Protein kinase Fus3-binding; This domain family is found in eukaryotes, and is approximately 190 amino acids in length. This domain is the penultimate C terminal domain from the protein ste5 which co-catalyzes the phosphorylation of fus3 by ste7. It is involved in the MAPK pathways. This domain is the minimal scaffold domain of ste5. It binds to the mitogen activated protein kinase fus3 before it is phosphorylated.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320308    594 TTISSILSLKREKPDNLAIILQIDFTKLKEEDSLiVVYNSLKALTIKFARLQFCFVDRNNYVLDYGSVLHKIDSLDSISN 673
Cdd:pfam12194   1 TTISSILSLKRERPDELVLVLQLDFRKLKDDDYL-TIYNTLKALTLKYPDLKLCIVDSEGFVITIGLVKDFLSNLDSLLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320308    674 LKSKSSSTQFSPIWLKNTLYPENIHEHLGIVAVSNSNMEAKKSILFQDYRCFTSFGRRRPNELKIKVGYLNVDYSDKIDE 753
Cdd:pfam12194  80 LVKDKGTIKFSPSWLKNTLYPAGILKNIGIVIISNSSMEEGKSCLLMDYSPFASKGRRRPNELKIKVGYLNVDYSDKISE 159

                         170       180
                  ....*....|....*....|..
gi 6320308    754 LVEASSWTFVLETLCYSFGLSF 775
Cdd:pfam12194 160 LVEIGSWNDLLEALCYSFSLNF 181

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enable efficient transfer of ubiquitin from E2 to the substrates.

                        10        20        30
                ....*....|....*....|....*....|...
gi 6320308  175 ASCTLCDEPISNRRKGEKIIELACGHLSHQECL 207
Cdd:cd16687   1 DSCCICLKPYKRREDNDEVIVFSCGHAYHSTCL 33

Protein kinase Fus3-binding; This domain family is found in eukaryotes, and is approximately 190 amino acids in length. This domain is the penultimate C terminal domain from the protein ste5 which co-catalyzes the phosphorylation of fus3 by ste7. It is involved in the MAPK pathways. This domain is the minimal scaffold domain of ste5. It binds to the mitogen activated protein kinase fus3 before it is phosphorylated.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320308    594 TTISSILSLKREKPDNLAIILQIDFTKLKEEDSLiVVYNSLKALTIKFARLQFCFVDRNNYVLDYGSVLHKIDSLDSISN 673
Cdd:pfam12194   1 TTISSILSLKRERPDELVLVLQLDFRKLKDDDYL-TIYNTLKALTLKYPDLKLCIVDSEGFVITIGLVKDFLSNLDSLLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320308    674 LKSKSSSTQFSPIWLKNTLYPENIHEHLGIVAVSNSNMEAKKSILFQDYRCFTSFGRRRPNELKIKVGYLNVDYSDKIDE 753
Cdd:pfam12194  80 LVKDKGTIKFSPSWLKNTLYPAGILKNIGIVIISNSSMEEGKSCLLMDYSPFASKGRRRPNELKIKVGYLNVDYSDKISE 159

                         170       180
                  ....*....|....*....|..
gi 6320308    754 LVEASSWTFVLETLCYSFGLSF 775
Cdd:pfam12194 160 LVEIGSWNDLLEALCYSFSLNF 181

RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 8 (Vps8) and similar proteins; Vps8 is the Rab-specific subunit of the endosomal tethering complex CORVET (class C core vacuole/endosome transport) that also includes Vps3 and a Class C Vps core complex composed of Vps11, Vps16, Vps18, and Vps33. CORVET operates at endosomes, controls traffic into late endosomes, and interacts with the Rab5/Vps21-GTP form. The CORVET-specific Vps3 and Vps8 subunits belong to the class D Vps. They form a subcomplex that interact with Rab5/Vps21, and is critical for localization and function of the CORVET tethering complex on endosomes. Vps8 contains an N-terminal WD40 repeat and a C-terminal C3H2C3-type RING-H2 finger.

                        10        20        30
                ....*....|....*....|....*....|...
gi 6320308  175 ASCTLCDEPISNRRKGEKIIELACGHLSHQECL 207
Cdd:cd16687   1 DSCCICLKPYKRREDNDEVIVFSCGHAYHSTCL 33

Protein kinase Fus3-binding; This domain family is found in eukaryotes, and is approximately 190 amino acids in length. This domain is the penultimate C terminal domain from the protein ste5 which co-catalyzes the phosphorylation of fus3 by ste7. It is involved in the MAPK pathways. This domain is the minimal scaffold domain of ste5. It binds to the mitogen activated protein kinase fus3 before it is phosphorylated.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320308    594 TTISSILSLKREKPDNLAIILQIDFTKLKEEDSLiVVYNSLKALTIKFARLQFCFVDRNNYVLDYGSVLHKIDSLDSISN 673
Cdd:pfam12194   1 TTISSILSLKRERPDELVLVLQLDFRKLKDDDYL-TIYNTLKALTLKYPDLKLCIVDSEGFVITIGLVKDFLSNLDSLLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320308    674 LKSKSSSTQFSPIWLKNTLYPENIHEHLGIVAVSNSNMEAKKSILFQDYRCFTSFGRRRPNELKIKVGYLNVDYSDKIDE 753
Cdd:pfam12194  80 LVKDKGTIKFSPSWLKNTLYPAGILKNIGIVIISNSSMEEGKSCLLMDYSPFASKGRRRPNELKIKVGYLNVDYSDKISE 159

                         170       180
                  ....*....|....*....|..
gi 6320308    754 LVEASSWTFVLETLCYSFGLSF 775
Cdd:pfam12194 160 LVEIGSWNDLLEALCYSFSLNF 181

RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 8 (Vps8) and similar proteins; Vps8 is the Rab-specific subunit of the endosomal tethering complex CORVET (class C core vacuole/endosome transport) that also includes Vps3 and a Class C Vps core complex composed of Vps11, Vps16, Vps18, and Vps33. CORVET operates at endosomes, controls traffic into late endosomes, and interacts with the Rab5/Vps21-GTP form. The CORVET-specific Vps3 and Vps8 subunits belong to the class D Vps. They form a subcomplex that interact with Rab5/Vps21, and is critical for localization and function of the CORVET tethering complex on endosomes. Vps8 contains an N-terminal WD40 repeat and a C-terminal C3H2C3-type RING-H2 finger.

                        10        20        30
                ....*....|....*....|....*....|...
gi 6320308  175 ASCTLCDEPISNRRKGEKIIELACGHLSHQECL 207
Cdd:cd16687   1 DSCCICLKPYKRREDNDEVIVFSCGHAYHSTCL 33