Annotations: 5SZG

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Mical/EHBP Rab binding (bMERB) domain-like	8047251	4005529	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Mical/EHBP Rab binding (bMERB) domain-like	8092904	3002641	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Mical/EHBP Rab binding (bMERB) domain-like	8092904	3002641	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	DUF3585	e5szgA1	A: alpha bundles	X: Long alpha-hairpin	H: bMERB domain (bivalent Mical/EHBP Rab binding) (From Topology)	T: bMERB domain (bivalent Mical/EHBP Rab binding)	F: DUF3585	ECOD (1.6)
B	DUF3585	e5szgB1	A: alpha bundles	X: Long alpha-hairpin	H: bMERB domain (bivalent Mical/EHBP Rab binding) (From Topology)	T: bMERB domain (bivalent Mical/EHBP Rab binding)	F: DUF3585	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF12130	Bivalent Mical/EHBP Rab binding domain (bMERB_dom)	Bivalent Mical/EHBP Rab binding domain	A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally ...	A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Protein-methionine sulfoxide oxidase MICAL3	FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding F-actin monooxygenase activity oxidoreductase activity monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding F-actin monooxygenase activity oxidoreductase activity monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen catalytic activity cytoskeletal protein binding actin binding protein binding molecular adaptor activity cation binding metal ion binding	cellular process cell division cellular component disassembly actin polymerization or depolymerization actin cytoskeleton organization protein-containing complex organization actin filament organization protein-containing complex disassembly actin filament depolymerization cellular component organization organelle organization actin filament-based process cellular component organization or biogenesis supramolecular fiber organization cellular process cell division cellular component disassembly actin polymerization or depolymerization actin cytoskeleton organization protein-containing complex organization actin filament organization protein-containing complex disassembly actin filament depolymerization cellular component organization organelle organization actin filament-based process cellular component organization or biogenesis supramolecular fiber organization protein depolymerization cytoskeleton organization localization secretion by cell exocytosis transport secretion export from cell establishment of localization vesicle-mediated transport	cell periphery cell cortex cellular anatomical structure intracellular anatomical structure cytoplasm cytosol plasma membrane membrane membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle cell periphery cell cortex cellular anatomical structure intracellular anatomical structure cytoplasm cytosol plasma membrane membrane membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen organelle nuclear lumen intercellular bridge Flemming body midbody cytoskeleton spindle membraneless organelle intracellular membraneless organelle microtubule cytoskeleton cell projection

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR050540	F-actin Monooxygenase Mical	Family
A, B	IPR001715	Calponin homology domain	Domain
A, B	IPR002938	FAD-binding domain	Domain
A, B	IPR022735	bMERB domain	Domain
A, B	IPR001781	Zinc finger, LIM-type	Domain
A, B	IPR036872	CH domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: Q7RTP6	atrial fibrillation glioblastoma medulloblastoma primitive neuroectodermal tumor atypical teratoid rhabdoid tumor large cell medulloblastoma non-alcoholic fatty liver disease progressive supranuclear palsy chronic obstructive pulmonary disease malignant glioma pilocytic astrocytoma

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.