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Database: UniProt
Entry: A0A2R6WMD2_MARPO
LinkDB: A0A2R6WMD2_MARPO
Original site: A0A2R6WMD2_MARPO 
ID   A0A2R6WMD2_MARPO        Unreviewed;       520 AA.
AC   A0A2R6WMD2;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=C-CAP/cofactor C-like domain-containing protein {ECO:0000259|PROSITE:PS51329};
GN   ORFNames=MARPO_0074s0004 {ECO:0000313|EMBL:PTQ35006.1};
OS   Marchantia polymorpha (Common liverwort) (Marchantia aquatica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=3197 {ECO:0000313|EMBL:PTQ35006.1, ECO:0000313|Proteomes:UP000244005};
RN   [1] {ECO:0000313|Proteomes:UP000244005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 {ECO:0000313|Proteomes:UP000244005};
RX   PubMed=28985561; DOI=10.1016/j.cell.2017.09.030;
RA   Bowman J.L., Kohchi T., Yamato K.T., Jenkins J., Shu S., Ishizaki K.,
RA   Yamaoka S., Nishihama R., Nakamura Y., Berger F., Adam C., Aki S.S.,
RA   Althoff F., Araki T., Arteaga-Vazquez M.A., Balasubrmanian S., Barry K.,
RA   Bauer D., Boehm C.R., Briginshaw L., Caballero-Perez J., Catarino B.,
RA   Chen F., Chiyoda S., Chovatia M., Davies K.M., Delmans M., Demura T.,
RA   Dierschke T., Dolan L., Dorantes-Acosta A.E., Eklund D.M., Florent S.N.,
RA   Flores-Sandoval E., Fujiyama A., Fukuzawa H., Galik B., Grimanelli D.,
RA   Grimwood J., Grossniklaus U., Hamada T., Haseloff J., Hetherington A.J.,
RA   Higo A., Hirakawa Y., Hundley H.N., Ikeda Y., Inoue K., Inoue S.I.,
RA   Ishida S., Jia Q., Kakita M., Kanazawa T., Kawai Y., Kawashima T.,
RA   Kennedy M., Kinose K., Kinoshita T., Kohara Y., Koide E., Komatsu K.,
RA   Kopischke S., Kubo M., Kyozuka J., Lagercrantz U., Lin S.S., Lindquist E.,
RA   Lipzen A.M., Lu C.W., De Luna E., Martienssen R.A., Minamino N.,
RA   Mizutani M., Mizutani M., Mochizuki N., Monte I., Mosher R., Nagasaki H.,
RA   Nakagami H., Naramoto S., Nishitani K., Ohtani M., Okamoto T., Okumura M.,
RA   Phillips J., Pollak B., Reinders A., Rovekamp M., Sano R., Sawa S.,
RA   Schmid M.W., Shirakawa M., Solano R., Spunde A., Suetsugu N., Sugano S.,
RA   Sugiyama A., Sun R., Suzuki Y., Takenaka M., Takezawa D., Tomogane H.,
RA   Tsuzuki M., Ueda T., Umeda M., Ward J.M., Watanabe Y., Yazaki K.,
RA   Yokoyama R., Yoshitake Y., Yotsui I., Zachgo S., Schmutz J.;
RT   "Insights into land plant evolution garnered from the Marchantia polymorpha
RT   genome.";
RL   Cell 171:287-304.e15(2017).
CC   -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659}.
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DR   EMBL; KZ772746; PTQ35006.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R6WMD2; -.
DR   EnsemblPlants; PTQ35006; PTQ35006; MARPO_0074s0004.
DR   Gramene; PTQ35006; PTQ35006; MARPO_0074s0004.
DR   OMA; KSQQTHK; -.
DR   Proteomes; UP000244005; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR   GO; GO:0008179; F:adenylate cyclase binding; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0019933; P:cAMP-mediated signaling; IBA:GO_Central.
DR   Gene3D; 2.160.20.70; -; 1.
DR   Gene3D; 1.25.40.330; Adenylate cyclase-associated CAP, N-terminal domain; 1.
DR   InterPro; IPR001837; Adenylate_cyclase-assoc_CAP.
DR   InterPro; IPR013912; Adenylate_cyclase-assoc_CAP_C.
DR   InterPro; IPR017901; C-CAP_CF_C-like.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR036223; CAP_C_sf.
DR   InterPro; IPR036222; CAP_N_sf.
DR   InterPro; IPR006599; CARP_motif.
DR   PANTHER; PTHR10652; ADENYLYL CYCLASE-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR10652:SF0; ADENYLYL CYCLASE-ASSOCIATED PROTEIN; 1.
DR   Pfam; PF08603; CAP_C; 1.
DR   SMART; SM00673; CARP; 2.
DR   SUPFAM; SSF69340; C-terminal domain of adenylylcyclase associated protein; 1.
DR   SUPFAM; SSF101278; N-terminal domain of adenylylcyclase associated protein, CAP; 1.
DR   PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000244005}.
FT   DOMAIN          360..497
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
FT   REGION          250..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..288
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   520 AA;  54820 MW;  10EE312AF244C7DC CRC64;
     MADAGALEAL VARLERVASL LEGRLETSPA LAKKPDVSSR SISALDLVKE NAKVDSADGA
     ISPSVAAFDE LLKTKLTRVK AAAVKIGGSV LKATEVLESA FAAERNIVLA FSQCKEPNSA
     GLQNLVKPLG EAIQKAHALT EGKRTDAFNH QKVIAESLST LSWVVYTGKD CGLSLPGPHV
     DESWPAAEFY NNKVLVEYKT KDPNHVEWAK AVKDLYIPGL RDYVKKFHTT GPAWNAKGID
     VSQFGMAATK APTAAPSAPP SAPRAPPPPP PPGPPPPPPP PPPPSGLASS SSGPAAPAPA
     ASMSEVFKEL SKGEAVTAGL RKVTDDMKTK NRADRTGAVP AISKSEKEAA VAPVKAVVKK
     PVFELQLGRK WVIEHQVGNK QLNIDDTNPR QSVYVFGCKD SIIHVKGKVN NITVDKSVKT
     ALVFSDVVAA CEIVNCTSVE VQCQGSAPTI AIDNTNGCQL YLSANSLHAS ITTAKSSEVN
     IMVPGATPEA DLVEHALPEQ FLNEFKDGQF ITTPVSHSGG
//
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