ID A0A151MK29_ALLMI Unreviewed; 1625 AA.
AC A0A151MK29;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=FYVE, RhoGEF and PH domain-containing protein 5 isoform A {ECO:0000313|EMBL:KYO24882.1};
GN Name=FGD5 {ECO:0000313|EMBL:KYO24882.1};
GN ORFNames=Y1Q_0023755 {ECO:0000313|EMBL:KYO24882.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO24882.1};
RN [1] {ECO:0000313|EMBL:KYO24882.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO24882.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO24882.1}.
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DR EMBL; AKHW03005996; KYO24882.1; -; Genomic_DNA.
DR RefSeq; XP_014461045.1; XM_014605559.2.
DR STRING; 8496.A0A151MK29; -.
DR GeneID; 102565684; -.
DR KEGG; amj:102565684; -.
DR CTD; 152273; -.
DR eggNOG; KOG1729; Eukaryota.
DR OrthoDB; 5385125at2759; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15742; FYVE_FGD5; 1.
DR CDD; cd15792; PH1_FGD5; 1.
DR CDD; cd13237; PH2_FGD5_FGD6; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR PANTHER; PTHR12673:SF13; FYVE, RHOGEF AND PH DOMAIN-CONTAINING PROTEIN 5; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 1069..1258
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1287..1381
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1416..1475
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1528..1624
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 33..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..170
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..194
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..308
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1625 AA; 182031 MW; AD33698AF174B413 CRC64;
MNHAEFTKPP LAPKPKIIGH LSPVVVPKFS PSLTRSDVLH NPNSMSRGPK PPIAPKPKLS
ADTEGTASVY TNNNLNKCTN GKLICSDGEL YEGNQQNTEC LDSEADDEYI VVPEDQLTGK
DCDDLDPEHD QSFKPSAENE TLETPEMAEE EEGYSTTNDE EICDAEITEA EGNDCSDRDE
PVEPESDELT DTGDCNESEA ICQMSSATPD VEEDGSKNME EEEEVDSIND PNETKTYLAG
EDEEAFNNQD IVKDNNEYNL ETDKILNRDE DLEGSICQDI ILTPVDVDES IPSCEPLGEE
EQENELSQTL EEEVSNPDTE VSPANNDELD DNAELVLATE EELVDDGCAS PDTLPDEVDG
ETDVGLEITE DEPDVEEDLE GASKEAAVEG EEVVPDNDNE TTVEKEENVD DGYQTTEMKS
EEETSETACE ASEDSEKGEE EMLKAENVDD SCQIIPFEND CNEEAIETPL ENSDENPEME
ETFLNDGNQL SHSQTLPESG YEPELETEST TDAFVEECGD NTIGVCESDD QLLEGSKENH
DSLEENDSNL PEQVPAEKDL DECDQSKAEA DCESERETGE SLPIPEVIVV PEESEERETI
YDSLDDPYVL PAETENPRDG EAVLGADIPY DHSKREELDP ENSLLSIDRK NIVTRTRSLS
GKMPGYVPET VPEESGPDTD LPSSNNDSVT KDLSNNLLTL EGKQMEANRA LPAKSRRFIL
YPRSYSVEGR DMPGSVYRES DGSTLDDSRI KRTEDNLSLP CVISSSGSFS QRNHLLPSSG
VSTPSSVVDI PPPFELACIT KKPITKSSPS LLIENESPDK YSKKKKSSFK RFLTLKFKKK
TENKVHVDVN VSSSRSSSES SYHGPARVLE LDRRSLSSSP QLKSHAGKLR ASESPTTILF
YKDGKRKGTP KSFSRSVSRV ESFEDRSRPP FMPLPLTKPR SISFPNADTS DYENIPAMSS
DYENIQIPPR RPTRAGTFTE FFEDPSRALS AANENDGYVD MSSFTGFENK QQTTDQETES
AYTEPYKVCP ISMIPVEDVT SDEEQKSSED EESSQGDSSL IHKKGGQSRA HLIAQELMSS
EKIYVEMLRL LHTDFYEAVL KVLGDEDESE EKEAKLKQGL SELPEIYTLH QEILGELEER
VLNWEEHQKV ADIFLSRESR FNHHTAYIMQ FDRNLALLDE TCLKSSQLAT VIQEFEQNAG
SSSMSMKHQL LKVVQRVFQY RVLLTDYLNN LCPDSAEYEN TQAALLIVSE ITDRANDRMQ
QGENLQKLVH IEHSVRGQSN LLQPGREFVK EGTLMKVSGK NRHPRHLFLM NDVLLYTYPQ
KDGKYRLKNT LAVSGMRVSR PVTEKAQNVL KIEYAEHCLT LSASSCSERD EWYSCISRSL
PDDYKAHNTS AFHNSIELRE RLGIPLGERP PTLVPVSHVM MCMNCGCDFT LTLRRHHCHA
CGKIVCRNCS RNKYALKYLK DRLAKVCDGC YAELKKRERP LSVIFPPTSS RCSGSAFSSV
FHNIHYSSFK KQKKIPSALM EVAASGEGST ISGYLSRCKR GKRHWKKLWF VIKGKVLYTY
TANEDKVATE SLPLLGFTIA PEKEEGSTDA VFHLYHKQTL FYSFRAEDYN SAQRWIEAME
EATIL
//
