PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686   1 MDQTKFPIVNAELSFFGHAHLGTGDPYTPGFPSFNHTQFPPSRSSGLPNIPVQTISRAAAEKLFGNMEGD-CPSDWKT-D 78
Cdd:cd02128    87 PDPADFPIDPSETALFGHVHLGTGDPYTPGFPSFNHTQFPPSQSSGLPNIPAQTISAAAAAKLLSKMGGPvCPSGWKGgD 166

                          90
                  ....*....|....*..
gi 2217345686  79 STCRMVTSESKNVKLTV 95
Cdd:cd02128   167 STCRLGTSSSKNVKLTV 183

PA_TfR: Protease-associated domain containing proteins like transferrin receptor (TfR). This group contains various PA domain-containing proteins similar to human TfR1 and TfR2. TfR1 and TfR2 are type II membrane proteins, belonging to the peptidase M28 family. TfR1 is homodimeric, widely expressed, and a key player in the uptake of iron-loaded transferrin (Tf) into cells. The TfR1 homodimer binds two molecules of Tf and this complex is internalized. In addition to its role in iron uptake, TfR1 may participate in cell growth and proliferation. TfR2 also binds Tf but with a significantly lower affinity than does TfR1. TfR2 is expressed chiefly in hepatocytes, hematopoietic cells, and duodenal crypt cells; its expression overlaps with that of hereditary hemochromatosis protein (HFE). TfR2 is involved in iron homeostasis. HFE and TfR2 interact in cells. By one model for serum iron sensing, at low or basal iron concentrations, HFE and TFR1 form a complex at the plasma membrane; at increased Tf, Tf competes with HFE for binding of TfR1, resulting in HFE disassociating from TfR1 and associating with TfR2 . The TfR1-TfR2 association might initiate a signal cascade leading to the induction of hepcidin (a small peptide hormone that controls systemic iron levels). Human mutations in TfR2 are associated with a form of hemochromatosis (HFE3). The significance of the PA domain to TfRs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686   1 MDQTKFPIVNAELSFFGHAHLGTGDPYTPGFPSFNHTQFPPSRSSGLPNIPVQTISRAAAEKLFGNMEGD-CPSDWKT-D 78
Cdd:cd02128    87 PDPADFPIDPSETALFGHVHLGTGDPYTPGFPSFNHTQFPPSQSSGLPNIPAQTISAAAAAKLLSKMGGPvCPSGWKGgD 166

                          90
                  ....*....|....*..
gi 2217345686  79 STCRMVTSESKNVKLTV 95
Cdd:cd02128   167 STCRLGTSSSKNVKLTV 183

Peptidase family M28;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686 106 NIFGVIKGfVEPDHYVVVGAQRDAW--GPGAAKSGVGTALLLKLAQmfsdmVLKDGFQPSRSIIFASWSAGDFGSVGATe 183
Cdd:pfam04389   1 NVIAKLPG-KAPDEVVLLSAHYDSVgtGPGADDNASGVAALLELAR-----VLAAGQRPKRSVRFLFFDAEEAGLLGSH- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686 184 wlegYLSSLHL---KAFTYINLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTGQF---LYQDSNWASkvekltlDN 257
Cdd:pfam04389  74 ----HFAKSHPplkKIRAVINLDMIGSGGPALLFQSGPKGSSLLEKYLKAAAKPYGVTLaedPFQERGGPG-------RS 142

                         170       180
                  ....*....|....*....|....*.
gi 2217345686 258 AAFPFLAYsGIPAVSFcfcEDTDYPY 283
Cdd:pfam04389 143 DHAPFIKA-GIPGLDL---AFTDFGY 164

M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor (TfR) and prostate-specific membrane antigen (PSMA, also called glutamate carboxypeptidase or GCP-II) subfamily. TfR and PSMA are homodimeric type II transmembrane proteins containing three distinct domains: protease-like, apical or protease-associated (PA) and helical domains. The protease-like domain is a large extracellular portion (ectodomain). In TfR, it contains a binding site for the transferrin molecule and has 28% identity to membrane glutamate carboxypeptidase II (mGCP-II or PSMA). The PA domain is inserted between the first and second strands of the central beta sheet in the protease-like domain. TfR1 is widely expressed, and is a key player in the uptake of iron-loaded transferrin (Tf) into cells. The TfR1 homodimer binds two molecules of Tf and the complex is then internalized. TfR1 may also participate in cell growth and proliferation. TfR2 binds Tf but with a significantly lower affinity than TfR1. It is expressed chiefly in hepatocytes, hematopoietic cells, and duodenal crypt cells; its expression overlaps with that of hereditary hemochromatosis protein (HFE). TfR2 is involved in iron homeostasis; in humans, mutations in TfR2 are associated with a form of hemochromatosis (HFE3). PSMA is over-expressed predominantly in prostate cancer (PCa) as well as in the neovasculature of most solid tumors, but not in the vasculature of normal tissues. PSMA is considered a biomarker for PCa and possibly for use as an imaging and therapeutic target. The extracellular domain of PSMA possesses two unique enzymatic functions: N-acetylated, alpha-linked acidic dipeptidase (NAALADase) which cleaves terminal glutamate from the neurodipeptide N-acetyl-aspartyl-glutamate (NAAG), and folate hydrolase (FOLH) which cleaves the terminal glutamates from gamma-linked polyglutamates (carboxypeptidase). A mutation in this gene may be associated with impaired intestinal absorption of dietary folates, resulting in low blood folate levels and consequent hyperhomocysteinemia. Expression of this protein in the brain may be involved in a number of pathological conditions associated with glutamate excitotoxicity. This gene likely arose from a duplication event of a nearby chromosomal region. Alternative splicing gives rise to multiple transcript variants. While related in sequence to peptidase M28 GCP-II, TfR lacks the metal ion coordination centers and protease activity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686 103 KILNIFGVIKGFVEPDHYVVVGAQRDAWGPGAAKSGVGTALLLKLAQMFSDMVLKDGFQPSRSIIFASWSAGDFGSVGAT 182
Cdd:cd03874    56 PITNVVGKIEGIEQPDRAIIIGAHRDSWGYGAGYPNSGTAVLLEIARLFQQLKKKFGWKPLRTIYFISWDGSEFGLAGST 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686 183 EWLEGYLSSLHLKAFTYINLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTGQFlyQDSNWASKVEKLTLDNAAFPF 262
Cdd:cd03874   136 ELGEDRKASLKDEVYAYINIDQLVIGNSELDVDAHPLLQSLFRKASKKVKFPGNEDW--WKHSPNAKVSNLHQYGDWTPF 213

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217345686 263 LAYSGIPAVSFCFCEDTD-YPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVIKLTHDVELN 326
Cdd:cd03874   214 LNHLGIPVAVFSFKNDRNaSYPINSSYDTFEWLEKFLDPDFELHSTLAEFVGLLVLSLAEDPLLP 278

M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also called aminopeptidase Y family) contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Plasma glutamate carboxypeptidase (PGCP) and glutamate carboxypeptidase II (NAALADase) hydrolyze dipeptides. Several members of the M28 peptidase family have PA domain inserts which may participate in substrate binding and/or in promoting conformational changes, which influence the stability and accessibility of the site to substrate. These include prostate-specific membrane antigen (PSMA), yeast aminopeptidase S (SGAP), human transferrin receptors (TfR1 and TfR2), plasma glutamate carboxypeptidase (PGCP) and several predicted aminopeptidases where relatively little is known about them. Also included in the M28 family are glutaminyl cyclases (QC), which are involved in N-terminal glutamine cyclization of many endocrine peptides. Nicastrin and nicalin belong to this family but lack the amino-acid conservation required for catalytically active aminopeptidases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686 104 ILNIFGVIKGFVEPDHYVVVGAQRDAW--GPGAAKSGVGTALLLKLAQMFSDMVlkdgFQPSRSIIFASWSAGDFGSVGA 181
Cdd:cd02690     1 GYNVIATIKGSDKPDEVILIGAHYDSVplSPGANDNASGVAVLLELARVLSKLQ----LKPKRSIRFAFWDAEELGLLGS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686 182 TEWLEGYLSSLHlKAFTYINLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTGQFLYQDsnwaSKVEKLTLDNAAFP 261
Cdd:cd02690    77 KYYAEQLLSSLK-NIRAALNLDMIGGAGPDLYLQTAPGNDALVEKLLRALAHELENVVYTVV----YKEDGGTGGSDHRP 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217345686 262 FLAySGIPAVSFCFCEDTDYPYLGTTMDTYKELieripeLNKVARAAAEVAGQFVIKL 319
Cdd:cd02690   152 FLA-RGIPAASLIQSESYNFPYYHTTQDTLENI------DKDTLKRAGDILASFLYRL 202

Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686 106 NIFGVIKGFVEPDHYVVVGAQRDAWG---PGAAKSGVGTALLLKLAQMFSDMvlkdGFQPSRSIIFASWSAGDFGSVGAT 182
Cdd:COG2234    48 NVIAEIPGTDPPDEVVVLGAHYDSVGsigPGADDNASGVAALLELARALAAL----GPKPKRTIRFVAFGAEEQGLLGSR 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686 183 EWLEGYLSSLHlKAFTYINLDkaVLGTSNFK-------VSASPLLYTLIEKTMQNVKHPVTGQF-----LYQDSnwaskv 250
Cdd:COG2234   124 YYAENLKAPLE-KIVAVLNLD--MIGRGGPRnylyvdgDGGSPELADLLEAAAKAYLPGLGVDPpeetgGYGRS------ 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217345686 251 ekltlDNAAFpflAYSGIPAVSFCFCEDTDYPYLGTTMDTYkELIERiPELNKVARAAAEVAGQF 315
Cdd:COG2234   195 -----DHAPF---AKAGIPALFLFTGAEDYHPDYHTPSDTL-DKIDL-DALAKVAQLLAALVYEL 249

Transferrin receptor-like dimerization domain; This domain is involved in dimerization of the transferrin receptor as shown in its crystal structure.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686 355 LSLQWLYSARGDFFRATSRLT---TDFGNAEKTDRFVMKKLNDRVMRVEYHFLSPYVSPKESPFRHVFWGSGSH------ 425
Cdd:pfam04253   1 LSLEPLRKAIEKFKKAAKEFDawaKKWEDIKEPDLLAVRAVNDKLMLFERAFLDPEGLPGRPWFKHVVFAPGLWtgyaga 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2217345686 426 TLPALLENLKlrkqnngAFNETLFRNQLALATWTIQGAANALS 468
Cdd:pfam04253  81 TFPGIRDAIE-------AGDWELAQKQISIVAKAIQSAAETLK 116

M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Some proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686 106 NIFGVIKGFVEPDHYVVVGAQRDAWG-----------PGAAKSGVGTALLLKLAQmfsdmVLKDGFQPSRSIIFASWSAG 174
Cdd:cd03877     3 NVVGVLEGSDLPDETIVIGAHYDHLGigggdsgdkiyNGADDNASGVAAVLELAR-----YFAKQKTPKRSIVFAAFTAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686 175 DFGSVGATEWLEgYLSSLHLKAFTYINLD--------KAVLGTSnfkvSASPLLYTLIEKTmqNVKHPVTGQFLYQDSNW 246
Cdd:cd03877    78 EKGLLGSKYFAE-NPKFPLDKIVAMLNLDmigrlgrsKDVYLIG----SGSSELENLLKKA--NKAAGRVLSKDPLPEWG 150

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2217345686 247 --ASkvekltlDNAAFpflAYSGIPAVSFCFCEDTDY 281
Cdd:cd03877   151 ffRS-------DHYPF---AKAGVPALYFFTGLHDDY 177

PA_GCPII_like: Protease-associated domain containing protein, glutamate carboxypeptidase II (GCPII)-like. This group contains various PA domain-containing proteins similar to GCPII including, GCPIII (NAALADase2) and NAALADase L. These proteins belong to the peptidase M28 family. GCPII is also known N-acetylated-alpha-linked acidic dipeptidase (NAALDase1), folate hydrolase or prostate-specific membrane antigen (PSMA). GCPII is found in various human tissues including prostate, small intestine, and the central nervous system. In the brain, GCPII is known as NAALDase1, it functions as a NAALDase hydrolyzing the neuropeptide N-acetyl-L-aspartyl-L-glutamate (alpha-NAAG), to release free glutamate. In the small intestine, GCPII releases the terminal glutamate from poly-gamma-glutamated folates. GCPII (PSMA) is a useful cancer marker; its expression is markedly increased in prostate cancer and in tumor-associated neovasculature. GCPIII hydrolyzes alpha-NAAG with a lower efficiency than does GCPII; NAALADase L is not able to hydrolyze alpha-NAAG. The GCPII PA domain (referred to as the apical domain) participates in substrate binding and may act as a protein-protein interaction domain.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217345686  22 GTGDPYTPGFPSF-NHTQFPPSRSSGLPNIPVQTISRAAAEKLFGNMEGD-CPSDWK 76
Cdd:cd02121   141 GPGDPLTPGYPSKpGAERRDKEESKGLPKIPSLPISYRDAQPLLKALGGPgAPSDWQ 197

M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686  78 DSTCRMVTSESKNVKLTVSNVLKEIKILNIFGVIKGFVEPDHYVVVGAQRDAW----------GPGAAKSGVGTALLLKL 147
Cdd:cd05642    62 ASGGRMTVEVPSYVQGPASRIPFPVNISNVVATLKGSEDPDRVYVVSGHYDSRvsdvmdyesdAPGANDDASGVAVSMEL 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217345686 148 AQMFSDmvlkdgFQPSRSIIFASWSAGDFGSVGATeWLEGYLSSLHLKAFTYINLDkaVLGTS 210
Cdd:cd05642   142 ARIFAK------HRPKATIVFTAVAGEEQGLYGST-FLAQTYRNNSVNVEGMLNND--IVGSS 195

M28 Zn-Peptidase Nicalin, Nicastrin-like protein; Peptidase M28 family, Nicalin (nicastrin-like protein) subfamily. Nicalin is distantly related to Nicastrin, a component of the Alzheimer's disease-associated gamma-secretase, and forms a complex with Nomo (nodal modulator) pM5. Similar to Nicastrin, Nicalin lacks the amino-acid conservation required for catalytically active aminopeptidases. Functional studies in zebrafish embryos and cultured human cells reveal that nicalin and Nomo collaborate to antagonize the Nodal/TGFbeta signaling pathway. Thus, nicastrin and nicalin are both associated with protein complexes involved in cell fate decisions during early embryonic development.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686  82 RMVTSESKN-VKLTVSNVL----KEIKILNIFGVIKG--FVEPDHYVVVGAQRDAWG------PGAAKSGVGTALLLKLA 148
Cdd:cd03882    46 VLIRSLSANgFKIVVSGNSpkaiSDWKITTIEGRLTGlgDGEKLPTIVIVAHYDTFGvapwlsSGADSNGSGVAALLELM 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686 149 QMFSDMVLKDGFQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAFTYINLDKAVLGTSNFK--VSASPLLYTLIEK 226
Cdd:cd03882   126 RLFSRLYSNPRTRAKYNLLFLLTGGGKLNYQGTKHWLESNLDHFLDNVEFVLCLDSIGSKDSDLYlhVSKPPKEGTHIQQ 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686 227 TMQNVKHPVtgQFLYQDSNWASKVEKLTLDNAAFPFLAYS--GIPAVSFCFCEDTDYPYLGTTMDTYKELieRIPELNKV 304
Cdd:cd03882   206 FLEELKSVA--KAPDKNLTVVHKKINLADTKLAWEHERFSikRLPAFTLSHLESHRSPLRNSIFDTRSSV--DEDKLKRN 281

                  ....*.
gi 2217345686 305 ARAAAE 310
Cdd:cd03882   282 TKIIAE 287

Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217345686 116 EPDHYVVVGAQRDAWGPGAAKSGVGTALLLKLAQMFSDmvlkDGFQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLK 195
Cdd:cd03873    33 DPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKE----NGFKPKGTIVVAFTADEEVGSGGGKGLLSKFLLAEDLK 108

                          90
                  ....*....|
gi 2217345686 196 AFTYINLDKA 205
Cdd:cd03873   109 VDAAFVIDAT 118