ID A0A2H3I7K8_9EURO Unreviewed; 1048 AA.
AC A0A2H3I7K8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=ABC transporter, integral membrane type 1 {ECO:0000313|EMBL:PCG96255.1};
GN ORFNames=PENO1_069240 {ECO:0000313|EMBL:PCG96255.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG96255.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG96255.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG96255.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:PCG96255.1}.
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DR EMBL; NPFK01000218; PCG96255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3I7K8; -.
DR STRING; 290292.A0A2H3I7K8; -.
DR OrthoDB; 1829487at2759; -.
DR Proteomes; UP000218381; 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; cd18580; ABC_6TM_ABCC_D2; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
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; IPR044726; ABCC_6TM_D2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR PANTHER; PTHR24223:SF442; ATP-BINDING CASSETTE SUB-FAMILY C MEMBER SUR; 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; 1.
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:UP000218381};
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 66..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 513..542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 562..587
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 666..684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 748..771
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..214
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 278..504
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 526..806
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 812..1045
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 469..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1048 AA; 115451 MW; 7E5AE1F90FFF4990 CRC64;
MIRGGLVTLV YDATLKLHSS KATDAAAVTH MSTDIDQITQ GMTNFDVLWA APIEVGLAIY
ILWREIGLAC LAPVGITVGC TLAAFVLGKL SRKAQRVWVN AVQLRTTATV SMLNNIKGIR
MSGLSSRFST NIQDLRVKEL AASKSYRHLT VLKNTIGTLP QVMGPVTAFV IYVLVRQNSN
SRLDPATAFT SLSLITLLSS PIFLFMFALP PFTASIACYD RIQKYLLSAD DETNGSSLGD
IKKSDGVPST NYPDTESNMM ELKTKHSMQD EGNDLVILDR ASFSFENHGP TVLHDISFSI
QKGNLVMLTG AVGSGKSTLL LAILGECFQV GGTLRRSPIL RIGYCGQTPW LRNLSVRQII
QGASSFDKDW YAIVLNACVL EPDLAILPEG DQTVIGSRGT SLSGGQKQRL SLARALYAKK
HLLLLDDITS GLDATTVQIV AQRVFGPDGL CRRHHMSVLL ATHDVNSGDE VCSSPQSEND
SLHKTSEPEQ SSNREKDAAL ADLARKVGDW RLYLYYFNTM GWALTAIFIM VSIAFTFCYN
FPTIWLQLWS ESESSHPGEH QVMYLVVYAV LGILAIILMS ASVWVLIVEM VPRSSIKLHK
MLLDTVLSAP FSFFISTDTG VTLNRFSQDM SLIDMQLPFG FLQAVDGVFE CIAAAALIAV
SSYWTALSFP VLILILYVLQ KFYLSTSRQM RFLDLEAKSP LYSHFLDTLH GLVTIRAFAW
HSEFQETNQK LLNDSQKPYY LMFSIQRWLN LVLDLVVTAI AVTIVAIASQ VHGLSSAGAL
GVALSNIVSF SRILTYLIQA WTQMETSIGA ISRLKSFTEE TSSEHLPEEV IVPKGFWPSR
GAIQFRSLTS GYGGKSSLIL SILRMTDIHG GTITIDGIDL ATLSRESVRE KLNVMPQDAM
ILSGSVRFNI DPSGKSDEEI LSALAEVGLL DLIESRGGLS STLDASALSS GQQQLICLTR
ALINPSRILI LDEATSNVDQ ETETKMVKLI QDRFRGCTVV AVAHRLRTIR DFDVILVLDQ
GRVLEYGRPD DLLQIPGSRF RELWESQR
//