Q06309 (CRK1_LEIME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cell division protein kinase 2 homolog CRK1
EC=2.7.11.23

Gene names

Name:

CRK1

Organism

Leishmania mexicana

Taxonomic identifier

5665 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmaniinae › Leishmania › Leishmania › Leishmania mexicana species complex

Protein attributes

Sequence length	301 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May be involved in some stage-specific role in the promastigote cell cycle.
Catalytic activity	ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
Enzyme regulation	Phosphorylation at Thr-15 or Tyr-16 inactivates the enzyme, while phosphorylation at Thr-160 activates it By similarity.
Subunit structure	Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin By similarity.
Developmental stage	Expressed in all life cycle stages, promastigote, metacyclic and amastigote forms but is found in the active form only in the promastigote stage.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II carboxy-terminal domain kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 301	301	Cell division protein kinase 2 homolog CRK1		PRO_0000085878
Regions
	Domain	5 – 297	293	Protein kinase
	Nucleotide binding	11 – 19	9	ATP By similarity
Sites
	Active site	127	1	Proton acceptor By similarity
	Binding site	34	1	ATP By similarity
Amino acid modifications
	Modified residue	160	1	Phosphothreonine; by CAK By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q06309 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 58EB39D006D88461	FASTA	301	34,473
	10 20 30 40 50 60 MTSRYERQEK IGEGTYGVVY KARDTSTAAT VALKRIRLDS EEEGVPCTAI REISLLKELR 70 80 90 100 110 120 HENIVKLLDV CHSEHRLTIV FEYLDLDLKK YLDRENGNLD AATIQHFMRD LLRGVAFCHQ 130 140 150 160 170 180 RSVLHRDLKP QNLLISREKE LKLGDFGLGR SFAIPVRKFT NEVVTLWYRP PDVLLGSMQY 190 200 210 220 230 240 GPPVDVWSVG CIFSEMATGT PLFAGKNDAD QLMRIFRFLG TPNNRVWPSM NQYPNSNNML 250 260 270 280 290 300 SQPEFLQNFE PEWSNVLGSV PGYEKLGCAG VDLLERLLRY EPSERITAAD ALNHPYFSLQ F

References

[1]

"A novel CDC2-related protein kinase from Leishmania mexicana, LmmCRK1, is post-translationally regulated during the life cycle." Mottram J.C., Kinnaird J.H., Shiels B.R., Tait A., Barry J.D. J. Biol. Chem. 268:21044-21052(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MNYC/BZ/62/M379.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X60385 Genomic DNA. Translation: CAA42936.1.
PIR	A48041.
3D structure databases
ProteinModelPortal	Q06309.
SMR	Q06309. Positions 3-298.
ModBase	Search...
Proteomic databases
PRIDE	Q06309.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CRK1_LEIME

Accession

Primary (citable) accession number: Q06309

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	April 3, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)