ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
O67074 | MKSSPKSLKMRDNLLDGTFVVIDLEATGFDVEKSEVIDLAAVRVEGGIITEKFSTLVYPGYFIPERIKKLTGITNAMLVGQPTIEEVLPEFLEFVGDNIVVGHFVEQDIKFINKYTKQYRGKKFRNPSLCTLKLARKVFPGLKKYSLKEIAENFGFETNGVHRALKDATLTAEIFIKILEELWFKYGIGDYYSLKRLEKGKF | Cofactor: Binds 2 divalent metal cations. Magnesium or manganese.
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease (By similarity).
Catalytic Activity: a 2'... |
P57337 | MNRKRTIILDTETTGINQTSLPHINHRIIEIGAVEIIDRCFTGNNFHVYIQPGRSIESGALKVHGITNKFLLDKPIFKDIADSFLNYIKNSILVIHNASFDVGFINQELEILNKKIKINTFCSIIDTLKIARELFPGKKNTLDALCTRYKINKSHRNLHSAIVDSYLLGKLYLLMTGGQDSLFSDNTINYKENFKKLKKNIQLKNNTLRILHPTLKENDLHEKYLQYMKDKSTCLWN | Cofactor: Binds 2 divalent metal cations. Magnesium or manganese.
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease (By similarity).
Catalytic Activity: a 2'... |
Q89AN3 | MKKYDRKIVLDIETTGMNPAGCFYKNHKIIEIGAVEMINNVFTGNNFHSYIQPNRLIDKQSFKIHGITDNFLLDKPKFHEISVKFLEYITNSDLIIHNAKFDVGFINYELNMINSDKRKISDYCNVVDTLPLARQLFPGKKNSLDALCNRYKINVSHRDFHSALIDAKLLAKVYTFMTSFQQSISIFDKNSNLNSIQKNAKLDSRVPFRSTLLLATKDELQQHMKYLKYVKQETGNCVWLEDKYN | Cofactor: Binds 2 divalent metal cations. Magnesium or manganese.
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease (By similarity).
Catalytic Activity: a 2'... |
P03007 | MSTAITRQIVLDTETTGMNQIGAHYEGHKIIEIGAVEVVNRRLTGNNFHVYLKPDRLVDPEAFGVHGIADEFLLDKPTFAEVADEFMDYIRGAELVIHNAAFDIGFMDYEFSLLKRDIPKTNTFCKVTDSLAVARKMFPGKRNSLDALCARYEIDNSKRTLHGALLDAQILAEVYLAMTGGQTSMAFAMEGETQQQQGEATIQRIVRQASKLRVVFATDEEIAAHEARLDLVQKKGGSCLWRA | Cofactor: Binds 2 divalent metal cations. Magnesium or manganese.
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease . Contacts both the beta sliding clamp (d... |
O68045 | MGLARLSLRLRIFLFFAALAMGNLAALVAGLVFGFHKLARPEALSGFVIGGTVAGLVILGLIGVVWALFDANLARPIERLAGSIRARTQTAVDSALDESAGRYLGDLAPAAAAIAQHLNETRSALTEAVQRETTRLAREKDRLETLLSDVPVGVLLCTADHALVFYNGQAVDLLGGAHAPGLDRRVFDYLHPAPIRHAHARLLATADPDAASDLLCATVADGRTLAARMRLISEGEDHQVRRLAGYVLTLRDVSADLRAHAGREALMDELFDRIRRPAAALQSLMGVLIAEDGPADPQARAQLREAARAEAGHLAQAIHS... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(... |
Q9ZCJ9 | MSSLREIILDTETTGLDPQQGHRIVEIGAIEMVNKVLTGKHFHFYINPERDMPFEAYKIHGISGEFLKDKPLFKTIANDFLKFIADSTLIIHNAPFDIKFLNHELSLLKRTEIKFLELTNTIDTLVMARNMFPGARYSLDALCKRFKVDNSGRQLHGALKDAALLAEVYVALTGGRQSTFKMINKPDEINNLAVKCVDVQQIKRGIVVKPTKEELQKHKEFIDKILIQA | Cofactor: Binds 2 divalent metal cations. Magnesium or manganese.
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease (By similarity).
Catalytic Activity: a 2'... |
O83649 | MIYDWVFAVHEHVAFTAFDTETTGLKAEEDRIIEIGAVTFDRKGIIARFSTLIFPDRAIPPDVSKINHITDDMLVNKPRFCEIVSDFSRFIKGTVLVAHNANFDVEFLNAELSLCKKQPLSHKVVDTYAMAQAVFPGLGRHQYRLQNLALQFGLTVHAAHRAEDDARVCMELFTTMIAHHAKQNGHCVNHAQSPTIKKLIQEIQASSTDCSQELF | Cofactor: Binds 2 divalent metal cations. Magnesium or manganese.
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease (By similarity).
Catalytic Activity: a 2'... |
P09122 | MSYQALYRVFRPQRFEDVVGQEHITKTLQNALLQKKFSHAYLFSGPRGTGKTSAAKIFAKAVNCEHAPVDEPCNECAACKGITNGSISDVIEIDAASNNGVDEIRDIRDKVKFAPSAVTYKVYIIDEVHMLSIGAFNALLKTLEEPPEHCIFILATTEPHKIPLTIISRCQRFDFKRITSQAIVGRMNKIVDAEQLQVEEGSLEIIASAADGGMRDALSLLDQAISFSGDILKVEDALLITGAVSQLYIGKLAKSLHDKNVSDALETLNELLQQGKDPAKLIEDMIFYFRDMLLYKTAPGLEGVLEKVKVDETFRELSEQ... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 62763
Sequence Length: 563
EC: 2.7.7.7
|
P57553 | MNYQILARKWRPQYFRDIIGQKHIVTAISNGLSLGRIHHAWLLSGTRGIGKTTIARLLAKSLNCQNGITSDPCRQCIICKEIEKGLCLDVIEIDGASRTKVEEMREILDSIYYSPIKSRFKVYLIDEVHMLSRHSFNALLKTLEEPPEHVKFVLATTDVDRIPKTIISRCLYFKLQIISEEKIFKFLKYILIKESIDTDEYSLKKIAYHAHGSIRDALNLLEHAINLGNGHVNIKNVTDMLGLLPEKYSFLLTDAVLKKDSKKTMLLLNKISSIGVEWEEILIEMLRFLYHISTSQSFPLVWEKIFTEKYKNQIQKIAQN... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 41607
Sequence L... |
Q8K983 | MNYQILARKWRPQSFKKIIGQKYIVKAISNGFSLGKIHHAWLLSGTRGVGKTTIARLIAKSLNCEIGITSLPCRKCTICQEIEKGICLDFIEIDAASRTKVEEIREILDNIYYTPSKSRFKVYLIDEVHMLSRHSFNALLKTLEEPPQHIKFILATTDVEKIPKTIRSRCLHFKLNILSEEDIFNFLKHILKKGGNNFDEEALKIISDYANGSMRDALNLLEHAMHLSKNNINLKNTTEMLGIPNKKHAFLLTKFLLEQDSKKMMCLLNKISKIGLEWQNILIEMMRFLHHIAMLKSYPKIWNQIFIKNNENEIKKIAEN... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 42186
Sequence L... |
Q8EQ56 | MQPSKVNKHRIIFHIDMNCFYASVEMAHNPSLKGKPLAIAGNPEERKGIIVTSSYEARGKGVKTTMPIWQAKKLCPDLILMRPNFDRYRAASREIFKMLAEITPYVQPVSIDEGYMDITDTIYAKDPLVTANQLQQRILSGLDIPCSIGIAPNKFLAKMASDMKKPLGITVLRKREVEKLLWPMSVEEMYGIGEKTAQKLNSIEIKTIGDLAKKNVYELKQLLGVNGERLQNRANGIDNRLVDPEAVHDFKSIGSSQTLPHDSTDVTELMQLIHELVDNVERRVKRKEAAGKTVQITIRYHDRKTITRSKKLYNYIDNHR... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
B1ZN03 | MILPTIVHLDADAFFVSCELALKPELRGTKCAVGGRERGIISSASYEARACGVYTPMPTTRALKVCPDLIMLPHTGGLYSRVSRQMFELCETLTPLVQRNSIDEGYLDLGPCGFKTSAEIEQAVHGLQHKIEQQLQITASFGLAVNKLVAQIASKLRKPKGFVVVPSGTEAEFLAPLPIGKLPGVGPKTEERLVGRHGIKLVRDLLARGEAELEAIFGDGWREMRDGALGIDDRPVETEHEDAKSYSQQETFDEDIASFAEIERVVKRMIDELLPKIREDGKRVRTMTVKVRYPDFSQESHGRSLSAGTDLEAPFYPLVT... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
Q6MA55 | MTLRKIIHIDMDAFYASVEMRDDPSLVLKPIAVGGDPDKRGVIATANYLARKFGVRSAMPSWKAKQLCPDLIILFPDFDKYKRESKAIHEIFHLFTDLIEPLSLDEAFLDVTDVDALRGSATWIAQEIRQLIWKERGLTASAGVAPNKFLAKVASDWHKPNGQFVLTPKEVDAFMVHLPVEKIFGIGHVMAKKLHSLGLMNCGDLQTLDITTLQKLFGSRAWNLYELCRGIDHRFVISDRIRKSLSVESTFLEDLNNLELCYQEIPNLIERLMIRYEKISNQYYKKKPFIKIKFADFTTTTVENTFFKAFDLETYQTLIR... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
Q6KZW2 | MIMLIDFDYFFAQVEEINDPSLKGKPVVVSVYSGRNERSGAVATSNYEARALGIKSGMPLYRALEIGKNRAVFLPIRKDFYQKYSDKIMDIISEYSEKMEIASIDEAYIDIDGNDCKIGIANEIKNRILNETGIKVSIGIGINKVIAKMAAEMAKPNGIKCISADETGEFLNNIKINDIPGIGKVLSKNLNEIGIEYLRDIKNFDVNKIKSILGESKTNYLYELYENKYFSPVEPRVKKNFGRYLTLPENTRDIDKIVPYLKKSIDAAYEKAPGIPQEISVVAIMEDLDIVSRSYTGNAIKRDDSINIALNLLNKIISED... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
Q3KH18 | MTQRKIIHVDCDCFYAAIEMRDDPSLAGKPLAVGGSADRRGVIATCNYEARAYGVRSAMSSGHALKLCPDLTIVKPRMDAYREASKEIHTIFSDYTDLIEPLSLDEAYLDVSDSAHFGGSATRIAQDIRRRVSNQLHITVSAGVAPNKFLAKIASDWRKPNGLFVITPDQVEEFVSGLPVSKLHGVGKVTADKLGKLGINDCLQLREWDKLALVREFGSFGERLWSLARGIDERLVHNDSRRQSISVENTYDVDLPDLRSCLDKLPELLETLKTRMARIDSSYRPGKPFVKVKFHDFTQTTLEQAGAGRDLGSYQLMLTQ... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
Q87Y22 | MTQRKIIHIDCDCFYAAIEMRDEPELAGKPLAVGGSAERRGVIATCNYEARAYGVRSAMSSRHALKLCPDLTIVKPRMEAYKEASREIHSIFRDYTDLIEPLSLDEAFLDVSDTHHFSGSATRIAQDIRRRVSNQLHITVSAGVAPNKFLAKIASDWKKPNGLFVITPDQVEDFVASLPVTKLHGVGKVTADKLGRLGIVDCADLRSRSKLALVREFGSFGERLWSLAHGIDDRPVQNDSRRQSVSVENTYDTDLPDLAACLEKLPALLETLGTRMERMEGQYRPGKPFVKVKFHDFTQTTLEQSGAGRDLGSYEQLLTQ... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
Q92076 | EEGWVPGPSLISLQMRVTPKLMRLAWDGFPLHYSEKHGWGYLVPGRQDNLPAASAEPEGPVCPHRAIERLYRQHCLQRGQEQPPEEAGVEDELMVLEGSSMWQKVEELSQLELDMERPGRAEQSQMQDEDGLPELVEESSQPSFHHGNGPYNDVNIPGCWFFKLPHKDGNENNVGSPFAKDFLPRMEDGTLRAAVGRTHGTRALEINKMVSFWRNAHKRVSSQVVVWLKKGELPRAVTRHPAYSEEEDYGAILPQVVTAGTITRRAVEPTWLTASNARADRVGSELKAMVQVPPGYSLVGADVDSQELWIAAVLGEAHFA... | Function: Involved in the replication of mitochondrial DNA. Associates with mitochondrial DNA (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 72855
Sequence Length: 647
Subcellular Location: Mitochondrion
EC: 2.7.7.7
|
P17396 | MHPFSRLFRNIQSLGEEEVQELLGPPEDALPLLAGEDLNHRVADALNLHLPTADLQWVHKTNAITGLYSNQAAQFNPNWIQPEFPELHLHNDLIQKLQQYFGPLTINEKRKLQLNFPARFFPKATKYFPLIKGIKNNYPNFALEHFFATANYLWTLWEAGILYLRKNQTTLTFKGKPYSWEHRQLVQHNGQQHKSHLQSRQNSSMVACSGHLLHNHLSSESVSVSTRNLSNNISDKSQKSTRTGLCSYKQIQTDRLEHLARISCGSKIFIGQQGSSPKTLYKSISSNFRNQTWAYNSSRNSGHTTWFSSASNSNKSRSRE... | Function: Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3... |
P11292 | SKRYSPPLNYEKSDFSSPGVRGRITRLDNNGTPPQCLWRSFYNTKPCGSYCIHHIVSSLDDWGPCTVTGDVTIKSPRTPRRITGGVFLVDKNPNNSSESRLVVDFSQFSRGHTRVHWPKFAVPNLQTLANLLSTNLQWLSLDVSAAFYHIPISPAAVPHLLVGSPGLERFTTCLSSSTHNGNDSQLQTMHALCTRHVYSSLLLLFKTYGRKLHLLAHPFIMGFRKLPMGVGLSPFLLAQFTSALASMVRRNFPHCVVFAYMDDLVLGARTSEHLTAIYSHICSVFLDLGIHLNVNKTKWWGNHLHFMGYVITSSGVLPQD... | Function: Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3... |
P30322 | EFPKYDSITELDVYCNQNNKSDVQMYNFITKLESEYGNITVTVYKGSKTISNDKSILNECELYFVFNIGSNKRVVCLADNKTWDQSLKYWNSSKYPYPRWCDEYLTESEFVRSIGEYKFHVNNGTVKYWEKYYNFPDMVFNYSDKKHDLRIGSLDLETYGDNCFELGLGNLNVYAGGFALNDGFKKLYYLNNDTELNSGEAIIKKMFGDLFDYIAEDRKARNNYTIYAHNLGRFDSVFIIRSLCSEGYKINGQWIDNSILYLKIVDSTRKLTIKLRDSIKLVPHSLDKALSSNGCNISKGMFPHKFVNKDTLNYIGDKPD... | Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 91922
Sequence Length: 797
Subcellular Location: Mitochondrion
EC: 2.7.7.7
|
P10582 | MQPARRHTKKKNMNYMRYESLTREQFERFLKDVHKCYRGEPRYVIPYEGHLIAVQDFEEPYPKAGAVTMLASAFMELLINRVYPSIQGSAKFTLQYRLNIDGNPINITLSKAIKLTYADGTRIANEFILKEIINVLNKYAENYQSCDVEAISVRAYSEGSIDLNQASIPTKDESLNYLKGALIKYSDINNLEIPKMGRRSKRRYQSYIPVDKTEMKNKTLFFVADLETLLLKRRDTDVDKTHVPYAGGYMMVDMEKWVNADHITTFYAHDYSKVCQDFHDMSEKMLTEMINRIVKDVQRRGSSMVVYFHNLSQFDGIMIL... | Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 107533
Sequence Length: 929
Subcellular Location: Mitochondrion
EC: 2.7.7.7
|
P33537 | MIKFYFTTFHMKFPARLFSTSGNRANFEENSSNEVQNQIKYLKDFKKENPKFNWESTTEPKHMILSNIGEYEKNDFNLKSLLNINEFNINVELLRQLFMKLDKNFTYALGVILRNVDSNTNISVDRHFLVNFNTDPVIILQQIYDRIIFLSEKYYLVPVDKLFIKLRKLNFKVKNPVFHPIAKEKTNIHTTIPKGKSKLSRAEFVPHTMDLKFYGVETKHDKEKNIRIFDNGKVILKVKIIKDGVYHLIDVISRDNRLLYQFEDVKHGDGLKRYWINDNMYYYYYDNTLVNVETPQKVGNIEPAKRDKTQDKKILAFDIE... | Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 119076
Sequence Length: 1021
Subcellular Location: Mitochondrion
EC: 2.7.7.7
|
P33538 | MSKFSFFNYRINMRNSHATLGSLPCFIKFNYLSSSSHSKFYSTSTDSPMGHIVSASKSSWYNYYSHKNYDPLTRESFHDELRGFISLYKKQFKEEKFFFMAKIKFNNNDIRSISTVQIGSTDPLEVLRLLEAITSTYMHTHTGISEAVSEPFEYELFSLGDGLPKGNIIFTFKPTSNPSIKTKYEHKSNIKRNKNINLSKKNPLNKFKYNGYTIPNTMDLSQWPNIHFINDGKNAVSLNNIIKSGVDNMTLSFFITINKKYNEITVLLNNTPIFKIKDEKIMSEDDLSSFKRTITENEQDKVYVFENGEMVFFSENVKTS... | Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 112830
Sequence Length: 969
Subcellular Location: Mitochondrion
EC: 2.7.7.7
|
A2RI77 | MAEEKVLEVKNLHVNFHTYAGDVKAIRNVSFDLEKGQTLAIVGESGSGKSVTTKTLMGLNAKNAEIPEGELLFKGRNLLDLKEEEWQKIRGNEISMIFQDPMTSLDPTMRIGKQIAEPLLKHNKGMSKADAMKRALELMQQVGIPDAEVHINDYPHQWSGGMRQRAVIAIALAADPEILIADEPTTALDVTIQAQIMHMMAELQERINSSIVFITHDLGVVAGFAHKVAVMYAGEIVEYGTVEEIFYNPQHPYTWGLLDSMPTVDSSVDRLVSIPGTPPDLLNPPKGDAFAARNKFALAIDFEEEPPYFEVSPTHFAKTW... | Function: Part of the ABC transporter DppABCDF involved in dipeptide transport . Responsible for energy coupling to the transport system (Probable).
Catalytic Activity: a dipeptide(out) + ATP + H2O = a dipeptide(in) + ADP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38910
Sequen... |
A0A0H2ZGN6 | MSLLDIKNLSVRFGDTTAVPVVDGLDLSVDKGEVLAIVGESGSGKSVTMMALMGLIDAPGWVSADHLRFDGHDMLTLKGRQRRRIVGKDMAMVFQDPMTALNPSYTVGYQIEEVLRLHLGLRGKALRQRALELLERVEIPAAASRLDAYPHQLSGGMSQRVAIAMAIAAEPKLLIADEPTTALDVTIQAQIMELLLNLQRDQDMALILITHDLAVVAETAQRVCVMYAGEAVEIGGVPALFDRPTHPYTEALIKAIPEHCAGEARLATLPGIVPGRYDRPRGCLLSPRCPYAQEHCRQERPALEAHERGAVRCFYPLNLL... | Function: Part of the ABC transporter DppABCDF involved in the uptake of various di/tripeptides . Is also involved in the uptake of phaseolotoxin, a toxic tripeptide inhibiting the enzyme ornithine carbamoyltransferase . Responsible for energy coupling to the transport system (Probable).
Catalytic Activity: a dipeptide... |
P26906 | MKRVKKLWGMGLALGLSFALMGCTANEQAGKEGSHDKAKTSGEKVLYVNNENEPTSFDPPIGFNNVSWQPLNNIMEGLTRLGKDHEPEPAMAEKWSVSKDNKTYTFTIRENAKWTNGDPVTAGDFEYAWKRMLDPKKGASSAFLGYFIEGGEAYNSGKGKKDDVKVTAKDDRTLEVTLEAPQKYFLSVVSNPAYFPVNEKVDKDNPKWFAESDTFVGNGPFKLTEWKHDDSITMEKSDTYWDKDTVKLDKVKWAMVSDRNTDYQMFQSGELDTAYVPAELSDQLLDQDNVNIVDQAGLYFYRFNVNMEPFQNENIRKAFA... | Function: Probably part of the ABC transporter DppBCDE involved in dipeptide transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 61819
Sequence Length: 543
Subcellular Location: Cell membrane
|
P37313 | MSTQEATLQQPLLQAIDLKKHYPVKKGMFAPERLVKALDGVSFNLERGKTLAVVGESGCGKSTLGRLLTMIEMPTGGELYYQGQDLLKHDPQAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSKEQRREKALSMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKDQIFNNPRHPYTQALLSATPRLNPDDRRERIKLSGELPSPLNPPPGCAFNARCRRRFGPCTQLQPQLKDYGGQL... | Function: Part of the ABC transporter DppABCDF involved in dipeptide transport . Responsible for energy coupling to the transport system (Probable).
Catalytic Activity: a dipeptide(out) + ATP + H2O = a dipeptide(in) + ADP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37560
Sequen... |
A2RI78 | MTEPKKVVEIKNLDLTFNKGKKGANKAINNVSLDIYEGETFGLVGESGSGKTTIGRAILKLYDNFITGGEILFEGKDVRNLKGSELREYRSEAQMIFQDPQASLNGRMRVKDIVAEGLDANGLVKTKAERDARVLELLRLVGLNDDHLTRYPHEFSGGQRQRIGIARALAVKPKFVVADEPISALDVSIQAQVVNLMRDIQAKENLTYLFIAHDLSMVKYISDRIGVMHWGKILEVGTSEQVYNHPIHPYTKSLLSSIPSPDPISERQRTPIVYDPTAELDGQEREMREITPGHFVFSTEAEAEVYKKNATL | Function: Part of the ABC transporter DppABCDF involved in dipeptide transport . Responsible for energy coupling to the transport system (Probable).
Catalytic Activity: a dipeptide(out) + ATP + H2O = a dipeptide(in) + ADP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34883
Sequen... |
Q8NLQ9 | MSEHAAEHHRDTQNFLTSEPHTTAIEDNKKRQPPKNLADGMIKALRPKQWVKNVLVLAAPLAAGADAIFNQRTIIDVAIAFVVFCFGASAIYLVNDARDVEADREHPTKRFRPIAAGVLPVGMAYGMAVALIALSIGLSFLATDGVALACVIGVYIALQLGYCFGWKHMPVIDIALVSSGFMLRAMAGGVAAGIELSQWFLLVAAFGSLFMASGKRYAEILLHERTGAKIRKSLESYTPTYLRFVWTMAATAVVMSYALWGFDLSQHSTDAGPWYQISMVPFTIAILRYAAGVDTGDGGAPDEVALSDKVLQVLALAWVF... | Cofactor: Divalent metal cations such as Mg(2+), Mn(2+) or Ca(2+).
Function: Involved in the biosynthesis of decaprenylphosphoryl arabinose (DPA) a precursor for arabinan synthesis in mycobacterial cell wall biosynthesis. Catalyzes the transfer of a 5-phosphoribosyl residue from phosphoribose diphosphate (pRpp) to deca... |
A0R626 | MDATHMSEEAQPTAGPPKNLVSGLIKAVRPRQWIKNLLVLAAPLAAVGSGIEYDYADVAAKVSVAFVVFCLAASSIYLINDARDVEADRAHPTKRFRPIAAGVVPEWMAYSLAGLLAVASLVISWWLTANLAIVMAVYIAVQLAYCFGLKHQAVLDICIVSSGFLIRAIAGGVAADIPLSQWFLLVMAFGSLFMAAGKRYAELQLAERTGAKIRKSLESYTSSYLRFVWTLSATAMVVCYGLWAFSRDRANDLMTLDAQDASWYAVTMIPFTIAILRYAVDIDGGIAGEPEEIALKDRVLQILFLAWIGTIGAAIYFS | Cofactor: Divalent metal cations such as Mg(2+), Mn(2+) or Ca(2+).
Function: Involved in the biosynthesis of decaprenylphosphoryl arabinose (DPA) a precursor for arabinan synthesis in mycobacterial cell wall biosynthesis. Catalyzes the transfer of a 5-phosphoribosyl residue from phosphoribose diphosphate (pRpp) to deca... |
Q95WU5 | MTLSAWIILVTLAMASVLTPEDNVRLRRLTAYVANADASIVLLTYTEYEEGTNHGNSMLWRINDPLEAEYPFDPDDISLLNAERVCPELVGVGDLQYSTHNQAFYFTAQGPDGTSQVYSYNHKLETCTQISFLPISVSNLKVSPKGNSVLFSAEIFVYPNNHASVDDPLNFAHDEFARIQARPYKAFAYEQLYTRHWDEDILPSQYRHLFAARLERSSEYDDDYVRITVDNSIDLMPRFDGDCPMRPFADASSYTFDSHGRYVAFVTQVGSTAAFYTNDSIWITDLQQFLDAKKPVRDVVLPLRCATCWNKARDQRPAFS... | Function: May be involved in metabolism of dipeptides or may affect host defense mechanisms.
Sequence Mass (Da): 87648
Sequence Length: 761
Subcellular Location: Membrane
EC: 3.4.14.-
|
Q8DPI7 | MKITNYEIYKLKKSGLTNQQILKVLEYGENVDQELLLGDIADISGCRNPAVFMERYFQIDDAHLSKEFQKFPSFSILDDCYPWDLSEIYDAPVLLFYKGNLDLLKFPKVAVVGSRACSKQGAKSVEKVIQGLENELVIVSGLAKGIDTAAHMAALQNGGKTIAVIGTGLDVFYPKANKRLQDYIGNDHLVLSEYGPGEQPLKFHFPARNRIIAGLCRGVIVAEAKMRSGSLITCERAMEEGRDVFAIPGSILDGLSDGCHHLIQEGAKLVTSGQDVLAEFEF | Function: Protein that helps load RecA onto ssDNA during transformation . Required for DNA transformation . Not required for DNA uptake but for a later stage of transformation . Thought to interact at the cell pole with newly imported transforming ssDNA which it binds cooperatively, protecting linear and circular ssDNA... |
A0R607 | MSTTEFPTTTKRLMGWGRTAPTVASVLSTSDPEVIVRAVTRAAEEGGRGVIARGLGRSYGDNAQNGGGLVIDMPALNRIHSIDSGTRLVDVDAGVSLDQLMKAALPHGLWVPVLPGTRQVTVGGAIGCDIHGKNHHSAGSFGNHVRSMELLTANGEVRHLTPAGPDSDLFWATVGGNGLTGIILRATIEMTPTETAYFIADGDVTGSLDETIAFHSDGSEANYTYSSAWFDAISKPPKLGRAAISRGSLAKLDQLPSKLQKDPLKFDAPQLLTLPDIFPNGLANKFTFMPIGELWYRKSGTYRNKVQNLTQFYHPLDMFG... | Function: Component of the DprE1-DprE2 complex that catalyzes the 2-step epimerization of decaprenyl-phospho-ribose (DPR) to decaprenyl-phospho-arabinose (DPA), a key precursor that serves as the arabinose donor required for the synthesis of cell-wall arabinans . DprE1 catalyzes the first step of epimerization, namely ... |
Q8NEX9 | MAALTDLSFMYRWFKNCNLVGNLSEKYVFITGCDSGFGNLLAKQLVDRGMQVLAACFTEEGSQKLQRDTSYRLQTTLLDVTKSESIKAAAQWVRDKVGEQGLWALVNNAGVGLPSGPNEWLTKDDFVKVINVNLVGLIEVTLHMLPMVKRARGRVVNMSSSGGRVAVIGGGYCVSKFGVEAFSDSIRRELYYFGVKVCIIEPGNYRTAILGKENLESRMRKLWERLPQETRDSYGEDYFRIYTDKLKNIMQVAEPRVRDVINSMEHAIVSRSPRIRYNPGLDAKLLYIPLAKLPTPVTDFILSRYLPRPADSV | Function: Displays weak conversion of all-trans-retinal to all-trans-retinol in the presence of NADH. Has apparently no steroid dehydrogenase activity.
Sequence Mass (Da): 35263
Sequence Length: 313
Subcellular Location: Cytoplasm
EC: 1.1.1.-
|
P42291 | MENFSIFNVTVNVWHADLDVGNSDLSLRALTGLLLSLLILSTLLGNTLVCLAVIKFRHLRSKVTNFFVISLAVSDLFVALLVMPWKAVTEVAGFWVFGDFCDTWVAFDIMCSTASILNLCIISLDRYWAIASPFRYERKMTQRVAFIMIGVAWTLSILISFIPVQLSWHKSHEADEELNGVNHTENCDSSLNRTYAISSSLISFYIPVVIMIGTYTRIYRIAQTQIRRISSLERAVEHAQRCSSRLSNENSLKTSFRKETKVLKTLSIIMGVFVFCWLPFFVLNCMIPFCHMNLPGQNEPEPPCVSETTFNIFVWFGWAN... | Function: This is one of the five types (D1 to D5) of receptors for dopamine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52641
Sequence Length: 465
Subcellular Location: Cell membrane
|
P35406 | MAVLDLNLTTVIDSGFMESDRSVRVLTGCFLSVLILSTLLGNTLVCAAVTKFRHLRSKVTNFFVISLAVSDLLVAVLVMPWKAVTEVAGFWPFGAFCDIWVAFDIMCSTASILNLCVISVDRYWAISSPFRYERKMTPRVAFVMISGAWTLSVLISFIPVQLKWHKAQPIGFLEVNASRRDLPTDNCDSSLNRTYAISSSLISFYIPVAIMIVTYTQIYRIAQKQIRRISALERAAESAQIRHDSMGSGSNMDLESSFKLSFKRETKVLKTLSVIMGVFVCCWLPFFILNCMVPFCKRTSNGLPCISPTTFDVFVWFGWA... | Function: Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase. Could be involved in growth hormone release.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40652
Sequence Length: 363
Subcellular Location: Cell membrane
|
P21728 | MRTLNTSAMDGTGLVVERDFSVRILTACFLSLLILSTLLGNTLVCAAVIRFRHLRSKVTNFFVISLAVSDLLVAVLVMPWKAVAEIAGFWPFGSFCNIWVAFDIMCSTASILNLCVISVDRYWAISSPFRYERKMTPKAAFILISVAWTLSVLISFIPVQLSWHKAKPTSPSDGNATSLAETIDNCDSSLSRTYAISSSVISFYIPVAIMIVTYTRIYRIAQKQIRRIAALERAAVHAKNCQTTTGNGKPVECSQPESSFKMSFKRETKVLKTLSVIMGVFVCCWLPFFILNCILPFCGSGETQPFCIDSNTFDVFVWFG... | Function: Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49293
Sequence Length: 446
Subcellular Location: Cell membrane
|
O02664 | NTLLVCAAVIRFRHLRSKVTNFFVISLAVSDLLVAVLVMPWKAVAEIAGFWPFGSFCNIWVAFDIMCSTASILNLCVISVDRYWAISSPFRYERKMTPKAAFILIGVAWTLSVLISFIPVQLSWHKAKPTSPPDGNATSLDETVDNCDSSLSRTYSISSSLVNFYNPVAIMXVTYTRIHR | Function: Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20114
Sequence Length: 180
Subcellular Location: Cell membrane
|
P18901 | MAPNTSTMDEAGLPAERDFSFRILTACFLSLLILSTLLGNTLVCAAVIRFRHLRSKVTNFFVISLAVSDLLVAVLVMPWKAVAEIAGFWPLGPFCNIWVAFDIMCSTASILNLCVISVDRYWAISSPFQYERKMTPKAAFILISVAWTLSVLISFIPVQLSWHKAKPTWPLDGNFTSLEDTEDDNCDTRLSRTYAISSSLISFYIPVAIMIVTYTSIYRIAQKQIRRISALERAAVHAKNCQTTAGNGNPVECAQSESSFKMSFKRETKVLKTLSVIMGVFVCCWLPFFISNCMVPFCGSEETQPFCIDSITFDVFVWFG... | Function: Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49428
Sequence Length: 446
Subcellular Location: Cell membrane
|
P24628 | MDPQNLSMYNDDINNGTNGTAVDQKPHYNYYAMLLTLLVFVIVFGNVLVCIAVSREKALQTTTNYLIVSLAVADLLVATLVMPWAVYMEVVGEWRFSRIHCDIFVTLDVMMCTASILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVMISVVWVLSFAISCPLLFGLNNTGSKVCIIDNPAFVIYSSIVSFYVPFIVTLLVYVQIYIVLRKRRKRVNTKRNSRGVAVDAHKDKCTHPEDVKLCSVFVKSNGSFPADKKKVILVQEAGKHPEDMEMEMMSSTSPPEKTKHKSASPDHNQLAVPATSNQCKNASLTSPVES... | Function: This is one of the five types (D1 to D5) of receptors for dopamine. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. In Xenopus D2R is involved in the regulation of the melanotrope cells of the intermediate pituitary during background adaptation of the animal.
PTM: Palm... |
Q8IS44 | MLSPFDWRRGISSSGTGGTMAAQPLSSTAATTAAATGATAATAATAATTSATLSTAAASTSTTAAPSAGATWINHHLAVEADSSQPANGSDAQAGVEGPTMPAGYLPLYEDVETAAEDAGYALIDDISEWLLGSVGSEAAVGGPENSTNLAVTGANGTLAWLEALNSTQPAQSNSSAEDGERGRYSLRSFVEQQLAGGGAAGAGDGGDAGIALIDSGEEAALDNVADAETDYGMLGGFGDAELLQRTATVARETLGNRTAPSTTSYDGGGSGDVGVAGGLAGTAGGGVGGAGGSGGSTFMLLLENFNDYFPNYNGSTVSG... | Function: Receptor for dopamine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 95057
Sequence Length: 905
Subcellular Location: Cell membrane
|
C5M444 | MTSNILLLLHPTVVTDQHIVENIKLKISNTHKDFHLSQTTIDRLTQGSIEFDNNSFDEIIYINPNEEQYREIPNSLMKLIFDLLKLNGKFTGDLPTDQNLDVLMNGFLIINQNEWNKPQPEETVVTLKKKSTTTNNNSNTSTIKKSFPMFKKLNNDNASTPGLTDSSAGTSEDETATVSNKRKLVESKLVYFSDDDDDDDYDGSSDGEDLINENDLIAESNKYKIIVPKKCELPNGKKRKKACKDCTCGLKELEEEEIKSQGKLQDTVLANMAQSATIEAIKIEERMKKNKIKFTEEDLSEIDFTVAGKTGGCGSCSLGD... | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold ... |
A8NWK4 | MAPTAVYTQKDSPSSSQPSSKGPALAIGSLETAQDGKYQSLITELEATRQVDKLLLDRLVDGATTLEPSKYNSVHVTLASSDYQSLQESTLRSLLTQLLTGLTPLGTLHLLNLTDGLKTLPSELTLSGFLVLSAAGENPGDSIVAQKPAHAIGASVSLKKRGSATTTSTTAFVTTTTTTSTSTTTATVTSAPSVPLLLRKRGDPAKKKALWALTTDASASPSTKIDADALLTAEDKARPVPTCAPVDRSAPRRKKACKNCSCGLAELEEEEKRNAPVVVIDSSIDGEGGAKAVDKAERERLLEAAKNAPKATSSCGSCFL... | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold ... |
P0CM12 | MPAPVPPTAFAQPSGPATQLVLGSMQRAPEYQALLTSLKSAAPPSSSVQGEMVDRILDNATTLPPPPLTIHLVLPLPLPSNLLSAIPPSTQIFIHIPADSESQLGALHSALASHSFTPVLPTPSPSTLAYTSPSAPSLPAVASEPSPAPSSSTPVTLSGARPLQLRRNGDKARKAALWAIDSPLIPDGGKSLLTPADRTRPDCVFPAENGKPVKRRRACKDCTCGLKELEQEEEAQTSAAVQEAQKAFFLEGDDDIPENLKKATEGMEGIWPADKRAEAKKTSSCGSCYLGDAFRCSSCPYLGLPPFKPGEQVQVSIGDD... | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold ... |
Q5CWQ7 | MTQLIITHQSDSKLEESEVFLSELNRIKKEEDKFGKFSSLSDLRAIVKKGEFRIVSIYLSSGSILGEIFTFEFLKEFYGVLDFGSVLKVNILALDSIDKVKAFERNLLFSGFIKVKKLKGDGLNSSDSDFEIVIKAEKPSWKPEEGKVLVDDIDLEGSVPDIKNYVPLGQGKESCKSKERACNNCNCGRADLEKEIGVEAARKVYQEKVETGTARSSCGNCYLGDAFRCSGCPYKGMPAFKPGEKVSLANAEGDANDHTVDMNLIHEEKVDLITTTFDDDGSGVNNVQSKGGVLKLNI | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosoli... |
B0WQ75 | MNFVQENNQVLYIWGGTISADIEQEVNQLKSIPGVKVNVENAERVLLGGYGQSQFDIILANVSTGNSELVSHLLKLTKPKGKAVFKDDSAAGGAETVRANLLLSGFINIASAEGNVYIAEKPNYEIGSAAKLSLGGGANKAKVAAVWKLDVDDDGEAEERIDEDELLDEEDKVKPSAESLRVCGTTGKRKACKDCSCGLAEELDAESKGAAVAAAQSAKSSCGSCYLGDAFRCATCPYLGMPAFKPGEKIQLSDTQMQADV | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosoli... |
O15692 | MNSLSLELNKEQEVLIISDVENSESIINQVKELSKTVTTSLSKEQQQIQNNFDHVIIISSKPFNSALISMYSNLLKKGGKLSIYQTNENETLVNSGMDFLIGGLVDFKATSNSTYKTIVHADKPSWDTNESSTINIPSTSSNNPWASIEGGDRINENDLVSENDKTSKPATTLDDCEVGKTKKACKNCTCGRAEEENQSKPKLTKEMIENPGVGSSCGNCSLGDAFRCGGCPYRGLPTFKVGEKIQLPDDFLVDDI | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosoli... |
Q9V3Y2 | MENFKGLQKSLYIWTDSADLDKRVEQLKAATGGDVALENVHRLSFSSYANSSFDLIVIECAQLTDSYVKLLHMLKPSGKLHLVSYIGPAASLLQEIKLSGFINCREDSPDALTAEKPGYETGSSARLSFAKKNASAVNVWKISGDDEELIDEEELLDEEDKQKPDPAGLRVCSTTGKRKACKNCSCGLAEELETEKQSQKATENAKSSCGNCYLGDAFRCSTCPYLGMPAFKPGEKVQLADNLLKSDI | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosoli... |
Q10SU5 | MVDWASDSDNDKFEWDTDGEAETSSAPALRNIDAPGPSTRLPQDANGKANGSGALVAEFMGMGFPKEMILKAIKEIGDTDTEQLLELLLTYQAIGGDASVGNCSASACAPQTLEVDEEEDDTNWDEYDTAGNCDRTPHSDGSGDEDFFQEMSEKDEKMKSLVNMGFPEDEAKMAIDRCGLDAPVAVLVDSIYASQEAGNGYSANLSDYEDTEFSSFGGRKKTRFVDGSKKRKRYGSGPSGNQVPFDGSHEEPMPLPNPMVGFSLPNERLRSVHRNLPDQALGPPFFYYENVALAPKGVWTTISRFLYDIQPEFVDSKYFC... | Function: Involved in de novo DNA methylation. Required for CpG and non-CpG methylation. Required for normal establishment and maintenance of RNA-directed DNA methylation (RdDM) mediated by small interfering RNAs (siRNAs). Regulates proper plant development in both vegetative and reproductive stages through DNA methyla... |
P0DW07 | MRNVTRSHMVLHQIQSVLKKYEEVSAQELYESLDKGTVQREFGVRSVDLSRLSVSEEQFSELLLLFKLYSDQQQQSSIEFVATVPSEVDVRLRKTIAVIREMIHGAQNTILVTGYAVSEYVDEIMERVLEKALAGVNVDIFLDRNPQTDRYIENIRGRNLPSNFNVYVYKGSQGYSSLHAKVIMVDEEKAFVSSANLSYNGIVNNIEIGTLVGGEKILVIKNVLLELVKNNYFEKIIWYA | Function: Component of antiviral defense system DISARM (defense island system associated with restriction-modification), composed of DrmE, DrmA, DrmB, DrmC and DrmMII. DISARM is probably a multi-gene restriction module, this subunit is probably a phospholipase or nuclease. Expression of DISARM in B.subtilis (strain BES... |
Q9VQS6 | MFAVMRIDNDDCRSDFRRKMRPKCEFICKYCQRRFTKPYNLMIHERTHKSPEITYSCEVCGKYFKQRDNLRQHRCSQCVWR | Function: Putative transcription factor. May function redundantly with odd and sob in leg joint formation during the larval stages, acting downstream of Notch activation. Acts in a hierarchy during foregut and hindgut patterning and morphogenesis, antagonizing lin to relieve the repressive effect on bowl. Involved in c... |
P26295 | MSKKLRNFLVRIIVAAFASFAVMAIPPYHHNTVLAKTVSVNQTYGEYKDYYTVIGESNIDQSAFPKIYKTTERVYKGQGTSEKRVTVSDVVYNPLDGYKRSTGAYGVVTKDMIDMSKGYREKWETNPEPSGWFRFYNRADNEEISEKEYDSRRTKSYKVTNNVPVVLTTLKGKKYNSHLFVASHLFADSLGGKSIRKNAITGTQMQNVGTRKGGMQYIEKKVLSHITKNPDVYVFYSAIPEYQGAELLARSVLVSALSSDGVINETVRVFNTADGFNINYEKGGLLTESPVSEIDNIEDSTTDEIENSVDDSEEIVYNDT... | Function: May have a role in S.equisimilis virulence.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 36844
Sequence Length: 327
EC: 3.1.21.1
|
Q44064 | MSRPSRVLGLPLLSLGLTLLVSTPLQAQEAQTFRAVKQDLVKLYQSHPSTFYCGCNIKFSGKKMAPDWESCGYLPRKQANRAARIEWEHVVPAWEFGHQLQCWQEGGRKNCGKSAEFNKMEGDMHNLFPAIGEVNGDRANYRFSDWNGKPNQYGKCQMLVDFKEQRVQPPKGPVRGQIARAYLYMGEQYGLRLAAQQRKLFEAWDRQYPADRWECERNRRIGKLQGNTNPFIEKQCQ | Function: Endonuclease which is capable of degrading plasmid DNA.
Sequence Mass (Da): 27377
Sequence Length: 237
Subcellular Location: Periplasm
EC: 3.1.21.-
|
Q566S6 | MERALGVGIGPLAAGTVGLLILLKVIQRLRRRPNIQDKVVVITGASSGLGKECARVFHAAGARLILCGRDQRRLQEVVEELGNKTYGKTKTYTPCTVTFDLSNTSVVCSAAAEILKRHGHVDVLINIAGVSYRGNILDTHVSVQREVMETNYFGPVALTQAILPSMVDRGSGHIVVISSVQGKISIPYRSAYAASKHAMQAYYDCLRAEVDSLGLHVSVLSPGYVRTNMSINAVTGDGSKYGVMDRTTATGADPVDVAKDILKAVCQKKKDVVMAGLGPTTAIYLRTLWPALYFRVMASRARKQTGKEE | Function: Putative oxidoreductase.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 33348
Sequence Length: 309
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.-.-
|
Q6IAN0 | MVSPATRKSLPKVKAMDFITSTAILPLLFGCLGVFGLFRLLQWVRGKAYLRNAVVVITGATSGLGKECAKVFYAAGAKLVLCGRNGGALEELIRELTASHATKVQTHKPYLVTFDLTDSGAIVAAAAEILQCFGYVDILVNNAGISYRGTIMDTTVDVDKRVMETNYFGPVALTKALLPSMIKRRQGHIVAISSIQGKMSIPFRSAYAASKHATQAFFDCLRAEMEQYEIEVTVISPGYIHTNLSVNAITADGSRYGVMDTTTAQGRSPVEVAQDVLAAVGKKKKDVILADLLPSLAVYLRTLAPGLFFSLMASRARKER... | Function: Putative oxidoreductase.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 35119
Sequence Length: 325
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.-.-
|
Q99J47 | MISPSFRKGMLKERVMDLASQTTILPLLFGCLGIFSLFRLLQRIRSKAYLRNAVVVVTGATSGLGRECAKVFHAAGAKLVLCGRNVKALEELSRELAGSSQGQTHQPFVVTFDLADPGTIAAAAAEILQCFGYVDVLINNAGISYRGTISDTIVDVDRKVMEINYFGPVALTKALLPSMVERKQGHIVAISSIQGKISIPFRSAYSASKHATQAFFDCLRAEMEEANIKVTVISPGYIHTNLSVNAVTADGSRYGALDKNTAQGRSAAEVAQDVFDAVGKKKKDVLLTDFVPSMAVYIRTLAPGLFFRIMASRARKERKS... | Function: Putative oxidoreductase.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 34987
Sequence Length: 323
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.-.-
|
Q0IH28 | MDLTSWAIFPLLLASIGVYGLYKLLQKLRSGAYLQAAVVVITGATSGLGKECAKVFYAAGSHLVLCGRDEERLKDLVQELNNMRLKSTQLHKPHMVIFDLSDVEAVNTAAKEILHLAGRVDILINNAGISYRGTILDTKVSVDRMVMDTNYFGPVALTKALLPSMIKNRRGHVVVISSVQGKISIPFRSAYSASKHATQAFFDCLRAEMSPYDIDVTVVNPGYIKTNLSLNAVTGDGSGYGVMDKNTADGRTPEEVAQTVLRAVGERRKELLVAGLVPTLAVYLRTLAPTLFFSIMSARAKKRTKAKGFITNSNLKAKIT... | Function: Putative oxidoreductase.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 35153
Sequence Length: 323
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.-.-
|
Q8CHS7 | MGLMAVLMLPLLLLGISGLLFIYQEASRLWSKSAVQNKVVVITDAISGLGKECARVFHAGGARLVLCGKNWEGLESLYATLTSVADPSKTFTPKLVLLDLSDISCVQDVAKEVLDCYGCVDILINNASVKVKGPAHKISLELDKKIMDANYFGPITLTKVLLPNMISRRTGQIVLVNNIQAKFGIPFRTAYAASKHAVMGFFDCLRAEVEEYDVVVSTVSPTFIRSYRASPEQRNWETSICKFFCRKLAYGVHPVEVAEEVMRTVRRKKQEVFMANPVPKAAVFIRTFFPEFFFAVVACGVKEKLNVPEEG | Function: NADH-dependent oxidoreductase which catalyzes the oxidation of all-trans-retinol to all-trans-retinal . Plays a role in the regulation of cardiac and skeletal muscle metabolic functions (Probable). Maintains Ca(2+) intracellular homeostasis by repressing Ca(2+) release from the sarcoplasmic reticulum (SR) in... |
P36655 | MAQRIFTLILLLCSTSVFAGLFDAPGRSQFVPADQAFAFDFQQNQHDLNLTWQIKDGYYLYRKQIRITPEHAKIADVQLPQGVWHEDEFYGKSEIYRDRLTLPVTINQASAGATLTVTYQGCADAGFCYPPETKTVPLSEVVANNAAPQPVSVPQQEQPTAQLPFSALWALLIGIGIAFTPCVLPMYPLISGIVLGGKQRLSTARALLLTFIYVQGMALTYTALGLVVAAAGLQFQAALQHPYVLIGLAIVFTLLAMSMFGLFTLQLPSSLQTRLTLMSNRQQGGSPGGVFVMGAIAGLICSPCTTAPLSAILLYIAQSG... | Function: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. ... |
P44919 | MKKLFLFFTLIFTAFAANSGLFDKKQTFLKVDDAFAFSATLSTDKSQLQAHWDIADGYYLYQDKISAELVGKSNPLSLHTQQAAELHQDPYFGEVKVFTHSIDGIFRGAFNNADDKVEITYQGCTEGFCYPPETKVLRIGDLVVSQKQIVEKTVEKNTALLSEQDRLADGLFHSKWAIFGFFVLGLGLAFTPCVLPMLPLLSAIVIGQQQRPNMMRAFSLAFLYVQGMALTYTLLGLAVAAIGLPFQIALQHPYVMIGLSILFVALALSMFGLFTIQLPNSLQNKLNTWSQKQTSGAFGGAFAMGMIAGLVASPCTSAPL... | Function: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction step... |
Q5QVU3 | MIQRFITCLAALTLVFAVVAPAHSVQSNPFQQDNQFLSVDQAFDFDSEVNDSKVTVSWVVAPEYYLYQHRFKVVPENALAAEPELPQGESHNDEFFGESIVYRNYVEWSFTLNPEFSGDTITVQYQGCADAGLCYPPTEKQIKLSSTSETAPATAPPNTDSSLFGIGEQHLIITLLLFFALGIGLAFTPCVFPMYPILSGVVLGNRERNWKNTLWLSFIYVQGMAITYSLLGLVVASAGMQYQAYFQHPVVLIVLAVLFALFALSMFGAYTLQLPISWQSKLQSFSGQQSGGNIVGVFIIGAISGLVASPCTTAPLSGAL... | Function: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction step... |
Q9JYM0 | MKKLICLFAVFLMLCGRAFALDANDLLPPEKAFVPELAVADDGVNVRFRIADGYYMYQAKIVGKTDPADLLGQPSFSKGEEKEDEFFGRQTVYHHEAQVAFPYAKAVGEPYKLVLTYQGCAEAGVCYPPVDTEFDIFGNGTYHPQTDEPASAKDRFLQPSSQNGSGALPPPKGDEGGDSRFKLSWDTLNANLLAFFLAGLGLSFTACMYPLLPIVSSIVVGDKKAGKARAFVLSVVYVQGLALTYTLVGIVAGLTGALLTVWLQQAWVVLAASALMVVLALSMFGLFNIQLPNAVQSYFQNQSSRLSGGKIVSVFIMGIL... | Function: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction step... |
Q7MZX2 | MIKRTLMLFLLLCSPLLTPAAANALFEQPGQNPYLPVDQAFMFDFQQKGDKLTLDWQIKPGYYLYHKQLHIEPQQATLGKITLPQGTAHRDEFFGETEVYFQQLIVNVPVTKANNNSNIVVTYQGCAAAGYCYPPETRLVPLSAVIPSKTTDAISAEPVHKTPESASNDQQHLPFSPLWAILIGIGIAFTPCVLPMYPLISSIILGSQRPKSLKQIFWLALSYVQGMAVTYTLLGLIVAAAGLQFQAALQHPYVLIGLSVLFILLALSMFGLYSLQLPSAVQTRLVNWSNQQKNGSLFGVFAMGALAGLICSPCTTAPLS... | Function: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction step... |
Q15ZS2 | MKLIASFSIFMLMSIWSFASLGQSNSFDSLFSNEPEFLKVDQAFVFDYVQNGDQLVVTWDIADDYYLYQQQFKAVSKNASLGEPIFPTGKMKEDEFFDEPQEVYYHKVSVTYPILQSQDDSAVKIRYQGCAEAGLCYPPTTQVVYLNAVNASDDLSNTDEASVESSGSVSQQFELADLLTGDQSLIWVLLIFLALGVGLAFTPCVFPMYPILSGIVIGQGKSISTSRAFVLSFVYVQGMALTYSLLGLVVASAGVQFQAALQHPIILGALIVVFALLALVMFGAWEFQLPSSWQEKLNGVSNQQKSGSYLGVLLMGAISG... | Function: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction step... |
D3RPC1 | MEQKKLAIIATKGSLDWAYPPFILASTAAALGYEVQVFFTFYGLQLLKKKPNLEVTPLGNPGMPMPMGMDKWFPVLGLALPGMQGMMTAMMKQKMKSKGVASIEELRELCQEAEVKMIACQMTVDLFDMPKAEFIDGVEYAGAAAFFEFAGESDICLYI | Function: Sulfur carrier protein probably involved in sulfur trafficking for oxidative dissimilatory sulfur metabolism. May be a component of a cytoplasmic sulfur relay system delivering sulfur to DsrC. Binds sulfur in the presence of sulfide in vitro.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): ... |
O87896 | MKFALQINEGPYQHQASDSAYQFAKAALEKGHEIFRVFFYHDGVNNSTRLTTPPQDDRHIVNRWAELAEQYELDMVVCVAAAQRRGIVDEGEASRNGKDATNIHPKFRISGLGQLVEAAIQADRLVVFGD | Function: Not known. Could be involved in the oxidation of intracellular sulfur.
Sequence Mass (Da): 14588
Sequence Length: 130
Subcellular Location: Cytoplasm
EC: 2.8.1.-
|
Q86MA2 | MTPRRVAKLVQFSGSYLNTEWARKFILGSLLQRYNPQSLTTVGSSAAGNSGEDASLDKELLHLQRSLSEVWSLPAQPLDAVSEGRILRLLARYATGEGVMSIEALNELSHVLSCIRGSPQRVEGPIDMEELLLAIGYAKPGDNLRRVAFAGELQYPPSALAHMRAHLRDDMERDGSDPFDILRVVTHNPAYAIDSASTSEVDDAIGVHKDPVTGEECFVVYVSDATVYCPFDSPLEQLTARLLTTTTYLPEGVFFMLPKPIVDAATLREDRPCRTFDIRFQIDEVTGELKNYSVGVGWLHKLRRITYDEVQALYDEEAQV... | Function: 3'-5'exoribonuclease which is involved in the post-transcriptional processing, editing and degradation of mitochondrial RNAs, including mRNAs, rRNAs and guided RNAs (gRNA) . As part of the mitochondrial 3' processome (MPsome), involved in the maturation of guided RNA (gRNA) precursors by catalyzing the proces... |
P39112 | MVVRRKVHVLLIARSFHSYTPCFRVTTRGKRQRSKSKQQAKVELDHTRELDNDQATETVVDRSVGPEKDIESINKDFLQRTKGLEPDIELKQLPQIKQEFNQRYKDRYVKPSEDWYVNSWRSLTKPKIPLYKLINSDFQLITKLKAPNPMEFQPVQLMESPLNVGDFVLLKMRPNELAMCVSLPSSTMDPRYTFVTIDGTMCFATKNRVLLRIPHKLPAGIHSLIQPESHHKHLPIGTVKNFSNQTNILPIVARQLITSRYPAQISKLAWKDLPITTKKLQLLHRSLQNYMGPWQIPFFTLVGLVQKLDLNKALDDKNGI... | Function: Essential for mitochondrial biogenesis.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 110822
Sequence Length: 969
Subcellular Location: Mitochondrion matrix
EC: 3.1.13.1
|
B9LV23 | MIAIVVSRADSASEHIGEHLLDLGDWERRDDPSRPDADGGGTYYRTDGFELREFDDLHIYLDDPAAAFGGGAGDETNDAASDDTDETPEFLAFVSRHSGETGELLTAHVTGNFGPAPYGGEPDTLARAAPGAEKRVVEALAAHAPEGYDVGIECTHHGPTDTSVPSLFVELGSDEPQWTDADAARAVARAVLDLRGTDADLVTDAGETTDEIDDDPHPRHVVGFGGGHYAPRFTRIVRETEWAVGHVGADWALGELGAPDANRDVIEQAFARSKANVAVIEGEKPDLEATVEALGHRVVSETWVRAVGDRPLPLVERLES... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
Q18KS1 | MIGLVVSSADTASVTISDQLHELVEWESHRDAAGDEYEQYDDFEMRTIDEWHLEAENASELFSTTPQIIAFLSRHSGDTGPLLTTHFTGNFGPAEYGGEPGSFAQACPMIQQTLLEAFDRYAPSKYDVGIECTHHGPTTVGAPSLFVELGSSKAEWNDPDGAHAVAQAILELSGEDAPANVETDRTVVGFGGGHYAPRFERIIRETDWVVGHIGADWALDSMGAPAANRDIINHAVTASDADVALVADDRPELTKVISQADIRVVQERWLRETTGVSRPMVSALENALVPIASGLRLGTPATEYDPATSDEFVITDRHTD... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
A2BKX3 | MLALIYSARDPAGSGTARIIRELLGGDRCSLPRAVECTLLSNGVYLVGFDADSIFLDFLGEVLPANIEGYVVLSRHSGGKPSLTVHHTGNPGPEAPYGGKPWSLAPAWPRTAAGLLRTYRRVAEEMGLTGEFQVTLEATHHGPTELEKPIVFIEIGSSEREWVRRDTQNAMAETVIRFMERDLVSVECSKVAIGIGDTHYPIKHTRNVLERGYCYSHIFSKHVLDNLTLELLEQALEKTRDKVDTVVLAKVPSRVKQLARSFAEKYGLQLEK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
A8ABM7 | MKVTVVYYPGDPAAKGAAEALEREYGIKALELPEDPPFFDFNSLAGDAFIVLSRHSSEKRVKAFTVHHTGNFGEAKLGGEPKRLGVAYPSLACSLLRAMNAFRREGYDVTYEATHHGPTSDKPLVFAEIGSVKEDWEDPANHEVLAKAVASWEEHRCEAPKAVWVGGPHYSKRATKRCLEGEACFGHIAPKYALDHLDEDLLRQMVERSFERPERAYVEKKSLKSELRLRVVKALEDLGLEVLVV | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
B1L7I3 | MSKRLALAYSKKDPAGSGMAREIKDMMGEEFEISDKRCELIEVDREILYINGSQFEGFDYLAVLSRHSGTPNHPIFTAHVSGNFGRARYGGDHFKLSIAIPSLMKEYLISVSKRAEEIGYWVGFEPTHHGPTLDIPTAFLEIGCDETAWRDERGLRAAAESVLEAIESWKDGKFVAAVAFGGPHINDHFTRVELFTRFAIGHAARKLDAEWVDGEMVKQAVSRNGEPTGVAIVDNKGLKGEDRERIEGALRDLGLEVIRVKKILRDELGEEEGEEI | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
A6UUZ4 | MKYLFINSSKDKAGINIRNNLEKLNNINNNCIIDFFETPKKLTELSKKDLPQDYDYYIFLSKHRSVSEKPTLTVHTSGNLTTDNSHGGNIEEVCCCDAILNTILLVNINKYNNLEKYKKLGFDVSFEAIHHAPTDLDVPSVFVEIGSSEKEWAIDEAGEIMANAIIDTISSIESKSYKKLDKVIAFGGGHYAPRFTKLSLSNKCFVGYIIPKYAKISEKVLQQLIQMQDFDYILFDWKGINSEDKKRYIEFFDKNNILWKKVKDLCY | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
P58850 | MTDTNPENVNNSKITIICSAPDLASQNIKKHLLALREWKPLELPENSGFSAVLESADGKFRLVDIEEIHVFQDGLDKKLEAAGLPAELIIFASKHRSKEEVKSLTVHCTGNSSNEARLGGHPKELAVSSPPAMKSILMEMKRLAKVKGLDYDVTLEVTHHGPTELNVPSLYAEIGSTEGQWEEPVPGEIVARAILTVSLEKVPTAVGFGGGHYAMRQTGLLLETAISFGHNFPKYQLEFVDEALIRQAVEKSNAEFAYFDRKSMKSADRKRISQILEKLGLKVLKESEIREKYGREE | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
A7IAL9 | MKVALIHSRDDVAGCTIRRHIEQCLDDAHGSANGRTYEFVEVGGRLINAEGVDATLDVNLVIFLSRHSSVNPVPVLTVHATGNFGAAELGGSPRTLAPAAPAMMQATLRALARYCPEGYRVSYEVTHHGPTGLSHPSFFVEIGSTEKEWVDPVAGRAVAEAVLGADPAGAVPLIGIGGTHYAPRETAIALSSRGAFGHIASSRLQVALLDRELVQAMVVQSRAVAAYIDRKAVLPGDVSRISAILDELGIPRLSETEITSLGHLAWEAYREVRALAATVGPQTRCFIHALEGTGPLVLVSLDPVLLSEAKRCDESALVQR... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
Q12UQ4 | MTEDNEVQIAGMSIVIVCSVVDPASQNIKEHLLKLRDWVEMSVPGGIFDDLSAVYQSGNFYIIEVTEHHIYQDGIDRKIEEAGLDCDLLIFASKHKSADGRRLLTAHFTGNPGSADFGGYPGELSMAAPFALRCLLRNMAELSESIGFDVSMESTHHGPSDLDVPSVYAEIGSSEVEWVDQDAGDIVARSILSVRSGFCPVGIGFGGGHYAARQSELVLGSDISFGHNFPNYQLQFVDVDMFRKAVERSGADLVYCDRKAMSSDEKKRINELADEFGLDVLRESDIKGMEGVCWDIFRIFWHKVRDEGLSGRVKVPVGLK... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
Q2FPX3 | MTPKEQSPTTLLISSRKDPAGSLIHEELYSFLEDDKRAHSHIRHWHAEERLIYLDGPSLPHDADRILFLSRHASERPRPVLTVHVTGNFGSADYGGRPNTLTPAATGLMHALINRLIIHAPEGYEVMYEATHHGPTDIPLPSCFIELGSTEKEWNDRIAARAVAQAVLDALLMDTSSVIPLAGFGGTHYAQRQTEITKLTRGGFGHIMPTRDIPHLTDALFQDIISSTGAFAIYIDGKSMSGKEERMITGLADKHTIPILGQGDLMRLFDLPFSEYMSIRNLAESLIPGSSIVLHTILEMPAPVSLTIPGELVDEVMKVA... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
P58851 | MRRVVILWNPDDPASKNIAESLTEDAEKLDTEDLQHYTVETWERDGVRFHLTAALGDLIEEDEARELARKFDVIVFASRHESRTKKPSLTVHVPGNPTPEAKFGGKPLEVCTADPAGMKAALLELKRFRDKRGLDYDVCYEVTHHGPRDPGAPCFFIEIGSDEERWTDEEAGEACARAILAAVDPPDVKAVVGYGGGHYAPAHTDAALSNRKLAYGHIVPDYAVDHDYLRDQFREVVDKTPRAREIIVDDRNLDSGIVERLEDLVRDRGLRLRDVEEVK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
A2STU3 | MIIDILNSDSDPAGRNIRAAIDELLKNPPEGGFPLFDGNEVTFHTVSGRIIHAEKSAVNPDADLIIVVSRHSSVNPVPVLTVHPAGNFGIAGLGGNDRELGLTSPAWMKSILQNHAEFVPEGYRVSYEITHHGPTDFPVPFFFVEVGSTEKEWNDPAACIAAAKSVLYARPSPEIVPLIGFGGTHYAVRQTAIGLETKGAFGHMMHTRDVGSVSKEMVSQMIAKSCGVFAAHIDRKALSKQEISHIEGILAEVGLEEITEGDLRKMNAMSFSTWVAYRDLAALQAPGLKIFPHGRIFDGDPAVVELPSDLFSAAFLGYEE... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-amino... |
Q65GR0 | MRLVVQRVTDASVSVGGETVGEIGLGLMVLVGVTHEDTSEDAAYLAEKLVNLRIFEDEGEKMNLSLLDVGGSVLSVSQFTLYGDTKKGRRPNFTKAAKPDQALQLYEEWNSMLRAKGVTVETGRFGEMMDVKLTNSGPVTFIMDSKA | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
Q8A2P0 | MRIVVQRVSHASVTIEGQCKSSIGKGMLILVGIEESDGQEDIDWLCKKIVNLRIFDDESGVMNKSILEDGGEILVISQFTLHASTKKGNRPSYIKAAKPEISVPLYERFCKDLSRALGKEIGTGTFGADMKVELLNDGPVTICMDTKNKE | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
Q8G4Q2 | MKVVLQRVSEASVDVVNELGTLDPTFEPQQIGPGFMILVGVTDGDGDKQIAWLAHKILNLRVFEDAQGKMNRSIQDIGGEILSISQFTLFADVHKGNRPSFIKAGKPEHADLMWIKFNEALRSGGVPVKEGRFGAHMRVGLVNDGPVTIVIDTEHDMPDGTR | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
Q88VQ3 | MRVIVQRSQQAQVSIDGKVRGTIDHGFVLLVGFQDGDGQAELDYIAHKILNLRVFSDADGKMNLNIQQVGGAILSISQFTLYAETRHGNRPSFTAAGNPELASKLYDTFNQQLAASGVTVATGEFGADMQVSLVNDGPVTICYDTDQR | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
Q8E988 | MIALIQRVSRASVVVDNQTIGAIDKGLLVLLGVEREDNREKMEKLATKVMSYRVFSDENGKMNLNLTQAGGSLLVVSQFTLAADTERGLRPSFSGAGTPEQALGLYEEFVAFCRTKGVNTETGQFAADMKVELVNDGPVTFHLQV | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
A0KRY8 | MIALIQRVSRASVVVDNQTIGAIDKGLLVLLGVEREDNREKMEKLATKVMSYRVFSDENGKMNLNLTQAGGSLLVVSQFTLAADTGRGLRPSFSGAGTPEQALGLYEDFVAFCRAQGVTTETGQFGADMKVELINDGPVTFNLQV | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active si... |
B8NR70 | MVKNNAGIVNMFEKRRTQTTTIPIIEIMREKRSEDLETEIVQGLQFDSLQLPQELLWDDAGQILFDDLCNSSTYYLTKKEKEILQKYSTDMAATIPEGSTLIELGCGSLRKTGILLSALEKSHKAVTYYALDVSQDSLENGLAQLHKGLGCLDHVELRGLWGTYEDAIAWLADQHPINVHNGITFLWMGNSMTNMHLAQAQSLLSRMTKTCIGSGIPCQILVSVDSCSAEDIVMGAYDTDSQPLKDFIMNGLKSANRILGKDVFCASDWTFGTVLDRVRHEVQVFYAPTRDVTIHIDSHPCKITKGEKIAVISSGKWPEP... | Function: N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the dimeric diketopiperazine alkaloid ditryptophenaline . The nonribosomal peptide synthase dtpA accepts L-tryptophan and L-phenylalanine as its substrates and forms the phenylalanyl-tryptophanyl cyclic dipeptide product cyclophen... |
P36837 | MNTTTPMGMLQQPRPFFMIFFVELWERFGYYGVQGVLAVFFVKQLGFSQEQAFVTFGAFAALVYGLISIGGYVGDHLLGTKRTIVLGALVLAIGYFMTGMSLLKPDLIFIALGTIAVGNGLFKANPASLLSKCYPPKDPRLDGAFTLFYMSINIGSLIALSLAPVIADRFGYSVTYNLCGAGLIIALLVYIACRGMVKDIGSEPDFRPMSFSKLLYVLLGSVVMIFVCAWLMHNVEVANLVLIVLSIVVTIIFFRQAFKLDKTGRNKMFVAFVLMLEAVVFYILYAQMPTSLNFFAINNVHHEILGFSINPVSFQALNPF... | Function: Proton-dependent permease that transports di- and tripeptides. Has a clear preference for dipeptides and tripeptides composed of L-amino acids, and discriminates dipeptides on the basis of the position of charges within the substrate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53575
Se... |
B8NR71 | MKTPEYLAPLREELAAALKQADNAWSFDIFKHTPKLESFTKECLRVFTPSGKKPLQLRSTGRTLSPGTKFSLPAQQAHLDPDNYPNPNIFDGYRFCDPQSGACDIRGTITPSAKWLIFGIGTSACPARLLATRISQTLFFKVLRKYDLRLKLDNGQPEVVYAATNMFVNFNTQMYVKSASI | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the dimeric diketopiperazine alkaloid ditryptophenaline . The nonribosomal peptide synthase dtpA accepts L-tryptophan and L-phenylalanine as its substrates and forms the phenylalanyl-tryptophanyl cyclic dipeptide product... |
P39276 | MKTPSQPRAIYYIVAIQIWEYFSFYGMRALLILYLTHQLGFDDNHAISLFSAYASLVYVTPILGGWLADRLLGNRTAVIAGALLMTLGHVVLGIDTNSTFSLYLALAIIICGYGLFKSNISCLLGELYDENDHRRDGGFSLLYAAGNIGSIAAPIACGLAAQWYGWHVGFALAGGGMFIGLLIFLSGHRHFQSTRSMDKKALTSVKFALPVWSWLVVMLCLAPVFFTLLLENDWSGYLLAIVCLIAAQIIARMMIKFPEHRRALWQIVLLMFVGTLFWVLAQQGGSTISLFIDRFVNRQAFNIEVPTALFQSVNAIAVML... | Function: Proton-dependent permease that transports di- and tripeptides. Shows significantly higher specificity towards dipeptides than tripeptides. Has a preference for dipeptides with a C-terminal Lys residue. Can bind Ala-Lys, Lys-Ala, Ala-Ala. Can also transport alanine and trialanine.
Location Topology: Multi-pass... |
P75742 | MNKHASQPRAIYYVVALQIWEYFSFYGMRALLILYLTNQLKYNDTHAYELFSAYCSLVYVTPILGGFLADKVLGNRMAVMLGALLMAIGHVVLGASEIHPSFLYLSLAIIVCGYGLFKSNVSCLLGELYEPTDPRRDGGFSLMYAAGNVGSIIAPIACGYAQEEYSWAMGFGLAAVGMIAGLVIFLCGNRHFTHTRGVNKKVLRATNFLLPNWGWLLVLLVATPALITILFWKEWSVYALIVATIIGLGVLAKIYRKAENQKQRKELGLIVTLTFFSMLFWAFAQQGGSSISLYIDRFVNRDMFGYTVPTAMFQSINAFA... | Function: Probable proton-dependent permease that transports dipeptides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54159
Sequence Length: 493
Subcellular Location: Cell inner membrane
|
O94469 | MVQPELTQSVGYGIVVGLGLGFAALMIFVSWSLKKFNNENQTSEHFNTASHSVRTGLVASAVVSSWTWASTLLTSAQKTYQYGVSGAFWYASGACVQILLFTVLAIELKRKAPNAHTFLEVVRARCGPIAHGVFLVFAYITNILVMAMLLCGGSATISSVTGMNTVAVCFLLPVGVIIYTMFGGIKATFLTDYIHTVIILVILIMFSLATYSADKKIGSPGKLYDMLKEAGDAHPVAGNAQGSYLTMRSQEGAIFFIINLAGNFGTVFVDNGYWQKAIAANPASALPGYILGGLAWFAIPWLAATTMGLVALGLENKPYF... | Function: Involved in active transport of urea.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71720
Sequence Length: 664
Subcellular Location: Membrane
|
Q8TFG0 | MEPILNQGYGYGFALGLGAAFALLMAIITKVLTACMGQTQNSERFSTASRSVKSGLISSSTVSAWTWPATLLSSGAWSYTYGIMGGFMYGVGGTIQITLFLFLAIQIKKKAPAAHTVSECFFIRFGKLGHCVYLFYCISTNVLVSSLLLLGGSQGFSSTTGMNTVAACFLLPLGVMVYTTLGGLKATFISDWIHTVMIYIILIVTCYTVYCSSSLIGSPAKMYDMLKEVQEVYPATGGQSYLSFKNSEMMYLTWSVMIGGLSSVFGDPGYSQRAIASDAKSVFQGYLMGGLCWWIIPMALGSSAGLACRALLLNPASVTY... | Function: Involved in active transport of urea.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72604
Sequence Length: 673
Subcellular Location: Endoplasmic reticulum membrane
|
Q9URY6 | MTETVLNQGYGYGIVIGLGFAFAIVMILVTYVLKRYVGEVQDSEHFTTASRSVKTGLISSAVVSSWTWPGTLLTSAGMAYEYGVCGSMWYSFAFTVQITFFTVIALQVKRVAPGAHTIVEIVKARFGQASHAVFLFYALGTNIIVSAMLLLGGSQAISAITGMHVVAAGFLLPLGVWLYTVSGGLKSTFLSDWTHTVIVYIVILITLFVAYTSSVHIGSIDKMYDLLTEVSKTNPSTGYKGSYLTVTNRDAVFVGWNIVIGGFATVFCDPSYGQKAIAAKPISAMKGYFAGGLAWLIVPWAMGSAAALSCLALTNNPVSV... | Function: Involved in active transport of urea.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71966
Sequence Length: 661
Subcellular Location: Membrane
|
F4KD71 | MATCPPFDFSTKYYDGDGGCQRQSSFFGGTTVLDQGVGYAVILGFGAFFAVFTSFLVWLEKRYVGARHTSEWFNTAGRNVKTGLIASVIVSQWTWAATILQSSNVAWQYGVSGPFWYASGATIQVLLFGVMAIEIKRKAPNAHTVCEIVKARWGTATHIVFLVFCLATNVVVTAMLLLGGSAVVNALTGVNLYAASFLIPLGVVVYTLAGGLKATFLASYVHSVIVHVALVVFVFLVYTSSKELGSPSVVYDRLKDMVAKSRSCTEPLSHHGQACGPVDGNFRGSYLTMLSSGGAVFGLINIVGNFGTVFVDNGYWVSAI... | Function: High-affinity urea-proton symporter involved in the active transport of urea across the plasma membrane into root cells. May play an important role in urea uptake by plant cells at low external urea concentrations.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75913
Sequence Length: 704
S... |
P33413 | MGEFKPPLPQGAGYAIVLGLGAVFAGMMVLTTYLLKRYQKEIITAEEFTTAGRSVKTGLVAAAVVSSWIWCSTLLTSSTKEYADGIFGGYAYAAGACFQIIAFAILAIKTKQMAPNAHTYLELVRTRYGKIGHGCYLFYAIATNILVTSMLLTSGSAVFSDLTGMNTIASCFLLPVGVVVYTLFGGIKATFLTDYMHTCVIIIIVLVFAFKVYATSDVLGSPGKVYDLVREAAKRHPVDGNYQGEYMTMTSKSAGILLIINLIGNFGTVFLDNGYWNKAISASPAASLKAYAIGGLAWFAVPSLISLTMGLACLAVETSP... | Function: Required for active transport of urea.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80617
Sequence Length: 735
Subcellular Location: Membrane
|
P36504 | CKQSCSFGPFTFVCDGNTK | Function: Is a potent inhibitor of human phospholipase A2.
PTM: Maturation of lantibiotics involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine or the formation of dialkylamine bonds with lysine. This is followed by membrane translocation and cleavage o... |
P36503 | CANSCSYGPLTWSCDGNTK | Function: Is a potent inhibitor of human phospholipase A2. Exhibits only a weak antibacterial activity against B.subtilis, and does not display antimicrobial activity against S.aureus, S.mitis, E.coli, K.pneumoniae, P.vulgaris and C.albicans.
PTM: Maturation of lantibiotics involves the enzymatic conversion of Thr, and... |
Q9Y6W6 | MPPSPLDDRVVVALSRPVRPQDLNLCLDSSYLGSANPGSNSHPPVIATTVVSLKAANLTYMPSSSGSARSLNCGCSSASCCTVATYDKDNQAQTQAIAAGTTTTAIGTSTTCPANQMVNNNENTGSLSPSSGVGSPVSGTPKQLASIKIIYPNDLAKKMTKCSKSHLPSQGPVIIDCRPFMEYNKSHIQGAVHINCADKISRRRLQQGKITVLDLISCREGKDSFKRIFSKEIIVYDENTNEPSRVMPSQPLHIVLESLKREGKEPLVLKGGLSSFKQNHENLCDNSLQLQECREVGGGASAASSLLPQPIPTTPDIENA... | Function: Protein phosphatase involved in the inactivation of MAP kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily. It preferably dephosphorylates p38.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 52642
Sequence Length: 482
Subcell... |
Q9ESS0 | MPPSPLDDRVVVALSRPVRPQDLNLCLDSSYLGSASPGSGSHAPVLATAVVTLKAANLTYMPSSSGSARSLNCGCSSTSCCTVATYDKDHQAQTQAIAAGTATTAIGTSTTCPANQMVNNNENTGSVLSPSGGVGSPVSGTPKQLASIKIIYPNDLAKKMTKCSKSHLPSQGPVIIDCRPFMEYNKSHIQGAVHINCADKISRRRLQQGKITVLDLISCREGKDSFKRIFSKEIIVYDENTNEPSRVTPSQPLHIVLESLKREGKEPLVLKGGLSSFKQNHGNLCDNSLQLQECREVGGGASAASSMLPQSVPTTPDIEN... | Function: Protein phosphatase involved in the inactivation of MAP kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily. It preferably dephosphorylates p38.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 52532
Sequence Length: 483
Subcell... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.