Q9UVL6 (Q9UVL6_CANAX) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Copper resistance-associated P-type ATPase EMBL AAF04593.1

Gene names

Name:

CRP1 EMBL AAF04593.1

Organism

Candida albicans (Yeast) EMBL AAF04593.1

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	1197 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Sequence similarities

Belongs to the cation transport ATPase (P-type) family. RuleBase RU000653

Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane RuleBase RU000653
Ligand	ATP-binding RuleBase RU000653 Nucleotide-binding
Molecular function	Hydrolase RuleBase RU000653
PTM	Phosphoprotein RuleBase RU000653
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro metal ion transport Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q9UVL6 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: FEC36A717ECEC1C7	FASTA	1,197	131,595
	10 20 30 40 50 60 MQKFIINFAN IHCDKCEGII RNVVSRYYKI SDETDLNANI KPSEVIFKLE NNEVTLYGND 70 80 90 100 110 120 LIDFHGDIKS IIKSLGKSGF DILSWDLHNG DETVSSSQIV NTNIQGANEP DGFIDIVGMY 130 140 150 160 170 180 HKFINSRNKK KHMKYCKVCQ ESQQHKKKST DSDFSSSSED TVVEIPHQEF RASFLVTGMT 190 200 210 220 230 240 CASCAQSITD NLRSILGESK NEDEPNFSVN VIQQSVVVII PNKQIINKIV DAINDMGFDC 250 260 270 280 290 300 KLIEVLPVQR SVNTKVTALI GGMTCAACAN SIDSAVKELP FILESGINVV TKAAQFVLED 310 320 330 340 350 360 DGGSNIAKLK ETIEDCGFDF ELLSTEKVNY TSGKQKPRSI NLKVNGMFCN HCPDIITQYL 370 380 390 400 410 420 TNYGDAVVIN DPISLDHPVI KFTYVPSQTL KTRKILFDLN HLKDDGNGGY TITPDEKGAF 430 440 450 460 470 480 ECEIIKPVTV DEHVRKLAHR EVLGLAIRLA IATLFAIPTF IFGIVAMSLL PKHHPFRIWV 490 500 510 520 530 540 EDPLWVGNVS RNSWILFILA TPVYFFAADT FHRKAIKEIK SLWFHKNSFK SRLLKFGSMN 550 560 570 580 590 600 LLMSLGTTVA YFASIVLIGL SATQKPMTHH GLHTTYFDSV VFLSFFLLIG KLLQSYSKSK 610 620 630 640 650 660 TADAISELSK LKQTEATLIE DNKDTRVDIQ LLEIGDQIRI GTGESPPVDC VLVEGSTEFD 670 680 690 700 710 720 ESALTGESTP VKHQEGHQIF SGTVNIGNSS VVGKVTSLEG DSLLNQIVNT VRDGQMRKAP 730 740 750 760 770 780 MERTADLITG YFVPLIIACA VITWVIWLAL GYSGALPQSY LDIDVGGWTV WSLEFAIAVF 790 800 810 820 830 840 VVACPCGIGL AAPTALFVGS GLAAKNGILA KGGGVAFQDG ANVNIVCFDK TGTLTKGELT 850 860 870 880 890 900 ITDFHFPDKS SIAKTFALQV ARDLEVPSHH PLGKAVKSFV TSYDGKSLTA NKIPQVETVP 910 920 930 940 950 960 GKGLRGQIIY DEGDDIWNEY KPTQAILGNE KLMEENDIEF TEKERQCLKK WKGECKSVIL 970 980 990 1000 1010 1020 VGLQCESYFK DSKFHLALIM AARDQLRPET KKVIEFLKHK DIECWMITGD NKLTADAIAK 1030 1040 1050 1060 1070 1080 EIGIENVVSE VLPDEKEAQI KKIRQLNSGG KKEPVIAMIG DGINDAPALA SADVGIALSS 1090 1100 1110 1120 1130 1140 GADLAVTSSD FILLNKMHPL VSLATLLDIC SKVFQRVKLN FGWSLVYNLI ALPIAAGVIY 1150 1160 1170 1180 1190 PYKNSRLDPV WASAAMALSS VSVVLSSLAL KLYKPSLKAE DFGVDDSTES ELSPNEV

References

[1]	"The high copper tolerance of Candida albicans is mediated by a P-type ATPase." Weissman Z., Berdicevsky I., Cavari B.Z., Kornitzer D. Proc. Natl. Acad. Sci. U.S.A. 97:3520-3525(2000) [PubMed: 10737803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: 1006 EMBL AAF04593.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF193508 Genomic DNA. Translation: AAF04593.1.
3D structure databases
HSSP	HSSP built from PDB template 1FVS based on UniProtKB P38995.
ProteinModelPortal	Q9UVL6.
ModBase	Search...
Protein family/group databases
TCDB	3.A.3.5.9. P-type ATPase (P-ATPase) superfamily.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR006416. ATPase_P-typ_heavy-metal. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR005834. Dehalogen-like_hydro. IPR023214. HAD-like_dom. IPR017969. Heavy-metal-associated_CS. IPR006121. HeavyMe-assoc_HMA. IPR000150. Hypothet_cof. [Graphical view]
Gene3D	G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 1 hit. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 2 hits. G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF00403. HMA. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SUPFAM	SSF56784. HAD-like_dom. 1 hit. SSF55008. HeavyMe_transpt. 2 hits.
TIGRFAMs	TIGR01525. ATPase-IB_hvy. 1 hit. TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. PS01229. COF_2. 1 hit. PS01047. HMA_1. 1 hit. PS50846. HMA_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q9UVL6_CANAX

Accession

Primary (citable) accession number: Q9UVL6

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 2000
Last sequence update:	May 1, 2000
Last modified:	October 19, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)