ID W2T3Z6_NECAM Unreviewed; 1021 AA.
AC W2T3Z6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=TFIIE alpha subunit {ECO:0000313|EMBL:ETN76633.1};
GN ORFNames=NECAME_11535 {ECO:0000313|EMBL:ETN76633.1};
OS Necator americanus (Human hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC Necator.
OX NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN76633.1, ECO:0000313|Proteomes:UP000053676};
RN [1] {ECO:0000313|Proteomes:UP000053676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441737; DOI=10.1038/ng.2875;
RA Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT "Genome of the human hookworm Necator americanus.";
RL Nat. Genet. 46:261-269(2014).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the TFIIE alpha subunit family.
CC {ECO:0000256|ARBA:ARBA00008947}.
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR EMBL; KI660215; ETN76633.1; -; Genomic_DNA.
DR RefSeq; XP_013298860.1; XM_013443406.1.
DR AlphaFoldDB; W2T3Z6; -.
DR STRING; 51031.W2T3Z6; -.
DR EnsemblMetazoa; NECAME_11535; NECAME_11535; NECAME_11535.
DR GeneID; 25351564; -.
DR KEGG; nai:NECAME_11535; -.
DR CTD; 25351564; -.
DR OMA; SNIMATN; -.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000053676; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR InterPro; IPR017919; TFIIE/TFIIEa_HTH.
DR InterPro; IPR002853; TFIIE_asu.
DR InterPro; IPR024550; TFIIEa/SarR/Rpc3_HTH_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11804:SF83; LD37516P; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR Pfam; PF02002; TFIIE_alpha; 1.
DR SMART; SM00531; TFIIE; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS51344; HTH_TFE_IIE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000053676};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 647..772
FT /note="HTH TFE/IIEalpha-type"
FT /evidence="ECO:0000259|PROSITE:PS51344"
FT REGION 930..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..989
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1013
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1021 AA; 117364 MW; 6D44FB32AD196A92 CRC64;
MFVFSESFAV FRLPHIPDET VENNTFMYNI AKGEDWPKLA TSTPKIKIMS ARDHMEKLSD
TEFQATIKHL YDTKEGLTEW QLRLLEWYLL EVRASGLDKT DEKTRKLIGS WSKFIDEYRS
KYISNIMATN DQVVFTITDK NMLKDAPPHV LQKLAVVAEQ WEEGPWRGRM TPHTLHPFMQ
YCGSRQLRAE AWEKWISKAS FEHDFYNNSV IVEELRHNKL IRRIRPVFID RMESWTAFAQ
AKEMMSGDLQ AHDMAYICRR EAEQHYDVDP LDLMNHFPFW PTFHNLTNII GHIFGLQFKD
ITESGLERAH PDAKIFSIMD ITTTEHLGRL YIDPYDRESK RGGWNTLLGR MESQSRGLDK
IIYLVGSAIA PTETSPSLLH HQQLQQLLFH VGRAIQMLLS RSPYRDIAIP WAPFYASDWD
AVDMFPAFLQ FFVYKPTLLQ SLSSPHLANG STISDEQANN ICLALSRATL WDSYRTLFWS
DYDLTIFEME DRKQKFWLDL YREMSKEYFP FKPGRNDYHP CSFIPIFGLQ PYMGMYYRKL
WTEMLALDIH ETFDYEDDVM KTGERLKTTV LSRGSGDVAK ELYRRFQGRD PSVGAICDFY
DPPSFYHLES EAVVKVAFTV MSTAAPASGG DTKSPETTVV TEVPPSLHRA LLMMVKNFFS
KGEWCGEEDR MNASTKFIWG SLNRLYETNV LNKEIVEHYL VVYYIMRSVC IREENLRSRL
NFDQKHLRQL LAALKNEKLV KDRLLQQKNE TGRNVSVIFY FINYRAIVNV LKYKIDHMRQ
MLEAREKNEL QKANYKCEQC GAQYEDMDID RIFDPQTGTL KCWRCQGDVT QDITGGPTQV
TRTLLARFNE QMLPLFAAIR ELAAAEPQQQ LLDFSTSAGG NRAQLGGVAH SFNSGPSIKY
ANADQITVDL NADANSKPVE EAKVVPTWLQ DDAIGGSEQE TATDTLSTGT DSVTNMPHTS
SSVSLSLMAE LEGVTDEPVA KRPRTSEGDN EANSAETGAE EDDEEDDDEE EEMISVAGKM
V
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