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Database: UniProt
Entry: A0A177CZL2_9PLEO
LinkDB: A0A177CZL2_9PLEO
Original site: A0A177CZL2_9PLEO 
ID   A0A177CZL2_9PLEO        Unreviewed;      2158 AA.
AC   A0A177CZL2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-SEP-2017, entry version 10.
DE   SubName: Full=Calcium-channel protein CCH1 {ECO:0000313|EMBL:OAG12945.1};
GN   ORFNames=CC84DRAFT_1255096 {ECO:0000313|EMBL:OAG12945.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Massarineae;
OC   Didymosphaeriaceae; Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG12945.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG12945.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG12945.1,
RC   ECO:0000313|Proteomes:UP000077069};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L.,
RA   Chaput D.L., Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003808};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU003808}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00448}.
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DR   EMBL; KV441548; OAG12945.1; -; Genomic_DNA.
DR   RefSeq; XP_018043310.1; XM_018184505.1.
DR   EnsemblFungi; OAG12945; OAG12945; CC84DRAFT_1255096.
DR   GeneID; 28767991; -.
DR   Proteomes; UP000077069; Unassembled WGS sequence.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU003808};
KW   Calcium channel {ECO:0000256|RuleBase:RU003808};
KW   Calcium transport {ECO:0000256|RuleBase:RU003808};
KW   Complete proteome {ECO:0000313|Proteomes:UP000077069};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU003808};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
FT   TRANSMEM    370    393       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    413    439       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    527    544       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    550    575       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    584    604       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    714    740       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    780    797       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    817    835       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    847    864       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    901    930       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    942    961       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    982   1006       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1209   1230       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1250   1272       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1287   1307       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1345   1366       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1464   1486       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1546   1566       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1578   1596       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1608   1628       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1634   1652       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1664   1688       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1764   1783       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1802   1837       EF-hand. {ECO:0000259|PROSITE:PS50222}.
SQ   SEQUENCE   2158 AA;  243243 MW;  2A13E886F32BB468 CRC64;
     MSSPDPHNNN IHRRSQTHQS IPLRDLHRPP DDHDGERHQG AQQHRQHRRT LSDRGRQLLR
     HSGQLASGQP WNSQYAPIAE TETSPSPTRT RTGGRPQLDT AAGASRRPTH VEDDGDFSPV
     DIGAFQAAIG FSGLGFQGET SPPLGPPMTP AQSYPQYGSD PYLGRSTSED HSFYAASTYD
     DRDTAHLTDA QNLQPVSGAA APLSSTPGNR SSFQSVRFLT PGGSTTGPSL GHDLEQHSPG
     GLRTSTGRKR SLSPGSIESP LHRAGTIMRN MSQRVVNISN EPEIAARTMR RKSSVRHPQD
     RLQEPPSFPA LPTYLHDGPS SPLASPIEKP PSPIEAKSSA QWQRPSNPFR GRSLGIFGPD
     NKLRLKLSDL LVHPVTEPLL LLLIVVQTVL LAVDASKDVY NFPRTKEWGS NDIDYAILGL
     FVVYTLETII RIIVSGFIIN APEYSTINRQ VGFRQAVLGN ARKLFGPQRQ PSIKRAETSI
     EQIPSVFRTF TTAQINPTIG PGNSRDQQRA RLAHRAYLRH SFNRTDFVAV VSFWISFVLG
     LTGVEHDKHI YIFKMLSCLR IIRLLNLTSG TAVILRSLKK AAPLLVNVAF LISFFWLLFA
     IVGVQSFKSS FRRHCVWIDP QGQSNFTNEE QFCGGHLENV PGIHPQPYIP APGMPAGTDK
     GFLCPKGSLC IEGTNPYSGT QSFDNILQSL QLVFVIMSSN TYSDLLYTIA DSDYLIGALF
     FAGGILILSL WLISLLIAVI TSSFQIIREE SKTSAFTGEH IEEEDQDNLP KQRVSNLKKF
     YERTSWVWIL IISYGLIAQA LKSANMSPSR AKFIDRSEIG VTFLLLLEII IRFIVDWRHF
     FRGKQNITDL LIAIITVVIQ IPAIKESHGG RAYAWLSVFQ IIRIYRVVLA VPMTRDLIMI
     VLGNVGGLLN LILFVFLLTF LASIFAAQLF RGEVPPEQDG DTLVVSFFTI YNSFLGMYQI
     LSSENWTTIM YSVTTSTETW GTSWIGATFC IIWFIFANFI VLNMFIAVIQ ENFDVSEDEK
     RLQQVKAFLQ NKEQGFNSSD GNLSLSSIFK LGHASRKDPL DYGSAATEML LKDAVVRDFL
     DDGDDSPHDE EPQPGIRPAP TIVGSGAMST FWQRLKRRIS NREPNPFYAP LDFGRAYEDL
     DPRRMAKEVV DATEKRKKAQ RDYLRKHPNY NVSLFIFRPY NPVRRFCQNI VGPGRGKDRI
     EGVAPSVPIW YTFSAFIYAA IIAMVLLACI TTPLYQREYF KTHEFSVRNW FVWTDLGFAV
     LFTAEALIKV IADGFLFTPN AYFRGSWGFI DGVVLITLWI NVITSLLNEG QITRTVGAFK
     ALRALRLLNI SDSARNHFHS LIVRGWWKLI SAAFVSLSLL IPFAIYGLNL FVGRMQSCND
     DGSNIFDLHD CVSEYDSNPF NDDWNVLAPR RASNPYYDFD NFGNSLFILF QIVSQEGWID
     VMWASEQITG VFTQPAPFAS QGNALYFVIF NLLGAVFVLT LFVSVFMRNY TEQTGVAFLT
     TDQRSWLELR KLLRQVSPSK RPSSTKVRET WEEWCYRRAV RKTGSWQRFI TGLLLAHLVL
     LCLEWYPGYG IWEQVRDYIF LLFTIIFIAN VVIRIIGLSW HRFRKSSWDV FSIFAVSGTF
     VTSILRLTNN SERVFAQLHK LGLVSIALLL IPRNNQLDQL FKTAAASLAS IMNLLATWFV
     LFLVYAIALT QTFGLTRFGE NETGNINFRS VPKALILLFR TSTGEGWNEL MEDFASIDHP
     YCTDGERYFE SDCGSPEWAR ALFVTWNILS MYIFVNLFVS LIYESFSYVY QRSSGLSVIS
     REEIRRFKQA WAEFDPNGTG FITKDQFPRL LGELSGIFEM RIYDGDFTVG SLIEECSTNS
     RRTSGLPVQG QKEPVEIDIK KLNRRLAELP IAEIRRRRMR MNTFYEEVIV SSDPDRGIQF
     TSLLMILAHH KVINDNKSLR LEEFLRRRAR LQRVEEAVRR NVVIGFFDTL YWSRRFRRVQ
     QQKEHGRMTA VPQFTVPEIF IDDEDAVDAE RGQRSITGSP MLSPVHSNTD TGGWRASGSD
     ARAPSPPADM TLRSRANSIQ TTPLGSPTRP NPLSPTRTSP QMSPFSPPPD GEWQFASALS
     RPPSPLEGEG ELAAPSSTGN RSRQNSAVSA ADVLEVLDNS AWGESIRRSF TQRRSGGR
//
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