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Conserved domains on  [gi|1973428429|ref|NP_001178014|]
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F-actin-monooxygenase MICAL3 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
515-625 1.64e-78

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: 254.49  E-value: 1.64e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  515 NESVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISP 594
Cdd:cd21251      1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1973428429  595 IMTGKEMASVGEPDKLSMVMYLTQFYEMFKD 625
Cdd:cd21251     81 IMTGKEMASVGEPDKLSMVMYLTQFYEMFKD 111
bMERB_dom pfam12130
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
1852-1983 2.96e-60

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: 202.74  E-value: 2.96e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1852 QLEQVEEKQRQLEERGVAVEKALRGEAGmGKKDDPKLMQEWFKLVQEKNAMVRYESELMIFARELELEDRQSRLQQELRE 1931
Cdd:pfam12130    1 ELEEIEERQRELEERGVELEKALRGEMS-GDEEEEQLLQEWFKLVNEKNALVRRESELMYLAKEQDLEERQARLEQELRE 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1973428429 1932 RMAVEDHLKTEEELSEEKKILNEMLEVVEQRDSLVALLEEQRLREKEEDKDL 1983
Cdd:pfam12130   80 LMSKPDWLKTEEDKQREEELLEELVEIVEQRDALVDSLEEDRLREEEEDEEL 131
LIM_Mical cd09439
The LIM domain of Mical (molecule interacting with CasL); The LIM domain of Mical (molecule ...
764-818 6.02e-38

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: 136.27  E-value: 6.02e-38
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAYDIEDGKFYCKPHY 818
Cdd:cd09439      1 CYFCKKRVYVMERLSAEGLFFHRSCFKCSYCGTTLRLGAYAFDRDDGKFYCKPHF 55
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
85-226 6.34e-10

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


:

Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 63.03  E-value: 6.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429   85 TNTKCLIIGAGPCGLRTAIDLSLLGAKVVVIEKRDAFSRNN-VLHLWPFTIHDLRGLGAK-------------KFYGKFC 150
Cdd:COG0654      2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGrGIALSPRSLELLRRLGLWdrllargapirgiRVRDGSD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  151 AGAIDHISI-------------RQLQLILLKVALILGIEIHVNVEFQGLVQPPEdqeneriGWRALVHPKThpvsEYEFE 217
Cdd:COG0654     82 GRVLARFDAaetglpaglvvprADLERALLEAARALGVELRFGTEVTGLEQDAD-------GVTVTLADGR----TLRAD 150

                   ....*....
gi 1973428429  218 VIIGGDGRR 226
Cdd:COG0654    151 LVVGADGAR 159
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1114-1507 4.90e-07

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.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 54.92  E-value: 4.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1114 LQSQTKVKADLELRVSENEEEKPSDTPKQEERGPSQVSSPSQPpqkqavlfSPAHSPGAEEAKPPP-ASITTKVKSPAEE 1192
Cdd:pfam05109  448 LPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTP--------SPSPRDNGTESKAPDmTSPTSAVTTPTPN 519
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1193 PLFPAPLLLREKPKAEGPEEQKTvhSPIRSQPVALPEARSPTSPTSSLQPESLLAPptpptppstqlpiCSQPQPSSDAS 1272
Cdd:pfam05109  520 ATSPTPAVTTPTPNATSPTLGKT--SPTSAVTTPTPNATSPTPAVTTPTPNATIPT-------------LGKTSPTSAVT 584
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1273 IPSP-TKSPIRFQPVP----------AKTSTPLTPLPvksqgdPKDRLSGPLAVEEALKRSDlVEEFWMKSAEIRRSLGL 1341
Cdd:pfam05109  585 TPTPnATSPTVGETSPqanttnhtlgGTSSTPVVTSP------PKNATSAVTTGQHNITSSS-TSSMSLRPSSISETLSP 657
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1342 TPVDRNKGSEPSLPSP---------ALKPISLKSYSVDKSPQDEglcllKPPSVPKRLGLPKSAGDQPP-------LLTP 1405
Cdd:pfam05109  658 STSDNSTSHMPLLTSAhptggenitQVTPASTSTHHVSTSSPAP-----RPGTTSQASGPGNSSTSTKPgevnvtkGTPP 732
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1406 KSPSDKELRSNQEERRDLSSSSGLGLHGSSSNMKTLGSQSFNTSDSTMLTPPSSPPPPPPPNEE----PATLRR-KPRQT 1480
Cdd:pfam05109  733 KNATSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATtylpPSTSSKlRPRWT 812
                          410       420
                   ....*....|....*....|....*..
gi 1973428429 1481 FERreasviPPPTPASFMRPPREAAQP 1507
Cdd:pfam05109  813 FTS------PPVTTAQATVPVPPTSQP 833
 
Name Accession Description Interval E-value
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
515-625 1.64e-78

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: 254.49  E-value: 1.64e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  515 NESVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISP 594
Cdd:cd21251      1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1973428429  595 IMTGKEMASVGEPDKLSMVMYLTQFYEMFKD 625
Cdd:cd21251     81 IMTGKEMASVGEPDKLSMVMYLTQFYEMFKD 111
bMERB_dom pfam12130
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
1852-1983 2.96e-60

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: 202.74  E-value: 2.96e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1852 QLEQVEEKQRQLEERGVAVEKALRGEAGmGKKDDPKLMQEWFKLVQEKNAMVRYESELMIFARELELEDRQSRLQQELRE 1931
Cdd:pfam12130    1 ELEEIEERQRELEERGVELEKALRGEMS-GDEEEEQLLQEWFKLVNEKNALVRRESELMYLAKEQDLEERQARLEQELRE 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1973428429 1932 RMAVEDHLKTEEELSEEKKILNEMLEVVEQRDSLVALLEEQRLREKEEDKDL 1983
Cdd:pfam12130   80 LMSKPDWLKTEEDKQREEELLEELVEIVEQRDALVDSLEEDRLREEEEDEEL 131
LIM_Mical cd09439
The LIM domain of Mical (molecule interacting with CasL); The LIM domain of Mical (molecule ...
764-818 6.02e-38

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: 136.27  E-value: 6.02e-38
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAYDIEDGKFYCKPHY 818
Cdd:cd09439      1 CYFCKKRVYVMERLSAEGLFFHRSCFKCSYCGTTLRLGAYAFDRDDGKFYCKPHF 55
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
524-624 4.40e-23

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: 95.82  E-value: 4.40e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGY-SGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSL--DEQNVEQNNQLAFDIAEKELGISPI-MTGK 599
Cdd:pfam00307    7 LLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnkSEFDKLENINLALDVAEKKLGVPKVlIEPE 86
                           90       100
                   ....*....|....*....|....*
gi 1973428429  600 EMAsvgEPDKLSMVMYLTQFYEMFK 624
Cdd:pfam00307   87 DLV---EGDNKSVLTYLASLFRRFQ 108
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
503-623 3.39e-20

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 97.32  E-value: 3.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  503 LVNSRTTPKLTRNESVARSSKLLGWCQRQTDGY-SGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQ--NVEQNN 579
Cdd:COG5069    109 LISRLTIATINEEGELTKHINLLLWCDEDTGGYkPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkkNKALNN 188
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1973428429  580 QLAFDIAEKELGISPIMTGKEMASVGEPDKLSMVMYLTQFYEMF 623
Cdd:COG5069    189 FQAFENANKVIGIARLIGVEDIVNVSIPDERSIMTYVSWYIIRF 232
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
524-619 4.77e-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: 78.13  E-value: 4.77e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429   524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVE----QNNQLAFDIAEKELGISPIMTGK 599
Cdd:smart00033    3 LLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVVLFEPE 82
                            90       100
                    ....*....|....*....|
gi 1973428429   600 EMASvGEPDKLSMVMYLTQF 619
Cdd:smart00033   83 DLVE-GPKLILGVIWTLISL 101
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
85-226 6.34e-10

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 63.03  E-value: 6.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429   85 TNTKCLIIGAGPCGLRTAIDLSLLGAKVVVIEKRDAFSRNN-VLHLWPFTIHDLRGLGAK-------------KFYGKFC 150
Cdd:COG0654      2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGrGIALSPRSLELLRRLGLWdrllargapirgiRVRDGSD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  151 AGAIDHISI-------------RQLQLILLKVALILGIEIHVNVEFQGLVQPPEdqeneriGWRALVHPKThpvsEYEFE 217
Cdd:COG0654     82 GRVLARFDAaetglpaglvvprADLERALLEAARALGVELRFGTEVTGLEQDAD-------GVTVTLADGR----TLRAD 150

                   ....*....
gi 1973428429  218 VIIGGDGRR 226
Cdd:COG0654    151 LVVGADGAR 159
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
764-817 1.13e-09

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: 55.85  E-value: 1.13e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429   764 CYFCQKRVYVMER-LSAEGKFFHRSCFKCDYCATTLRLSAYAydIEDGKFYCKPH 817
Cdd:smart00132    2 CAGCGKPIYGTERvLRALGKVWHPECFKCATCGKPLSGDTFF--EKDGKLYCKDC 54
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
764-819 2.07e-09

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


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 55.03  E-value: 2.07e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAydIEDGKFYCKPHYC 819
Cdd:pfam00412    1 CAGCNRPIYDRELVRALGKVWHPECFRCAVCGKPLTTGDFY--EKDGKLYCKHDYY 54
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1114-1507 4.90e-07

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: 54.92  E-value: 4.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1114 LQSQTKVKADLELRVSENEEEKPSDTPKQEERGPSQVSSPSQPpqkqavlfSPAHSPGAEEAKPPP-ASITTKVKSPAEE 1192
Cdd:pfam05109  448 LPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTP--------SPSPRDNGTESKAPDmTSPTSAVTTPTPN 519
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1193 PLFPAPLLLREKPKAEGPEEQKTvhSPIRSQPVALPEARSPTSPTSSLQPESLLAPptpptppstqlpiCSQPQPSSDAS 1272
Cdd:pfam05109  520 ATSPTPAVTTPTPNATSPTLGKT--SPTSAVTTPTPNATSPTPAVTTPTPNATIPT-------------LGKTSPTSAVT 584
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1273 IPSP-TKSPIRFQPVP----------AKTSTPLTPLPvksqgdPKDRLSGPLAVEEALKRSDlVEEFWMKSAEIRRSLGL 1341
Cdd:pfam05109  585 TPTPnATSPTVGETSPqanttnhtlgGTSSTPVVTSP------PKNATSAVTTGQHNITSSS-TSSMSLRPSSISETLSP 657
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1342 TPVDRNKGSEPSLPSP---------ALKPISLKSYSVDKSPQDEglcllKPPSVPKRLGLPKSAGDQPP-------LLTP 1405
Cdd:pfam05109  658 STSDNSTSHMPLLTSAhptggenitQVTPASTSTHHVSTSSPAP-----RPGTTSQASGPGNSSTSTKPgevnvtkGTPP 732
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1406 KSPSDKELRSNQEERRDLSSSSGLGLHGSSSNMKTLGSQSFNTSDSTMLTPPSSPPPPPPPNEE----PATLRR-KPRQT 1480
Cdd:pfam05109  733 KNATSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATtylpPSTSSKlRPRWT 812
                          410       420
                   ....*....|....*....|....*..
gi 1973428429 1481 FERreasviPPPTPASFMRPPREAAQP 1507
Cdd:pfam05109  813 FTS------PPVTTAQATVPVPPTSQP 833
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1822-1986 5.03e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 5.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1822 KLTRRVQKAARRQAKQEELKRLHRA-----------------QIIQRQLEQVEEKQRQLEERGVAVEkALRGEAGMGKKD 1884
Cdd:TIGR02168  204 SLERQAEKAERYKELKAELRELELAllvlrleelreeleelqEELKEAEEELEELTAELQELEEKLE-ELRLEVSELEEE 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1885 DPKLMQEWFKLVQEKNAMvryESELMIFARELE-LEDRQSRLQQELRERMAVEDHLKTEEELSEEKK--ILNEMLEVVEQ 1961
Cdd:TIGR02168  283 IEELQKELYALANEISRL---EQQKQILRERLAnLERQLEELEAQLEELESKLDELAEELAELEEKLeeLKEELESLEAE 359
                          170       180
                   ....*....|....*....|....*
gi 1973428429 1962 RDSLVALLEEQRLREKEEDKDLEAA 1986
Cdd:TIGR02168  360 LEELEAELEELESRLEELEEQLETL 384
PHA03247 PHA03247
large tegument protein UL36; Provisional
1147-1408 3.91e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 3.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1147 PSQVSSPSQPPQKQAVlfSPAHSPGAEEAKPPPASITTKVKSPAEEPLFPAPLLLREKPKAEGPEEQKTVHSPIRSQPVA 1226
Cdd:PHA03247  2673 AAQASSPPQRPRRRAA--RPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT 2750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1227 LPEARSPTSPTSSLQPESLLAPPTPP----------TPPSTQLPICSQPQPSSDASIPSPTKSPIRFQPVPAKTSTPLTP 1296
Cdd:PHA03247  2751 PGGPARPARPPTTAGPPAPAPPAAPAagpprrltrpAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1297 lPVKSQGDPKDRLSGPLAVEEALkrsdlveEFWMKSAeirrslglTPVDRNKGSEPSLPSPALKP----ISLKSYSVDKS 1372
Cdd:PHA03247  2831 -PTSAQPTAPPPPPGPPPPSLPL-------GGSVAPG--------GDVRRRPPSRSPAAKPAAPArppvRRLARPAVSRS 2894
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1973428429 1373 PQDEGLcllkPPSVPKRLGLPKSAgdQPPLLTPKSP 1408
Cdd:PHA03247  2895 TESFAL----PPDQPERPPQPQAP--PPPQPQPQPP 2924
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
87-274 1.00e-05

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 50.02  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429   87 TKCLIIGAGPCGLRTAIDLSLLGAKVVVIEKRDAF---SRNNVLHlwPFTIHDLRGLG---------------AKKFYGK 148
Cdd:pfam01494    2 TDVLIVGGGPAGLMLALLLARAGVRVVLVERHATTsvlPRAHGLN--QRTMELLRQAGledrilaegvphegmGLAFYNT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  149 FCAGAIDHIS-------IRQLQL--ILLKVALILGIEIHVNVEFQGLVQppeDQENERIgwRALVHpKTHPVSEYEFEVI 219
Cdd:pfam01494   80 RRRADLDFLTspprvtvYPQTELepILVEHAEARGAQVRFGTEVLSLEQ---DGDGVTA--VVRDR-RDGEEYTVRAKYL 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1973428429  220 IGGDGRRNTLE---GFRRKEFRGKLAIAITANFINRNTTaeAKVEEISGVAFIFNQKF 274
Cdd:pfam01494  154 VGCDGGRSPVRktlGIEFEGFEGVPFGSLDVLFDAPDLS--DPVERAFVHYLIYAPHS 209
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1816-1986 1.07e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1816 EEELSAKLTRRVQKAARRQAKQEELKRLH-RAQIIQRQLEQVEEKQ-RQLEERGVAVEKALrgeagmgkkddpklmQEWF 1893
Cdd:COG1196    322 EEELAELEEELEELEEELEELEEELEEAEeELEEAEAELAEAEEALlEAEAELAEAEEELE---------------ELAE 386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1894 KLVQEKNAMVRYESELMIFARELE-LEDRQSRLQQELRERMAVEDHLKTEEE------LSEEKKILNEMLEVVEQRDSLV 1966
Cdd:COG1196    387 ELLEALRAAAELAAQLEELEEAEEaLLERLERLEEELEELEEALAELEEEEEeeeealEEAAEEEAELEEEEEALLELLA 466
                          170       180
                   ....*....|....*....|
gi 1973428429 1967 ALLEEQRLREKEEDKDLEAA 1986
Cdd:COG1196    467 ELLEEAALLEAALAELLEEL 486
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1119-1399 1.57e-05

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 49.77  E-value: 1.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1119 KVKADLELRVSENEEEKPSDTPKQEERGPSQVSSPSQPPQKQavlfspahsPGAEEAKPPPASITTKVKSPAEEPLfPAP 1198
Cdd:NF033839   263 KIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQ---------PEKKEVKPEPETPKPEVKPQLEKPK-PEV 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1199 LLLREKPKAEGPEEQKTVHSPIRSQPVA-LPEAR-SPTSPTSSLQPESLLAPPTPPTPPstqlpicSQPQPSSDasiPSP 1276
Cdd:NF033839   333 KPQPEKPKPEVKPQLETPKPEVKPQPEKpKPEVKpQPEKPKPEVKPQPETPKPEVKPQP-------EKPKPEVK---PQP 402
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1277 TKSPIRFQPVPAKTSTPLTPLPVKSQGDPKDRLSGPlaveealkRSDLVEEFWMKSAEIRRSLGlTPvDRNKGSEPSLPS 1356
Cdd:NF033839   403 EKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKP--------KPEVKPQPEKPKPEVKPQPE-TP-KPEVKPQPEKPK 472
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1973428429 1357 PALKPISLKSYSVDKSPQDEGlcllKPPSVPKRLGLPKSAGDQ 1399
Cdd:NF033839   473 PEVKPQPEKPKPDNSKPQADD----KKPSTPNNLSKDKQPSNQ 511
PTZ00121 PTZ00121
MAEBL; Provisional
1800-1985 3.78e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 3.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1800 LERSSQKSKREPRTYTEEELSAKLTRRVQ--KAARRQAKQEELKRlhraqiiQRQLEQVEEKQRQLEERGVAVEKAlrge 1877
Cdd:PTZ00121  1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEekKKADELKKAEELKK-------AEEKKKAEEAKKAEEDKNMALRKA---- 1583
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1878 aGMGKKDDPKLMQEWFKLVQEKNAM----VRYESELMIFARELELEDRQSRLQQELRERMAVE----DHLKTEEELSEEK 1949
Cdd:PTZ00121  1584 -EEAKKAEEARIEEVMKLYEEEKKMkaeeAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkkaEELKKAEEENKIK 1662
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1973428429 1950 KILNEMLEVVEQRDSLVALLEEQRLREKEEDKDLEA 1985
Cdd:PTZ00121  1663 AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
PRK08244 PRK08244
monooxygenase;
86-143 9.12e-05

monooxygenase;


Pssm-ID: 236199 [Multi-domain]  Cd Length: 493  Bit Score: 47.43  E-value: 9.12e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1973428429   86 NTKCLIIGAGPCGLRTAIDLSLLGAKVVVIEKRDA---FSRNNVLHLWPFTIHDLRGLGAK 143
Cdd:PRK08244     2 KYEVIIIGGGPVGLMLASELALAGVKTCVIERLKEtvpYSKALTLHPRTLEILDMRGLLER 62
Bthiol_YpdA TIGR04018
putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, ...
88-117 1.39e-03

putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, including YpdA from Bacillus subtilis, are apparent oxidoreductases present only in species with an active bacillithiol system. They have been suggested actually to be thiol disulfide oxidoreductases (TDOR), although the evidence is incomplete. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 188533 [Multi-domain]  Cd Length: 316  Bit Score: 42.94  E-value: 1.39e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1973428429   88 KCLIIGAGPCGLRTAIDLSLLGAKVVVIEK 117
Cdd:TIGR04018    1 DVIIIGAGPCGLACAIEAQKAGLSYLIIEK 30
 
Name Accession Description Interval E-value
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
515-625 1.64e-78

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: 254.49  E-value: 1.64e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  515 NESVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISP 594
Cdd:cd21251      1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1973428429  595 IMTGKEMASVGEPDKLSMVMYLTQFYEMFKD 625
Cdd:cd21251     81 IMTGKEMASVGEPDKLSMVMYLTQFYEMFKD 111
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
516-625 1.47e-74

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: 243.02  E-value: 1.47e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  516 ESVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPI 595
Cdd:cd21195      1 SGDIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPV 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1973428429  596 MTGKEMASVGEPDKLSMVMYLTQFYEMFKD 625
Cdd:cd21195     81 TTGKEMASAQEPDKLSMVMYLSKFYELFRG 110
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
520-624 9.12e-68

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: 223.32  E-value: 9.12e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  520 RSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGK 599
Cdd:cd22198      1 RPEELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQ 80
                           90       100
                   ....*....|....*....|....*
gi 1973428429  600 EMASVGEPDKLSMVMYLTQFYEMFK 624
Cdd:cd22198     81 EMASLAVPDKLSMVSYLSQFYEAFK 105
bMERB_dom pfam12130
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
1852-1983 2.96e-60

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: 202.74  E-value: 2.96e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1852 QLEQVEEKQRQLEERGVAVEKALRGEAGmGKKDDPKLMQEWFKLVQEKNAMVRYESELMIFARELELEDRQSRLQQELRE 1931
Cdd:pfam12130    1 ELEEIEERQRELEERGVELEKALRGEMS-GDEEEEQLLQEWFKLVNEKNALVRRESELMYLAKEQDLEERQARLEQELRE 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1973428429 1932 RMAVEDHLKTEEELSEEKKILNEMLEVVEQRDSLVALLEEQRLREKEEDKDL 1983
Cdd:pfam12130   80 LMSKPDWLKTEEDKQREEELLEELVEIVEQRDALVDSLEEDRLREEEEDEEL 131
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
516-624 1.59e-58

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: 197.03  E-value: 1.59e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  516 ESVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPI 595
Cdd:cd21250      1 ESDIRPNKLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPV 80
                           90       100
                   ....*....|....*....|....*....
gi 1973428429  596 MTGKEMASVGEPDKLSMVMYLTQFYEMFK 624
Cdd:cd21250     81 TTGKEMASAEEPDKLSMVMYLSKFYELFR 109
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
524-624 5.62e-46

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: 160.98  E-value: 5.62e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMAS 603
Cdd:cd21253      6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDMVA 85
                           90       100
                   ....*....|....*....|.
gi 1973428429  604 VGEPDKLSMVMYLTQFYEMFK 624
Cdd:cd21253     86 LKVPDKLSILTYVSQYYNYFH 106
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
524-624 3.91e-42

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: 149.99  E-value: 3.91e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMAS 603
Cdd:cd21197      5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDMVT 84
                           90       100
                   ....*....|....*....|.
gi 1973428429  604 VGEPDKLSMVMYLTQFYEMFK 624
Cdd:cd21197     85 MHVPDRLSIITYVSQYYNHFR 105
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
521-623 2.89e-38

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: 139.10  E-value: 2.89e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  521 SSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKeLGISPIMTGKE 600
Cdd:cd21198      3 GQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDPAD 81
                           90       100
                   ....*....|....*....|...
gi 1973428429  601 MASVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21198     82 MVLLSVPDKLSVMTYLHQIRAHF 104
LIM_Mical cd09439
The LIM domain of Mical (molecule interacting with CasL); The LIM domain of Mical (molecule ...
764-818 6.02e-38

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: 136.27  E-value: 6.02e-38
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAYDIEDGKFYCKPHY 818
Cdd:cd09439      1 CYFCKKRVYVMERLSAEGLFFHRSCFKCSYCGTTLRLGAYAFDRDDGKFYCKPHF 55
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
524-626 1.87e-36

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: 133.84  E-value: 1.87e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMAS 603
Cdd:cd21252      5 LQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPEDMVS 84
                           90       100
                   ....*....|....*....|...
gi 1973428429  604 VGEPDKLSMVMYLTQFYEMFKDS 626
Cdd:cd21252     85 MKVPDCLSIMTYVSQYYNHFSNP 107
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
524-623 4.23e-36

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: 133.26  E-value: 4.23e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMAS 603
Cdd:cd21216     15 LLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKMLDAEDIVN 94
                           90       100
                   ....*....|....*....|
gi 1973428429  604 VGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21216     95 TPRPDERSVMTYVSCYYHAF 114
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
524-623 1.64e-34

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: 128.80  E-value: 1.64e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMAS 603
Cdd:cd21291     15 LLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGIPQLLDVEDVCD 94
                           90       100
                   ....*....|....*....|
gi 1973428429  604 VGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21291     95 VAKPDERSIMTYVAYYFHAF 114
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
520-623 3.50e-33

second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409043  Cd Length: 105  Bit Score: 124.45  E-value: 3.50e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  520 RSSK--LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMT 597
Cdd:cd21194      1 KSAKdaLLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 1973428429  598 GKEMAsVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21194     81 AEDVD-VARPDEKSIMTYVASYYHYF 105
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
521-623 2.74e-32

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: 121.88  E-value: 2.74e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  521 SSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKeLGISPIMTGKE 600
Cdd:cd21254      3 SQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEPSD 81
                           90       100
                   ....*....|....*....|...
gi 1973428429  601 MASVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21254     82 MVLLAVPDKLTVMTYLYQIRAHF 104
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
520-623 2.94e-32

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: 121.73  E-value: 2.94e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  520 RSSK--LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMT 597
Cdd:cd21248      1 RSAKdaLLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLD 80
                           90       100
                   ....*....|....*....|....*.
gi 1973428429  598 gKEMASVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21248     81 -PEDVNVEQPDEKSIITYVVTYYHYF 105
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
523-623 9.17e-31

second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409038  Cd Length: 105  Bit Score: 117.49  E-value: 9.17e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  523 KLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTgKEMA 602
Cdd:cd21189      5 ALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLD-PEDV 83
                           90       100
                   ....*....|....*....|.
gi 1973428429  603 SVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21189     84 DVPEPDEKSIITYVSSLYDVF 104
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
520-623 8.59e-30

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: 115.10  E-value: 8.59e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  520 RSSK--LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMT 597
Cdd:cd21319      4 RSAKdaLLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLD 83
                           90       100
                   ....*....|....*....|....*.
gi 1973428429  598 GKEMASvGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21319     84 PEDVFT-ENPDEKSIITYVVAFYHYF 108
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
520-623 3.21e-29

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


Pssm-ID: 409098  Cd Length: 109  Bit Score: 113.42  E-value: 3.21e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  520 RSSK--LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMT 597
Cdd:cd21249      3 RSAKeaLLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
                           90       100
                   ....*....|....*....|....*.
gi 1973428429  598 GKEMAsVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21249     83 PEDVA-VPHPDERSIMTYVSLYYHYF 107
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
521-623 3.81e-29

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: 112.96  E-value: 3.81e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  521 SSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEkELGISPIMTGKE 600
Cdd:cd21255      3 SQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFA-SLGVPRLLEPAD 81
                           90       100
                   ....*....|....*....|...
gi 1973428429  601 MASVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21255     82 MVLLPIPDKLIVMTYLCQLRAHF 104
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
524-621 6.72e-29

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: 112.14  E-value: 6.72e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMAs 603
Cdd:cd21187      5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDVN- 83
                           90
                   ....*....|....*...
gi 1973428429  604 VGEPDKLSMVMYLTQFYE 621
Cdd:cd21187     84 VEQPDKKSILMYVTSLFQ 101
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
516-623 4.14e-28

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


Pssm-ID: 409170  Cd Length: 119  Bit Score: 110.53  E-value: 4.14e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  516 ESVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPI 595
Cdd:cd21321      2 EKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTKL 81
                           90       100
                   ....*....|....*....|....*...
gi 1973428429  596 MTgKEMASVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21321     82 LD-PEDVNVDQPDEKSIITYVATYYHYF 108
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
524-624 7.05e-28

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: 109.76  E-value: 7.05e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKeLGISPIMTGKEMAS 603
Cdd:cd21199     13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAES-VGIPTTLTIDEMVS 91
                           90       100
                   ....*....|....*....|.
gi 1973428429  604 VGEPDKLSMVMYLTQFYEMFK 624
Cdd:cd21199     92 MERPDWQSVMSYVTAIYKHFE 112
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
524-624 1.25e-27

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: 108.66  E-value: 1.25e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMaS 603
Cdd:cd21192      8 LLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLEVEDV-L 86
                           90       100
                   ....*....|....*....|.
gi 1973428429  604 VGEPDKLSMVMYLTQFYEMFK 624
Cdd:cd21192     87 VDKPDERSIMTYVSQFLRMFP 107
LIM_Mical_like cd09358
The LIM domain of Mical (molecule interacting with CasL) like family; The LIM domain of Mical ...
764-818 2.36e-26

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: 103.12  E-value: 2.36e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAYdiEDGKFYCKPHY 818
Cdd:cd09358      1 CAVCGKTVYPMERLVADGKLFHKSCFRCSHCNKTLRLGNYAS--LEGKLYCKPHF 53
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
513-623 2.53e-25

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


Pssm-ID: 409171  Cd Length: 130  Bit Score: 103.21  E-value: 2.53e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  513 TRNESVARSSK--LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKEL 590
Cdd:cd21322      9 TEDNRETRSAKdaLLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHL 88
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1973428429  591 GISPIMTgKEMASVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21322     89 GLTKLLD-PEDVNMEAPDEKSIITYVVSFYHYF 120
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
524-623 4.94e-25

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: 101.33  E-value: 4.94e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMaS 603
Cdd:cd21320      7 LLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPEDI-S 85
                           90       100
                   ....*....|....*....|
gi 1973428429  604 VGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21320     86 VDHPDEKSIITYVVTYYHYF 105
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
522-619 5.83e-25

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: 100.77  E-value: 5.83e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  522 SKLLGWCQRQTDGYsgvNVTDLTMSWKSGLALCAIIHRYRPDLI-DFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKE 600
Cdd:cd21184      4 SLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLENATKAMDIAEEELGIPKIITPED 80
                           90
                   ....*....|....*....
gi 1973428429  601 MASvGEPDKLSMVMYLTQF 619
Cdd:cd21184     81 MVS-PNVDELSVMTYLSYF 98
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
517-624 9.35e-25

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: 100.50  E-value: 9.35e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  517 SVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIM 596
Cdd:cd21196      1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVV 80
                           90       100
                   ....*....|....*....|....*...
gi 1973428429  597 TGKemASVGEPDKLSMVMYLTQFYEMFK 624
Cdd:cd21196     81 SAQ--AVVAGSDPLGLIAYLSHFHSAFK 106
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
522-624 1.03e-24

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: 100.50  E-value: 1.03e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  522 SKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEM 601
Cdd:cd21200      4 QMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEVEDM 83
                           90       100
                   ....*....|....*....|....
gi 1973428429  602 ASVG-EPDKLSMVMYLTQFYEMFK 624
Cdd:cd21200     84 VRMGnRPDWKCVFTYVQSLYRHLR 107
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
512-624 7.23e-24

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: 98.18  E-value: 7.23e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  512 LTRNESVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEkELG 591
Cdd:cd21257      1 LAREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVG 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1973428429  592 ISPIMTGKEMASVGEPDKLSMVMYLTQFYEMFK 624
Cdd:cd21257     80 IKPSLELSEMMYTDRPDWQSVMQYVAQIYKYFE 112
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
516-623 1.00e-23

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: 98.22  E-value: 1.00e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  516 ESVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPI 595
Cdd:cd21288      7 EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKM 86
                           90       100
                   ....*....|....*....|....*...
gi 1973428429  596 MTGKEMASVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21288     87 LDAEDIVNTPKPDERAIMTYVSCFYHAF 114
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
516-623 2.25e-23

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


Pssm-ID: 409138  Cd Length: 124  Bit Score: 97.10  E-value: 2.25e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  516 ESVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPI 595
Cdd:cd21289      7 EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKM 86
                           90       100
                   ....*....|....*....|....*...
gi 1973428429  596 MTGKEMASVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21289     87 LDAEDIVNTPKPDEKAIMTYVSCFYHAF 114
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
516-623 3.55e-23

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: 96.69  E-value: 3.55e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  516 ESVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPI 595
Cdd:cd21287      7 EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKM 86
                           90       100
                   ....*....|....*....|....*...
gi 1973428429  596 MTGKEMASVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21287     87 LDAEDIVGTARPDEKAIMTYVSSFYHAF 114
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
524-624 4.40e-23

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: 95.82  E-value: 4.40e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGY-SGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSL--DEQNVEQNNQLAFDIAEKELGISPI-MTGK 599
Cdd:pfam00307    7 LLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLnkSEFDKLENINLALDVAEKKLGVPKVlIEPE 86
                           90       100
                   ....*....|....*....|....*
gi 1973428429  600 EMAsvgEPDKLSMVMYLTQFYEMFK 624
Cdd:pfam00307   87 DLV---EGDNKSVLTYLASLFRRFQ 108
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
516-627 2.18e-22

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


Pssm-ID: 409139  Cd Length: 125  Bit Score: 94.38  E-value: 2.18e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  516 ESVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPI 595
Cdd:cd21290     10 EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKM 89
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1973428429  596 MTGKEMASVGEPDKLSMVMYLTQFYEMFKDSL 627
Cdd:cd21290     90 LDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQ 121
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
524-623 3.03e-22

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: 93.54  E-value: 3.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGIsPIMTGKEMAS 603
Cdd:cd21243     10 LLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGI-PRLLDPEDVD 88
                           90       100
                   ....*....|....*....|
gi 1973428429  604 VGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21243     89 VDKPDEKSIMTYVAQFLKKY 108
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
524-623 8.42e-22

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


Pssm-ID: 409075  Cd Length: 103  Bit Score: 91.76  E-value: 8.42e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMAS 603
Cdd:cd21226      5 LLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDVMT 84
                           90       100
                   ....*....|....*....|
gi 1973428429  604 vGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21226     85 -GNPDERSIVLYTSLFYHAF 103
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
522-620 1.16e-21

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: 92.07  E-value: 1.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  522 SKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEM 601
Cdd:cd21260      4 NMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVEDM 83
                           90
                   ....*....|....*....
gi 1973428429  602 ASVGEPDKLSMVMYLTQFY 620
Cdd:cd21260     84 VRMSVPDSKCVYTYIQELY 102
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
524-624 6.80e-21

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: 89.51  E-value: 6.80e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGIsPIMTGKEMAS 603
Cdd:cd21244     10 LLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKI-PRLLEPEDVD 88
                           90       100
                   ....*....|....*....|.
gi 1973428429  604 VGEPDKLSMVMYLTQFYEMFK 624
Cdd:cd21244     89 VVNPDEKSIMTYVAQFLQYSK 109
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
523-623 2.81e-20

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: 87.73  E-value: 2.81e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  523 KLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKeLGISPIMTgKEMA 602
Cdd:cd21239      5 RLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLD-PEDV 82
                           90       100
                   ....*....|....*....|.
gi 1973428429  603 SVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21239     83 DVSSPDEKSVITYVSSLYDVF 103
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
512-624 3.04e-20

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: 88.21  E-value: 3.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  512 LTRNESVARSSKLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEkELG 591
Cdd:cd21256      7 LAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVG 85
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1973428429  592 ISPIMTGKEMASVGEPDKLSMVMYLTQFYEMFK 624
Cdd:cd21256     86 IKSTLDINEMVRTERPDWQSVMTYVTAIYKYFE 118
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
503-623 3.39e-20

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 97.32  E-value: 3.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  503 LVNSRTTPKLTRNESVARSSKLLGWCQRQTDGY-SGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQ--NVEQNN 579
Cdd:COG5069    109 LISRLTIATINEEGELTKHINLLLWCDEDTGGYkPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkkNKALNN 188
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1973428429  580 QLAFDIAEKELGISPIMTGKEMASVGEPDKLSMVMYLTQFYEMF 623
Cdd:COG5069    189 FQAFENANKVIGIARLIGVEDIVNVSIPDERSIMTYVSWYIIRF 232
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
523-623 3.76e-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: 87.40  E-value: 3.76e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  523 KLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKeLGISPIMTGKEMa 602
Cdd:cd21240      8 KLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLDAEDV- 85
                           90       100
                   ....*....|....*....|.
gi 1973428429  603 SVGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21240     86 DVPSPDEKSVITYVSSIYDAF 106
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
524-620 5.76e-20

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: 86.97  E-value: 5.76e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMAS 603
Cdd:cd21259      6 LLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVEDMVR 85
                           90
                   ....*....|....*..
gi 1973428429  604 VGEPDKLSMVMYLTQFY 620
Cdd:cd21259     86 MREPDWKCVYTYIQEFY 102
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
524-623 3.16e-19

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: 84.62  E-value: 3.16e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMAs 603
Cdd:cd21234      5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPEDVA- 83
                           90       100
                   ....*....|....*....|
gi 1973428429  604 VGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21234     84 VQLPDKKSIIMYLTSLFEVL 103
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
524-628 8.12e-19

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: 83.82  E-value: 8.12e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDS-LDEQNVEQNNQLAFDIAEKELGISPIMTGKEMA 602
Cdd:cd21233      5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSvVSQQSATERLDHAFNIARQHLGIEKLLDPEDVA 84
                           90       100
                   ....*....|....*....|....*.
gi 1973428429  603 SVgEPDKLSMVMYLTQFYEMFKDSLS 628
Cdd:cd21233     85 TA-HPDKKSILMYVTSLFQVLPQQVS 109
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
523-621 1.78e-18

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: 82.76  E-value: 1.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  523 KLLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTgKEMA 602
Cdd:cd21238      6 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 84
                           90
                   ....*....|....*....
gi 1973428429  603 SVGEPDKLSMVMYLTQFYE 621
Cdd:cd21238     85 DVPQPDEKSIITYVSSLYD 103
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
524-624 8.99e-18

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: 80.86  E-value: 8.99e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMAS 603
Cdd:cd21258      6 LLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVEDMMI 85
                           90       100
                   ....*....|....*....|..
gi 1973428429  604 VG-EPDKLSMVMYLTQFYEMFK 624
Cdd:cd21258     86 MGkKPDSKCVFTYVQSLYNHLR 107
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
524-620 1.71e-17

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: 80.01  E-value: 1.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMAS 603
Cdd:cd21261      6 LLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVEDMMV 85
                           90
                   ....*....|....*...
gi 1973428429  604 VG-EPDKLSMVMYLTQFY 620
Cdd:cd21261     86 MGrKPDPMCVFTYVQSLY 103
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
524-623 3.02e-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: 79.06  E-value: 3.02e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYsGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMAs 603
Cdd:cd21245      8 LLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPEDVM- 85
                           90       100
                   ....*....|....*....|
gi 1973428429  604 VGEPDKLSMVMYLTQFYEMF 623
Cdd:cd21245     86 VDSPDEQSIMTYVAQFLEHF 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
524-619 4.77e-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: 78.13  E-value: 4.77e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429   524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVE----QNNQLAFDIAEKELGISPIMTGK 599
Cdd:smart00033    3 LLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVVLFEPE 82
                            90       100
                    ....*....|....*....|
gi 1973428429   600 EMASvGEPDKLSMVMYLTQF 619
Cdd:smart00033   83 DLVE-GPKLILGVIWTLISL 101
LIM1_SF3 cd09440
The first Lim domain of pollen specific protein SF3; The first Lim domain of pollen specific ...
762-818 1.07e-16

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: 75.96  E-value: 1.07e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1973428429  762 DTCYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAYdiEDGKFYCKPHY 818
Cdd:cd09440      3 QKCKACDKTVYLVDQLSADGVVYHKSCFRCSHCKGTLKLSNYSS--MEGVLYCKPHF 57
LIM_Eplin_like cd09442
The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin) like proteins; The Lim domain of ...
764-818 1.39e-16

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: 75.21  E-value: 1.39e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAYdiEDGKFYCKPHY 818
Cdd:cd09442      1 CTVCQKRVYPMERLIADKQNFHKSCFRCEHCNSKLSLGNYAS--LHGRIYCKPHF 53
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
528-601 6.15e-15

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


Pssm-ID: 432229  Cd Length: 85  Bit Score: 71.56  E-value: 6.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  528 CQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFD------SLDEQNVEQNNQLAFDIAEKELGISPIM-TGKE 600
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEdiclkeSMSLADSLYNIQLLQEFCQRHLGNRCCHlTLED 80

                   .
gi 1973428429  601 M 601
Cdd:pfam11971   81 L 81
LIM_Eplin_alpha_beta cd09485
The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin); The Lim domain of Epithelial ...
764-818 1.34e-14

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: 69.52  E-value: 1.34e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAYdiEDGKFYCKPHY 818
Cdd:cd09485      1 CVSCQKTVYPLERLVANQQIYHNSCFRCSYCNTKLSLGTYAS--LHGNIYCKPHF 53
LIM_Eplin_like_1 cd09486
a LIM domain subfamily on a group of proteins with unknown function; This model represents a ...
764-818 6.38e-14

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: 67.68  E-value: 6.38e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAydIEDGKFYCKPHY 818
Cdd:cd09486      1 CSSCQKTVYPMERLVADKLVFHNSCFCCKHCNAKLSLGSYA--ALHGEFYCKPHF 53
LIM2_SF3 cd09441
The second Lim domain of pollen specific protein SF3; The second Lim domain of pollen specific ...
764-818 1.80e-12

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: 64.03  E-value: 1.80e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAydIEDGKFYCKPHY 818
Cdd:cd09441      1 CVACGKTVYPIEKVTVEGTSYHKSCFKCSHGGCTISPSNYA--AHEGRLYCKHHH 53
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
524-621 2.08e-12

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: 65.05  E-value: 2.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  524 LLGWCQRQTDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFD---SLDEQNVEQNNQLAFDIAEKE-LGISPIMTGK 599
Cdd:cd00014      4 LLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkkPKSPFKKRENINLFLNACKKLgLPELDLFEPE 83
                           90       100
                   ....*....|....*....|..
gi 1973428429  600 EMasVGEPDKLSMVMYLTQFYE 621
Cdd:cd00014     84 DL--YEKGNLKKVLGTLWALAL 103
LIM_Mical_like_1 cd09444
This domain belongs to the LIM domain family which are found on Mical (molecule interacting ...
764-817 6.04e-12

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: 62.04  E-value: 6.04e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAYDIEDGKFYCKPH 817
Cdd:cd09444      1 CAACGQHVHLVQRHLVDGKLYHRNCFRCKECSSTLLPGSYKAGPEPGTFVCTHH 54
LIM_Mical_like_2 cd09445
This domain belongs to the LIM domain family which are found on Mical (molecule interacting ...
764-818 7.41e-12

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: 62.10  E-value: 7.41e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSayAYDIEDGKFYCKPHY 818
Cdd:cd09445      1 CRSCGKPVYKMEEIIAEKHIYHKNCFRCKDCNKQLKVD--NYQSHEGNLYCKVHF 53
LIM_Ltd-1 cd09443
The LIM domain of LIM and transglutaminase domains protein (Ltd-1); The LIM domain of LIM and ...
764-817 8.96e-12

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: 61.67  E-value: 8.96e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAYDIEDGKFYCKPH 817
Cdd:cd09443      1 CPRCGKTAYPAESVDKDGTFYHKGCFKCRECGTRLSLKTFTFVQGDGEVYCARH 54
LIM_like_1 cd09400
LIM domain in proteins of unknown function; LIM domain in proteins of unknown function: LIM ...
762-814 1.47e-11

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: 61.29  E-value: 1.47e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1973428429  762 DTCYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYaYDIEDGKFYC 814
Cdd:cd09400      3 EPCASCGLPVFLAERLLIEGKVYHRTCFKCARCGVQLTPGSF-YETEYGSYCC 54
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
764-818 3.01e-11

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: 60.02  E-value: 3.01e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAydIEDGKFYCKPHY 818
Cdd:cd08368      1 CAGCGKPIEGRELLRALGKKWHPECFKCAECGKPLGGDSFY--EKDGKPYCEKCY 53
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
523-619 8.08e-11

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: 60.47  E-value: 8.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  523 KLLGWCQrqtDGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLI-DFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEM 601
Cdd:cd21230      5 RLLGWIQ---NKIPQLPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLITPEEI 81
                           90
                   ....*....|....*...
gi 1973428429  602 ASvGEPDKLSMVMYLTQF 619
Cdd:cd21230     82 IN-PNVDEMSVMTYLSQF 98
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
538-619 9.42e-11

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: 60.39  E-value: 9.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  538 VNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEQNNQLAFDiAEKELGISPIMTGKEMASvGEPDKLSMVMYLT 617
Cdd:cd21185     17 VDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMAD-PEVEHLGIMAYAA 94

                   ..
gi 1973428429  618 QF 619
Cdd:cd21185     95 QL 96
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
539-626 2.21e-10

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


Pssm-ID: 409078  Cd Length: 105  Bit Score: 59.32  E-value: 2.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  539 NVTDLTMSWKSGLALCAIIHRYRPDLI-DFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEMASvGEPDKLSMVMYLT 617
Cdd:cd21229     20 KITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPEDLSS-PHLDELSGMTYLS 98

                   ....*....
gi 1973428429  618 QFyeMFKDS 626
Cdd:cd21229     99 YF--MKEDG 105
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
85-226 6.34e-10

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 63.03  E-value: 6.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429   85 TNTKCLIIGAGPCGLRTAIDLSLLGAKVVVIEKRDAFSRNN-VLHLWPFTIHDLRGLGAK-------------KFYGKFC 150
Cdd:COG0654      2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGrGIALSPRSLELLRRLGLWdrllargapirgiRVRDGSD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  151 AGAIDHISI-------------RQLQLILLKVALILGIEIHVNVEFQGLVQPPEdqeneriGWRALVHPKThpvsEYEFE 217
Cdd:COG0654     82 GRVLARFDAaetglpaglvvprADLERALLEAARALGVELRFGTEVTGLEQDAD-------GVTVTLADGR----TLRAD 150

                   ....*....
gi 1973428429  218 VIIGGDGRR 226
Cdd:COG0654    151 LVVGADGAR 159
LIM_LASP cd09447
The LIM domain of LIM and SH3 Protein (LASP); The LIM domain of LIM and SH3 Protein (LASP): ...
764-818 8.86e-10

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: 55.84  E-value: 8.86e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAY-AYdieDGKFYCKPHY 818
Cdd:cd09447      1 CARCGKTVYPTEKLNCLDKIWHKGCFKCEVCGMTLNMKNYkGY---NKKPYCNAHY 53
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
764-817 1.13e-09

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: 55.85  E-value: 1.13e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429   764 CYFCQKRVYVMER-LSAEGKFFHRSCFKCDYCATTLRLSAYAydIEDGKFYCKPH 817
Cdd:smart00132    2 CAGCGKPIYGTERvLRALGKVWHPECFKCATCGKPLSGDTFF--EKDGKLYCKDC 54
LIM_CRP_like cd09326
The LIM domains of Cysteine Rich Protein (CRP) family; The LIM domains of Cysteine Rich ...
764-820 1.64e-09

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: 55.29  E-value: 1.64e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATtlRLSAYAYDIEDGKFYCKPhyCY 820
Cdd:cd09326      1 CPRCGKSVYAAEEVIAAGKSWHKSCFTCAVCNK--RLDSTTLAEHDGEIYCKS--CY 53
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
764-819 2.07e-09

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


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 55.03  E-value: 2.07e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAydIEDGKFYCKPHYC 819
Cdd:pfam00412    1 CAGCNRPIYDRELVRALGKVWHPECFRCAVCGKPLTTGDFY--EKDGKLYCKHDYY 54
LIM_CRIP cd09478
The LIM domain of Cysteine-Rich Intestinal Protein (CRIP); The LIM domain of Cysteine-Rich ...
764-820 6.45e-09

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: 53.73  E-value: 6.45e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAYdiEDGKFYCKpHYCY 820
Cdd:cd09478      1 CPKCDKEVYFAERVTSLGKDWHRPCLKCEKCGKTLTPGSHAE--HDGKPYCN-HPCY 54
LIM_TLP_like cd09401
The LIM domains of thymus LIM protein (TLP); The LIM domain of thymus LIM protein (TLP) like ...
764-820 1.63e-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: 52.34  E-value: 1.63e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAydIEDGKFYCkpHYCY 820
Cdd:cd09401      1 CPKCGKPVYFAEKKTSLGRDWHKPCLRCEKCKKTLTPGQHS--EHEGKPYC--NKCY 53
LIM1_TLP cd09476
The first LIM domain of thymus LIM protein (TLP); The first LIM domain of thymus LIM protein ...
764-820 4.39e-08

The first LIM domain of thymus LIM protein (TLP); The first 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: 188860  Cd Length: 54  Bit Score: 51.12  E-value: 4.39e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAYdiEDGKFYC-KPhyCY 820
Cdd:cd09476      1 CPRCDKTVYFAEKVSSLGKNWHRFCLKCERCSKILSPGGHAE--HDGKPYChKP--CY 54
LIM2_CRP3 cd09482
The second LIM domain of Cysteine Rich Protein 3 (CRP3/MLP); The second LIM domain of Cysteine ...
764-820 5.32e-08

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: 51.17  E-value: 5.32e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRlSAYAYDiEDGKFYCKphYCY 820
Cdd:cd09482      1 CPRCGKSVYAAEKVMGGGKPWHKTCFRCAICGKSLE-STTVTD-KDGELYCK--VCY 53
LIM1_CRP1 cd09479
The first LIM domain of Cysteine Rich Protein 1 (CRP1); The first LIM domain of Cysteine Rich ...
764-820 5.81e-08

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: 51.17  E-value: 5.81e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAydIEDGKFYCKPhyCY 820
Cdd:cd09479      3 CGVCQKTVYFAEEVQCEGRSFHKSCFLCMVCKKNLDSTTVA--VHGEEIYCKS--CY 55
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
1816-1974 1.08e-07

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 57.06  E-value: 1.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1816 EEELSAKLTRRVQKAARRQAKQEE-----LKRL--HRAQIIQRQLEQVEEKQRQLEERGVAVEKALRGEAGMGK-KDDPK 1887
Cdd:pfam17380  408 EEERQRKIQQQKVEMEQIRAEQEEarqreVRRLeeERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKeKRDRK 487
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1888 LMQEWFKLVQE------KNAMVRYESELMIFarELELEDRQSRLQQELRERMAvEDHLKTEEELSEEKKILNEMLEVVEQ 1961
Cdd:pfam17380  488 RAEEQRRKILEkeleerKQAMIEEERKRKLL--EKEMEERQKAIYEEERRREA-EEERRKQQEMEERRRIQEQMRKATEE 564
                          170
                   ....*....|...
gi 1973428429 1962 RDSLVALLEEQRL 1974
Cdd:pfam17380  565 RSRLEAMEREREM 577
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
523-619 2.83e-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: 50.94  E-value: 2.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  523 KLLGWCQRQTdgySGVNVTDLTMSWKSGLALCAIIHRYRPDLI-DFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEM 601
Cdd:cd21315     20 RLLGWIQSKV---PDLPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIKPEEM 96
                           90
                   ....*....|....*...
gi 1973428429  602 ASvGEPDKLSMVMYLTQF 619
Cdd:cd21315     97 VN-PKVDELSMMTYLSQF 113
LIM1_MLP84B_like cd09404
The LIM domain of Mlp84B and Mlp60A; The LIM domain of Mlp84B and Mlp60A: Mlp84B and Mlp60A ...
764-820 4.57e-07

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: 48.25  E-value: 4.57e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATtlRLSAYAYDIEDGKFYCKPhyCY 820
Cdd:cd09404      2 CPKCGKSVYAAEERLAGGYKWHKMCFKCGMCNK--LLDSTNCAEHEGELYCKQ--CH 54
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1114-1507 4.90e-07

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: 54.92  E-value: 4.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1114 LQSQTKVKADLELRVSENEEEKPSDTPKQEERGPSQVSSPSQPpqkqavlfSPAHSPGAEEAKPPP-ASITTKVKSPAEE 1192
Cdd:pfam05109  448 LPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTP--------SPSPRDNGTESKAPDmTSPTSAVTTPTPN 519
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1193 PLFPAPLLLREKPKAEGPEEQKTvhSPIRSQPVALPEARSPTSPTSSLQPESLLAPptpptppstqlpiCSQPQPSSDAS 1272
Cdd:pfam05109  520 ATSPTPAVTTPTPNATSPTLGKT--SPTSAVTTPTPNATSPTPAVTTPTPNATIPT-------------LGKTSPTSAVT 584
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1273 IPSP-TKSPIRFQPVP----------AKTSTPLTPLPvksqgdPKDRLSGPLAVEEALKRSDlVEEFWMKSAEIRRSLGL 1341
Cdd:pfam05109  585 TPTPnATSPTVGETSPqanttnhtlgGTSSTPVVTSP------PKNATSAVTTGQHNITSSS-TSSMSLRPSSISETLSP 657
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1342 TPVDRNKGSEPSLPSP---------ALKPISLKSYSVDKSPQDEglcllKPPSVPKRLGLPKSAGDQPP-------LLTP 1405
Cdd:pfam05109  658 STSDNSTSHMPLLTSAhptggenitQVTPASTSTHHVSTSSPAP-----RPGTTSQASGPGNSSTSTKPgevnvtkGTPP 732
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1406 KSPSDKELRSNQEERRDLSSSSGLGLHGSSSNMKTLGSQSFNTSDSTMLTPPSSPPPPPPPNEE----PATLRR-KPRQT 1480
Cdd:pfam05109  733 KNATSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATtylpPSTSSKlRPRWT 812
                          410       420
                   ....*....|....*....|....*..
gi 1973428429 1481 FERreasviPPPTPASFMRPPREAAQP 1507
Cdd:pfam05109  813 FTS------PPVTTAQATVPVPPTSQP 833
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1822-1986 5.03e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 5.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1822 KLTRRVQKAARRQAKQEELKRLHRA-----------------QIIQRQLEQVEEKQRQLEERGVAVEkALRGEAGMGKKD 1884
Cdd:TIGR02168  204 SLERQAEKAERYKELKAELRELELAllvlrleelreeleelqEELKEAEEELEELTAELQELEEKLE-ELRLEVSELEEE 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1885 DPKLMQEWFKLVQEKNAMvryESELMIFARELE-LEDRQSRLQQELRERMAVEDHLKTEEELSEEKK--ILNEMLEVVEQ 1961
Cdd:TIGR02168  283 IEELQKELYALANEISRL---EQQKQILRERLAnLERQLEELEAQLEELESKLDELAEELAELEEKLeeLKEELESLEAE 359
                          170       180
                   ....*....|....*....|....*
gi 1973428429 1962 RDSLVALLEEQRLREKEEDKDLEAA 1986
Cdd:TIGR02168  360 LEELEAELEELESRLEELEEQLETL 384
LIM1_CRP cd09402
The first LIM domain of Cysteine Rich Protein (CRP); The first LIM domain of Cysteine Rich ...
764-820 5.25e-07

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: 48.04  E-value: 5.25e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAydIEDGKFYCKPhyCY 820
Cdd:cd09402      1 CGACEKTVYHAEEVQCEGRSFHKSCFLCMVCRKNLDSTTVA--AHEDEIYCKS--CY 53
LIM_LASP_like cd09359
The LIM domain of LIM and SH3 Protein (LASP)-like proteins; The LIM domain of LIM and SH3 ...
764-818 9.61e-07

The LIM domain of LIM and SH3 Protein (LASP)-like proteins; The LIM domain of LIM and SH3 Protein (LASP) like proteins: This family contains two types of LIM containing proteins; LASP and N-RAP. 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. N-RAP is a muscle-specific protein concentrated at myotendinous junctions in skeletal muscle and intercalated disks in cardiac muscle. LIM domain is found at the N-terminus of N-RAP and the C-terminal of N-RAP contains a region with multiple of nebulin repeats. N-RAP functions as a scaffolding protein that organizes alpha-actinin and actin into symmetrical I-Z-I structures in developing myofibrils. Nebulin repeat is known as actin binding domain. The N-RAP is hypothesized to form antiparallel dimerization via its LIM domain. 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: 188745  Cd Length: 53  Bit Score: 47.65  E-value: 9.61e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAYdiEDGKFYCKPHY 818
Cdd:cd09359      1 CARCGKIVYPTEKVNCLDKTWHKACFHCEVCKMTLNMNNYKG--YQKKPYCNAHY 53
LIM2_CRP cd09403
The second LIM domain of Cysteine Rich Protein (CRP); The second LIM domain of Cysteine Rich ...
764-820 1.95e-06

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: 46.80  E-value: 1.95e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAYdiEDGKFYCKPhyCY 820
Cdd:cd09403      1 CPRCGKSVYAAEKIIGAGKPWHKNCFRCAKCGKSLESTTLAD--KDGEIYCKG--CY 53
PHA03247 PHA03247
large tegument protein UL36; Provisional
1147-1408 3.91e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 3.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1147 PSQVSSPSQPPQKQAVlfSPAHSPGAEEAKPPPASITTKVKSPAEEPLFPAPLLLREKPKAEGPEEQKTVHSPIRSQPVA 1226
Cdd:PHA03247  2673 AAQASSPPQRPRRRAA--RPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT 2750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1227 LPEARSPTSPTSSLQPESLLAPPTPP----------TPPSTQLPICSQPQPSSDASIPSPTKSPIRFQPVPAKTSTPLTP 1296
Cdd:PHA03247  2751 PGGPARPARPPTTAGPPAPAPPAAPAagpprrltrpAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1297 lPVKSQGDPKDRLSGPLAVEEALkrsdlveEFWMKSAeirrslglTPVDRNKGSEPSLPSPALKP----ISLKSYSVDKS 1372
Cdd:PHA03247  2831 -PTSAQPTAPPPPPGPPPPSLPL-------GGSVAPG--------GDVRRRPPSRSPAAKPAAPArppvRRLARPAVSRS 2894
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1973428429 1373 PQDEGLcllkPPSVPKRLGLPKSAgdQPPLLTPKSP 1408
Cdd:PHA03247  2895 TESFAL----PPDQPERPPQPQAP--PPPQPQPQPP 2924
LIM1_LIMK cd09364
The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain ...
764-818 4.00e-06

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: 45.56  E-value: 4.00e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATtlRLSAYAYDiEDGKFYCKPHY 818
Cdd:cd09364      1 CAGCRGKILDSQYVQALNQDWHCDCFRCSVCSD--SLSNWYFE-KDGKLYCRKDY 52
LIM2_CRP2 cd09840
The second LIM domain of Cysteine Rich Protein 2 (CRP2); The second LIM domain of Cysteine ...
764-820 4.71e-06

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: 45.48  E-value: 4.71e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAYdiEDGKFYCKPhyCY 820
Cdd:cd09840      1 CSRCGDSVYAAEKIMGAGKPWHKNCFRCAKCGKSLESTTLTE--KEGEIYCKG--CY 53
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1075-1505 6.05e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 51.71  E-value: 6.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1075 PAETEGEAAEDGDPGDTGAELDDQHWSDDIPSDAetehrlqsqtkvKADLELRVSENEEEKPSDTPKQEERGPSQVSSPS 1154
Cdd:PHA03307    24 PPATPGDAADDLLSGSQGQLVSDSAELAAVTVVA------------GAAACDRFEPPTGPPPGPGTEAPANESRSTPTWS 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1155 QPPQKQAVlFSPAHSPGA--EEAKPPPASIttkvkSPAEEPLFPAPLLLREKPKAEGPEEQKTVHSPIrsqPVALPEARS 1232
Cdd:PHA03307    92 LSTLAPAS-PAREGSPTPpgPSSPDPPPPT-----PPPASPPPSPAPDLSEMLRPVGSPGPPPAASPP---AAGASPAAV 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1233 PTSPTSSLQPESLLAPPTPptppstqlpicSQPQPSSDASIPSPTKSPIRFQPVPAKTSTPL-------TPLPVKSQGDP 1305
Cdd:PHA03307   163 ASDAASSRQAALPLSSPEE-----------TARAPSSPPAEPPPSTPPAAASPRPPRRSSPIsasasspAPAPGRSAADD 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1306 KDRLSGPLAVEEALKRSDLVEEfwmKSAEIRRSLGLTPVDRNKGSEPSLPSPalkpislksysvDKSPQDEglcllkPPS 1385
Cdd:PHA03307   232 AGASSSDSSSSESSGCGWGPEN---ECPLPRPAPITLPTRIWEASGWNGPSS------------RPGPASS------SSS 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1386 VPKRLGLPKSAGDQPPLLTPKSPSDKELRSNQEERRDLSSSSGlglhgsssnmktlgsqsfNTSDSTMLTPPSSPPPPPP 1465
Cdd:PHA03307   291 PRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSS------------------ESSRGAAVSPGPSPSRSPS 352
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1973428429 1466 PNEEPATLRRKPRQTfeRREASVIPPPTPASFMRPPREAA 1505
Cdd:PHA03307   353 PSRPPPPADPSSPRK--RPRPSRAPSSPAASAGRPTRRRA 390
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
523-619 7.22e-06

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


Pssm-ID: 409161  Cd Length: 114  Bit Score: 47.11  E-value: 7.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  523 KLLGWCQRQtdgYSGVNVTDLTMSWKSGLALCAIIHRYRPDLI-DFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEM 601
Cdd:cd21312     16 RLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEI 92
                           90
                   ....*....|....*...
gi 1973428429  602 ASvGEPDKLSMVMYLTQF 619
Cdd:cd21312     93 VD-PNVDEHSVMTYLSQF 109
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
87-274 1.00e-05

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 50.02  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429   87 TKCLIIGAGPCGLRTAIDLSLLGAKVVVIEKRDAF---SRNNVLHlwPFTIHDLRGLG---------------AKKFYGK 148
Cdd:pfam01494    2 TDVLIVGGGPAGLMLALLLARAGVRVVLVERHATTsvlPRAHGLN--QRTMELLRQAGledrilaegvphegmGLAFYNT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  149 FCAGAIDHIS-------IRQLQL--ILLKVALILGIEIHVNVEFQGLVQppeDQENERIgwRALVHpKTHPVSEYEFEVI 219
Cdd:pfam01494   80 RRRADLDFLTspprvtvYPQTELepILVEHAEARGAQVRFGTEVLSLEQ---DGDGVTA--VVRDR-RDGEEYTVRAKYL 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1973428429  220 IGGDGRRNTLE---GFRRKEFRGKLAIAITANFINRNTTaeAKVEEISGVAFIFNQKF 274
Cdd:pfam01494  154 VGCDGGRSPVRktlGIEFEGFEGVPFGSLDVLFDAPDLS--DPVERAFVHYLIYAPHS 209
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
520-569 1.05e-05

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: 46.91  E-value: 1.05e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1973428429  520 RSSKLLGWCQRQTdGYSGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDS 569
Cdd:cd21224      1 VLSLLLKWCQAVC-AHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDA 49
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1816-1986 1.07e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1816 EEELSAKLTRRVQKAARRQAKQEELKRLH-RAQIIQRQLEQVEEKQ-RQLEERGVAVEKALrgeagmgkkddpklmQEWF 1893
Cdd:COG1196    322 EEELAELEEELEELEEELEELEEELEEAEeELEEAEAELAEAEEALlEAEAELAEAEEELE---------------ELAE 386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1894 KLVQEKNAMVRYESELMIFARELE-LEDRQSRLQQELRERMAVEDHLKTEEE------LSEEKKILNEMLEVVEQRDSLV 1966
Cdd:COG1196    387 ELLEALRAAAELAAQLEELEEAEEaLLERLERLEEELEELEEALAELEEEEEeeeealEEAAEEEAELEEEEEALLELLA 466
                          170       180
                   ....*....|....*....|
gi 1973428429 1967 ALLEEQRLREKEEDKDLEAA 1986
Cdd:COG1196    467 ELLEEAALLEAALAELLEEL 486
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1027-1520 1.11e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 50.84  E-value: 1.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1027 DPLAIQADVHWTHIREREEEERMLPPSESSTSRAPLDEDDLEEDVDSEPAETEGEAAEDGDPGDTGAEldDQHWSDDIPS 1106
Cdd:PTZ00449   463 DIYMLKFDEYWTRISKIQFTQEIKKLIKKSKKKLAPIEEEDSDKHDEPPEGPEASGLPPKAPGDKEGE--EGEHEDSKES 540
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1107 DAETEHRLQSQTKvKADLELRVSENEEEKPSDTPKQEER--GPSQVSSPSQPpqkqavlfspahspgaEEAKPPPASITT 1184
Cdd:PTZ00449   541 DEPKEGGKPGETK-EGEVGKKPGPAKEHKPSKIPTLSKKpeFPKDPKHPKDP----------------EEPKKPKRPRSA 603
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1185 KVKSPAEEPLFPAPLLLREKPKAegPEEQKTVHSPIrsqpvalpearSPTSPTSSLQPESLLAPPTPPTPPSTQLPI--- 1261
Cdd:PTZ00449   604 QRPTRPKSPKLPELLDIPKSPKR--PESPKSPKRPP-----------PPQRPSSPERPEGPKIIKSPKPPKSPKPPFdpk 670
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1262 ------------CSQPQPSSDASIPSPTKSPIRFQPVPAKTSTPLT---PLPVKSQGDPKDRLSgPLAVEEALKRSDLve 1326
Cdd:PTZ00449   671 fkekfyddyldaAAKSKETKTTVVLDESFESILKETLPETPGTPFTtprPLPPKLPRDEEFPFE-PIGDPDAEQPDDI-- 747
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1327 EFWMKSAEIRRSLGLTPVDRnkgSEPSLPSPALKPISLKSYSvdKSPQDEglclLKPPSVPKRLGlPKSAGDQPPLLTPK 1406
Cdd:PTZ00449   748 EFFTPPEEERTFFHETPADT---PLPDILAEEFKEEDIHAET--GEPDEA----MKRPDSPSEHE-DKPPGDHPSLPKKR 817
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1407 SPSDKELRSNQeerrDLSSSSGLGLHGSSSNMKTLG-SQSFNTSDSTMLTPPSSPPPP---------PPPNEEPATLRRK 1476
Cdd:PTZ00449   818 HRLDGLALSTT----DLESDAGRIAKDASGKIVKLKrSKSFDDLTTVEEAEEMGAEARkivvdddgtEADDEDTHPPEEK 893
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1973428429 1477 PRQTFERREasviPPPTPAsfmRPPREAAQPPREEVRKSFVESV 1520
Cdd:PTZ00449   894 HKSEVRRRR----PPKKPS---KPKKPSKPKKPKKPDSAFIPSI 930
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1817-1987 1.27e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1817 EELSAKLTRRVQKAARRQAKQEELKRLhraqiiQRQLEQVEEKQRQLEERGVAVEKALRGEAgmgkkddpkLMQEWFKLV 1896
Cdd:COG4717     74 KELEEELKEAEEKEEEYAELQEELEEL------EEELEELEAELEELREELEKLEKLLQLLP---------LYQELEALE 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1897 QEKNAM-VRYESELMIFARELELEDRQSRLQQELRERMAVEDHLKTEEELSEEKKiLNEMLEVVEQRDSLVALLEEQRLR 1975
Cdd:COG4717    139 AELAELpERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE-LQDLAEELEELQQRLAELEEELEE 217
                          170
                   ....*....|..
gi 1973428429 1976 EKEEDKDLEAAM 1987
Cdd:COG4717    218 AQEELEELEEEL 229
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
1800-1987 1.41e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 50.12  E-value: 1.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1800 LERSSQKS-KREPRTYTEEELSAKLTR----------RVQK---------AARRQAKQEElKRLHRAQIIQRQLEQVEEK 1859
Cdd:pfam17380  350 LERIRQEErKRELERIRQEEIAMEISRmrelerlqmeRQQKnervrqeleAARKVKILEE-ERQRKIQQQKVEMEQIRAE 428
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1860 Q---RQLEERGVAVEKALRGEagmgkkddpKLMQEWFKLVQEKNAMVRYESELMIFARELELEDRQSRLQQELReRMAVE 1936
Cdd:pfam17380  429 QeeaRQREVRRLEEERAREME---------RVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR-RKILE 498
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1973428429 1937 DHLKTEEELSEEKKILNEMLEvVEQRDSLVALLEEQRLREKEEDKDLEAAM 1987
Cdd:pfam17380  499 KELEERKQAMIEEERKRKLLE-KEMEERQKAIYEEERRREAEEERRKQQEM 548
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1119-1399 1.57e-05

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 49.77  E-value: 1.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1119 KVKADLELRVSENEEEKPSDTPKQEERGPSQVSSPSQPPQKQavlfspahsPGAEEAKPPPASITTKVKSPAEEPLfPAP 1198
Cdd:NF033839   263 KIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQ---------PEKKEVKPEPETPKPEVKPQLEKPK-PEV 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1199 LLLREKPKAEGPEEQKTVHSPIRSQPVA-LPEAR-SPTSPTSSLQPESLLAPPTPPTPPstqlpicSQPQPSSDasiPSP 1276
Cdd:NF033839   333 KPQPEKPKPEVKPQLETPKPEVKPQPEKpKPEVKpQPEKPKPEVKPQPETPKPEVKPQP-------EKPKPEVK---PQP 402
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1277 TKSPIRFQPVPAKTSTPLTPLPVKSQGDPKDRLSGPlaveealkRSDLVEEFWMKSAEIRRSLGlTPvDRNKGSEPSLPS 1356
Cdd:NF033839   403 EKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKP--------KPEVKPQPEKPKPEVKPQPE-TP-KPEVKPQPEKPK 472
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1973428429 1357 PALKPISLKSYSVDKSPQDEGlcllKPPSVPKRLGLPKSAGDQ 1399
Cdd:NF033839   473 PEVKPQPEKPKPDNSKPQADD----KKPSTPNNLSKDKQPSNQ 511
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1150-1670 1.88e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 50.08  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1150 VSSPSQPPQKQAVLFSPAhsPGAEEAKPppasittkVKSPAEEPLFPAPLLLREKPKAEGPEEQKTVHSPIRSQPVALPE 1229
Cdd:PRK10263   346 VASVDVPPAQPTVAWQPV--PGPQTGEP--------VIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQP 415
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1230 ARSPTSPTSSLQPESLLAPPTPPTPPSTQLPICSQPQPSSDAsiPSPTKSPIRFQPVPAKTSTPLTPLPVKSQGDPKDrl 1309
Cdd:PRK10263   416 AQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFA--PQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVE-- 491
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1310 sgPLAVEEALKRSD----LVEEFWMKSAEIRRSLGL------TPVDRNKGSEPSLPSPALKPISLKSYSVDKSPQDEGL- 1378
Cdd:PRK10263   492 --PEPVVEETKPARpplyYFEEVEEKRAREREQLAAwyqpipEPVKEPEPIKSSLKAPSVAAVPPVEAAAAVSPLASGVk 569
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1379 ------CLLKPPSVPKrLGLPKSAGDQPPL---LTPKSPSDKELRSnqEERRDLSSssglglHGSSSNMKTLGSQSFNTS 1449
Cdd:PRK10263   570 katlatGAAATVAAPV-FSLANSGGPRPQVkegIGPQLPRPKRIRV--PTRRELAS------YGIKLPSQRAAEEKAREA 640
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1450 DSTMLTPPSSPPPPPPPNEEPATLRRKPRQTFERREASVIPPPTPASfmrpPREAAQPPREEVRKSFVESVDEI------ 1523
Cdd:PRK10263   641 QRNQYDSGDQYNDDEIDAMQQDELARQFAQTQQQRYGEQYQHDVPVN----AEDADAAAEAELARQFAQTQQQRysgeqp 716
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1524 ----PFA-DDVEDTYDDKTEDSSLQEKFFTP-------PSCWSRSEKLPAKENGRLPPLEQEVQPQKRALPlvsaeaKEL 1591
Cdd:PRK10263   717 aganPFSlDDFEFSPMKALLDDGPHEPLFTPivepvqqPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAP------QPQ 790
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1592 AEERMRAREKSVKSQALRDAMAKQLSRMQAMEMVSSR---SRPAPSPGKEPGlEATKHPSL------RGSQEPTLKheAT 1662
Cdd:PRK10263   791 YQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQpqyQQPQQPVAPQPQ-DTLLHPLLmrngdsRPLHKPTTP--LP 867

                   ....*...
gi 1973428429 1663 SEEILSPP 1670
Cdd:PRK10263   868 SLDLLTPP 875
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1799-1988 1.94e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 49.15  E-value: 1.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1799 ILERSSQKSKREPRTYTEEELSAKLTRRVQK--AARRQAKQEELKRLHRA-QIIQRQLEQVEEKQRQLEErgvavEKALR 1875
Cdd:pfam13868   82 IEEREQKRQEEYEEKLQEREQMDEIVERIQEedQAEAEEKLEKQRQLREEiDEFNEEQAEWKELEKEEER-----EEDER 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1876 GEAGMGKKDdpKLMQEWFKLVQEKNAmvRYESELMIFARELELEDRQSRLQQELRERMAVEDHLKTEE--ELSEEKKILN 1953
Cdd:pfam13868  157 ILEYLKEKA--EREEEREAEREEIEE--EKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERqkEREEAEKKAR 232
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1973428429 1954 EMLEVVEQRDSLVALLEEQRLREKEEDKDLEAAML 1988
Cdd:pfam13868  233 QRQELQQAREEQIELKERRLAEEAEREEEEFERML 267
LIM1_CRP2 cd09480
The first LIM domain of Cysteine Rich Protein 2 (CRP2); The first LIM domain of Cysteine Rich ...
764-820 2.60e-05

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: 43.44  E-value: 2.60e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAydIEDGKFYCKPhyCY 820
Cdd:cd09480      2 CGACGRTVYHAEEVQCDGRSFHKCCFLCMVCRKNLDSTTVA--IHDQEIYCKS--CY 54
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1800-1982 2.74e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 2.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1800 LERSSQKSKRepRTYTEEELSAKLTRRVQKAARRQAKQEELKRLHRAQiiQRQLEQVEEKQRQLEERGVAVEKALRGEAG 1879
Cdd:TIGR02168  311 LANLERQLEE--LEAQLEELESKLDELAEELAELEEKLEELKEELESL--EAELEELEAELEELESRLEELEEQLETLRS 386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1880 mgkkddpklmqewfKLVQEKNAMVRYESELMIFARELE-LEDRQSRLQQE---LRERMAVEDHLKTEEELSEEKKILNem 1955
Cdd:TIGR02168  387 --------------KVAQLELQIASLNNEIERLEARLErLEDRRERLQQEieeLLKKLEEAELKELQAELEELEEELE-- 450
                          170       180
                   ....*....|....*....|....*....
gi 1973428429 1956 lEVVEQRDSLVALLE--EQRLREKEEDKD 1982
Cdd:TIGR02168  451 -ELQEELERLEEALEelREELEEAEQALD 478
LIM1_abLIM cd09327
The first LIM domain of actin binding LIM (abLIM) proteins; The first LIM domain of actin ...
764-818 3.21e-05

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: 43.01  E-value: 3.21e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429  764 CYFCQKRVyVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAydIEDGKFYCKPHY 818
Cdd:cd09327      1 CYKCGKKC-KGEVLRVQDKYFHIKCFTCKVCGCDLAQGGFF--VKEGEYYCTDDY 52
PTZ00121 PTZ00121
MAEBL; Provisional
1800-1985 3.78e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 3.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1800 LERSSQKSKREPRTYTEEELSAKLTRRVQ--KAARRQAKQEELKRlhraqiiQRQLEQVEEKQRQLEERGVAVEKAlrge 1877
Cdd:PTZ00121  1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEekKKADELKKAEELKK-------AEEKKKAEEAKKAEEDKNMALRKA---- 1583
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1878 aGMGKKDDPKLMQEWFKLVQEKNAM----VRYESELMIFARELELEDRQSRLQQELRERMAVE----DHLKTEEELSEEK 1949
Cdd:PTZ00121  1584 -EEAKKAEEARIEEVMKLYEEEKKMkaeeAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkkaEELKKAEEENKIK 1662
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1973428429 1950 KILNEMLEVVEQRDSLVALLEEQRLREKEEDKDLEA 1985
Cdd:PTZ00121  1663 AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1817-1986 3.95e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 3.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1817 EELSAKLTRRVQKAARRQAKQEELKRlhRAQIIQRQLEQVEEKQRQLEERGvaveKALRGEAGMGKKDDPKLMQEWFKLV 1896
Cdd:COG1196    235 RELEAELEELEAELEELEAELEELEA--ELAELEAELEELRLELEELELEL----EEAQAEEYELLAELARLEQDIARLE 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1897 QEKNAMVRYESELMifARELELEDRQSRLQQELRERMAVEDHLKTEEELSEEK--KILNEMLEVVEQRDSLVALLEEQRL 1974
Cdd:COG1196    309 ERRRELEERLEELE--EELAELEEELEELEEELEELEEELEEAEEELEEAEAElaEAEEALLEAEAELAEAEEELEELAE 386
                          170
                   ....*....|..
gi 1973428429 1975 REKEEDKDLEAA 1986
Cdd:COG1196    387 ELLEALRAAAEL 398
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1822-1986 5.49e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 5.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1822 KLTRRVQKAARRQAKQEELKRLhRAQIIQRQLEQVEEKQRQLEERGVAVEKALRGEAGmgkkddpklmqewfKLVQEKNA 1901
Cdd:COG1196    204 PLERQAEKAERYRELKEELKEL-EAELLLLKLRELEAELEELEAELEELEAELEELEA--------------ELAELEAE 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1902 MVRYESELmifareLELEDRQSRLQQELRERMAVEDHLKTEEELSEEKKI--LNEMLEVVEQRDSLVALLEEQRLREKEE 1979
Cdd:COG1196    269 LEELRLEL------EELELELEEAQAEEYELLAELARLEQDIARLEERRRelEERLEELEEELAELEEELEELEEELEEL 342

                   ....*..
gi 1973428429 1980 DKDLEAA 1986
Cdd:COG1196    343 EEELEEA 349
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
523-619 5.62e-05

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


Pssm-ID: 409162  Cd Length: 110  Bit Score: 44.31  E-value: 5.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  523 KLLGWCQRQTdgySGVNVTDLTMSWKSGLALCAIIHRYRPDLI-DFDSLDEQNVEQNNQLAFDIAEKELGISPIMTGKEM 601
Cdd:cd21313     12 RLLGWIQNKI---PYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGVPQVITPEEI 88
                           90
                   ....*....|....*...
gi 1973428429  602 ASvGEPDKLSMVMYLTQF 619
Cdd:cd21313     89 IH-PDVDEHSVMTYLSQF 105
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
1800-1981 7.23e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 47.81  E-value: 7.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1800 LERSSQKSKREPRtyteEELSAKLTRRVQKAARRQAKQEELKRlhRAQIIQRQLEQVEEKQRQL-----EERGVAVEKAL 1874
Cdd:pfam17380  293 FEKMEQERLRQEK----EEKAREVERRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELerirqEERKRELERIR 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1875 RGEAGMgkkdDPKLMQEWFKLV---QEKNAMVRYESELmifARELEL--EDRQSRLQQELRERMAVEDhlKTEEELSEEK 1949
Cdd:pfam17380  367 QEEIAM----EISRMRELERLQmerQQKNERVRQELEA---ARKVKIleEERQRKIQQQKVEMEQIRA--EQEEARQREV 437
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1973428429 1950 KILNEMLEVVEQRDSLVALLEEQ---RLREKEEDK 1981
Cdd:pfam17380  438 RRLEEERAREMERVRLEEQERQQqveRLRQQEEER 472
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1816-1986 7.44e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 7.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1816 EEELSAKLTRRVQKAARRQAKQEELKRLHRAQiiQRQLEQVEEKQRQLEERGVAVEKALRGEAgmgkkddpklmqewfKL 1895
Cdd:COG1196    357 EAELAEAEEALLEAEAELAEAEEELEELAEEL--LEALRAAAELAAQLEELEEAEEALLERLE---------------RL 419
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1896 VQEKNAmvryeselmifARELELEDRQSRLQQELRERMAVEDHLKTEEELSEEKKILNEMLEVVEQRDSLVALLEEQRLR 1975
Cdd:COG1196    420 EEELEE-----------LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
                          170
                   ....*....|.
gi 1973428429 1976 EKEEDKDLEAA 1986
Cdd:COG1196    489 AAARLLLLLEA 499
PRK08244 PRK08244
monooxygenase;
86-143 9.12e-05

monooxygenase;


Pssm-ID: 236199 [Multi-domain]  Cd Length: 493  Bit Score: 47.43  E-value: 9.12e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1973428429   86 NTKCLIIGAGPCGLRTAIDLSLLGAKVVVIEKRDA---FSRNNVLHLWPFTIHDLRGLGAK 143
Cdd:PRK08244     2 KYEVIIIGGGPVGLMLASELALAGVKTCVIERLKEtvpYSKALTLHPRTLEILDMRGLLER 62
PRK11633 PRK11633
cell division protein DedD; Provisional
1135-1237 1.01e-04

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 45.76  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1135 KPSDTPKQEERGPSQVSSPSQPPQ--KQAVLFSPAHSPGAEEAKPPPASITTKVKSPAEEPLFPAPlllREKPKAEgPEE 1212
Cdd:PRK11633    46 KPGDRDEPDMMPAATQALPTQPPEgaAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKP---VEKPKPK-PKP 121
                           90       100
                   ....*....|....*....|....*
gi 1973428429 1213 QKTVHSPIRSQPVALPEARSPTSPT 1237
Cdd:PRK11633   122 QQKVEAPPAPKPEPKPVVEEKAAPT 146
LIM_ALP_like cd09360
The LIM domain of ALP (actinin-associated LIM protein) family; This family represents the LIM ...
779-817 1.14e-04

The LIM domain of ALP (actinin-associated LIM protein) family; This family represents the LIM domain of ALP (actinin-associated LIM protein) family. Four proteins: ALP, CLP36, RIL, and Mystique have been classified into the ALP subfamily of LIM domain proteins. Each member of the subfamily contains an N-terminal PDZ domain and a C-terminal LIM domain. Functionally, these proteins bind to alpha-actinin through their PDZ domains and bind or other signaling molecules through their LIM domains. ALP proteins have been implicated in cardiac and skeletal muscle structure, function and disease, platelet, and epithelial cell motility. 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: 188746 [Multi-domain]  Cd Length: 52  Bit Score: 41.59  E-value: 1.14e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1973428429  779 AEGKFFHRSCFKCDYCATTLRLSAYaYDIEDgKFYCKPH 817
Cdd:cd09360     15 ARDKNRHPECFVCADCGLNLKNKGY-FFIED-ELYCETH 51
LIM1_CRP3 cd09481
The first LIM domain of Cysteine Rich Protein 3 (CRP3/MLP); The first LIM domain of Cysteine ...
764-820 1.19e-04

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: 41.66  E-value: 1.19e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAydIEDGKFYCKPhyCY 820
Cdd:cd09481      2 CGACEKTVYHAEEIQCNGRSFHKTCFICMACRKALDSTTVA--AHESEIYCKT--CY 54
LIM1_LIMK1 cd09462
The first LIM domain of LIMK1 (LIM domain Kinase 1); The first LIM domain of LIMK1 (LIM domain ...
764-818 1.35e-04

The first LIM domain of LIMK1 (LIM domain Kinase 1); The first LIM domain of LIMK1 (LIM domain Kinase 1): LIMK1 belongs to the LIMK protein family, which comprises 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 depolymerization. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK1 is expressed in all tissues and is localized to focal adhesions in the cell. LIMK1 can form homodimers upon binding of HSP90 and is activated by Rho effector Rho kinase and MAPKAPK2. LIMK1 is important for normal central nervous system development, and its deletion has been implicated in the development of the human genetic disorder Williams syndrome. Moreover, LIMK1 up-regulates the promoter activity of urokinase type plasminogen activator and induces its mRNA and protein expression in breast cancer cells. The LIM domains 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: 188846 [Multi-domain]  Cd Length: 74  Bit Score: 42.18  E-value: 1.35e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLrlsAYAYDIEDGKFYCKPHY 818
Cdd:cd09462     22 CASCGQSIYDGQYLQALNSDWHADCFRCCECGASL---SHWYYEKDGRLFCKKDY 73
PRK06126 PRK06126
hypothetical protein; Provisional
87-124 1.44e-04

hypothetical protein; Provisional


Pssm-ID: 235704 [Multi-domain]  Cd Length: 545  Bit Score: 46.91  E-value: 1.44e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1973428429   87 TKCLIIGAGPCGLRTAIDLSLLGAKVVVIEKRDAFSRN 124
Cdd:PRK06126     8 TPVLIVGGGPVGLALALDLGRRGVDSILVERKDGTAFN 45
LIM1_UF1 cd09397
LIM domain in proteins of unknown function; The first Lim domain of a LIM domain containing ...
768-818 1.76e-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: 41.09  E-value: 1.76e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1973428429  768 QKRVYvmerlSAEGKF---FHRSCFKCDYCATTLRLSAYAYdIEDGKFYCKPHY 818
Cdd:cd09397     10 GKSIS-----SKDGELsgqWHRECFVCTTCGCPFQFSVPCY-VLDDKPYCQQHY 57
LIM1_Ajuba_like cd09352
The first LIM domain of Ajuba-like proteins; The first LIM domain of Ajuba-like proteins: ...
764-818 1.88e-04

The first LIM domain of Ajuba-like proteins; The first LIM domain of Ajuba-like proteins: Ajuba like LIM protein family includes three highly homologous proteins Ajuba, Limd1, and WTIP. Members of the family contain three tandem C-terminal LIM domains and a proline-rich N-terminal region. This family of proteins functions as scaffolds, participating in the assembly of numerous protein complexes. In the cytoplasm, Ajuba binds Grb2 to modulate serum-stimulated ERK activation. Ajuba also recruits the TNF receptor-associated factor 6 (TRAF6) to p62 and activates PKCKappa activity. Ajuba interacts with alpha-catenin and F-actin to contribute to the formation or stabilization of adheren junctions by linking adhesive receptors to the actin cytoskeleton. Although Ajuba is a cytoplasmic protein, it can shuttle into the nucleus. In nucleus, Ajuba functions as a corepressor for the zinc finger-protein Snail. It binds to the SNAG repression domain of Snail through its LIM region. Arginine methyltransferase-5 (Prmt5), a protein in the complex, is recruited to Snai l through an interaction with Ajuba. This ternary complex functions to repress E-cadherin, a Snail target gene. In addition, Ajuba contains functional nuclear-receptor interacting motifs and selectively interacts with retinoic acid receptors (RARs) and rexinoid receptor (RXRs) to negatively regulate retinoic acid signaling. Wtip, the Wt1-interacting protein, was originally identified as an interaction partner of the Wilms tumour protein 1 (WT1). Wtip is involved in kidney and neural crest development. Wtip interacts with the receptor tyrosine kinase Ror2 and inhibits canonical Wnt signaling. LIMD1 was reported to inhibit cell growth and metastases. The inhibition may be mediated through an interaction with the protein barrier-to-autointegration (BAF), a component of SWI/SNF chromatin-remodeling protein; or through the interaction with retinoblastoma protein (pRB), resulting in inhibition of E2F-mediated transcription, and expression of the majority of genes with E2F1- responsive elements. Recently, Limd1 was shown to interact with the p62/sequestosome protein and influence IL-1 and RANKL signaling by facilitating the assembly of a p62/TRAF6/a-PKC multi-protein complex. The Limd1-p62 interaction affects both NF-kappaB and AP-1 activity in epithelial cells and osteoclasts. Moreover, LIMD1 functions as tumor repressor to block lung tumor cell line in vitro and in vivo. Recent studies revealed that LIM proteins Wtip, LIMD1 and Ajuba interact with components of RNA induced silencing complexes (RISC) as well as eIF4E and the mRNA m7GTP cap-protein complex and are required for microRNA-mediated gene silencing. 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: 188738  Cd Length: 54  Bit Score: 40.88  E-value: 1.88e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1973428429  764 CYFCQKRVY-VMERLSAEGKFFHRSCFKCDYCATTLRLSAYaYDIeDGKFYCKPHY 818
Cdd:cd09352      1 CVKCGKGVYgASQACQAMGNLYHTNCFTCCSCGRTLRGKAF-YNV-NGKVYCEEDY 54
PHA03247 PHA03247
large tegument protein UL36; Provisional
1167-1740 2.35e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1167 AHSPGAEEAKPPPASITTKVKSPAEEPLFPAPLLLREKPKAEgpeeqkTVHSPIRSQPVALPEARSPTS--PTSSLQPES 1244
Cdd:PHA03247  2486 ARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGE------PVHPRMLTWIRGLEELASDDAgdPPPPLPPAA 2559
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1245 llapptpptppstqlpicsqPQPSSDASIPSPTKSPIRFQP----------VPAKTSTPLTplPVKSQGDPKdRLSGPLA 1314
Cdd:PHA03247  2560 --------------------PPAAPDRSVPPPRPAPRPSEPavtsrarrpdAPPQSARPRA--PVDDRGDPR-GPAPPSP 2616
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1315 VEEALKRSDlveefwmKSAEIRRSLGLTPVDRNKGSEPSLPSPALKP-ISLKSYSVDKSPQDEGLCLLKPPSVPKRLGLP 1393
Cdd:PHA03247  2617 LPPDTHAPD-------PPPPSPSPAANEPDPHPPPTVPPPERPRDDPaPGRVSRPRRARRLGRAAQASSPPQRPRRRAAR 2689
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1394 KSAGDQPPLLTPKSPsdkelrSNQEERRDLSSSSGLGLhgsssnmkTLGSQSFNTSdSTMLTPPSSPPPPPPPNEEPATL 1473
Cdd:PHA03247  2690 PTVGSLTSLADPPPP------PPTPEPAPHALVSATPL--------PPGPAAARQA-SPALPAAPAPPAVPAGPATPGGP 2754
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1474 RRKPRQTFERREASVIPPPTPASfmRPPREAAQPPreevRKSFVESVDEIPFADDVEDTYDDKTEDSSLQEKFFTP---- 1549
Cdd:PHA03247  2755 ARPARPPTTAGPPAPAPPAAPAA--GPPRRLTRPA----VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPagpl 2828
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1550 PSCWSRSEKLPAKENGRLPP---LEQEVQPQ---KRALPLVSAEAKELAEERMRAREKSvksqalRDAMAKQlSRMQAME 1623
Cdd:PHA03247  2829 PPPTSAQPTAPPPPPGPPPPslpLGGSVAPGgdvRRRPPSRSPAAKPAAPARPPVRRLA------RPAVSRS-TESFALP 2901
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1624 MVSSRSRPAPSPGKEPGLEATKHPSLRgsQEPTLKHEATSEEILSPPSDSGGPDGSVTSSEGSSGKSKKRSSLFSPRRNK 1703
Cdd:PHA03247  2902 PDQPERPPQPQAPPPPQPQPQPPPPPQ--PQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRV 2979
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1973428429 1704 KEKKSKGEGGRPPEKP--------------SLSLPEDVAAKPKSLWKSVFS 1740
Cdd:PHA03247  2980 PQPAPSREAPASSTPPltghslsrvsswasSLALHEETDPPPVSLKQTLWP 3030
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1838-1987 2.77e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.29  E-value: 2.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1838 EELKRLHR----AQIIQRQLEQVEEKQRQLEErgvAVEKALRGEAGMGKKDDPKLMQEWFKLVQEKNAMVRYESELMI-- 1911
Cdd:pfam13868    6 DELRELNSkllaAKCNKERDAQIAEKKRIKAE---EKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEqi 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1912 ------FARELELEDRQSRLQQELRERMAVEDHLKTEEELSEEKKILNEMLEVVEQRDSLVallEEQRLREKEEDKDLEA 1985
Cdd:pfam13868   83 eereqkRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWK---ELEKEEEREEDERILE 159

                   ..
gi 1973428429 1986 AM 1987
Cdd:pfam13868  160 YL 161
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1799-1981 3.45e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 3.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1799 ILERSSQKSKREPRTYTEEELSAKLTR---RVQKAARRQAKQEELKRLhRAQIIQRQLEQVEEKQRQLEERGVAVEKAL- 1874
Cdd:PRK03918   330 IKELEEKEERLEELKKKLKELEKRLEEleeRHELYEEAKAKKEELERL-KKRLTGLTPEKLEKELEELEKAKEEIEEEIs 408
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1875 -----RGEAGMGKKDDPKLMQEWFK-----------LVQE--KNAMVRYESELMIFAREL-ELEDRQSRLQQELRErmaV 1935
Cdd:PRK03918   409 kitarIGELKKEIKELKKAIEELKKakgkcpvcgreLTEEhrKELLEEYTAELKRIEKELkEIEEKERKLRKELRE---L 485
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1973428429 1936 EDHLKTEEELSEEKKILNEMLEVVEQrdslvalLEEQRLREKEEDK 1981
Cdd:PRK03918   486 EKVLKKESELIKLKELAEQLKELEEK-------LKKYNLEELEKKA 524
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1816-1988 3.50e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.91  E-value: 3.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1816 EEELSAKLTRRVQKAARRQAKQEELKRLHRAQIIQRQLEQVEEKQRQLEERgVAVEKALRgeagmgkkddpKLMQEWFKL 1895
Cdd:pfam13868   50 EEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQER-EQMDEIVE-----------RIQEEDQAE 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1896 VQEKNAMVRYESELMIFARELELEDRQSRLQQELRERMAVEDHLKTEEELSEEKKIlnEMLEVVEQRDSLVALLEEQRLR 1975
Cdd:pfam13868  118 AEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREA--EREEIEEEKEREIARLRAQQEK 195
                          170
                   ....*....|...
gi 1973428429 1976 EKEEDKDLEAAML 1988
Cdd:pfam13868  196 AQDEKAERDELRA 208
LIM2_Lhx1_Lhx5 cd09375
The second LIM domain of Lhx1 (also known as Lim1) and Lhx5; The second LIM domain of Lhx1 ...
779-818 3.90e-04

The second LIM domain of Lhx1 (also known as Lim1) and Lhx5; The second LIM domain of Lhx1 (also known as Lim1) and Lhx5. Lhx1 and Lhx5 are closely related members of 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. Lhx1 is required for regulating the vertebrate head organizer, the nervous system, and female reproductive tract development. During embryogenesis in the mouse, Lhx1 is expressed early in mesodermal tissue, then later during urogenital, kidney, liver, and nervous system development. In the adult, expression is restricted to the kidney and brain. A mouse embryos with Lhx1 gene knockout cannot grow normal anterior head structures, kidneys, and gonads, but with normally developed trunk and tail morphology. In the developing nervous system, Lhx1 is required to direct the trajectories of motor axons in the limb. Lhx1 null female mice lack the oviducts and uterus. Lhx5 protein may play complementary or overlapping roles with Lhx1. The expression of Lhx5 in the anterior portion of the mouse neural tube suggests a role in patterning of the forebrain. 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: 188761  Cd Length: 56  Bit Score: 40.04  E-value: 3.90e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1973428429  779 AEGKFFHRSCFKCDYCATTLRLSAYAYDIEDGKFYCKPHY 818
Cdd:cd09375     17 ARDKVFHLNCFTCMVCRKQLSTGEELYILDENKFICKEDY 56
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1799-1984 4.08e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 4.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1799 ILERSSQKSKREPRTytEEELSaKLTRRVQKAARRQAKQEELKRL------------HRAQIIQRQLEQVEEKQRQLEER 1866
Cdd:PRK03918   205 VLREINEISSELPEL--REELE-KLEKEVKELEELKEEIEELEKEleslegskrkleEKIRELEERIEELKKEIEELEEK 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1867 gVAVEKALRGEAgmgkKDDPKLMQEWFKLVQEKN----AMVRYESELMIFAREL-ELEDRQSRLQqELRERmavedhlkt 1941
Cdd:PRK03918   282 -VKELKELKEKA----EEYIKLSEFYEEYLDELReiekRLSRLEEEINGIEERIkELEEKEERLE-ELKKK--------- 346
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1973428429 1942 EEELSEEKKILNEMLEVVEQRDSLVALLEeqRLREKEEDKDLE 1984
Cdd:PRK03918   347 LKELEKRLEELEERHELYEEAKAKKEELE--RLKKRLTGLTPE 387
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1801-1984 4.79e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 45.35  E-value: 4.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1801 ERSSQKSKREpRTYTEEELS-----AKLTRRVQKAARRQAKQEELKRLHRAQIIQRQLEQVEEKQRQleERGVAVEKALR 1875
Cdd:pfam02463  145 EIIAMMKPER-RLEIEEEAAgsrlkRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKAL--EYYQLKEKLEL 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1876 GEAGMGKKDDPKLMQEWFKLVQEKNAMVRYESELMIF-----ARELELEDRQSRLQQELRERMAVEDHLKTEEELSEEKK 1950
Cdd:pfam02463  222 EEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQeiekeEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1973428429 1951 ILNEMLEVVEQRDSLVALLEEQRLREKEEDKDLE 1984
Cdd:pfam02463  302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1801-1985 5.85e-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: 45.06  E-value: 5.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1801 ERSSQKSKREPRTYTEEELSAKLTRRVQKAARRQAKQEELKRLHRAQiiQRQLEQVEEKQRQLEERGVAVEKALrgeagm 1880
Cdd:TIGR02169  689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL--KERLEELEEDLSSLEQEIENVKSEL------ 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1881 gKKDDPKLMQEWFKLVQEKNAMvryeselmifaRELELEDRQSRLQQelrermaVEDHL-KTEEELSEEKKILNEMLEVV 1959
Cdd:TIGR02169  761 -KELEARIEELEEDLHKLEEAL-----------NDLEARLSHSRIPE-------IQAELsKLEEEVSRIEARLREIEQKL 821
                          170       180
                   ....*....|....*....|....*.
gi 1973428429 1960 EQRDSLVALLEEQRLREKEEDKDLEA 1985
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKE 847
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
94-245 5.99e-04

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 43.80  E-value: 5.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429   94 AGPCGLRTAIDLSLLGAKVVVIEKR---------DAFSRNNVLHLWPFTIHD----------LRGLGAKKFYGKFCAGAI 154
Cdd:COG0644      1 AGPAGSAAARRLARAGLSVLLLEKGsfpgdkicgGGLLPRALEELEPLGLDEplerpvrgarFYSPGGKSVELPPGRGGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  155 DHISIRQLQLILLKVALILGIEIHVNVEFQGLvqppeDQENERIgwraLVHpkTHPVSEYEFEVIIGGDGRR----NTLE 230
Cdd:COG0644     81 YVVDRARFDRWLAEQAEEAGAEVRTGTRVTDV-----LRDDGRV----VVR--TGDGEEIRADYVVDADGARsllaRKLG 149
                          170
                   ....*....|....*
gi 1973428429  231 GFRRKEFRGKLAIAI 245
Cdd:COG0644    150 LKRRSDEPQDYALAI 164
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1805-1987 6.13e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 6.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1805 QKSKREPRTYTE-EELSAKLTRRVQKAARRQAKQEELKRlhRAQIIQRQLEQVEEK----QRQLEERGVAVEKALRGEAg 1879
Cdd:PRK03918   518 EELEKKAEEYEKlKEKLIKLKGEIKSLKKELEKLEELKK--KLAELEKKLDELEEElaelLKELEELGFESVEELEERL- 594
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1880 mgkKDDPKLMQEWFKLVQEKNAMVRYESELMIFAREL-----ELEDRQSRLQQ------ELRERMAVEDHLKTEE---EL 1945
Cdd:PRK03918   595 ---KELEPFYNEYLELKDAEKELEREEKELKKLEEELdkafeELAETEKRLEElrkeleELEKKYSEEEYEELREeylEL 671
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1973428429 1946 SEEKKILNEMLEVVE-QRDSLVALLE------EQRLREKEEDKDLEAAM 1987
Cdd:PRK03918   672 SRELAGLRAELEELEkRREEIKKTLEklkeelEEREKAKKELEKLEKAL 720
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
87-243 6.61e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 43.85  E-value: 6.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429   87 TKCLIIGAGPCGLRTAIDLSLLGAKVVVIEkrdafSRNNVLHLWPFTIHDLRGLGAKKFYGKFCAGAIDHISiRQLQLIL 166
Cdd:pfam07992    1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE-----DEGTCPYGGCVLSKALLGAAEAPEIASLWADLYKRKE-EVVKKLN 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  167 LKVALILGIEIhVNVEFQG---LVQPPEDQENERIGWRALV-----HPKTHPVSEYEFEVIIGGDGRRNTlEGFRRKEFR 238
Cdd:pfam07992   75 NGIEVLLGTEV-VSIDPGAkkvVLEELVDGDGETITYDRLViatgaRPRLPPIPGVELNVGFLVRTLDSA-EALRLKLLP 152

                   ....*
gi 1973428429  239 GKLAI 243
Cdd:pfam07992  153 KRVVV 157
LIM2_Enigma cd09456
The second LIM domain of Enigma; The second LIM domain of Enigma: Enigma was initially ...
764-818 7.72e-04

The second LIM domain of Enigma; The second LIM domain of Enigma: Enigma was initially characterized in humans as a protein containing three LIM domains at the C-terminus and a PDZ domain at N-terminus. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. Enigma is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. 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: 188840 [Multi-domain]  Cd Length: 52  Bit Score: 39.21  E-value: 7.72e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429  764 CYFCQKRVyVMERLSAEGKFFHRSCFKCDYCATTLRLSAYAydIEDGKFYCKPHY 818
Cdd:cd09456      1 CAKCKKKI-TGEIMHALKMTWHVHCFTCAACKTPIRNRAFY--MEEGAPYCERDY 52
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
1127-1312 8.89e-04

MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 43.05  E-value: 8.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1127 RVSENEEEKPSDTPkQEERGPSQVSSPSQPPQKQAVLfSPAHSPGAEEAKPPPASITTKVKSPAEEPLFPAPLLLREK-- 1204
Cdd:pfam15822   14 KTSAVSNPKPGQPP-QGWPGSNPWNNPSAPPAVPSGL-PPSTAPSTVPFGPAPTGMYPSIPLTGPSPGPPAPFPPSGPsc 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1205 PKAEGPEEQKTVHSPIRSQPVALPEAR---------SPTSPTSS--LQPESLLAPPTPPTPPSTQLPICSQPQPSSDA-S 1272
Cdd:pfam15822   92 PPPGGPYPAPTVPGPGPIGPYPTPNMPfpelprpygAPTDPAAAapSGPWGSMSSGPWAPGMGGQYPAPNMPYPSPGPyP 171
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1973428429 1273 IPSPTKSPIRFQPVPAKTSTPLTPLPVKSQGDPKDRLSGP 1312
Cdd:pfam15822  172 AVPPPQSPGAAPPVPWGTVPPGPWGPPAPYPDPTGSYPMP 211
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
90-118 1.20e-03

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 43.54  E-value: 1.20e-03
                           10        20
                   ....*....|....*....|....*....
gi 1973428429   90 LIIGAGPCGLRTAIDLSLLGAKVVVIEKR 118
Cdd:COG1249      7 VVIGAGPGGYVAAIRAAQLGLKVALVEKG 35
COG2509 COG2509
FAD-dependent dehydrogenase [General function prediction only];
90-123 1.27e-03

FAD-dependent dehydrogenase [General function prediction only];


Pssm-ID: 441999 [Multi-domain]  Cd Length: 466  Bit Score: 43.56  E-value: 1.27e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1973428429   90 LIIGAGPCGLRTAIDLSLLGAKVVVIEK-RDAFSR 123
Cdd:COG2509     34 VIVGAGPAGLFAALELAEAGLKPLVLERgKDVEER 68
Bthiol_YpdA TIGR04018
putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, ...
88-117 1.39e-03

putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, including YpdA from Bacillus subtilis, are apparent oxidoreductases present only in species with an active bacillithiol system. They have been suggested actually to be thiol disulfide oxidoreductases (TDOR), although the evidence is incomplete. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 188533 [Multi-domain]  Cd Length: 316  Bit Score: 42.94  E-value: 1.39e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1973428429   88 KCLIIGAGPCGLRTAIDLSLLGAKVVVIEK 117
Cdd:TIGR04018    1 DVIIIGAGPCGLACAIEAQKAGLSYLIIEK 30
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
90-121 1.39e-03

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 43.28  E-value: 1.39e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1973428429   90 LIIGAGPCGLRTAIDLSLLGAKVVVIEKRDAF 121
Cdd:COG1053      7 VVVGSGGAGLRAALEAAEAGLKVLVLEKVPPR 38
PHA03247 PHA03247
large tegument protein UL36; Provisional
1140-1432 1.41e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1140 PKQEERGPSQVSSPSQPPQKQAVLFSPAHSPGAEEAKPPPASITTKVKSPAEEPLFPAPLllrekpkaegPEEQKTVHSP 1219
Cdd:PHA03247  2741 PPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPS----------PWDPADPPAA 2810
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1220 IRSQPVALPEARSPTS---PTSSLQPESLLAPPtppTPPSTQLPICSQPQPSSDASIPSPTKSPirfqpvPAKTSTPLTP 1296
Cdd:PHA03247  2811 VLAPAAALPPAASPAGplpPPTSAQPTAPPPPP---GPPPPSLPLGGSVAPGGDVRRRPPSRSP------AAKPAAPARP 2881
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1297 lpvksqgdPKDRLSGPlaveeALKRSdlVEEFWMKSAEIRR----SLGLTPVDRNKGSEPSLPSPALKPISLKSYSVDKS 1372
Cdd:PHA03247  2882 --------PVRRLARP-----AVSRS--TESFALPPDQPERppqpQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPT 2946
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1973428429 1373 PQDEGLCLLKPPS--------VPKRLGLPKSAGDQPPLLTPKSPSDKELRSNQEERRDLSSSSGLGLH 1432
Cdd:PHA03247  2947 TDPAGAGEPSGAVpqpwlgalVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALH 3014
LIM2_Lhx2_Lhx9 cd09377
The second LIM domain of Lhx2 and Lhx9 family; The second LIM domain of Lhx2 and Lhx9 family: ...
784-818 1.52e-03

The second LIM domain of Lhx2 and Lhx9 family; The second LIM domain of Lhx2 and Lhx9 family: Lhx2 and Lhx9 are highly homologous LHX regulatory proteins. They 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. Although Lhx2 and Lhx9 are highly homologous, they seems to play regulatory roles in different organs. In animals, Lhx2 plays important roles in eye, cerebral cortex, limb, the olfactory organs, and erythrocyte development. Lhx2 gene knockout mice exhibit impaired patterning of the cortical hem and the telencephalon of the developing brain, and a lack of development in olfactory structures. Lhx9 is expressed in several regions of the developing mouse brain, the spinal cord, the pancreas, in limb mesenchyme, and in the urogenital region. Lhx9 plays critical roles in gonad development. Homozygous mice lacking functional Lhx9 alleles exhibit numerous urogenital defects, such as gonadal agenesis, infertility, and undetectable levels of testosterone and estradiol coupled with high FSH levels. Lhx9 null mice are phenotypically female, even those that are genotypically male. 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: 188763  Cd Length: 59  Bit Score: 38.41  E-value: 1.52e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1973428429  784 FHRSCFKCDYCATTLRLSAYaYDIEDGKFYCKPHY 818
Cdd:cd09377     26 FHLNCFTCATCNKPLTKGDH-FGMRDGLVYCRLHY 59
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1801-1984 1.61e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1801 ERSSQKSKREPRTYTEEEL-SAKLTRRVQKAARRQAKQEELKRLHRAQI--IQRQLEQVEEKQRQLEERGVAVEKALRG- 1876
Cdd:PRK03918   413 RIGELKKEIKELKKAIEELkKAKGKCPVCGRELTEEHRKELLEEYTAELkrIEKELKEIEEKERKLRKELRELEKVLKKe 492
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1877 ----------------EAGMGKKDDPKLMQEW--FKLVQEKNAMVR---------------YESELMIFAREL-ELEDRQ 1922
Cdd:PRK03918   493 seliklkelaeqlkelEEKLKKYNLEELEKKAeeYEKLKEKLIKLKgeikslkkelekleeLKKKLAELEKKLdELEEEL 572
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1973428429 1923 SRLQQELRERmAVEDHLKTEEELSEEKKILNEMLEVVEQRDSLVALLEEQRLREKEEDKDLE 1984
Cdd:PRK03918   573 AELLKELEEL-GFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFE 633
LIM2_Enigma_like cd09362
The second LIM domain of Enigma-like family; The second LIM domain of Enigma-like family: The ...
764-818 1.71e-03

The second LIM domain of Enigma-like family; The second LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling 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: 188748 [Multi-domain]  Cd Length: 52  Bit Score: 38.23  E-value: 1.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429  764 CYFCQKRVyVMERLSAEGKFFHRSCFKCDYCATTLRLSayAYDIEDGKFYCKPHY 818
Cdd:cd09362      1 CARCHKKI-LGEVMHALKQTWHVSCFVCAACKQPIGNS--LFHMEDGEPYCEKDY 52
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
87-117 1.76e-03

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 42.80  E-value: 1.76e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1973428429   87 TKCLIIGAGPCGLRTAIDLSLLGAKVVVIEK 117
Cdd:COG0492      1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEG 31
PRK12704 PRK12704
phosphodiesterase; Provisional
1857-1979 1.82e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1857 EEKQRQLEERGVAVEKALRGEAGMGKKDdpKLMQ---EWFKLVQEknamvrYESELMIfaRELELEDRQSRLQQE---LR 1930
Cdd:PRK12704    30 EAKIKEAEEEAKRILEEAKKEAEAIKKE--ALLEakeEIHKLRNE------FEKELRE--RRNELQKLEKRLLQKeenLD 99
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1973428429 1931 ERMavEDHLKTEEELSEEKKILNEMLEVVEQRDSLVALLEEQRLREKEE 1979
Cdd:PRK12704   100 RKL--ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1831-1987 2.00e-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: 41.83  E-value: 2.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1831 ARRQAKQEELKRLH-RAQIIQRQLEQVEEKQRQLEERGVAVEKALrgeagmgKKDDPKLMQewfklvqeknamVRYESEL 1909
Cdd:COG1579     31 AELAELEDELAALEaRLEAAKTELEDLEKEIKRLELEIEEVEARI-------KKYEEQLGN------------VRNNKEY 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1910 MIFARELE-LEDRQSRLQQELRERMAVEDHLK-----TEEELSEEKKILNEmleVVEQRDSLVALLEEQRLREKEEDKDL 1983
Cdd:COG1579     92 EALQKEIEsLKRRISDLEDEILELMERIEELEeelaeLEAELAELEAELEE---KKAELDEELAELEAELEELEAEREEL 168

                   ....
gi 1973428429 1984 EAAM 1987
Cdd:COG1579    169 AAKI 172
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1816-1980 2.00e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.60  E-value: 2.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1816 EEELSAKLTRRvQKAARRQAKQEELKRLHRA--QIIQRQLEQVEEKQRQLEERGVAVEKALRGEAgmGKKDDPKLMQEWF 1893
Cdd:pfam13868  152 EEDERILEYLK-EKAEREEEREAEREEIEEEkeREIARLRAQQEKAQDEKAERDELRAKLYQEEQ--ERKERQKEREEAE 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1894 KLVQEKNAMVRYESELMIFARELELEDRQsrLQQELRERMAVEDHLKTEEELSEEKKILNEMLEVVEQRDSLVALLEEQR 1973
Cdd:pfam13868  229 KKARQRQELQQAREEQIELKERRLAEEAE--REEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQR 306

                   ....*..
gi 1973428429 1974 LREKEED 1980
Cdd:pfam13868  307 AAEREEE 313
LIM1_LIMK2 cd09463
The first LIM domain of LIMK2 (LIM domain Kinase 2); The first LIM domain of LIMK2 (LIM domain ...
764-819 2.05e-03

The first LIM domain of LIMK2 (LIM domain Kinase 2); The first LIM domain of LIMK2 (LIM domain Kinase 2): LIMK2 is a member of the LIMK protein family, which comprises 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, altering the rate of actin depolymerization. LIMK activity is activated by phosphorylation of a threonine residue within the activation loop of the kinase by p21-activated kinases 1 and 4 and by Rho kinase. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK2 is expressed in all tissues. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The activity of LIM kinase 2 to regulate cofilin phosphorylation is inhibited by the direct binding of Par-3. LIMK2 activation promotes cell cycle progression. The phenotype of Limk2 knockout mice shows a defect in spermatogenesis. The LIM domains 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: 188847 [Multi-domain]  Cd Length: 53  Bit Score: 37.93  E-value: 2.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1973428429  764 CYFCQKRVYVMERLSAEGKFFHRSCFKCDYCATTLrlSAYAYDiEDGKFYCKPHYC 819
Cdd:cd09463      1 CTGCGGRIQDSFHYRVVQEAWHNSCFQCSVCQDLL--TNWYYE-KDGKLYCHKHYW 53
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
90-198 2.32e-03

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 42.38  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429   90 LIIGAGPCGLRTAIDLSLLGAKVVVIEKRDAF----SRNN--VLHLWpftihdLRGLGAKKFYgKFCAGAIDHISirqlq 163
Cdd:pfam01266    3 VVIGGGIVGLSTAYELARRGLSVTLLERGDDPgsgaSGRNagLIHPG------LRYLEPSELA-RLALEALDLWE----- 70
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1973428429  164 lillkvALILGIEIHVNVEFQGLVQPPEDQENERI 198
Cdd:pfam01266   71 ------ELEEELGIDCGFRRCGVLVLARDEEEEAL 99
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
1153-1420 2.49e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.61  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1153 PSQPPqkqavlfSPAHSPGAEEAKP-PPASITTKVKSPAEEplfpaplllrEKPkaegPEEQKTVHSPIrSQPVALPEAR 1231
Cdd:PLN03209   324 PSQRV-------PPKESDAADGPKPvPTKPVTPEAPSPPIE----------EEP----PQPKAVVPRPL-SPYTAYEDLK 381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1232 SPTSPTSSlQPESLLAPPTPPTPPSTQLPicSQPQPSSDASIPSPTKSPIrfqPVPAKTSTPLTPLPVKSQGDPKDRLS- 1310
Cdd:PLN03209   382 PPTSPIPT-PPSSSPASSKSVDAVAKPAE--PDVVPSPGSASNVPEVEPA---QVEAKKTRPLSPYARYEDLKPPTSPSp 455
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1311 -GPLAVEEALKRSDLVEEfwmksaeirrsLGLTPVDRNKGSEPSLPSPALKPISLKSYSVDKSPQDEglcllKPPSVPKR 1389
Cdd:PLN03209   456 tAPTGVSPSVSSTSSVPA-----------VPDTAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTS-----PSPAAPVG 519
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1973428429 1390 LGLPKSAGDQPPLLT---PKSPSDKELRSNQEER 1420
Cdd:PLN03209   520 KVAPSSTNEVVKVGNsapPTALADEQHHAQPKPR 553
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
1132-1303 2.55e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.61  E-value: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1132 EEEKPSDTPKQEERGPSqVSSPSQPPQKQAVLFSPAhSPGA--EEAKPP-------PASITTKVKS------PAEEPLFP 1196
Cdd:PLN03209   337 DGPKPVPTKPVTPEAPS-PPIEEEPPQPKAVVPRPL-SPYTayEDLKPPtspiptpPSSSPASSKSvdavakPAEPDVVP 414
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1197 APLLLREKPKAEGPEEQKTVHSPIrSQPVALPEARSPTSPTSSlqPESLLAPPTPPTPPSTQLPICSQPQPSSDASIPSP 1276
Cdd:PLN03209   415 SPGSASNVPEVEPAQVEAKKTRPL-SPYARYEDLKPPTSPSPT--APTGVSPSVSSTSSVPAVPDTAPATAATDAAAPPP 491
                          170       180
                   ....*....|....*....|....*...
gi 1973428429 1277 TK-SPIRFQPVPAKTSTPLTPLPVKSQG 1303
Cdd:PLN03209   492 ANmRPLSPYAVYDDLKPPTSPSPAAPVG 519
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1800-1995 2.89e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.65  E-value: 2.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1800 LERSSQKSKREPRTYTEEELSAKLTRRVQKAARRQAKQEELKRLHRAQIIQRQLEQVEEKQRQLEERGVAVEKALRGEAg 1879
Cdd:pfam02463  213 YQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLL- 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1880 mgKKDDPKLMQEWFKLVQEKNAMVRYESELMIFARELELEDRQSRLQQELRERMAVEDHLKTEEELSEEKKILNEMLEVV 1959
Cdd:pfam02463  292 --AKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLE 369
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1973428429 1960 EQRDSLVALLEEQRLREKEEDKDLEAAMLCKGFSLD 1995
Cdd:pfam02463  370 QLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
91-149 3.08e-03

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 37.90  E-value: 3.08e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1973428429   91 IIGAGPCGLRTAIDLSLLGAKVVVIEKRD-----AFSR--NNVLHLWPF-TIHDLRGLGAKKFYGKF 149
Cdd:pfam13450    1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDrlggnAYSYrvPGYVFDYGAhIFHGSDEPNVRDLLDEL 67
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1838-1986 3.56e-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: 41.06  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1838 EELKRLHRAQIIQRQLEQVEEKQRQLEERGVAVEKALRGEAGmgkkddpklmqewfKLVQEKNAMVRYESELMIFARELE 1917
Cdd:COG1579      4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEA--------------RLEAAKTELEDLEKEIKRLELEIE 69
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1973428429 1918 -LEDRQSRLQQEL------RERMAVE---DHLKTEEELSEEkkilnEMLEVVEQRDSLVALLEEQRLREKEEDKDLEAA 1986
Cdd:COG1579     70 eVEARIKKYEEQLgnvrnnKEYEALQkeiESLKRRISDLED-----EILELMERIEELEEELAELEAELAELEAELEEK 143
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
88-123 3.74e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 41.53  E-value: 3.74e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1973428429   88 KCLIIGAGPCGLRTAIDLSLLGAKVVVIEKRDAFSR 123
Cdd:pfam07992  154 RVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLR 189
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1799-1986 3.95e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.27  E-value: 3.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1799 ILERSSQKSKREPRTYTEEELSAKLTRRVQKAARRQAKQEELKRLhraqiIQRQLEQVEEKQRQLEERGVAVEKALRGEA 1878
Cdd:pfam02463  246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKL-----LAKEEEELKSELLKLERRKVDDEEKLKESE 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1879 GMGKKDDPKLMQEWFKLVQEKNAMVryESELMIFARELELED-RQSRLQQELRERMAVEDHLKTEEELSEEKKILNEMLE 1957
Cdd:pfam02463  321 KEKKKAEKELKKEKEEIEELEKELK--ELEIKREAEEEEEEElEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1973428429 1958 ---VVEQRDSLVALLEEQRLREKEEDKDLEAA 1986
Cdd:pfam02463  399 lksEEEKEAQLLLELARQLEDLLKEEKKEELE 430
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
90-120 4.04e-03

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 42.07  E-value: 4.04e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1973428429   90 LIIGAGPCGLRTAIDLSLLGAKVVVIEKRDA 120
Cdd:PRK05249     9 VVIGSGPAGEGAAMQAAKLGKRVAVIERYRN 39
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
90-122 4.32e-03

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 41.78  E-value: 4.32e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1973428429   90 LIIGAGPCGLRTAIDLSLLGAKVVVIEKRDAFS 122
Cdd:PRK08132    27 VVVGAGPVGLALAIDLAQQGVPVVLLDDDDTLS 59
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1136-1327 4.51e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.17  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1136 PSDTPKQEERGPSQVSSPSQPPQKqavlfSPAHSPGAEEAKPPPASITTKvKSPAEEPLFPAPLLLREKPKAEGPEEQKT 1215
Cdd:PRK12323   381 PVAQPAPAAAAPAAAAPAPAAPPA-----APAAAPAAAAAARAVAAAPAR-RSPAPEALAAARQASARGPGGAPAPAPAP 454
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1216 VHSPIRSQPVALPEARSPTSPTSSLQPESLLAPPTPPTPPStqlpicsqPQPSSDASIPSPTKSPIRFQPVPAKTSTPLT 1295
Cdd:PRK12323   455 AAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDD--------PPPWEELPPEFASPAPAQPDAAPAGWVAESI 526
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1973428429 1296 PLPVKSQGDPKDRLSGPLAVEEALKRSDLVEE 1327
Cdd:PRK12323   527 PDPATADPDDAFETLAPAPAAAPAPRAAAATE 558
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1767-1969 4.85e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 4.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1767 SGQRRASPIVRAELhLRRQLSFSEDSDLSSDDILERSSQKSKREPRTYTEEELSAKLTRRVQKAARRQAKQEELKRL-HR 1845
Cdd:COG4717     62 QGRKPELNLKELKE-LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALeAE 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1846 AQIIQRQLEQVEEKQRQLEERGVAVEkALRGEAGMGKKDDPKLMQEWfkLVQEKNAMVRYESEL-MIFARELELEDRQSR 1924
Cdd:COG4717    141 LAELPERLEELEERLEELRELEEELE-ELEAELAELQEELEELLEQL--SLATEEELQDLAEELeELQQRLAELEEELEE 217
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1973428429 1925 LQQELRERMAVEDHLKTEEELSEEKKILNEMLEVVEQRDSLVALL 1969
Cdd:COG4717    218 AQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALL 262
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
1801-1981 4.97e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.86  E-value: 4.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1801 ERSSQKSKREPRTYTEEELSAKLTRRVQKAARRQAKQEELKRLHRAQIIQRQLEQVEEKQRQLEErgvavekalrgeagm 1880
Cdd:pfam15709  341 ERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEE--------------- 405
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1881 gkkddpklmQEWFKLVQEKNAMVRYESELMIFARelELEDRQSRLQQELRERMAVEDHLKTEEE--LSEEKKILNEMLEv 1958
Cdd:pfam15709  406 ---------EERKQRLQLQAAQERARQQQEEFRR--KLQELQRKKQQEEAERAEAEKQRQKELEmqLAEEQKRLMEMAE- 473
                          170       180
                   ....*....|....*....|...
gi 1973428429 1959 vEQRdslvalLEEQRLREKEEDK 1981
Cdd:pfam15709  474 -EER------LEYQRQKQEAEEK 489
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1816-1933 5.31e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 5.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1816 EEELSAKLTRR-VQKAARRQAKQEELKRLHRAQIIQRQLEQVEEKQRQLEERGVAVEKALRGEAGMGKKDDPKLM----- 1889
Cdd:pfam13868  212 QEEQERKERQKeREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMkrleh 291
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1973428429 1890 -QEWFKLVQEKNAMVR--YESELMIFARELELEDRQSRLQQELRERM 1933
Cdd:pfam13868  292 rRELEKQIEEREEQRAaeREEELEEGERLREEEAERRERIEEERQKK 338
PTZ00121 PTZ00121
MAEBL; Provisional
1800-1986 5.53e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 5.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1800 LERSSQKSKREPRTYTEEELSAKLTRRVQKAARRQAKQEELKRLHRAQIIQRQLEQVEEKQRQLEERGVAVEKALRGEAG 1879
Cdd:PTZ00121  1383 AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEA 1462
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1880 MGKKDDPKLMQEWFKLVQEK---NAMVRYESELMIFARELELEDRQSRLQQELRErmaVEDHLKTEEELSEEKKILNEML 1956
Cdd:PTZ00121  1463 KKKAEEAKKADEAKKKAEEAkkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKK---AEEAKKADEAKKAEEAKKADEA 1539
                          170       180       190
                   ....*....|....*....|....*....|
gi 1973428429 1957 EVVEQRDSLVALLEEQRLREKEEDKDLEAA 1986
Cdd:PTZ00121  1540 KKAEEKKKADELKKAEELKKAEEKKKAEEA 1569
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
1834-1984 5.94e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.70  E-value: 5.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1834 QAKQEELKRL-HRAQIIQRQLEQVEEKQRQLEERGVAVEKALRGEAgmgkkddpklmqEWFKLVQEKNA-MVRYESELMI 1911
Cdd:pfam01576    8 QAKEEELQKVkERQQKAESELKELEKKHQQLCEEKNALQEQLQAET------------ELCAEAEEMRArLAARKQELEE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1912 FARELEL-----EDRQSRLQQElRERMA-----VEDHLKTEE----ELSEEKKILNEMLEVVEQRdslVALLEEQRLREK 1977
Cdd:pfam01576   76 ILHELESrleeeEERSQQLQNE-KKKMQqhiqdLEEQLDEEEaarqKLQLEKVTTEAKIKKLEED---ILLLEDQNSKLS 151

                   ....*..
gi 1973428429 1978 EEDKDLE 1984
Cdd:pfam01576  152 KERKLLE 158
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1817-1982 6.05e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 6.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1817 EELSAKLTRRVQKAARRQAKQEELkrlhraqIIQRQLEQVEEKQRQLEErgvavEKALRgeagmgkkddpKLMQEWfKLV 1896
Cdd:pfam13868  183 EREIARLRAQQEKAQDEKAERDEL-------RAKLYQEEQERKERQKER-----EEAEK-----------KARQRQ-ELQ 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1897 QEKNAMVRYESELMIFARELELEDRQS--RLQQELRERMAVEDHlKTEEELSEEKKILNEMLEVVEQ---RDSLVALLEE 1971
Cdd:pfam13868  239 QAREEQIELKERRLAEEAEREEEEFERmlRKQAEDEEIEQEEAE-KRRMKRLEHRRELEKQIEEREEqraAEREEELEEG 317
                          170
                   ....*....|.
gi 1973428429 1972 QRLREKEEDKD 1982
Cdd:pfam13868  318 ERLREEEAERR 328
LIM2_ENH cd09457
The second LIM domain of the Enigma Homolog (ENH) family; The second LIM domain of the Enigma ...
764-818 6.22e-03

The second LIM domain of the Enigma Homolog (ENH) family; The second LIM domain of the Enigma Homolog (ENH) family: ENH was initially identified in rat brain. Same as enigma, it contains three LIM domains at the C-terminus and a PDZ domain at N-terminus. ENH is implicated in signal transduction processes involving protein kinases. It has also been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ENH is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. 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: 188841 [Multi-domain]  Cd Length: 52  Bit Score: 36.54  E-value: 6.22e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1973428429  764 CYFCQKRVyVMERLSAEGKFFHRSCFKCDYCATTLRLSayAYDIEDGKFYCKPHY 818
Cdd:cd09457      1 CGRCQRKI-LGEVINALKQTWHVSCFVCVACHNPIRNN--VFHLEDGEPYCETDY 52
LIM1_FHL cd09343
The first LIM domain of Four and a half LIM domains protein (FHL); The first LIM domain of ...
761-819 6.54e-03

The first LIM domain of Four and a half LIM domains protein (FHL); The first LIM domain of Four and a half LIM domains protein (FHL): LIM-only protein family consists of five members, designated FHL1, FHL2, FHL3, FHL5 and LIMPETin. The first four members are composed of four complete LIM domains arranged in tandem and an N-terminal single zinc finger domain with a consensus sequence equivalent to the C-terminal half of a LIM domain. LIMPETin is an exception, containing six LIM domains. FHL1, 2 and 3 are predominantly expressed in muscle tissues, and FHL5 is highly expressed in male germ cells. FHL proteins exert their roles as transcription co-activators or co-repressors through a wide array of interaction partners. For example, FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. FHL2 has shown to interact with more than 50 different proteins, including receptors, structural proteins, transcription factors and cofactors, signal transducers, splicing factors, DNA replication and repair enzymes, and metabolic enzymes. FHL3 int eracts with many transcription factors, such as CREB, BKLF/KLF3, CtBP2, MyoD, and MZF_1. FHL5 is a tissue-specific coactivator of CREB/CREM family transcription factors. 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: 188729  Cd Length: 59  Bit Score: 36.65  E-value: 6.54e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429  761 SDTCYFCQKRVYVMER-LSAEGKFFHRSCFKCDYCATTLRLSAYAydIEDGKFYCKPHYC 819
Cdd:cd09343      2 ANTCEECKKKIGCDSKdLSYKDRHWHEGCFKCFKCQRSLVDKPFA--AKDEDLLCTECYS 59
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1816-1986 6.97e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 6.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1816 EEELSAKLTRRVQKAARRQAKQEELKRLHRA--------QIIQRQLEQVEEKQRQLEERGVAVEKALRGEagmgKKDDPK 1887
Cdd:COG4942     33 QQEIAELEKELAALKKEEKALLKQLAALERRiaalarriRALEQELAALEAELAELEKEIAELRAELEAQ----KEELAE 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1888 LMQEWFKlvqeknaMVRYESELMIFARE--LELEDRQSRLQQELRERMAVEDHLK--------TEEELSEEKKILNEML- 1956
Cdd:COG4942    109 LLRALYR-------LGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRadlaelaaLRAELEAERAELEALLa 181
                          170       180       190
                   ....*....|....*....|....*....|
gi 1973428429 1957 EVVEQRDSLVALLEEQRLREKEEDKDLEAA 1986
Cdd:COG4942    182 ELEEERAALEALKAERQKLLARLEKELAEL 211
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
91-119 8.28e-03

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 40.93  E-value: 8.28e-03
                           10        20
                   ....*....|....*....|....*....
gi 1973428429   91 IIGAGPCGLRTAIDLSLLGAKVVVIEKRD 119
Cdd:PRK11749   145 VIGAGPAGLTAAHRLARKGYDVTIFEARD 173
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1816-1977 8.59e-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: 8.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1816 EEELSAKLTRRVQKAARRQAKQEELKRLhraqiiQRQLEQVEEKQRQLEERGVAVE-----KALRGEAGMGKKDDPKLMQ 1890
Cdd:COG1579     37 EDELAALEARLEAAKTELEDLEKEIKRL------ELEIEEVEARIKKYEEQLGNVRnnkeyEALQKEIESLKRRISDLED 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1891 EwfklvqEKNAMVRYEselmifarelELEDRQSRLQQELRERMAVEDHLKTEEElSEEKKILNEMLEVVEQRDSLVALLE 1970
Cdd:COG1579    111 E------ILELMERIE----------ELEEELAELEAELAELEAELEEKKAELD-EELAELEAELEELEAEREELAAKIP 173
                          170
                   ....*....|...
gi 1973428429 1971 E------QRLREK 1977
Cdd:COG1579    174 PellalyERIRKR 186
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1815-1983 8.92e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 8.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1815 TEEELSAKLTRRVQKAARRQAKQEELKRLH-RAQIIQRQLEQVEEKQRQLEERgvavEKALRGEAGMGKKDDPKLMQEWF 1893
Cdd:COG4372     50 LREELEQAREELEQLEEELEQARSELEQLEeELEELNEQLQAAQAELAQAQEE----LESLQEEAEELQEELEELQKERQ 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1973428429 1894 KLVQEKNAMVRYESEL--MIFARE---LELEDRQSRLQQELRERMAVEDHL---KTEEELSEEKKILNEMLEVVEQRDSL 1965
Cdd:COG4372    126 DLEQQRKQLEAQIAELqsEIAEREeelKELEEQLESLQEELAALEQELQALseaEAEQALDELLKEANRNAEKEEELAEA 205
                          170
                   ....*....|....*...
gi 1973428429 1966 VALLEEQRLREKEEDKDL 1983
Cdd:COG4372    206 EKLIESLPRELAEELLEA 223
 
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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