ID A0A1V6VAL5_9EURO Unreviewed; 1269 AA.
AC A0A1V6VAL5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
GN ORFNames=PENCOP_c001G00238 {ECO:0000313|EMBL:OQE47539.1};
OS Penicillium coprophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE47539.1, ECO:0000313|Proteomes:UP000191500};
RN [1] {ECO:0000313|Proteomes:UP000191500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQE47539.1}.
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DR EMBL; MDDG01000001; OQE47539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6VAL5; -.
DR STRING; 36646.A0A1V6VAL5; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000191500; 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:0005507; F:copper ion binding; IEA:InterPro.
DR CDD; cd00371; HMA; 4.
DR Gene3D; 3.30.70.100; -; 4.
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; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006122; HMA_Cu_ion-bd.
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 InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR NCBIfam; TIGR00003; copper ion binding protein; 1.
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; 3.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
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; 4.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 4.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW Ion transport {ECO:0000256|ARBA:ARBA00022796};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000191500};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT TRANSMEM 506..530
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 604..623
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 635..655
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 792..815
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 835..863
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1188..1210
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1234..1254
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 22..87
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 242..308
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 328..393
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 413..482
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 158..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1269 AA; 137324 MW; 563C186542779C42 CRC64;
MSSGSKYQSS DLEADHQNLD TQTSLFFVTN VHCASCVAYI TEVLSETPSV GNIEVTILTH
EVRASHSTTV RPADLVNALI HAAFEVHYVT TFDQRGKPIA ELDTSSWNYR GSTLFSSPRA
SVSSISSNIK ERIQSNSHRR HIANCDACRK EELEALSRHS SRTELGPLDE KSSQTPFRPL
SKHPEKDITV TNLETTPGNA VQESLRSFTT SETKVQPDVS APNLPADIAE LPSPSAESAD
EFTAQISIGG MSCASCANSI TAQVQQLEFV KEITVNLLTN SATVIYVGPR GNSDEIIEQI
NDAGFEASLD EVNQLPKPPA SAERAANYVS EIAITGMTCG SCVGGVTRGL EELPFIHDVS
VNLLSHSGRV EFEGRDNLGK IIEKIEDLGY DAIVNSVSPM KVGTEKLSTV QIRTISIQVD
GMFCHHCPQT VLGAVKSVPG VTIEEALSEK TPILKITYTP RPPLLTLRTI ISAINSANDS
FRATVYHPPS IEDRSRAIQH HERSRLLARL LFVFITTIPT FLIGIVFMSL VSSENSVRMY
LEQPMWAGSV TRIEWALFIM TTPVMFYGTD VFHARALKEV YALWRPGSRV PILRRFYRFG
SMNLLISAGT SVAYISSLAV LIVDASVGTK SSAHSTTYFD SVVFLTLFIL AGRFLEAYSK
ARTGDAVTSL GKLRPSEALL SDETFQRGVK RTSVDFLEVG DVVSVPHGAS PPADGVIVDS
ASYQFDESSL TGESRPVKKT VNDIVYTGSV NVGQPVRIRI TELGGSSMLD RIIAVVREGQ
SKRAPLERVA DLLTSHFVPI ITLIAISTFI IWLALGHSGV LPADYLDVAH GGWTFWALEF
AISVFVVACP CGLALAAPTA LFVGGGLAAK HGILVKGGGE AFQEASRLNA IVFDKTGTLT
EGGSLKVSDH EVLTSDPEVA KAAWALARKM EESSNHPIAQ AITEFCKAQQ SSYVKSSDVH
EISGQGMKGI FTVSGSEHEE QYEAAIGNER LLKSLLSPET DTYFISNLLA KYQSAGKSTA
VLSLRQVHTQ STEPSNFIPA IIFATSDTIR PEAVEIVSQL QKRHVDVFMC TGDNQTTAHA
VADMIGIPRS KVMANVLPAE KASFVRQIQD RSPDATPADG KTTIVAFVGD GVNDSPALAA
ADVSIAMASG SDVAINSASF ILLNSDLSTI LQLVLLSRRV FNRVRMNFGW AVIYNLCLVP
VAAGILYPIV SGHHEKNIDG HMIMASEHWR LSPVWAALAM ALSSISVVLS SLALRVDKES
ILKIVSRKK
//
