PharMolix/UniProtQA huggingface dataset:
Protein: IL1A_SHEEP
Sequence: MAKVPDLFEDLKNCYSENEDYSSEIDHLSLNQKSFYDASYEPLREDHMNKFMSLDTSETSKTSRLSFKENVVMVTANGKILKKRRLSLNQFITDDDLEAIANDTEEEIIKPRSAHYSFQSNVKYNFMRVIHQECILNDALNQSIIRDMSGPYMTAATLNNLEEAVKFDMVAYVSEEDSQLPVTLRISKTQLFVSAQNEDEPVLHKEMPETPKIIKDETNLLFFWEKHGSMDYFKSVAHPKLFIATKQEKLVHMASGPPSITDFLILEK
What is the function of this protein?
Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems.  After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex.  Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4.  In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways.  Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage.  In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as signal for genotoxic stress without loss of cell integrity.
What are the official names of this protein?
Interleukin-1 alpha, IL-1 alpha.
What is the protein family that this protein belongs to?
Belongs to the IL-1 family.
What are the subcellular locations of this protein?
Nucleus. Cytoplasm. Secreted. Note=The lack of a specific hydrophobic segment in the precursor sequence suggests that IL-1 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. Recruited to DNA damage sites and secreted after genotoxic stress.
Protein: DXR_PSEMY
Sequence: MSTVQQITVLGATGSIGLSTLDVIARHPERYAVFALSGFSRLAELETLCVQHRPRYVVVPDAAAAHALQGSLRAAALPTEVLVGEEGLCAVAGHGEVDCVMAAIVGAAGLRPTLAAVQAGKKVLLANKEALVMSGALFMQAVRESGATLLPIDSEHNAIFQCLPGDYGRGLQAVGVRRVLLTASGGPFRETPLAELERVTPEQACAHPNWSMGRKISVDSASMMNKGLELIEACWLFDARPEQIEVVIHRQSVIHSLVDYVDGSVLAQLGNPDMRTPIAHALAWPQRIDSGVSPLDLFAIGRLDFERPDEQRFPCLRLAREAAQVGGSAPAMLNAANEVAVDAFLQRRIRFSDIARMIEFVLNAESARAVEALDAVFEADRRARALAGEWLARH
What is the function of this protein?
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
What are the official names of this protein?
1-deoxy-D-xylulose 5-phosphate reductoisomerase, DXP reductoisomerase, 1-deoxyxylulose-5-phosphate reductoisomerase, 2-C-methyl-D-erythritol 4-phosphate synthase.
What is the protein family that this protein belongs to?
Belongs to the DXR family.
Protein: MTND2_PECAS
Sequence: MSGLTIFSDSDASQPIWQSQDADAIQKQLNDIGVRFERWEASQKLSDAPSSEEVLAVYQHEIDKLVAEKGYQSWDVISMRSDNPQCAELRTKFLSEHIHHEDEVRFFVEGAGLFCLHLNGKIYQILCEKNDLLSVPAGTAHWFDMGPEPHFTAIRLFDNPEGWIAHFTGDKIADVYPKLEC
What is the function of this protein?
Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site.  Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway.  Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
What are the official names of this protein?
Acireductone dioxygenase 2, 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase 2, DHK-MTPene dioxygenase 2, Acireductone dioxygenase (Fe(2+)-requiring) 2, ARD' 2, Fe-ARD 2, Acireductone dioxygenase (Ni(2+)-requiring) 2, ARD 2, Ni-ARD 2.
What is the protein family that this protein belongs to?
Belongs to the acireductone dioxygenase (ARD) family.
Protein: NPT1_YEAST
Sequence: MSEPVIKSLLDTDMYKITMHAAVFTNFPDVTVTYKYTNRSSQLTFNKEAINWLKEQFSYLGNLRFTEEEIEYLKQEIPYLPSAYIKYISSSNYKLHPEEQISFTSEEIEGKPTHYKLKILVSGSWKDTILYEIPLLSLISEAYFKFVDIDWDYENQLEQAEKKAETLFDNGIRFSEFGTRRRRSLKAQDLIMQGIMKAVNGNPDRNKSLLLGTSNILFAKKYGVKPIGTVAHEWVMGVASISEDYLHANKNAMDCWINTFGAKNAGLALTDTFGTDDFLKSFRPPYSDAYVGVRQDSGDPVEYTKKISHHYHDVLKLPKFSKIICYSDSLNVEKAITYSHAAKENGMLATFGIGTNFTNDFRKKSEPQVKSEPLNIVIKLLEVNGNHAIKISDNLGKNMGDPATVKRVKEELGYTERSWSGDNEAHRWT
What is the function of this protein?
Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate (PubMed:9521740).  Essential for growth under anaerobic conditions (PubMed:12062417).
What are the official names of this protein?
Nicotinate phosphoribosyltransferase, NAPRTase.
What is the protein family that this protein belongs to?
Belongs to the NAPRTase family.
What are the subcellular locations of this protein?
Cytoplasm. Nucleus.
Protein: AROC_CYTH3
Sequence: MSNTYGTIFRITTFGESHGNAVGVIVDGCPPNIEIDEAFIQSEMARRKPGQSKIVTQRQEDDEIEILSGVFEGKSTGTPIAMMVRNADQRSKDYSHIADRFRPSHADYTYQEKYGFRDYRGGGRSSARETLARVAAGALAKMILAKVNIKIQAYVSQVGPLKLTTDYKALNIPNAETNIIRCPDDAVAAKMIEFIDETRKNKDTIGGVVSCVIEGVPVGLGEPVFDKLHAELGKAMLSINAVKGFEYGSGFEGVEQFGSQHNDKFYADEQGNVRTQTNNSGGIQGGISNGEDIYFRVAFKPVATIMIDQESINDKGETVTVSGKGRHDPCVVPRAVPIVEAMAAIVMVDFYLRNKAIRLD
What is the function of this protein?
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis.  This reaction introduces a second double bond into the aromatic ring system.
What are the official names of this protein?
Chorismate synthase, CS, 5-enolpyruvylshikimate-3-phosphate phospholyase.
What is the protein family that this protein belongs to?
Belongs to the chorismate synthase family.
Protein: COBS_VIBPA
Sequence: MSESKSSRQATLRYQMELFLLAVSFFSRLPVPSDLPYSEERMNQAGRYFALVGVILGVLCALVFYFTQLIFPDSVAIVLTMAFSLLLTGAFHEDGLTDMADGIGGGMTVERRLSIMKDSRIGTYGAATLVMALLAKFVLWSELVHLPDFWLVIVVAYTTSRALAATLIYDMPYVSDSDTSKSKPLASKQSSSEVAILLFTAGVASLFLGVIQTSFIVIVLFAFRFAFKRWLTKRIGGFTGDCLGAAQQLSELLVYLTLIAFYQNI
What is the function of this protein?
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin).  Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
What are the official names of this protein?
Adenosylcobinamide-GDP ribazoletransferase, Cobalamin synthase, Cobalamin-5'-phosphate synthase.
What is the protein family that this protein belongs to?
Belongs to the CobS family.
What are the subcellular locations of this protein?
Cell inner membrane; Multi-pass membrane protein.
Protein: PIG12_CLAP2
Sequence: MKMGMAKHSPRNKEYLCLTICGYRKEGMSEEAYRNHMVNVSAPMTKDLMVKYGIRRWTQIHNQNATRALMAELFDPQMCRLADFDCFSQVVFDNIEDYKRMKQDPWYKKHLMHDHEMFADTKRSMMTIGWIKEFVVDGKAV
What is the function of this protein?
Decarboxylase; part of the ergochrome gene cluster responsible for the typical purple-black color of the ergot sclerotia (PubMed:28955461).  The ergochrome gene cluster produces several ergot pigments including the yellow ergochrome secalonic acid and its derivatives, as well as the red anthraquinones endocrocin and clavorubin (PubMed:28955461).  The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) CPUR_05437 (By similarity).  The atrochrysone carboxyl ACP thioesterase CPUR_05436 then breaks the thioester bond and releases the atrochrysone carboxylic acid from CPUR_05437 (By similarity).  The decarboxylase CPUR_05434 then catalyzes the concerted decarboxylation-elimination required to convert atochrysone carboxylic acid into emodin anthrone, which is further oxidized to emodin by the anthrone oxygenase CPUR_05435 (By similarity).  Emodin is further modified to yield monodictyphenone via several steps involving CPUR_05427, CPUR_05428, CPUR_05429 and CPUR_05430 (By similarity).  The short chain dehydrogenase/reductase CPUR_05418 then catalyzes the C-5 ketoreduction to give the xanthone skeleton of the monomeric units (PubMed:32105084).  Ergochromes formation requires further dimerization steps of different xanthone units, probably catalyzed by the cytochrome P450 monooxygenase CPUR_05419 (PubMed:28955461).  CPUR_05425, CPUR_05426 and CPUR_05431 are unique to Claviceps, thus it is likely that they are involved in further modification of xanthone units or in their dimerization (PubMed:28955461).  The yellow ergochromes and the red anthraquinone pigments endocrocin and clavorubin are products from the same PKS derived precursors and the latter are likely shunt products in the pathway of xanthone biosynthesis (PubMed:28955461).  It is proposed that atrochrysone carboxylic acid released from the PKS CPUR_05437 can also be converted to endocrocin anthrone which is further oxidized into endocrocin by CPUR_05435 (By similarity).  Endocrocin could be then modified to clavorubin, possibly by CPUR_05423 and CPUR_05431 (PubMed:28955461).  Clavorubin is the principal anthraquinone metabolite produced by the cluster with a much higher yield compared to endocrocin (PubMed:28955461).
What are the official names of this protein?
Decarboxylase CPUR_05434, Ergochrome gene cluster protein CPUR_05434.
What is the protein family that this protein belongs to?
Belongs to the tpcK family.
Protein: AROC_STRSV
Sequence: MRYLTAGESHGPRLTAIIEGVPAGLPLTADYINAELKRRQGGYGRGARMKIESDQVEITSGVRHGLTMGGPITLNVTNLDHQKWQEIMSAADVDEKKKGLRKITKPRPGHADLVGGMKYRFDDLRNSLERSSARETTMRVAVGAVAKRLLEEIGVEVASHIVTFGGIDINVPNNLTVGEIKERAAQSEVSIVNPDREEEIKAYIDQIKKDGDTIGGVIETVVGGVPVGLGSYVQWDKKLDAKIAQGVVSINAFKGVEFGVGFEAGRLKGSQVMDEILWSEEDGFTRRTNNLGGFEGGMTNGQPIVVRGVMKPIPTLYKPLMSVDIETHEPYKATVERSDPTALPAAGVVMESVVATVLATEVLEKFSSDNLEELKDAVARHREFVKNF
What is the function of this protein?
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis.  This reaction introduces a second double bond into the aromatic ring system.
What are the official names of this protein?
Chorismate synthase, CS, 5-enolpyruvylshikimate-3-phosphate phospholyase.
What is the protein family that this protein belongs to?
Belongs to the chorismate synthase family.
Protein: TIG_CARHZ
Sequence: MKVTKETLEKSRVELTIEVEAEEVSKAYEKAYKKIAQKVVIPGFRKGKAPRVLVERHVGKEYILEEALDELLPESYVKAVNEAGIEPVDKPEVSLVSYGVNEPLVYKAVVDVKPEVELGQYTGLEVTKMPVEVTDEEVEKELEYLQNRYAKLITVEDGEAKFGDIVVIDFAGKMNGEPLEGGSADNYRLELGSKVFIPGFEEQIVGMKPGETKEINVTFPEDYQKEDLAGKPAVFTVTLKEIKRKELAPLDDEFAKDVSEFSTLAELKEDLKKKIAQTKENISREKMEAEVVEKAVDNANVEIPASMVNHEVEHILHHFEEELKYRRLTLEQYLNYQKKTLDELKEELKPRAERNVKTELVLEAIAKKEGITATDEEIDKELGKIAELYQQPVEEIKKLFAQRMDDLAYSIVRRKTIDFLVENAKAV
What is the function of this protein?
Involved in protein export.  Acts as a chaperone by maintaining the newly synthesized protein in an open conformation.  Functions as a peptidyl-prolyl cis-trans isomerase.
What are the official names of this protein?
Trigger factor, TF, PPIase.
What is the protein family that this protein belongs to?
Belongs to the FKBP-type PPIase family. Tig subfamily.
What are the subcellular locations of this protein?
Cytoplasm. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm.
Protein: GP_BUNSH
Sequence: MICILILFAVTAASPVYQRCFQDGAIVKQNPSKEAVTEVCLKDDVSMIKTEARYIKNATGVFSNNVAIRKWLVSDWHDCRPKKITGGHINVIEVGDDLSLHTESYVCSADCTIGVDKETAQVRLQTDTTNHFEIAGTIVKSGWFKSTTYITLDQTCEHLKVSCGPKSIQFHACFNQHMSCVRFLHRTILPGSIANSICQNIEIIILVTLTLLIFILLSVLSKTYICYLLMPVFIPIAYAYGIIYNKSCKKCKLCGLVYHPFTECGTHCVCGARYDTSDRMKLHRASGLCPGYKSLRAARVMCKSKGPASILSVITAILILTFVTPINSMVVGESKEVFELEQLPDDMLDMALRINFYYFVCIMNYAVTWGLIIIGLLIGLLFKKYQHRFSNLYAMYCEECDMYHDRSGLKRNGDFTNKCRQCTCGQYEDATGLMTHRKTYNCLVRYKAKWVMNFLIAYMLLTLIKDSAIVVQAAGTDFTTCLETENINWNCTGPFLNLGNCQKQQKKEPYANIATQLKGLQAISVLDMPMIASIPEDIAGALRYIEEKETFHVQLTAEYAMLSRYCDYYAQFSDNSGYSQTTWRVYLRSHDFDACILYPNQHFCRCVKRGDKCSSSNGDFANEMKNYYSGKQNKFDKDLNLALMALHHAFRGTSSAYIATMLSKKSNDDLIAYTNKIKEKFPGNALLKAIVDYIAYMKSLSEMSSFKYDEFWDDLLYKSAPTKAPSLSRGSEPSYNFKLVVSSRSIKSCKNVKSVVCLSPRSGVSYDSIIACGDPNGPSVYRKPSDGVFQSNADQSTYCLADSHCLEDFEVVSQEELDAIKKSKCWEAEYPDVKLSKLTDGVKSCRMKDSGNCNVAANRWPIIQCENDKFYYSELQKDYDKTQDIGHFCLSPGCSTVRFPINPKHISNCNWQVSRSSIAKIDVHNIEDIDQYRKAITQKLQTSLSLFKYAKTKNLPHIKPIYKYITIEGTETAEGIESAYIESEIPALAGTSIGFKITSKEGKHLLDVIGYVKSASCSSIYTKLYTTGPTSGINTKHDELCTGPCPAKINHQTGWLTFAKERTSSWGCEEFGCLAISDGCVFGSCQDIIRDELTVYRKETDEVTDVELCLTFSDKTYCTNLNPITPIITDLFEVQFKTVETYSLPRIVAIQNHEIKIGQVNDLGVYSKGCGNVQKVNGTVYGNGVPKFDYLCHLASRKEVIVRKCFDNDYQACKFLQSPASYRLEEDSGTVTVIDYKKILGTIKMKAILGDVKYKTFADNVDMTAEGSCTGCINCFENIHCELTLHTTIEASCPIVSTCTVFHDRILVTPNEHKYALKVVCTEKPGNTLTIRICNTKVEASLALVDAKPILELAPVDQTAYIREKDERCKTWMCRVRDEGLQVILEPFKNLFGSYIGIFYTFIISIIALLIIIYIVLPICFKLRDTLRKHEDAYKREMKIR
What is the function of this protein?
Glycoprotein C and Glycoprotein N interact with each other and are present at the surface of the virion.  They are able to attach the virion to a cell receptor and to promote fusion of membranes after endocytosis of the virion (By similarity).
What are the official names of this protein?
Envelopment polyprotein, M polyprotein.
What is the protein family that this protein belongs to?
Belongs to the orthobunyavirus envelope glycoprotein family.
What are the subcellular locations of this protein?
[Glycoprotein C]: Virion membrane; Single-pass type I membrane protein. Host Golgi apparatus membrane; Single-pass type I membrane protein. Host endoplasmic reticulum membrane; Single-pass type I membrane protein. Note=Glycoprotein C alone is retained in the membrane of the endoplasmic reticulum, but not transported to the Golgi. Coexpression of Glycoprotein C and Glycoprotein N results in efficient transport of Glycoprotein C to the Golgi complex, indicating that their interaction is essential for proper targeting to this organelle, where virion budding occurs (By similarity). SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane; Single-pass type I membrane protein. Host Golgi apparatus membrane; Single-pass type I membrane protein. Note=Glycoprotein N is retained in the Golgi complex through a Golgi retention signal, which resides in the Glycoprotein N transmembrane region. SUBCELLULAR LOCATION: [Non-structural protein M]: Host Golgi apparatus membrane; Multi-pass membrane protein.
Protein: CYB_PYTRG
Sequence: MPHHYILTLFGLLPVATNISTWWNFGSMLLTCLMLQVLTGFFLAVHYTANINLAFSSIIHITRDVPYGWLMQNLHAIGASMFFICIYIHIARGLYYGSHLNKETWMSGITLLITLIATAFFGYVLPGGQMSFRAATGITNLLTAVPYLGATMTTWLWGGFAINDPTLTRFFALHFILPFAIISLSSLHIILLHEEGSSNPLGTNPDIDKIPFHPYHSYKDLLLLTLMLLTLMITVSFFPDIFNDPDNFSKANPLVTPQHIKPEWYFLFAYGILRSIPNKLGGALALVMSIMILLTAPLTHTAHLRPMTFRPLSQLMFWTLISTFITITWAATKPVEPPYIIISQTTATLYFTFFISTPILGWIENKMMNSC
What is the function of this protein?
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain.  The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c.  Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
What are the official names of this protein?
Cytochrome b, Complex III subunit 3, Complex III subunit III, Cytochrome b-c1 complex subunit 3, Ubiquinol-cytochrome-c reductase complex cytochrome b subunit.
What is the protein family that this protein belongs to?
Belongs to the cytochrome b family.
What are the subcellular locations of this protein?
Mitochondrion inner membrane; Multi-pass membrane protein.
Protein: CH602_PROMP
Sequence: MAKRIIYNEQARRALERGIDILAESVAVTLGPKGRNVVLEKKFGAPQIINDGVTIAKEIELEDHIENTGVALIRQAASKTNDAAGDGTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKATEFLVGKIEENSKPISDSTAIAQCGTIAAGNDEEVGEMIANAMDKVGKEGVISLEEGKSMTTELEVTEGMRFDKGYISPYFATDTERMEAVLDEPYILLTDKKIALVQDLVPVLEQIAKTGKPLVIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDMAVLTNGQLITEDAGLKLENATLEMLGTGRRITINKETTTIVAEGNEKAVTARCDQIKKQMDETDSSYDKEKLQERLAKLAGGVAVIKVGAATETEMKDKKLRLEDAINATKAAVEEGIVPGGGTTLAHLAPILKEWADKALSGEELIGANIVEASLTSPLMRIAENAGSNGAVIAENVKSKPFNDGFNAATGDYVDMSAAGIVDPAKVTRSGLQNAASIAGMVLTTECIVADLPEKKDAAPAGAPGMGGDFDY
What is the function of this protein?
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding.  The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
What are the official names of this protein?
Chaperonin GroEL 2, 60 kDa chaperonin 2, Chaperonin-60 2, Cpn60 2.
What is the protein family that this protein belongs to?
Belongs to the chaperonin (HSP60) family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: GH101_RENSM
Sequence: MPFRGRRRQSALRGLSLAATFCLAAGSSGISGALFATPAQADPLPTAAGLSINSANLTVEVSADFPQALSYTETSSAKHLSGARTLASSITINGTDQPVKVSSQKADAQTVNYLITPNNLAGVSLDAQLRVEGMTLTFKISKIKDTAENRVNNLQIKNQDLVTVSSQEPGATVASAVVSVDRAVSGDTITNLSSTTALDPTAKRSMLAIAATDQLAAGFETNSLYDSGNTIGPSDQGKFWRQALADGTGADGKPAVKMAVSSGAWLYRSAGSDQTEELPWSKVVISGDANADGKVDWQDGAIAYRSIESKPAGGDDVKNRVVTHIPFNFASQATHPFLRTLDDVKHIALATDGLGQMALEKGYTSEGHDSANSDFGGNFNERAGGLTDFNAMLSGGSAYGATFGVHINNTEAYPEANSFSNDFVDPTKKGWNWLDQSFYIDQQRDILSGSQQQRIDQLRSEAGPNLTMAYVDVYYESGWKSYRLQKGLKDAGFSVASEFATAMPANNTWSHWANDEKHGGSNNIKAGTQILRFVDNSQRDIWNPDPLLGTSHIVEWEGWTNQNDYNAFLKNIWGNNLPVKFLQQQQITSWKSRSVDLTGGLKVTGTSLADRVISQQGVPVLKGSNYLLPWSAAPVSFGSGAVNDTTQNKLYHYSADGGTSTWQLTPQFATASSLQIYKLTDYGRELIGSVPVVNGSVTLTAEANQAYVLVADASVTTVPADPSYGAGSKVKDPGFNSAGLKDWNATGGAAVERTAQGLLVAKLGQGSSAISQTLGSLDPGSYSIGAWVEIEPTTLTVTPAGGAPISVTVDQSGAENFVASDEKRGTYFQRLRVLVDIANAGAPQLSISAPAGEAAVRIDDVRVVKANKVPTTGILSENFENTDQGWLPFIKGDAGGQTDPRTHIAKLNAPYTQKGWNGKTTSDVLDDTYSLHSHEENQGLVYRTSNYTLPLQAGRQYRVSFDYQASLANQYTWVSGYDSGKNPVQTASTAIPVATDTTRWSQTLSAGSCGPAWVGLQRTGSSGGAEFSMDNLLVEDLGPSAETPACASLSLTSGQDVIEQGQTNTFSASFSSSEAQSIAGLSVALDLPAGWTASAATPATAATLPAGGSLETQWKVQVPADADGDYTIKAKASYQTTVDPIGSRSATTETAVYTLPKPPTKDTYASDMQWIGTPSNGWGPVEKDQANGEQAQGDGPPLKLGGVTYPKGLGAHAASSIRYYVGSQCSAFTAVIGIDDFQKLKGQAVFSVLGDGNSLYTSPVMKGGAAAQTITVPLNGAKYVDLKVAISGANNGNAWSDWANAKFLCSAPVAPITLQPTLSVPTDSLQPGSAFTVRVDQLKSGSTAKAELHSDPIDLGSVQANNDGVASFQVTLAQDAPLGNHQIVVTGTDKNGLAATGTVDAQIKAANPNPGTGSNPGTGSNPGTDPGTGSAGGNSSGGGANGSGANGTYVNGSGGSFGNGAGMDAKTGSNSASSLAETGFSGLVLPLGIGLMLLLIGAAAIIVRRHRHS
What is the function of this protein?
Probably involved in the breakdown of mucin-type O-linked glycans.  Specifically removes the T-antigen disaccharide (Gal-beta-1,3-GalNAc-alpha) from extracellular host glycoproteins.
What are the official names of this protein?
Putative endo-alpha-N-acetylgalactosaminidase.
What is the protein family that this protein belongs to?
Belongs to the glycosyl hydrolase 101 family. A subfamily.
What are the subcellular locations of this protein?
Secreted, cell wall; Peptidoglycan- anchor.
Protein: UREG_BORPE
Sequence: MHDISSLTTRTKALPPLRVGVGGPVGSGKTTLLEMVCKAMYPQFDLIAITNDIYTKEDQRLLTLSGALPPERILGVETGGCPHTAIREDASINLIAIDQMLEQFPDADIVFVESGGDNLAATFSPELSDLTLYIIDVASGEKIPRKGGPGITKSDLFIINKTDLAPYVGADLAVMEADTRRMRGDKPFVMCNLKTGDGLDQVIAFLKTEGLFRG
What is the function of this protein?
Facilitates the functional incorporation of the urease nickel metallocenter.  This process requires GTP hydrolysis, probably effectuated by UreG.
What are the official names of this protein?
Urease accessory protein UreG.
What is the protein family that this protein belongs to?
Belongs to the SIMIBI class G3E GTPase family. UreG subfamily.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: HSLU_PSEAB
Sequence: MSMTPREIVHELNRHIIGQDDAKRAVAIALRNRWRRMQLPAELRAEVTPKNILMIGPTGVGKTEIARRLARLANAPFIKVEATKFTEVGYVGRDVESIIRDLADAAVKMLREQEIQKVKYRAEDAAEERILDALLPAARPAMGFGDEPAREDSNTRQLFRKRLREGQLDDKEIDIEVADNPAGVEIMAPPGMEEMTNQLQNLFSGMSKGKKKTRKLKVAEALKLIRDEEAVRLVNEEELKARALEAVEQHGIVFIDEIDKIAKRANAGGADVSREGVQRDLLPLIEGCTVNTKLGMVKTDHILFIASGAFHLSKPSDLVPELQGRLPIRVELKALSPNDFERILTEPHASLTEQYRELLKTEGLAIEFAEDGIKRLAEIAWQVNEKTENIGARRLHTLLERLLEEVSFSAADLASEHSDKPILIDAGYVNSHLGELAEDEDLSRYIL
What is the function of this protein?
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity.  The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV.  HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
What are the official names of this protein?
ATP-dependent protease ATPase subunit HslU, Unfoldase HslU.
What is the protein family that this protein belongs to?
Belongs to the ClpX chaperone family. HslU subfamily.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: SODC_PAUKA
Sequence: MVKGVAVLSSSEGVSGTIYFTQEGDGPTTVTGNVSGLKPGPHGFHVHALGDTTNGCLSTGPHFNPAGKEHGAPDDEVRHAGDLGNVTVGEDGTAAFTIVDKQIPLTGPHSIIGRAVVVHADPDDLGKGGHELSKTTGNTGGRVACGINGLQG
What is the function of this protein?
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
What are the official names of this protein?
Superoxide dismutase [Cu-Zn].
What is the protein family that this protein belongs to?
Belongs to the Cu-Zn superoxide dismutase family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: SSRP_DESVV
Sequence: MSKKAPGANVIAQNKKARHIYELSDNHEAGISLTGSEVKSLRAGHVNFRDSYVDFRNGEAFLVGLHIAPYDNAGYAQHDPDRDRKLLLHAHEIENLARSVEQKGYTVVPTKLYFARGKVKVDIAVGRGKKLHDQREDLKRRAEDRDTQRELARF
What is the function of this protein?
Required for rescue of stalled ribosomes mediated by trans-translation.  Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes.  tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB.  tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame.  During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA.  The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation.  The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
What are the official names of this protein?
SsrA-binding protein, Small protein B.
What is the protein family that this protein belongs to?
Belongs to the SmpB family.
What are the subcellular locations of this protein?
Cytoplasm. Note=The tmRNA-SmpB complex associates with stalled 70S ribosomes.