RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024455868 529 NTKLEVRKIPPELNNITQLNEHFSKFGTIVNIQVAFQNDPEAALIQYLTNDEARKAISSTEAVLNNRFIRVHWHRE 604
Cdd:cd12517     1 NTKLEVRKIPQELNNITQLNEHFSKFGTIVNIQVAFGGDPEAALIQYTTNEEARRAISSTEAVLNNRFIRVLWHRE 76

PWI domain;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024455868   7 DALKSWLAKLLEPICDADPSALANYVVALVKKDKP-EKELKafcaDQLDVFLQKETSGFVDKLFE 70
Cdd:pfam01480   1 EVLKPWIEKKITEILGFEDDVVVEYVVNLLEEKFPdPKELQ----IQLTGFLDKDAAKFVKELWK 61

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455868 681 DVQEALKKKQEAMKLQQDMRKKKQEMLEKQIECQKMLISKLEKNKAMKPEERAEIMKTLKELAGKISQLKDELKTSSTAS 760
Cdd:COG4942   164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243

                  ....*..
gi 2024455868 761 TPSKLKS 767
Cdd:COG4942   244 PAAGFAA 250

RNA recognition motif (RRM) found in vertebrate RNA-binding protein 27 (RBM27); This subgroup corresponds to the RRM of RBM27 which contains a single RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain). Although the specific function of the RRM in RBM27 remains unclear, it shows high sequence similarity with RRM1of RBM26, which functions as a cutaneous lymphoma (CL)-associated antigen.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024455868 529 NTKLEVRKIPPELNNITQLNEHFSKFGTIVNIQVAFQNDPEAALIQYLTNDEARKAISSTEAVLNNRFIRVHWHRE 604
Cdd:cd12517     1 NTKLEVRKIPQELNNITQLNEHFSKFGTIVNIQVAFGGDPEAALIQYTTNEEARRAISSTEAVLNNRFIRVLWHRE 76

PWI domain;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024455868   7 DALKSWLAKLLEPICDADPSALANYVVALVKKDKP-EKELKafcaDQLDVFLQKETSGFVDKLFE 70
Cdd:pfam01480   1 EVLKPWIEKKITEILGFEDDVVVEYVVNLLEEKFPdPKELQ----IQLTGFLDKDAAKFVKELWK 61

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteriztic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024455868 534 VRKIPPELNNiTQLNEHFSKFGTIVNIQVAFQNDPEA---ALIQYLTNDEARKAISST-EAVLNNRFIR 598
Cdd:pfam00076   3 VGNLPPDTTE-EDLKDLFSKFGPIKSIRLVRDETGRSkgfAFVEFEDEEDAEKAIEALnGKELGGRELK 70

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455868 113 EEERDSRKKKHsspQRSRaDSSEQRTRDKRRDDGKWRDYDRYYDRSDLYRDKSSWRRGR--SKSRSKSRGLSRSRSRSRG 190
Cdd:TIGR01642   3 EEPDREREKSR---GRDR-DRSSERPRRRSRDRSRFRDRHRRSRERSYREDSRPRDRRRydSRSPRSLRYSSVRRSRDRP 78

                          90       100
                  ....*....|....*....|....
gi 2024455868 191 RSKDHDANRNVEHRERSKFKSERN 214
Cdd:TIGR01642  79 RRRSRSVRSIEQHRRRLRDRSPSN 102

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455868 683 QEALKKKQE-AMKLQQDMRKKKQEM--LEKQIECQKMLISKLEKNKAMKPEERAEIMKTLKELAGKISQLKDELKTssta 759
Cdd:pfam20492  26 QEELEESEEtAEELEEERRQAEEEAerLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIARLEEEVER---- 101

                          90       100
                  ....*....|....*....|..
gi 2024455868 760 stpsKLKSKTEAQKELLDAELD 781
Cdd:pfam20492 102 ----KEEEARRLQEELEEAREE 119

MAEBL; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455868  684 EALKKKQEAMKLQQDMRKKKQEMLEKQIECQKmliSKLEKNKAMKPEERAEIMKTLKELAGKISQLK--DEL-KTSSTAS 760
Cdd:PTZ00121  1381 DAAKKKAEEKKKADEAKKKAEEDKKKADELKK---AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKkaDEAkKKAEEAK 1457

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2024455868  761 TPSKLKSKTEAQKELLDAEldfhKRLSSGEDTTELRKKLNQLQVEAARL 809
Cdd:PTZ00121  1458 KAEEAKKKAEEAKKADEAK----KKAEEAKKADEAKKKAEEAKKKADEA 1502

RNA recognition motif (RRM) found in vertebrate RNA-binding protein 27 (RBM27); This subgroup corresponds to the RRM of RBM27 which contains a single RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain). Although the specific function of the RRM in RBM27 remains unclear, it shows high sequence similarity with RRM1of RBM26, which functions as a cutaneous lymphoma (CL)-associated antigen.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024455868 529 NTKLEVRKIPPELNNITQLNEHFSKFGTIVNIQVAFQNDPEAALIQYLTNDEARKAISSTEAVLNNRFIRVHWHRE 604
Cdd:cd12517     1 NTKLEVRKIPQELNNITQLNEHFSKFGTIVNIQVAFGGDPEAALIQYTTNEEARRAISSTEAVLNNRFIRVLWHRE 76

RNA recognition motif 1 (RRM1) found in vertebrate RNA-binding protein 26 (RBM26) and similar proteins; This subfamily corresponds to the RRM1 of RBM26, and the RRM of RBM27. RBM26, also known as cutaneous T-cell lymphoma (CTCL) tumor antigen se70-2, represents a cutaneous lymphoma (CL)-associated antigen. It contains two RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The RRMs may play some functional roles in RNA-binding or protein-protein interactions. RBM27 contains only one RRM; its biological function remains unclear.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024455868 529 NTKLEVRKIPPELNNITQLNEHFSKFGTIVNIQVAFqnDPEAALIQYLTNDEARKAISSTEAVLNNRFIRVHWH 602
Cdd:cd12257     1 KTTLEVRNIPPELNNITKLREHFSKFGTIVNIQVNY--NPESALVQFSTSEEANKAYRSPEAVFNNRFIKVFWH 72

PWI domain;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024455868   7 DALKSWLAKLLEPICDADPSALANYVVALVKKDKP-EKELKafcaDQLDVFLQKETSGFVDKLFE 70
Cdd:pfam01480   1 EVLKPWIEKKITEILGFEDDVVVEYVVNLLEEKFPdPKELQ----IQLTGFLDKDAAKFVKELWK 61

RNA recognition motif 1 (RRM1) found in vertebrate RNA-binding protein 26 (RBM26) and similar proteins; This subfamily corresponds to the RRM1 of RBM26, and the RRM of RBM27. RBM26, also known as cutaneous T-cell lymphoma (CTCL) tumor antigen se70-2, represents a cutaneous lymphoma (CL)-associated antigen. It contains two RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The RRMs may play some functional roles in RNA-binding or protein-protein interactions. RBM27 contains only one RRM; its biological function remains unclear.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024455868 862 DELLQHFSKFGDIEDLQEEDSPLSVVLTFKSRSEAENAANQGSK-FKDRRLQISWY 916
Cdd:cd12257    17 TKLREHFSKFGTIVNIQVNYNPESALVQFSTSEEANKAYRSPEAvFNNRFIKVFWH 72

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024455868 861 KDELLQHFSKFGDIEDLQ-----EEDSPLSVVLTFKSRSEAENA--ANQGSKFKDRRLQIS 914
Cdd:cd00590    12 EEDLRELFSKFGEVVSVRivrdrDGKSKGFAFVEFESPEDAEKAleALNGTELGGRPLKVS 72

RNA recognition motif;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024455868  861 KDELLQHFSKFGDIEDLQ---EEDSPLS---VVLTFKSRSEAENA--ANQGSKFKDRRLQI 913
Cdd:smart00360  13 EEELRELFSKFGKVESVRlvrDKETGKSkgfAFVEFESEEDAEKAleALNGKELDGRPLKV 73

RNA recognition motif (RRM) found in 80 kDa MCM3-associated protein (Map80) and similar proteins; This subfamily corresponds to the RRM of Map80, also termed germinal center-associated nuclear protein (GANP), involved in the nuclear localization pathway of MCM3, a protein necessary for the initiation of DNA replication and also involves in controls that ensure DNA replication is initiated once per cell cycle. Map80 contains one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024455868 530 TKLEVRKIPPELNNITQLNEHFSKFGTIVNIQVafQNDPEAALIQYLTNDEARKA 584
Cdd:cd12443     1 TAIVCKNIPEELNDKEILRRHFSKFGKVARVFC--NPRKNLAIVHFKDHESAALA 53

RNA recognition motif 3 (RRM3) found in plant polypyrimidine tract-binding protein homolog 3 (PTBPH3); This subgroup corresponds to the RRM3 of PTBPH3. Although its biological roles remain unclear, PTBPH3 shows significant sequence similarity to polypyrimidine tract binding protein (PTB) that is an important negative regulator of alternative splicing in mammalian cells and also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. Like PTB, PTBPH3 contains four RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain).

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024455868 534 VRKIPPELNNITQLNEHFSKFGTIVNIQVaFQNDPEAALIQYLTNDEARKAISS 587
Cdd:cd12698     6 VSNLNPEKVDVDKLFNLFSLYGNIVRIKI-LRNKPDHALIQMSDPFQAELAVNY 58

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455868 683 QEALKKKQE-AMKLQQDMRKKKQEM--LEKQIECQKMLISKLEKNKAMKPEERAEIMKTLKELAGKISQLKDELKTssta 759
Cdd:pfam20492  26 QEELEESEEtAEELEEERRQAEEEAerLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIARLEEEVER---- 101

                          90       100
                  ....*....|....*....|..
gi 2024455868 760 stpsKLKSKTEAQKELLDAELD 781
Cdd:pfam20492 102 ----KEEEARRLQEELEEAREE 119

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455868 683 QEALKKKQEAMKLQQDMRKKKQEmLEKQIECQKMLISKLEKNKAMKPEERAEIMKTLKELAGKISQLKDELKTSSTASTP 762
Cdd:COG3883   150 AELEAKLAELEALKAELEAAKAE-LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228

                          90
                  ....*....|..
gi 2024455868 763 SKLKSKTEAQKE 774
Cdd:COG3883   229 AAAAAAAAAAAA 240

Zinc finger C-x8-C-x5-C-x3-H type (and similar);

                          10        20
                  ....*....|....*....|....
gi 2024455868 280 KRRCQDYDERGFCVLGDLCQFDHG 303
Cdd:pfam00642   3 TELCRFFLRTGYCKYGDRCKFAHG 26

Nup53/35/40-type RNA recognition motif; Members of this family belong to the nucleor pore complex, NPC, the only gateway between the nucleus and the cytoplasm. The NPC consists of several subcomplexes each one of which is made up of multiple copies of several individual Nup, Nic or Sec protein subunits. In yeast, this Nup or nucleoporin subunit is numbered Nup53, Nup40 in Schizo. pombe and in vertebrates as Nup35. This subunit forms part of the inner ring within the membrane and interacts directly with Nup-Ndc1, considered to be an anchor for the NPC in the pore membrane. This region of the Nup is the RNA-recognition region.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024455868 852 TVGGFIEEEKDELLQHFSKFGDI-EDLQEEDSPLSVVLTFKSRSEAENAAN 901
Cdd:pfam05172   5 TVFGFPPSITNIVLLHFSRFGEIvSHVPGPTNGNWMHLTYSSRSSAQKALS 55

RNA recognition motif (RRM) found in polypyrimidine tract-binding protein 1 (PTB or hnRNP I), heterogeneous nuclear ribonucleoprotein L (hnRNP-L), and similar proteins; This subfamily corresponds to the RRM2 of polypyrimidine tract-binding protein 1 (PTB or hnRNP I), polypyrimidine tract-binding protein 2 (PTBP2 or nPTB), regulator of differentiation 1 (Rod1), heterogeneous nuclear ribonucleoprotein L (hnRNP-L), heterogeneous nuclear ribonucleoprotein L-like (hnRNP-LL), polypyrimidine tract-binding protein homolog 3 (PTBPH3), polypyrimidine tract-binding protein homolog 1 and 2 (PTBPH1 and PTBPH2), and similar proteins, and RRM3 of PTBPH1 and PTBPH2. PTB is an important negative regulator of alternative splicing in mammalian cells and also functions at several other aspects of mRNA metabolism, including mRNA localization, stabilization, polyadenylation, and translation. PTBP2 is highly homologous to PTB and is perhaps specific to the vertebrates. Unlike PTB, PTBP2 is enriched in the brain and in some neural cell lines. It binds more stably to the downstream control sequence (DCS) RNA than PTB does but is a weaker repressor of splicing in vitro. PTBP2 also greatly enhances the binding of two other proteins, heterogeneous nuclear ribonucleoprotein (hnRNP) H and KH-type splicing-regulatory protein (KSRP), to the DCS RNA. The binding properties of PTBP2 and its reduced inhibitory activity on splicing imply roles in controlling the assembly of other splicing-regulatory proteins. Rod1 is a mammalian polypyrimidine tract binding protein (PTB) homolog of a regulator of differentiation in the fission yeast Schizosaccharomyces pombe, where the nrd1 gene encodes an RNA binding protein negatively regulates the onset of differentiation. ROD1 is predominantly expressed in hematopoietic cells or organs. It might play a role controlling differentiation in mammals. hnRNP-L is a higher eukaryotic specific subunit of human KMT3a (also known as HYPB or hSet2) complex required for histone H3 Lys-36 trimethylation activity. It plays both, nuclear and cytoplasmic, roles in mRNA export of intronless genes, IRES-mediated translation, mRNA stability, and splicing. hnRNP-LL protein plays a critical and unique role in the signal-induced regulation of CD45 and acts as a global regulator of alternative splicing in activated T cells. This family also includes polypyrimidine tract binding protein homolog 3 (PTBPH3) found in plant. Although its biological roles remain unclear, PTBPH3 shows significant sequence similarity to other family members, all of which contain four RNA recognition motifs (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain). Although their biological roles remain unclear, both PTBPH1 and PTBPH2 show significant sequence similarity to PTB. However, in contrast to PTB, they have three RRMs.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024455868 543 NITQLNEHFSKFGTIVNIqVAFQNDPE-AALIQYLTNDEARKAISsteaVLNNRFI 597
Cdd:cd12422    14 TVDVLHQVFSPYGAVEKI-VIFEKGTGvQALVQFDSVESAEAAKK----ALNGRNI 64

RNA recognition motif 1 (RRM1) found in yeast meiotic activator RIM4 and similar proteins; This subfamily corresponds to the RRM1 of RIM4, also termed regulator of IME2 protein 4, a putative RNA binding protein that is expressed at elevated levels early in meiosis. It functions as a meiotic activator required for both the IME1- and IME2-dependent pathways of meiotic gene expression, as well as early events of meiosis, such as meiotic division and recombination, in Saccharomyces cerevisiae. RIM4 contains two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The family also includes a putative RNA-binding protein termed multicopy suppressor of sporulation protein Msa1. It is a putative RNA-binding protein encoded by a novel gene, msa1, from the fission yeast Schizosaccharomyces pombe. Msa1 may be involved in the inhibition of sexual differentiation by controlling the expression of Ste11-regulated genes, possibly through the pheromone-signaling pathway. Like RIM4, Msa1 also contains two RRMs, both of which are essential for the function of Msa1.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024455868 547 LNEHFSKFGTIVNIQVA--FQNDPeAALIQYLTNDEARKAISSTE-AVLNNRFIRV 599
Cdd:cd12453    23 VTNHFSKWGELLNVKVLkdWSNRP-YAFVQYTNTEDAKNALVNGHnTLLDGRHLRV 77

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024455868  697 QDMRKKKQEMLE---KQIECQKMLISKLEKNKAMKPEERAEimktlkelagkisqLKDELKTSSTAstpsklKSKTEAQK 773
Cdd:pfam01576  348 QEMRQKHTQALEeltEQLEQAKRNKANLEKAKQALESENAE--------------LQAELRTLQQA------KQDSEHKR 407

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2024455868  774 ELLDAEL-DFHKRLSSGEDT-TELRKKLNQLQVE 805
Cdd:pfam01576  408 KKLEGQLqELQARLSESERQrAELAEKLSKLQSE 441