ID   CPAS2_DICDI             Reviewed;        3933 AA.
AC   Q54BW4;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Circularly permutated Ras protein 2;
DE            Short=DdiCPRas2;
GN   Name=cpras2; ORFNames=DDB_G0293376;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=18510733; DOI=10.1186/1745-6150-3-21;
RA   Elias M., Novotny M.;
RT   "cpRAS: a novel circularly permuted RAS-like GTPase domain with a highly
RT   scattered phylogenetic distribution.";
RL   Biol. Direct 3:21-21(2008).
CC   -!- DOMAIN: In contrast to other GTP-binding proteins, it is characterized
CC       by a circular permutation of the GTPase motifs described by a G4-G3-G1
CC       pattern.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. CpRas family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000204; EAL60755.1; -; Genomic_DNA.
DR   RefSeq; XP_629170.1; XM_629168.1.
DR   STRING; 44689.DDB0231848; -.
DR   PaxDb; Q54BW4; -.
DR   PRIDE; Q54BW4; -.
DR   EnsemblProtists; EAL60755; EAL60755; DDB_G0293376.
DR   GeneID; 8629191; -.
DR   KEGG; ddi:DDB_G0293376; -.
DR   dictyBase; DDB_G0293376; cpras2.
DR   eggNOG; KOG0395; Eukaryota.
DR   HOGENOM; CLU_224152_0_0_1; -.
DR   InParanoid; Q54BW4; -.
DR   OMA; LTRYRIW; -.
DR   PRO; PR:Q54BW4; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR041246; Bact_MG10.
DR   InterPro; IPR001599; Macroglobln_a2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR020849; Small_GTPase_Ras-type.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR24070; PTHR24070; 2.
DR   Pfam; PF00207; A2M; 1.
DR   Pfam; PF07703; A2M_BRD; 1.
DR   Pfam; PF17973; bMG10; 1.
DR   Pfam; PF00071; Ras; 2.
DR   SMART; SM01360; A2M; 1.
DR   SMART; SM01359; A2M_N_2; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF48239; SSF48239; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   3: Inferred from homology;
KW   Coiled coil; GTP-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..3933
FT                   /note="Circularly permutated Ras protein 2"
FT                   /id="PRO_0000371348"
FT   REGION          23..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1022..1054
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2817..2839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3036..3086
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3107..3142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3733..3754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          12..46
FT                   /evidence="ECO:0000255"
FT   COILED          167..215
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        23..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..189
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2817..2833
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3052..3086
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3107..3125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3126..3142
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         2853..2857
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         2913..2916
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         2976..2983
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   3933 AA;  442696 MW;  F1DF725250CB8834 CRC64;
     MSNSFDNFDF SVHEVKKQEL ESILLQQEQE KQAKEEKESI KDTDDKPIED TEHSTNNDKP
     IEPVESVEST PTTTTTTKPT DEASSSSNNN NNKIDVTIEK KEGDITGIEL EELLSKIPST
     YQLSTINKTI QGFSTDIREP TDKPFENTSN IETTRQLKFP PPLVPPKTEA ERLEQEQKQK
     QYDENRKETD RKLELELERL KNKKEEVEQI RAYFQPGDQK PIDYVIELTF NIFPSDIVDK
     ETNKLLWCPE VSPRNPGFAR DKPTNGWTFD QFQRTLTYTP IESWKKSTLY TITIPAEIKV
     SPTNIITTQG QQFEFTTETL KIELFMPASI REYSHNQTIF IGFNQKVSPQ ELLPFIQATN
     LRSAPAHVAK GTPNVLQFIH EEIMKQDPIL KDLVTGYEGR NIGIKPTFGF NSSSTVIISV
     LQGAPSLEGT VKKLLTEQKD FRTLQSFKPN ITTAPYSPHI DLVISFGNLN SLANPSEITW
     RPKVTPSFPD GDWVLSANSL VYKLSDNSNW PSSTSYTVFF ENGPKSTSGE QMEEIELKFQ
     TASINLTGAF GYDGINFESL NINSKSASTS NTFSNNVILI FRYNQIVNEE SFKKIFSFKV
     DQLLSKAVEY QIISNAAEFH SITTFRKAIK ENYLRFIDTQ EPGSWFAIKP LKPLGDDLGY
     SIEFDGSLQS MEGPLPTKLD GGYNNYFFAT YPQLTCTTDL VHDSFKVSFN QPIVNNSYDY
     NNYVLTPDAF ISSRTDVQIE LDYLPVGPSV LPLIQPPIEG TWSALTRNIL SFKAASFDLI
     KPATTYTILP QPNSQFTTPW GKVFDKAIFG EVTTTLPNVN FRYPTLSSIK ANQLFCLSFN
     QPVDPESVIA NVRLQPDTFL SAKKFEVQLV TKISLEEFED IDYSFKNAKL DGRLVFFRSV
     KPLPIGSIKF SVLPGVRSLE GPLISKDETY FGTLVVEKFS IIGTSPVDGA IIHSPYFFFI
     NFNKPLKSKD ALVYIDLTEN HGPEETLTTI VDKITAIASV SASIASSDSS SSNQLIENQN
     NITTTTTTTT TNNNNNNNEV GESTTPNLPI TTTTTNKNKE IDWDQFITIK PKPEKSTAKW
     TYEIIGKIYR LKIEDFSIWN ASTNYQIIVD KSIESKYGET MEKDTVFDFY TPYNGIESVH
     PSPGFIVNTD KSDIFAIHFH QRINPVEILK VLKVEGVDSF NKKIKNIVLS NVDREQVPSE
     YLSQMSTSFS DPLNYIMFVR MSTVVPNSSL TLTVGPNIPS AEGPELNPNK LTYTFKISDH
     LHINSTTYYA SDRTLQILFK QPLNLTGPAL QKKIPLPESW IPTITPEISS EIQRTWTAQL
     NTSNTLQNGY SMICCKFETS LPFSTKFTFK LPDCIESETG EFYQQGIDSE DKYEFKTSTL
     QLVTSVPMNG HQTALLSRPV LICFNQKVDV VELLKYLTIS QVSTSEKKKT KFTLEESSDF
     THIEKSVGYE QDHWISLRTN PPLIPNSSYS ITLKEGAPSL EGPLLTKEAI NIFFTTNCTR
     VYASINSDQA HISFSEPLIH LPINGSSGGS SSSSLPSSEP IIPTITIKPD PGVPLTWKAG
     AGETIICNEK VSTWKQSTEY KFSFPEDLVS SKGYVMDQST LDNLTIKTSV NSIIDKSGYP
     TLTDSIHFIR FSQNIDPKKQ ISKMKIFSKS GLFNSKTNHE VRLATKDEID EKVIFSEHLD
     HNINYSRLKL FIGDVYDPAD PTDLLIYKFV KPLPPNTQIQ YEFEEFTSTQ GQLTWVKPFY
     NYSIKSLPPL SIIDSESSFG KKTPFYFGDT LVIKFNNTLS TSTFQANMIR VEPDIPYSIT
     LDDQSIFLKD FKYDQFQNTD IEFKIILNTN QIMDSTGQHI DISTIVGTGG IFNKNDSTLT
     YRLKVVPRNF QSTFKLPFLS SSSTNGIVTF DNSDLNSKPA ICLRSKNINQ YVIQLYKLNP
     YIDYPQFLDE EVDTKTLQKF TSLKSVPAVD QPILKSGELV HCRMVDIEIP SHEVDIEIDT
     YIDLFEGLTN KELMIGHIGV VLYPTQNALY PNVGKNTVTP LRRCWVQCTR LNIGAVTDQK
     ILSCWSNSTV DGSVVPNVKI SSLSTVNYTQ FRMKEQKKSN NLIALQKHVG NLVDGVTNEH
     GLLHLPLQNN YSEIHIVAEN PINKDVCLLP KVFVQPNSTF KAISWYVFDD QSLYRPKTTV
     QIKGYLRFLF RDQFEHKLSV YNFQSTLVIK YILEDGAGLT VLKGETKLNS FSAFNFSLDL
     PDTINLGKTT LKLSLADEND FHLLNEQNQK IRIKSDTGKT LRTSFIHSFD VQEFKRPEFV
     ASASFLYNET NGFTGSSYIQ VKSNYFEGAS LPDCETSWKV SSCKANFVPP KMSKYQFGYV
     ENDKLLKLVD HSIKREKTIT GKTDDDGLHT VKTTFNGKAP NPPSSVYIDT SVDISDINQQ
     TTTSTVRYIL HPTHNFVGIK PSFNNDKPLI IHDGNKNTPL KLMMIVCDEN GIPQPDIGIS
     ITISPISGYH QFDIPLINEN HQSTIVSTDT EFQHSFILSE PNYKPKENIL YNISATIYEK
     PDNKFTTTIP LLINWSLSEY KSNDLLDSST IGKTTTTTTT TTTTTSNNNE TKQPIKLEEF
     KFKEIKNVNI SLDKKSYISG EKCLVSIDYF EMPYQCVLSI INNGVVFTKA YEITNGKDRV
     EFDIQEEWAP LCSVLCDVRN VGDHYLQGTT KLSITPTTKQ LTITVKPEEE IVEPGADTNI
     NVHVTDSTGA NVANAEVCLL VIDESIIALS QHNVENPLNI FYPNSSSEHA KSMLSSYFHG
     LSSASVLLQP KLKQGTAIIA GTQQPIIKPD TYNHILEKKI LINSNDNDNF NYSSYNNNNN
     NNNRYNTPVR NGNIGRPTRR GSGTDKVLLD ILDTAGQEEY SAMRDQYYRH GDAFILAYSI
     NSRSSFQNLQ SYYNQLCRIK DCDSYACVIV IGTKADLEDQ RQVSKEDGLL YARSLGAAFI
     ETSAKTGFNV HTAFAIVSKL SAGYTGTAEN KIVIVGDGGI GKSALTVRYV QSCFVEQYDP
     TIEDSYRKQV SLDDDPSLDG FIPDSLRADM EGNSTLQSAS LMKKRSKKSS FGGFGGSGSS
     SSRKYKEKSP SSSSTRTSVS TSLSSRSETL GEVGLLDFGG SDKKLSRKSS LVEEESKRQY
     DDDDESKSES SEYDDDDDQD YEKDGLFETE LSSLSMMRKD FNALANFTPS VFTNEVGKIT
     IPIHLPDNLT RYRIWGVVCS KDEQKFGKGE SLITSKVLVS TRCVPPRFLN INDSCTIGIV
     VSNNSNNNRM VKIGVKCSEH LTILNSNGTS TFGHFSFVEQ KKRKIIYINV KTLNTGVGSI
     QISCVSGKYG DAMQVSIPIF NPPTTRTTSV YGVIDDGAGV IQPIEMPQDS LPIFGSLGLD
     ISSTILQNIH DAFLSVYNYP FERTENLASA AIGIASLYHI IGEQKSSRNL PPSKIVKSKI
     GKLFLDLRNR QNENGDFSTW PSYAGHSNLS FQKNDFESVH AIQAIATLIE YGYEIESSKM
     KQLVKNSIDW LDRYILVNLQ SKDQFILATV SYALFTLYCI HSKKNKSSVT QLAMKFYQTH
     TYSILSLESL AWILGTLQGN DSSVVKKRDE IITYLMRNSF EENNCLYFNS YYDKLIRSQL
     FHSLERTTAI IARSLIQSRY NIDVVSKVII GLMDRKENGT WKNIQTNCWV ITAVAEFSST
     FERSSPKCLS RGWLVNTSDS SNLKTTFCGQ TPYFDGKSTI SYSIEVPLSI LYSKSDLENV
     KFNNIIKSDK QQVIEPSSNV DENSEKVETQ PSSSTTSIIS IPKSELWLQK EGKGKLYYRM
     NIKYATVDLS TEEHFNGLTI HRQYSPKSKS DKMEFDSETG VLKVSVGSKV LVTLNVQTEV
     DRYNLALVDK FAGGFDIVDK TDFRLEGTVW EFQNQRDERC EVFTNQMERG KYTYKYTLRA
     STRGEYLIPS ACIEEMYDPD VFGRTNSLRV IIN