ID U4UIU1_DENPD Unreviewed; 937 AA.
AC U4UIU1;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=D910_07195 {ECO:0000313|EMBL:ERL89835.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL89835.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL89835.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KB632191; ERL89835.1; -; Genomic_DNA.
DR MEROPS; M12.A04; -.
DR Proteomes; UP000030742; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF250; ADAM METALLOPROTEASE; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00023049};
KW Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT TRANSMEM 691..716
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 198..394
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 400..488
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 637..669
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 815..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..900
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 309..389
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 349..373
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 351..356
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 460..480
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 641..651
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 659..668
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 937 AA; 102207 MW; 438B2EE0C6D70040 CRC64;
MTHCFADEPL PAADFHRHSV IRPRMYHGRY GRHLPDTRTQ NGRHQQHIVV AMELGGAEAW
LDLTLNQRLL AKGFFHRRQV NGSRVVERPN EEEINHCHYV GKVRGRPESW AALSTCHGLQ
GVVFDGHELH YVEKGGPHHL LYAHSDLREH NKTCGYRGAA AGPAHAHSST DNRILRYKRS
SDSATVIRGP YNANRDSKYL ELVLVVDNRE FKELGENQRR VVDHCKTIAN IINGLYAPLN
IFIALVGVVV WSEHDEIIFS LNGDTTLANF LHYRKNKLLL EHPNDNAQLL TKFNFEQGVV
GKALKGPMCT FEYSGGVNND HSPVVGLVAT TIAHEMGHNF GMEHDTVDCQ CPEERCIMAP
SSSTVAPTHW SSCSLNYLLL AFTHGMDYCL KNKPEFLFDS PVCGNGFVEP GEQCDCGMSQ
HCENPCCDSA TCMLHANASC ATGECCDLST CKPKGAGTEC RSAQYECDLP EYCTGQSEFC
PPDIFKMDTE RCDEGRAFCY HGFCRTRTDQ CKLLWGDTGK SSDDQCYDMN TKGSRHGNCG
YNKFNESFAK CDRESVLCGM LHCKHLNERL EFGMESVAIL SHSFINKKGS IIPCRTAIVD
LGTNQIDPGM TPDGAKCGDG KMCVNQRCRD VLSLRKQSPH CDKDCHGNGW CNSLGHCHCK
DGFAPPLCEY PGPGGSEDSG PASDPNAHQG VVVAMFIIFL GVVPMVALTA ILLYYARYNL
KLSWPKAPTT ATYVEGGVAR KAGGFRGGVA ICRPALISTT NAEGIVRSHT ISHSIKSLVE
VAQQGQGRGL RLRAGQSLAA ARRVAAPCRP AQRVLRQLQG LQPDADEGGG ACGAGPRPLH
QQPPEPPRAE DQLVPAGXEL HLQRQGADLA AEERAQGAGA AGARRPGRRA QDRHQSHSVV
SEAGREGGAR EGCAQEAARP DGAAHAADLG PGAADAH
//
