Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281361577   161 KSGSDINLTCLAmqSPVPPSFIYWYK-GKRVMNYSQRGGInvitERSTRTSKLLIAKATPADSGNYTC 227
Cdd:smart00410   7 KEGESVTLSCEA--SGSPPPEVTWYKqGGKLLAESGRFSV----SRSGSTSTLTISNVTPEDSGTYTC 68

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361577   53 REVTATVGQAALLHCRVRNLGDRA---VSWIRKRDLHILTVGILTYTNDQ-------RFQSLHSEGSDEWTLRISSPQPR 122
Cdd:pfam07686   4 REVTVALGGSVTLPCTYSSSMSEAstsVYWYRQPPGKGPTFLIAYYSNGSeegvkkgRFSGRGDPSNGDGSLTIQNLTLS 83

                          90       100
                  ....*....|....*....|....*
gi 281361577  123 DSGTYECQVSTEPKISQGFRLNVVV 147
Cdd:pfam07686  84 DSGTYTCAVIPSGEGVFGKGTRLTV 108

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281361577   161 KSGSDINLTCLAmqSPVPPSFIYWYK-GKRVMNYSQRGGInvitERSTRTSKLLIAKATPADSGNYTC 227
Cdd:smart00410   7 KEGESVTLSCEA--SGSPPPEVTWYKqGGKLLAESGRFSV----SRSGSTSTLTISNVTPEDSGTYTC 68

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281361577 166 INLTCLAMQSPVPpsFIYWYKGKRVMNYSQRGGINVITERSTrtskLLIAKATPADSGNYTC 227
Cdd:cd00096    1 VTLTCSASGNPPP--TITWYKNGKPLPPSSRDSRRSELGNGT----LTISNVTLEDSGTYTC 56

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361577   53 REVTATVGQAALLHCRVRNLGDRA---VSWIRKRDLHILTVGILTYTNDQ-------RFQSLHSEGSDEWTLRISSPQPR 122
Cdd:pfam07686   4 REVTVALGGSVTLPCTYSSSMSEAstsVYWYRQPPGKGPTFLIAYYSNGSeegvkkgRFSGRGDPSNGDGSLTIQNLTLS 83

                          90       100
                  ....*....|....*....|....*
gi 281361577  123 DSGTYECQVSTEPKISQGFRLNVVV 147
Cdd:pfam07686  84 DSGTYTCAVIPSGEGVFGKGTRLTV 108

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E and, D strands in one sheet and A', G, F, C, C', and C" strands in the other.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361577  53 REVTATVGQAALLHCRVRNL-GDRAVSWIRKRD------LHILTVGILTYTND--QRFQSLHSEGSDeWTLRISSPQPRD 123
Cdd:cd00099    6 RSLSVQEGESVTLSCEVSSSfSSTYIYWYRQKPgqgpefLIYLSSSKGKTKGGvpGRFSGSRDGTSS-FSLTISNLQPED 84

                 ....*....
gi 281361577 124 SGTYECQVS 132
Cdd:cd00099   85 SGTYYCAVS 93

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281361577  153 LGNAELFIKSGSDINLTCLAMQSPVPPSFIyWYKGKRVMNYSQRGginVITERSTRTSKLLIAKATPADSGNYTC 227
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGSPGPDVT-WSKEGGTLIESLKV---KHDNGRTTQSSLLISNVTKEDAGTYTC 71

Immunoglobulin I-set domain;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281361577  160 IKSGSDINLTCLAMQSPvPPSfIYWYKGKRVMNYSQRGginVITERSTRTSkLLIAKATPADSGNYTC 227
Cdd:pfam07679  12 VQEGESARFTCTVTGTP-DPE-VSWFKDGQPLRSSDRF---KVTYEGGTYT-LTISNVQPDDSGKYTC 73

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281361577 166 INLTCLAMQSPVPpsFIYWYKGKRVMNYSQRGGINVITERSTrtskLLIAKATPADSGNYTC 227
Cdd:cd00096    1 VTLTCSASGNPPP--TITWYKNGKPLPPSSRDSRRSELGNGT----LTISNVTLEDSGTYTC 56

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here are composed of the immunoglobulin (Ig) variable domain of the beta chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta, polypeptide chains with variable (V) and constant (C) regions. This group includes the variable domain of the alpha chain of alpha/beta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361577  53 REVTATVGQAALLHCRVrNLGDRAVSWIRKRDLHILTvgILTYTNDQ-----------RFQSLHSEGSdEWTLRISSPQP 121
Cdd:cd05899    6 RYLIKRRGQSVTLRCSQ-KSGHDNMYWYRQDPGKGLQ--LLFYSYGGglneegdlpgdRFSASRPSLT-RSSLTIKSAEP 81

                         90
                 ....*....|.
gi 281361577 122 RDSGTYECQVS 132
Cdd:cd05899   82 EDSAVYLCASS 92

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281361577 163 GSDINLTCLAMQSPVPPSFiYWYKGKRVMNYSQrgGINVITERSTRTSKLLIAKATPADSGNYTC 227
Cdd:cd05750   14 GSKLVLKCEATSENPSPRY-RWFKDGKELNRKR--PKNIKIRNKKKNSELQINKAKLEDSGEYTC 75

Immunoglobulin (Ig)-like variable (V) domain of the Signal-Regulatory Protein (SIRP); The members here are composed of the immunoglobulin (Ig)-like domain of the Signal-Regulatory Protein (SIRP). The SIRPs belong to the "paired receptors" class of membrane proteins that comprise several genes coding for proteins with similar extracellular regions, but very different transmembrane/cytoplasmic regions with different (activating or inhibitory) signaling potentials. They are commonly on NK cells, but are also on many myeloid cells. Their extracellular region contains three immunoglobulin superfamily domains, a single V-set, and two C1-set IgSF domains. Their cytoplasmic tails that contain either ITIMs or transmembrane regions have positively charged residues that allow an association with adaptor proteins, such as DAP12/KARAP, containing ITAMs. There are 3 distinct SIRP members: alpha, beta, and gamma. SIRP alpha (also known as CD172a or SRC homology 2 domain-containing protein tyrosine phosphatase substrate 1/Shps-1) is a membrane receptor that interacts with a ligand CD47 expressed on many cells and gives an inhibitory signal through immunoreceptor tyrosine-based inhibition motifs in the cytoplasmic region that interact with phosphatases SHP-1 and SHP-2. SIRP beta has a short cytoplasmic region and associates with a transmembrane adapter protein DAP12 containing immunoreceptor tyrosine-based activation motifs to give an activating signal. SIRP gamma contains a very short cytoplasmic region lacking obvious signaling motifs, but also binds CD47 with much less affinity. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281361577 160 IKSGSDINLTClAMQSPVPPSFIYWYKG---KRVMNYSQRGG-------INVITERSTRTSKLLIAKATPADSGNYTC 227
Cdd:cd16097   11 VAAGESATLHC-TVTSLIPVGPIQWFRGagpGRELIYNQKEGhfprvttVSDLTKRNNMDFSIRISNITPADAGTYYC 87

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281361577  55 VTATVGQAALLHCRVRnlGDRA--VSWirKRDLHILTVGiltytndqRFQSLhsegsDEWTLRISSPQPRDSGTYECQ 130
Cdd:cd05725    7 QVVLVDDSAEFQCEVG--GDPVptVRW--RKEDGELPKG--------RYEIL-----DDHSLKIRKVTAGDMGSYTCV 67

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281361577  163 GSDINLTClAMQSPVPPSFIyWYKGKRVMNYSQRgginviterstrtskLLIAKATPADSGNYTC 227
Cdd:pfam13895  14 GEPVTLTC-SAPGNPPPSYT-WYKDGSAISSSPN---------------FFTLSVSAEDSGTYTC 61

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 281361577  93 LTYTNDQRFQSLHSEGSD---EWTLRISSPQPRDSGTYECQVS 132
Cdd:cd05856   36 ITWLKDNKPLTPPEIGENkkkKWTLSLKNLKPEDSGKYTCHVS 78

First (N-terminal) immunoglobulin (Ig)-like domain of nectin-like molecule-1 (Necl-1); member of the V-set of Ig superfamily (IgSF) domains; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of nectin-like molecule-1, Necl-1 (also known as celll adhesion molecule 3 (CADM3), SynCAM2, or IGSF4). Nectin-like molecules have similar domain structures to those of nectins. At least five nectin-like molecules have been identified (Necl-1 - Necl-5). They all have an extracellular region containing three Ig-like domains, a transmembrane region, and a cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1 has Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue and is important to the formation of synapses, axon bundles, and myelinated axons.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361577  54 EVTATVGQAALLHCRVRNLGDRAVSWIRKRDlHILTVGILTYTNDQRFQSLHSEgSDEWTLRISSPQPRDSGTYECQVST 133
Cdd:cd05882    6 DETVAVGGTVTLKCGVKEHDNSSLQWSNTAQ-QTLYFGEKRALRDNRIQLVKST-PTELIISISNVQLSDEGEYTCSIFT 83

                 ..
gi 281361577 134 EP 135
Cdd:cd05882   84 MP 85

Immunoglobulin (Ig)-like variable (V) domain of Cluster of Differentiation (CD) 8 alpha chain; The members here are composed of the immunoglobulin (Ig)-like variable domain of the Cluster of Differentiation (CD) 8 alpha. The CD8 glycoprotein plays an essential role in the control of T-cell selection, maturation, and the T-cell receptor (TCR)-mediated response to peptide antigen. CD8 is comprised of alpha and beta subunits and is expressed as either an alpha/alpha or alpha/beta dimer. Both dimeric isoforms can serve as a coreceptor for T cell activation and differentiation, however they have distinct physiological roles, different cellular distributions, unique binding partners, etc. Each CD8 subunit is comprised of an extracellular domain containing a V-type Ig-like domain, a single pass transmembrane portion, and a short intracellular domain. The Ig domain of CD8 alpha binds to antibodies. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361577  51 SRREVTATVGQAALLHCRVRNLGDRAVSWIR--KRDLHILTvgILTYT------------NDQRFQSlhSEGSDEWTLRI 116
Cdd:cd05720    4 SPRKRDAQLGQKVELVCEVLNSVPQGCSWLFqpRGSAPQPT--FLLYLsssnktkwaeglDSKRFSG--SRSGSSYVLTL 79

                         90
                 ....*....|....*.
gi 281361577 117 SSPQPRDSGTYECQVS 132
Cdd:cd05720   80 KDFRKEDEGYYFCSVI 95

First (N-terminal) immunoglobulin (Ig)-like domain of the nectin-like molecules; member of the V-set of Ig superfamily (IgSF) domains; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of the nectin-like molecules Necl-1 (also known as cell adhesion molecule 3 (CADM3)), Necl-2 (CADM1), Necl-3 (CADM2), and similar proteins. At least five nectin-like molecules have been identified (Necl-1 to Necl-5). They all have an extracellular region containing three Ig-like domains, a transmembrane region, and a cytoplasmic region. The N-terminal Ig-like domain of the extracellular region belongs to the V-type subfamily of Ig domains, is essential to cell-cell adhesion, and plays a part in the interaction with the envelope glycoprotein D of various viruses. Necl-1, Necl-2, and Necl-3 have Ca(2+)-independent homophilic and heterophilic cell-cell adhesion activity. Necl-1 is specifically expressed in neural tissue, and is important to the formation of synapses, axon bundles, and myelinated axons. Necl-2 is expressed in a wide variety of tissues and is a putative tumour suppressor gene which is downregulated in aggressive neuroblastoma. Necl-3 accumulates in central and peripheral nervous system tissue and has been shown to selectively interact with oligodendrocytes. This group also contains Class-I MHC-restricted T-cell-associated molecule (CRTAM), whose expression pattern is consistent with its expression in Class-I MHC-restricted T-cells.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361577  55 VTATVGQAALLHCRVRNLGDRAVSWIRKRDlHILTVGILTYTNDQRFQSLHSEGSdEWTLRISSPQPRDSGTYECQVSTE 134
Cdd:cd05717    6 VTVVEGETLTLKCQVSLRDDSSLQWLNPNG-QTIYFNDKRALRDSRYQLLNHSAS-ELSISVSNVTLSDEGVYTCLHYTD 83

                 .
gi 281361577 135 P 135
Cdd:cd05717   84 P 84

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281361577 158 LFIKSGSDINLTClamqsPV---PPSFIYWYKGKRVMNYSQRgginVITERSTRTSKLLIAKATPADSGNYT 226
Cdd:cd05748    2 IVVRAGESLRLDI-----PIkgrPTPTVTWSKDGQPLKETGR----VQIETTASSTSLVIKNAKRSDSGKYT 64

C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361577  89 TVGILTYTNDQRF---QSLHSEGSDEWTLRISSP---QPRdsgtyECQV-------STEPKISQGF-----RLNVVVSRA 150
Cdd:cd18808   83 SIGVITPYRAQVAlirELLRKRGGLLEDVEVGTVdnfQGR-----EKDViilslvrSNESGGSIGFlsdprRLNVALTRA 157

                         90
                 ....*....|....*.
gi 281361577 151 K----ILGNAELFIKS 162
Cdd:cd18808  158 KrgliIVGNPDTLSKD 173