Domain of unknown function (DUF3480); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 350 to 362 amino acids in length. This domain is found associated with pfam01363.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508810  329 LPTPPYLFGILIQKWETPWAKVFPIRLLLRLGAEYRLYPCPLFSVRFRKPLFGETGHTIMNLLADFRNYQYTLPVVQGLV 408
Cdd:pfam11979   1 LPTPPYLFGVLIHKWEVPWAKVFPLRLMLRLGAEYRYYPCPLVSVRFRKSLYGEIGHTIMNLLADFRNYQYTLPVVPGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508810  409 VDMEVRKTSIKIPSNRYNEMMKAMNKSNEHVLAGGACFNEKADSHLVCVQNDDGNYQTQAISIHNQPRKVTGASFFVFSG 488
Cdd:pfam11979  81 IHMEDKKTTILIPKNRYDEVMKVLNKSNEHVLAIGANFSEEADSHLVCVQNDDGNYQTQAISIHGKPRKVTGASFIVFNG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508810  489 ALKSSSGYLAKSSIVEDGVMVQITAENMDSLRQALREMKDFTITCGKADAEDPQEQIHIQWVDDDKTVNKGVVSPIDGKS 568
Cdd:pfam11979 161 ALKSSSGFLAKSSIVEDGLMVQITPEKMEELRQALREMKDFTITCGKLDDEDSKEVVNIKWVDDDPKFNIGVKSPIDGKS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508810  569 MESITNVKIFHGSEYKANGKVIRWTEVFFLENDDHHNCLSDPADHSRLTEHVAKAFCLALCPHLKLLKEDGMTKLGLRVT 648
Cdd:pfam11979 241 LEGVPSIRIHQGSDYKGKGKLIRWTEVFYLQKEDDSSRPSDPADISRLAETIAKACCAALVPHLDLLKAAGITKLGLRVT 320

                         330       340       350
                  ....*....|....*....|....*....|...
gi 119508810  649 LDSDQVGYQAGSNGQPLPSQYMNDLDSALVPVI 681
Cdd:pfam11979 321 LDPDEVEYQAGSNGQPLPPLYMNSLDNALIPVL 353

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
                 ....*....|....*....|....*....|..
gi 119508810   7 KVFCASCCSLKCKLLYMDRKEARVCVICHSVL 38
Cdd:cd15729   37 KVLCSACCSLKARLEYLDNKEARVCVPCYQTL 68

Domain of unknown function (DUF3480); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 350 to 362 amino acids in length. This domain is found associated with pfam01363.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508810  329 LPTPPYLFGILIQKWETPWAKVFPIRLLLRLGAEYRLYPCPLFSVRFRKPLFGETGHTIMNLLADFRNYQYTLPVVQGLV 408
Cdd:pfam11979   1 LPTPPYLFGVLIHKWEVPWAKVFPLRLMLRLGAEYRYYPCPLVSVRFRKSLYGEIGHTIMNLLADFRNYQYTLPVVPGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508810  409 VDMEVRKTSIKIPSNRYNEMMKAMNKSNEHVLAGGACFNEKADSHLVCVQNDDGNYQTQAISIHNQPRKVTGASFFVFSG 488
Cdd:pfam11979  81 IHMEDKKTTILIPKNRYDEVMKVLNKSNEHVLAIGANFSEEADSHLVCVQNDDGNYQTQAISIHGKPRKVTGASFIVFNG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508810  489 ALKSSSGYLAKSSIVEDGVMVQITAENMDSLRQALREMKDFTITCGKADAEDPQEQIHIQWVDDDKTVNKGVVSPIDGKS 568
Cdd:pfam11979 161 ALKSSSGFLAKSSIVEDGLMVQITPEKMEELRQALREMKDFTITCGKLDDEDSKEVVNIKWVDDDPKFNIGVKSPIDGKS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508810  569 MESITNVKIFHGSEYKANGKVIRWTEVFFLENDDHHNCLSDPADHSRLTEHVAKAFCLALCPHLKLLKEDGMTKLGLRVT 648
Cdd:pfam11979 241 LEGVPSIRIHQGSDYKGKGKLIRWTEVFYLQKEDDSSRPSDPADISRLAETIAKACCAALVPHLDLLKAAGITKLGLRVT 320

                         330       340       350
                  ....*....|....*....|....*....|...
gi 119508810  649 LDSDQVGYQAGSNGQPLPSQYMNDLDSALVPVI 681
Cdd:pfam11979 321 LDPDEVEYQAGSNGQPLPPLYMNSLDNALIPVL 353

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
                 ....*....|....*....|....*....|..
gi 119508810   7 KVFCASCCSLKCKLLYMDRKEARVCVICHSVL 38
Cdd:cd15729   37 KVLCSACCSLKARLEYLDNKEARVCVPCYQTL 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
                   ....*....|....*....|....*....|...
gi 119508810     7 KVFCASCCSLKCKLLYMDR-KEARVCVICHSVL 38
Cdd:smart00064  34 RIFCSKCSSKKAPLPKLGIeRPVRVCDDCYENL 66

Domain of unknown function (DUF3480); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 350 to 362 amino acids in length. This domain is found associated with pfam01363.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508810  329 LPTPPYLFGILIQKWETPWAKVFPIRLLLRLGAEYRLYPCPLFSVRFRKPLFGETGHTIMNLLADFRNYQYTLPVVQGLV 408
Cdd:pfam11979   1 LPTPPYLFGVLIHKWEVPWAKVFPLRLMLRLGAEYRYYPCPLVSVRFRKSLYGEIGHTIMNLLADFRNYQYTLPVVPGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508810  409 VDMEVRKTSIKIPSNRYNEMMKAMNKSNEHVLAGGACFNEKADSHLVCVQNDDGNYQTQAISIHNQPRKVTGASFFVFSG 488
Cdd:pfam11979  81 IHMEDKKTTILIPKNRYDEVMKVLNKSNEHVLAIGANFSEEADSHLVCVQNDDGNYQTQAISIHGKPRKVTGASFIVFNG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508810  489 ALKSSSGYLAKSSIVEDGVMVQITAENMDSLRQALREMKDFTITCGKADAEDPQEQIHIQWVDDDKTVNKGVVSPIDGKS 568
Cdd:pfam11979 161 ALKSSSGFLAKSSIVEDGLMVQITPEKMEELRQALREMKDFTITCGKLDDEDSKEVVNIKWVDDDPKFNIGVKSPIDGKS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119508810  569 MESITNVKIFHGSEYKANGKVIRWTEVFFLENDDHHNCLSDPADHSRLTEHVAKAFCLALCPHLKLLKEDGMTKLGLRVT 648
Cdd:pfam11979 241 LEGVPSIRIHQGSDYKGKGKLIRWTEVFYLQKEDDSSRPSDPADISRLAETIAKACCAALVPHLDLLKAAGITKLGLRVT 320

                         330       340       350
                  ....*....|....*....|....*....|...
gi 119508810  649 LDSDQVGYQAGSNGQPLPSQYMNDLDSALVPVI 681
Cdd:pfam11979 321 LDPDEVEYQAGSNGQPLPPLYMNSLDNALIPVL 353

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
                 ....*....|....*....|....*....|..
gi 119508810   7 KVFCASCCSLKCKLLYMDRKEARVCVICHSVL 38
Cdd:cd15729   37 KVLCSACCSLKARLEYLDNKEARVCVPCYQTL 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
                   ....*....|....*....|....*....|...
gi 119508810     7 KVFCASCCSLKCKLLYMDR-KEARVCVICHSVL 38
Cdd:smart00064  34 RIFCSKCSSKKAPLPKLGIeRPVRVCDDCYENL 66