ID A0A3Q7X1I8_CICAR Unreviewed; 2210 AA.
AC A0A3Q7X1I8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Methyl-CpG-binding domain-containing protein 9 {ECO:0000313|RefSeq:XP_027187624.1};
GN Name=LOC101489788 {ECO:0000313|RefSeq:XP_027187624.1};
OS Cicer arietinum (Chickpea) (Garbanzo).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_027187624.1};
RN [1] {ECO:0000313|RefSeq:XP_027187624.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_027187624.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_027187624.1; XM_027331823.1.
DR STRING; 3827.A0A3Q7X1I8; -.
DR PaxDb; 3827-XP_004489317-1; -.
DR OrthoDB; 1216725at2759; -.
DR Proteomes; UP000087171; Chromosome Ca2.
DR GO; GO:0000785; C:chromatin; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15519; PHD1_Lid2p_like; 1.
DR CDD; cd15489; PHD_SF; 1.
DR Gene3D; 3.30.160.360; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47162:SF10; METHYL-CPG-BINDING DOMAIN-CONTAINING PROTEIN 9; 1.
DR PANTHER; PTHR47162; OS02G0192300 PROTEIN; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF15612; WHIM1; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000087171};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 81..137
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1277..1327
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1537..1557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1877..1897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2016..2044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2170..2210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2016..2036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2189..2210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2210 AA; 244068 MW; 96EAC637C09C8456 CRC64;
MIMELTDSTA GNIPPPPPPP PPPHHNHQDT RSILCIDLNE IPSPSSSFPE TLPDFTIDIV
RTYHENPAPP PGGPAPLPGG PTPCAACSKS GGGGGSVLVC DGCERSFHLA CAGIRGGGGR
QSAASLREWV CSECLAGGVK SKRWPLGVKS KQLLDINSSP PSDADGEELH DARKHTLGDK
SFGAPVAYSN FYNGGVFGFQ RASGVVTQAV RVGFEDILNH TKSMSRRFEE AYMDLPPGIH
SSSNNTAINV PSQSPNETKV LQALRDFISE KHGVLEEGWR VEFRKSMITS DPYAVYCAPD
GKIFDSVYEV ANFLGLPSGF NSMESEVRNE MSFSLGGPHL SRKRKSSKTL AANGFVEKQG
TLINSNYKDY SSDGLNMECA NAQGTVPKAT EIRRKENGHS DLHQSTDELP LQFKDFYVLS
LGKVDGRPSY YDVNVIFPVG YKSCWHDKIT GSLFTCEVLD GGDPGPIFRI KRCSCSEFPI
PVGSTILSMQ SHCHFVSETN EGQRETNDSM DLDGDESIQM ILLESRAPTE NDILSCFASC
SNESCASEGL RPVAGLVHDN TGNSFANNME FSDDIIISQK LLNACKDICE KKGTLKLYCK
HVESETGLHK WDLRNETSDT HFTLLDKFCG SPGSVSIPDA IYADNDLKGL YERLEKWLEQ
DRFGFDVEFV QEILEQLPGV QDSLQYELLS SRNNSSSLPT VENGFLKVEC KGQSKYQDEE
EAVQGLYRRP KKARLTERYV KEHRCPPPGK SLCSRAPTEL IGDIFQVWEL LQRFHEILDL
REPLLLEELE KELINPWFDE LDFPEKSERG MGGSQLLSSK GGVGDCRLIC EAGPSSSAES
SFIQVETEAM KEEAQVKLAS FTYVRCFGVA LTKAHNSLLR VLIGELQSKV AALVDPNSEE
TRTRRGRRKD IDSAVPAKRT KVNMLPINEL TWPELARRYI LAFLSMDGNL ESAEITARES
GKVFRCLRGD GGLLCGSLTG VAGMQADALL LAEASKKIFG SLSRENDALI IEEEESDAKG
TSEIKLTNDG NIPEWAQVLE PVRKLPTNVG TRIRKCVNDA LVKNPPDWAR KRLEHSISKQ
VYKGNASGPT KKAVLSVLKD VVEGMHQNPN KGRKKKIVIS ISDIIMKKCR TVLRRAAAAD
DSKVFCNLLG RKLINSSDND DEGLLGSPAM VARPLDFRTI DLRLASGAYD GSHEAFLEDV
RELWSTVRVA FGDYPDLVEL AEKLSQNFEF LYKEEVVAYI QKFTEYAKVE CLSEEMRKEV
DDFIASTIEI PKAPWDEGVC KVCGIDRDDD SVLLCDKCDG EYHTYCLNPP LARIPKGNWY
CPACIDGNHA TQNVTELAQI AGKRRSKKFQ GEVNCLYLEA LTHLSAVIEE KEYWEYNVGE
RTLLLKFLCD ELLNSSLIRQ HLEQCSELSV ELHQKLRALS VEWKNLKIKE DVLSTKAAKF
DALSQSATGE IGLKEGFPSL FSNTSKCLVK PHTATTNASG VGALVDSLTS EEIPKEKCRF
NSVDKSISVT HSDSDSQNLN SIEGQHRSVP VAVESQCTDK SPKSFPSPNH MPQEINGYSG
ATHIQGSHQQ WEVRDASTSA TYQQGKCVPV EVSQIAVNES EPYHLELNSI KRNISLLQDS
MTSIGAQLLK LSVRREFLGI DSTGRLYWAL ATPRGHSRII VDASAVLQHG RGLSVGKDSS
EKFSALQHCA LSEKNNYKML GLIKDCSPLM SQPFNALGNS SPWIAYETDS EIEELLGWLK
DNDPKEKELR DSIMLRSKYR LQESINAHTE GQVEDQGSVY LPRNAVSNSL VTKATSLLEM
KFGPFFELDT AEVLKKQSKK ARTTNDEKLY RCECLEPIWP SSKHCLYCHK TFLSDVEFEG
HNDGKCNAGL LALEKNKDKS GSSNGRGNSK CDTSHEKSRA DAVTAGTSIN RCSKLSSSLI
KFSNEDSSCP FNFEDICSKF VTNDSNKELV REIGLIGSDG VPSFVPFISP FVSDYTPFLT
LKDDGIVDGV SKASESLVSS ETTDGAGVCH DYKSGKSTES LSANENNQAG KSNKSSLGEQ
RDGKGVDGCC VVPLSSLRPL VGKVSHILRQ LKINLLDMEA ALPKVALRPS KAQLDRRQAW
RAFVKSAETI YQMVQAIITL EDMIKTEFLR NDWWYWSSYS AAAKSSTLPS LALRIYSLDS
AIMYEKMPNS SFADSSDPPA IAELKPVIPA DADKSKASRK SNRKRKEQDG
//