EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich in cysteine (SPARC) and similar proteins; This family includes secreted protein acidic and rich in cysteine (SPARC), secreted protein, acidic and rich in cysteine-like 1 (SPARCL1), and similar proteins. SPARC is a prototypic collagen-binding matricellular protein that is involved in extracellular matrix (ECM) assembly and fibrosis through binding both fibrillar collagen and basal lamina collagen IV. It regulates the activity of matrix metalloproteinases (MMPs), as well as the growth factor signaling mediated by cell surface receptors including vascular endothelial growth factor (VEGF) receptor, basic fibroblast growth factor (bFGF), and transforming growth factor (TGF) beta1. It also shows survival activity in tumor progression. SPARC contains an N-terminal acidic 52-residue segment followed by a follistatin-like (FS) domain, and an alpha-helical EC domain with 2 unusual calcium-binding EF-hands and the collagen-binding site. SPARCL1 is the closest family member to SPARC. It shares the three primary domains contained within SPARC with an expanded N-terminal domain. SPARCL1 may function as both a tumor suppressor and as a regulator of angiogenesis. It can bind to collagens and be counter-adhesive to wild-type dermal fibroblasts, but do not influence rates of cell proliferation. Moreover, SPARCL1 can influence central nervous system (CNS) development and synaptic rearrangement.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160369 501 CTDFEVAQFPLRMRDWLKNILMQLYEPNPKHGGYLnekqrskvkkiyldekrllagdhpiELLLRDFKKNYHMYVYPVHW 580
Cdd:cd16231     1 CLDEELSEFPLRMRDWLKNVMVQLAERDELHEGLT-------------------------EKELEDFQKNYKMYVYPVHW 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907160369 581 QFNELDQHPADRILTHSELAPLRASLVPMEHCITRFFEECDPNKDKHITLKEWGHCFGIKE 641
Cdd:cd16231    56 KFCDLDQHPHDRYLSHHELAPLRAPLVPMEHCTTPFLETCDADNDKLISLKEWGACLGLKE 116

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160369  212 GAPSDNQEEGKEPLEEQPTSKWEGNR--EQSDDTLEESSQPTQISKTEKHQSEQGNQGQESDSEAEGEDKAAGSKEHIPH 289
Cdd:TIGR00927  664 GGEAEQEGETETKGENESEGEIPAERkgEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVED 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160369  290 TEQQDQEGKAGLEAIGNQKDTDEKAvstePTDAAVVPRSHGGAGDNGGGDDSKHGAGDDYFIPSQEFLEAERMHSLSYYL 369
Cdd:TIGR00927  744 EGEGEAEGKHEVETEGDRKETEHEG----ETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQS 819

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1907160369  370 KYGGGEETTTGESENRREAADNQ-EAKKAESSPNAE-PSDEGNSRE 413
Cdd:TIGR00927  820 ETQADDTEVKDETGEQELNAENQgEAKQDEKGVDGGgGSDGGDSEE 865

EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich in cysteine (SPARC) and similar proteins; This family includes secreted protein acidic and rich in cysteine (SPARC), secreted protein, acidic and rich in cysteine-like 1 (SPARCL1), and similar proteins. SPARC is a prototypic collagen-binding matricellular protein that is involved in extracellular matrix (ECM) assembly and fibrosis through binding both fibrillar collagen and basal lamina collagen IV. It regulates the activity of matrix metalloproteinases (MMPs), as well as the growth factor signaling mediated by cell surface receptors including vascular endothelial growth factor (VEGF) receptor, basic fibroblast growth factor (bFGF), and transforming growth factor (TGF) beta1. It also shows survival activity in tumor progression. SPARC contains an N-terminal acidic 52-residue segment followed by a follistatin-like (FS) domain, and an alpha-helical EC domain with 2 unusual calcium-binding EF-hands and the collagen-binding site. SPARCL1 is the closest family member to SPARC. It shares the three primary domains contained within SPARC with an expanded N-terminal domain. SPARCL1 may function as both a tumor suppressor and as a regulator of angiogenesis. It can bind to collagens and be counter-adhesive to wild-type dermal fibroblasts, but do not influence rates of cell proliferation. Moreover, SPARCL1 can influence central nervous system (CNS) development and synaptic rearrangement.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160369 501 CTDFEVAQFPLRMRDWLKNILMQLYEPNPKHGGYLnekqrskvkkiyldekrllagdhpiELLLRDFKKNYHMYVYPVHW 580
Cdd:cd16231     1 CLDEELSEFPLRMRDWLKNVMVQLAERDELHEGLT-------------------------EKELEDFQKNYKMYVYPVHW 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907160369 581 QFNELDQHPADRILTHSELAPLRASLVPMEHCITRFFEECDPNKDKHITLKEWGHCFGIKE 641
Cdd:cd16231    56 KFCDLDQHPHDRYLSHHELAPLRAPLVPMEHCTTPFLETCDADNDKLISLKEWGACLGLKE 116

Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40/osteonectin is a multifunctional glycoprotein which modulates cellular interaction with the extracellular matrix by its binding to structural matrix proteins such as collagen and vitronectin. The protein it composed of an N-terminal acidic region, a follistatin (FS) domain and an EF-hand calcium binding domain. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a small hydrophobic core of alpha/beta structure (Kazal domain) and has five disulfide bonds and a conserved N-glycosylation site. The FSL_SPARC domain is a member of the superfamily of kazal-like proteinase inhibitors and follistatin-like proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160369 419 CTNFQCKRGHICKTDPQGKPHCVCQDPetCPPA-KILDQACGTDNQTYASSCHLFATKCRLEGTKKGH------QLQLDY 491
Cdd:cd01328     2 CENHHCGAGKVCEVDDENTPKCVCIDP--CPEEvDDRRKVCTNDNETFDSDCELYRTRCLCKGGKKGCrgpkyqHLHLDY 79

                  ....*..
gi 1907160369 492 FGACKSI 498
Cdd:cd01328    80 YGECKEI 86

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907160369  441 VCqdPETCPpaKILDQACGTDNQTYASSCHLFATKCrlegtKKGHQLQLDYFGAC 495
Cdd:smart00280   1 DC--PEACP--REYDPVCGSDGVTYSNECHLCKAAC-----ESGKSIEVKHDGPC 46

EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich in cysteine (SPARC) and similar proteins; This family includes secreted protein acidic and rich in cysteine (SPARC), secreted protein, acidic and rich in cysteine-like 1 (SPARCL1), and similar proteins. SPARC is a prototypic collagen-binding matricellular protein that is involved in extracellular matrix (ECM) assembly and fibrosis through binding both fibrillar collagen and basal lamina collagen IV. It regulates the activity of matrix metalloproteinases (MMPs), as well as the growth factor signaling mediated by cell surface receptors including vascular endothelial growth factor (VEGF) receptor, basic fibroblast growth factor (bFGF), and transforming growth factor (TGF) beta1. It also shows survival activity in tumor progression. SPARC contains an N-terminal acidic 52-residue segment followed by a follistatin-like (FS) domain, and an alpha-helical EC domain with 2 unusual calcium-binding EF-hands and the collagen-binding site. SPARCL1 is the closest family member to SPARC. It shares the three primary domains contained within SPARC with an expanded N-terminal domain. SPARCL1 may function as both a tumor suppressor and as a regulator of angiogenesis. It can bind to collagens and be counter-adhesive to wild-type dermal fibroblasts, but do not influence rates of cell proliferation. Moreover, SPARCL1 can influence central nervous system (CNS) development and synaptic rearrangement.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160369 501 CTDFEVAQFPLRMRDWLKNILMQLYEPNPKHGGYLnekqrskvkkiyldekrllagdhpiELLLRDFKKNYHMYVYPVHW 580
Cdd:cd16231     1 CLDEELSEFPLRMRDWLKNVMVQLAERDELHEGLT-------------------------EKELEDFQKNYKMYVYPVHW 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907160369 581 QFNELDQHPADRILTHSELAPLRASLVPMEHCITRFFEECDPNKDKHITLKEWGHCFGIKE 641
Cdd:cd16231    56 KFCDLDQHPHDRYLSHHELAPLRAPLVPMEHCTTPFLETCDADNDKLISLKEWGACLGLKE 116

Secreted protein acidic and rich in cysteine Ca binding region; The SPARC_Ca_bdg domain of Secreted Protein Acidic and Rich in Cysteine is responsible for the anti-spreading activity of human urothelial cells. It is rich in alpha-helices. This extracellular calcium-binding domain contains two EF-hands that each coordinates one Ca2+ ion, forming a helix-loop-helix structure that not only drives the conformation of the protein but is also necessary for biological activity. The anti-spreading activity was dependent on the coordination of Ca2+ by a Glu residue at the Z position of EF-hand 2.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160369 499 PACTDFEVAQFPLRMRDWLKNILMQLYEPNPKHggylnekqrskvkkiyldekrllagDHPIELLLRDFKKNYHMYVYPV 578
Cdd:pfam10591   1 PCCTDEELAEFPRRMRDWLKLLLEALRNRRERK-------------------------DHSSTLEKRDESLLYPCCKDPL 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907160369 579 HWQFNELDQHpADRILTHSELAPLRASLVPMEHCITRFFEECDPNKDKHITLKEWGH 635
Cdd:pfam10591  56 GWMFKRLDTN-DDLLLDHEELAPIRAPLKPEEHCIKPFFESCDANKDKLISLEEWCC 111

EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich in cysteine (SPARC)-like proteins; The SPARC protein family represents a diverse group of proteins that share a follistatin-like (FS) domain and an extracellular calcium-binding (EC) domain with two EF-hand motifs. It includes SPARC (for secreted protein acidic and rich in cysteine, also termed osteonectin/ON, or basement-membrane protein 40/BM-40), SPARC-like protein 1 (for secreted protein, acidic and rich in cysteines-like 1/ SPARCL1, also termed high endothelial venule protein/Hevi, or MAST 9, or SC-1, or RAGS-1, or QR1, or ECM 2), testicans 1, 2, and 3 (also termed SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycans, or SPOCK), secreted modular calcium-binding protein SMOC-1 (also termed SPARC-related modular calcium-binding protein 1) and SMOC-2 (also termed SPARC-related modular calcium-binding protein 2, or smooth muscle-associated protein 2/SMAP-2), follistatin-related protein 1 (FRP-1, also termed follistatin-like protein 1/fstl-1, TSC-36/Flik, TGF-beta inducible protein). The SPARC proteins have been implicated in modulating cell interaction with the extracellular milieu, including regulation of extracellular matrix assembly and deposition, counter-adhesion, effects on extracellular protease activity, and modulation of growth factor/cytokine signaling pathways, as well as in development and disease.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160369 501 CTDFEVAQFPLRMRDWLKNILMQLYEPNPkhggylnekqrskvkkiyldekrllagdhpiELLLRDFKKNYHMYVYPVHW 580
Cdd:cd00252     1 CPGSELMQFPDRLLDWLLLLKEQDENRSY-------------------------------DNNKRGHDLSGTMRKEIAQW 49

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907160369 581 QFNELDQhPADRILTHSELAPLRASLVPMEHCITRFFEECDPNKDKHITLKEWGHCFGI 639
Cdd:cd00252    50 EFDNLDN-NKDGKLDKRELAPFRAPLMPLEHCARGFFESCDLNKDKKISLQEWLGCFGV 107

EF-hand, extracellular calcium-binding (EC) motif, found in testicans; Testicans are nervous system-expressed proteoglycans that play important roles in the regulation of protease activity, as well as in the determination of age at menarche. Testican-1 (TICN1, also termed protein SPOCK) is a secreted chimeric proteoglycan that is highly expressed in brain and carries both chondroitin and heparan sulfate glycosaminoglycan side chains. It has been implicated in autoimmune disease. It also acts as a regulator of bone morphogenetic protein (BMP) signaling and show critical functions in the nervous system. Testican-2 (TICN2, also termed protein SPOCK2) is an extracellular heparan sulphate proteoglycan highly expressed in brain. It may play regulatory roles in the development of the central nervous system. It also participates in diverse steps of neurogenesis. TICN1, but not TICN2, inhibits cathepsin L. TICN1 also inhibits attachment and neurite outgrowth in cultures of N2A neuroblastoma cells, While TICN2 is able to inhibit neurite outgrowth from primary cerebellar cells. Testicans contain an N-terminal signal peptide, a testican-specific domain followed by a follistatin-like (FS) domain, an extracellular calcium-binding (EC) domain including a pair of EF hands, a thyroglobulin-like domain (TY), and a C-terminal region with two putative glycosaminoglycan attachment sites. The substitution of a ligating Asp residue by Tyr orTyr in the +Y position of EF hand 2 in testican-2 could prevent Ca2+ binding to this site and also cause EF-hand 1 to bind one Ca2+ with low affinity. The substitution of a ligating Asp residue by Phe or Tyr in the +Y position of EF-hand 2 in testicans could prevent Ca2+ binding to this site and also cause EF-hand 1 to bind one Ca2+ ion with low affinity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907160369 501 CTDFEVAQFPLRMRDWLKNILMQlyepnpkhgGYLNEKQRSKvkkiyldeKRLLAGDHPIellLRDfkknyhmyvyPVHW 580
Cdd:cd16232     1 CTESELSEMGDRLLDWFSVLHEQ---------SNKAKKTSSS--------KRFDKSHLPE---CKP----------SVGW 50

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907160369 581 QFNELDQHpADRILTHSELAPLraSLVPMEHCITRFFEECDPNKDKHITLKEWGHCF 637
Cdd:cd16232    51 MFNQLDTN-NDLHLSQSELYDL--ELDKYEPCIKPFLDSCDRNKDGKISSDEWCDCF 104

EF-hand, extracellular calcium-binding (EC) motif, found in secreted modular calcium-binding protein SMOC-1, SMOC-2, and similar proteins; SMOC proteins corresponds to a group matricellular proteins that are involved in direct or indirect modulation of growth factor signaling pathways and play diverse roles in physiological processes involving extensive tissue remodeling, migration, proliferation, and angiogenesis. They may mediate intercellular signaling and cell type-specific differentiation during gonad and reproductive tract development. SMOC-1 is localized in basement membranes. Its mutations have been found to be associated with individuals with Warrdenburg Anopthalmia Syndrome. SMOC-2 is ubiquitously expressed and is involved in angiogenesis and the regulation of cell cycle progression. It enhances the angiogenic effect of basic fibroblast growth factor (bFGF) and vascular endothelial growth factor (VEGF). It has also been implicated in generalized vitiligo. SMOC proteins consist of a follistatin-like (FS) domain, two thyroglobulin-like (TY) domains, a novel domain conserved only in SMOC proteins, and an extracellular calcium-binding (EC) domain with two EF-hand calcium-binding motifs.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907160369 578 VHWQFNELDQHpADRILTHSELAPLRA---SLVPMEHCITRFFEECDPNKDKHITLKEWGHCFGI 639
Cdd:cd16234    41 LDWKFSQLDKN-KNGVLERKEWKPFKRllkKAVKPKKCARKFPKYCDVNKDKKISLTEWLNCLGV 104

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907160369  441 VCqdPETCPpaKILDQACGTDNQTYASSCHLFATKCrlegtKKGHQLQLDYFGAC 495
Cdd:smart00280   1 DC--PEACP--REYDPVCGSDGVTYSNECHLCKAAC-----ESGKSIEVKHDGPC 46

Follistatin/Osteonectin-like EGF domain; Members of this family are predominantly found in osteonectin and follistatin and adopt an EGF-like fold.

                          10        20
                  ....*....|....*....|..
gi 1907160369 419 CTNFQCKRGHICKTDPQGKPHC 440
Cdd:pfam09289   1 CENFQCKRGKVCKVDKEGKPHC 22

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907160369 448 CPpaKILDQACGTDNQTYASSCHLFATKCRlegtkKGHQLQLDYFGAC 495
Cdd:cd00104     1 CP--KEYDPVCGSDGKTYSNECHLGCAACR-----SGRSITVAHNGPC 41

EF-hand, extracellular calcium-binding (EC) motif, found in secreted modular calcium-binding protein 1 (SMOC-1); SMOC-1, also termed SPARC-related modular calcium-binding protein 1, or smooth muscle-associated protein 1 (SMAP-1), is an Arf6 GTPase-activating protein (GAP) that directly interacts with clathrin and regulates the clathrin-dependent endocytosis of transferrin receptors from the plasma membrane. It is predominantly localized in basement membranes. SMOC-1 acts as a regulator of osteoblast differentiation and is involved in inhibition of transforming growth factor-beta (TGF-beta) signaling through production of nitric oxide. It also plays an essential role in ocular and limb development and functions as a regulator of bone morphogenic protein (BMP) signaling. It interacts with a matricellular protein, tenascin C in addition to the serum proteins, fibulin-1 and C-reactive protein, but not collagens. Two point mutations in the SMOC1 gene may cause Waardenburg Anophtalmia Syndrome. Moreover, SMOC-1 is involved in direct or indirect modulation of growth factor signaling pathways and plays a role in physiological processes involving extensive tissue remodeling. SMOC-1 contains a follistatin-like (FS) domain, two thyroglobulin-like (TY) domains, a novel domain, which is found only in the homologous SMOC-2, and an extracellular calcium-binding (EC) domain with two EF-hand calcium-binding motifs.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907160369 578 VHWQFNELDQHPADRIlTHSELAPLRASL---VPMEHCITRFFEECDPNKDKHITLKEWGHCFGIKE 641
Cdd:cd16240    50 VHWYFSQLDNNSSNDI-NKKELKPFKRYVkkkAKPKKCARRFTDYCDLNKDKSISLQELKGCLGVSK 115

EF-hand, extracellular calcium-binding (EC) motif, found in testican-1 (TICN1); TICN1, also termed protein SPOCK, or SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycan 1 (Spock1), is a secreted chimeric proteoglycan that is highly expressed in brain and carries both chondroitin and heparan sulfate glycosaminoglycan side chains. It promotes resistance against Pseudomonas aeruginosa-induced keratitis through regulation of matrix metalloproteinase (MMP)-2 expression and activation. It also acts as a potential cancer prognostic marker that promotes the proliferation and metastasis of gallbladder cancer cells by activating the PI3K/Akt pathway. Moreover, TICN1 corresponding gene SPOCK1 is a novel transforming growth factor-beta target gene that regulates lung cancer cell epithelial-mesenchymal transition. It is also up-regulated by chromodomain helicase/adenosine triphosphatase DNA binding protein 1-like (CHD1L), and promotes human hepatocellular carcinoma (HCC) cell invasiveness and metastasis. Furthermore, TICN1 inhibits the lysosomal cysteine protease cathepsin L in intracellular vesicles and in the extracellular milieu. TICN1 contains an N-terminal signal sequence known to direct nascent polypeptides to the extracellular space, an unique region to the testicans, a follistatin (FS)-like domain generally involving five disulfide bridges, an extracellular calcium-binding (EC) domain including a pair of EF hands, and a thyroglobulin type-1 (TY) domain followed by a C-terminal acidic region with high density of negatively charged amino acids. The substitution of a ligating Asp residue by Phe291 in the +Y position of EF-hand 2 in TICN1 could prevent Ca2+ binding to this site and also cause EF-hand 1 to bind one Ca2+ ion with low affinity.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907160369 580 WQFNELDQHpADRILTHSELAPLRasLVPMEHCITRFFEECDPNKDKHITLKEWGHCF 637
Cdd:cd16237    54 WMFNKLDMN-YDLLLDPSEISAIY--LDKYEPCMKPLFNSCDSFKDGKLSNNEWCYCF 108

Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.

                          10        20
                  ....*....|....*....|....
gi 1907160369 448 CPpaKILDQACGTDNQTYASSCHL 471
Cdd:cd01327     5 CP--KDYDPVCGTDGVTYSNECLL 26