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Database: UniProt
Entry: H2F5M2_9ASPA
LinkDB: H2F5M2_9ASPA
Original site: H2F5M2_9ASPA 
ID   H2F5M2_9ASPA            Unreviewed;      2285 AA.
AC   H2F5M2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Protein Ycf2 {ECO:0000256|HAMAP-Rule:MF_01330};
GN   Name=ycf2 {ECO:0000256|HAMAP-Rule:MF_01330,
GN   ECO:0000313|EMBL:AEX93955.1};
OS   Tulbaghia violacea.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AEX93955.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC   Allioideae; Tulbaghieae; Tulbaghia.
OX   NCBI_TaxID=51492 {ECO:0000313|EMBL:AEX93955.1};
RN   [1] {ECO:0000313|EMBL:AEX93955.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22291168; DOI=10.3732/ajb.1100491;
RA   Steele P.R., Hertweck K.L., Mayfield D., McKain M.R., Leebens-Mack J.,
RA   Pires J.C.;
RT   "Quality and quantity of data recovered from massively parallel sequencing:
RT   Examples in Asparagales and Poaceae.";
RL   Am. J. Bot. 99:330-348(2012).
CC   -!- FUNCTION: Probable ATPase of unknown function. Its presence in a non-
CC       photosynthetic plant (Epifagus virginiana) and experiments in tobacco
CC       indicate that it has an essential function which is probably not
CC       related to photosynthesis. {ECO:0000256|ARBA:ARBA00002329,
CC       ECO:0000256|HAMAP-Rule:MF_01330}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000256|HAMAP-
CC       Rule:MF_01330}.
CC   -!- SIMILARITY: Belongs to the Ycf2 family. {ECO:0000256|ARBA:ARBA00009361,
CC       ECO:0000256|HAMAP-Rule:MF_01330}.
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DR   EMBL; JQ274045; AEX93955.1; -; Genomic_DNA.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd19505; RecA-like_Ycf2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01330; Ycf2; 1.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008543; Uncharacterised_Ycf2.
DR   PANTHER; PTHR33078:SF95; PROTEIN YCF2; 1.
DR   PANTHER; PTHR33078; PROTEIN YCF2-RELATED; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF05695; DUF825; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01330};
KW   Chloroplast {ECO:0000313|EMBL:AEX93955.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01330}; Plastid {ECO:0000313|EMBL:AEX93955.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        74..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1630..1800
FT                   /note="ATPase AAA-type core"
FT                   /evidence="ECO:0000259|Pfam:PF00004"
FT   BINDING         1634..1641
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01330"
SQ   SEQUENCE   2285 AA;  268210 MW;  DA1BEFA9B2FDCB77 CRC64;
     MKRHQFKSWI LELREILREI KNSHYFLDSW IKFDSVGSFT NIFFHQERFM KLFDPRIWSI
     LLSRDSRGST SNRYFTIKGV VLLVVVVLIS RITNRKTVER KNLYLMGLLP IPMNSIGPRN
     ETLEESFWSS NINRLIVSLL YLPKGKKISE SCFMDPQEST WVLPINKKCI MPESNRGSRW
     WRNRIGKKRD SSCKIANEIV AGIEISFKEK DSKYLEFLFL SYTDDPIRKD HDWELFDRLS
     PRKKRNIINL NSGQLFEILG KDLICYLMSA FREKRPIEGE GFFKQQGAEA TIQSNDNDIE
     HVSHLFSRNK WGIFLQNCAQ FHMWQFRQDL FVSWGKNQHE SDFLRNVSRE NWIWLDNVWL
     VNKDRFFSRV RNVLSNIQYD STRSIFVQVT DSSQSKGSSD QSRDHFNSIR NEDSEYHTLI
     DQTEIQQLKE RSILWDPSFL QTERTEIESD RFPKCLFGSS SMSRLFTKRE KQMNNHLLPK
     EIEEFLGNPT SRSFFSDRWS ELHLGSNPTE RSTRDQKFLK KKQDVSFVPS RRSENKEMVD
     ILKIITYLQN TVSIHPISSD PGCDMVPKDE PDMDSSNKIS FLKINLFLDL FHLFHDRNKG
     GYTLHHDFES EERFQEMADL FTLSITEPDL VYHRGFAFSI DSYGLDQKKF LNEVFNSRDE
     SKKKSLLVLP PLFYEENESF YRRIRKKSVR IYCGNDLEDP KLKTAVFASN NIMEAVNQYR
     LIRNLIQIQY SIYEYIRNVS NRFFLMNRSD RNFEYGIQRD QIGNDTLNHI TIMKYTINQH
     LSNLKKSQKK WFDPLISRTE RSMNRDPDAY RYKWSNGSKN FQEHLEHFVS EQKNRFQVVF
     DRLCMNQYSI DWSEAIDKQD LSKSLRFFLS KSLLFLSKSL PFFFVSIGNT PIHRSEIHIY
     ELKGPNDQPC NQLLESIGVQ IVHLNKLKPF LLDDRDTSQR PKFLINGGTI LPFLFKKIPK
     WMIDSFHTRN NCGKSFDNTD SYFSMISHDR DNWLNPVKPF HRSSLISSFY KANRLRFLND
     PHHFWFYCNK RFPFSVEKTR IHNDDLTYGQ FLNILFIRNK IFSLCVGKKK HIFLERETIS
     PIESQVSDIF IPNDFLQSGD ETYNLYKSFH FPIRSDPFVR RAIYSIADIS ATFLREEQIV
     NFERTYCQPL SDMNLSDSEG KNLHQYLSFN SNMGLIHTPC SEKYLPSGKR KKRSLCLKKY
     VEKGQMYGTF QRNSAFSNLS KWNLFQTYMP WFLTSTGCKY LNFTLLDTFS DPLPILSISS
     SQKFVSIFHD IMYGSDISWP IPQKILPQWT LISEISNKCL QNLLLSEEMI HRNNESSVPL
     IWAHLRSRNA REFLYSILFL LLVAGYLVRI HLLFFSRAFS ELQTELEKIK SLMIPSYMIE
     LRKLLDRYPT SELNSFWLKN LFLVALEQLG DSLEEIRGSA SGGNMLLGDG PAYGVKSIRS
     KKKYLNINLI DLISIIPNPI NRITFSRNTR HLSRTSKEIY SLIRKRKNVN GDWIDDKIES
     WVANSHSIDD EEREFLVQFS TLMLMTEKRI DQILLSLTHS DPLSKNDSGY QMIEQPGSIY
     LRYLVDIQKK YLMNYEFNRS CLAERRIFLA HYQTITYSQT SCGANSFHFP SHGKPFSLRL
     ALSLSPSRGI LVIGSIGTGR SCLVKYLATN SYVPFITVFP NKFLDDKSKD YLIDDIDIDD
     SDDIHIDDSD DIDDDLDTEL LTMTNVLTMY MAPKIDRFDI TLQFELAKAM SPCIIWIPNI
     HDLYVNESNY LSLGLLENYL SRDCERCSTR NILVIASTHI PKKVDPALIA PNKLNTCIKI
     RRLLIPQQRK HFFTLSYTRG FHLEKKMFHT NGFGSITMGS NARDLVALIN EALSISITQK
     KSIIETNTIR SALHRQTWDL RSQIRSVQDH GVLFYQIGRA VAQNVLLSNC PIDPISIYMK
     KKSCKEGDLY LYKWYFELGT SMKKLTILLY LLSCSAGSVA QDLWSSPRFG EKNRITSYGF
     VENDSDLVHG LLEVEGALAG SSRTEKDCSQ FDNNRVTLLL RSEPRNPLDM MQNGSFSIVD
     QRFFYEKYES ELEEGAPDPQ QIEEDLFNHI VWAPRIWRPC GNLFDCIERP TELGFPYWAG
     SFRGKRIIYH KKDELQKNDS EFLQSGTMQY QTRDRSSKEQ GFFRISQFIW DPADPFFFLF
     KDQPFVSVFS RREFFADEEI SKGLITYQTN PPTSIYKRWF IKNTQEKHFE LLIHRQRWLR
     TNSSLSNGSF RSNTPSESYQ YLSNLFLSNG TLLDQMAKTL LRKRWLFPDE MKHLIHVTGE
     RFPIP
//
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