Annotations: 1GGT

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1ggta2	All beta proteins	Immunoglobulin-like beta-sandwich	Transglutaminase, two C-terminal domains	Transglutaminase, two C-terminal domains	Transglutaminase, two C-terminal domains	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1ggta1	All beta proteins	Immunoglobulin-like beta-sandwich	E set domains	Transglutaminase N-terminal domain	Transglutaminase N-terminal domain	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1ggta4	Alpha and beta proteins (a+b)	Cysteine proteinases	Cysteine proteinases	Transglutaminase core	Transglutaminase catalytic domain	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1ggtb2	All beta proteins	Immunoglobulin-like beta-sandwich	Transglutaminase, two C-terminal domains	Transglutaminase, two C-terminal domains	Transglutaminase, two C-terminal domains	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1ggtb1	All beta proteins	Immunoglobulin-like beta-sandwich	E set domains	Transglutaminase N-terminal domain	Transglutaminase N-terminal domain	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1ggtb4	Alpha and beta proteins (a+b)	Cysteine proteinases	Cysteine proteinases	Transglutaminase core	Transglutaminase catalytic domain	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Cysteine proteinases	8055403	3001808	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	CsgC/transglutaminase domain-like	8055474	3002048	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	E set domains	8055027	3000070	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	CsgC/transglutaminase domain-like	8055219	3002048	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	E set domains	8055027	3000070	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	CsgC/transglutaminase domain-like	8055474	3002048	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	CsgC/transglutaminase domain-like	8055219	3002048	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Cysteine proteinases	8055403	3001808	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	Transglut_N	e1ggtA8	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Transglut_N	ECOD (1.6)
A	Transglut_C_1	e1ggtA6	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Transglut_C_1	ECOD (1.6)
A	Transglut_C	e1ggtA7	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Transglut_C	ECOD (1.6)
A	Transglut_core	e1ggtA5	A: a+b complex topology	X: Cysteine proteinases-like	H: Cysteine proteinases (From Topology)	T: Cysteine proteinases	F: Transglut_core	ECOD (1.6)
B	Transglut_N	e1ggtB7	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Transglut_N	ECOD (1.6)
B	Transglut_C_1	e1ggtB6	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Transglut_C_1	ECOD (1.6)
B	Transglut_C	e1ggtB3	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Transglut_C	ECOD (1.6)
B	Transglut_core	e1ggtB5	A: a+b complex topology	X: Cysteine proteinases-like	H: Cysteine proteinases (From Topology)	T: Cysteine proteinases	F: Transglut_core	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)
A	3.90.260.10	Alpha Beta	Alpha-Beta Complex	Coagulation Factor XIII	Chain A, domain 2	CATH (4.3.0)
B	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)
B	3.90.260.10	Alpha Beta	Alpha-Beta Complex	Coagulation Factor XIII	Chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00868	Transglutaminase family (Transglut_N)	Transglutaminase family	-	Domain
A, B	PF00927	Transglutaminase family, C-terminal ig like domain (Transglut_C)	Transglutaminase family, C-terminal ig like domain	-	Domain
A, B	PF01841	Transglutaminase-like superfamily (Transglut_core)	Transglutaminase-like superfamily	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	COAGULATION FACTOR XIII	aminoacyltransferase activity protein-glutamine gamma-glutamyltransferase activity catalytic activity, acting on a protein acyltransferase activity transferase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding	multicellular organismal process regulation of body fluid levels wound healing response to stimulus hemostasis biological regulation blood coagulation response to stress coagulation regulation of biological quality response to wounding protein activation cascade primary metabolic process gene expression multicellular organismal process regulation of body fluid levels wound healing response to stimulus hemostasis biological regulation blood coagulation response to stress coagulation regulation of biological quality response to wounding protein activation cascade primary metabolic process gene expression macromolecule biosynthetic process protein maturation biosynthetic process blood coagulation, fibrin clot formation metabolic process cellular process protein metabolic process macromolecule metabolic process peptide cross-linking macromolecule modification protein modification process	cellular anatomical structure extracellular region extracellular space blood microparticle protein-containing complex catalytic complex transferase complex cell periphery extracellular matrix external encapsulating structure collagen-containing extracellular matrix membrane-bounded organelle vesicle lumen intracellular anatomical structure cellular anatomical structure extracellular region extracellular space blood microparticle protein-containing complex catalytic complex transferase complex cell periphery extracellular matrix external encapsulating structure collagen-containing extracellular matrix membrane-bounded organelle vesicle lumen intracellular anatomical structure intracellular vesicle membrane-enclosed lumen cytoplasmic vesicle lumen intracellular membrane-bounded organelle secretory granule lumen endomembrane system intracellular organelle lumen intracellular organelle cytoplasmic vesicle organelle lumen organelle secretory granule secretory vesicle cytoplasm platelet alpha granule vesicle platelet alpha granule lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036985	Transglutaminase-like superfamily	Homologous Superfamily
A, B	IPR036238	Transglutaminase, C-terminal domain superfamily	Homologous Superfamily
A, B	IPR013808	Transglutaminase, active site	Active Site
A, B	IPR013783	Immunoglobulin-like fold	Homologous Superfamily
A, B	IPR002931	Transglutaminase-like	Domain
A, B	IPR014756	Immunoglobulin E-set	Homologous Superfamily
A, B	IPR038765	Papain-like cysteine peptidase superfamily	Homologous Superfamily
A, B	IPR001102	Transglutaminase, N-terminal	Domain
A, B	IPR008958	Transglutaminase, C-terminal	Domain
A, B	IPR050779	Protein-glutamine gamma-glutamyltransferases	Family
A, B	IPR023608	Protein-glutamine gamma-glutamyltransferase, animal	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: P00488	congenital factor XIII deficiency factor XIII, A subunit, deficiency of Venous Thrombosis allergic contact dermatitis myocardial infarction thrombophilia malignant ependymoma myopathy pancreatic intraductal papillary-mucinous neoplasm pituitary cancer adrenal cortex carcinoma thrombophilia due to thrombin defect Becker muscular dystrophy diabetes mellitus exocrine pancreatic carcinoma congenital factor XIII deficiency factor XIII, A subunit, deficiency of Venous Thrombosis allergic contact dermatitis myocardial infarction thrombophilia malignant ependymoma myopathy pancreatic intraductal papillary-mucinous neoplasm pituitary cancer adrenal cortex carcinoma thrombophilia due to thrombin defect Becker muscular dystrophy diabetes mellitus exocrine pancreatic carcinoma invasive ductal breast carcinoma lung carcinoma malignant pancreatic neoplasm ovarian cancer pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia Sjogren syndrome tuberculosis Duchenne muscular dystrophy limb-girdle muscular dystrophy malignant colon neoplasm pancreatic intraductal papillary-mucinous carcinoma Pick disease Alzheimer disease ductal breast carcinoma in situ glioblastoma interstitial cystitis lung cancer

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	protein-glutamine gamma-glutamyltransferase (eukaryotic) M-CSA #149	Eukaryotic transglutaminase is able to catalyse the Ca(II) dependent acyl transfer between glutamine and the side chain amino group of lysine. It is unknown what the biological function of this is in fish, but the human homologue is blood clotting factor XIII which forms cross-links between these two residues in fibrin, thus plays a key role in the clotting cascade. The activation of the clotting factor is a subject of study in the hope of designing inhibitors which could be of pharmacological importance.	Defined by 5 residues: TRP:A-279CYS:A-314HIS:A-373ASP:A-396TYR:A-560 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.3.2.13 (PDB Primary Data) Search M-CSA Motif + EC 2.3.2.13

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.