ID I1CM38_RHIO9 Unreviewed; 1674 AA.
AC I1CM38;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific {ECO:0000256|ARBA:ARBA00015839};
DE EC=2.1.1.354 {ECO:0000256|ARBA:ARBA00012182};
DE AltName: Full=SET domain-containing protein 1 {ECO:0000256|ARBA:ARBA00030093};
GN ORFNames=RO3G_14229 {ECO:0000313|EMBL:EIE89518.1};
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE89518.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE89518.1, ECO:0000313|Proteomes:UP000009138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC {ECO:0000313|Proteomes:UP000009138};
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000256|ARBA:ARBA00000944};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. {ECO:0000256|ARBA:ARBA00008170}.
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DR EMBL; CH476744; EIE89518.1; -; Genomic_DNA.
DR STRING; 246409.I1CM38; -.
DR VEuPathDB; FungiDB:RO3G_14229; -.
DR eggNOG; KOG1080; Eukaryota.
DR eggNOG; KOG2399; Eukaryota.
DR InParanoid; I1CM38; -.
DR OMA; CFANETT; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd19169; SET_SETD1; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 1.20.1420.30; NCX, central ion-binding region; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR024657; COMPASS_Set1_N-SET.
DR InterPro; IPR004837; NaCa_Exmemb.
DR InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR044570; Set1-like.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR037841; SET_SETD1A/B.
DR PANTHER; PTHR45814; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR PANTHER; PTHR45814:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR Pfam; PF11764; N-SET; 1.
DR Pfam; PF01699; Na_Ca_ex; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM01291; N-SET; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000009138};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}; S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 562..581
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 714..799
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 1535..1652
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1658..1674
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 301..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1366..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..824
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1056
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1303
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1395
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1674 AA; 191237 MW; E1802FD0F132022E CRC64;
MKSERGLCFF IGWFSFIVTL TAFTIFAKGS KTNMISAFSN NCSNIELQKD QCEFVQSSCD
GFTAIYLKLY YCLGIWKQAA AIILLICLLV LFGAISIVAS DFFCPNLQTI SSKLQLSESM
AGVTILAFGN GSPDLFSTFS AMDSGAGSLA IGELIGAAFF IVAVVSGCMG IIKPFQSQRV
TFMRDATYLL GAALIMTWIA YNQSIHWYHG IILIVYYVSY VVVVMLGAYR NRGYNNANMI
EQKPAHEIDL VDESTCLLPN DLTTKRRKYG KPSSLLIPAR RFSVNSNLSD SYSQRVRHSL
QPTTPEGISP TSATFISHPN NRLPRTKSTH STRTYKRSIT PKPGFRTSIF GAIEFQEKIN
SFRRAMSSQV IPSPTRRERQ ASMPAHGCIY QYNTNIHQKN RPRALTSSAT QDYFTYLSTQ
QEPTAATTRT NDGQLESNGY PELIVPEIRL APPTNDDEEQ HSEEFYDCQH TPQHSFYHSM
RDQSYSTLDC ESYLTASQSY NELVSPTYSF MDQCFSSSLT DNHMSALFGQ EENAIEEEEI
TLIQSLFPTL QDFRKKTTFS KVNAIIAAPF VLVFTLTLPV AELKEQKVDD VLGFGEDSNE
ARQQQQSAST LAVNNYLSVP LSDNEAPFSE GNSAGDLVAN TALTKIGFPT MAISACYAGP
LLSKSTSVLP LQDPRIDKAN YEKNFSKGKF LYKRRLHIVE YKFDEHSVGP KPLTKVLVSQ
LSPLMTETQI TTYFSIYGQV SLVEIEKCPT TGGSLGIAHV HFENDAIQDG HVCACQAVEK
GNGRRMGSAE SVRVCFDATG EKLREAIKQA SGIKSDKPTT ERSHTLLRSR QPSPRKNDDY
RYGEDSRRHD ARHHYSRYDY YDDDYGYSRH HHGSRPPHYH SSRYPPPRYS DHYHYDHPSR
HSRWSHHYRS RSRSRERYYK ERDNDWGRDR SKRHTDDKRY IEEKPHVQYP LLLISRKCLP
FIRGALEDLK KMFYYYNCID VYSDDENWVI VFDSLPLAKK ALIATNQQSL LGHKLVITSK
FPVTDYEKPA EKVINETINK PQSESDKNRH NHTNTEEKSN YNSIATITTT TNDNSTLSNS
FMDIIPNKPV TAQDLIFQQL ADIFISDVKS RIAGPVIHDF IKTERAKRLE ASLNDSKEAR
LDNVQMVQKS IIESITTNST KLPRFKKKQQ FELPTKRKFD TLLNDYNETS GSSAHISKHQ
KTQEETTPAF TTGSSSEEGE YRTEPESSDQ EEDDLSVRIR QKERRTRRLC DYLSDEEESD
EDDTVRQELH EDEEESDDGE DDEEFEFENG SVEQYESDED DDFENFISNK KRKRAYNKKQ
SIVNKRQRKL DAYTDNEEEY EAIKAKKKPG RKKKYTFIDK VQNGTLSNSS LYTEEDHEKQ
EEQEEQEQEE EEEFDREALE KILLEHTDVS DLEETSKDDE GSVFNPFNET QDVEEFYFLR
AAILEKYEDK EQGPVTNIVR GGCARACVVT KIPDAVKATY LPRNKALIEF PSESGKISSR
ATRVNNRRLA IGMEMQKKTI DSDILKFNQL KSRKKQLKFA KSPIHDWGLF AEEHIDVNDM
VIEYVGEMIR QQVAEEREKQ YERCGIGSSY LFRVDDDTVI DATKRGSIAR FINHCCSPNC
SAKIITVDKQ KKIVIYANRD IEPGEEITYD YKFPIEAEKI PCLCGSKFCK GTLN
//
