| Analysis | Hit | start | end | length | Note | Hit coverage | Hit length | Hit pident | Hit pcons | eValue | Hit description |
| blastp_kegg | bfu:BC1G_10535 | 1 | 1259 | 1259 | Gaps:23 | 83.01 | 1489 | 94.50 | 0.16 | 0.0 | hypothetical protein |
| ssl:SS1G_04234 | 1 | 1259 | 1259 | Gaps:17 | 87.61 | 1445 | 87.91 | 3.40 | 0.0 | hypothetical protein |
| mgr:MGG_09947 | 1 | 1253 | 1253 | Gaps:46 | 84.93 | 1473 | 60.99 | 12.95 | 0.0 | MG09947.4 hypothetical protein |
| ncr:NCU03263 | 1 | 1241 | 1241 | Gaps:53 | 83.19 | 1493 | 59.98 | 14.65 | 0.0 | similar to transmembrane protein |
| fgr:FG06885.1 | 1 | 1253 | 1253 | Gaps:49 | 83.51 | 1492 | 58.59 | 14.37 | 0.0 | hypothetical protein |
| cim:CIMG_04470 | 1 | 1230 | 1230 | Gaps:23 | 81.52 | 1510 | 57.76 | 16.08 | 0.0 | hypothetical protein |
| nfi:NFIA_114570 | 1 | 1242 | 1242 | Gaps:70 | 82.97 | 1521 | 58.32 | 13.71 | 0.0 | membrane bound C2 domain protein (vp115) putative |
| afm:AFUA_7G01840 | 1 | 1242 | 1242 | Gaps:71 | 82.12 | 1538 | 58.04 | 13.94 | 0.0 | membrane bound C2 domain protein (vp115) |
| afv:AFLA_071000 | 1 | 1242 | 1242 | Gaps:56 | 83.21 | 1507 | 56.78 | 15.31 | 0.0 | membrane bound C2 domain protein (vp115) putative |
| aor:AO090038000561 | 1 | 1242 | 1242 | Gaps:56 | 83.21 | 1507 | 56.78 | 15.23 | 0.0 | Ca2+-dependent lipid-binding protein CLB1/vesicle protein vp115/Granuphilin A contains C2 domain |
| blastp_uniprot_sprot | sp|Q03640|TCB3_YEAST | 1 | 1216 | 1216 | Gaps:129 | 80.45 | 1545 | 29.61 | 20.27 | 1e-141 | Tricalbin-3 OS Saccharomyces cerevisiae GN TCB3 PE 1 SV 1 |
| sp|Q12466|TCB1_YEAST | 3 | 969 | 967 | Gaps:64 | 78.84 | 1186 | 33.05 | 18.93 | 1e-130 | Tricalbin-1 OS Saccharomyces cerevisiae GN TCB1 PE 1 SV 1 |
| sp|P48231|TCB2_YEAST | 3 | 1013 | 1011 | Gaps:75 | 82.85 | 1178 | 30.33 | 21.62 | 1e-117 | Tricalbin-2 OS Saccharomyces cerevisiae GN TCB2 PE 1 SV 1 |
| sp|Q9UT00|YKH3_SCHPO | 1 | 1021 | 1021 | Gaps:55 | 74.78 | 1225 | 35.04 | 22.49 | 1e-113 | Uncharacterized protein PYUK71.03c OS Schizosaccharomyces pombe GN SPAPYUK71.03c PE 1 SV 1 |
| sp|O14065|YC31_SCHPO | 1 | 984 | 984 | Gaps:71 | 65.43 | 1429 | 28.24 | 20.64 | 1e-98 | Uncharacterized protein C962.01 OS Schizosaccharomyces pombe GN SPCC962.01 PE 2 SV 3 |
| sp|Q9USG8|MU190_SCHPO | 3 | 476 | 474 | Gaps:104 | 47.47 | 1188 | 20.92 | 20.39 | 2e-19 | Meiotically up-regulated gene 190 protein OS Schizosaccharomyces pombe GN mug190 PE 1 SV 1 |
| sp|Q9Z1X1|ESYT1_RAT | 1 | 557 | 557 | Gaps:99 | 52.57 | 1088 | 24.83 | 17.48 | 6e-17 | Extended synaptotagmin-1 OS Rattus norvegicus GN Esyt1 PE 2 SV 1 |
| sp|Q3U7R1|ESYT1_MOUSE | 1 | 557 | 557 | Gaps:101 | 52.38 | 1092 | 25.70 | 17.83 | 6e-17 | Extended synaptotagmin-1 OS Mus musculus GN Esyt1 PE 2 SV 2 |
| sp|Q6PFQ7|RASL2_MOUSE | 848 | 976 | 129 | Gaps:15 | 14.21 | 802 | 39.47 | 20.18 | 1e-13 | Ras GTPase-activating protein 4 OS Mus musculus GN Rasa4 PE 2 SV 1 |
| sp|O43374|RASL2_HUMAN | 851 | 970 | 120 | Gaps:12 | 16.19 | 803 | 33.08 | 16.15 | 1e-12 | Ras GTPase-activating protein 4 OS Homo sapiens GN RASA4 PE 2 SV 2 |
| blastp_pdb | 3hn8_C | 851 | 967 | 117 | Gaps:16 | 43.58 | 296 | 36.43 | 17.05 | 1e-09 | mol:protein length:296 Synaptotagmin-3 |
| 3hn8_B | 851 | 967 | 117 | Gaps:16 | 43.58 | 296 | 36.43 | 17.05 | 1e-09 | mol:protein length:296 Synaptotagmin-3 |
| 3hn8_A | 851 | 967 | 117 | Gaps:16 | 43.58 | 296 | 36.43 | 17.05 | 1e-09 | mol:protein length:296 Synaptotagmin-3 |
| 1dqv_A | 851 | 967 | 117 | Gaps:16 | 43.58 | 296 | 36.43 | 17.05 | 1e-09 | mol:protein length:296 SYNAPTOTAGMIN III |
| 1dsy_A | 851 | 931 | 81 | Gaps:5 | 61.87 | 139 | 39.53 | 9.30 | 1e-07 | mol:protein length:139 PROTEIN KINASE C ALPHA TYPE |
| 3gpe_A | 851 | 931 | 81 | Gaps:5 | 62.77 | 137 | 39.53 | 9.30 | 1e-07 | mol:protein length:137 Protein kinase C alpha type |
| 2ep6_A | 843 | 937 | 95 | Gaps:6 | 69.92 | 133 | 43.01 | 15.05 | 1e-07 | mol:protein length:133 MCTP2 protein |
| 2r83_B | 851 | 941 | 91 | Gaps:4 | 33.45 | 284 | 34.74 | 21.05 | 1e-07 | mol:protein length:284 Synaptotagmin-1 |
| 2r83_A | 851 | 941 | 91 | Gaps:4 | 33.45 | 284 | 34.74 | 21.05 | 1e-07 | mol:protein length:284 Synaptotagmin-1 |
| 3f05_A | 851 | 941 | 91 | Gaps:4 | 66.43 | 143 | 33.68 | 21.05 | 4e-07 | mol:protein length:143 Synaptotagmin-1 |
| rpsblast_cdd | gnl|CDD|34643 | 3 | 1025 | 1023 | Gaps:51 | 80.85 | 1227 | 35.28 | 19.05 | 0.0 | COG5038 COG5038 Ca2+-dependent lipid-binding protein contains C2 domain [General function prediction only]. |
| gnl|CDD|176009 | 207 | 621 | 415 | Gaps:13 | 100.00 | 124 | 61.29 | 16.94 | 8e-43 | cd04044 C2A_Tricalbin-like C2 domain first repeat present in Tricalbin-like proteins. 5 to 6 copies of the C2 domain are present in Tricalbin a yeast homolog of Synaptotagmin which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids inositol polyphosphates and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain such as protein kinase C or membrane trafficking proteins which contain at least two C2 domains such as synaptotagmin 1. However there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues primarily aspartates that serve as ligands for calcium ions. This cd contains the first C2 repeat C2A and has a type-II topology. |
| gnl|CDD|176005 | 496 | 967 | 472 | Gaps:2 | 100.00 | 115 | 66.09 | 12.17 | 9e-43 | cd04040 C2D_Tricalbin-like C2 domain fourth repeat present in Tricalbin-like proteins. 5 to 6 copies of the C2 domain are present in Tricalbin a yeast homolog of Synaptotagmin which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids inositol polyphosphates and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain such as protein kinase C or membrane trafficking proteins which contain at least two C2 domains such as synaptotagmin 1. However there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues primarily aspartates that serve as ligands for calcium ions. This cd contains the fifth C2 repeat C2E and has a type-II topology. |
| gnl|CDD|176010 | 208 | 938 | 731 | Gaps:10 | 100.00 | 120 | 61.67 | 25.83 | 8e-41 | cd04045 C2C_Tricalbin-like C2 domain third repeat present in Tricalbin-like proteins. 5 to 6 copies of the C2 domain are present in Tricalbin a yeast homolog of Synaptotagmin which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids inositol polyphosphates and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain such as protein kinase C or membrane trafficking proteins which contain at least two C2 domains such as synaptotagmin 1. However there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues primarily aspartates that serve as ligands for calcium ions. This cd contains the third C2 repeat C2C and has a type-II topology. |
| gnl|CDD|176017 | 361 | 967 | 607 | Gaps:7 | 100.00 | 111 | 57.66 | 18.92 | 1e-33 | cd04052 C2B_Tricalbin-like C2 domain second repeat present in Tricalbin-like proteins. 5 to 6 copies of the C2 domain are present in Tricalbin a yeast homolog of Synaptotagmin which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids inositol polyphosphates and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain such as protein kinase C or membrane trafficking proteins which contain at least two C2 domains such as synaptotagmin 1. However there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues primarily aspartates that serve as ligands for calcium ions. This cd contains the second C2 repeat C2B and has a type-II topology. |
| gnl|CDD|175973 | 210 | 952 | 743 | Gaps:7 | 100.00 | 102 | 73.53 | 20.59 | 3e-23 | cd00030 C2 C2 domain. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids inositol polyphosphates and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain such as protein kinase C or membrane trafficking proteins which contain at least two C2 domains such as synaptotagmin 1. However there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues primarily aspartates that serve as ligands for calcium ions. |
| gnl|CDD|176007 | 492 | 957 | 466 | Gaps:1 | 87.60 | 121 | 51.89 | 20.75 | 5e-19 | cd04042 C2A_MCTP_PRT C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP). MCTPs are involved in Ca2+ signaling at the membrane. MCTP is composed of a variable N-terminal sequence three C2 domains two transmembrane regions (TMRs) and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region the others being synaptotagmins extended synaptotagmins and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids inositol polyphosphates and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain such as protein kinase C or membrane trafficking proteins which contain at least two C2 domains such as synaptotagmin 1. However there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues primarily aspartates that serve as ligands for calcium ions. This cd contains the first C2 repeat C2A and has a type-II topology. |
| gnl|CDD|143935 | 210 | 934 | 725 | Gaps:8 | 100.00 | 85 | 63.53 | 15.29 | 5e-18 | pfam00168 C2 C2 domain. |
| gnl|CDD|175991 | 851 | 963 | 113 | Gaps:15 | 99.19 | 123 | 36.07 | 14.75 | 3e-17 | cd04025 C2B_RasA1_RasA4 C2 domain second repeat present in RasA1 and RasA4. RasA1 and RasA4 are GAP1s (GTPase activating protein 1s ) Ras-specific GAP members which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. Both proteins contain two C2 domains a Ras-GAP domain a plextrin homology (PH)-like domain and a Bruton's Tyrosine Kinase (BTK) zinc binding domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids inositol polyphosphates and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain such as protein kinase C or membrane trafficking proteins which contain at least two C2 domains such as synaptotagmin 1. However there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues primarily aspartates that serve as ligands for calcium ions. This cd contains the second C2 repeat C2B and has a type-I topology. |
| gnl|CDD|128535 | 209 | 938 | 730 | Gaps:8 | 100.00 | 101 | 56.44 | 18.81 | 2e-16 | smart00239 C2 Protein kinase C conserved region 2 (CalB). Ca2+-binding motif present in phospholipases protein kinases C and synaptotamins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids inositol polyphosphates and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles. |
| rpsblast_kog | gnl|CDD|36542 | 848 | 938 | 91 | Gaps:10 | 9.16 | 1103 | 37.62 | 9.90 | 1e-11 | KOG1328 KOG1328 KOG1328 Synaptic vesicle protein BAIAP3 involved in vesicle priming/regulation [Intracellular trafficking secretion and vesicular transport Signal transduction mechanisms]. |
| gnl|CDD|36248 | 204 | 937 | 734 | Gaps:9 | 75.60 | 168 | 45.67 | 18.90 | 4e-11 | KOG1030 KOG1030 KOG1030 Predicted Ca2+-dependent phospholipid-binding protein [General function prediction only]. |
| gnl|CDD|36246 | 356 | 968 | 613 | Gaps:62 | 60.33 | 421 | 44.88 | 15.75 | 4e-10 | KOG1028 KOG1028 KOG1028 Ca2+-dependent phospholipid-binding protein Synaptotagmin required for synaptic vesicle and secretory granule exocytosis [Signal transduction mechanisms Intracellular trafficking secretion and vesicular transport]. |
| gnl|CDD|35915 | 851 | 931 | 81 | Gaps:5 | 12.59 | 683 | 38.37 | 9.30 | 4e-10 | KOG0696 KOG0696 KOG0696 Serine/threonine protein kinase [Signal transduction mechanisms]. |
| gnl|CDD|37270 | 836 | 973 | 138 | Gaps:36 | 31.00 | 800 | 26.21 | 15.32 | 5e-09 | KOG2059 KOG2059 KOG2059 Ras GTPase-activating protein [Signal transduction mechanisms]. |