ID U7PMR4_SPOS1 Unreviewed; 1330 AA.
AC U7PMR4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
GN ORFNames=HMPREF1624_07145 {ECO:0000313|EMBL:ERS96236.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS96236.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|RuleBase:RU362081}.
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DR EMBL; KI440850; ERS96236.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PMR4; -.
DR STRING; 1391915.U7PMR4; -.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_0_2_1; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000018087; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 2.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 2.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF32; COPPER RESISTANCE P-TYPE ATPASE (EUROFUNG); 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF08282; Hydrolase_3; 1.
DR PRINTS; PR00119; CATATPASE.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000018087};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 484..508
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 808..829
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 849..880
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1251..1276
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1288..1309
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 17..84
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 290..355
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 106..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1330 AA; 140649 MW; FFEF73749A6DAEEE CRC64;
MAPPLNRASR PFGQEAVTTS ILLGNLHCPS CVSTIREVLQ EACADHIRWV SPNIVTSVVT
VEHDADTSLR DMVTALADAG FDICGVTSSS GDDIVDLDLS APSAEALTAD PGIPSRPGTA
DAQPGGAHDN DGDENGEHED EDKGKGKGHD ITPAMPSSPR DAADASSSAW GLTPLVRWLS
GPRVEPRRSF ATTSRLAQAH LSNCEQCRQL QSAGISPLPL HKTEVGPSKS KLDEAAVSKG
SSSSNTNTST NTNKINNTPS TSSSQTNAAD MDKSFVTVEH EDAPTNRPIW RASLAVGGMT
CAVCVNAITD DLKKKDWVTK VTVNLISNSA TVEFDDKDKE SKIVEAIEDL GYDATIDSMV
RVDPPKPKTA LQQANGAGGD GADPEQPERT VEVRIDGLYC EHCPDRIARS LAGFRRPSLE
IITKPTPQRP IIKLKYVPEA PNFTIRHILA AIEASDSELS ASIYHPPTLE ERSKMIQAKH
QRQIMYRVIF TGLVCIPTFV IGIVYMSLLP STNNGRMYMT APWASGISRS QIALFILATP
VYFFCADIFH VRAFKEVRAL WRRNSRTPFL QRFYRFGSMN TLMSLGTTIA YVSSVSQMIA
AAAHEAAEIS DANFYFDSVV FLSFFLLCGR LIESYSKSRT GDAVEMLGRL RPTTAILVEE
SVAASLEEKD VIESIETVQS VASTEHDAAP GTPTLRSAPD ATNKSGRIVQ ADLLDFGDVV
RILHGASPPA DGVIVQGRSN FDESSLTGES RLVPKTVGDE VFSGTVNKDA PVLVRVTGAS
GTSMLDQIVA VVREGQTKRA PMEQIADLLT TYFVPVVTLV AISTWIIWLS LGLSGSIPGH
FLDVSSGGWV AFSLQFAIAV FVVACPCGLG LAAPTAIFVA GGMAAKYGIL AKGGGEAFEK
ASRIDCVVFD KTGTLTMGGE PTVTDSAVFT SGGGDGGDAD DGHDQDQDSA LSKDKTSDLL
AALQAVEENS GHPIAKAIVT FCEASTHAAG PGGRVDDLQE IPGRGMRAVF HSRAGNERSF
EIMIGNEALM KDFSVAISDR VVALLQQWKT EAKSVALAAT RSLGAGAGAG QPWTLAAALS
IADPVRPEAA AIVKTLQSRG VLVYMLSGDN AVTAAAVAQQ IGIPADQVIA EVLPTEKAAK
VQYLQASLPA HTSRFGRVAK PTTVAEAAPS HAPNASSPPD AAAANGGRRA VVAMVGDGIN
DSPALTQADV GIAVGSGSDV AISSADFVLV QSNLQAVVTL LELSRVVFRR IAFNFGWALV
YNVVAVPIAA GVLYPIRTAT TNHVRLDPVW ASLAMALSSI SVVMSSLALR SRIPGLGFRP
TVVKTPATST
//
