ID M2QS23_CERS8 Unreviewed; 1316 AA.
AC M2QS23;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CERSUDRAFT_81221 {ECO:0000313|EMBL:EMD39893.1};
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:EMD39893.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD39893.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD39893.1,
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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KB445793; EMD39893.1; -; Genomic_DNA.
DR STRING; 914234.M2QS23; -.
DR HOGENOM; CLU_000604_17_2_1; -.
DR OrthoDB; 1067095at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd18577; ABC_6TM_Pgp_ABCB1_D1_like; 1.
DR CDD; cd18578; ABC_6TM_Pgp_ABCB1_D2_like; 1.
DR CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 2.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24222; ABC TRANSPORTER B FAMILY; 1.
DR PANTHER; PTHR24222:SF76; MYCOBACTIN IMPORT ATP-BINDING_PERMEASE PROTEIN IRTA; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 747..771
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 791..812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 863..888
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 894..913
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 974..995
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1007..1030
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..381
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 416..661
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 748..1035
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1070..1310
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1316 AA; 143095 MW; 44D286D4C3C905B1 CRC64;
MAGSLTHSDE TQGEKSAPKK GGFFSRNKDE RNIDSDEKIE KHVTVAEEKP KEQGLAPVSF
TSLFCFSTKT DLAMDFIGLI AAAAAGAAQP LMSLLFGNLT QGFVTFGMTL EEAQAGNATA
QALLPSAAAT FKHDAARNAN YLVYIGIGMF VCTYTYMYTW VYTGEINAKR IRERYLQAVL
RQDIAYFDRI GAGEVTTRIQ TDTHLVQQGI SEKVALVTNF LAAFATGFIL AYARCWRLAL
AMTSILPCIA ITGGVMNKFV SGFMQTSLAS VADGGTLAEE VISTVRTTQA FGTQRILADL
YDKRISGSRI ADMSAAVWHG AGLAVFFFVI YGAYALAFDF GSTLINHGEA NAGQIVNVIL
SILIGSFSLA LLAPEMQAIT HGRGAAAKLF ETIFRVPDID SSNEGGLKPE KCVGEITFEH
VKFNYPSRLD VPIVKNLSIT FPAGKTTALV GASGSGKSTC IQLVERFYDP LEGVVKLDGN
DLKDLNLKWL RSQIGLVSQE PTLFATTIKG NVAHGLINTP WENESEEEKM RLIKEACIKA
NADGFITKLP MGYDTMVGER GFLLSGGQKQ RIAIARAIVS DPRILLLDEA TSALDTQSEG
IVQNALDKAA AGRTTITIAH RLSTIKDADC IYVMGDGLVL ESGTHNELLS RENGAYARLV
QAQKLREARE KRAQDEDDSE TAGSAEEDIE KQAAEEVPLQ RQKSGRSLAS EILEQRAKEH
GEEKHSYSVP YLMRRMGRIN RDDWKRYAFG IVAAICNGCT YPAFGIVYAK GINAFSDTSN
SARRHDGDRT ALWFFLIAIL SAIAIGSQNY LFASSAANLT AKLRSISFRA ILRQDVEFFD
KDENNTGQLT SALSDNPQKI NGLAGVTLGA IVQSASTLIA GSIIGLAFAW KIGLVGIACT
PVLVSAGYIR LRVVVLKDEQ NKKAHEQSAQ LACEAAGAIR TVASLTREAD CCKLYSESLE
EPLRNSNSKA IYSNAIYSLS QSMSFFVIAL VFWYGSRLVA SLEFTTFQFF VGLMSTTFSA
IQAGSVFSFV PDMSSAKGAA ADIVTLLDSR PEIDAESTEG EIPQNVSGRI RFENVHFRYP
TRPGVRVLRD LNLTVEPGTY VALVGASGCG KSTTIQLIER FYDPLTGNVY LDEQPISKYN
VAEYRKHIAL VSQEPTLYAG SIRFNILLGA TKPFEEVTQE EIEAACRNAN ILDFILSLPQ
GFDTEVGGKG SQLSGGQKQR IAIARALLRN PKVLLLDEAT SALDSTSEKV VQEALDQAAK
GRTTIAIAHR LSTIQNADCI YFIKDGAVSE AGTHDELLAR RGDYYEYVQL QALSRN
//
