ID A0A183QSA5_9TREM Unreviewed; 1055 AA.
AC A0A183QSA5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=GPN-loop GTPase 2 {ECO:0000256|ARBA:ARBA00014588};
DE AltName: Full=ATP-binding domain 1 family member B {ECO:0000256|ARBA:ARBA00029700};
OS Schistosoma rodhaini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6188 {ECO:0000313|WBParaSite:SROB_0000655201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SROB_0000655201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
CC -!- FUNCTION: Small GTPase required for proper localization of RNA
CC polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly
CC step prior to nuclear import. {ECO:0000256|ARBA:ARBA00003181}.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family.
CC {ECO:0000256|ARBA:ARBA00005290}.
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DR STRING; 6188.A0A183QSA5; -.
DR WBParaSite; SROB_0000655201-mRNA-1; SROB_0000655201-mRNA-1; SROB_0000655201.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd17871; GPN2; 1.
DR Gene3D; 1.10.1410.10; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR004130; Gpn.
DR InterPro; IPR030231; Gpn2.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21231:SF3; GPN-LOOP GTPASE 2; 1.
DR PANTHER; PTHR21231; XPA-BINDING PROTEIN 1-RELATED; 1.
DR Pfam; PF03029; ATP_bind_1; 2.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 540..657
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 1031..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1055 AA; 119458 MW; 9C0817E630296AB4 CRC64;
MLLNSAVYRS LARRSILLTC SPTSVPYIID KFLKIGGSVN RAVYWPSQNG IQPVGTLLIQ
SSSPESLRYT LHKIPSLHCI HCVVNSERKK SMFRLPMFRI NSDPSIWPVE NVEKYSSYQY
PGRLCVESNL SIRPSVPSSK EMTSILMSCQ SFDDQVSTLY HLTRLTEQDI LARFVLSDSI
EXXXXILGFI FRGTEVSIFG SVLNGLGSIS SDIDLVVKLP LNYDNLQYLC DSKPNCMTSD
LFRTKIISLD PDFLKNKFLY FLQRMLRKLD XXXXYSQVYH GRVPIIHSDR ISILKVGLDI
SSLTESTLVN NGESTHHGTK MAEILHFLTL CIPEIPKSVA LIKYLARKLR LTRNGPSPGF
TNFKLISLFI NFLQVSNYAP SFIRLQSLIE NSIALDSASA FSVHLHFPDL NPFPSMEDLL
GNFLVYVCSI KPCDIIIDLR NGCLTPRLES TDNEYTDHMI TPGKHFILCP DPTYPQCNIW
SGINEDHWSK FVQICRVLQD TLEMQCNKNE NSKWGLLALT DLDDCTKSKF VNVSDYYQLN
FLALCASDYY KGCIFHRNIK GFIVQTGDPT GTGKNGQSIW KKRFKDEFHD SLKHNARGIM
SMANNGPDSN GSQFFITYSK QTMLDMKYSI FGKYYHTSSD QNQINIDYVM MSADSKPYPF
PNGLHLFGQL VIGPPGSGKT TYCAAMHDFL VKLGRKVAVI NLDPANDSLP YPCAINMADL
ICLDEVMDYL GLGPNGGLIY CMEYLYTNRS WLANQLAALK QKDPKIYLIF DLPGQVSQLC
DVDHATKLFT CKRLCVELYT HHPCMRQLVC YLTNKPTNLK LNTKNQLSLP SSSIQSSSSN
DEVPNSLDLQ LTSVHLIDSH YCSDAGKFIA CVLTSLSAML QLSIPHVNIF SKADLIEQYG
ELDFNLDFFT EVLDLQYLID CLHKTTNNTD QLLFNCKYTR LNQAIIDLIQ DHSIVQFLLL
DIQDLSHIER VMRYVDXXXX XXXXXXXXXX ANGYVFGTNE QHNLQSLLHS ASGVELAPDW
IGMIQEKYTS KKNDDNHNID NNVQNDDEPH IDLFS
//