ID A0A1F5L2L4_9EURO Unreviewed; 1864 AA.
AC A0A1F5L2L4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGE47445.1};
GN ORFNames=PENARI_c044G09507 {ECO:0000313|EMBL:OGE47445.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE47445.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE47445.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE47445.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636}.
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:OGE47445.1}.
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DR EMBL; LXJU01000044; OGE47445.1; -; Genomic_DNA.
DR STRING; 1835702.A0A1F5L2L4; -.
DR OrthoDB; 1829487at2759; -.
DR Proteomes; UP000177622; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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 GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR CDD; cd18579; ABC_6TM_ABCC_D1; 1.
DR CDD; cd18580; ABC_6TM_ABCC_D2; 1.
DR CDD; cd03250; ABCC_MRP_domain1; 1.
DR CDD; cd02186; alpha_tubulin; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
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; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR044726; ABCC_6TM_D2.
DR InterPro; IPR002452; Alpha_tubulin.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR24223:SF404; ABC MULTIDRUG TRANSPORTER (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01162; ALPHATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR PROSITE; PS00227; TUBULIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000177622};
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 31..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 492..514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 526..547
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 871..895
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 921..945
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1013..1037
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1109..1129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1135..1156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 275..552
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 599..826
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 884..1164
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1202..1451
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1864 AA; 206690 MW; 7B225FC1B0236D00 CRC64;
MSCPAGSDNL LGPRVNLSCR PFDFTLLFED ALFTVLPTSL FLLAATARLS VLVRAPVKVN
SHRLATWKLA VLGLLLLFHL LYLAFRIQDP HLYTSLALAS SILDVVVIMI SLLLSWLEDQ
RSIRPSDLMI IYFAVTSILS LARARTLWLL SVNATKSAIL WTLVCVGTAA VLSIESVHKT
QRLRMAYRQP SKEVTASFWV RSFFIWVIPL FRTGFSTILS VHDMPNVDDA LTGAEAERKI
LKAWACVEPG SKHRLLRAAC RAYFLPLISA IVPRLCLSAF KFCQPFLISA TLNFVSSPST
PENKIYGSAL VGAYVLTYLG MAISNAVYWR QAFRLNTMSR AGLIPLIYRQ TTKLRSGDFK
DKPAITLMGT DVERIVSTLH ALHEVWAAPL EVGVGIFLLE RQLGVACLIP AVISLLAVIA
TVPISQKSNI AISRWIERVQ ARLSVTSSML QDMKSIKMLG LTEKLFESVS QLRRVELQVS
ERFRRLLVGQ VILSNIPLTL APFATFSIFT IISAAKGSES LLSTRVFTSL SLISLMTAPL
LIFVQLLPSL YQSIACFDRI EMYCTKVPFD FADENVWADS IELSDTLSNL PPTSQDSVVE
FHKASFSWSQ ETSPVLHHLE FAVKRKMITA VIGPVGSGKS TLLESALGET VLTEGSISPF
QSTVAYCPQT AWIVNDTIRQ NITGPSSFDP KWYKFVIWAC ALENDLEDIP GGDLSKAGSS
GVTLSGGQKQ RISLARGLYS RAPVLVLDDV FSGLDNKSIS TITSRLFASD GHFKDSGRTV
ILATHNHRVL AYADEIIVLD DGKVTNITTY DCIRHSLPQD SDTESSEASS DEKVYNVSKL
QTKNSDPIVQ LREAEETDQD MSRRDGTWSV YAYYLQSAGW KMIVILATSV VLFGFSDKFT
TIWLQRWSDA NEQHPNQKPG LYLGVYAGLF GISLVSLVAA CWALFVRVIN NTGLMMHAHL
LRSTLNAPFS FFQKVDAGLT TNRFSQDMEL IDMTLPSQAI NTYLGLSNCC VQLVILCIMG
KYLTITVPAL GVILFFVQRY YLRTSRQVRL LDIEAKSPLF THFVETMQGI SAIRAMKWKV
PFQERLEDAL NRSQKPFYML FCIQQWLQLV LDCVVMALAV ILVSLVVSLK SQFSAGSIGV
ALNLILSFNT DLMILIKSWT MLETSIGAVS RVQSFVKDTP SEIEPEGTMA DLPPQWPAYG
EVIFQNTVAR YSPDAPPILN NVSLSIKQGE KIAICGPSGS GKTSLILGLL QMIELQSGSI
QIDGMDLSTL QCHEVRSRVN VIPQEPFFIP GTLRFNLDRG TAISSLPDAC LIDALETVGL
WKKIASGDGG LDQPLSVSDW SMGERQLLAL ARALVMKSAI LVLDEATSRH VLRSLQFVDW
ETEATMQAII EREFASQTVI SVVCHIHIGQ AGVQIGNAAW ELYVHPLPHH SHAKTRDSYL
LEHGLNADGS INPDVTDDTV TSGSYETFFT ETTSGKYVPR AIFVDLDPSP IDEIRTGTYR
QLFHPEQLIS GKEDAANNYA RGHYTVGKDI SESVVDRIRR VADNCSSLQG FMIFHSYGGG
TGSGFGALLL ERITTEFSRK SKLEFSVYPS PRTSTAVVEP YNAVLSTHST IENSDCTFLV
DNDAVYDLCR RNLDIPRPGY EHMNGLIAQV VSSITSSLRF DGVLNVDLAE FQTNLVPYPR
IHYPLISYAP VNSEKSSSHE SFKVQDLTFK CFEPRNQMVI CDLQKGKYMA VALLYKGDIV
LRDCVQAVAA LKAKTSFNLV QWCPTGFKLG INYQKPVRVP GSQLAPVDRS VSMLANTTAI
AEAWCRLDHK FDLMYSKRAF VHWYVGEGME EGEFSEARED LAALEKDYEE VAEDSVVEAG
ETEY
//
