ID N4XG72_COCH4 Unreviewed; 1028 AA.
AC N4XG72;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
GN ORFNames=COCC4DRAFT_131401 {ECO:0000313|EMBL:ENI07548.1};
OS Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T) (Southern
OS corn leaf blight fungus) (Bipolaris maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665024 {ECO:0000313|EMBL:ENI07548.1, ECO:0000313|Proteomes:UP000012338};
RN [1] {ECO:0000313|EMBL:ENI07548.1, ECO:0000313|Proteomes:UP000012338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C4 / ATCC 48331 / race T {ECO:0000313|Proteomes:UP000012338};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000012338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C4 / ATCC 48331 / race T {ECO:0000313|Proteomes:UP000012338};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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; KB733449; ENI07548.1; -; Genomic_DNA.
DR RefSeq; XP_014081457.1; XM_014225982.1.
DR AlphaFoldDB; N4XG72; -.
DR GeneID; 25837036; -.
DR HOGENOM; CLU_001771_0_2_1; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000012338; 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; IPR017969; Heavy-metal-associated_CS.
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 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 PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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; 2.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
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}.
FT TRANSMEM 261..288
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 308..327
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 392..409
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 543..566
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 586..614
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 943..966
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 986..1006
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..57
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 81..146
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 1028 AA; 110615 MW; C5B47A8D96ABE711 CRC64;
MTCSSCVSAI THAVEAHAWV QSVNINLLTN SGVVVFAGKS KCDELVETIE DCGFDVEVEK
LEEVQDTASE PKPSKQKTEL WRATYLLGGL TCSSCVGNVT QALEPHAWIK SIDVNLVSNS
ATIVFTGKEH LSEIEEIIED VGYTATLDHV ILDDTPAIQA IERTIAVRID GMFCEHCPSN
IIQGLQEAFA DKQTFVLEDP PISLENPILH IRYVPAPPTF TIRHIISTIS NLHPVFTPSI
FHPPTIEERA RQMHAQERKR TLLRLTLCVI IAIPTFILGI VFMSLISAEN PIRKYLMQPM
WAGNVTRLSW ALFILATPVY FFAADTFHRR AIKEIKALWR PGSRTPILHR FTRFGSMNML
ISLGTTIAYL ASIAELALAA TEMSHGSMHD SYFDAVVFLT MFLLIGRFLE AYSKAKTGDA
VTSLGKLRPS EAILVDSEQG DDKIPTDLLE IGDVVRVHHG ASPPFDGEIV EGSSSFDESS
LTGESRPVKK VEGDTVYSGT MNKGSPVQTK ITSIEGMSML DQIINAVREG QSRRAPVERA
ADVITSHFVP FVISVAITTW LVWLILGKTG AIPNDWKNEG AGGWELWSLR FAIAVFVIAC
PCGIGLAAPT ALFVGGGLAA KHGILVRGGG EAFQEASSLD CIVFDKTGTL TQGGDPAVTN
HQLSGDQNSS LVLGLVKALE QNSNHPIARA LVSFCNREDH ITPTVVDIDE VPGKGLKGTF
RVDGQDITAI VGNEAFMTDH SVPIPPSTAT LLSTWQSRGD SIALAALFMP PCTLLPSHSS
SESLSTALTE TLPAPTWHLA CAFSIADALR PEAHSVIAAL HARGISTWML SGDNPTTANA
VGAQIGIPSS NIIAGVLPEQ KAQKIKYLQQ TLRSSNRTQK RATIAMVGDG INDAPALSTA
DLSIAIGSGS DIALSSSSFI LINSRLTTIL TLLDLSRVVF RRVYFNFGWA LVYNMVAMPI
AAGVLYPITT TGGGGGKGEH VKLDPVWAAL AMALSSVSVV CSSLLLRSRL PGVGFRVRRE
GSGGVETG
//
