ID M2PEM6_CERS8 Unreviewed; 1158 AA.
AC M2PEM6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN ORFNames=CERSUDRAFT_117207 {ECO:0000313|EMBL:EMD34329.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD34329.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD34329.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD34329.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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DR EMBL; KB445803; EMD34329.1; -; Genomic_DNA.
DR AlphaFoldDB; M2PEM6; -.
DR STRING; 914234.M2PEM6; -.
DR HOGENOM; CLU_002360_4_1_1; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 2.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 148..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 854..876
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 966..986
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1037..1054
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1066..1087
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1107..1128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 91..172
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 61..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1158 AA; 127705 MW; 43B42C4429152EB2 CRC64;
MSSEAAISEK LAQVQDEETL HTRAVVFPDD YGDIHEEKIT HGVPRPKGPE MKREMTKEDK
ELAAAGYGHL DEEKKGKDKS SGPKFENVDI HEHQLSLKEL ASALETDFEH KDPGNSHGLT
AEEAKVRLTR DGRNVLTPPK KKSAFRKYLD CLLTMFNILL VIAGILEYIL LGIDFKDNFA
NTYLGGILIG VAFLNAFIEF YQMQKSEAIL ASFLAMIPPS CHVVRDGSIT SIPAADLVKG
DVVLLRTGDK TPADVIIFSS TELKVDNSNL TGESEAQERF ATYDGCKSRP VEATNLVFNS
TLIVNGEGWG VVVRTGDHTL IGQIAALTGG ESGNQSPLAI EIGRFVMMIS SIAIVFAVVF
FAVGISTVYK GKAAQTVTFA VSILVAFVPE GLPSVVTLLL SIAAKRMAQQ NVLVKDLQGV
ETLGTLTLLA TDKTGTLTRN QMTVTNLWSG GKMYTAFQSN NDSETTEAFS INAPGMREMV
DIAALNSRVK FDKMDLPFEQ RAILGDATET GLTRFAGRHI GDYDKAQKEF PKVFEIPFNS
SNKWALVILN KPHEDGNLTL YIKGAPERVL AKCSTYLNDG RVEPMSDDFK KLYDEAYNYM
ASRGHRVIAC AQKLLPASAY GPSHAFSKKD GEYPSTDYCF CGLISLEDPP KHGVREAIGT
LRLAGIKVMM VTGDHPKTAE AIARKINLIL GDTKETLSAR TGRPVEEIYE DEVDAVVVHG
DDIDGLQGWQ WDQIFAKNEI VFARTSPQHK LEIVKHAQAL GHIVGVTGDG VNDSPALKKA
DLGIAMNISG SDVSKEAANM ILLDDNFAST VKGVAEGRQI FVNLKRSIQY TMTHITPEVI
PQLLYVVVPI PLPLSAILIL VIDLGFELFV ALSFAWDKPE TEDGLMRMSP RKPVNDRTIM
ALKTRALERT KTLRRDTENQ EVIQPSKISV WKNKLKQYTT RRYWVELLSP AEGETLVDGK
LLSYSYIEAG LIETLGTLVA YFVVFFKNGF SPSDLRKAQQ ASIHQAYFTN SSPDFINYRG
EVITASKQVD ALAQAQSIVY LSIFIIQCFN VFAVKAKFSF PFGKSIVGNV WNFVGIFAGA
CLGMFIVYTP PLHVVFGGTD KLSPLYWLIP AAFGVLLLVW SSVRVLFLRK GIEQSRVKDI
KGLMMFPTMR TMSMRSKH
//
