START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626   1 MDYKAIAQQTAEQVLAYNQDLSGWKLIKSSKKVTVSSKTSRIFHGNLYRVEGIIPESAAHLSDFLFKHDHRVSWDKSLKG 80
Cdd:cd08904    1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPEHRIKWDKSLQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626  81 FNVIHKIDSDTLICHTITQSFAMGSISPRDFIDLVHIKHYERNVDIISTKSVDFPGYAPTSTYIRGFNHPSGYVCSPLKE 160
Cdd:cd08904   81 YKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 148677626 161 NPAYSKLVIFVQTEMKGKLPASVIEKSMPSNLVSFLLNVKDGVK 204
Cdd:cd08904  161 NPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204

Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD6 and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD6 is expressed in male germ cells of normal rats, and in the steroidogenic Leydig cells of perinatal hypothyroid testes. It may play a pivotal role in the steroidogenesis as well as in the spermatogenesis of normal rats. STARD6 has also been detected in the rat nervous system, and may participate in neurosteroid synthesis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626   1 MDYKAIAQQTAEQVLAYNQDLSGWKLIKSSKKVTVSSKTSRIFHGNLYRVEGIIPESAAHLSDFLFKHDHRVSWDKSLKG 80
Cdd:cd08904    1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPEHRIKWDKSLQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626  81 FNVIHKIDSDTLICHTITQSFAMGSISPRDFIDLVHIKHYERNVDIISTKSVDFPGYAPTSTYIRGFNHPSGYVCSPLKE 160
Cdd:cd08904   81 YKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 148677626 161 NPAYSKLVIFVQTEMKGKLPASVIEKSMPSNLVSFLLNVKDGVK 204
Cdd:cd08904  161 NPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204

in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626    23 GWKLIKSSKK--VTVSSKTSRIFHGNLYRVEGIIPESAAHLS-DFLFKHDHRVSWDKSLKGFNVIHKIDSDTLICHtITQ 99
Cdd:smart00234  19 GWVLSSENENgdEVRSIFSPGRKPGEAFRLVGVVPMVCADLVeELMDDLEYRPEWDKNVAKAETLEVIDNGTVIYH-YVS 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626   100 SFAMGSISPRDFIDLVHIKHYERNVDIISTKSVDFPGYAPTSTYIRGFNHPSGYVCSPLKENPaySKLVIFVQTEMKGKL 179
Cdd:smart00234  98 KFAAGPVSPRDFVFVRYWREDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGP--SKVTWVSHADLKGWL 175

                          170
                   ....*....|....*..
gi 148677626   180 PASVIEKSMPSNLVSFL 196
Cdd:smart00234 176 PHWLVRSLIKSGLAEFA 192

Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD6 and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD6 is expressed in male germ cells of normal rats, and in the steroidogenic Leydig cells of perinatal hypothyroid testes. It may play a pivotal role in the steroidogenesis as well as in the spermatogenesis of normal rats. STARD6 has also been detected in the rat nervous system, and may participate in neurosteroid synthesis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626   1 MDYKAIAQQTAEQVLAYNQDLSGWKLIKSSKKVTVSSKTSRIFHGNLYRVEGIIPESAAHLSDFLFKHDHRVSWDKSLKG 80
Cdd:cd08904    1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPEHRIKWDKSLQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626  81 FNVIHKIDSDTLICHTITQSFAMGSISPRDFIDLVHIKHYERNVDIISTKSVDFPGYAPTSTYIRGFNHPSGYVCSPLKE 160
Cdd:cd08904   81 YKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 148677626 161 NPAYSKLVIFVQTEMKGKLPASVIEKSMPSNLVSFLLNVKDGVK 204
Cdd:cd08904  161 NPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204

Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD5, and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD5 is ubiquitously expressed, with highest levels in liver and kidney. STARD5 functions in the kidney within the proximal tubule cells where it is associated with the Endoplasmic Reticulum (ER), and may participate in ER-associated cholesterol transport. It binds cholesterol and 25-hydroxycholesterol. Expression of the gene encoding STARD5 is increased by ER stress, and its mRNA and protein levels are elevated in a type I diabetic mouse model of human diabetic nephropathy.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626   1 MDYKAIAQQTAEQVLAYNQDLSGWKLIKSSKKVTVSSKTSRIFHGNLYRVEGIIPESAAHLSDFL--FKHDHRVSWDKSL 78
Cdd:cd08903    1 MDYAELAESVADKMLLYRRDESGWKTCRRTNEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLkpAAGGLRVKWDQNV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626  79 KGFNVIHKIDSDTLICHTITQSFAMGSISPRDFIDLVHIKHYERNVDIISTKSVDFPGYAPTSTYIRGFNHPSGYVCSPL 158
Cdd:cd08903   81 KDFEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSNATNVEHPLCPPQAGFVRGFNHPCGCFCEPV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 148677626 159 KENPAYSKLVIFVQTEMKGKLPASVIEKSMPSNLVSFLLNVKDGVK 204
Cdd:cd08903  161 PGEPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAVK 206

Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and STARD3 (also known as metastatic lymph node 64/MLN64). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. This STARD1-like subfamily has a high affinity for cholesterol. STARD1/StAR can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads. STARD3 may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626   5 AIAQQTAEQVLAynqdLSGWKLIKSSKK-VTVSSKTSRiFHGNLYRVEGIIPESAAHLSDFLFKHDHR-VSWDKSLKGFN 82
Cdd:cd08868   11 AEALARAWSILT----DPGWKLEKNTTWgDVVYSRNVP-GVGKVFRLTGVLDCPAEFLYNELVLNVESlPSWNPTVLECK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626  83 VIHKIDSDTLICHTITQSFAMGSISPRDFIDLVHIKhYERNVDIISTKSVDFPGYAPTSTYIRGFNHPSGYVCSPLKENP 162
Cdd:cd08868   86 IIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWG-IRENCYLSSGVSVEHPAMPPTKNYVRGENGPGCWILRPLPNNP 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 148677626 163 AYSKLVIFVQTEMKGKLPASVIEKSMPSNLVSFLLNVKDGVKT 205
Cdd:cd08868  165 NKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRKRIAT 207

START domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626    8 QQTAEQVLAYNQDLS--GWKLIKSSKKVTVSSKTSRIFHGNLYRVEGIIPESAAHL-SDFLFKHDHRVSWDKSLKGFNVI 84
Cdd:pfam01852   3 AEEAAQELLKLALSDepGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLvAELLKDMEYRAQWDKDVRSAETL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626   85 HKIDSDTLICHTITQSFAMGSISPRDFIDLVHIKHYERNVDIISTKSVDFPGYAPTSTYIRGFNHPSGYVCSPLKENpaY 164
Cdd:pfam01852  83 EVISSGGDLQYYVAALVAPSPLSPRDFVFLRYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNG--P 160

                         170       180
                  ....*....|....*....|....*....
gi 148677626  165 SKLVIFVQTEMKGKLPA----SVIEKSMP 189
Cdd:pfam01852 161 SKVTWVSHADLKGWLPSwllrSLYKSGMP 189

Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD3 (also known as metastatic lymph node 64/MLN64) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD3 has a high affinity for cholesterol. It may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626  12 EQVLAYNQDlsgWKLIKSSKKVTVSSKTSRIFHGNLYRVEGIIPESAAHL-SDFLFKHDHRVSWDKSLKGFNVIHKIDSD 90
Cdd:cd08906   18 EQILAQEEN---WKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVyQEVILQPEKMVLWNKTVSACQVLQRVDDN 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626  91 TLICHTITQSFAMGSISPRDFidlVHIKHYERNVD--IISTKSVDFPGYAPTSTYIRGFNHPSGYVCSPLKENPAYSKLV 168
Cdd:cd08906   95 TLVSYDVAAGAAGGVVSPRDF---VNVRRIERRRDryVSAGISTTHSHKPPLSKYVRGENGPGGFVVLKSASNPSVCTFI 171

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 148677626 169 IFVQTEMKGKLPASVIEKSMPSNLVSFLLNVKDGVK 204
Cdd:cd08906  172 WILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRIR 207

Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD10 (also known as CGI-52, PTCP-like, and SDCCAG28). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD10 binds phophatidylcholine and phosphatidylethanolamine. This protein is widely expressed and is synthesized constitutively in many organs. It may function in the liver in the export of phospholipids into bile. It is concentrated in the sperm flagellum, and may play a role in energy metabolism. In the mammary gland it may participate in the enrichment of lipids in milk, and be a potential marker of differentiation. Its expression is induced in this gland during gestation and lactation. It is overexpressed in mammary tumors from Neu/ErbB2 transgenic mice, in several breast carcinoma cell lines, and in 35% of primary human breast cancers, and may cooperate with c-erbB receptor signaling in breast oncogenesis. It is a potential marker of disease outcome in breast cancer; loss of STARD10 expression in breast cancer strongly predicts an aggressive disease course. The lipid transfer activity of STRAD10 is downregulated by phosphorylation of its Ser284 by CK2 (casein kinase 2).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626  19 QDLSGWKLIKSSKKVTVSSKTSRIFHGNLYRVEGIIPE-SAAHLSDFLFKHDHRVSWDKS-LKGFNvIHKIDSDTLICHt 96
Cdd:cd08871   20 DSTDGWKLKYNKNNVKVWTKNPENSSIKMIKVSAIFPDvPAETLYDVLHDPEYRKTWDSNmIESFD-ICQLNPNNDIGY- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626  97 itQSFAMGS-ISPRDFIDLVHIKHYERNVDIISTkSVDFPGYAPTSTYIRGFNHPSGYVCSPLKENPaySKLVIFVQTEM 175
Cdd:cd08871   98 --YSAKCPKpLKNRDFVNLRSWLEFGGEYIIFNH-SVKHKKYPPRKGFVRAISLLTGYLIRPTGPKG--CTLTYVTQNDP 172

                        170
                 ....*....|...
gi 148677626 176 KGKLPASVIEKSM 188
Cdd:cd08871  173 KGSLPKWVVNKAT 185

Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian brown fat-inducible STARD14 (also known as Acyl-Coenzyme A Thioesterase 11 or ACOT11, BFIT, THEA, THEM1, KIAA0707, and MGC25974) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD14/ACOT11 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Human STARD14 displays acetyl-CoA thioesterase activity towards medium(C12)- and long(C16)-chain fatty acyl-CoA substrates. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. There are two splice variants of human STARD14, named BFIT1 and BFIT2, which differ in their C-termini. Human BFIT2 is equivalent to mouse mBFIT/Acot11, whose transcription is increased two fold in obesity-resistant mice compared with obesity-prone mice.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626  15 LAYNqDLSGWKLIKSSKKVTVSSKTSRIFHGNL-------YRVEGIIPESAAHLSDFLFKHDHRVSWDKSLKGFNVIHKI 87
Cdd:cd08913   44 LSYN-NVSALKMLVAKDNWVLSSEKNQVRLYTLeedkflsFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQV 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626  88 DSDTLICHTITQSFAMGSiSPRDFIDLVHIKHYERNVD--IISTKSVDFPGYAPTSTYIRGFNHPSGYVCSPLKE----- 160
Cdd:cd08913  123 DEDDAIYHVTSPSLSGHG-KPQDFVILASRRKPCDNGDpyVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDqltkv 201

                        170       180
                 ....*....|....*....|
gi 148677626 161 ---NPAYSKLVIFVQTEMKG 177
Cdd:cd08913  202 syyNQATPGVLPYISTDIAG 221

Ceramide-binding START domain of mammalian STARD11 and related domains; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD11 and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD11 can mediate transfer of the natural ceramide isomers, dihydroceramide and phytoceramide, as well as ceramides having C14, C16, C18, and C20 chains. They can also transfer diacylglycerol, but with a lower efficiency. STARD11 is synthesized from two major transcripts: a larger one encoding Goodpasture antigen-binding protein (GPBP)/ceramide transporter long form (CERTL); and a smaller one encoding GPBPdelta26/CERT, which is deleted for 26 amino acids. Both splicing variants mediate ceramide transfer from the ER to the Golgi, in a non-vesicular manner. It is likely that these two carry out different functions in specific sub-cellular locations. These proteins have roles in brain homeostasis and disease processes. GPBP/CERTL exists in multiple isoforms originating from alternative translation initiation sites and post-translational modifications. Goodpasture syndrome is a human disorder caused by antibodies directed against the a3-chain of collagen type IV. GPBP/CERTL binds and phosphorylates this antigen. The human gene encoding STARD11 is referred to as COL4A3BP referring to its collagen binding function. It is unknown whether the ceramide-transfer function of GPBP/CERTL is related to this collagen interaction. The expression of GPBP/CERTL is elevated in these and other spontaneous autoimmune disorders including cutaneous lupus erythematosus, pemphigoid, and lichen planus. GPBL/CERTL contains an N-terminal pleckstrin homology domain (PH), which targets the protein to the Golgi, a middle region containing two serine-rich domains (SR1, SR2), a FFAT (two phenylalanine amino acids in an acidic tract) motif which is involved in endoplasmic reticulum targeting, and this C-terminal SMART domain. The shorter splicing variant, CERT, lacks the SR2 domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677626  50 VEGIIPESAAHlsdFLFKHDHRVSWDKSLKGFNVIHKIDSDTLICHTItqsfaMGSI---SPRDFIDLVHIKHYERNVD- 125
Cdd:cd08872   60 VKGVTGHEVCH---YFFDPDVRMDWETTLENFHVVETLSQDTLIFHQT-----HKRVwpaAQRDALFVSHIRKIPALEEp 131

                         90       100
                 ....*....|....*....|....*.
gi 148677626 126 ------IISTKSVDFPGYAPTSTYIR 145
Cdd:cd08872  132 nahdtwIVCNFSVDHDSAPLNNKCVR 157