FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the first FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 682443595  187 RTHWQKNGYNDVCTEpsCGKRLGPVNGNINCRKCGRLFCEDHTMYQMKLSRSAQHEPVRGFWCRCCETCYKSREGYND 264
Cdd:cd15761     1 RSHWKKPSGKSRCSE--CGKTLNKKNGIVNCRKCGELFCNEHCRNRIKLNNSAEYDPKNGKWCRCCEKCFTSRPGYND 76

Rabenosyn Rab binding domain; Rabenosyn-5 (Rbsn) is a multivalent effector with interacts with the Rab family.Rsbn contains distinct Rab4 and Rab5 binding sites within residues 264-500 and 627-784 respectively. Rab proteins are GTPases involved in the regulation of all stages of membrane trafficking.

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 682443595   611 EQKFMVSEMIADANKRRKFDEVSSLSMNMEDLSKEIDQV 649
Cdd:pfam11464    1 EQIFLVESMIKQAKKARRFDEVATLEENLRELQREIDRL 39

Rad18-like CCHC zinc finger; Yeast Rad18p functions with Rad5p in error-free post-replicative DNA repair. This zinc finger is likely to bind nucleic-acids.

                            10        20
                    ....*....|....*....|...
gi 682443595     83 KLICPICNEEMMtLLQLNRHLDD 105
Cdd:smart00734    1 LVQCPVCFREVP-ENLINSHLDS 22

FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the first FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 682443595  187 RTHWQKNGYNDVCTEpsCGKRLGPVNGNINCRKCGRLFCEDHTMYQMKLSRSAQHEPVRGFWCRCCETCYKSREGYND 264
Cdd:cd15761     1 RSHWKKPSGKSRCSE--CGKTLNKKNGIVNCRKCGELFCNEHCRNRIKLNNSAEYDPKNGKWCRCCEKCFTSRPGYND 76

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443595   336 VTWEEDAKVAKCPFCQQEFgNWTFRRHHCRICGRVVCADsrtgCSSEIGLNvsrsmhvpflvasyyyhaeayidtdIPPG 415
Cdd:pfam01363    1 PVWVPDSSATVCMICSKPF-TFFRRRHHCRNCGRVFCSA----CSSKKISL-------------------------LPEL 50

                           90
                   ....*....|....*...
gi 682443595   416 SMNIDVRMCRDCRTTIFS 433
Cdd:pfam01363   51 GSNKPVRVCDACYDTLQK 68

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 682443595    187 RTHWQKNGYNDVCtePSCGKRLGPVNGNINCRKCGRLFCEDHTMYQMKLSRSAQHEPVrgfwcRCCETCYKSREG 261
Cdd:smart00064    1 RPHWIPDEEVSNC--MGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIERPV-----RVCDDCYENLNG 68

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443595   864 VIISLVYLGLYTGAINTVNPTGD--LDITEVLLYVFTLGFLCDEFSKFWKVG---RFYLGFWNVFNLILYSLLTISFVtr 938
Cdd:pfam00520    7 FILLLILLNTIFLALETYFQPEEplTTVLEILDYVFTGIFTLEMLLKIIAAGfkkRYFRSPWNILDFVVVLPSLISLV-- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443595   939 cialshpieddhdgqrerfNELSYNFLAFSAPMFWgRLLLFMDTFRFFG---AMLVVLKVMMKEslIFFALLIVVIVGFL 1015
Cdd:pfam00520   85 -------------------LSSVGSLSGLRVLRLL-RLLRLLRLIRRLEglrTLVNSLIRSLKS--LGNLLLLLLLFLFI 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443595  1016 QAFIGM-----------------DNVDNKSDATVFILQNMANAILGSPDFSGFDAFAPPFGIILYYIFTFTVMVILLNIL 1078
Cdd:pfam00520  143 FAIIGYqlfggklktwenpdngrTNFDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLF 222

                          250
                   ....*....|..
gi 682443595  1079 IALYNSAYEDIT 1090
Cdd:pfam00520  223 IAVIIDNFQELT 234

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 682443595   188 THWQKNGYNDVCtePSCGKRLGPVNGNINCRKCGRLFCEDHTMYQM-KLSRSAQHEPVrgfwcRCCETCYK 257
Cdd:pfam01363    1 PVWVPDSSATVC--MICSKPFTFFRRRHHCRNCGRVFCSACSSKKIsLLPELGSNKPV-----RVCDACYD 64

Rad18-like CCHC zinc finger; Yeast Rad18p functions with Rad5p in error-free post-replicative DNA repair. This zinc finger is likely to bind nucleic-acids.

                            10        20
                    ....*....|....*....|...
gi 682443595     83 KLICPICNEEMMtLLQLNRHLDD 105
Cdd:smart00734    1 LVQCPVCFREVP-ENLINSHLDS 22

FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the first FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 682443595  187 RTHWQKNGYNDVCTEpsCGKRLGPVNGNINCRKCGRLFCEDHTMYQMKLSRSAQHEPVRGFWCRCCETCYKSREGYND 264
Cdd:cd15761     1 RSHWKKPSGKSRCSE--CGKTLNKKNGIVNCRKCGELFCNEHCRNRIKLNNSAEYDPKNGKWCRCCEKCFTSRPGYND 76

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443595   336 VTWEEDAKVAKCPFCQQEFgNWTFRRHHCRICGRVVCADsrtgCSSEIGLNvsrsmhvpflvasyyyhaeayidtdIPPG 415
Cdd:pfam01363    1 PVWVPDSSATVCMICSKPF-TFFRRRHHCRNCGRVFCSA----CSSKKISL-------------------------LPEL 50

                           90
                   ....*....|....*...
gi 682443595   416 SMNIDVRMCRDCRTTIFS 433
Cdd:pfam01363   51 GSNKPVRVCDACYDTLQK 68

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 682443595    187 RTHWQKNGYNDVCtePSCGKRLGPVNGNINCRKCGRLFCEDHTMYQMKLSRSAQHEPVrgfwcRCCETCYKSREG 261
Cdd:smart00064    1 RPHWIPDEEVSNC--MGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIERPV-----RVCDDCYENLNG 68

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443595   864 VIISLVYLGLYTGAINTVNPTGD--LDITEVLLYVFTLGFLCDEFSKFWKVG---RFYLGFWNVFNLILYSLLTISFVtr 938
Cdd:pfam00520    7 FILLLILLNTIFLALETYFQPEEplTTVLEILDYVFTGIFTLEMLLKIIAAGfkkRYFRSPWNILDFVVVLPSLISLV-- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443595   939 cialshpieddhdgqrerfNELSYNFLAFSAPMFWgRLLLFMDTFRFFG---AMLVVLKVMMKEslIFFALLIVVIVGFL 1015
Cdd:pfam00520   85 -------------------LSSVGSLSGLRVLRLL-RLLRLLRLIRRLEglrTLVNSLIRSLKS--LGNLLLLLLLFLFI 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443595  1016 QAFIGM-----------------DNVDNKSDATVFILQNMANAILGSPDFSGFDAFAPPFGIILYYIFTFTVMVILLNIL 1078
Cdd:pfam00520  143 FAIIGYqlfggklktwenpdngrTNFDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLF 222

                          250
                   ....*....|..
gi 682443595  1079 IALYNSAYEDIT 1090
Cdd:pfam00520  223 IAVIIDNFQELT 234

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; The family includes Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and protein VAC1 (Vac1p). scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The FYVE domain in both Vps27p and Vac1p harbors a zinc-binding site composed of seven Cysteines and one Histidine, which is different from that of other FYVE domain containing proteins.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 682443595  203 SCGKRLGPVNGNINCRKCGRLFCEDHTMYQMKLSRSAqHEPVRGFWCRCCETCY 256
Cdd:cd15736     4 TCSRTFNLNIRAHHCRKCGKLFCRRHLPNMIPLNLSA-YDPRNGKWYRCCHSCF 56

FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443595  346 KCPFCQQEFGnWTFRRHHCRICGRVVCADsrtgCSSEIGLnvsrsmhvpflvasyyyhaeayidtdIPPGSMNIDVRMCR 425
Cdd:cd00065     1 RCMLCGKKFS-LFRRRHHCRRCGRVFCSK----CSSKKLP--------------------------LPSFGSGKPVRVCD 49

                  ..
gi 682443595  426 DC 427
Cdd:cd00065    50 SC 51

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443595   914 RFYLG-FWNVFNLILYSLLTISFVTR------CI-ALSHPIEddhdgQRERF--NELSYNFLAFSAPMFWGRLLLFMDTF 983
Cdd:TIGR00870  416 FEYIHqLWNILDFGMNSFYLATFLDRpfailfVTqAFLVLRE-----HWLRFdpTLIEEALFAFALVLSWLNLLYIFRGN 490

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443595   984 RFFGAMLVVLKVMMKESLI-FFALLIVVIVGFLQAF-----------IGMDNVDNKSDA--------TVF-ILQNMANAI 1042
Cdd:TIGR00870  491 QHLGPLQIMIGRMILGDILrFLFIYAVVLFGFACGLnqlyqyydelkLNECSNPHARSCekqgnaysTLFeTSQELFWAI 570

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443595  1043 LGSPDFSGFD-AFAPPFGIILYYIFTFTVMVILLNILIALYNSAYEDITGNALDEYMALFAQKTMQYVRapDENVFIAPF 1121
Cdd:TIGR00870  571 IGLGDLLANEhKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMSYER--EGGTCPPPF 648

                   ...
gi 682443595  1122 NLI 1124
Cdd:TIGR00870  649 NII 651

FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar proteins; FGD6, also termed zinc finger FYVE domain-containing protein 24 is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) whose biological function remains unclear. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Moreover, the FYVE domain of FGD6 is a canonical FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 682443595  338 WEEDAKVAKCPFCQQEFgNWTFRRHHCRICGRVVCAdsrtGCSS 381
Cdd:cd15743     3 WIPDSRVTMCMICTSEF-TVTWRRHHCRACGKVVCG----SCSS 41

FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar proteins; ZFYV1, also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYV1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by wortmannin, a PI3-kinase inhibitor. In addition to C-terminal tandem FYVE domain, ZFYV1 contains an N-terminal putative C2H2 type zinc finger and a possible nucleotide binding P-loop.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 682443595  338 WEEDAKVAKCPFCQQEFGNwTFRRHHCRICGRVVCADsrtgCSSEIGLNVSR 389
Cdd:cd15734     2 WVPDSEIKECSVCKRPFSP-RLSKHHCRACGQGVCDD----CSKNRRPVPSR 48

FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 682443595  202 PSCGKRLGPVNGNINCRKCGRLFCEDHTMYQMKLSRSAQHEPVrgfwcRCCETCY 256
Cdd:cd00065     3 MLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSFGSGKPV-----RVCDSCY 52

FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE domain-containing protein 16 (ZFY16), or endosome-associated FYVE domain protein, is a FYVE domain-containing protein that is localized to EEA1-containing endosomes. It is regulated by phosphoinositol lipid and engaged in endosome-mediated receptor modulation. Endofin is involved in Bone morphogenetic protein (BMP) signaling through interacting with Smad1 preferentially and enhancing Smad1 phosphorylation and nuclear localization upon BMP stimulation. It also functions as a scaffold protein that brings Smad4 to the proximity of the receptor complex in Transforming growth factor (TGF)-beta signaling. Moreover, endofin is a novel tyrosine phosphorylation target downstream of epidermal growth factor receptor (EGFR) in EGF-signaling. In addition, endofin plays a role in endosomal trafficking by recruiting cytosolic TOM1, an important molecule for membrane recruitment of clathrin, onto endosomal membranes.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 682443595  337 TWEEDAKVAKCPFCQQEFgnwTF--RRHHCRICGRVVCAD 374
Cdd:cd15729     6 VWVPDSEAPNCMQCEVKF---TFtkRRHHCRACGKVLCSA 42

FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This family includes a group of uncharacterized rab GTPase-binding effector proteins found in bilateria. Although their biological functions remain unclear, they all contain a FYVE domain that harbors a putative phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding site.

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 682443595  336 VTWEEDAKVAKCPFCQQEFGNwTFRRHHCRICGRVVCAD 374
Cdd:cd15739     2 VRWQHEDDVDQCPNCKTPFSV-GKRKHHCRHCGKIFCSD 39

FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed FYVE domain-containing centrosomal protein (FYVE-CENT), or spastizin, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that localizes to the centrosome and midbody. ZFY26 and its interacting partners TTC19 and KIF13A are required for cytokinesis. It also interacts with Beclin 1, a subunit of class III phosphatidylinositol 3-kinase complex, and may have potential implications for carcinogenesis. In addition, it has been considered as the causal agent of a rare form of hereditary spastic paraplegia. ZFY26 contains a FYVE domain that is important for targeting of FYVE-CENT to the midbody.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 682443595  338 WEEDAKVAKCPFCQQEFGNWTFRRHHCRICGRVVCADsrtgCS 380
Cdd:cd15724     1 WVPDEAVSVCMVCQVERFSMFNRRHHCRRCGRVVCSS----CS 39

FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, also termed FYVE finger-containing phosphoinositide kinase, or 1-phosphatidylinositol 3-phosphate 5-kinase, or phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase), is a phosphoinositide 5-kinase that forms a complex with its regulators, the scaffolding protein Vac14 and the lipid phosphatase Fig4. The complex is responsible for synthesizing phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2] from phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). Then phosphatidylinositol-5-phosphate (PtdIns5P) is generated directly from PtdIns(3,5)P2. PtdIns(3,5)P2 and PtdIns5P regulate endosomal trafficking and responses to extracellular stimuli. At this point, PIKfyve is vital in early embryonic development. Moreover, PIKfyve forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, which plays a role in receptor tyrosine kinase (RTK) degradation. The phosphorylation of PIKfyve by AKT can facilitate Epidermal growth factor receptor (EGFR) degradation. In addition, PIKfyve may participate in the regulation of the glutamate transporters EAAT2, EAAT3 and EAAT4, and the cystic fibrosis transmembrane conductance regulator (CFTR). It is also essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle. It can be activated by protein kinase B (PKB/Akt) and further up-regulates human ether-a-go-go (hERG) channels. This family also includes the yeast and plant orthologs of human PIKfyve, Fab1. PIKfyve and its orthologs share a similar architecture. They contain an N-terminal FYVE domain, a middle region related to the CCT/TCP-1/Cpn60 chaperonins that are involved in productive folding of actin and tubulin, a second middle domain that contains a number of conserved cysteine residues (CCR) unique to this family, and a C-terminal lipid kinase domain related to PtdInsP kinases.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 682443595  338 WEEDAKVAKCPFCQQEFGnwTFRR-HHCRICGRVVCAdsrTGCSSEI 383
Cdd:cd15725     2 WMPDSSCKECYECSEKFT--TFRRrHHCRLCGQIFCS---RCCNQEI 43

FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also termed FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2), or zinc finger FYVE domain-containing protein 11, is an dual specificity protein phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). It is localizes to early endosomes, as well as to Rab11- and Sec15-positive recycling endosomes, and regulates sorting from early endosomes. Moreover, MTMR4 is preferentially associated with and dephosphorylated the activated regulatory Smad proteins (R-Smads) in cytoplasm to keep transforming growth factor (TGF) beta signaling in homeostasis. It also functions as an essential negative modulator for the homeostasis of bone morphogenetic protein (BMP)/decapentaplegic (Dpp) signaling. In addition, MTMR4 acts as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4) and may play a role in the biological process of muscle breakdown. MTMR4 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 682443595  338 WEEDAKVAKCPFCQQEFgnWTF-RRHHCRICGRVVCADsrtgCSS 381
Cdd:cd15733     1 WVPDHAASHCFGCDCEF--WLAkRKHHCRNCGNVFCAD----CSN 39

FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1 and RUFY2. RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. Both RUFY1 and RUFY2 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 682443595  338 WEEDAKVAKCPFCQQEFgNWTFRRHHCRICGRVVCADsrtgCSS 381
Cdd:cd15721     1 WADDKEVTHCQQCEKEF-SLSRRKHHCRNCGGIFCNS----CSD 39

FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar proteins; WDFY3, also termed autophagy-linked FYVE protein (Alfy), is a ubiquitously expressed phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein required for selective macroautophagic degradation of aggregated proteins. It regulates the protein degradation through the direct interaction with the autophagy protein Atg5. Moreover, WDFY3 acts as a scaffold that bridges its cargo to the macroautophagic machinery via the creation of a greater complex with Atg12, Atg16L, and LC3. It also functionally associates with sequestosome-1/p62 (SQSTM1) in osteoclasts. WDFY3 shuttles between the nucleus and cytoplasm. It predominantly localizes to the nucleus and nuclear membrane under basal conditions, but is recruited to cytoplasmic ubiquitin-positive protein aggregates under stress conditions. WDFY3 contains a PH-BEACH domain assemblage, five WD40 repeats and a PtdIns3P-binding FYVE domain.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443595  338 WEEDAKVAKCPFCQQEFgNWTFRRHHCRICGRVVCADsrtgCS---SEIG-LNVSRSMHV 393
Cdd:cd15719     3 WVKDEGGDSCTGCSVRF-SLTERRHHCRNCGQLFCSK----CSrfeSEIRrLRISRPVRV 57

FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also termed Myotubularin-related phosphatase 3, or FYVE domain-containing dual specificity protein phosphatase 1 (FYVE-DSP1), or zinc finger FYVE domain-containing protein 10, is a ubiquitously expressed phosphoinositide 3-phosphatase specific for phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and PIKfyve, which produces PtdIns(3,5)P2 from PtdIns3P. It regulates cell migration through modulating phosphatidylinositol 5-phosphate (PtdIns5P) levels. MTMR3 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain. Unlike conventional FYVE domains, the FYVE domain of MTMR3 neither confers endosomal localization nor binds to PtdIns3P. It is also not required for the enzyme activity of MTMR3. In contrast, the PH-G domain binds phosphoinositides.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 682443595  338 WEEDAKVAKCPFCQQEFgnW-TFRRHHCRICGRVVCAdsrtGCSseiglnvSRSMHVP 394
Cdd:cd15732     2 WVPDHLAASCYGCEREF--WlASRKHHCRNCGNVFCG----SCC-------NQKLPVP 46

FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins; ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 682443595  347 CPFCQQEFGnWTFRRHHCRICGRVVCADsrtgCSS 381
Cdd:cd15728    10 CYECGVKFG-ITTRKHHCRHCGRLLCSK----CST 39

FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar proteins; Phafin-2, also termed endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains (EAPF), or pleckstrin homology domain-containing family F member 2 (PKHF2), or PH domain-containing family F member 2, or PH and FYVE domain-containing protein 2, or zinc finger FYVE domain-containing protein 18, is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 682443595  338 WEEDAKVAKCPFCQQEFGNWTFRRHHCRICGRVVCADsrtgCSSEIGLNVSRSMHvPFLVASYYY 402
Cdd:cd15755     2 WVPDSEATVCMRCQKAKFTPVNRRHHCRKCGFVVCGP----CSEKKFLLPSQSSK-PVRVCDFCY 61

FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) and similar proteins; Hrs, also termed protein pp110, is a tyrosine phosphorylated protein that plays an important role in the signaling pathway of HGF. It is localized to early endosomes and an essential component of the endosomal sorting and trafficking machinery. Hrs interacts with hypertonia-associated protein Trak1, a novel regulator of endosome-to-lysosome trafficking. It can also forms an Hrs/actinin-4/BERP/myosin V protein complex that is required for efficient transferrin receptor (TfR) recycling but not for epidermal growth factor receptor (EGFR) degradation. Moreover, Hrs, together with STAM proteins, STAM1 and STAM2, and EPs15, forms a multivalent ubiquitin-binding complex that sorts ubiquitinated proteins into the multivesicular body pathway, and plays a regulatory role in endocytosis/exocytosis. Furthermore, Hrs functions as an interactor of the neurofibromatosis 2 tumor suppressor protein schwannomin/merlin. It is also involved in the inhibition of citron kinase-mediated HIV-1 budding. Hrs contains a single ubiquitin-interacting motif (UIM) that is crucial for its function in receptor sorting, and a FYVE domain that harbors double Zn2+ binding sites.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 682443595  346 KCPFCQQEFGNWTfRRHHCRICGRVVCADsrtgCSS 381
Cdd:cd15720     7 ECHRCRVQFGVFQ-RKHHCRACGQVFCGK----CSS 37

Rad18-like CCHC zinc finger; Yeast Rad18p functions with Rad5p in error-free post-replicative DNA repair. This zinc finger is likely to bind nucleic-acids.

                            10        20
                    ....*....|....*....|...
gi 682443595     83 KLICPICNEEMMtLLQLNRHLDD 105
Cdd:smart00734    1 LVQCPVCFREVP-ENLINSHLDS 22

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; The family includes Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and protein VAC1 (Vac1p). scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The FYVE domain in both Vps27p and Vac1p harbors a zinc-binding site composed of seven Cysteines and one Histidine, which is different from that of other FYVE domain containing proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 682443595  347 CPFCQQEFGNWTfRRHHCRICGRVVCADSrtgCSSEIGLNVS 388
Cdd:cd15736     2 CHTCSRTFNLNI-RAHHCRKCGKLFCRRH---LPNMIPLNLS 39

Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse group of secondary transporters that includes uniporters, symporters, and antiporters. MFS proteins facilitate the transport across cytoplasmic or internal membranes of a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides. They do so using the electrochemical potential of the transported substrates. Uniporters transport a single substrate, while symporters and antiporters transport two substrates in the same or in opposite directions, respectively, across membranes. MFS proteins are typically 400 to 600 amino acids in length, and the majority contain 12 transmembrane alpha helices (TMs) connected by hydrophilic loops. The N- and C-terminal halves of these proteins display weak similarity and may be the result of a gene duplication/fusion event. Based on kinetic studies and the structures of a few bacterial superfamily members, GlpT (glycerol-3-phosphate transporter), LacY (lactose permease), and EmrD (multidrug transporter), MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Bacterial members function primarily for nutrient uptake, and as drug-efflux pumps to confer antibiotic resistance. Some MFS proteins have medical significance in humans such as the glucose transporter Glut4, which is impaired in type II diabetes, and glucose-6-phosphate transporter (G6PT), which causes glycogen storage disease when mutated.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443595  972 FWGRLLLFMDTFRFFGAMLVVLKVMMKESLIFFALLIVVIVGFLQAFIGM----DNVDNKSDATVFILQNMANAILGspd 1047
Cdd:cd06174   266 LIGRKPLLLIGLLLMALGLALLLLAPSLLLLLLLLLLLGFGLGGLLPLSFaliaELFPPEIRGTAFGLLNTFGFLGG--- 342

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 682443595 1048 fsgfdAFAPP-FGIILYYIFTFTVMVILLNILIALY 1082
Cdd:cd06174   343 -----AIGPLlAGFLLAATFGLTGAFLVLAVLLLLA 373

Stage II sporulation protein M; SpoIIM is on e of four stage II sporulation proteins that is necessary for the forespore inside the mother-cell to be properly internalized through the breakdown of peptidoglycans trapped between the membranes of the septum separating the forespore and the mother-cell. The four proteins working in sequence are SpoIIB, pfam05036, SpoIIM, SpoIIP, pfam07454, and finally SpoIID, pfam08486. D, M and P are in a complex with each other and the complex assembles in a hierarchical manner such that M, which serves as a membrane anchor, recruits P to the septum and P, in turn, recruits D to the septum.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443595  1000 SLIFFALLIVVivgflqAFIGMDNVDNKSDATVFILQNMANAILGSPDFSGFDAFappFGIILYYIFTFTVMVIL----- 1074
Cdd:pfam01944    1 ALLLFLVGIIL------GALLANSLSDKQELLAYLGSFLEIFGSYYINGPAPSFF---LQIFTNNLKVALLIFLLgltli 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682443595  1075 --LNILIALYNSAyedITGnaldeymaLFAQKTMQYVRAPDENVFIAPFNLIEI--------FGLILPFEWwISKRTYMK 1144
Cdd:pfam01944   72 glPTILILFFNGF---ILG--------TVGFLVAQLGGLLLFLAFILPHGILELpaiiiagaAGLRLGWAL-LKPGFRTR 139

                          170       180
                   ....*....|....*....|....*....
gi 682443595  1145 LNDY--------VMAVIYAPLLIVAAFFE 1165
Cdd:pfam01944  140 GRALkeagrellKYLLGLVPLLLIAALIE 168