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 1958742585   1 MDYKAIAQQSAEQVLAYNQDLSGWKVVKTSKKVTVSSKASKLFQGNLYRIEGVIPELPAHLSDFLYKSEHRVSWDKSLKA 80
Cdd:cd08904     1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPEHRIKWDKSLQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742585  81 FNMIHKIDSDTLICHTITQSFAMGSISPRDFIDLVHIKHQDGNMDIISTRSVEFPGYPPTSHYIRGYNHPSGYVCSPLKD 160
Cdd:cd08904    81 YKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPE 160

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 1958742585   1 MDYKAIAQQSAEQVLAYNQDLSGWKVVKTSKKVTVSSKASKLFQGNLYRIEGVIPELPAHLSDFLYKSEHRVSWDKSLKA 80
Cdd:cd08904     1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPEHRIKWDKSLQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742585  81 FNMIHKIDSDTLICHTITQSFAMGSISPRDFIDLVHIKHQDGNMDIISTRSVEFPGYPPTSHYIRGYNHPSGYVCSPLKD 160
Cdd:cd08904    81 YKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPE 160

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 1958742585   48 YRIEGVIPELPAHLS-DFLYKSEHRVSWDKSLKAFNMIHKIDSDTLICHtITQSFAMGSISPRDFIDLVHIKHQDGNMDI 126
Cdd:smart00234  46 FRLVGVVPMVCADLVeELMDDLEYRPEWDKNVAKAETLEVIDNGTVIYH-YVSKFAAGPVSPRDFVFVRYWREDEDGSYA 124

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958742585  127 ISTRSVEFPGYPPTSHYIRGYNHPSGYVCSPLKDP 161
Cdd:smart00234 125 VVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNG 159

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 1958742585   1 MDYKAIAQQSAEQVLAYNQDLSGWKVVKTSKKVTVSSKASKLFQGNLYRIEGVIPELPAHLSDFLYKSEHRVSWDKSLKA 80
Cdd:cd08904     1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPEHRIKWDKSLQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742585  81 FNMIHKIDSDTLICHTITQSFAMGSISPRDFIDLVHIKHQDGNMDIISTRSVEFPGYPPTSHYIRGYNHPSGYVCSPLKD 160
Cdd:cd08904    81 YKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPE 160

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 1958742585   1 MDYKAIAQQSAEQVLAYNQDLSGWKVVKTSKKVTVSSKASKLFQGNLYRIEGVIPELPAHLSDFLyKSEH---RVSWDKS 77
Cdd:cd08903     1 MDYAELAESVADKMLLYRRDESGWKTCRRTNEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCL-KPAAgglRVKWDQN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742585  78 LKAFNMIHKIDSDTLICHTITQSFAMGSISPRDFIDLVHIK-HQDGNMDIISTrSVEFPGYPPTSHYIRGYNHPSGYVCS 156
Cdd:cd08903    80 VKDFEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKrYEDGTISSNAT-NVEHPLCPPQAGFVRGFNHPCGCFCE 158

                  ..
gi 1958742585 157 PL 158
Cdd:cd08903   159 PV 160

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 1958742585   5 AIAQQSAEQVLAynqdLSGWKVVKTSKK-VTVSSKASKlFQGNLYRIEGVIPELPAHL-SDFLYKSEHRVSWDKSLKAFN 82
Cdd:cd08868    11 AEALARAWSILT----DPGWKLEKNTTWgDVVYSRNVP-GVGKVFRLTGVLDCPAEFLyNELVLNVESLPSWNPTVLECK 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958742585  83 MIHKIDSDTLICHTITQSFAMGSISPRDFIDLVHIKHQdGNMDIISTRSVEFPGYPPTSHYIRGYNHPSGYVCSPLKD 160
Cdd:cd08868    86 IIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIR-ENCYLSSGVSVEHPAMPPTKNYVRGENGPGCWILRPLPN 162

Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD4 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. STARD4 plays an important role in steroidogenesis, trafficking cholesterol into mitochondria. It specifically binds cholesterol, and demonstrates limited binding to another sterol, 7alpha-hydroxycholesterol. STARD4 is ubiquitously expressed, with highest levels in liver and kidney.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742585  24 WKVVKTSKKVTVSSKASKLFQGNLYRIEGVIPELPAHLSDFLYKSEHRVSWDKSLKAFNMIHKIDSDTLICHTITQSFAM 103
Cdd:cd08902    25 WRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRPGPYRLDWDSLMTSMDIIEEFEENCCVMRYTTAGQLL 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958742585 104 GSISPRDFIDLVH-IKHQDGNMDiiSTRSVEFPGYPPtsHYIRGYNHPSGYVCSPLKD 160
Cdd:cd08902   105 NIISPREFVDFSYtTQYEDGLLS--CGVSIEYEEARP--NFVRGFNHPCGWFCVPLKD 158

Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) 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. STARD1 has a high affinity for cholesterol. It 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742585   1 MDYKAIAQQSAEQVLAYNQDLSGWKvvKTSKKVTVSSKASKLFQ--GNLYRIEGVIPELPAHL-SDFLYKSEHRVSWDKS 77
Cdd:cd08905     4 MSYIKQGEEALQKSLSILQDQEGWK--TEIVAENGDKVLSKVVPdiGKVFRLEVVVDQPLDNLySELVDRMEQMGEWNPN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742585  78 LKAFNMIHKIDSDTLICHTITQSFAMGSISPRDFIDLVHIKHQdGNMDIISTRSVEFPGYPPTSHYIRGYNHPSGYVCSP 157
Cdd:cd08905    82 VKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKRR-GSTCVLAGMATHFGLMPEQKGFIRAENGPTCIVLRP 160

                  ...
gi 1958742585 158 LKD 160
Cdd:cd08905   161 LAG 163

Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily 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), STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114), 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. STARD14/ACOT11 and STARD15/ACOT12 are type II acetyl-CoA thioesterases; they catalyze 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. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, STARD14 and STARD15 each 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. Human STARD15 may have roles in cholesterol metabolism and in beta-oxidation.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742585  22 SGWKVVKTSKKVTVSSKASKLFQGnlYRIEgVIPELPAHLS-DFLYKSEHRVSWDKSLKAFNMIHKIDSDTLICHTITQS 100
Cdd:cd08873    55 SDWTVASSTTSVTLYTLEQDGVLS--FCVE-LKVQTCASDAfDLLSDPFKRPEWDPHGRSCEEVKRVGEDDGIYHTTMPS 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958742585 101 faMGSISPRDFIDLVHIKH--QDGNMDIISTRSVEFPGYPPTSHYIRGYNHPSGYV 154
Cdd:cd08873   132 --LTSEKPNDFVLLVSRRKpaTDGDPYKVAFRSVTLPRVPQTPGYSRTEVACAGFV 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 1958742585   9 QSAEQVLAYNqDLSGWKVVKTSKKVTVSSKASKLFQGNL-------YRIEGVIpELPAH-----LSDFLYKSEhrvsWDK 76
Cdd:cd08913    38 PSNQVYLSYN-NVSALKMLVAKDNWVLSSEKNQVRLYTLeedkflsFKVEMVV-HVDAAqafllLSDLRRRPE----WDK 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742585  77 SLKAFNMIHKIDSDTLICHTITQSFAMGSiSPRDFIDLVHIKHQDGNMD--IISTRSVEFPGYPPTSHYIRGYNHPSGYV 154
Cdd:cd08913   112 HYRSCELVQQVDEDDAIYHVTSPSLSGHG-KPQDFVILASRRKPCDNGDpyVIALRSVTLPTHPPTPEYTRGETLCSGFC 190

                  ....*.
gi 1958742585 155 CSPLKD 160
Cdd:cd08913   191 IWEESD 196

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 1958742585  69 EHRVSWDKSLKAFNMIHKIDSDTLICHTItqsfaMGSI---SPRDFIDLVHIKH-------QDGNMDIISTRSVEFPGYP 138
Cdd:cd08872    76 DVRMDWETTLENFHVVETLSQDTLIFHQT-----HKRVwpaAQRDALFVSHIRKipaleepNAHDTWIVCNFSVDHDSAP 150

                  ....*....
gi 1958742585 139 PTSHYIRGY 147
Cdd:cd08872   151 LNNKCVRAK 159

C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38), STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP), and STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13). 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. Proteins belonging to this subfamily also have a RhoGAP domain. Some, including STARD12, -and -13, also have an N-terminal SAM (sterile alpha motif) domain; these have a SAM-RhoGAP-START domain organization. This subfamily is involved in cancer development. A large spectrum of cancers have dysregulated genes encoding these proteins. The precise function of the START domain in this subfamily is unclear.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742585  23 GWKVVKTSKKVTVSSKasKLFQGNLYRIEGVIPELPAHLSDFLykseHRV-----SWDKSLKAFNMIHKIDSDTLICHTI 97
Cdd:cd08869    20 GWVSVSSSDHVELAFK--KVDDGHPLRLWRASTEVEAPPEEVL----QRIlrerhLWDDDLLQWKVVETLDEDTEVYQYV 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958742585  98 TQSfaMGSISPRDFIDL-VHIKHQDGNMDIISTRSVEFPG 136
Cdd:cd08869    94 TNS--MAPHPTRDYVVLrTWRTDLPKGACVLVETSVEHTE 131