Q6C1K8 (Q6C1K8_YARLI) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase RuleBase RU004435
EC=3.4.19.12 RuleBase RU004435

Gene names

Ordered Locus Names:	YALI0F15367g
ORF Names:	YALI0_F15367g EMBL CAG78263.1

Organism

Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) [Reference proteome] EMBL CAG78263.1

Taxonomic identifier

284591 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia › Yarrowia lipolytica

Protein attributes

Sequence length	992 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). RuleBase RU004435
Sequence similarities	Belongs to the peptidase C19 family. RuleBase RU004434

Ontologies

Keywords
Biological process	Ubl conjugation pathway RuleBase RU004434
Molecular function	Hydrolase Protease Thiol protease RuleBase RU004434
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q6C1K8 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 27E1DC759B181325	FASTA	992	111,194
	10 20 30 40 50 60 MSSAVHYAAL SPHRGCGLSL SPQLRDDVSH CATQGGAKPN NHGQPHTNHH FQLNRTPVVP 70 80 90 100 110 120 MRYTNLEELG KAARQATGAV SGFKPKRMVD LALSQIEQYK QMLEMDLELA AYHIFQAREI 130 140 150 160 170 180 LFVCIPRHPD YDKFQAKKGP FHETYVELCD LAETDRRVLE LISTVKGKYV REKTSGVRRQ 190 200 210 220 230 240 SNDDLLQSID DTIRGFSHLD VQQQSAPPTE TDPLKDKLEK LRGRSPEVQR ATLTTNGSST 250 260 270 280 290 300 TTTKNGVMPP PKISPPPVPV PQNGGYVRQS YVGPASVPSP PPHSVTPPTP PRHTITLKAP 310 320 330 340 350 360 QLISYLGHAP ETLLLLDIRP RADFQKCHIA APNVVCVEPH LLEADMTDEQ VEEKMLAALT 370 380 390 400 410 420 TEEFERFMAR SAFEIVVFYD QNSTSYQTRP LKILLKALYS QAFKRPLQRP PCLLVGGLDE 430 440 450 460 470 480 WRHSGAATSF IDTRSPLQQR AELARTQTDP TPVASYDPNR VYSHPYASNY ASYAYSYGPN 490 500 510 520 530 540 QSSPTPPPVP TTPPPKPPSA MSSSSSLNLP QSMALSSSTS LPDPSSYKNQ MYSCHPYLNE 550 560 570 580 590 600 PLPESRHHTH GVSQPAQAAR SSHGYYSHAL PQLSVNTASS PIKQPPSAYS PKEKHNGEFP 610 620 630 640 650 660 SYKSVRQPIP QSPYLPHLAP MSGSPPPMSL TFTTGLKNLG NTCYINCIIQ CLATSQLTKI 670 680 690 700 710 720 IVNQAYKHRV NMKSKLGYKG ALIAKYADLV QALVANAYPY LVPTSFKGII AHVNSQFSGM 730 740 750 760 770 780 EQHDCQEFLT FILDGLHEEL NSVGDGQYKP RELTESEEKR REEMSVRIVS SLEWERYLKS 790 800 810 820 830 840 ASSFIVDEFQ GQYQSKLQCT VCKMTSTTYT AFSSLTLPIP KYAGATLPTL YDCFNQFTQP 850 860 870 880 890 900 ELLEGENMWQ CPTCKKPRPT IKSMKISRLP ETLIIHLKRF DHSRGYGDKL NTFVTYPLEM 910 920 930 940 950 960 DLTRYWPPPT SEDEPFLKKL LPRGQTAPFR YSLFGVANHY GTLRGGHYTS FCKRGKLGWC 970 980 990 YFDDTVVNRN VNERAVVNKN AYVLFYQRRH NP

References

[1]

"Genome evolution in yeasts." Genolevures Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382132 Genomic DNA. Translation: CAG78263.1.
RefSeq	XP_505454.1. XM_505454.1.
3D structure databases
ProteinModelPortal	Q6C1K8.
ModBase	Search...
Protein-protein interaction databases
STRING	4952.Q6C1K8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2908061.
KEGG	yli:YALI0F15367g.
Phylogenomic databases
KO	K11839.
OMA	YIVFYER.
OrthoDB	EOG4HX88F.
Family and domain databases
Gene3D	3.40.250.10. 1 hit.
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR001763. Rhodanese-like_dom. [Graphical view]
Pfam	PF00581. Rhodanese. 1 hit. PF00443. UCH. 1 hit. [Graphical view]
SMART	SM00450. RHOD. 1 hit. [Graphical view]
SUPFAM	SSF52821. Rhodanese-like. 1 hit.
PROSITE	PS50206. RHODANESE_3. 1 hit. PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q6C1K8_YARLI

Accession

Primary (citable) accession number: Q6C1K8

Entry history

Integrated into UniProtKB/TrEMBL:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)