ID F8QFA2_SERL3 Unreviewed; 960 AA.
AC F8QFA2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
GN ORFNames=SERLA73DRAFT_127002 {ECO:0000313|EMBL:EGN93061.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
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; GL945495; EGN93061.1; -; Genomic_DNA.
DR AlphaFoldDB; F8QFA2; -.
DR STRING; 936435.F8QFA2; -.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_0_2_1; -.
DR InParanoid; F8QFA2; -.
DR OMA; KFGSMNM; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000008063; 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; 1.
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 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; 1.
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 PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 1.
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:UP000008063};
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 178..201
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 221..240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 272..293
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 499..522
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 542..570
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 902..924
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 930..951
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..57
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 354..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 960 AA; 103047 MW; 67A6CCC6752C63AB CRC64;
MTCSSCSGTI TEMVSQLSGV SEVTVNLLGN SASVVVDCKE TINLVTETID DCGFEGEVIK
VEPVSHADNE DEVTDGSRTI SLRVDGMFCQ HCPGKIMSSL EKLSPEITFI KSLTDYNDPI
LELSYKPSLP SFTIRNIVSA ITSVEPTYFK ISVYRPPSLE QRTRTMQVRE QNALLQRLVF
AVITAIPTFI IGVVYMSLIK SSNSSKRYLL EPMWNGNASR LQWAMFFLAT PVMFYSAGLF
HRRSIREIKA LWRKGSTTPI IKRFTRFGSM NLLVSTGVSV AYFSSIALLA LSASQHPSPN
GVGQTTTYFD SVVFLTMFLL AGRFLEAYSK ARTADAITAL GSLRPTEALL IAPKTSSDLI
SPPTPSSKGE TDSADLEKGD PTSDGGVLST QPGFVASKVN VDFLEVGDVV RVLHGATPPA
DGIIVSSSDG AFDESSLTGE SRLVKKKTGD RVFLGTVNKS TVVDVKIDTI GGITMLDHIV
KVVREGQTRR APIERIADII TGFFVPAVTL LAVITWVIWL SLGLSGALPS DYLNIAVGGW
TVWSFEFAIA VFVVACPCGI GLAAPTALLV GSGLAAKYGI LARGGGEAFQ EMAQLDIVVF
DKTGTLTEGG EPRVADCEVV FQGSDGSSRW NRGTVLGIAS ELESASSHPL GTAVRHYCGA
EGASSISGSA FEEVPGRGLS ADFDGLECSA IIGNEAWMYE HDVMINDFIS QKLEVWKTEA
KSVILLAIKE RSEEESHFRV AAIFSVSDPL RPEAKAIVRC LQDQGIGTWM ISGDNEVTAK
AVAQTVGIPA TNVIAGVLPH EKAEGIRHLQ QNGTKRTLPR WQTFFTTNLK RRLNDRCVVA
MVGDGINDAP ALAASDVGIA IGSGSDVALS SASFILVSSD LQSLLTLSDL SRKVFNRVKL
NFLWALVYNL IALPVAAGVI YPAGHARLDP VWASLAMALS SVSVVCSSLL LKLYKEPKTA
//
