Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and Sec7 domain containing) is an guanine nucleotide exchange factor for ADP ribosylation factor 6 (ARF6), which is involved in membrane recycling. EFA6 has four structurally related polypeptides: EFA6A, EFA6B, EFA6C and EFA6D. It consists of a N-terminal proline rich region (PR), a SEC7 domain, a PH domain, a PR, a coiled-coil region, and a C-terminal PR. The EFA6 PH domain regulates its association with the plasma membrane. EFA6 activates Arf6 through its Sec7 catalytic domain and modulates this activity through its C-terminal domain, which rearranges the actin cytoskeleton in fibroblastic cell lines. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543632 563 PDSVVEYYSGFLMRKYVRETDGGKTPFGRRSWRMVYARLRGLVLYFDTDEHPKAT-SRYASLENAVSLHHALAEPAPDYK 641
Cdd:cd13295   1 DPNAVEYKKGYLMRKCCADPDGKKTPFGKRGWKMFYATLKGLVLYLHKDEYGCKKaLRYESLRNAISVHHSLATKATDYT 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 17543632 642 KKSFVFRVRIAHGGEILFQTSNQKELQEWCEKINFVAAAFSSPTLP 687
Cdd:cd13295  81 KKPHVFRLRTADWREYLFQASDTKEMQSWIEAINLVAAAFSAPPLP 126

Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and Sec7 domain containing) is an guanine nucleotide exchange factor for ADP ribosylation factor 6 (ARF6), which is involved in membrane recycling. EFA6 has four structurally related polypeptides: EFA6A, EFA6B, EFA6C and EFA6D. It consists of a N-terminal proline rich region (PR), a SEC7 domain, a PH domain, a PR, a coiled-coil region, and a C-terminal PR. The EFA6 PH domain regulates its association with the plasma membrane. EFA6 activates Arf6 through its Sec7 catalytic domain and modulates this activity through its C-terminal domain, which rearranges the actin cytoskeleton in fibroblastic cell lines. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543632 563 PDSVVEYYSGFLMRKYVRETDGGKTPFGRRSWRMVYARLRGLVLYFDTDEHPKAT-SRYASLENAVSLHHALAEPAPDYK 641
Cdd:cd13295   1 DPNAVEYKKGYLMRKCCADPDGKKTPFGKRGWKMFYATLKGLVLYLHKDEYGCKKaLRYESLRNAISVHHSLATKATDYT 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 17543632 642 KKSFVFRVRIAHGGEILFQTSNQKELQEWCEKINFVAAAFSSPTLP 687
Cdd:cd13295  81 KKPHVFRLRTADWREYLFQASDTKEMQSWIEAINLVAAAFSAPPLP 126

Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the central domain of the guanine-nucleotide-exchange factors (GEFs) of the ADP-ribosylation factor family of small GTPases (ARFs) . It carries the exchange factor activity.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543632 364 NLNQTAVPSTSTNSVGGE-REAAQIARNLYELKNCTSTQVADRLNEQNEFSFLILVKYLELFQFSTTRIDAALREFLSRV 442
Cdd:cd00171  13 NRKPKKGISFLIEKGFLEdDSPKEIAKFLYETEGLNKKAIGEYLGENNEFNSLVLHEFVDLFDFSGLRLDEALRKFLQSF 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543632 443 ELRGESSARERLLRVFSARYLECNPAIFD-SLDEVHTLTCALLLLNSDLHGPNMGKKMTARDFITNIAHTGCT--FKREM 519
Cdd:cd00171  93 RLPGEAQKIDRLLEKFSERYCECNPGIFSsSADAAYTLAYSIIMLNTDLHNPNVKKKMTLEDFIKNLRGINDGedFPREF 172

                       170
                ....*....|...
gi 17543632 520 LKTLFQSIKDNAI 532
Cdd:cd00171 173 LKELYDSIKNNEI 185

Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 family.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543632   381 EREAAQIARNLYELKNCTSTQVADRLNEQNEFSFLILVKYLELFQFSTTRIDAALREFLSRVELRGESSARERLLRVFSA 460
Cdd:pfam01369  30 EDDPESIAKFLFETPGLDKKAIGEYLGKPDEFNIEVLKAFVDLFDFKGLRIDEALRLFLESFRLPGEAQKIDRIMEAFAE 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17543632   461 RYLECNPAIFDSLDEVHTLTCALLLLNSDLHGPNMGKKMTARDFITNI--AHTGCTFKREMLKTLFQSIKDNAI 532
Cdd:pfam01369 110 RYYEQNPGVFANADAAYVLAYSIIMLNTDLHNPNVKKKMTLEDFIRNLrgINDGKDFPDEYLEEIYDSIKKNEI 183

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543632    569 YYSGFLMRKyvretdggkTPFGRRSWRMVYARLRGLVLYFDTDEHPKATSRYASLenaVSLHHALAEPAPDYK--KKSFV 646
Cdd:smart00233   2 IKEGWLYKK---------SGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKGS---IDLSGCTVREAPDPDssKKPHC 69

                           90       100       110
                   ....*....|....*....|....*....|...
gi 17543632    647 FRVRIAHGGEILFQTSNQKELQEWCEKINFVAA 679
Cdd:smart00233  70 FEIKTSDRKTLLLQAESEEEREKWVEALRKAIA 102

Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and Sec7 domain containing) is an guanine nucleotide exchange factor for ADP ribosylation factor 6 (ARF6), which is involved in membrane recycling. EFA6 has four structurally related polypeptides: EFA6A, EFA6B, EFA6C and EFA6D. It consists of a N-terminal proline rich region (PR), a SEC7 domain, a PH domain, a PR, a coiled-coil region, and a C-terminal PR. The EFA6 PH domain regulates its association with the plasma membrane. EFA6 activates Arf6 through its Sec7 catalytic domain and modulates this activity through its C-terminal domain, which rearranges the actin cytoskeleton in fibroblastic cell lines. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543632 563 PDSVVEYYSGFLMRKYVRETDGGKTPFGRRSWRMVYARLRGLVLYFDTDEHPKAT-SRYASLENAVSLHHALAEPAPDYK 641
Cdd:cd13295   1 DPNAVEYKKGYLMRKCCADPDGKKTPFGKRGWKMFYATLKGLVLYLHKDEYGCKKaLRYESLRNAISVHHSLATKATDYT 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 17543632 642 KKSFVFRVRIAHGGEILFQTSNQKELQEWCEKINFVAAAFSSPTLP 687
Cdd:cd13295  81 KKPHVFRLRTADWREYLFQASDTKEMQSWIEAINLVAAAFSAPPLP 126

Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the central domain of the guanine-nucleotide-exchange factors (GEFs) of the ADP-ribosylation factor family of small GTPases (ARFs) . It carries the exchange factor activity.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543632 364 NLNQTAVPSTSTNSVGGE-REAAQIARNLYELKNCTSTQVADRLNEQNEFSFLILVKYLELFQFSTTRIDAALREFLSRV 442
Cdd:cd00171  13 NRKPKKGISFLIEKGFLEdDSPKEIAKFLYETEGLNKKAIGEYLGENNEFNSLVLHEFVDLFDFSGLRLDEALRKFLQSF 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543632 443 ELRGESSARERLLRVFSARYLECNPAIFD-SLDEVHTLTCALLLLNSDLHGPNMGKKMTARDFITNIAHTGCT--FKREM 519
Cdd:cd00171  93 RLPGEAQKIDRLLEKFSERYCECNPGIFSsSADAAYTLAYSIIMLNTDLHNPNVKKKMTLEDFIKNLRGINDGedFPREF 172

                       170
                ....*....|...
gi 17543632 520 LKTLFQSIKDNAI 532
Cdd:cd00171 173 LKELYDSIKNNEI 185

Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 family.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543632   381 EREAAQIARNLYELKNCTSTQVADRLNEQNEFSFLILVKYLELFQFSTTRIDAALREFLSRVELRGESSARERLLRVFSA 460
Cdd:pfam01369  30 EDDPESIAKFLFETPGLDKKAIGEYLGKPDEFNIEVLKAFVDLFDFKGLRIDEALRLFLESFRLPGEAQKIDRIMEAFAE 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17543632   461 RYLECNPAIFDSLDEVHTLTCALLLLNSDLHGPNMGKKMTARDFITNI--AHTGCTFKREMLKTLFQSIKDNAI 532
Cdd:pfam01369 110 RYYEQNPGVFANADAAYVLAYSIIMLNTDLHNPNVKKKMTLEDFIRNLrgINDGKDFPDEYLEEIYDSIKKNEI 183

ARF guanine nucleotide exchange factor (ARF-GEF); Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543632   376 NSVGGEREaaQIARNLYELKNCTSTQVADRLNEQNEFSFLILVKYLELFQFSTTRIDAALREFLSRVELRGESSARERLL 455
Cdd:PLN03076  642 NKVGESPE--EIAAFLKDASGLNKTLIGDYLGEREDLSLKVMHAYVDSFDFQGMEFDEAIRAFLQGFRLPGEAQKIDRIM 719

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543632   456 RVFSARYLECNPAIFDSLDEVHTLTCALLLLNSDLHGPNMGKKMTARDFITNI--AHTGCTFKREMLKTLFQSIKDNAIS 533
Cdd:PLN03076  720 EKFAERYCKCNPKAFSSADTAYVLAYSVIMLNTDAHNPMVKNKMSADDFIRNNrgIDDGKDLPEEFMRSLYERISKNEIK 799

                  ..
gi 17543632   534 LQ 535
Cdd:PLN03076  800 MK 801

ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with a RhoGAP domain. These proteins functions as a GTPase-activating protein (GAP) for RHOA and CDC42. ARHGAP21 controls the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating the activity of the small GTPase Cdc42. It is recruited to the Golgi by to GTPase, ARF1, through its PH domain and its helical motif. It is also required for CTNNA1 recruitment to adherens junctions. ARHGAP21 and it related proteins all contains a PH domain and a RhoGAP domain. Some of the members have additional N-terminal domains including PDZ, SH3, and SPEC. The ARHGAP21 PH domain interacts with the GTPbound forms of both ARF1 and ARF6 ARF-binding domain/ArfBD. The members here include: ARHGAP15, ARHGAP21, and ARHGAP23. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543632 582 TDGGKTpFGRRSWRMVYARLRGLVLYFDTDEHPKATSRYASL--ENAVSLHHALAEPAPDYKKKSFVFRVRIAHGGEILF 659
Cdd:cd01253  13 TDKGKR-VSDRSWKQAWAVLRGHSLYLYKDKREQTPALSIELgsEQRISIRGCIVDIAYSYTKRKHVFRLTTSDFSEYLF 91

                        90
                ....*....|....*
gi 17543632 660 QTSNQKELQEWCEKI 674
Cdd:cd01253  92 QAEDRDDMLGWIKAI 106

PH domain; PH stands for pleckstrin homology.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543632   569 YYSGFLMRKyvretdggkTPFGRRSWRMVYARL-RGLVLYFDTDEHPKAtsryASLENAVSLHHALAE--PAPDYKKKSF 645
Cdd:pfam00169   2 VKEGWLLKK---------GGGKKKSWKKRYFVLfDGSLLYYKDDKSGKS----KEPKGSISLSGCEVVevVASDSPKRKF 68

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 17543632   646 VFRVRIAHGGE---ILFQTSNQKELQEWCEKINFVAA 679
Cdd:pfam00169  69 CFELRTGERTGkrtYLLQAESEEERKDWIKAIQSAIR 105

Beta-spectrin pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with RhoGAP domain. The ARHGAP members here all have a PH domain upstream of their C-terminal RhoGAP domain. Some have additional N-terminal SH3 and WW domains. The members here include: ARHGAP9, ARHGAP12, ARHGAP15, and ARHGAP27. ARHGAP27 and ARHGAP12 shared the common-domain structure, consisting of SH3, WW, PH, and RhoGAP domains. The PH domain of ArhGAP9 employs a non-canonical phosphoinositide binding mechanism, a variation of the spectrin- Ins(4,5)P2-binding mode, that gives rise to a unique PI binding profile, namely a preference for both PI(4,5)P2 and the PI 3-kinase products PI(3,4,5)P3 and PI(3,4)P2. This lipid binding mechanism is also employed by the PH domain of Tiam1 and Slm1. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543632 582 TDGGKTPfgRRSWRMVYARLRGLVLYFDTDEHPKA--TSRYASLENAVSLHHALAEPAPDYKKKSFVFRVRIAHGGEILF 659
Cdd:cd13233  12 AENGKKL--RKNWSTSWVVLTSSHLLFYKDAKSAAksGNPYSKPESSVDLRGASIEWAKEKSSRKNVFQISTVTGTEFLL 89

                        90
                ....*....|.
gi 17543632 660 QTSNQKELQEW 670
Cdd:cd13233  90 QSDNDTEIREW 100

KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA (Caenorhabditis elegans homolog unc-104) and KIFIB transport synaptic vesicle precursors that contain synaptic vesicle proteins, such as synaptophysin, synaptotagmin and the small GTPase RAB3A, but they do not transport organelles that contain plasma membrane proteins. They have a N-terminal motor domain, followed by a coiled-coil domain, and a C-terminal PH domain. KIF1A adopts a monomeric form in vitro, but acts as a processive dimer in vivo. KIF1B has alternatively spliced isoforms distinguished by the presence or absence of insertion sequences in the conserved amino-terminal region of the protein; this results in their different motor activities. KIF1A and KIF1B bind to RAB3 proteins through the adaptor protein mitogen-activated protein kinase (MAPK) -activating death domain (MADD; also calledDENN), which was first identified as a RAB3 guanine nucleotide exchange factor (GEF). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 17543632 625 NAVSLHHALAEPAPDYK---KKSFVFRVRIAHGGeILFQTSNQKELQEWCEKIN 675
Cdd:cd01233  47 GVINLSTARVEYSPDQEallGRPNVFAVYTPTNS-YLLQARSEKEMQDWLYAID 99

Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the first PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543632 571 SGFLMRKyvretdgGKTpfgRRSWRMVYARLRG--LVLYFDTDEHpkatsryaSLENAVSLH--HALAePAPDyKKKSFV 646
Cdd:cd13298   9 SGYLLKR-------SRK---TKNWKKRWVVLRPcqLSYYKDEKEY--------KLRRVINLSelLAVA-PLKD-KKRKNV 68

                        90       100       110
                ....*....|....*....|....*....|...
gi 17543632 647 FRV----RIAHggeilFQTSNQKELQEWCEKIN 675
Cdd:cd13298  69 FGIytpsKNLH-----FRATSEKDANEWVEALR 96