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Conserved domains on  [gi|79559926|ref|NP_179803|]
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binding protein [Arabidopsis thaliana]

Protein Classification

U-box domain-containing protein( domain architecture ID 11477564)

U-box domain-containing protein contains a modified RING finger and functions as an E3 ubiquitin ligase that mediates the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
49-2150 0e+00

cellulose synthase-interactive protein; Provisional


:

Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 3544.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926    49 RTTSMEDPDGTLASVAQCIEQLRQGSSSAQEREYCLKQLLDLIEMRENAFSAVGSHSQAVPVLVSLLRSGSVGVKIQAAT 128
Cdd:PLN03200    1 RTSEMDDPDGTLASVAQCIEQLRAKSSSPQEKELTTARLLELAKTREEARKAIGSHSQAMPLLVSLLRSGTLGAKVNAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   129 VLGSLCKENELRVKVLLGGCIPPLLGLLKSSSVEGQIAAAKTIYAVSEGGVKDHVGSKIFSTEGVVPVLWDQLRSGNKKG 208
Cdd:PLN03200   81 VLGVLCKEEDLRVKVLLGGCIPPLLSLLKSGSAEAQKAAAEAIYAVSSGGLSDHVGSKIFSTEGVVPSLWDQLQPGNKQD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   209 E-VDGLLTGALKNLSSTTEGFWSETIRAGGVDVLVKLLTSGQSSTLSNVCFLLACMMMEDASVCSSVLTADITKQLLKLL 287
Cdd:PLN03200  161 KvVEGLLTGALRNLCGSTDGFWSATLEAGGVDILVKLLSSGNSDAQANAASLLARLMMAFESSISKVLDAGAVKQLLKLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   288 GSGNEAPVRAEAAAALKSLSAQSKEAKREIANSNGIPVLINATIAPSKEFMQGEYAQALQENAMCALANISGGLSYVISS 367
Cdd:PLN03200  241 GQGNEVSVRAEAAGALEALSSQSKEAKQAIADAGGIPALINATVAPSKEFMQGEFAQALQENAMGALANICGGMSALILY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   368 LGQSLESCSSPAQTADTLGALASALMIYDGKAETTRASDPLVVEQTLLKQFKPRLPFLVQERTIEALASLYGNSILSVKL 447
Cdd:PLN03200  321 LGELSESPRSPAPIADTLGALAYALMVFDSSAESTRAFDPTVIEQILVKLLKPRDTKLVQERIIEALASLYGNAYLSRKL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   448 SNSDAKRLLVGLITMAVNEVQDELVKALLMLCNHEGSLWQALQGREGIQLLISLLGLSSEQQQECAVALLCLLSNENDES 527
Cdd:PLN03200  401 NHAEAKKVLVGLITMATADVQEELIRALSSLCCGKGGLWEALGGREGVQLLISLLGLSSEQQQEYAVALLAILTDEVDES 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   528 KWAITAAGGIPPLVQILETGSAKAREDSATILRNLCNHSEDIRACVESADAVPALLWLLKNGSPNGKEIAAKTLNHLIHK 607
Cdd:PLN03200  481 KWAITAAGGIPPLVQLLETGSQKAKEDSATVLWNLCCHSEDIRACVESAGAVPALLWLLKNGGPKGQEIAAKTLTKLVRT 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   608 SDTATISQLTALLTSDLPESKIYVLDALKSMLSVVPFNDMLREGSASNDAIETMIKLMSSGKEETQANSASALAAIFQSR 687
Cdd:PLN03200  561 ADAATISQLTALLLGDLPESKVHVLDVLGHVLSVASLEDLVREGSAANDALRTLIQLLSSSKEETQEKAASVLADIFSSR 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   688 KDLRESALALKTLLSAIKLLNVDSERILVESCRCLAAILLSIKENRDVAISAREALPTIVSLANSSVLEVAEQGMCALAN 767
Cdd:PLN03200  641 QDLCESLATDEIINPCIKLLTNNTEAVATQSARALAALSRSIKENRKVSYAAEDAIKPLIKLAKSSSIEVAEQAVCALAN 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   768 LILDSEVSEKVIVEDIILSATRILREGTVSGKTLAAAAIARLLSRRRIDSALTDSVNRAGTVLTLVSLLESADGRSDAIS 847
Cdd:PLN03200  721 LLSDPEVAAEALAEDIILPLTRVLREGTLEGKRNAARALAQLLKHFPVDDVLKDSVQCRGTVLALVDLLNSTDLDSSATS 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   848 EALDALAIFSRS-GANGNVKPAWAVLAESPNSMAPIVSSIvSVANPSLQDKAIEVLSRLCRDQPIVLGNMVNNARDCVSS 926
Cdd:PLN03200  801 EALEALALLARTkGGANFSHPPWAVLAEVPSSLEPLVRCL-AEGHPLVQDKAIEILSRLCRDQPVVLGDLIANASKCISS 879
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   927 IAKRVINTRDPKIKIGGAAIIICAAKVDDQKMIENLNETQLCAKFVQALVGILDSvqdqeKDEKDKICICIHPKEKEEDE 1006
Cdd:PLN03200  880 LADRIINSSSLEVKIGGTALLICAAKEHRQLVMEALDESGYLKLLIQALVDMLKQ-----NSKKESLSIEIQTPRGFLES 954
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1007 EEEATENREGSTGATVISGDNLAIWLLSVLSCHDEKSRAVILESEGIELITDRIGNRFL--QADNGEDANIWVCALLLAI 1084
Cdd:PLN03200  955 NLFADGDDFEVPDPATILGGTVALWLLSVIASHDAKSKLAIMEAGGIEVLTEKLASYTSnrQAEFEDSESIWISALLLAI 1034
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1085 LFQDREITRAHATMKAVPVLSNLVKSEEYADRYFAAQALASLVCNGSRGTLLSVANSGAAAGFISLLGCSDDDIKELLQL 1164
Cdd:PLN03200 1035 LFQDRDVVRAPATMRAIPSLANLLKSEETIDRYFAAQALASLVCNGSRGTLLAVANSGAVGGLISLLGCAESDISNLVAL 1114
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1165 SQEFTLVRYPDQVALERLFRVEDIRVGATSRKAIPLLVELLKPIPDRPGAPLLSLNLLTQLAGDCPQNMIVMVESGALEG 1244
Cdd:PLN03200 1115 SEEFSLVRNPDQVALERLFRVEDIRVGATARKAIPLLVDLLKPIPDRPGAPPLALGLLTQLAEGSDVNKLAMAEAGALDA 1194
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1245 LSKYLSLGPQDEQEEAATGLLGILFSSAEIRRHESAFGAVSQLVAVLRLGGRGARYSAAKALDSLFTADHIRNAESSRQA 1324
Cdd:PLN03200 1195 LTKYLSLGPQDSTEEAASELLRILFSSPELRRHESAFGAVNQLVAVLRLGSRSARYSAARALQELFSAEHIRDSELARQA 1274
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1325 VQPLVEILNTGSEREQHAAIAALVRLLSDNPSRALAVADVEMNAVDVLCRILSSNYTMELKGDAAELCYVLFANTRIRST 1404
Cdd:PLN03200 1275 VQPLVEMLNTGSESEQHAAIGALIKLSSGNPSKALAIADVEGNALENLCKILSSDSSLELKEDAAELCRVLFTNTRIRST 1354
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1405 VAAARCVEPLVSLLVTEFSPAQHSVVRALDKLVDDEQLAELVAAHGAVVPLVGLLYGKNYVLHEAISRALVKLGKDRPAC 1484
Cdd:PLN03200 1355 PAAARCIEPLISLLVSESSTAQEAGVCALDRLLDDEQLAELVAAHGAVVPLVGLVVGTNYVLHEAAISALIKLGKDRPPC 1434
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1485 KLEMVKAGVIDCVLDILHEAPDFLCAAFSELLRILTNNATIAKGQSAAKVVEPLFHLLTRLEFGADGQHSALQVLVNILE 1564
Cdd:PLN03200 1435 KLDMVKAGIIERVLDILPEAPDSLCSAIAELLRILTNNSSIAKGQSAAKVVEPLFLLLTRPDLGTWGQHSALQALVNILE 1514
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1565 HPQCRADYTLTPHQVIEPLIPLLESPSPAVQQLAAELLSHLLYEEHLQKDPLTQLAIGPLIHVLGSGIHLLQQRAVKALV 1644
Cdd:PLN03200 1515 KPQCLASLTLTPSQAIEPLIPLLESPSQAVQQLAAELLSHLLAEEHFQQDITTQNAVVPLVRLAGIGILSLQQRAVKALE 1594
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1645 SIALTWPNEIAKEGGVSELSKVILQADPSLSNVLWESAASILVIILQFSSEFYLEVPVAVLVRLLRSASENTVVGALNAL 1724
Cdd:PLN03200 1595 SISLSWPKAVADAGGIFELSKVILQADPQPPHALWESAASVLSNILRFSSEYYFEVPVAVLVKLLRSTSESTVVVALNAL 1674
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1725 LVLESDDGTSAESMAESGAIEALLDLLRSHQCEDTAARLLEVLLNNVKIRDSKATKTAILPLSQYLLDPQTQAQQARLLA 1804
Cdd:PLN03200 1675 LVLERDDSSSAEQMAESGAIEALLELLRSHQCEEAAARLLEALFNNVKVREMKATKYAIAPLSQYLLDPQTRSQQARLLA 1754
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1805 TLALGDLFQNEALARSTDAASACRALVNVLEEQPTEEMKVVAICALQNLVMYSRSNKRAVAEAGGVQVVLDLISSSDPET 1884
Cdd:PLN03200 1755 ALALGDLFQHEGLARSTDAVSACRALVSLLEDQPTEEMKMVAICALQNLVMHSRTNKRAVAEAGGVQVVQELLLSSNPDT 1834
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1885 SVQAAMFVKLLFSNHTVQEYASSETVRAITAAIEKDLWATGTVNDEYLKALNSLFNNFPRLRATEPATLSIPHLVTSLKT 1964
Cdd:PLN03200 1835 SGQAALLIKLLFSNHTIQEYASSELIRALTAALEKDLWSTATVNEEVLRALNVLFSNFPKLRATEAATLCIPHLVGALKS 1914
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1965 GSEATQEAALDALFLLRQAWSACPAEVSRAQSVAAADAIPLLQYLIQSGPPRFQEKAEFLLQCLPGTLVVTIKRGNNMKQ 2044
Cdd:PLN03200 1915 GSEAAQEAALDTLFLLRQSWSAMPAEVARAQAMAAAEAIPVLQMLMKSGPPRFHERAESLLQCLPGSLTVTIKRGNNLKQ 1994
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  2045 SVGNPSVFCKITLGNNPPRQTKVISTGPNPEWDESFSWSFESPPKGQKLHISCKNKSKMGKSSFGKVTIQIDRVVMLGAV 2124
Cdd:PLN03200 1995 SMGNTNAFCKLTLGNGPPRQTKVVSHSSSPEWKEGFTWAFDSPPKGQKLHISCKSKNTFGKSSLGKVTIQIDRVVMEGTY 2074
                        2090      2100
                  ....*....|....*....|....*...
gi 79559926  2125 AGEYSLLPES-KSG-PRNLEIEFQWSNK 2150
Cdd:PLN03200 2075 SGEYSLNPESnKDGsSRTLEIEFQWSNR 2102
 
Name Accession Description Interval E-value
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
49-2150 0e+00

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 3544.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926    49 RTTSMEDPDGTLASVAQCIEQLRQGSSSAQEREYCLKQLLDLIEMRENAFSAVGSHSQAVPVLVSLLRSGSVGVKIQAAT 128
Cdd:PLN03200    1 RTSEMDDPDGTLASVAQCIEQLRAKSSSPQEKELTTARLLELAKTREEARKAIGSHSQAMPLLVSLLRSGTLGAKVNAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   129 VLGSLCKENELRVKVLLGGCIPPLLGLLKSSSVEGQIAAAKTIYAVSEGGVKDHVGSKIFSTEGVVPVLWDQLRSGNKKG 208
Cdd:PLN03200   81 VLGVLCKEEDLRVKVLLGGCIPPLLSLLKSGSAEAQKAAAEAIYAVSSGGLSDHVGSKIFSTEGVVPSLWDQLQPGNKQD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   209 E-VDGLLTGALKNLSSTTEGFWSETIRAGGVDVLVKLLTSGQSSTLSNVCFLLACMMMEDASVCSSVLTADITKQLLKLL 287
Cdd:PLN03200  161 KvVEGLLTGALRNLCGSTDGFWSATLEAGGVDILVKLLSSGNSDAQANAASLLARLMMAFESSISKVLDAGAVKQLLKLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   288 GSGNEAPVRAEAAAALKSLSAQSKEAKREIANSNGIPVLINATIAPSKEFMQGEYAQALQENAMCALANISGGLSYVISS 367
Cdd:PLN03200  241 GQGNEVSVRAEAAGALEALSSQSKEAKQAIADAGGIPALINATVAPSKEFMQGEFAQALQENAMGALANICGGMSALILY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   368 LGQSLESCSSPAQTADTLGALASALMIYDGKAETTRASDPLVVEQTLLKQFKPRLPFLVQERTIEALASLYGNSILSVKL 447
Cdd:PLN03200  321 LGELSESPRSPAPIADTLGALAYALMVFDSSAESTRAFDPTVIEQILVKLLKPRDTKLVQERIIEALASLYGNAYLSRKL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   448 SNSDAKRLLVGLITMAVNEVQDELVKALLMLCNHEGSLWQALQGREGIQLLISLLGLSSEQQQECAVALLCLLSNENDES 527
Cdd:PLN03200  401 NHAEAKKVLVGLITMATADVQEELIRALSSLCCGKGGLWEALGGREGVQLLISLLGLSSEQQQEYAVALLAILTDEVDES 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   528 KWAITAAGGIPPLVQILETGSAKAREDSATILRNLCNHSEDIRACVESADAVPALLWLLKNGSPNGKEIAAKTLNHLIHK 607
Cdd:PLN03200  481 KWAITAAGGIPPLVQLLETGSQKAKEDSATVLWNLCCHSEDIRACVESAGAVPALLWLLKNGGPKGQEIAAKTLTKLVRT 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   608 SDTATISQLTALLTSDLPESKIYVLDALKSMLSVVPFNDMLREGSASNDAIETMIKLMSSGKEETQANSASALAAIFQSR 687
Cdd:PLN03200  561 ADAATISQLTALLLGDLPESKVHVLDVLGHVLSVASLEDLVREGSAANDALRTLIQLLSSSKEETQEKAASVLADIFSSR 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   688 KDLRESALALKTLLSAIKLLNVDSERILVESCRCLAAILLSIKENRDVAISAREALPTIVSLANSSVLEVAEQGMCALAN 767
Cdd:PLN03200  641 QDLCESLATDEIINPCIKLLTNNTEAVATQSARALAALSRSIKENRKVSYAAEDAIKPLIKLAKSSSIEVAEQAVCALAN 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   768 LILDSEVSEKVIVEDIILSATRILREGTVSGKTLAAAAIARLLSRRRIDSALTDSVNRAGTVLTLVSLLESADGRSDAIS 847
Cdd:PLN03200  721 LLSDPEVAAEALAEDIILPLTRVLREGTLEGKRNAARALAQLLKHFPVDDVLKDSVQCRGTVLALVDLLNSTDLDSSATS 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   848 EALDALAIFSRS-GANGNVKPAWAVLAESPNSMAPIVSSIvSVANPSLQDKAIEVLSRLCRDQPIVLGNMVNNARDCVSS 926
Cdd:PLN03200  801 EALEALALLARTkGGANFSHPPWAVLAEVPSSLEPLVRCL-AEGHPLVQDKAIEILSRLCRDQPVVLGDLIANASKCISS 879
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   927 IAKRVINTRDPKIKIGGAAIIICAAKVDDQKMIENLNETQLCAKFVQALVGILDSvqdqeKDEKDKICICIHPKEKEEDE 1006
Cdd:PLN03200  880 LADRIINSSSLEVKIGGTALLICAAKEHRQLVMEALDESGYLKLLIQALVDMLKQ-----NSKKESLSIEIQTPRGFLES 954
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1007 EEEATENREGSTGATVISGDNLAIWLLSVLSCHDEKSRAVILESEGIELITDRIGNRFL--QADNGEDANIWVCALLLAI 1084
Cdd:PLN03200  955 NLFADGDDFEVPDPATILGGTVALWLLSVIASHDAKSKLAIMEAGGIEVLTEKLASYTSnrQAEFEDSESIWISALLLAI 1034
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1085 LFQDREITRAHATMKAVPVLSNLVKSEEYADRYFAAQALASLVCNGSRGTLLSVANSGAAAGFISLLGCSDDDIKELLQL 1164
Cdd:PLN03200 1035 LFQDRDVVRAPATMRAIPSLANLLKSEETIDRYFAAQALASLVCNGSRGTLLAVANSGAVGGLISLLGCAESDISNLVAL 1114
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1165 SQEFTLVRYPDQVALERLFRVEDIRVGATSRKAIPLLVELLKPIPDRPGAPLLSLNLLTQLAGDCPQNMIVMVESGALEG 1244
Cdd:PLN03200 1115 SEEFSLVRNPDQVALERLFRVEDIRVGATARKAIPLLVDLLKPIPDRPGAPPLALGLLTQLAEGSDVNKLAMAEAGALDA 1194
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1245 LSKYLSLGPQDEQEEAATGLLGILFSSAEIRRHESAFGAVSQLVAVLRLGGRGARYSAAKALDSLFTADHIRNAESSRQA 1324
Cdd:PLN03200 1195 LTKYLSLGPQDSTEEAASELLRILFSSPELRRHESAFGAVNQLVAVLRLGSRSARYSAARALQELFSAEHIRDSELARQA 1274
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1325 VQPLVEILNTGSEREQHAAIAALVRLLSDNPSRALAVADVEMNAVDVLCRILSSNYTMELKGDAAELCYVLFANTRIRST 1404
Cdd:PLN03200 1275 VQPLVEMLNTGSESEQHAAIGALIKLSSGNPSKALAIADVEGNALENLCKILSSDSSLELKEDAAELCRVLFTNTRIRST 1354
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1405 VAAARCVEPLVSLLVTEFSPAQHSVVRALDKLVDDEQLAELVAAHGAVVPLVGLLYGKNYVLHEAISRALVKLGKDRPAC 1484
Cdd:PLN03200 1355 PAAARCIEPLISLLVSESSTAQEAGVCALDRLLDDEQLAELVAAHGAVVPLVGLVVGTNYVLHEAAISALIKLGKDRPPC 1434
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1485 KLEMVKAGVIDCVLDILHEAPDFLCAAFSELLRILTNNATIAKGQSAAKVVEPLFHLLTRLEFGADGQHSALQVLVNILE 1564
Cdd:PLN03200 1435 KLDMVKAGIIERVLDILPEAPDSLCSAIAELLRILTNNSSIAKGQSAAKVVEPLFLLLTRPDLGTWGQHSALQALVNILE 1514
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1565 HPQCRADYTLTPHQVIEPLIPLLESPSPAVQQLAAELLSHLLYEEHLQKDPLTQLAIGPLIHVLGSGIHLLQQRAVKALV 1644
Cdd:PLN03200 1515 KPQCLASLTLTPSQAIEPLIPLLESPSQAVQQLAAELLSHLLAEEHFQQDITTQNAVVPLVRLAGIGILSLQQRAVKALE 1594
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1645 SIALTWPNEIAKEGGVSELSKVILQADPSLSNVLWESAASILVIILQFSSEFYLEVPVAVLVRLLRSASENTVVGALNAL 1724
Cdd:PLN03200 1595 SISLSWPKAVADAGGIFELSKVILQADPQPPHALWESAASVLSNILRFSSEYYFEVPVAVLVKLLRSTSESTVVVALNAL 1674
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1725 LVLESDDGTSAESMAESGAIEALLDLLRSHQCEDTAARLLEVLLNNVKIRDSKATKTAILPLSQYLLDPQTQAQQARLLA 1804
Cdd:PLN03200 1675 LVLERDDSSSAEQMAESGAIEALLELLRSHQCEEAAARLLEALFNNVKVREMKATKYAIAPLSQYLLDPQTRSQQARLLA 1754
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1805 TLALGDLFQNEALARSTDAASACRALVNVLEEQPTEEMKVVAICALQNLVMYSRSNKRAVAEAGGVQVVLDLISSSDPET 1884
Cdd:PLN03200 1755 ALALGDLFQHEGLARSTDAVSACRALVSLLEDQPTEEMKMVAICALQNLVMHSRTNKRAVAEAGGVQVVQELLLSSNPDT 1834
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1885 SVQAAMFVKLLFSNHTVQEYASSETVRAITAAIEKDLWATGTVNDEYLKALNSLFNNFPRLRATEPATLSIPHLVTSLKT 1964
Cdd:PLN03200 1835 SGQAALLIKLLFSNHTIQEYASSELIRALTAALEKDLWSTATVNEEVLRALNVLFSNFPKLRATEAATLCIPHLVGALKS 1914
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1965 GSEATQEAALDALFLLRQAWSACPAEVSRAQSVAAADAIPLLQYLIQSGPPRFQEKAEFLLQCLPGTLVVTIKRGNNMKQ 2044
Cdd:PLN03200 1915 GSEAAQEAALDTLFLLRQSWSAMPAEVARAQAMAAAEAIPVLQMLMKSGPPRFHERAESLLQCLPGSLTVTIKRGNNLKQ 1994
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  2045 SVGNPSVFCKITLGNNPPRQTKVISTGPNPEWDESFSWSFESPPKGQKLHISCKNKSKMGKSSFGKVTIQIDRVVMLGAV 2124
Cdd:PLN03200 1995 SMGNTNAFCKLTLGNGPPRQTKVVSHSSSPEWKEGFTWAFDSPPKGQKLHISCKSKNTFGKSSLGKVTIQIDRVVMEGTY 2074
                        2090      2100
                  ....*....|....*....|....*...
gi 79559926  2125 AGEYSLLPES-KSG-PRNLEIEFQWSNK 2150
Cdd:PLN03200 2075 SGEYSLNPESnKDGsSRTLEIEFQWSNR 2102
C2 pfam00168
C2 domain;
2030-2130 4.24e-15

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 73.12  E-value: 4.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   2030 GTLVVTIKRGNN--MKQSVGNPSVFCKITLGNNPPR-QTKVISTGPNPEWDESFSWSFeSPPKGQKLHISCKNKSKMGKS 2106
Cdd:pfam00168    1 GRLTVTVIEAKNlpPKDGNGTSDPYVKVYLLDGKQKkKTKVVKNTLNPVWNETFTFSV-PDPENAVLEIEVYDYDRFGRD 79
                           90       100
                   ....*....|....*....|....*
gi 79559926   2107 SF-GKVTIQIDRVVMLGAVAGEYSL 2130
Cdd:pfam00168   80 DFiGEVRIPLSELDSGEGLDGWYPL 104
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
2032-2122 7.18e-14

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.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 69.40  E-value: 7.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926 2032 LVVTIKRGNNM--KQSVGNPSVFCKITLGNNPPRQTKVISTGPNPEWDESFSWSFEsPPKGQKLHISCKNKSKMGKSSF- 2108
Cdd:cd00030    1 LRVTVIEARNLpaKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVL-DPESDTLTVEVWDKDRFSKDDFl 79
                         90
                 ....*....|....
gi 79559926 2109 GKVTIQIDRVVMLG 2122
Cdd:cd00030   80 GEVEIPLSELLDSG 93
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
2031-2118 3.96e-11

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (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.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 61.73  E-value: 3.96e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926    2031 TLVVTIKRGNNM--KQSVGNPSVFCKITLGNNPP--RQTKVISTGPNPEWDESFSWSFeSPPKGQKLHISCKNKSKMGKS 2106
Cdd:smart00239    1 TLTVKIISARNLppKDKGGKSDPYVKVSLDGDPKekKKTKVVKNTLNPVWNETFEFEV-PPPELAELEIEVYDKDRFGRD 79
                            90
                    ....*....|...
gi 79559926    2107 SF-GKVTIQIDRV 2118
Cdd:smart00239   80 DFiGQVTIPLSDL 92
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
105-165 4.96e-03

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 41.80  E-value: 4.96e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79559926  105 SQAVPVLVSLLRSGSVGVKIQAATVLGSLCKENE-LRVKVLLGGCIPPLLGLLKSSSVEGQI 165
Cdd:COG5064  156 AGAVPLFIQLLSSTEDDVREQAVWALGNIAGDSEgCRDYVLQCGALEPLLGLLLSSAIHISM 217
 
Name Accession Description Interval E-value
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
49-2150 0e+00

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 3544.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926    49 RTTSMEDPDGTLASVAQCIEQLRQGSSSAQEREYCLKQLLDLIEMRENAFSAVGSHSQAVPVLVSLLRSGSVGVKIQAAT 128
Cdd:PLN03200    1 RTSEMDDPDGTLASVAQCIEQLRAKSSSPQEKELTTARLLELAKTREEARKAIGSHSQAMPLLVSLLRSGTLGAKVNAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   129 VLGSLCKENELRVKVLLGGCIPPLLGLLKSSSVEGQIAAAKTIYAVSEGGVKDHVGSKIFSTEGVVPVLWDQLRSGNKKG 208
Cdd:PLN03200   81 VLGVLCKEEDLRVKVLLGGCIPPLLSLLKSGSAEAQKAAAEAIYAVSSGGLSDHVGSKIFSTEGVVPSLWDQLQPGNKQD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   209 E-VDGLLTGALKNLSSTTEGFWSETIRAGGVDVLVKLLTSGQSSTLSNVCFLLACMMMEDASVCSSVLTADITKQLLKLL 287
Cdd:PLN03200  161 KvVEGLLTGALRNLCGSTDGFWSATLEAGGVDILVKLLSSGNSDAQANAASLLARLMMAFESSISKVLDAGAVKQLLKLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   288 GSGNEAPVRAEAAAALKSLSAQSKEAKREIANSNGIPVLINATIAPSKEFMQGEYAQALQENAMCALANISGGLSYVISS 367
Cdd:PLN03200  241 GQGNEVSVRAEAAGALEALSSQSKEAKQAIADAGGIPALINATVAPSKEFMQGEFAQALQENAMGALANICGGMSALILY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   368 LGQSLESCSSPAQTADTLGALASALMIYDGKAETTRASDPLVVEQTLLKQFKPRLPFLVQERTIEALASLYGNSILSVKL 447
Cdd:PLN03200  321 LGELSESPRSPAPIADTLGALAYALMVFDSSAESTRAFDPTVIEQILVKLLKPRDTKLVQERIIEALASLYGNAYLSRKL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   448 SNSDAKRLLVGLITMAVNEVQDELVKALLMLCNHEGSLWQALQGREGIQLLISLLGLSSEQQQECAVALLCLLSNENDES 527
Cdd:PLN03200  401 NHAEAKKVLVGLITMATADVQEELIRALSSLCCGKGGLWEALGGREGVQLLISLLGLSSEQQQEYAVALLAILTDEVDES 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   528 KWAITAAGGIPPLVQILETGSAKAREDSATILRNLCNHSEDIRACVESADAVPALLWLLKNGSPNGKEIAAKTLNHLIHK 607
Cdd:PLN03200  481 KWAITAAGGIPPLVQLLETGSQKAKEDSATVLWNLCCHSEDIRACVESAGAVPALLWLLKNGGPKGQEIAAKTLTKLVRT 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   608 SDTATISQLTALLTSDLPESKIYVLDALKSMLSVVPFNDMLREGSASNDAIETMIKLMSSGKEETQANSASALAAIFQSR 687
Cdd:PLN03200  561 ADAATISQLTALLLGDLPESKVHVLDVLGHVLSVASLEDLVREGSAANDALRTLIQLLSSSKEETQEKAASVLADIFSSR 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   688 KDLRESALALKTLLSAIKLLNVDSERILVESCRCLAAILLSIKENRDVAISAREALPTIVSLANSSVLEVAEQGMCALAN 767
Cdd:PLN03200  641 QDLCESLATDEIINPCIKLLTNNTEAVATQSARALAALSRSIKENRKVSYAAEDAIKPLIKLAKSSSIEVAEQAVCALAN 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   768 LILDSEVSEKVIVEDIILSATRILREGTVSGKTLAAAAIARLLSRRRIDSALTDSVNRAGTVLTLVSLLESADGRSDAIS 847
Cdd:PLN03200  721 LLSDPEVAAEALAEDIILPLTRVLREGTLEGKRNAARALAQLLKHFPVDDVLKDSVQCRGTVLALVDLLNSTDLDSSATS 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   848 EALDALAIFSRS-GANGNVKPAWAVLAESPNSMAPIVSSIvSVANPSLQDKAIEVLSRLCRDQPIVLGNMVNNARDCVSS 926
Cdd:PLN03200  801 EALEALALLARTkGGANFSHPPWAVLAEVPSSLEPLVRCL-AEGHPLVQDKAIEILSRLCRDQPVVLGDLIANASKCISS 879
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   927 IAKRVINTRDPKIKIGGAAIIICAAKVDDQKMIENLNETQLCAKFVQALVGILDSvqdqeKDEKDKICICIHPKEKEEDE 1006
Cdd:PLN03200  880 LADRIINSSSLEVKIGGTALLICAAKEHRQLVMEALDESGYLKLLIQALVDMLKQ-----NSKKESLSIEIQTPRGFLES 954
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1007 EEEATENREGSTGATVISGDNLAIWLLSVLSCHDEKSRAVILESEGIELITDRIGNRFL--QADNGEDANIWVCALLLAI 1084
Cdd:PLN03200  955 NLFADGDDFEVPDPATILGGTVALWLLSVIASHDAKSKLAIMEAGGIEVLTEKLASYTSnrQAEFEDSESIWISALLLAI 1034
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1085 LFQDREITRAHATMKAVPVLSNLVKSEEYADRYFAAQALASLVCNGSRGTLLSVANSGAAAGFISLLGCSDDDIKELLQL 1164
Cdd:PLN03200 1035 LFQDRDVVRAPATMRAIPSLANLLKSEETIDRYFAAQALASLVCNGSRGTLLAVANSGAVGGLISLLGCAESDISNLVAL 1114
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1165 SQEFTLVRYPDQVALERLFRVEDIRVGATSRKAIPLLVELLKPIPDRPGAPLLSLNLLTQLAGDCPQNMIVMVESGALEG 1244
Cdd:PLN03200 1115 SEEFSLVRNPDQVALERLFRVEDIRVGATARKAIPLLVDLLKPIPDRPGAPPLALGLLTQLAEGSDVNKLAMAEAGALDA 1194
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1245 LSKYLSLGPQDEQEEAATGLLGILFSSAEIRRHESAFGAVSQLVAVLRLGGRGARYSAAKALDSLFTADHIRNAESSRQA 1324
Cdd:PLN03200 1195 LTKYLSLGPQDSTEEAASELLRILFSSPELRRHESAFGAVNQLVAVLRLGSRSARYSAARALQELFSAEHIRDSELARQA 1274
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1325 VQPLVEILNTGSEREQHAAIAALVRLLSDNPSRALAVADVEMNAVDVLCRILSSNYTMELKGDAAELCYVLFANTRIRST 1404
Cdd:PLN03200 1275 VQPLVEMLNTGSESEQHAAIGALIKLSSGNPSKALAIADVEGNALENLCKILSSDSSLELKEDAAELCRVLFTNTRIRST 1354
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1405 VAAARCVEPLVSLLVTEFSPAQHSVVRALDKLVDDEQLAELVAAHGAVVPLVGLLYGKNYVLHEAISRALVKLGKDRPAC 1484
Cdd:PLN03200 1355 PAAARCIEPLISLLVSESSTAQEAGVCALDRLLDDEQLAELVAAHGAVVPLVGLVVGTNYVLHEAAISALIKLGKDRPPC 1434
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1485 KLEMVKAGVIDCVLDILHEAPDFLCAAFSELLRILTNNATIAKGQSAAKVVEPLFHLLTRLEFGADGQHSALQVLVNILE 1564
Cdd:PLN03200 1435 KLDMVKAGIIERVLDILPEAPDSLCSAIAELLRILTNNSSIAKGQSAAKVVEPLFLLLTRPDLGTWGQHSALQALVNILE 1514
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1565 HPQCRADYTLTPHQVIEPLIPLLESPSPAVQQLAAELLSHLLYEEHLQKDPLTQLAIGPLIHVLGSGIHLLQQRAVKALV 1644
Cdd:PLN03200 1515 KPQCLASLTLTPSQAIEPLIPLLESPSQAVQQLAAELLSHLLAEEHFQQDITTQNAVVPLVRLAGIGILSLQQRAVKALE 1594
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1645 SIALTWPNEIAKEGGVSELSKVILQADPSLSNVLWESAASILVIILQFSSEFYLEVPVAVLVRLLRSASENTVVGALNAL 1724
Cdd:PLN03200 1595 SISLSWPKAVADAGGIFELSKVILQADPQPPHALWESAASVLSNILRFSSEYYFEVPVAVLVKLLRSTSESTVVVALNAL 1674
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1725 LVLESDDGTSAESMAESGAIEALLDLLRSHQCEDTAARLLEVLLNNVKIRDSKATKTAILPLSQYLLDPQTQAQQARLLA 1804
Cdd:PLN03200 1675 LVLERDDSSSAEQMAESGAIEALLELLRSHQCEEAAARLLEALFNNVKVREMKATKYAIAPLSQYLLDPQTRSQQARLLA 1754
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1805 TLALGDLFQNEALARSTDAASACRALVNVLEEQPTEEMKVVAICALQNLVMYSRSNKRAVAEAGGVQVVLDLISSSDPET 1884
Cdd:PLN03200 1755 ALALGDLFQHEGLARSTDAVSACRALVSLLEDQPTEEMKMVAICALQNLVMHSRTNKRAVAEAGGVQVVQELLLSSNPDT 1834
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1885 SVQAAMFVKLLFSNHTVQEYASSETVRAITAAIEKDLWATGTVNDEYLKALNSLFNNFPRLRATEPATLSIPHLVTSLKT 1964
Cdd:PLN03200 1835 SGQAALLIKLLFSNHTIQEYASSELIRALTAALEKDLWSTATVNEEVLRALNVLFSNFPKLRATEAATLCIPHLVGALKS 1914
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  1965 GSEATQEAALDALFLLRQAWSACPAEVSRAQSVAAADAIPLLQYLIQSGPPRFQEKAEFLLQCLPGTLVVTIKRGNNMKQ 2044
Cdd:PLN03200 1915 GSEAAQEAALDTLFLLRQSWSAMPAEVARAQAMAAAEAIPVLQMLMKSGPPRFHERAESLLQCLPGSLTVTIKRGNNLKQ 1994
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926  2045 SVGNPSVFCKITLGNNPPRQTKVISTGPNPEWDESFSWSFESPPKGQKLHISCKNKSKMGKSSFGKVTIQIDRVVMLGAV 2124
Cdd:PLN03200 1995 SMGNTNAFCKLTLGNGPPRQTKVVSHSSSPEWKEGFTWAFDSPPKGQKLHISCKSKNTFGKSSLGKVTIQIDRVVMEGTY 2074
                        2090      2100
                  ....*....|....*....|....*...
gi 79559926  2125 AGEYSLLPES-KSG-PRNLEIEFQWSNK 2150
Cdd:PLN03200 2075 SGEYSLNPESnKDGsSRTLEIEFQWSNR 2102
C2 pfam00168
C2 domain;
2030-2130 4.24e-15

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 73.12  E-value: 4.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926   2030 GTLVVTIKRGNN--MKQSVGNPSVFCKITLGNNPPR-QTKVISTGPNPEWDESFSWSFeSPPKGQKLHISCKNKSKMGKS 2106
Cdd:pfam00168    1 GRLTVTVIEAKNlpPKDGNGTSDPYVKVYLLDGKQKkKTKVVKNTLNPVWNETFTFSV-PDPENAVLEIEVYDYDRFGRD 79
                           90       100
                   ....*....|....*....|....*
gi 79559926   2107 SF-GKVTIQIDRVVMLGAVAGEYSL 2130
Cdd:pfam00168   80 DFiGEVRIPLSELDSGEGLDGWYPL 104
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
2032-2122 7.18e-14

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.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 69.40  E-value: 7.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926 2032 LVVTIKRGNNM--KQSVGNPSVFCKITLGNNPPRQTKVISTGPNPEWDESFSWSFEsPPKGQKLHISCKNKSKMGKSSF- 2108
Cdd:cd00030    1 LRVTVIEARNLpaKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVL-DPESDTLTVEVWDKDRFSKDDFl 79
                         90
                 ....*....|....
gi 79559926 2109 GKVTIQIDRVVMLG 2122
Cdd:cd00030   80 GEVEIPLSELLDSG 93
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
2031-2118 3.96e-11

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (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.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 61.73  E-value: 3.96e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926    2031 TLVVTIKRGNNM--KQSVGNPSVFCKITLGNNPP--RQTKVISTGPNPEWDESFSWSFeSPPKGQKLHISCKNKSKMGKS 2106
Cdd:smart00239    1 TLTVKIISARNLppKDKGGKSDPYVKVSLDGDPKekKKTKVVKNTLNPVWNETFEFEV-PPPELAELEIEVYDKDRFGRD 79
                            90
                    ....*....|...
gi 79559926    2107 SF-GKVTIQIDRV 2118
Cdd:smart00239   80 DFiGQVTIPLSDL 92
C2B_Synaptotagmin-like cd04050
C2 domain second repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
2032-2113 2.92e-06

C2 domain second repeat present in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. 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.


Pssm-ID: 176015 [Multi-domain]  Cd Length: 105  Bit Score: 47.94  E-value: 2.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926 2032 LVVTIKRGNN--MKQSVGNPSVFCKITLGNNpPRQTKVISTGPNPEWDESFSWsFESPPKGQKLHISCKNKSKmgKSSFG 2109
Cdd:cd04050    2 LFVYLDSAKNlpLAKSTKEPSPYVELTVGKT-TQKSKVKERTNNPVWEEGFTF-LVRNPENQELEIEVKDDKT--GKSLG 77

                 ....
gi 79559926 2110 KVTI 2113
Cdd:cd04050   78 SLTL 81
C2A_Ferlin cd08373
C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
2062-2146 3.31e-06

C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. 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.


Pssm-ID: 176019 [Multi-domain]  Cd Length: 127  Bit Score: 48.40  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926 2062 PRQTKVISTGPNPEWDESFSWSFESPPK-GQKLHISCKNKSKMGKSSF-GKVTIQIDRVVMLGAVAGEYSLLPESKSGPR 2139
Cdd:cd08373   27 KKKTRVLENELNPVWNETFEWPLAGSPDpDESLEIVVKDYEKVGRNRLiGSATVSLQDLVSEGLLEVTEPLLDSNGRPTG 106

                 ....*..
gi 79559926 2140 NlEIEFQ 2146
Cdd:cd08373  107 A-TISLE 112
C2_putative_Elicitor-responsive_gene cd04049
C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive ...
2030-2132 5.43e-05

C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive proteins are triggered in response to specific elicitor molecules such as glycolproteins, peptides, carbohydrates and lipids. A host of defensive responses are also triggered resulting in localized cell death. Antimicrobial secondary metabolites, such as phytoalexins, or defense-related proteins, including pathogenesis-related (PR) proteins are also produced. There is a single C2 domain present here. 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. Members have a type-II topology.


Pssm-ID: 176014 [Multi-domain]  Cd Length: 124  Bit Score: 44.63  E-value: 5.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926 2030 GTLVVTIKRGNNMKQS--VGNPSVFCKITLGNNPpRQTKVIS-TGPNPEWDESFSWSFESPPKGQKLHISCK--NKSKMG 2104
Cdd:cd04049    1 GTLEVLLISAKGLQDTdfLGKIDPYVIIQCRTQE-RKSKVAKgDGRNPEWNEKFKFTVEYPGWGGDTKLILRimDKDNFS 79
                         90       100
                 ....*....|....*....|....*....
gi 79559926 2105 KSSF-GKVTIQIDRVVMLGAVAGEYSLLP 2132
Cdd:cd04049   80 DDDFiGEATIHLKGLFEEGVEPGTAELVP 108
C2_Ras_p21A1 cd08400
C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating ...
2049-2149 8.78e-05

C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating protein 1), a Ras-specific GAP member, 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. RasA1 contains a C2 domain, a Ras-GAP domain, a pleckstrin homology (PH)-like domain, a SH3 domain, and 2 SH2 domains. 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. Members here have a type-I topology.


Pssm-ID: 176045 [Multi-domain]  Cd Length: 126  Bit Score: 44.28  E-value: 8.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926 2049 PSVFCKITLGNNPPRQTKViSTGPNPEWDESFswSFES-PPKGQKLHISCKNKSKMGK-SSFGKVTIQIDRVVMLGAVAG 2126
Cdd:cd08400   22 PHPYCVISLNEVKVARTKV-REGPNPVWSEEF--VFDDlPPDVNSFTISLSNKAKRSKdSEIAEVTVQLSKLQNGQETDE 98
                         90       100
                 ....*....|....*....|....*.
gi 79559926 2127 EYSLLPESKSG---PRNLEIEFQWSN 2149
Cdd:cd08400   99 WYPLSSASPLKggeWGSLRIRARYSH 124
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
2032-2116 1.21e-04

C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The members in this cd are named after the Human C21orf25 which contains a single C2 domain. Several other members contain a C1 domain downstream of the C2 domain. No other information on this protein is currently known. 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.


Pssm-ID: 176060 [Multi-domain]  Cd Length: 126  Bit Score: 43.90  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926 2032 LVVTIKRGNNMKQSVGNPSVFCKITLgNNPPR--QTKVISTGPNPEWDESFswSFESPPKGQKLHISCKNKSKMGKSSF- 2108
Cdd:cd08678    1 LLVKNIKANGLSEAAGSSNPYCVLEM-DEPPQkyQSSTQKNTSNPFWDEHF--LFELSPNSKELLFEVYDNGKKSDSKFl 77

                 ....*...
gi 79559926 2109 GKVTIQID 2116
Cdd:cd08678   78 GLAIVPFD 85
C2B_MCTP_PRT_plant cd08378
C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
2046-2111 3.66e-04

C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset; MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four 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 second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176024 [Multi-domain]  Cd Length: 121  Bit Score: 42.30  E-value: 3.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79559926 2046 VGNPsVFCKITLGNNPpRQTKVISTGPNPEWDESFSWSFESPPkGQKLHISCKNKSKMGKSSFGKV 2111
Cdd:cd08378   15 NSND-PVVEVKLGNYK-GSTKAIERTSNPEWNQVFAFSKDRLQ-GSTLEVSVWDKDKAKDDFLGGV 77
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
524-563 4.80e-04

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 39.36  E-value: 4.80e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 79559926    524 NDESKWAITAAGGIPPLVQILETGSAKAREDSATILRNLC 563
Cdd:pfam00514    1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
C2_Intersectin cd08375
C2 domain present in Intersectin; A single instance of the C2 domain is located C terminally ...
2030-2079 1.53e-03

C2 domain present in Intersectin; A single instance of the C2 domain is located C terminally in the intersectin protein. Intersectin functions as a scaffolding protein, providing a link between the actin cytoskeleton and the components of endocytosis and plays a role in signal transduction. In addition to C2, intersectin contains several additional domains including: Eps15 homology domains, SH3 domains, a RhoGEF domain, and a PH 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. The members here have topology I.


Pssm-ID: 176021 [Multi-domain]  Cd Length: 136  Bit Score: 40.83  E-value: 1.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 79559926 2030 GTLVVTIKRGNNMK--QSVGNPSVFCKITLGNNPpRQTKVISTGPNPEWDES 2079
Cdd:cd08375   15 GRLMVVIVEGRDLKpcNSNGKSDPYCEVSMGSQE-HKTKVVSDTLNPKWNSS 65
C2_ArfGAP cd04038
C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating ...
2029-2109 2.34e-03

C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating protein which regulates the ADP ribosylation factor Arf, a member of the Ras superfamily of GTP-binding proteins. The GTP-bound form of Arf is involved in Golgi morphology and is involved in recruiting coat proteins. ArfGAP is responsible for the GDP-bound form of Arf which is necessary for uncoating the membrane and allowing the Golgi to fuse with an acceptor compartment. These proteins contain an N-terminal ArfGAP domain containing the characteristic zinc finger motif (Cys-x2-Cys-x(16,17)-x2-Cys) and C-terminal C2 domain. C2 domains were first identified in Protein Kinase C (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.


Pssm-ID: 176003 [Multi-domain]  Cd Length: 145  Bit Score: 40.39  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926 2029 PGTLVVTIKRGNN-----MKQSvgNPSVFckITLGNNPPRqTKVISTGPNPEWDESFSWSFESPPKGQKLHISCKNK--- 2100
Cdd:cd04038    1 LGLLKVRVVRGTNlavrdFTSS--DPYVV--LTLGNQKVK-TRVIKKNLNPVWNEELTLSVPNPMAPLKLEVFDKDTfsk 75
                         90
                 ....*....|
gi 79559926 2101 -SKMGKSSFG 2109
Cdd:cd04038   76 dDSMGEAEID 85
HEAT_EZ pfam13513
HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats ...
1552-1605 2.49e-03

HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514). These EZ repeats are found in subunits of cyanobacterial phycocyanin lyase and other proteins and probably carry out a scaffolding role.


Pssm-ID: 463906 [Multi-domain]  Cd Length: 55  Bit Score: 38.12  E-value: 2.49e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 79559926   1552 QHSALQVLVNILEHPQCRADYTLTphQVIEPLIPLLESPSPAVQQLAAELLSHL 1605
Cdd:pfam13513    4 REAAALALGSLAEGGPDLLAPAVP--ELLPALLPLLNDDSDLVREAAAWALGRL 55
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
2032-2130 4.63e-03

C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins are uncharacterized human proteins. They were compiled by the Kazusa mammalian cDNA project which identified more than 2000 human genes. They are identified by 4 digit codes that precede the KIAA designation. Many KIAA genes are still functionally uncharacterized including KIAA1228. 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.


Pssm-ID: 175996 [Multi-domain]  Cd Length: 127  Bit Score: 39.18  E-value: 4.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926 2032 LVVTIKRGNN--MKQSVGNPSVFCKITL----GNNPPRQTKVISTGPNPEWDESFSWSFESPP-KGQKLHISCKNKSKM- 2103
Cdd:cd04030   18 LIVTVHKCRNlpPCDSSDIPDPYVRLYLlpdkSKSTRRKTSVKKDNLNPVFDETFEFPVSLEElKRRTLDVAVKNSKSFl 97
                         90       100
                 ....*....|....*....|....*....
gi 79559926 2104 --GKSSFGKVTIQIDRVVMLGAVAGEYSL 2130
Cdd:cd04030   98 srEKKLLGQVLIDLSDLDLSKGFTQWYDL 126
SRP1 COG5064
Karyopherin (importin) alpha [Intracellular trafficking and secretion];
105-165 4.96e-03

Karyopherin (importin) alpha [Intracellular trafficking and secretion];


Pssm-ID: 227396 [Multi-domain]  Cd Length: 526  Bit Score: 41.80  E-value: 4.96e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79559926  105 SQAVPVLVSLLRSGSVGVKIQAATVLGSLCKENE-LRVKVLLGGCIPPLLGLLKSSSVEGQI 165
Cdd:COG5064  156 AGAVPLFIQLLSSTEDDVREQAVWALGNIAGDSEgCRDYVLQCGALEPLLGLLLSSAIHISM 217
C2B_Synaptotagmin-1 cd08402
C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking ...
2023-2113 6.21e-03

C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 1, a member of the class 1 synaptotagmins, is located in the brain and endocranium and localized to the synaptic vesicles and secretory granules. It functions as a Ca2+ sensor for fast exocytosis. It, like synaptotagmin-2, has an N-glycosylated N-terminus. Synaptotagmin 4, a member of class 4 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmin-11, has an Asp to Ser substitution in its C2A domain. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. 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.


Pssm-ID: 176047 [Multi-domain]  Cd Length: 136  Bit Score: 38.92  E-value: 6.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926 2023 FLLQCLP--GTLVVTIKRGNNMKQ-SVGNPS-VFCKITLGNNPPR----QTKVISTGPNPEWDESFswSFESPP-KGQK- 2092
Cdd:cd08402    6 FSLRYVPtaGKLTVVILEAKNLKKmDVGGLSdPYVKIHLMQNGKRlkkkKTTIKKRTLNPYYNESF--SFEVPFeQIQKv 83
                         90       100
                 ....*....|....*....|...
gi 79559926 2093 -LHISCKNKSKMGKSSF-GKVTI 2113
Cdd:cd08402   84 hLIVTVLDYDRIGKNDPiGKVVL 106
C2A_Synaptotagmin-like cd04024
C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
2065-2147 8.40e-03

C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. 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-I topology.


Pssm-ID: 175990 [Multi-domain]  Cd Length: 128  Bit Score: 38.56  E-value: 8.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79559926 2065 TKVISTGPNPEWDESFSWSFESpPKGQKLHISCKNKSKM-GKSSFGKVTIQIDRVVMLGAVAGEYSLLP-ESKSGPRN-- 2140
Cdd:cd04024   39 TQTIPNTLNPKWNYWCEFPIFS-AQNQLLKLILWDKDRFaGKDYLGEFDIALEEVFADGKTGQSDKWITlKSTRPGKTsv 117
                         90
                 ....*....|.
gi 79559926 2141 ----LEIEFQW 2147
Cdd:cd04024  118 vsgeIHLQFSW 128
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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