C-terminal domain of SPAR protein; This domain is found st the C-terminus of many spine-associated Rap GTPase-activating - SPAR - proteins in eukaryotes. This domain is found associated with pfam02145, pfam00595. The exact function is not known.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371360 1002 KRHQSDGNEIAHTRLRASTRDLQaSPKPTSKSTIEEDLKKLIDLESPTPESQknfkfhalsSPQSPFPTTPTSRRALHRT 1081
Cdd:pfam11881    1 KRHQSDGNVSGQPRLRASLRDLR-SPQKNYKSTIEEDLKKLIIMDSPPPEEQ---------ERKPSFPGNPSPRRSLQRT 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371360 1082 LSDESIYSSQREHFFTSRASLLDQALPNDVLFS--STYPSLP--KSLPLRRPSYTLGMKSLHGEFSASDSSLTDIQETRR 1157
Cdd:pfam11881   71 LSDESICSGQREPSFSSRDSVLDQALPSDVLFSctSTLPRSPttRSAPLRRASYALGMKSLHGDLSASDLSLTDLRDRRP 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371360 1158 QPIPDPGLMPLPDAASDLDWSNLVDAAKAYEVQRASFFAASDENHRPLSAASNSDQLEEQALVQMKSYSS--SKDPSPTL 1235
Cdd:pfam11881  151 LRRLDPGLMPLPDTAAGLDWSHLVDAAKAFEVQRAASFFSLDDNHRSPDAASSPQQLSLQVAPQTPRTTStsSEESPADL 230

                          250
                   ....*....|..
gi 1720371360 1236 ASKVDQLEGMLK 1247
Cdd:pfam11881  231 TGKVYQLEAMLK 242

PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SIPA1, and related domains. The Rap-GTPase activating protein SIPA1 (also known as GTPase-activating protein Spa-1, p130 SPA1) is a metastasis promoter; a polymorphism in a region of the Sipa1 gene encoding the PDZ domain is associated with metastasis. The SIPA1 PDZ domain binds ribosomal RNA processing 1 homolog B (Rrp1b). SIPA1 also forms a complex with water channel aquaporin-2 (AQP2) and plays a role in trafficking of AQP2, targeted positioning of which strictly regulates body water homeostasis; the SIPA1 PDZ domain binds AQP2. Rrp1b or AQP2 binding inhibits the RapGAP activity of SIPA1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SIPA1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720371360  459 EMTLRRNGLGQLGFHVNYEGIVADVEPYGYAWQAGLRQGSRLVEICKVAVATLSHEQMIDLLRTSVTVKVVII 531
Cdd:cd06745      1 ELTLRRNGLGQLGFHVNYEGFVTEVERFGFAWQAGLRQGSRLVEICKVPVATLTHEQMIDLLRTSVKVKVTVI 73

C-terminal domain of SPAR protein; This domain is found st the C-terminus of many spine-associated Rap GTPase-activating - SPAR - proteins in eukaryotes. This domain is found associated with pfam02145, pfam00595. The exact function is not known.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371360 1002 KRHQSDGNEIAHTRLRASTRDLQaSPKPTSKSTIEEDLKKLIDLESPTPESQknfkfhalsSPQSPFPTTPTSRRALHRT 1081
Cdd:pfam11881    1 KRHQSDGNVSGQPRLRASLRDLR-SPQKNYKSTIEEDLKKLIIMDSPPPEEQ---------ERKPSFPGNPSPRRSLQRT 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371360 1082 LSDESIYSSQREHFFTSRASLLDQALPNDVLFS--STYPSLP--KSLPLRRPSYTLGMKSLHGEFSASDSSLTDIQETRR 1157
Cdd:pfam11881   71 LSDESICSGQREPSFSSRDSVLDQALPSDVLFSctSTLPRSPttRSAPLRRASYALGMKSLHGDLSASDLSLTDLRDRRP 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371360 1158 QPIPDPGLMPLPDAASDLDWSNLVDAAKAYEVQRASFFAASDENHRPLSAASNSDQLEEQALVQMKSYSS--SKDPSPTL 1235
Cdd:pfam11881  151 LRRLDPGLMPLPDTAAGLDWSHLVDAAKAFEVQRAASFFSLDDNHRSPDAASSPQQLSLQVAPQTPRTTStsSEESPADL 230

                          250
                   ....*....|..
gi 1720371360 1236 ASKVDQLEGMLK 1247
Cdd:pfam11881  231 TGKVYQLEAMLK 242

PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SIPA1, and related domains. The Rap-GTPase activating protein SIPA1 (also known as GTPase-activating protein Spa-1, p130 SPA1) is a metastasis promoter; a polymorphism in a region of the Sipa1 gene encoding the PDZ domain is associated with metastasis. The SIPA1 PDZ domain binds ribosomal RNA processing 1 homolog B (Rrp1b). SIPA1 also forms a complex with water channel aquaporin-2 (AQP2) and plays a role in trafficking of AQP2, targeted positioning of which strictly regulates body water homeostasis; the SIPA1 PDZ domain binds AQP2. Rrp1b or AQP2 binding inhibits the RapGAP activity of SIPA1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SIPA1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720371360  459 EMTLRRNGLGQLGFHVNYEGIVADVEPYGYAWQAGLRQGSRLVEICKVAVATLSHEQMIDLLRTSVTVKVVII 531
Cdd:cd06745      1 ELTLRRNGLGQLGFHVNYEGFVTEVERFGFAWQAGLRQGSRLVEICKVPVATLTHEQMIDLLRTSVKVKVTVI 73

PDZ domain; PDZ domains are found in diverse signaling proteins.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371360  459 EMTLRRNGLGQLGF-------HVNYEGIVADVEPYGYAWQAGLRQGSRLVEICKVAVATLSHEQMIDLLRTSV-TVKVVI 530
Cdd:pfam00595    1 QVTLEKDGRGGLGFslkggsdQGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGgKVTLTI 80

                   .
gi 1720371360  531 I 531
Cdd:pfam00595   81 L 81

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720371360 1235 LASKVDQLEG---MLKMLREDLKKEKE----DKAQLQAEVEHLREDNLRLQEESQNASDKLK 1289
Cdd:COG3074      9 LEAKVQQAVDtieLLQMEVEELKEKNEeleqENEELQSENEELQSENEQLKTENAEWQERIR 70

C-terminal domain of SPAR protein; This domain is found st the C-terminus of many spine-associated Rap GTPase-activating - SPAR - proteins in eukaryotes. This domain is found associated with pfam02145, pfam00595. The exact function is not known.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371360 1002 KRHQSDGNEIAHTRLRASTRDLQaSPKPTSKSTIEEDLKKLIDLESPTPESQknfkfhalsSPQSPFPTTPTSRRALHRT 1081
Cdd:pfam11881    1 KRHQSDGNVSGQPRLRASLRDLR-SPQKNYKSTIEEDLKKLIIMDSPPPEEQ---------ERKPSFPGNPSPRRSLQRT 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371360 1082 LSDESIYSSQREHFFTSRASLLDQALPNDVLFS--STYPSLP--KSLPLRRPSYTLGMKSLHGEFSASDSSLTDIQETRR 1157
Cdd:pfam11881   71 LSDESICSGQREPSFSSRDSVLDQALPSDVLFSctSTLPRSPttRSAPLRRASYALGMKSLHGDLSASDLSLTDLRDRRP 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371360 1158 QPIPDPGLMPLPDAASDLDWSNLVDAAKAYEVQRASFFAASDENHRPLSAASNSDQLEEQALVQMKSYSS--SKDPSPTL 1235
Cdd:pfam11881  151 LRRLDPGLMPLPDTAAGLDWSHLVDAAKAFEVQRAASFFSLDDNHRSPDAASSPQQLSLQVAPQTPRTTStsSEESPADL 230

                          250
                   ....*....|..
gi 1720371360 1236 ASKVDQLEGMLK 1247
Cdd:pfam11881  231 TGKVYQLEAMLK 242

PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SIPA1, and related domains. The Rap-GTPase activating protein SIPA1 (also known as GTPase-activating protein Spa-1, p130 SPA1) is a metastasis promoter; a polymorphism in a region of the Sipa1 gene encoding the PDZ domain is associated with metastasis. The SIPA1 PDZ domain binds ribosomal RNA processing 1 homolog B (Rrp1b). SIPA1 also forms a complex with water channel aquaporin-2 (AQP2) and plays a role in trafficking of AQP2, targeted positioning of which strictly regulates body water homeostasis; the SIPA1 PDZ domain binds AQP2. Rrp1b or AQP2 binding inhibits the RapGAP activity of SIPA1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SIPA1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720371360  459 EMTLRRNGLGQLGFHVNYEGIVADVEPYGYAWQAGLRQGSRLVEICKVAVATLSHEQMIDLLRTSVTVKVVII 531
Cdd:cd06745      1 ELTLRRNGLGQLGFHVNYEGFVTEVERFGFAWQAGLRQGSRLVEICKVPVATLTHEQMIDLLRTSVKVKVTVI 73

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371360   456 ESVEMTLRRNGlGQLGFHVNYEG------IVADVEPYGYAWQAGLRQGSRLVEICKVAVATLSHEQMIDLLR-TSVTVKV 528
Cdd:smart00228    1 EPRLVELEKGG-GGLGFSLVGGKdegggvVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKkAGGKVTL 79

                    ....*
gi 1720371360   529 VIIPP 533
Cdd:smart00228   80 TVLRG 84

PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SHANK1, SHANK2, SHANK3, and related domains. SHANK family proteins, SHANK1 (also known as somatostatin receptor-interacting protein, SSTR-interacting protein, SSTRIP), SHANK2 (also known as cortactin-binding protein 1, proline-rich synapse-associated protein 1), and SHANK3 (proline-rich synapse-associated protein 2) are synaptic scaffolding proteins which are highly enriched in the post-synaptic densities of excitatory synapses. They have been implicated in synaptic transmission, synapse formation, synaptic plasticity, and cytoskeletal remodeling, and are regulators of Cav1 calcium current and CREB target expression. Many protein ligands have been identified for the Shank PDZ domain, such as GKAP (also known as SAPAP), betaPIX (a guanine nucleotide exchange factor used by Rho GTPase family members Rac1 and Cdc42), alpha-latrotoxin, neuroligin, group I metabotropic glutamate receptors (mGluRs), and L-type calcium channels. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SHANK-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720371360  482 DVEPYGYAWQAGLRQGSRLVEICKVAVATLSHEQMIDLLRTS---VTVKVV 529
Cdd:cd06746     48 SVDPGGVADKAGLKKGDFLLEINGEDVVKASHEQVVNLIRQSgntLVLKVV 98

PDZ domain; PDZ domains are found in diverse signaling proteins.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371360  459 EMTLRRNGLGQLGF-------HVNYEGIVADVEPYGYAWQAGLRQGSRLVEICKVAVATLSHEQMIDLLRTSV-TVKVVI 530
Cdd:pfam00595    1 QVTLEKDGRGGLGFslkggsdQGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGgKVTLTI 80

                   .
gi 1720371360  531 I 531
Cdd:pfam00595   81 L 81

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720371360 1235 LASKVDQLEGMLKMLREDLKKEKEDKAQLQAEVEHLREDNLRLQEESQNASDKLKK 1290
Cdd:pfam06005    9 LETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRG 64

PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of harmonin isoforms a, b, and c, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This harmonin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720371360  459 EMTLRRNGLGQLGFHV--NYE---GI-VADVEPYGYAWQAGLRQGSRLVEICKVAVATLSHEQMIDLLRT--SVTVKV 528
Cdd:cd06737      4 LVRLDRRGPESLGFSVrgGLEhgcGLfVSHVSPGSQADNKGLRVGDEIVRINGYSISQCTHEEVINLIKTkkTVSLKV 81

PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SNX27, and related domains. SNX27 is involved in retrograde transport from endosome to plasma membrane. The PDZ domain of SNX27 links cargo identification to retromer-mediated transport. SNX27 binds to the retromer complex (vacuolar protein sorting 26(VPS26)-VPS29-VPS35), via its PDZ domain binding to VPS26. The SNX27 PDZ domain also binds to cargo including the G-protein-coupled receptors (GPCRs): beta2-adrenergic receptor (beta2AR), beta1AR, parathyroid hormone receptor (PTHR), alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs), NMDA receptors, 5-hydroxytryptamine 4a receptors, frizzled receptors, and somatostatin receptor subtype 5 (SSTR5). Additional binding partners of the SNX27 PDZ domain include G protein-gated inwardly rectifying potassium (Kir3) channels, angiotensin-converting enzyme 2 (ACE2), and PTEN (phosphatase and tensin homolog deleted on chromosome 10); PTEN binding to SNX27 prevents SNX27's association with the retromer complex. SNX27 has been reported to be a host factor needed for efficient entry of an engineered SARS-CoV-2 variant, the spike protein of which contains a deletion at the S1/S2 subunit cleavage site; the PDZ domain of SNX27 binds angiotensin-converting enzyme 2 (ACE2), and may be involved in recycling ACE2 to the plasma membrane, thereby promoting viral entry. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SNX27-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1720371360  480 VADVEPYGYAWQAGLRQGSRLVEICKVAVATLSHEQMIDLLRTSV 524
Cdd:cd23070     40 VSAVLEGGAADKAGVRKGDRILEVNGVNVEGATHKQVVDLIKSGG 84

PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ARHGEF11, ARHGEF12, and related domains. This subfamily includes the GEFs (guanine exchange factors) ARHGEF11 (Rho guanine nucleotide exchange factor 11, known as PDZ-RhoGEF) and ARHGEF12 (Rho guanine nucleotide exchange factor 12, also known as leukemia-associated RhoGEF). GEFs activate Rho GTPases by promoting GTP binding. ARHGEF11/12 are regulators of G protein signaling (RGS) domain-containing GEFs; the RGS domain mediates their binding to and activation of Galpha (and Gq also in the case of ARHGEF12), in response to G-protein coupled receptor activation. ARHGEF11 and 12 are involved in serum-signaling, and regulate Yes-Associated Protein (YAP1)-dependent transcription. The ARHGEF12 PDZ domain binds plexin-B1 and the receptor tyrosine kinase insulin-like growth factor receptor (IGF-R1) beta-subunit. ARHGEF12 also interacts with glutamate receptor delta-1(GluD1), a postsynaptic organizer of inhibitory synapses in cortical pyramidal neurons. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ARHGEF11-12-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720371360  460 MTLRRNGLGqLGFHVNYEGI--VADVEPYGYAWQAGLRQGSRLVEICKVAVATLSHEQMIDLLRTSVTVKV 528
Cdd:cd23069      4 VVIQRDENG-YGLTVSGDNPvfVQSVKEGGAAYRAGVQEGDRIIKVNGTLVTHSNHLEVVKLIKSGSYVAL 73

CRISPR type I-D/CYANO-associated protein Csc3/Cas10d; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family is a CRISPR-associated (Cas) family strictly associated with the Cyano subtype of CRISPR/Cas locus, found in several species of Cyanobacteria and several archaeal species. This family is designated Csc3 for CRISPR/Cas Subtype Cyano protein 3, as it is often the third gene upstream of the core cas genes, cas3-cas4-cas1-cas2.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720371360  126 AGQSTEEEMYNNESAGPAFEEFLQLLGERVRLKG----------FEKYRAQLDTKTDSTGTHSL-YTTYKDYEIMFHVST 194
Cdd:TIGR03174  440 ASQSAEEEGYFAAHLSPTRQIFLDYLDEYLSIQGwelhqtfiaeLNNYNAYAKTKRGKQPICSLsSGEFPSEEQMDSVVL 519

                           90
                   ....*....|..
gi 1720371360  195 MLPYTPNNKQQL 206
Cdd:TIGR03174  520 FLPQQYSNKNPL 531