ID A0A2T7P990_POMCA Unreviewed; 1499 AA.
AC A0A2T7P990;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Mab-21-like HhH/H2TH-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=C0Q70_09246 {ECO:0000313|EMBL:PVD29985.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD29985.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD29985.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD29985.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD29985.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the mab-21 family.
CC {ECO:0000256|ARBA:ARBA00008307}.
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:PVD29985.1}.
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DR EMBL; PZQS01000005; PVD29985.1; -; Genomic_DNA.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg5.
DR Gene3D; 1.10.1410.40; -; 2.
DR Gene3D; 3.30.460.90; -; 2.
DR InterPro; IPR024810; Mab-21-like.
DR InterPro; IPR046903; Mab-21-like_nuc_Trfase.
DR InterPro; IPR046906; Mab-21_HhH/H2TH-like.
DR PANTHER; PTHR10656; CELL FATE DETERMINING PROTEIN MAB21-RELATED; 1.
DR PANTHER; PTHR10656:SF76; CYCLIC GMP-AMP SYNTHASE-LIKE PROTEIN-RELATED; 1.
DR Pfam; PF03281; Mab-21; 2.
DR Pfam; PF20266; Mab-21_C; 1.
DR SMART; SM01265; Mab-21; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 121..307
FT /note="Mab-21-like nucleotidyltransferase"
FT /evidence="ECO:0000259|Pfam:PF03281"
FT DOMAIN 1192..1352
FT /note="Mab-21-like nucleotidyltransferase"
FT /evidence="ECO:0000259|Pfam:PF03281"
FT DOMAIN 1404..1488
FT /note="Mab-21-like HhH/H2TH-like"
FT /evidence="ECO:0000259|Pfam:PF20266"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1499 AA; 167155 MW; 38F27E296AB31197 CRC64;
MMRVGGFGDG GGGGARARLS ASTKSMGSGV STSRTMSCRG TRSSELDLIK EADEVMKAAE
IEKSPNPTRQ GNQFFDDEVK LGGDEKRHAA HEFSRLRNNL LESLDTGSEW KWEVLNSGSS
YDGTKVTRPD EMDCMFFPGN ISEDWMEIDF HGAPPGFCFV KLKKISELDS KYEGLKGLCE
DSTMRINATK FKKMTFKLFK KGIENTRNAK AGRAGPGAAA LPVEYRVIPS SVGKGLLPMS
VDLVPALRFT MWPKKLTTLL KKLPPKVAEG VEEAGLHVVP KPCLDDRYEE DRDFLWRLSF
SAAEKEMTKF LDGKYRNPAA GTTCRKQVLR LMKRILEISK GFKNSKTKRF CANAKELKLA
VTTLQKRRKV TIKHFSTFTI RTALWDSFYV QHRDDDHWHI SKKRSRLLDT LELLKKMLMG
QTTVSQFFVP ELDIMSSVPV EEREFLYIIF TIIFNKMETK HKEDSSPSLP RSQKGKENTP
HAGRKSSAAS KPPSAGQSQK GRTSQSAKGP RTVPLEANDT PIMEETEGKK FKGENSPTPT
STPKSKRKGR QGADDKTKTT HTGERYIDGG IHPPSQTSSP SESANSERKQ ARGARTKHCV
PLSSIGPEET ADHEPEVSRV QRRNTKASSN SKSTSLDKLP GEKQNKSSNL KSTGKKHQET
ADEPQKFSSG ESLSSLSTST CLEEIADEEQ EVYSASELNM ESEARSKFSS PGTSILQNEI
RGGEQKLSSE STSKMSNARA RGKISSPLTS KSQEESADDK HEVATVSTST LKKQGTQRRP
KLSTHSTSTS LEEIACEKHE TSSVPTSTPK RQEKGKHPST SQSLEKTAED GCQSQSSSTP
QKEEETQVSS TTLKKKGTGT RSKPSSNSTS TSPEKISNEE NESLSQLTST KSKRRESGAK
EKLFSPPTST NHEDIAGEEH KVSSASTSTL KKRGTRGKYE LPSPLITETN DQMSNEELEV
SSELTSPLNS AAEATGKSSP PTSTIHCHTE GTEHEVSPAS TATLKRGETK RKGKSCPLAS
KSGEETADRE LQFPSDCTST LHEKGGEDKL KHTEIVKQGE GAPEGMSSVP AAEIQEETER
EIISPSTLIE LKASKETASS TQKPKPSKRK INDSREMKLI KKADKVMDKA LIEISANPTR
NGNDFFDEEV KLEQKEKLHA SSNWQTLCQQ IRESLKEGSA WKWKVLNSGS SYDGTKVARA
DEVDCMFIPK SIPDEWMEID ISGAPPEFCF IKLRDLPISD PKYLAFKELC GDQGMVKSAL
FRTKAFDLFT KGIAKNRHAK AGQPSATAAA FPVNYYVIPT ETQGMLPISL DLVPALHFTT
WPEKLKGFLS KLPQEKREDV EKVGFHAVPK QCLDDRDPSS AVVTTYRKHV MRMVKRILEL
CKGIDNPKRS RRCPSVQELN KAVTTLREQK SVEIKYFSTF QIRMLFWDYF YVRLPEDVDW
ERSKWRTRLQ ETFRNLRKML TGEKQVEHFF VPGLNTMENV PIEEREFLYI IFYIAEKIF
//
