E3 ubiquitin-protein ligase RNF152 C-terminus; This family represents the C-terminal region of the E3 ubiquitin ligase RNF152 containing the hydrophobic transmembrane domain, responsible for the lysosomal localization of the protein as well as its ubiquitination activity. This protein polyubiquitinates several proteins and itself, which leads to proteasome degradation. It has been shown that RNF152 has also pro-apoptotic activity, dependent on its RING finger and transmembrane domains. In addition, the transmembrane domain of RNF152 is necessary for negative regulation of the mTORC1 pathway in an amino-acid-sensitive manner, as it mediates RNF152-RagA interaction and RagA ubiquitination.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729262  67 SQLPDDPEVLAVIAIPHTSEHTPVFIKLPSNGCYMLPLPISKERTLLPGDMGCRLLPGSQQKSLTVVTIPaEQQPLQGGA 146
Cdd:pfam19325   1 SQLPDDPDVLAVISVPHTSEHTPVFIRLPSNGCYMLPLPVSKEGALLPGDLGCRLLPGSQQKSVGVVTIA-EQQPLQGHD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039729262 147 PPEAVEEEPDRRGVVKSSTWSGVCTVILVACVLVFLLGIVLHNMSCISKRFTVISCG 203
Cdd:pfam19325  80 GLEAGEEEGERRGGVKSSTWTGVCTVILVACVLLFLLGIVLHNMSCISKRFTVISCG 136

E3 ubiquitin-protein ligase RNF152 C-terminus; This family represents the C-terminal region of the E3 ubiquitin ligase RNF152 containing the hydrophobic transmembrane domain, responsible for the lysosomal localization of the protein as well as its ubiquitination activity. This protein polyubiquitinates several proteins and itself, which leads to proteasome degradation. It has been shown that RNF152 has also pro-apoptotic activity, dependent on its RING finger and transmembrane domains. In addition, the transmembrane domain of RNF152 is necessary for negative regulation of the mTORC1 pathway in an amino-acid-sensitive manner, as it mediates RNF152-RagA interaction and RagA ubiquitination.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729262  67 SQLPDDPEVLAVIAIPHTSEHTPVFIKLPSNGCYMLPLPISKERTLLPGDMGCRLLPGSQQKSLTVVTIPaEQQPLQGGA 146
Cdd:pfam19325   1 SQLPDDPDVLAVISVPHTSEHTPVFIRLPSNGCYMLPLPVSKEGALLPGDLGCRLLPGSQQKSVGVVTIA-EQQPLQGHD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039729262 147 PPEAVEEEPDRRGVVKSSTWSGVCTVILVACVLVFLLGIVLHNMSCISKRFTVISCG 203
Cdd:pfam19325  80 GLEAGEEEGERRGGVKSSTWTGVCTVILVACVLLFLLGIVLHNMSCISKRFTVISCG 136

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1039729262   7 DSLLECQICFNYYsprRRPKLLDCKHTCCSVCLQqmRTSQKDVRCPWCR 55
Cdd:TIGR00599  24 DTSLRCHICKDFF---DVPVLTSCSHTFCSLCIR--RCLSNQPKCPLCR 67

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1039729262   7 DSLLECQICFNYYsprRRPKLLDCKHTCCSVCLQQMRTSQKDvrCPWCR 55
Cdd:COG5432    23 DSMLRCRICDCRI---SIPCETTCGHTFCSLCIRRHLGTQPF--CPVCR 66

E3 ubiquitin-protein ligase RNF152 C-terminus; This family represents the C-terminal region of the E3 ubiquitin ligase RNF152 containing the hydrophobic transmembrane domain, responsible for the lysosomal localization of the protein as well as its ubiquitination activity. This protein polyubiquitinates several proteins and itself, which leads to proteasome degradation. It has been shown that RNF152 has also pro-apoptotic activity, dependent on its RING finger and transmembrane domains. In addition, the transmembrane domain of RNF152 is necessary for negative regulation of the mTORC1 pathway in an amino-acid-sensitive manner, as it mediates RNF152-RagA interaction and RagA ubiquitination.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729262  67 SQLPDDPEVLAVIAIPHTSEHTPVFIKLPSNGCYMLPLPISKERTLLPGDMGCRLLPGSQQKSLTVVTIPaEQQPLQGGA 146
Cdd:pfam19325   1 SQLPDDPDVLAVISVPHTSEHTPVFIRLPSNGCYMLPLPVSKEGALLPGDLGCRLLPGSQQKSVGVVTIA-EQQPLQGHD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039729262 147 PPEAVEEEPDRRGVVKSSTWSGVCTVILVACVLVFLLGIVLHNMSCISKRFTVISCG 203
Cdd:pfam19325  80 GLEAGEEEGERRGGVKSSTWTGVCTVILVACVLLFLLGIVLHNMSCISKRFTVISCG 136

RING finger, HC subclass, found in RING finger protein RNF183, RNF223, RNF225 and similar proteins; RNF183 is an E3 ubiquitin-protein ligase that is upregulated during intestinal inflammation and is negatively regulated by miR-7. It promotes intestinal inflammation by increasing the ubiquitination and degradation of inhibitor of kappa B, thereby resulting in secondary activation of the Nuclear factor-kappaB (NF-kB) pathway. The interaction between RNF183-mediated ubiquitination and miRNA may be an important novel epigenetic mechanism in the pathogenesis of inflammatory bowel disease (IBD). The biological function of RNF223 and RNF225 remains unclear. Members of this family contain an N-terminal C3HC4-type RING-HC finger.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039729262  10 LECQICFNYYSPR-RRPKLLDCKHTCCSVCLQQM----RTSQKDVRCPWCRGITKLP 61
Cdd:cd16556     1 LECSICFSSYDNTfKTPKLLDCGHTFCLECLARLslasPPQAERVPCPLCRQPTVLP 57

RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar proteins; TRIM32, also known as 72 kDa Tat-interacting protein, zinc finger protein HT2A, or BBS11, is an E3 ubiquitin-protein ligase that promotes degradation of several targets, including actin, PIASgamma, Abl interactor 2, dysbindin, X-linked inhibitor of apoptosis (XIAP), p73 transcription factor, thin filaments and Z-bands during fasting. It plays important roles in neuronal differentiation of neural progenitor cells, as well as in controlling cell fate in skeletal muscle progenitor cells. It reduces PI3K-Akt-FoxO signaling in muscle atrophy by promoting plakoglobin-PI3K dissociation. It also functions as a pluripotency-reprogramming roadblock that facilitates cellular transition towards differentiation by modulating the levels of Oct4 and cMyc. Moreover, TRIM32 is an intrinsic influenza A virus (IAV) restriction factor which senses and targets the polymerase basic protein 1 (PB1) for ubiquitination and protein degradation. It also plays a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo, binds specifically to the activation domain of HIV-1 Tat, and can also interact with the HIV-2 and EIAV Tat proteins in vivo. Furthermore, TRIM32 regulates myoblast proliferation by controlling turnover of NDRG2 (N-myc downstream-regulated gene). It negatively regulates tumor suppressor p53 to promote tumorigenesis. It also facilitates degradation of MYCN on spindle poles and induces asymmetric cell division in human neuroblastoma cells. In addition, TRIM32 plays important roles in regulation of hyperactivities and positively regulates the development of anxiety and depression disorders induced by chronic stress. It also plays a role in regeneration by affecting satellite cell cycle progression via modulation of the SUMO ligase PIASy (PIAS4). Defects in TRIM32 leads to limb-girdle muscular dystrophy type 2H (LGMD2H), sarcotubular myopathies (STM) and Bardet-Biedl syndrome. TRIM32 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The NHL domain mediates the interaction with Argonaute proteins and consequently allows TRIM32 to modulate the activity of certain miRNAs.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039729262  10 LECQICFNYYSP-RRRPKLLDCKHTCCSVCLQQMR--TSQKDVRCPWCRGI 57
Cdd:cd16587     1 LECPICLESFDEgQLRPKLLHCGHTICEQCLEKLLasLSINGVRCPFCRKV 51

RING finger, HC subclass, found in SH3 domain-containing RING finger protein 2 (SH3RF2) and similar proteins; SH3RF2, also known as heart protein phosphatase 1-binding protein (HEPP1), plenty of SH3s (POSH)-eliminating RING protein (POSHER), protein phosphatase 1 regulatory subunit 39, or RING finger protein 158 (RNF158), is a putative E3 ubiquitin-protein ligase that acts as an anti-apoptotic regulator for the c-Jun N-terminal kinase (JNK) pathway by binding to and promoting the proteasomal degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal C3HC4-type RING-HC finger responsible for the E3 ligase activity and four Src Homology 3 (SH3) domains, which are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1039729262  10 LECQICFNYYSPRrrPKLLDCKHTCCSVCLQQMRTSQKDVRCPWCR 55
Cdd:cd16749     1 LECPVCFEKLDVT--AKVLPCQHTFCKPCLQRIFKARKELRCPECR 44

RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and similar proteins; NHL-1 functions as an E3 ubiquitin-protein ligase in the presence of both UBC-13 and UBC-1 within the ubiquitin pathway of Caenorhabditis elegans. It acts in chemosensory neurons to promote stress resistance in distal tissues by the transcription factor DAF-16 activation but is dispensable for the activation of heat shock factor 1 (HSF-1). NHL-1 belongs to the TRIM (tripartite motif)-NHL family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as an NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039729262   7 DSLLECQICFNYYsprRRPKLLDCKHT-CCSVCLQQM-RTSQKDVRCPWCR 55
Cdd:cd16524     3 EQLLTCPICLDRY---RRPKLLPCQHTfCLSPCLEGLvDYVTRKLKCPECR 50

RING finger, HC subclass, found in RING finger protein 186 (RNF186) and similar proteins; RNF186 is an E3 ubiquitin-protein ligase with an N-terminal C3HC4-type RING-HC finger and two putative C-terminal transmembrane domains which enable it to localize in a certain organelle. It regulates RING-dependent self-ubiquitination, as well as endoplasmic reticulum (ER) stress-mediated apoptosis through interaction with the Bcl-2 family protein BNip1.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039729262  10 LECQICFNYYS-PRRRPKLLDCKHTCCSVCLQQMRTSQKD---VRCPWCR 55
Cdd:cd16557     2 LECLVCRNPYScFVRKPKLLACQHAFCAICLKLILCEQDGtwsVTCPLCR 51

RING finger, HC subclass, found in Arabidopsis thaliana protein KEEP ON GOING (KEG) and similar proteins; KEG, also called RING-type E3 ubiquitin transferase KEG, is a RING E3 ubiquitin-protein ligase that mediates E2-dependent protein ubiquitination. It is essential for Arabidopsis growth and development. It acts as a negative regulator of abscisic acid signaling. It is required for ABSCISIC ACID-INSENSITIVE5 (ABI5) degradation, by mediating its ubiquitination. Together with EDR1, KEG may regulate endocytic trafficking and/or the formation of signaling complexes on trans-Golgi network (TGN)/ early endosome (EE) vesicles during stress responses. KEG is a multidomain protein that includes a C3HC4-type RING-HC finger, a kinase domain, ankyrin repeats, and 12 HERC2-like (for HECT and RCC1-like) repeats.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039729262  11 ECQIC-FNYYSPRRRPKLLDCKHTCCSVCLQQM--RTSQKDVRCPWCRGITK 59
Cdd:cd23140     3 ECSVCsEGYNEDERVPLLLQCGHTFCKDCLSQMfiRCTDLTLKCPRCRQSVL 54

zinc-RING finger domain;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1039729262  11 ECQICFNYYSPRRRPKLLDCKHTCCSVCLQQMrtsQKDVRCPWCR 55
Cdd:pfam14634   1 HCNKCFKELSKTRPFYLTSCGHIFCEECLTRL---LQERQCPICK 42

RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated protein 1 (ScPSH1) and similar proteins; ScPSH1 is a Cse4-specific E3 ubiquitin ligase that interacts with the kinetochore protein Pat1 and targets the degradation of budding yeast centromeric histone H3 variant, CENP-ACse4, which is essential for faithful chromosome segregation. ScPSH1 contains a C3HC4-type RING-HC finger and a DNA directed RNA polymerase domain.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1039729262   8 SLLECQICFNYYSprrRPKLLDCKHTCCSVCLQQMRTSQKDVRCPWCR 55
Cdd:cd16568     3 ETQECIICHEYLY---EPMVTTCGHTYCYTCLNTWFKSNRSLSCPDCR 47

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1039729262   7 DSLLECQICFNYYsprRRPKLLDCKHTCCSVCLQQMRTSQKDvrCPWCR 55
Cdd:COG5432    23 DSMLRCRICDCRI---SIPCETTCGHTFCSLCIRRHLGTQPF--CPVCR 66

RING finger, HC subclass, found in RING finger protein 208 (RNF208) and similar proteins; RNF208 is an E3 ubiquitin-protein ligase whose activity can be modulated by S-nitrosylation. It contains a C3HC4-type RING-HC finger.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039729262  10 LECQIC-FNYYSPRRRPKLLDCKHTCCSVCLQQM---RTSQKDVRCPWCRGITKL 60
Cdd:cd16559     2 LLCPTCgHSYNFTNKRPRILSCLHSVCEECLQILyesCPKYKFISCPTCKRETVL 56

RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar proteins; TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5, enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into the development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. TRIM65 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729262  10 LECQICFNYYsprRRPKLLDCKHTCCSVCLQQM--RTSQKDVRCPWCRGITKLPPG 63
Cdd:cd16609     4 LTCSICLGLY---QDPVTLPCQHSFCRACIEDHwrQKDEGSFSCPECRAPFPEGPT 56

RING finger, HC subclass, found in promyelocytic leukemia protein (PML) and similar proteins; Protein PML, also known as RING finger protein 71 (RNF71) or tripartite motif-containing protein 19 (TRIM19), is predominantly a nuclear protein with a broad intrinsic antiviral activity. It is the eponymous component of PML nuclear bodies (PML NBs) and has been implicated in a wide variety of cell processes, including DNA damage signaling, apoptosis, and transcription. PML interferes with the replication of many unrelated viruses, including human immunodeficiency virus 1 (HIV-1), human foamy virus (HFV), poliovirus, influenza virus, rabies virus, EMCV, adeno-associated virus (AAV), and vesicular stomatitis virus (VSV). It also selectively interacts with misfolded proteins through distinct substrate recognition sites and conjugates these proteins with the small ubiquitin-like modifiers (SUMOs) through its SUMO ligase activity. PML belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1039729262  10 LECQICFNYYsprRRPKLLDCKHTCCSVCLQQM---RTSQKDVRCPWCR 55
Cdd:cd16579     5 LRCPGCKAEY---KCPKLLPCLHTVCSGCLEALaeqASETTEFQCPICK 50

RING finger, HC subclass, found in the family of RING finger proteins RNF19A, RNF19B and similar proteins; The family includes RING finger protein RNF19A and RNF19B, both of which are transmembrane (TM) domain-containing RBR-type E3 ubiquitin-protein ligases. RNF19A, also known as double ring-finger protein (Dorfin) or p38, localizes to the ubiquitylated inclusions in Parkinson's disease (PD), dementia with Lewy bodies, multiple system atrophy, and amyotrophic lateral sclerosis (ALS). It interacts with Psmc3, a protein component of the 19S regulatory cap of the 26S proteasome, and further participates in the ubiquitin-proteasome system in acrosome biogenesis, spermatid head shaping, and development of the head-tail coupling apparatus and tail. It modulates the ubiquitination and degradation of calcium-sensing receptor (CaR), which may contribute to a general mechanism for CaR quality control during biosynthesis. Moreover, RNF19A can also ubiquitylate mutant superoxide dismutase 1 (SOD1), the causative gene of familial ALS. It may associate with endoplasmic reticulum-associated degradation (ERAD) pathway, which is related to the pathogenesis of neurodegenerative disorders, such as PD or Alzheimer's disease. RNF19B, also known as IBR domain-containing protein 3 or natural killer lytic-associated molecule (NKLAM), plays a role in controlling tumor dissemination and metastasis. It is involved in the cytolytic function of natural killer (NK) cells and cytotoxic T lymphocytes (CTLs). It interacts with ubiquitin conjugates UbcH7 and UbcH8, and ubiquitinates uridine kinase like-1 (URKL-1) protein, targeting it for degradation. Moreover, RNF19B is a novel component of macrophage phagosomes and plays a role in macrophage anti-bacterial activity. It functions as a novel modulator of macrophage inducible nitric oxide synthase (iNOS) expression. Both RNF19A and RNF19B contain an RBR domain followed by three TMs. The RBR domain was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039729262  10 LECQICFNYYSPRRRPKLLDCKHTCCSVCLQQ-----MRTSQKDVRCPWC 54
Cdd:cd16629     1 LECPLCLDDLSPEFFPILLSCEHRSCRDCLRQyltieISESRVNISCPEC 50

RING finger, HC subclass, found in SH3 domain-containing RING finger proteins SH3RF1, SH3RF2, SH3RF3, and similar proteins; SH3RF1, also known as plenty of SH3s (POSH), RING finger protein 142 (RNF142), or SH3 multiple domains protein 2 (SH3MD2), is a trans-Golgi network-associated pro-apoptotic scaffold protein with E3 ubiquitin-protein ligase activity. SH3RF2, also known as heart protein phosphatase 1-binding protein (HEPP1), plenty of SH3s (POSH)-eliminating RING protein (POSHER), protein phosphatase 1 regulatory subunit 39, or RING finger protein 158 (RNF158), is a putative E3 ubiquitin-protein ligase that acts as an anti-apoptotic regulator for the c-Jun N-terminal kinase (JNK) pathway by binding to and promoting the proteasomal degradation of SH3RF1 (or POSH) that is required for pro-apoptotic JNK activation. SH3RF3, also known as plenty of SH3s 2 (POSH2) or SH3 multiple domains protein 4 (SH3MD4), is a scaffold protein with E3 ubiquitin-protein ligase activity. It was identified in the screen for interacting partners of p21-activated kinase 2 (PAK2) and may play a role in regulating c-Jun N-terminal kinase (JNK) mediated apoptosis in certain conditions. Members of this subfamily contain an N-terminal C3HC4-type RING-HC finger responsible for the E3 ligase activity and four Src Homology 3 (SH3) domains, which are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1039729262  10 LECQICFNYYSprRRPKLLDCKHTCCSVCLQQMRTSQKDVRCPWCR 55
Cdd:cd16570     1 LECPVCLERLD--VSAKVLPCQHTFCKRCLQIIVASRGELRCPECR 44

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1039729262   12 CQICFNYYSprRRPKLLDCKHTCCSVCLQQMRTSqKDVRCPWC 54
Cdd:smart00184   1 CPICLEEYL--KDPVILPCGHTFCRSCIRKWLES-GNNTCPIC 40