ID I1CMI7_RHIO9 Unreviewed; 1115 AA.
AC I1CMI7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Zinc-hook domain-containing protein {ECO:0000259|PROSITE:PS51131};
GN ORFNames=RO3G_14378 {ECO:0000313|EMBL:EIE89667.1};
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:EIE89667.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE89667.1, 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000256|ARBA:ARBA00009439}.
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DR EMBL; CH476745; EIE89667.1; -; Genomic_DNA.
DR AlphaFoldDB; I1CMI7; -.
DR STRING; 246409.I1CMI7; -.
DR VEuPathDB; FungiDB:RO3G_14378; -.
DR eggNOG; KOG0962; Eukaryota.
DR InParanoid; I1CMI7; -.
DR OMA; NIIFCHQ; -.
DR OrthoDB; 5477220at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR PANTHER; PTHR18867:SF12; DNA REPAIR PROTEIN RAD50; 1.
DR PANTHER; PTHR18867; RAD50; 1.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00471}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009138};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00471}.
FT DOMAIN 510..607
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT COILED 143..170
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 230..257
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 444..482
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 578..745
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 800..918
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 557
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 1115 AA; 128662 MW; BB5D5CDEDA7E6331 CRC64;
MVCSRSLAVT QRRATVTQKT IDNSLLRYDP VTGEAFSISS RCADMDAELP LHLGVPKAIL
DNVIFCHQEE SNWPLSESSL LKKKFDDIFS SKRYAVALDN IKDVKKEAVQ DVKIGNVRLE
ALKADTVKAK KIRADLTQLN QQTAAKLNAL DLIEAKIDQA QQEVARLSDV FRDIHLTSDQ
IQQIINKRDF YLTTIHSLQD TLSPRPESTE ELKRLLDEHR VSEGRVSDER DGLMEKRRGL
ERKLKTAQDE LSRKHTTVGK LMAAKEQMED QMQRRIELIE SINSTHNLSF SIHDGSKAAA
LLRKQVATLE AKQKKDKMAA LNQQNTLSDE LQLLKSQHMS IIESKKHLTK LIENDKMQIE
SLRTKLSEFD VSANEIEEGK ERVEKEVRER ASFENQTLSF ILANEIETVG NNLKRILPRK
ADRERTYKEH LETIEYLLGK RPDAKDLEKD LLQFKEEKER NVKELKESRD TANKEFSAAE
GKIGVARHHI SVRRKDIQKY ETTIRAACGD HDLMDTLNAT EKTIMDLREQ LANIHGAELI
YGKFFEKAKA SKCCPLCTRG FGEDAQNDAF QGKLQTIMKR IPDQREKLNE KLKKSEEKKV
RLRAAQGDWI KLEALKKDVG SIEKNLMEFE SEKDHALNRA DVASAELIEI ESYTNKVDRL
LKPAEEMSRL LKECDVLQKN ITEIEDELSY MGSTRTLTDC QKDMEELSLK RVGLDMQLKE
YEENMKTHME QLKKVEHDIA PLEEQVQATT EAHEKAVDAW RMTEENMRAQ QNMYLRHADR
LDEFNRRIAR EEASVGAGKF ENTMKEIADL ESLMDRLQVD IKSTLDQINV IEKDEAERRT
VERDLQDQIT FRERQVDLAN CENELRQLQE KQGDVDVALL SEQLKKAQDN ETNYIDQRGS
IRGELVQMRD QIRRYEAELA NDYASVDGRY GELFIDVKSK ELAIGDLEKY SKILQMAIMK
YHTLKMQDLN KMIRELWVNT YQGGDIDYIE VRADDEGTTA NRSFNYRVVM IQNGSELNMR
GRCSAGQKVL ASIIIRLALA ETFCVNCGVF TLDEPTTNLD RENIESLAQS IVRIIQRKRG
QSNFQFVVIT HDEEFVEYLS RYDILGQYYR VKKDD
//
