 2883 VRRLARP--------------AVSRSTESFALPPDQPERPPQPQA--------------------PPPPQPQPQPPPPPQ 2928
                         490       500
                  ....*....|....*....|....*.
gi 33667117   697 EEKKPHLQGKPGRPLSPANVPALPGE 722
Cdd:PHA03247 2929 PQPPPPPPPRPQPPLAPTTDPAGAGE 2954
PHA03247 PHA03247
large tegument protein UL36; Provisional
295-672 2.27e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.96  E-value: 2.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   295 PARASVPAAPNPAATSATSVHVRSPARPSESRLAPT-----PTEGKVRPRVtnsspMGWSSAAPCTAAAASHPAVPPSAP 369
Cdd:PHA03247 2483 PAEARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAPAilpdePVGEPVHPRM-----LTWIRGLEELASDDAGDPPPPLPP 2557
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   370 DPRPATPQGGGAPRVAAPQTTLSSSSTSAATVDPPAwtpsasrtQQARNKffqtsaVPPGTSLSGRGPTPSLVLSKDssk 449
Cdd:PHA03247 2558 AAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPP--------QSARPR------APVDDRGDPRGPAPPSPLPPD--- 2620
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   450 eqarnflkqalsaleeagAPAPGRPSPATAAVPSSQPKTEAPQASPLAKPLQSSSPRVLGLPSRMEPPAplstssTSQAS 529
Cdd:PHA03247 2621 ------------------THAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLG------RAAQA 2676
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   530 ALPPAGRRNLAESSGVGRVGAGSRPKPEAPMAKGKSTTLTQDMSTSLQEgQEDGPAGWRANLKPVDRRSPAERTL----- 604
Cdd:PHA03247 2677 SSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGP-AAARQASPALPAAPAPPAVPAGPATpggpa 2755
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33667117   605 KPKEPRALAEPRAGEAPRKVSGSFAGSvhITLTPVRPDRTPRPASPGPSLPARSPSPPRRRRLAVPAS 672
Cdd:PHA03247 2756 RPARPPTTAGPPAPAPPAAPAAGPPRR--LTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPA 2821
PHA03247 PHA03247
large tegument protein UL36; Provisional
231-733 4.47e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.19  E-value: 4.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   231 GEPGTFVCTSHLPAAASASPKLTGLVPR--QPGAMGVDSRTSCSPQKAQ-------EANKARPSAWEPAAGNSPARASVP 301
Cdd:PHA03247 2549 GDPPPPLPPAAPPAAPDRSVPPPRPAPRpsEPAVTSRARRPDAPPQSARprapvddRGDPRGPAPPSPLPPDTHAPDPPP 2628
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   302 AAPNPAATSATSVHVRSPARPSESRLAPTP--------TEGKVRPRVTNSSPMGWSSAAPCTA----AAASHPAVPPSAP 369
Cdd:PHA03247 2629 PSPSPAANEPDPHPPPTVPPPERPRDDPAPgrvsrprrARRLGRAAQASSPPQRPRRRAARPTvgslTSLADPPPPPPTP 2708
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   370 DPRPaTPQGGGAPRVAAPQTTLSSSSTSAATVDPPAwTPSASRTQQARNkffqTSAVPPGTSLSGRgPTPSlvlsKDSSK 449
Cdd:PHA03247 2709 EPAP-HALVSATPLPPGPAAARQASPALPAAPAPPA-VPAGPATPGGPA----RPARPPTTAGPPA-PAPP----AAPAA 2777
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   450 EQARNFLKQALSALEEAGAPAPGRPSPATAAVPSSQPKTEAPQASPLAKPLQSSSPRVLGLPSRMEPPAPlstsstsqaS 529
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP---------P 2848
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   530 ALPPAGrrNLAESSGVGRvgagsRPKPEAPMAKGKSTTLTQDMSTSlqegqedgpagwranlKPVDRRSPAERTLKPKEP 609
Cdd:PHA03247 2849 SLPLGG--SVAPGGDVRR-----RPPSRSPAAKPAAPARPPVRRLA----------------RPAVSRSTESFALPPDQP 2905
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   610 RALAEPRAGEAPRkvsgsfagsvhiTLTPVRPDRTPRPASPGPSLPARSPSPPRRRRLAVPASLDVCDNWLRPEPPGQEA 689
Cdd:PHA03247 2906 ERPPQPQAPPPPQ------------PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVA 2973
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 33667117   690 rvqswkeeekKPHLQGKPGRPLSPANVPAlpgetvTSPVRLHPD 733
Cdd:PHA03247 2974 ----------VPRFRVPQPAPSREAPASS------TPPLTGHSL 3001
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
20-102 3.58e-09

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


Pssm-ID: 409079  Cd Length: 103  Bit Score: 55.08  E-value: 3.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  20 DVNICNMTTSFRDGLAFCAILHRHRPDLI-NFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDMVALKVpDRLSILTY 98
Cdd:cd21230  16 QLPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLITPEEIINPNV-DEMSVMTY 94

                ....
gi 33667117  99 VSQY 102
Cdd:cd21230  95 LSQF 98
PHA03247 PHA03247
large tegument protein UL36; Provisional
134-595 7.15e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 59.95  E-value: 7.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   134 APVQAAKLPSPAPARKPPLSPAQTNPVVQrrnEGAGGPPPKTDQALAGSLVSSTCGVCGKHVHLVQRHLADGRLYH---- 209
Cdd:PHA03247 2591 APPQSARPRAPVDDRGDPRGPAPPSPLPP---DTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRprra 2667
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   210 RSCFRCKQCSCTLHSGAYKATGEPGTfvctshlPAAASASPKLTGLVPR-QPGAMGVDSRTSCSPQKAQEANKARPSAwe 288
Cdd:PHA03247 2668 RRLGRAAQASSPPQRPRRRAARPTVG-------SLTSLADPPPPPPTPEpAPHALVSATPLPPGPAAARQASPALPAA-- 2738
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   289 PAAGNSPARASVPAAPNPAATSATSVHVRSPARPSESRLAPTPTegKVRPRVTNSSPMGWSSAAPCTAAAASHPAVPPSA 368
Cdd:PHA03247 2739 PAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR--LTRPAVASLSESRESLPSPWDPADPPAAVLAPAA 2816
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   369 PDPRPATPQGGGAPRVAAPQTTLSSSSTSAATVDPPAwtpsasrtqqarnkffqtSAVPPGTSLSGRGPT-PSLVLSKDS 447
Cdd:PHA03247 2817 ALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG------------------GSVAPGGDVRRRPPSrSPAAKPAAP 2878
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   448 SKEQARNFLKQALSALEEAGAPAPGRPSPATAAVPSSQPKteaPQASPLAKPLQSSSPRVLGLPSRMEPPAPLSTSSTSQ 527
Cdd:PHA03247 2879 ARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQ---PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEP 2955
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33667117   528 ASALPPAGRRNLAESSGVGRVGAGSRPKPEAPMAKGKSTTLTQDM---------STSLQEGQEDGPAGWRANLKPVD 595
Cdd:PHA03247 2956 SGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSlsrvsswasSLALHEETDPPPVSLKQTLWPPD 3032
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
20-102 1.27e-08

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: 53.54  E-value: 1.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  20 DVNICNMTTSFRDGLAFCAILHRHRPDLI-NFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDMVALKVpDRLSILTY 98
Cdd:cd21229  18 ELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPEDLSSPHL-DELSGMTY 96

                ....
gi 33667117  99 VSQY 102
Cdd:cd21229  97 LSYF 100
LIM_Mical_like_2 cd09445
This domain belongs to the LIM domain family which are found on Mical (molecule interacting ...
188-241 2.85e-08

This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins; The LIM domain on proteins of unknown function: This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL)-like proteins. Known members of the Mical-like family includes single LIM domain containing proteins, Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2), and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth, and mobility. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188829 [Multi-domain]  Cd Length: 53  Bit Score: 50.93  E-value: 2.85e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKAtgEPGTFVCTSH 241
Cdd:cd09445   1 CRSCGKPVYKMEEIIAEKHIYHKNCFRCKDCNKQLKVDNYQS--HEGNLYCKVH 52
PHA03247 PHA03247
large tegument protein UL36; Provisional
120-519 3.65e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.64  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   120 RASEDSEEEPSGKKAPvqAAKLPSPAPARKPPLSPAQTNPVVQRRNEGAGGPPPKTDQALAGSLVSstcgvcgkhvhLVQ 199
Cdd:PHA03247 2599 RAPVDDRGDPRGPAPP--SPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVS-----------RPR 2665
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   200 RHLADGRLYHRSC----FRCKQCSCTLHSGAYKATGEPGTFVCTSHLPAAASASPKLTG------LVPRQPGAMGVDSRT 269
Cdd:PHA03247 2666 RARRLGRAAQASSppqrPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGpaaarqASPALPAAPAPPAVP 2745
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   270 SCSPQKAQEANKARPSAwePAAGNSPARASVPAAPNPAATSATSVHVRSPARPS-ESRLAPTPTEGKVRPRvTNSSPMGW 348
Cdd:PHA03247 2746 AGPATPGGPARPARPPT--TAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESlPSPWDPADPPAAVLAP-AAALPPAA 2822
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   349 SSAAPCTAAAASHPAVPPSAPDPRPATPQGGGAPRVAAPQTTLSSSSTSAATVDPPAWTPSASRTQQARNKFFQTSAVPP 428
Cdd:PHA03247 2823 SPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPP 2902
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   429 GTslSGRGPTPslvlskdSSKEQARNFLKQALSALEEAGAPAPGRPSPATAAVPSSQPKTEAPQASPLAKPLQSSSPRVL 508
Cdd:PHA03247 2903 DQ--PERPPQP-------QAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVA 2973
                         410
                  ....*....|.
gi 33667117   509 GLPSRMEPPAP 519
Cdd:PHA03247 2974 VPRFRVPQPAP 2984
LIM_TLP_like cd09401
The LIM domains of thymus LIM protein (TLP); The LIM domain of thymus LIM protein (TLP) like ...
188-227 7.06e-08

The LIM domains of thymus LIM protein (TLP); The LIM domain of thymus LIM protein (TLP) like proteins: This family includes the LIM domains of TLP and CRIP (Cysteine-Rich Intestinal Protein). TLP is the distant member of the CRP family of proteins. TLP has two isomers (TLP-A and TLP-B) and sharing approximately 30% with each of the three other CRPs. Like CRP1, CRP2 and CRP3/MLP, TLP has two LIM domains, connected by a flexible linker region. Unlike the CRPs, TLP lacks the nuclear targeting signal (K/R-K/R-Y-G-P-K) and is localized solely in the cytoplasm. TLP is specifically expressed in the thymus in a subset of cortical epithelial cells. TLP has a role in development of normal thymus and in controlling the development and differentiation of thymic epithelial cells. CRIP is a short LIM protein with only one LIM domain. CRIP gene is developmentally regulated and can be induced by glucocorticoid hormones during the first three postnatal weeks. The domain shows close sequence homology to LIM domain of thymus LIM protein. However, unlike the TLP proteins which have two LIM domains, the members of this family have only one LIM domain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188785 [Multi-domain]  Cd Length: 53  Bit Score: 49.65  E-value: 7.06e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAY 227
Cdd:cd09401   1 CPKCGKPVYFAEKKTSLGRDWHKPCLRCEKCKKTLTPGQH 40
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
188-241 7.75e-08

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 49.69  E-value: 7.75e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 33667117    188 CGVCGKHVHLVQRHL-ADGRLYHRSCFRCKQCSCTLHSGAYKATGepGTFVCTSH 241
Cdd:smart00132   2 CAGCGKPIYGTERVLrALGKVWHPECFKCATCGKPLSGDTFFEKD--GKLYCKDC 54
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
20-104 1.59e-07

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


Pssm-ID: 409164  Cd Length: 118  Bit Score: 50.55  E-value: 1.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  20 DVNICNMTTSFRDGLAFCAILHRHRPDLI-NFSALKKENIYENNKLAFRVAEEHLGIPALLDAEDMVALKVpDRLSILTY 98
Cdd:cd21315  31 DLPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIKPEEMVNPKV-DELSMMTY 109

                ....*.
gi 33667117  99 VSQYYN 104
Cdd:cd21315 110 LSQFPN 115
LIM_Eplin_like cd09442
The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin) like proteins; The Lim domain of ...
188-241 2.14e-07

The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin) like proteins; The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin) like proteins: This family contains Epithelial Protein Lost in Neoplasm in Neoplasm (Eplin), xin actin-binding repeat-containing protein 2 (XIRP2) and a group of protein with unknown function. The members of this family all contain a single LIM domain. Epithelial Protein Lost in Neoplasm is a cytoskeleton-associated tumor suppressor whose expression inversely correlates with cell growth, motility, invasion and cancer mortality. Eplin interacts and stabilizes F-actin filaments and stress fibers, which correlates with its ability to suppress anchorage independent growth. In epithelial cells, Eplin is required for formation of the F-actin adhesion belt by binding to the E-cadherin-catenin complex through alpha-catenin. Eplin is expressed in two isoforms, a longer Eplin-beta and a shorter Eplin-alpha. Eplin-alpha mRNA is detected in various tissues and cell lines, but is absent or down regulated in cancer cells. Xirp2 contains a LIM domain and Xin re peats for binding to and stabilising F-actin. Xirp2 is expressed in muscles and is significantly induced in the heart in response to systemic administration of angiotensin II. Xirp2 is an important effector of the Ang II signaling pathway in the heart. The expression of Xirp2 is activated by myocyte enhancer factor (MEF)2A, whose transcriptional activity is stimulated by angiotersin II. Thus, Xirp2 plays important pathological roles in the angiotensin II induced hypertension. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188826 [Multi-domain]  Cd Length: 53  Bit Score: 48.25  E-value: 2.14e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKATGepGTFVCTSH 241
Cdd:cd09442   1 CTVCQKRVYPMERLIADKQNFHKSCFRCEHCNSKLSLGNYASLH--GRIYCKPH 52
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
5-102 2.40e-07

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: 49.61  E-value: 2.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   5 RALQQWCRQQCEgyrDVNICNMTTSFRDGLAFCAILHRHRPDLINFSALKKENIYENNKLAFRVAEEhLGIPALLDAEDM 84
Cdd:cd21185   4 KATLRWVRQLLP---DVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEM 79
                        90
                ....*....|....*...
gi 33667117  85 VALKVpDRLSILTYVSQY 102
Cdd:cd21185  80 ADPEV-EHLGIMAYAAQL 96
LIM_Eplin_like_1 cd09486
a LIM domain subfamily on a group of proteins with unknown function; This model represents a ...
188-242 2.41e-07

a LIM domain subfamily on a group of proteins with unknown function; This model represents a LIM domain subfamily of Eplin-like family. This family shows highest homology to the LIM domains on Eplin and XIRP2 protein families. Epithelial Protein Lost in Neoplasm is a cytoskeleton-associated tumor suppressor whose expression inversely correlates with cell growth, motility, invasion and cancer mortality. Xirp2 is expressed in muscles and is an important effector of the Ang II signaling pathway in the heart. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188870 [Multi-domain]  Cd Length: 53  Bit Score: 48.04  E-value: 2.41e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKATgePGTFVCTSHL 242
Cdd:cd09486   1 CSSCQKTVYPMERLVADKLVFHNSCFCCKHCNAKLSLGSYAAL--HGEFYCKPHF 53
LIM_Ltd-1 cd09443
The LIM domain of LIM and transglutaminase domains protein (Ltd-1); The LIM domain of LIM and ...
188-222 3.03e-07

The LIM domain of LIM and transglutaminase domains protein (Ltd-1); The LIM domain of LIM and transglutaminase domains protein (Ltd-1): This family includes mouse Ky protein and Caenorhabditis elegans Ltd-1 protein. The members of this family consists a N-terminal Lim domain and a C-terminal transglutaminase domain. The mouse Ky protein has putative function in muscle development. The mouse with ky mutant exhibits combined posterior and lateral curvature of the spine. The Ltd-1 gene in C. elegans is expressed in developing hypodermal cells from the twofold stage embryo through adulthood. These data define the ltd-1 gene as a novel marker for C. elegans epithelial cell development. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188827 [Multi-domain]  Cd Length: 55  Bit Score: 47.80  E-value: 3.03e-07
                        10        20        30
                ....*....|....*....|....*....|....*
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTL 222
Cdd:cd09443   1 CPRCGKTAYPAESVDKDGTFYHKGCFKCRECGTRL 35
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
11-84 5.15e-07

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


Pssm-ID: 432229  Cd Length: 85  Bit Score: 48.06  E-value: 5.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117    11 CRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINF-------SALKKENIYeNNKLAFRVAEEHLGI-PALLDAE 82
Cdd:pfam11971   1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLediclkeSMSLADSLY-NIQLLQEFCQRHLGNrCCHLTLE 79

                  ..
gi 33667117    83 DM 84
Cdd:pfam11971  80 DL 81
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
188-227 6.14e-07

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 46.93  E-value: 6.14e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAY 227
Cdd:cd08368   1 CAGCGKPIEGRELLRALGKKWHPECFKCAECGKPLGGDSF 40
LIM_CRP_like cd09326
The LIM domains of Cysteine Rich Protein (CRP) family; The LIM domains of Cysteine Rich ...
188-224 7.22e-07

The LIM domains of Cysteine Rich Protein (CRP) family; The LIM domains of Cysteine Rich Protein (CRP) family: Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to a short glycine-rich repeats (GRRs). The known CRP family members include CRP1, CRP2, and CRP3/MLP. CRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription control, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network. CRP1, CRP2, and CRP3/MLP are involved in promoting protein assembly along the actin-based cytoskeleton. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188712  Cd Length: 53  Bit Score: 46.82  E-value: 7.22e-07
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHS 224
Cdd:cd09326   1 CPRCGKSVYAAEEVIAAGKSWHKSCFTCAVCNKRLDS 37
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
276-566 7.77e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 53.25  E-value: 7.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   276 AQEANKARPSAWEPAAGNSPARASVPAAPNPAATSATSVHVRSPARPSESRLAPTPTEGKVRPRVTNSSPMGWSSAAPCT 355
Cdd:PHA03307   98 ASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLS 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   356 AAAASHPAVPPSAPDPRPATPQGGGAPR-------VAAPQTTLSSSSTSAATVDPPAWTPSASRTQQARNKFFQTSAVPP 428
Cdd:PHA03307  178 SPEETARAPSSPPAEPPPSTPPAAASPRpprrsspISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPL 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   429 GTSLSGRGPTPSLVLSKDSSKEQARNFLKQALSALEEAGAPAPGRP-SPATAAVPSSQPKTEAPQASPLAKPLQSSSPRV 507
Cdd:PHA03307  258 PRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPgSGPAPSSPRASSSSSSSRESSSSSTSSSSESSR 337
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 33667117   508 LGLPSRMEPPAPLSTSSTSQASALPPAGRRNlaeSSGVGRVGAGSRPKPEAPMAKGKST 566
Cdd:PHA03307  338 GAAVSPGPSPSRSPSPSRPPPPADPSSPRKR---PRPSRAPSSPAASAGRPTRRRARAA 393
LIM2_SF3 cd09441
The second Lim domain of pollen specific protein SF3; The second Lim domain of pollen specific ...
188-241 9.36e-07

The second Lim domain of pollen specific protein SF3; The second Lim domain of pollen specific protein SF3: SF3 is a Lim protein that is found exclusively in mature plant pollen grains. It contains two LIM domains. The exact function of SF3 is unknown. It may be a transcription factor required for the expression of late pollen genes. It is possible that SF3 protein is involved in controlling pollen-specific processes such as male gamete maturation, pollen tube formation, or even fertilization. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188825 [Multi-domain]  Cd Length: 61  Bit Score: 46.69  E-value: 9.36e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKAtgEPGTFVCTSH 241
Cdd:cd09441   1 CVACGKTVYPIEKVTVEGTSYHKSCFKCSHGGCTISPSNYAA--HEGRLYCKHH 52
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
243-505 1.78e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 51.77  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  243 PAAASASPKLTGLVPRQPGAMGVDSRTSCSPQKAQEANKARPSAWEPAAGNSPARASVPAAPNPAATSATSVHVRSPARP 322
Cdd:PRK07003 360 PAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRG 439
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  323 SESRLAPTPTEGKVRPRVTNSSPMGWSSAAPCTAAAASHPAVPPSAPDPR--PATPQGGGAPRVAAPQTTLSSSSTSAAT 400
Cdd:PRK07003 440 DDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAfePAPRAAAPSAATPAAVPDARAPAAASRE 519
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  401 VDPPAWTPSASRTQQARnkffQTSAVPPgtsLSGRGPTPSLVLSKDS----SKEQARNFLKQALSALEEAGAPAPGRPSP 476
Cdd:PRK07003 520 DAPAAAAPPAPEARPPT----PAAAAPA---ARAGGAAAALDVLRNAgmrvSSDRGARAAAAAKPAAAPAAAPKPAAPRV 592
                        250       260       270
                 ....*....|....*....|....*....|...
gi 33667117  477 A----TAAVPSSQPKTEAPQASPLAKPLQSSSP 505
Cdd:PRK07003 593 AvqvpTPRARAATGDAPPNGAARAEQAAESRGA 625
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
240-580 4.15e-06

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 50.34  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   240 SHLPAAASASPKLTGLVPRQPGAMGVDSRTSCSPQKAQEANKARPSAWEPAAGNSPARASVPAAPNPAATSA-TSVHVRS 318
Cdd:pfam17823 128 QSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAAsSAPATLT 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   319 PARPSESRLAPT--PTEGKVRPRVTNSSPMgwsSAAPCTAAAASHPAVPPSAPDPRPATPQGGGAPRVAAPQTTLSSSST 396
Cdd:pfam17823 208 PARGISTAATATghPAAGTALAAVGNSSPA---AGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDPHARRLSPAK 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   397 SAATvDPPAWTPSASRTQQARNKFFQTSAVPPGTSLSGRgPTPSLvlskdsskeqarnflkqalSALEEAGAPAPGRPSP 476
Cdd:pfam17823 285 HMPS-DTMARNPAAPMGAQAQGPIIQVSTDQPVHNTAGE-PTPSP-------------------SNTTLEPNTPKSVAST 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   477 ATAAVPSSQPKTEAPQASPLAKPLQSSSPRVLGlPSRMEPPAPLSTSSTSQASALPPAGRRNLAESSgvgrvgAGSRPKP 556
Cdd:pfam17823 344 NLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEA-TSPTTQPSPLLPTQGAAGPGILLAPEQVATEAT------AGTASAG 416
                         330       340
                  ....*....|....*....|....
gi 33667117   557 EAPMAKGKSTTLTQDMSTSLQEGQ 580
Cdd:pfam17823 417 PTPRSSGDPKTLAMASCQLSTQGQ 440
LIM_Eplin_alpha_beta cd09485
The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin); The Lim domain of Epithelial ...
188-241 4.46e-06

The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin); The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin): Epithelial Protein Lost in Neoplasm is a cytoskeleton-associated tumor suppressor whose expression inversely correlates with cell growth, motility, invasion and cancer mortality. Eplin interacts and stabilizes F-actin filaments and stress fibers, which correlates with its ability to suppress anchorage independent growth. In epithelial cells, Eplin is required for formation of the F-actin adhesion belt by binding to the E-cadherin-catenin complex through alpha-catenin. Eplin is expressed in two isoforms, a longer Eplin-beta and a shorter Eplin-alpha. Eplin-alpha mRNA is detected in various tissues and cell lines, but is absent or down regulated in cancer cells. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188869 [Multi-domain]  Cd Length: 53  Bit Score: 44.49  E-value: 4.46e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKATGepGTFVCTSH 241
Cdd:cd09485   1 CVSCQKTVYPLERLVANQQIYHNSCFRCSYCNTKLSLGTYASLH--GNIYCKPH 52
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
286-655 7.33e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.98  E-value: 7.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  286 AWEPAAGNSPARASVPAAPNPAATSATSVHvRSPARPSESRLAPTPTEGKVRPRVTNSSPMGWSSAAPCTAAAASHPAVP 365
Cdd:PRK07764 391 AGAPAAAAPSAAAAAPAAAPAPAAAAPAAA-AAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPA 469
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  366 PSAPDPR--------PATPQGGGAPrvAAPQTTLSSSSTSAATVDPPAWtpSASRTQQARNKFFQTSAVPPGTSLSG-RG 436
Cdd:PRK07764 470 PAAAPEPtaapapapPAAPAPAAAP--AAPAAPAAPAGADDAATLRERW--PEILAAVPKRSRKTWAILLPEATVLGvRG 545
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  437 PTpsLVLSKDSSKEqARNF--------LKQAL-------------------SALEEAGAPAPGRPSPATAAVPSSQPKTE 489
Cdd:PRK07764 546 DT--LVLGFSTGGL-ARRFaspgnaevLVTALaeelggdwqveavvgpapgAAGGEGPPAPASSGPPEEAARPAAPAAPA 622
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  490 APQASPLAKPLQSSSPRVLGLPSRMEPPAPLSTSSTSQASALPPAGR-RNLAESSGVGRVGAGSRPKPEAPMAKGKSTTL 568
Cdd:PRK07764 623 APAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWpAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA 702
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  569 TQDMSTSLQEGQEDGPAGWRANLKPVDRRSPAERTLKPKEPRALAEPRAGEAPRkvSGSFAGSVHITLTPVRPDRTPRPA 648
Cdd:PRK07764 703 PAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPA--QPPPPPAPAPAAAPAAAPPPSPPS 780

                 ....*..
gi 33667117  649 SPGPSLP 655
Cdd:PRK07764 781 EEEEMAE 787
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
244-654 7.60e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.17  E-value: 7.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   244 AAASASPKLTGLVPRQPGAMGVDSR---TSCSPQKAQEANKARPSAWEPAAGNSPARASVPAAPNPAATSATSVhvrSPA 320
Cdd:PHA03307   24 PPATPGDAADDLLSGSQGQLVSDSAelaAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAP---ASP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   321 RPSESRLAPTPTEGKVRPRVTNSS-------PMGWSSAAPCTAAAASHPAVPPSAPDPRPATPQGGGAPR-----VAAPQ 388
Cdd:PHA03307  101 AREGSPTPPGPSSPDPPPPTPPPAspppspaPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRqaalpLSSPE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   389 TTLSSSSTSAATVDPPAWTPSASRTQQARNKFFQTSAVPPGTSLSGRGPTPSLVLSKDSSKEQARNflkqalsaLEEAGA 468
Cdd:PHA03307  181 ETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSG--------CGWGPE 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   469 PAPGRPSPATAAVPSSQPKTEAPQASPLAKPLQSSSPRVLGLPSRMEPPAPlstsstsqASALPPAGRRNLAESSGVGRV 548
Cdd:PHA03307  253 NECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSP--------GSGPAPSSPRASSSSSSSRES 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   549 G-AGSRPKPEAPMAKGKSTTLTQDMSTSLQEGQEDGPAGWRANLKPVDRRSPAERTLKPKEPRALAEPRAGEA--PRKVS 625
Cdd:PHA03307  325 SsSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRarRRDAT 404
                         410       420
                  ....*....|....*....|....*....
gi 33667117   626 GSFAGSVHITLTPVRPDRTPRPASPGPSL 654
Cdd:PHA03307  405 GRFPAGRPRPSPLDAGAASGAFYARYPLL 433
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
259-494 9.00e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 49.49  E-value: 9.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  259 QPGAMGVDSrTSCSPQKAQEANKARPSAWEPAAGNSPARASVPAAPNPAATSATSVHVRSPARPSESRLAPTPTegkvrp 338
Cdd:PRK12323 364 RPGQSGGGA-GPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAA------ 436
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  339 RVTNSSPMGWSSAAPCTAAAASHPAVPPSAPDPRPATPQGGGAPRVAAPQTTLSSSSTsaatvDPPAWTpsasrtqqarn 418
Cdd:PRK12323 437 RQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADD-----DPPPWE----------- 500
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33667117  419 kffQTSAVPPGTSLSGRGPTPSLVLSKDSSKEQARnflkQALSALEEAGAPAPGRPSPATAAVPSSQPKTEAPQAS 494
Cdd:PRK12323 501 ---ELPPEFASPAPAQPDAAPAGWVAESIPDPATA----DPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRAS 569
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
738-885 2.04e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117    738 EEIQRQLQDIERRLDALELRGVELEKRLRAAEGDDAEDSLMVDwfWLIHEKQLLLRQE-------------SELMYKSKA 804
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK--DLGEEEQLRVKEKigeleaeiaslerSIAEKEREL 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117    805 QRLEEQQLDIEGELRRLMAKPEAL-KSLQERRREQELLEQYVSTVNDRsdivdsLDEDRLREQEEDQMLRDMIEKLGLQR 883
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIEELeREIEEERKRRDKLTEEYAELKEE------LEDLRAELEEVDKEFAETRDELKDYR 391

                   ..
gi 33667117    884 KK 885
Cdd:TIGR02169  392 EK 393
LIM3_abLIM cd09329
The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin ...
188-227 2.24e-05

The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188715 [Multi-domain]  Cd Length: 52  Bit Score: 42.69  E-value: 2.24e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHsGAY 227
Cdd:cd09329   1 CAGCGQEIKNGQALLALDKQWHVWCFKCKECGKVLT-GEY 39
PRK10263 PRK10263
DNA translocase FtsK; Provisional
244-504 2.42e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 48.54  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   244 AAASASPKLTglvprQPGAMGVDSRTSCSPQKAQEANKARPS-AWEPAAGNSPARASVpaAPNPAATSATSVHVRSPARP 322
Cdd:PRK10263  321 AVAAAATTAT-----QSWAAPVEPVTQTPPVASVDVPPAQPTvAWQPVPGPQTGEPVI--APAPEGYPQQSQYAQPAVQY 393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   323 SESRLAPTPTEGKVRPRVTNSSPmgwssaapCTAAAASHPAVPPSAPDPRPATPQGGGAPRVAAPQTTLSSSSTSAATVD 402
Cdd:PRK10263  394 NEPLQQPVQPQQPYYAPAAEQPA--------QQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTE 465
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   403 PPAWTPSASRTQ-QARNKFFQTSAVPPGTSLSGRGPT-PSLVLSKDSSKEQARNflKQALSAL-----EEAGAPAPGRPS 475
Cdd:PRK10263  466 QTYQQPAAQEPLyQQPQPVEQQPVVEPEPVVEETKPArPPLYYFEEVEEKRARE--REQLAAWyqpipEPVKEPEPIKSS 543
                         250       260
                  ....*....|....*....|....*....
gi 33667117   476 PATAAVPSSQPKTEAPQASPLAKPLQSSS 504
Cdd:PRK10263  544 LKAPSVAAVPPVEAAAAVSPLASGVKKAT 572
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
286-497 2.64e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 47.95  E-value: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  286 AWEPAAGN---SPARASVP--AAPNPAATSATSVHVRSPARPSESRLAPTPTEGKVRPRVTNSSPMGWSSAAPCTAAAAS 360
Cdd:PRK12323 362 AFRPGQSGggaGPATAAAApvAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASA 441
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  361 HPAVPPSAPDPRP-ATPQGGGAPRVAAPQTTlsssstsaatvdPPAWTPSASRTQQARNKFFQTSAVPPGTSLSGRGPTP 439
Cdd:PRK12323 442 RGPGGAPAPAPAPaAAPAAAARPAAAGPRPV------------AAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASP 509
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 33667117  440 SLVLSkdsskEQARNFLKQALSALEEAGAPAPGRPSPATAAVPSSQPKTEAPQASPLA 497
Cdd:PRK12323 510 APAQP-----DAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVA 562
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
272-514 3.12e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.67  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  272 SPQKAQEANKARPSAWEPA-AGNSPARASVPAAPNPAATSATSVHVRSPARPSESRLAPTPTEGKVRPRVTNSSPMGWSS 350
Cdd:PRK07764 591 APGAAGGEGPPAPASSGPPeEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWP 670
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  351 AAPCTAAaashPAVPPSAPDPRPATPQGGGAPRVAAPQttlsssstsaatvdpPAWTPSASRTQQARNkffQTSAVPPGT 430
Cdd:PRK07764 671 AKAGGAA----PAAPPPAPAPAAPAAPAGAAPAQPAPA---------------PAATPPAGQADDPAA---QPPQAAQGA 728
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  431 SLSGRGPTPSLVLSKDSSKEQArnflkqalSALEEAGAPAPGRPSPATAAVPSSQPKTEAPQASPLAKPLQSSSPRVLGL 510
Cdd:PRK07764 729 SAPSPAADDPVPLPPEPDDPPD--------PAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRD 800

                 ....
gi 33667117  511 PSRM 514
Cdd:PRK07764 801 AEEV 804
LIM1_CRP cd09402
The first LIM domain of Cysteine Rich Protein (CRP); The first LIM domain of Cysteine Rich ...
188-224 3.71e-05

The first LIM domain of Cysteine Rich Protein (CRP); The first LIM domain of Cysteine Rich Protein (CRP): Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to a short glycine-rich repeats (GRRs). The CRP family members include CRP1, CRP2, CRP3/MLP. CRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription control, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network. It is evident that CRP1, CRP2, and CRP3/MLP are involved in promoting protein assembly along the actin-based cytoskeleton. Although members of the CRP family share common binding partners, they are also capable of recognizing different and specific targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188786  Cd Length: 53  Bit Score: 41.88  E-value: 3.71e-05
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHS 224
Cdd:cd09402   1 CGACEKTVYHAEEVQCEGRSFHKSCFLCMVCRKNLDS 37
LIM1_MLP84B_like cd09404
The LIM domain of Mlp84B and Mlp60A; The LIM domain of Mlp84B and Mlp60A: Mlp84B and Mlp60A ...
188-225 3.93e-05

The LIM domain of Mlp84B and Mlp60A; The LIM domain of Mlp84B and Mlp60A: Mlp84B and Mlp60A belong to the CRP LIM domain protein family. The Mlp84B protein contains five copies of the LIM domains, each followed by a Glycin Rich Region (GRR). However, only the first LIM domain of Mlp84B is in this family. Mlp60A exhibits only one LIM domain linked to a glycin-rich region. Mlp84B and Mlp60A are muscle specific proteins and have been implicated in muscle differentiation. While Mlp84B transcripts are enriched at the terminal ends of muscle fibers, Mlp60A transcripts are found throughout the muscle fibers. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188788  Cd Length: 54  Bit Score: 42.09  E-value: 3.93e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQC-------SCTLHSG 225
Cdd:cd09404   2 CPKCGKSVYAAEERLAGGYKWHKMCFKCGMCnklldstNCAEHEG 46
LIM2_TLP cd09477
The second LIM domain of thymus LIM protein (TLP); The second LIM domain of thymus LIM protein ...
188-227 5.05e-05

The second LIM domain of thymus LIM protein (TLP); The second LIM domain of thymus LIM protein (TLP): TLP is the distant member of the CRP family of proteins. TLP has two isomers (TLP-A and TLP-B) and sharing approximately 30% with each of the three other CRPs. Like CRP1, CRP2 and CRP3/MLP, TLP has two LIM domains, connected by a flexible linker region. Unlike the CRPs, TLP lacks the nuclear targeting signal (K/R-K/R-Y-G-P-K) and is localized solely in the cytoplasm. TLP is specifically expressed in the thymus in a subset of cortical epithelial cells. TLP has a role in development of normal thymus and in controlling the development and differentiation of thymic epithelial cells. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188861  Cd Length: 54  Bit Score: 41.54  E-value: 5.05e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAY 227
Cdd:cd09477   1 CPGCGKPVYFAEKVMSLGRNWHRPCLRCQRCKKTLTAGGH 40
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
272-388 7.09e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 46.63  E-value: 7.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  272 SPQKAQEANKARPSAWEPAAGnSPARASVPAAPNPAATSATSVHVRSPARPSESRLAPTPTEGKVRPRvtNSSPMGWSSA 351
Cdd:PRK14951 372 AAAPAEKKTPARPEAAAPAAA-PVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAP--AAAPAAVALA 448
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 33667117  352 APCTAAAASHPAVPPSAPDPRPATPQGGGAPRVAAPQ 388
Cdd:PRK14951 449 PAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAA 485
LIM1_CRP1 cd09479
The first LIM domain of Cysteine Rich Protein 1 (CRP1); The first LIM domain of Cysteine Rich ...
188-232 8.84e-05

The first LIM domain of Cysteine Rich Protein 1 (CRP1); The first LIM domain of Cysteine Rich Protein 1 (CRP1): Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to a short glycine-rich repeats (GRRs). The CRP family members include CRP1, CRP2, CRP3/MLP and TLP. CRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription circuits, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network. CRP1 can associate with the actin cytoskeleton and are capable of interacting with alpha-actinin and zyxin. CRP1 was shown to regulate actin filament bundling by interaction with alpha-actinin and direct binding to actin filaments. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188863  Cd Length: 56  Bit Score: 41.16  E-value: 8.84e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKATGE 232
Cdd:cd09479   3 CGVCQKTVYFAEEVQCEGRSFHKSCFLCMVCKKNLDSTTVAVHGE 47
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
738-844 9.66e-05

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 42.56  E-value: 9.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   738 EEIQRQLQDIERRLDALELRgvelEKRLRAAEGDDAEDSLMVDWFWLIHEKQlllRQESElmykSKAQRLEEQQLDIEGE 817
Cdd:pfam13863  13 LALDAKREEIERLEELLKQR----EEELEKKEQELKEDLIKFDKFLKENDAK---RRRAL----KKAEEETKLKKEKEKE 81
                          90       100
                  ....*....|....*....|....*..
gi 33667117   818 LRRLMAKPEALKSlqERRREQELLEQY 844
Cdd:pfam13863  82 IKKLTAQIEELKS--EISKLEEKLEEY 106
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
738-893 1.27e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 1.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117 738 EEIQRQLQDIERRLDALELRGVELEKRLRAAEgddaedslmvdwfwliHEKQLLLRQESELMYKSKAQRLEEQQLDIEGE 817
Cdd:COG4717  84 EEKEEEYAELQEELEELEEELEELEAELEELR----------------EELEKLEKLLQLLPLYQELEALEAELAELPER 147
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33667117 818 LRRLMAKPEALKSLQERRREqelLEQYVSTVndRSDIVDSLDEDRLREQEEDQMLRDMIEKLGLQRKKSKFRLSKI 893
Cdd:COG4717 148 LEELEERLEELRELEEELEE---LEAELAEL--QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
LIM2_CRP2 cd09840
The second LIM domain of Cysteine Rich Protein 2 (CRP2); The second LIM domain of Cysteine ...
188-224 1.44e-04

The second LIM domain of Cysteine Rich Protein 2 (CRP2); The second LIM domain of Cysteine Rich Protein 2 (CRP2): Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to short glycine-rich repeats (GRRs). The CRP family members include CRP1, CRP2, CRP3/MLP and TLPCRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription circuits, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network.CRP3 also called Muscle LIM Protein (MLP), which is a striated muscle-specific factor that enhances myogenic differentiation. The second LIM domain of CRP3/MLP interacts with cytoskeletal protein beta-spectrin. CRP3/MLP also interacts with the basic helix-loop-helix myogenic transcription factors MyoD, myogenin, and MRF4 thereby increasing their affinity for specific DNA regulatory elements. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188871 [Multi-domain]  Cd Length: 54  Bit Score: 40.48  E-value: 1.44e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHS 224
Cdd:cd09840   1 CSRCGDSVYAAEKIMGAGKPWHKNCFRCAKCGKSLES 37
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
738-889 1.63e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 1.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117 738 EEIQRQLQDIERRLDALELRGVELEKRLRAAEGDDAEdslmvdwfwLIHEKQLLLRQESELmyKSKAQRLEEQQLDIEGE 817
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYE---------LLAELARLEQDIARL--EERRRELEERLEELEEE 324
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33667117 818 LRRLMAKPEALKSLQERRREQ--ELLEQYVSTVNDRSDIVDSLDED-RLREQEEDQMLRDMIEKLGLQRKKSKFR 889
Cdd:COG1196 325 LAELEEELEELEEELEELEEEleEAEEELEEAEAELAEAEEALLEAeAELAEAEEELEELAEELLEALRAAAELA 399
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
738-884 1.88e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117 738 EEIQRQLQDIERRLDALELRGVELEKRLRAAEG--DDAEDSLMVDwfwlihEKQLLLRQESELMYKSKAQRLEEQQLDIE 815
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAelAEAEEALLEA------EAELAEAEEELEELAEELLEALRAAAELA 399
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33667117 816 GELRRLMAKPEALKSLQERRRE-----QELLEQYVSTVNDRSDIVDSLDEDRLREQEEDQMLRDMIEKLGLQRK 884
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEeleelEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
219-646 1.95e-04

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 45.29  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   219 SCTLHSGAYKA----TGEPGTFVCTSHLPAAASASPKLTGLVPRQPGAMGVDSRTScspqKAQEANKARPSAWEPAAGNS 294
Cdd:pfam05109 431 SPTLNTTGFAApnttTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGAS----PVTPSPSPRDNGTESKAPDM 506
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   295 PARASVPAAPNPAATSATsvhvrsPARPSESRLAPTPTEGKVRPRVTNSSPMgwssaapctaaaashpavpPSAPDPRPA 374
Cdd:pfam05109 507 TSPTSAVTTPTPNATSPT------PAVTTPTPNATSPTLGKTSPTSAVTTPT-------------------PNATSPTPA 561
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   375 --TPqgggAPRVAAPQTTLSSSSTSAATVDPPAWTPSASRTQQARNKFFQTsavppgtsLSGRGPTPSLVLSKdsskeqa 452
Cdd:pfam05109 562 vtTP----TPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHT--------LGGTSSTPVVTSPP------- 622
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   453 rnflKQALSALEEAGAPAPGRPSPATAAVPSSQPKTEAPQASPLAK---PLQSSSPRVLGLPSRMEPPAPLSTSSTSQAS 529
Cdd:pfam05109 623 ----KNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTshmPLLTSAHPTGGENITQVTPASTSTHHVSTSS 698
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   530 ALPPAGrrNLAESSGVGRVGAGSRP---------------KPEAPMAKGK---STTLTQDMSTSLQEGQEDGPAGWRANL 591
Cdd:pfam05109 699 PAPRPG--TTSQASGPGNSSTSTKPgevnvtkgtppknatSPQAPSGQKTavpTVTSTGGKANSTTGGKHTTGHGARTST 776
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33667117   592 KPV-----DRRSPAER----TLKPKEPRALAEPRAGEAPRKVSGSFAgsvhitLTPVRPDRTPR 646
Cdd:pfam05109 777 EPTtdyggDSTTPRTRynatTYLPPSTSSKLRPRWTFTSPPVTTAQA------TVPVPPTSQPR 834
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
728-884 1.98e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117    728 VRLHPDYLSPEEIQRQLQDIERRLDALELRGVELEKRLRAAEGD-----DAEDSLMVDWFWLiHEKQLLLRQESElMYKS 802
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEElesleAELEELEAELEEL-ESRLEELEEQLE-TLRS 386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117    803 KAQRLEEQQLDIEGELRRLMAKPEALKSLQERRREQELLEQYVSTVNDRSDIVDSLDEDRLREQEEDQMLRDMIEKLGLQ 882
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466

                   ..
gi 33667117    883 RK 884
Cdd:TIGR02168  467 RE 468
LIM2_CRP3 cd09482
The second LIM domain of Cysteine Rich Protein 3 (CRP3/MLP); The second LIM domain of Cysteine ...
188-238 2.19e-04

The second LIM domain of Cysteine Rich Protein 3 (CRP3/MLP); The second LIM domain of Cysteine Rich Protein 3 (CRP3/MLP): Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to short glycine-rich repeats (GRRs). The CRP family members include CRP1, CRP2, CRP3/MLP and TLPCRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription circuits, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network.CRP3 also called Muscle LIM Protein (MLP), which is a striated muscle-specific factor that enhances myogenic differentiation. The second LIM domain of CRP3/MLP interacts with cytoskeletal protein beta-spectrin. CRP3/MLP also interacts with the basic helix-loop-helix myogenic transcription factors MyoD, myogenin, and MRF4 thereby increasing their affinity for specific DNA regulatory elements. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188866 [Multi-domain]  Cd Length: 54  Bit Score: 40.00  E-value: 2.19e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAykATGEPGTFVC 238
Cdd:cd09482   1 CPRCGKSVYAAEKVMGGGKPWHKTCFRCAICGKSLESTT--VTDKDGELYC 49
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
738-890 2.34e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 2.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117 738 EEIQRQLQDIERRLDALELRGVELEKRLRAAEG--DDAEDSLMVdwfwLIHEKQLLLRQESELmyKSKAQRLEEQQLDIE 815
Cdd:COG4372  76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEeaEELQEELEE----LQKERQDLEQQRKQL--EAQIAELQSEIAERE 149
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33667117 816 GELRRLMAKpeaLKSLQERRREQELLEQYVSTVNDRSDIVDSLDEDRLREQEEDQMLRDMIEKLGLQRKKSKFRL 890
Cdd:COG4372 150 EELKELEEQ---LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
LIM1_UF1 cd09397
LIM domain in proteins of unknown function; The first Lim domain of a LIM domain containing ...
188-226 2.52e-04

LIM domain in proteins of unknown function; The first Lim domain of a LIM domain containing protein: The functions of the proteins are unknown. The members of this family contain two copies of LIM domain. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188783 [Multi-domain]  Cd Length: 58  Bit Score: 39.94  E-value: 2.52e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 33667117 188 CGVCGKHVHLVQRHLADGRL---YHRSCFRCKQCSCTLHSGA 226
Cdd:cd09397   1 CRKCGLEIEGKSISSKDGELsgqWHRECFVCTTCGCPFQFSV 42
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
728-844 2.61e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 2.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117 728 VRLHPDYLSPEEIQRQLQDIERRLDALELRG---VELEKRLRAAEGD--DAEDSL--MVDWFWLIHEKQL--LLRQESEL 798
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLeelRELEEELEELEAElaELQEELeeLLEQLSLATEEELqdLAEELEEL 204
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 33667117 799 myKSKAQRLEEQQLDIEGELRRLMAKPEALKSLQERRREQELLEQY 844
Cdd:COG4717 205 --QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
188-227 2.77e-04

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 39.62  E-value: 2.77e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 33667117   188 CGVCGKHV---HLVQrhlADGRLYHRSCFRCKQCSCTLHSGAY 227
Cdd:pfam00412   1 CAGCNRPIydrELVR---ALGKVWHPECFRCAVCGKPLTTGDF 40
LIM2_CRP cd09403
The second LIM domain of Cysteine Rich Protein (CRP); The second LIM domain of Cysteine Rich ...
188-224 3.41e-04

The second LIM domain of Cysteine Rich Protein (CRP); The second LIM domain of Cysteine Rich Protein (CRP): Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to a short glycine-rich repeats (GRRs). The CRP family members include CRP1, CRP2, CRP3/MLP. CRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription control, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network. It is evident that CRP1, CRP2, and CRP3/MLP are involved in promoting protein assembly along the actin-based cytoskeleton. Although members of the CRP family share common binding partners, they are also capable of recognizing different and specific targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residu es, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188787  Cd Length: 54  Bit Score: 39.48  E-value: 3.41e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHS 224
Cdd:cd09403   1 CPRCGKSVYAAEKIIGAGKPWHKNCFRCAKCGKSLES 37
LIM1_abLIM cd09327
The first LIM domain of actin binding LIM (abLIM) proteins; The first LIM domain of actin ...
188-239 3.53e-04

The first LIM domain of actin binding LIM (abLIM) proteins; The first LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188713 [Multi-domain]  Cd Length: 52  Bit Score: 39.16  E-value: 3.53e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 33667117 188 CGVCGK----HVHLVQrhladGRLYHRSCFRCKQCSCTLHSGAYkaTGEPGTFVCT 239
Cdd:cd09327   1 CYKCGKkckgEVLRVQ-----DKYFHIKCFTCKVCGCDLAQGGF--FVKEGEYYCT 49
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
738-877 4.29e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 4.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  738 EEIQRQLQDIERRLDALELRGVE---LEKRLRAAEGDDAEdslmvdwfwLIHEKQLLLRQESELmyKSKAQRLEEQQLDI 814
Cdd:COG4913  664 ASAEREIAELEAELERLDASSDDlaaLEEQLEELEAELEE---------LEEELDELKGEIGRL--EKELEQAEEELDEL 732
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33667117  815 EGELRRLMAKPEALKSLQ-ERRREQELLEQYVSTVndRSDIVDSLD-EDRLREQEEDQMLRDMIE 877
Cdd:COG4913  733 QDRLEAAEDLARLELRALlEERFAAALGDAVEREL--RENLEERIDaLRARLNRAEEELERAMRA 795
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
288-656 4.75e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 4.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   288 EPAAGNSPARASVPAAPNPAA------------------TSATSVHVRSPARPSESRLAPTPTEGKVRPRVTNSSPMGWS 349
Cdd:PHA03307   12 EAAAEGGEFFPRPPATPGDAAddllsgsqgqlvsdsaelAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   350 SAAPCTAAAASH---------------PAVPPSAPDPRPATPQGGGAPRVAAPQTTLSSSSTSAATVDPPAWTPSASRTQ 414
Cdd:PHA03307   92 LSTLAPASPAREgsptppgpsspdpppPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQ 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   415 QARNkffqtSAVPPGTSLSGRGPTPSLVLSKDSskeqarnflkqalsalEEAGAPAPGRPSPATAAVPSSQPKTEAPQAS 494
Cdd:PHA03307  172 AALP-----LSSPEETARAPSSPPAEPPPSTPP----------------AAASPRPPRRSSPISASASSPAPAPGRSAAD 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   495 PL-AKPLQSSSPRVLGLPSRMEPPAPLSTSSTSQASALPPAGRRNLAESSGVGRVG-----AGSRPKPEAPMAKGKSTTL 568
Cdd:PHA03307  231 DAgASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASsssspRERSPSPSPSSPGSGPAPS 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   569 TQDMSTSLQEGQEDGPAGWRANlKPVDRRSPAERTLKPKEPRALAEPRAGEAPRKVSGSFAGSvHITLTPVRPDRTPRPA 648
Cdd:PHA03307  311 SPRASSSSSSSRESSSSSTSSS-SESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPS-RAPSSPAASAGRPTRR 388

                  ....*...
gi 33667117   649 SPGPSLPA 656
Cdd:PHA03307  389 RARAAVAG 396
LIM1_CRP2 cd09480
The first LIM domain of Cysteine Rich Protein 2 (CRP2); The first LIM domain of Cysteine Rich ...
188-224 5.26e-04

The first LIM domain of Cysteine Rich Protein 2 (CRP2); The first LIM domain of Cysteine Rich Protein 2 (CRP2): The CRP family members include CRP1, CRP2, CRP3/MLP and TLP. CRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription circuits, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network. CRP2 specifically binds to protein inhibitor of activated STAT-1 (PIAS1) and a novel human protein designed CRP2BP (for CRP2 binding partner). PIAS1 specifically inhibits the STAT-1 pathway and CRP2BP is homologous to members of the histone acetyltransferase family raising the possibility that CRP2 is a modulator of cytokine-controlled pathways or is functionally active in the transcriptional regulatory network. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188864  Cd Length: 55  Bit Score: 38.82  E-value: 5.26e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHS 224
Cdd:cd09480   2 CGACGRTVYHAEEVQCDGRSFHKCCFLCMVCRKNLDS 38
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
425-624 5.95e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.71  E-value: 5.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  425 AVPPGTSLSGRGPtPSLVLSKDSSKEQARnflkQALSALEEAGAPAPGRPSPATAAVPSSQPKTEAPQA-SPLAKPLQSS 503
Cdd:PRK12323 362 AFRPGQSGGGAGP-ATAAAAPVAQPAPAA----AAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARrSPAPEALAAA 436
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  504 SPRVLGLPSRMEPPAPLSTSSTSQASALPPAG-RRNLAESSGVGRVGAGSRPKPEAPMAKGKSTTLTQDMSTSLQEGQED 582
Cdd:PRK12323 437 RQASARGPGGAPAPAPAPAAAPAAAARPAAAGpRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDA 516
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 33667117  583 GPAGWRANL--KPVDRRSPAERTLKPKEPRALAEPRAGEAPRKV 624
Cdd:PRK12323 517 APAGWVAESipDPATADPDDAFETLAPAPAAAPAPRAAAATEPV 560
LIM_CRIP cd09478
The LIM domain of Cysteine-Rich Intestinal Protein (CRIP); The LIM domain of Cysteine-Rich ...
188-227 6.36e-04

The LIM domain of Cysteine-Rich Intestinal Protein (CRIP); The LIM domain of Cysteine-Rich Intestinal Protein (CRIP): CRIP is a short protein with only one LIM domain. CRIP gene is developmentally regulated and can be induced by glucocorticoid hormones during the first three postnatal weeks. The domain shows close sequence homology to LIM domain of thymus LIM protein. However, unlike the TLP proteins which have two LIM domains, the members of this family have only one LIM domain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188862  Cd Length: 54  Bit Score: 38.71  E-value: 6.36e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAY 227
Cdd:cd09478   1 CPKCDKEVYFAERVTSLGKDWHRPCLKCEKCGKTLTPGSH 40
LIM2_Rga cd09395
The second LIM domain of Rga GTPase-Activating Proteins; The second LIM domain of Rga ...
188-231 6.82e-04

The second LIM domain of Rga GTPase-Activating Proteins; The second LIM domain of Rga GTPase-Activating Proteins: The members of this family contain two tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Rga activates GTPases during polarized morphogenesis. In yeast, a known regulating target of Rga is CDC42p, a small GTPase. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188781  Cd Length: 53  Bit Score: 38.23  E-value: 6.82e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKATG 231
Cdd:cd09395   1 CKNCGKKIDDTAILLSSDEAYCSDCFRCRRCSRDITDLKYAKTK 44
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
738-889 6.95e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 6.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117    738 EEIQRQLQDIERRLDALELRGVELEKRLRAAEGDDAEDSLMVDwfwlIHEKQLLLRQEselmyksKAQRLEEQQLDIEGE 817
Cdd:TIGR02169  871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE----KKRKRLSELKA-------KLEALEEELSEIEDP 939
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117    818 LRRLMAKPEALKSL----QERRR-EQEL----------LEQYVSTVNDRSDivdsLDEDRLREQEEDQMLRDMIEKLGlQ 882
Cdd:TIGR02169  940 KGEDEEIPEEELSLedvqAELQRvEEEIralepvnmlaIQEYEEVLKRLDE----LKEKRAKLEEERKAILERIEEYE-K 1014

                   ....*..
gi 33667117    883 RKKSKFR 889
Cdd:TIGR02169 1015 KKREVFM 1021
LIM1_LIMK cd09364
The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain ...
188-231 7.76e-04

The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain Kinase ): LIMK protein family is comprised of two members LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerisation. LIMKs can function in both cytoplasm and nucleus and are expressed in all tissues. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. However, LIMK1 and LIMk2 have different cellular locations. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The LIM domains of LIMK have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188750 [Multi-domain]  Cd Length: 53  Bit Score: 38.24  E-value: 7.76e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKATG 231
Cdd:cd09364   1 CAGCRGKILDSQYVQALNQDWHCDCFRCSVCSDSLSNWYFEKDG 44
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
738-879 8.00e-04

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 41.66  E-value: 8.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117 738 EEIQRQLQDIERRLDAL----ELRGVELEKRLRAAEGDDAEDSLMvDWfwlIHEKQLLLRQESelmYKSKAQRLEEQQLD 813
Cdd:cd00176  75 EEIQERLEELNQRWEELrelaEERRQRLEEALDLQQFFRDADDLE-QW---LEEKEAALASED---LGKDLESVEELLKK 147
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33667117 814 IEGELRRLMAKPEALKSLQERRreQELLEQyvSTVNDRSDIVDSLDEDRLREQEEDQMLRDMIEKL 879
Cdd:cd00176 148 HKELEEELEAHEPRLKSLNELA--EELLEE--GHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
738-887 8.02e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 8.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  738 EEIQRQLQDIERRLDALELRGVELEKRLRAAEGDDAEDSLMVDWFWLIHEKQLLLRQESELM--YKSKAQRLE------E 809
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYeeYLDELREIEkrlsrlE 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  810 QQLD-IEGELRRLMAKPEALKSLQER----RREQELLEQYVSTVNDRSDIVDSLdeDRLREQEEDQMLRDMIEKLGLQRK 884
Cdd:PRK03918 321 EEINgIEERIKELEEKEERLEELKKKlkelEKRLEELEERHELYEEAKAKKEEL--ERLKKRLTGLTPEKLEKELEELEK 398

                 ...
gi 33667117  885 KSK 887
Cdd:PRK03918 399 AKE 401
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
362-561 8.05e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.30  E-value: 8.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  362 PAVPPSAPDPRPATPQGGGAprvAAPQTTLSSSSTSAATVDPPAWTPSASRTQQARNKffqtSAVPPGTSLSGRGPTPSL 441
Cdd:PRK07003 374 ARVAGAVPAPGARAAAAVGA---SAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPA----APAPPATADRGDDAADGD 446
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  442 VLSKDSSKEQARNFLKQALSALEEAGAPAPGR-PSPATAAVPSSQPKTEAPQASPLAKPlQSSSPRVLGLPSRMEPPAPL 520
Cdd:PRK07003 447 APVPAKANARASADSRCDERDAQPPADSGSASaPASDAPPDAAFEPAPRAAAPSAATPA-AVPDARAPAAASREDAPAAA 525
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 33667117  521 STSSTSQASALPPAGR---------------RN--LAESSGVGRvGAGSRPKPEAPMA 561
Cdd:PRK07003 526 APPAPEARPPTPAAAApaaraggaaaaldvlRNagMRVSSDRGA-RAAAAAKPAAAPA 582
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
5-104 1.07e-03

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 39.59  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117   5 RALQQWCRQQCE--GYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFS----ALKKENIYENNKLAFRVAEEhLGIPAL 78
Cdd:cd21218  13 EILLRWVNYHLKkaGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKElvleVLSEEDLEKRAEKVLQAAEK-LGCKYF 91
                        90       100
                ....*....|....*....|....*.
gi 33667117  79 LDAEDMVAlkvPDRLSILTYVSQYYN 104
Cdd:cd21218  92 LTPEDIVS---GNPRLNLAFVATLFN 114
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
738-888 1.08e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117 738 EEIQRQLQDIERRLDAL--ELRGVELEKRLRAAEGDDAEDSLMVDwfwlihEKQLLLRQESELMYKSKAQRLEEQQLDIE 815
Cdd:COG4372  41 DKLQEELEQLREELEQAreELEQLEEELEQARSELEQLEEELEEL------NEQLQAAQAELAQAQEELESLQEEAEELQ 114
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33667117 816 GELRRLMAKPEALKslQERRREQELLEQYVSTVNDRSDIVDSLDEDRLREQEEDQMLRDMIEKLGLQRKKSKF 888
Cdd:COG4372 115 EELEELQKERQDLE--QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
LIM1_CRP3 cd09481
The first LIM domain of Cysteine Rich Protein 3 (CRP3/MLP); The first LIM domain of Cysteine ...
188-229 1.14e-03

The first LIM domain of Cysteine Rich Protein 3 (CRP3/MLP); The first LIM domain of Cysteine Rich Protein 3 (CRP3/MLP): Cysteine-rich proteins (CRPs) are characterized by the presence of two LIM domains linked to short glycine-rich repeats (GRRs). The CRP family members include CRP1, CRP2, CRP3/MLP and TLPCRP1, CRP2 and CRP3 share a conserved nuclear targeting signal (K/R-K/R-Y-G-P-K), which supports the fact that these proteins function not only in the cytoplasm but also in the nucleus. CRPs control regulatory pathways during cellular differentiation, and involve in complex transcription circuits, and the organization as well as the arrangement of the myofibrillar/cytoskeletal network.CRP3 also called Muscle LIM Protein (MLP), which is a striated muscle-specific factor that enhances myogenic differentiation. CRP3/MLP interacts with cytoskeletal protein beta-spectrin. CRP3/MLP also interacts with the basic helix-loop-helix myogenic transcriptio n factors MyoD, myogenin, and MRF4 thereby increasing their affinity for specific DNA regulatory elements. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188865  Cd Length: 54  Bit Score: 37.81  E-value: 1.14e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKA 229
Cdd:cd09481   2 CGACEKTVYHAEEIQCNGRSFHKTCFICMACRKALDSTTVAA 43
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
741-880 1.17e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  741 QRQLQDIERRLDALELRGVELEKRLRAAEG--DDAEDSLMVdwfwlihEKQLLLRQESELMYKSKAQRLEEqqldIEGEL 818
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAelDALQERREA-------LQRLAEYSWDEIDVASAEREIAE----LEAEL 677
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33667117  819 RRLMAKPEALKSLQERRRE-QELLEQYVSTVNDRSDIVDSLDEDRLREQEEDQMLRDMIEKLG 880
Cdd:COG4913  678 ERLDASSDDLAALEEQLEElEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
243-438 1.26e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.56  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  243 PAAASASPKLTGLVPRQPGAMgvdsrtscSPQKAQEANKARPSAWEPAAGNSPArASVPAAPNPAATSATSvhvRSPARP 322
Cdd:PRK12323 406 PAAAPAAAAAARAVAAAPARR--------SPAPEALAAARQASARGPGGAPAPA-PAPAAAPAAAARPAAA---GPRPVA 473
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  323 SESRLAPTPTEGKVRPRVTNSSPMGWSSAAPCTaaaashPAVPPSAPDPRPATPQGGGAPRVAAPQTTLSSSSTSAATVD 402
Cdd:PRK12323 474 AAAAAAPARAAPAAAPAPADDDPPPWEELPPEF------ASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAA 547
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 33667117  403 PPAWTPSASRTQQArnkffqtSAVPPGTSLSGRGPT 438
Cdd:PRK12323 548 APAPRAAAATEPVV-------APRPPRASASGLPDM 576
flhF PRK06995
flagellar biosynthesis protein FlhF;
282-376 1.72e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 41.88  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  282 ARPSAWEPAAGNSPARASVPAAPNPAATSATSVHVRSPARPSESRLAPTPTegkvRPRVTNSSPMGWSSAAPCTAAAASH 361
Cdd:PRK06995  57 AAPAAAQPPPAAAPAAVSRPAAPAAEPAPWLVEHAKRLTAQREQLVARAAA----PAAPEAQAPAAPAERAAAENAARRL 132
                         90
                 ....*....|....*
gi 33667117  362 PAVPPSAPDPRPATP 376
Cdd:PRK06995 133 ARAAAAAPRPRVPAD 147
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
372-561 1.82e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.17  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  372 RPATPQGGGAPR--VAAPQTTLSSSSTSAATVDPPAWTPSASRTQQArnkffQTSAVPPGTSLSGRGPTPSLVLSKDSSK 449
Cdd:PRK12323 364 RPGQSGGGAGPAtaAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAP-----AAAAAARAVAAAPARRSPAPEALAAARQ 438
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  450 EQARNFLKQALSALEEAGAPAPGRPSPATAAVPssqPKTEAPQASPLAKPLQSSSPRVLGLPSRMEPPAPLSTSSTSQAS 529
Cdd:PRK12323 439 ASARGPGGAPAPAPAPAAAPAAAARPAAAGPRP---VAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPD 515
                        170       180       190
                 ....*....|....*....|....*....|..
gi 33667117  530 ALPPAGRRNLAESSGVGRVGAGSRPKPEAPMA 561
Cdd:PRK12323 516 AAPAGWVAESIPDPATADPDDAFETLAPAPAA 547
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
738-879 2.08e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  738 EEIQRQLQDIERRLDALELRGVELEKRLRAAE-----------GDDAEDSLMVDwfwLIHEkqlllrqeselmYKSKAQR 806
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEAEalleagkcpecGQPVEGSPHVE---TIEE------------DRERVEE 479
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33667117  807 LEEQQLDIEGELRRLMAKPEALKSLQERRREQELLEQYVSTVNDR-SDIVDSLDEDRLREQEedqmLRDMIEKL 879
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELiAERRETIEEKRERAEE----LRERAAEL 549
dnaA PRK14086
chromosomal replication initiator protein DnaA;
295-504 2.15e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 41.73  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  295 PARASVPAAPNPAATSATSVHVRSPARPSESRLAPTPTEGKVRPRVTNSSPMgwssaapctaaaashPAVPPSAPDPRPA 374
Cdd:PRK14086  81 PIRIAITVDPSAGEPAPPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPG---------------LPRQDQLPTARPA 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  375 TPQ------GGGAPRVAAPQTTLSSSSTSAATVDPPAWTPSASRTQQARNKFFQTSAVPPGTSLSGRGPTPSlvLSKDSS 448
Cdd:PRK14086 146 YPAyqqrpePGAWPRAADDYGWQQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPD--WDRPRR 223
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 33667117  449 KEQARNFLKQALSALEEAGAPAPGRPSPATAAVPSSQPKTEAPQASPLAKPLQSSS 504
Cdd:PRK14086 224 DRTDRPEPPPGAGHVHRGGPGPPERDDAPVVPIRPSAPGPLAAQPAPAPGPGEPTA 279
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
737-878 2.40e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 2.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117 737 PEEIQR--QLQDIERRLDALELRGVELEKRLRAAEG----------------DDAEDSlmvdwfwlIHEKQLLLRQESEL 798
Cdd:COG1579   3 PEDLRAllDLQELDSELDRLEHRLKELPAELAELEDelaalearleaaktelEDLEKE--------IKRLELEIEEVEAR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117 799 MYKSKAQ------------------RLEEQQLDIEGELRRLMAKPEALKSLQERRREQ--ELLEQYVSTVNDRSDIVDSL 858
Cdd:COG1579  75 IKKYEEQlgnvrnnkeyealqkeieSLKRRISDLEDEILELMERIEELEEELAELEAElaELEAELEEKKAELDEELAEL 154
                       170       180
                ....*....|....*....|
gi 33667117 859 DEDRLREQEEDQMLRDMIEK 878
Cdd:COG1579 155 EAELEELEAEREELAAKIPP 174
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
245-342 2.52e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 41.68  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  245 AASASPKLTGLVPRQPGAMGVDSrtscSPQKAQEANKARPSAWEPA---AGNSPARASVPAAPNPAATSATSVHVRSPAR 321
Cdd:PRK14971 376 KQHIKPVFTQPAAAPQPSAAAAA----SPSPSQSSAAAQPSAPQSAtqpAGTPPTVSVDPPAAVPVNPPSTAPQAVRPAQ 451
                         90       100
                 ....*....|....*....|.
gi 33667117  322 PSESRLAPTPTEGKVRPRVTN 342
Cdd:PRK14971 452 FKEEKKIPVSKVSSLGPSTLR 472
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
283-519 2.91e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 41.37  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  283 RPSAWEPAA-GNSPARASVPAAPNPAATSATSVHVRSPARPSESRLAPTPTEGKVRPRVTNSSPMgwssaapctaaaash 361
Cdd:PRK07003 354 RMLAFEPAVtGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAA--------------- 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  362 PAVPPSAPDPRPATPQGGG-APRVAAPQTTLSSSSTSAATVDPPAWTPSASRTQQARNKFFQTSAVPPGTSLSGRgpTPS 440
Cdd:PRK07003 419 AATRAEAPPAAPAPPATADrGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPA--PRA 496
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33667117  441 LVLSKDSSKEQARNFLKQALSALEEAGAPAPGRPSPATAAVPSSQPKTEAPQASPLAKPLQSSSPRVLGLPSRMEPPAP 519
Cdd:PRK07003 497 AAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAGGAAAALDVLRNAGMRVSSDRGARAAAAA 575
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
410-762 3.36e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.21  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  410 ASRTQQARNKFFQTSAVPPGTSLSGRGPTPSLVLSKDSSKEQARNFLKQALSALEEAGAPAPGRPSPATAAVPSSQP--- 486
Cdd:PTZ00449 497 APIEEEDSDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPtls 576
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  487 -KTEAPQASPLAK----PLQSSSPRVLGLPSRmePPAPlstsstsqasalppagrrNLAESSGVGRvgagSRPKPEAPMA 561
Cdd:PTZ00449 577 kKPEFPKDPKHPKdpeePKKPKRPRSAQRPTR--PKSP------------------KLPELLDIPK----SPKRPESPKS 632
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  562 KGKSTTLTQDMSTSLQEGqedgPAGWRANLKPVDRRSPAERTLKPK----EPRALAEPRAGEAPRKVSGSFAGSVHITL- 636
Cdd:PTZ00449 633 PKRPPPPQRPSSPERPEG----PKIIKSPKPPKSPKPPFDPKFKEKfyddYLDAAAKSKETKTTVVLDESFESILKETLp 708
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  637 -TPVRPDRTPRPASPgpSLPARSPSPPRRRRLAVPASLDVCDNWLRP--------EPPGQEARVQSWKEEEKKPHLQGKP 707
Cdd:PTZ00449 709 eTPGTPFTTPRPLPP--KLPRDEEFPFEPIGDPDAEQPDDIEFFTPPeeertffhETPADTPLPDILAEEFKEEDIHAET 786
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 33667117  708 GRPLSPANVPALPGETVTSPVRLHPdylspeeiqrQLQDIERRLDALELRGVELE 762
Cdd:PTZ00449 787 GEPDEAMKRPDSPSEHEDKPPGDHP----------SLPKKRHRLDGLALSTTDLE 831
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
738-844 4.42e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 4.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117 738 EEIQRQLQDIERRLDALELRGVELEKRLRAAEGDDAEdslmvdwfwlihEKQLLLRQESELmyKSKAQRLEEQQLDIEGE 817
Cdd:COG1579  92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAE------------LEAELAELEAEL--EEKKAELDEELAELEAE 157
                        90       100
                ....*....|....*....|....*...
gi 33667117 818 LRRLMAKPEAL-KSLqerrrEQELLEQY 844
Cdd:COG1579 158 LEELEAEREELaAKI-----PPELLALY 180
PHA03379 PHA03379
EBNA-3A; Provisional
266-519 4.56e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 40.81  E-value: 4.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  266 DSRTSCSPQKAQEANKARPsaWEPAAGNSPARA-------SVPAAPNPAATSATSVHVR---------SPARPSESR--- 326
Cdd:PHA03379 490 DGRPACAPVPAPAGPIVRP--WEASLSQVPGVAfapvmpqPMPVEPVPVPTVALERPVCpappliamqGPGETSGIVrvr 567
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  327 -------LAPTPTEG----KVRPRVTNSSPMGWSSAAPCTAAAASHPAVPPSAPDPRPATPQGGGAPRVAAPQTTLSSSS 395
Cdd:PHA03379 568 erwrpapWTPNPPRSpsqmSVRDRLARLRAEAQPYQASVEVQPPQLTQVSPQQPMEYPLEPEQQMFPGSPFSQVADVMRA 647
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  396 TSAATVDPPAWTPSASRTQQARnkffqTSAVPPGTSLSGRGPTPSLVLSK-DSSKEQARNFLKQALSALEEAGAPAPGRP 474
Cdd:PHA03379 648 GGVPAMQPQYFDLPLQQPISQG-----APLAPLRASMGPVPPVPATQPQYfDIPLTEPINQGASAAHFLPQQPMEGPLVP 722
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 33667117  475 S----PATAAVPSSQPKTEAPQA--SPLAKPLQSSSPRVLGLPsrmEPPAP 519
Cdd:PHA03379 723 ErwmfQGATLSQSVRPGVAQSQYfdLPLTQPINHGAPAAHFLH---QPPME 770
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
738-880 4.70e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 4.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117 738 EEIQRQLQDIERRLDALELRGVELEKRLRAAEGDDAEDSLMVdwfwlihEKQLLLRQESELMYKSKAQRLEEQQLDIEGE 817
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL-------AEEELELEEALLAEEEEERELAEAEEERLEE 719
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33667117 818 LRRLMAKPEALKSLQERRREQELLEQYVSTVNDRSDIVDSLDEDRLREQEEDqmLRDMIEKLG 880
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER--LEREIEALG 780
LIM_LASP cd09447
The LIM domain of LIM and SH3 Protein (LASP); The LIM domain of LIM and SH3 Protein (LASP): ...
188-228 5.05e-03

The LIM domain of LIM and SH3 Protein (LASP); The LIM domain of LIM and SH3 Protein (LASP): LASP family contains two highly homologous members, LASP-1 and LASP-2. LASP contains a LIM motif at its amino terminus, a src homology 3 (SH3) domains at its C-terminal part, and a nebulin-like region in the middle. LASP-1 and -2 are highly conserved in their LIM, nebulin-like, and SH3 domains ,but differ significantly at their linker regions. Both proteins are ubiquitously expressed and involved in cytoskeletal architecture, especially in the organization of focal adhesions. LASP-1 and LASP-2, are important during early embryo- and fetogenesis and are highly expressed in the central nervous system of the adult. However, only LASP-1 seems to participate significantly in neuronal differentiation and plays an important functional role in migration and proliferation of certain cancer cells while the role of LASP-2 is more structural. The expression of LASP-1 in breast tumors is increased significantly. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188831  Cd Length: 53  Bit Score: 35.81  E-value: 5.05e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 33667117 188 CGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYK 228
Cdd:cd09447   1 CARCGKTVYPTEKLNCLDKIWHKGCFKCEVCGMTLNMKNYK 41
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
738-882 5.07e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 5.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  738 EEIQRQLQDIERRLDALElRGVELEKRLRAAEGD----DAEDSLMVDWFwlihekqllLRQESELmykskaqrLEEQQLD 813
Cdd:COG4913  238 ERAHEALEDAREQIELLE-PIRELAERYAAARERlaelEYLRAALRLWF---------AQRRLEL--------LEAELEE 299
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33667117  814 IEGELRRLMAKPEALKSLQE--RRREQELLEQYVSTVNDRsdiVDSLD------EDRLREQEED-QMLRDMIEKLGLQ 882
Cdd:COG4913  300 LRAELARLEAELERLEARLDalREELDELEAQIRGNGGDR---LEQLEreierlERELEERERRrARLEALLAALGLP 374
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
738-879 5.24e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 5.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117    738 EEIQRQLQDIERRLDALELRGVELEKRLRAAEG-----------------------DDAEDSLMVDWFWLIHEKQLLLRQ 794
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKelyalaneisrleqqkqilrerlANLERQLEELEAQLEELESKLDEL 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117    795 ESEL-MYKSKAQRLEEQQLDIEGELRRLMAKPEALKSLQERRREQelLEQYVSTVNDRSDIVDSLDEDRLREQEEDQMLR 873
Cdd:TIGR02168  336 AEELaELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ--LETLRSKVAQLELQIASLNNEIERLEARLERLE 413

                   ....*.
gi 33667117    874 DMIEKL 879
Cdd:TIGR02168  414 DRRERL 419
LIM2_Lhx7_Lhx8 cd09383
The second LIM domain of Lhx7 and Lhx8; The second LIM domain of Lhx7 and Lhx8: Lhx7 and Lhx8 ...
188-225 6.53e-03

The second LIM domain of Lhx7 and Lhx8; The second LIM domain of Lhx7 and Lhx8: Lhx7 and Lhx8 belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs such as the pituitary gland and the pancreas. Studies using mutant mice have revealed roles for Lhx7 and Lhx8 in the development of cholinergic neurons in the telencephalon and in basal forebrain development. Mice lacking alleles of the LIM-homeobox gene Lhx7 or Lhx8 display dramatically reduced number of forebrain cholinergic neurons. In addition, Lhx7 mutation affects male and female mice differently, with females appearing more affected than males. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188769  Cd Length: 55  Bit Score: 35.78  E-value: 6.53e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 33667117 188 CGVCGKHVH---LVQRhlADGRLYHRSCFRCKQCSCTLHSG 225
Cdd:cd09383   1 CSRCGRHIHstdWVRR--AKGNVYHLACFACFSCKRQLSTG 39
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
259-405 6.70e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 6.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  259 QPGAMGVDSRTSCSPQKAQEANKARPSAWEPAAGNSPARASV-PAAPNPAATSATSVHVRSPARPSESRLAPTP--TEGK 335
Cdd:PRK07764 632 AAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAgGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPaaTPPA 711
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  336 VRPRVTNSSPMGWSSAAPCTAAAASHPAVPPSAPDPRPATPQGGGAPRVAAPQTTLSSSSTSAATVDPPA 405
Cdd:PRK07764 712 GQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSE 781
COG5373 COG5373
Uncharacterized membrane protein [Function unknown];
450-519 7.22e-03

Uncharacterized membrane protein [Function unknown];


Pssm-ID: 444140 [Multi-domain]  Cd Length: 854  Bit Score: 39.98  E-value: 7.22e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117 450 EQARNFLKQALSALEEAGAPAPGRPSPATAAVPSSQPKTEAPQASPLAKPLQSSSPRVLGLPSRMEPPAP 519
Cdd:COG5373  31 EELEAELAEAAEAASAPAEPEPEAAAAATAAAPEAAPAPVPEAPAAPPAAAEAPAPAAAAPPAEAEPAAA 100
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
738-891 8.20e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 8.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117    738 EEIQRQLQDIERRLdalelrgVELEKRLRAAEGDdaedslmvdwfwlIHEKQLLLRQESELMykskaQRLEEQQLDIegE 817
Cdd:TIGR02169  794 PEIQAELSKLEEEV-------SRIEARLREIEQK-------------LNRLTLEKEYLEKEI-----QELQEQRIDL--K 846
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33667117    818 LRRLMAKpEALKSLQERRRE-QELLEQYVSTVNDRSDIVDSLDEDRLREQEEDQMLRDMIEKLGLQRKKSKFRLS 891
Cdd:TIGR02169  847 EQIKSIE-KEIENLNGKKEElEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
224-387 8.72e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.83  E-value: 8.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  224 SGAYKATGEPGTFVCTSHLPAAASASPKLTGLVPRQPGAMGVDSRTSCSPQKAQEANKARPSAWEPAAGNSPAR--ASVP 301
Cdd:PRK07003 377 AGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPakANAR 456
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  302 AAPNPAATSATSvhvrSPARPSESRLAPTPTegkVRPRVTNSSPMGWSSAAPCTAAAASHPAVPPSAPDPRPATPQGGGA 381
Cdd:PRK07003 457 ASADSRCDERDA----QPPADSGSASAPASD---APPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPA 529

                 ....*.
gi 33667117  382 PRVAAP 387
Cdd:PRK07003 530 PEARPP 535
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
241-650 9.30e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 39.67  E-value: 9.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  241 HLPAAASASPKLTGlvprQPGAMGVDSRTScSPQKAQEANKA-------RPSAwePAAGNSPARASVPAAPNPAATSATS 313
Cdd:PTZ00449 534 HEDSKESDEPKEGG----KPGETKEGEVGK-KPGPAKEHKPSkiptlskKPEF--PKDPKHPKDPEEPKKPKRPRSAQRP 606
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  314 VHVRSPARPSESRLAPTPTegkvRPRVTNSspmgwssaapctaaaashPAVPPSAPDP-RPATPQGGGAPRVAAPqttls 392
Cdd:PTZ00449 607 TRPKSPKLPELLDIPKSPK----RPESPKS------------------PKRPPPPQRPsSPERPEGPKIIKSPKP----- 659
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  393 sSSTSAATVDPP-------AWTPSASRTQQARNKFF----------QTSAVPPGTSLSGRGPTPSlVLSKDSSkeqarnf 455
Cdd:PTZ00449 660 -PKSPKPPFDPKfkekfydDYLDAAAKSKETKTTVVldesfesilkETLPETPGTPFTTPRPLPP-KLPRDEE------- 730
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  456 lkqalSALEEAGAPAPGRPSPATAAVPSSQPKT---EAPQASPLAKPLQSSSPRVLGLPSRMEPPAPLSTSSTSQASALP 532
Cdd:PTZ00449 731 -----FPFEPIGDPDAEQPDDIEFFTPPEEERTffhETPADTPLPDILAEEFKEEDIHAETGEPDEAMKRPDSPSEHEDK 805
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667117  533 PAG-------RRNLAESSGVGRVGAGSRPKPEAPMAKGKSTTLTQDMS----TSLQEGQEDGPAGWRANLKPVDRRSPAE 601
Cdd:PTZ00449 806 PPGdhpslpkKRHRLDGLALSTTDLESDAGRIAKDASGKIVKLKRSKSfddlTTVEEAEEMGAEARKIVVDDDGTEADDE 885
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 33667117  602 RTLKPKEpRALAEPRAGEAPRKVSgsfagsvhitlTPVRPDRTPRPASP 650
Cdd:PTZ00449 886 DTHPPEE-KHKSEVRRRRPPKKPS-----------KPKKPSKPKKPKKP 922
 
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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