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Database: UniProt
Entry: TYCC_BREPA
LinkDB: TYCC_BREPA
Original site: TYCC_BREPA 
ID   TYCC_BREPA              Reviewed;        6486 AA.
AC   O30409;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   19-JAN-2010, entry version 79.
DE   RecName: Full=Tyrocidine synthetase 3;
DE   AltName: Full=Tyrocidine synthetase III;
DE   Includes:
DE     RecName: Full=ATP-dependent asparagine adenylase;
DE              Short=AsnA;
DE     AltName: Full=Asparagine activase;
DE   Includes:
DE     RecName: Full=ATP-dependent glutamine adenylase;
DE              Short=GlnA;
DE     AltName: Full=Glutamine activase;
DE   Includes:
DE     RecName: Full=ATP-dependent tyrosine adenylase;
DE              Short=TyrA;
DE     AltName: Full=Tyrosine activase;
DE   Includes:
DE     RecName: Full=ATP-dependent valine adenylase;
DE              Short=ValA;
DE     AltName: Full=Valine activase;
DE   Includes:
DE     RecName: Full=ATP-dependent ornithine adenylase;
DE              Short=OrnA;
DE     AltName: Full=Ornithine activase;
DE   Includes:
DE     RecName: Full=ATP-dependent leucine adenylase;
DE              Short=LeuA;
DE     AltName: Full=Leucine activase;
GN   Name=tycC;
OS   Brevibacillus parabrevis.
OC   Bacteria; Firmicutes; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=54914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8185 / IAM 1031 / IFO 3331 / NCDO 717 / NCIB 8598;
RX   MEDLINE=98012987; PubMed=9352938;
RA   Mootz H.D., Marahiel M.A.;
RT   "The tyrocidine biosynthesis operon of Bacillus brevis: complete
RT   nucleotide sequence and biochemical characterization of functional
RT   internal adenylation domains.";
RL   J. Bacteriol. 179:6843-6850(1997).
RN   [2]
RP   STRUCTURE BY NMR OF 3032-3113.
RX   MEDLINE=20264307; PubMed=10801488; DOI=10.1016/S0969-2126(00)00120-9;
RA   Weber T., Baumgartner R., Renner C., Marahiel M.A., Holak T.A.;
RT   "Solution structure of PCP, a prototype for the peptidyl carrier
RT   domains of modular peptide synthetases.";
RL   Structure 8:407-418(2000).
CC   -!- FUNCTION: Incorporates six amino acids (for tyrocidine A, Asn,
CC       Gln, Tyr, Val, Orn, and Leu) in their L-configuration into the
CC       peptide product.
CC   -!- COFACTOR: Binds 6 phosphopantetheines covalently (By similarity).
CC   -!- PATHWAY: Antibiotic biosynthesis; tyrocidine biosynthesis.
CC   -!- SUBUNIT: Large multienzyme complex of tycA, tycB and tycC.
CC   -!- DOMAIN: Consists of six modules, and harbors a putative
CC       thioesterase domain at its C-terminal end. Each module
CC       incorporates one amino acid into the peptide product and can be
CC       further subdivided into domains responsible for substrate
CC       adenylation, thiolation, condensation (not for the initiation
CC       module), and epimerization (optional), and N methylation
CC       (optional).
CC   -!- MISCELLANEOUS: Tyrocidine is a mixture of four cyclic
CC       decapeptides, tyrocidine A (D-Phe-Pro-Phe-D-Phe-Asn-Gln-Tyr-Val-
CC       Orn-Leu), B, C, and D, in which Phe, at positions 3, 4, and Tyr
CC       residues are gradually replaced by Trp, depending on the relative
CC       concentrations of these amino acids in the growth medium.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family.
CC   -!- SIMILARITY: Contains 6 acyl carrier domains.
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DR   EMBL; AF004835; AAC45930.1; -; Genomic_DNA.
DR   PDB; 1DNY; NMR; -; A=3032-3113.
DR   PDB; 2GDW; NMR; -; A=3033-3113.
DR   PDB; 2GDX; NMR; -; A=3033-3113.
DR   PDB; 2GDY; NMR; -; A=3033-3113.
DR   PDB; 2GE1; Model; -; B=3033-3113.
DR   PDB; 2JGP; X-ray; 1.85 A; A=5116-5633.
DR   PDB; 2K2Q; NMR; -; A=3033-3112.
DR   PDBsum; 1DNY; -.
DR   PDBsum; 2GDW; -.
DR   PDBsum; 2GDX; -.
DR   PDBsum; 2GDY; -.
DR   PDBsum; 2GE1; -.
DR   PDBsum; 2JGP; -.
DR   PDBsum; 2K2Q; -.
DR   DIP; DIP-29492N; -.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR006163; Phsphopanteth_bd.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR006162; PPantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   Pfam; PF00501; AMP-binding; 6.
DR   Pfam; PF00668; Condensation; 6.
DR   Pfam; PF00550; PP-binding; 6.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00823; PKS_PP; 6.
DR   PROSITE; PS50075; ACP_DOMAIN; 6.
DR   PROSITE; PS00455; AMP_BINDING; 6.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 6.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic biosynthesis; Ligase; Multifunctional enzyme;
KW   Phosphopantetheine; Repeat.
FT   CHAIN         1   6486       Tyrocidine synthetase 3.
FT                                /FTId=PRO_0000193095.
FT   DOMAIN      970   1037       Acyl carrier 1.
FT   DOMAIN     2007   2074       Acyl carrier 2.
FT   DOMAIN     3045   3112       Acyl carrier 3.
FT   DOMAIN     4080   4147       Acyl carrier 4.
FT   DOMAIN     5124   5191       Acyl carrier 5.
FT   DOMAIN     6167   6234       Acyl carrier 6.
FT   REGION      466   1038       Domain 1 (asparagine-activating).
FT   REGION     1521   2070       Domain 2 (glutamine-activating).
FT   REGION     2536   3113       Domain 3 (tyrosine-activating).
FT   REGION     3590   4149       Domain 4 (valine-activating).
FT   REGION     4606   5203       Domain 5 (ornithine-activating).
FT   REGION     5658   6245       Domain 6 (leucine-activating).
FT   MOD_RES    1000   1000       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
FT   MOD_RES    2037   2037       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
FT   MOD_RES    3075   3075       O-(pantetheine 4'-phosphoryl)serine.
FT   MOD_RES    4110   4110       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
FT   MOD_RES    5154   5154       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
FT   MOD_RES    6197   6197       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
FT   HELIX      3044   3057
FT   HELIX      3076   3088
FT   HELIX      3095   3100
FT   HELIX      3104   3112
FT   HELIX      5123   5136
FT   TURN       5147   5151
FT   HELIX      5154   5168
FT   HELIX      5174   5179
FT   HELIX      5183   5192
FT   STRAND     5208   5211
FT   HELIX      5214   5225
FT   TURN       5229   5232
FT   STRAND     5236   5242
FT   HELIX      5246   5259
FT   HELIX      5261   5264
FT   STRAND     5265   5270
FT   STRAND     5273   5278
FT   STRAND     5287   5290
FT   HELIX      5293   5302
FT   STRAND     5315   5323
FT   STRAND     5326   5334
FT   HELIX      5335   5337
FT   HELIX      5340   5354
FT   HELIX      5366   5376
FT   HELIX      5380   5392
FT   STRAND     5415   5422
FT   HELIX      5425   5438
FT   HELIX      5442   5458
FT   STRAND     5463   5469
FT   HELIX      5475   5477
FT   STRAND     5486   5492
FT   HELIX      5500   5516
FT   HELIX      5522   5528
FT   STRAND     5542   5548
FT   STRAND     5558   5564
FT   STRAND     5575   5584
FT   STRAND     5589   5596
FT   TURN       5597   5599
FT   HELIX      5602   5621
FT   HELIX      5627   5629
SQ   SEQUENCE   6486 AA;  724033 MW;  4934900AF07DF786 CRC64;
     MKKQENIAKI YPLTPLQEGM LFHAVTDTGS SAYCLQMSAT IEGDFHLPLF EKSLNKLVEN
     YEVLRTAFVY QNMQRPRQVV FKERKVTVPC ENIAHLPSAE QDAYIQAYTK QHHAFDLTKD
     NLMKAAIFQT AENKYRLVWA FHHIIVDGWT LGVLLHKLLT YYAALRKGEP IPREATKPYS
     EYIKWLDKQN KDEALAYWQN YLAGYDHQAA FPKKKLGTEA SRYEHVEAMF TIAPEKTQQL
     IQIANQNQAT MSSVFQALWG ILASTYKNAD DVVFGSVVSG RPPQIQGIES MVGLFINTIP
     TRVQTNKQQT FSELLQTVQK QALASATYDF APLYEIQSTT VLKQELIDHL VTFENYPDHS
     MKHLEESLGF QFTVESGDEQ TSYDLNVVVA LAPSNELYVK LSYNAAVYES SFVNRIEGHL
     RTVIDQVIGN PHVHLHEIGI ITEEEKQQLL VAYNDTAAEY PRDKTIFELI AEQASRTPAK
     AAVVCGEDTL TYQELMERSA QLANALREKG IASGSIVSIM AEHSLELIVA IMAVLRSGAA
     YLPIDPEYPQ DRIQYLLDDS QTTLLLTQSH LQPNIRFAGS VLYLDDRSLY EGGSTSFAPE
     SKPDDLAYMI YTSGSTGNPK GAMITHQGLV NYIWWANKVY VQGEAVDFPL YSSISFDLTV
     TSIFTPLLSG NTIHVYRGAD KVQVILDIIK DNKVGIIKLT PTHLKLIEHI DGKASSIRRF
     IVGGENLPTK LAKQIYDHFG ENVQIFNEYG PTETVVGCMI YLYDPQTTTQ ESVPIGVPAD
     NVQLYLLDAS MQPVPVGSLG EMYIAGDGVA KGYFNRPELT KEKFIDNPFR PGTKMYRTGD
     LAKWLPDGNM EYAGRMDYQV KIRGHRIEMG EIETRLTQHE AVKEAVVIVE KDESGQNVLY
     AYLVSERELT VAELREFLGR TLPSYMIPSF FIRLAEIPLT ANGKVERKKL PKPAGAVVTG
     TAYAAPQNEI EAKLAEIWQQ VLGISQVGIH DDFFDLGGHS LKAMTVVFQV SKALEVELPV
     KALFEHPTVA ELARFLSRSE KTEYTAIQPV AAQEFYPVSS AQKRMYILQQ FEGNGISYNI
     SGAILLEGKL DYARFASAVQ QLAERHEALR TSFHRIDGEP VQKVHEEVEV PLFMLEAPED
     QAEKIMREFV RPFDLGVAPL MRTGLLKLGK DRHLFLLDMH HIISDGVSSQ ILLREFAELY
     QGADLQPLSL QYKDFAAWQN ELFQTEAYKK QEQHWLNTFA DEIPLLNLPT DYPRPSVQSF
     AGDLVLFAAG KELLERLQQV ASETGTTLYM ILLAAYNVLL SKYTGQEDII VGTPVAGRSH
     ADVENIMGIF VNTLALRNQP ASSKTFAQFL QEVKQNALAA YDHQDYPFEE LVEKLAIQRD
     ISRNPLFDTL FSLENANQQS LAIAELTASP YELFNKISKF DLALNASESP ADIQFQLTFA
     TKLFKKETVE RMARHYLEIL RWISEQPTAS LADIDMMTEA EKRTLLLNVN DTFVERTAAT
     ALHQLVEEQA ARTPDEVAVV YEEYALTYRE LNARANQLAR LLRSHGTGPD TLIGIMVDRS
     PGMVVGMLAV LKAGGAYTPI DPSYPPERIQ YMLSDSQAPI LLTQRHLQEL AAYQGEIIDV
     DEEAIYTGAD TNLDNVAGKD DLAYVIYTSG STGNPKGVMI SHQAICNHML WMRETFPLTT
     EDAVLQKTPF SFDASVWEFY LPLITGGQLV LAKPDGHRDI AYMTRLIRDE KITTLQMVPS
     LLDLVMTDPG WSACTSLQRV FCGGEALTPA LVSRFYETQQ AQLINLYGPT ETTIDATYWP
     CPRQQEYSAI PIGKPIDNVR LYVVNASNQL QPVGVAGELC IAGDGLARGY WQREELTKAS
     FVDNPFEPGG TMYRTGDMVR YLPDGHIEYL GRIDHQVKIR GHRIELGEIE ATLLQHEAVK
     AVVVMARQDG KGQNSLYAYV VAEQDIQTAE LRTYLSATLP AYMVPSAFVF LEQLPLSANG
     KVDRKALPQP EDAAASAAVY VAPRNEWEAK LAAIWESVLG VEPIGVHDHF FELGGHSLKA
     MHVISLLQRS FQVDVPLKVL FESPTIAGLA PLVAAARKGT YTAIPPVEKQ EYYPVSAAQK
     RMFILQQMEG AGISYNMPGF MYLDGKLDTE RLQQALKSLV QRHESLRTSF HSVQGETVQR
     VHDDVDLAIS FGEATEAETR QIAEQFIQPF DLGTAPLLRA GLIKLAPERH LFMLDLHHIV
     VDGVSIGLLI EEFAQLYHGE ELPALRIQYK DFAKWQQDWF QTEEFAEQEA YWLNTFTGEI
     PVLNLPTDYP RPSVKSFAGD RFVFGSGTAL PKQLHQLAQE TGTTLYMVLL AAYNVLLSKY
     SRQEDIIVGA PTAGRSHAET ESIVGMFVNT LALRNEPAGG KTFRDFLAEV KINTLGAFEH
     QDYPLDELVD KLDMQRDLSR NPLFDTVFIL QNMEQKPFEM EQLTITPYSA EVKQAKFDLS
     LEAYEENAEI IFSLDYSTKL FSRETIEKIA THFIQILRAV IAEPEMPLSE ITMLTEAEKQ
     RLLVDFNGAH KDFPQNKTLQ ALFEEQAEKS PQATAVEISG QPLSYQELNE RANQLAATLR
     ERGVQPDQPV GIMANRSVEM VVGILAILKA GGAYVPIDPE YPEERVAYML TDCQARLVLT
     QKHLGAKLGS SVTAECLYLD DESNYGVHRS NLQPINTASD LAYIIYTSGT TGKPKGVMVE
     HRGIVNNVLW KKAEYQMKVG DRSLLSLSFA FDAFVLSFFT PVLSGATVVL AEDEEAKDPV
     SLKKLIAASR CTLMTGVPSL FQAILECSTP ADIRPLQTVT LGGEKITAQL VEKCKQLNPD
     LVIVNEYGPT ESSVVATWQR LAGPDAAITI GRPIANTSLY IVNQYHQLQP IGVVGEICIG
     GRGLARGYWN KPALTEEKFV SHPFAAGERM YKTGDLGKWL PDGTIEYIGR IDEQVKVRGY
     RIEIGEIESA LLAAEKLTAA VVVVYEDQLG QSALAAYFTA DEQLDVTKLW SHLSKRLPSY
     MIPAHFVQLD QLPLTPNGKV DKKALPKPEG KPVTEAQYVA PTNAVESKLA EIWERVLGVS
     GIGILDNFFQ IGGHSLKAMA VAAQVHREYQ VELPLKVLFA QPTIKALAQY VATSGKETYV
     PIEPAPLQEY YPVSSAQKRM YVLRQFADTG TVYNMPSALY IEGDLDRKRF EAAIHGLVER
     HESLRTSFHT VNGEPVQRVH EHVELNVQYA EVTEAQVEPT VESFVQAFDL TKAPLLRVGL
     FKLAAKRHLF LLDMHHIISD GVSAGIIMEE FSKLYRGEEL PALSVHYKDF AVWQSELFQS
     DVYTEHENYW LNAFSGDIPV LNLPADFSRP LTQSFEGDCV SFQADKALLD DLHKLAQESQ
     STLFMVLLAA YNVLLAKYSG QEDIVVGTPI AGRSHADIEN VLGMFVNTLA LRNYPVETKH
     FQAFLEEVKQ NTLQAYAHQD YPFEALVEKL DIQRDLSRNP LFDTMFILQN LDQKAYELDG
     LKLEAYPAQA GNAKFDLTLE AHEDETGIHF ALVYSTKLFQ RESIERMAGH FLQVLRQVVA
     DQATALREIS LLSEEERRIV TVDFNNTFAA YPRDLTIQEL FEQQAAKTPE HAAVVMDGQM
     LTYRELNEKA NQLAHVLRQN GVGKESIVGL LADRSLEMIT GIMGILKAGG AYLGLDPEHP
     SERLAYMLED GGVKVVLVQK HLLPLVGEGL MPIVLEEESL RPEDCGNPAI VNGASDLAYV
     MYTSGSTGKP KGVMVEHRNV TRLVMHTNYV QVRESDRMIQ TGAIGFDAMT FEIFGALLHG
     ASLYLVSKDV LLDAEKLGDF LRTNQITTMW LTSPLFNQLS QDNPAMFDSL RALIVGGEAL
     SPKHINRVKS ALPDLEIWNG YGPTENTTFS TCYLIEQHFE EQIPIGKPIA NSTAYIVDGN
     NQPQPIGVPG ELCVGGDGVA RGYVNKPELT AEKFVPNPFA PGETMYRTGD LARWLPDGTI
     EYLGRIDQQV KIRGYRIELG EIETVLSQQA QVKEAVVAVI EEANGQKALC AYFVPEQAVD
     AAELREAMSK QLPGYMVPAY YVQMEKLPLT ANGKVDRRAL PQPSGERTTG SAFVAAQNDT
     EAKLQQIWQE VLGIPAIGIH DNFFEIGGHS LKAMNVITQV HKTFQVELPL KALFATPTIH
     ELAAHIAESA FEQFETIQPV EPAAFYPVSF AQKRMYILHQ FEGSGISYNV PSVLVLEGKL
     DYDRFAAAIQ SLVKRHESLR TSFHSVNGEP LQRVHPDVEL PVRLLEATED QSESLIQELI
     QPFDLEIAPL FRVNLIKLGA ERHLFFMDMH HIISDGVSLA VIVEEIASLY AGKQLSDLRI
     QYKDFAVWQT KLAQSDRFQK QEDFWTRTFA GEIPLLNLPH DYPRPSVQSF DGDTVALGTG
     HHLLEQLRKL AAETGTTLFM VLLAAYHVLL SKYAGQEEIV VGTPIAGRSH ADVERIVGMF
     VNTLALKNTA AGSLSFRAFL EDVKQNALHA FEHQDYPFEH LVEKLQVRRD LSRNPLFDTM
     FSLGLAESAE GEVADLKVSP YPVNGHIAKF DLSLDAMEKQ DGLLVQFSYC TKLFAKETVD
     RLAAHYVQLL QTITADPDIE LARISVLSKA ETEHMLHSFL ATKTAYPTDK TFQKLFEEQV
     EKTPNEIAVL FGNEQLTYQE LNAKANQLAR VLRRKGVKPE STVGILVDRS LYMVIGMLAV
     LKAGGTFVPI DPDYPLERQA FMLEDSEAKL LLTLQKMNSQ VAFPYETFYL DTETVDQEET
     GNLEHVAQPE NVAYIIYTSG TTGKPKGVVI EHRSYANVAF AWKDEYHLDS FPVRLLQMAS
     FAFDVSTGDF ARALLTGGQL VICPNGVKMD PASLYETIRR HEITIFEATP ALIMPLMHYV
     YENELDMSQM KLLILGADSC PAEDFKTLLA RFGQKMRIIN SYGVTEACID TSYYEETDVT
     AIRSGTVPIG KPLPNMTMYV VDAHLNLQPV GVVGELCIGG AGVARGYLNR PELTEEKFVP
     NPFAPGERLY RTGDLAKWRA DGNVEFLGRN DHQVKIRGVR IELGEIETQL RKLDGITEAV
     VVAREDRGQE KELCAYVVAD HKLDTAELRA NLLKELPQAM IPAYFVTLDA LPLTANGKVD
     RRSLPAPDVT MLRTTEYVAP RSVWEARLAQ VWEQVLNVPQ VGALDDFFAL GGHSLRAMRV
     LSSMHNEYQV DIPLRILFEK PTIQELAAFI EETAKGNVFS IEPVQKQAYY PVSSAQKRMY
     ILDQFEGVGI SYNMPSTMLI EGKLERTRVE AAFQRLIARH ESLRTSFAVV NGEPVQNIHE
     DVPFALAYSE VTEQEARELV SSLVQPFDLE VAPLIRVSLL KIGEDRYVLF TDMHHSISDG
     VSSGILLAEW VQLYQGDVLP ELRIQYKDFA VWQQEFSQSA AFHKQEAYWL QTFADDIPVL
     NLPTDFTRPS TQSFAGDQCT IGAGKALTEG LHQLAQATGT TLYMVLLAAY NVLLAKYAGQ
     EDIIVGTPIT GRSHADLEPI VGMFVNTLAM RNKPQREKTF SEFLQEVKQN ALDAYGHQDY
     PFEELVEKLA IARDLSRNPL FDTVFTFQNS TEEVMTLPEC TLAPFMTDET GQHAKFDLTF
     SATEEREEMT IGVEYSTSLF TRETMERFSR HFLTIAASIV QNPHIRLGEI DMLLPEEKQQ
     ILAGFNDTAV SYALDKTLHQ LFEEQVDKTP DQAALLFSEQ SLTYSELNER ANRLARVLRA
     KGVGPDRLVA IMAERSPEMV IGILGILKAG GAYVPVDPGY PQERIQYLLE DSNAALLLSQ
     AHLLPLLAQV SSELPECLDL NAELDAGLSG SNLPAVNQPT DLAYVIYTSG TTGKPKGVMI
     PHQGIVNCLQ WRRDEYGFGP SDKALQVFSF AFDGFVASLF APLLGGATCV LPQEAAAKDP
     VALKKLMAAT EVTHYYGVPS LFQAILDCST TTDFNQLRCV TLGGEKLPVQ LVQKTKEKHP
     AIEINNEYGP TENSVVTTIS RSIEAGQAIT IGRPLANVQV YIVDEQHHLQ PIGVVGELCI
     GGAGLARGYL NKPELTAEKF VANPFRPGER MYKTGDLVKW RTDGTIEYIG RADEQVKVRG
     YRIEIGEIES AVLAYQGIDQ AVVVARDDDA TAGSYLCAYF VAATAVSVSG LRSHLAKELP
     AYMIPSYFVE LDQLPLSANG KVDRKALPKP QQSDATTREY VAPRNATEQQ LAAIWQEVLG
     VEPIGITDQF FELGGHSLKA TLLIAKVYEY MQIELPLNLI FQYPTIEKVA DFITHKRFES
     RYGTAILLNQ ETARNVFCFT PIGAQSVYYQ KLAAEIQGVS LYSFDFIQDD NRMEQYIAAI
     TAIDPSGPYT LMGYSSGGNL AFEVAKELEE RGYGVTDIIL FDSYWKDKAI ERTVAETEND
     IAQLFAEIGE NTEMFNMTQE DFQLYAANEF VKQSFVRKTV SYVMFHNNLV NTGMTTAAIH
     LIQSELEADE EAPVAAKWNE SAWANATQRL LTYSGHGIHS RMLAGDYASQ NASILQNILQ
     ELFILK
//
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Ontology (6)   
   GO (6)   
Chemical substance (1)   
   KEGG COMPOUND (1)   
DNA sequence (1)   
   EMBL (1)   
3D Structure (7)   
   PDB (7)   
Protein domain (25)   
   InterPro (9)   
   Pfam (4)   
   PROSITE (3)   
   Blocks (8)   
   PRINTS (1)   
Literature (2)   
   PubMed (2)   
All databases (42)   
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