ID M7C911_CHEMY Unreviewed; 841 AA.
AC M7C911;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=GPN-loop GTPase 3 {ECO:0000256|ARBA:ARBA00014587};
DE AltName: Full=ATP-binding domain 1 family member C {ECO:0000256|ARBA:ARBA00029702};
GN ORFNames=UY3_05623 {ECO:0000313|EMBL:EMP37092.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP37092.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- FUNCTION: Small GTPase required for proper localization of RNA
CC polymerase II (RNAPII). May act at an RNAP assembly step prior to
CC nuclear import. {ECO:0000256|ARBA:ARBA00002411}.
CC -!- SIMILARITY: Belongs to the ARPC3 family.
CC {ECO:0000256|ARBA:ARBA00010856}.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family.
CC {ECO:0000256|ARBA:ARBA00005290}.
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DR EMBL; KB523138; EMP37092.1; -; Genomic_DNA.
DR AlphaFoldDB; M7C911; -.
DR STRING; 8469.M7C911; -.
DR eggNOG; KOG1174; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005885; C:Arp2/3 protein complex; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IEA:InterPro.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR CDD; cd17872; GPN3; 1.
DR Gene3D; 1.10.1760.10; Actin-related protein 2/3 complex subunit 3; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR InterPro; IPR007204; ARPC3.
DR InterPro; IPR036753; ARPC3_sf.
DR InterPro; IPR004130; Gpn.
DR InterPro; IPR030228; Gpn3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR21231:SF7; GPN-LOOP GTPASE 3; 1.
DR PANTHER; PTHR21231; XPA-BINDING PROTEIN 1-RELATED; 1.
DR Pfam; PF03029; ATP_bind_1; 1.
DR Pfam; PF04062; P21-Arc; 2.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF69060; Arp2/3 complex 21 kDa subunit ARPC3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 2.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 618..651
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 751..784
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 789..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..824
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 95054 MW; 0C653CF07892468F CRC64;
MVQHCAAINR SVQVVNLDPA AEFFNYPLMA DIRELIEVDD VMEDDSLRFG PNGGLVFCME
YFANNFDWLE DCLGHVEDDY ILFDCPGQIE LYTHLPVMKQ LVEQLQQWEF RVCGVFLVDS
QFMVESFKFI SGVLAALSAM ISLEIPQINI MTKMDLLSKK AKTEIEKYLD PDTYSVIEDS
ANILKSTMFK KLTKAICGLI DDYSMVRFLP YDHSDEESIN IVLQHIDFAI QYGEDLEFKE
PKAYHSTLMD SDIKLIGNMA LLPIRSQFKG PAPRETKDTD IIDEAIYYFK ANVFFKNYEI
KCNSKGQGEK EMYTLGITNF PIPGEPGFPL NALYAKPGNK QEDEVMRAYL QQLRQETGLR
LCEKVFDPQS DKPSKCLPSE IEVKYKMAEC YTMLKQDKDA IAILDGIPSR QRTPKINMML
ANLYKKAGQE RSSVTSYKEV LRQCPLALDA ILGLLSLSVK GAEVASMTMN VIQSIPNLDW
LSVWIKAYAF VHTGDNTRAI NTICSLEKKS LLRDNVDLLG SLADLYFRAG DNKNSILKFE
QAQMLDPYLI KGMDVYGYLL ARDGRLEDVE NLGCRLFNIS DQHAEPWVVS GCHSFYSKRY
SRALYLGAKA IQLNSNSVQA LLLKGAALRN MGRVQEAIIH FREAIRLAPC RLDCLIDCYL
ASNSIREAMV MANNVYKTLG ANAQTLTLLA TVCLEDPVTQ EKAKTLLDKA LTQRPDYIKA
VVKKAELLSR EQKYEDGIAL LRNALANQSD CVLHRILGDF LVAVSEYQEA MDQYSIALSL
DPNDQKSLEG MQKMEKEESP TDATQEEDVD DMEGSGEEGD LEGSDSEAAQ WADQEQWFGM
Q
//
