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Conserved domains on  [gi|1005686841|ref|NP_001307999|]
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prominin-2 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Prominin super family cl25943
Prominin; The prominins are an emerging family of proteins that among the multispan membrane ...
1-461 0e+00

Prominin; The prominins are an emerging family of proteins that among the multispan membrane proteins display a novel topology. Mouse prominin and human prominin (mouse)-like 1 (PROML1) are predicted to contain five membrane spanning domains, with an N-terminal domain exposed to the extracellular space followed by four, alternating small cytoplasmic and large extracellular, loops and a cytoplasmic C-terminal domain. The exact function of prominin is unknown although in humans defects in PROM1, the gene coding for prominin, cause retinal degeneration.


The actual alignment was detected with superfamily member pfam05478:

Pssm-ID: 461660 [Multi-domain]  Cd Length: 799  Bit Score: 680.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005686841   1 MVQEENSTFNALPALAAMQTSSVVQELKKAVAQQPEGVRTLAEGFPgLEAASRWAQALQEVEESSRPYLQEVQRYETYRW 80
Cdd:pfam05478 339 IVQEGLDRFNNIPEKVKNQTAGVVPPLKRALAQIREQIRTLATDIP-RDALSAVSSDIHNTERSSRTFLDVVEKYGSYRW 417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005686841  81 IVGCVLCSVVLFVVLCNLLGLNLGIWGLSARDDPSHPEAKGEAGARFLMAGVGLSFLFAAPLILLVFATFLVGGNVQTLV 160
Cdd:pfam05478 418 LIGLILCSLILLIVVCLLLGLLCGICGLRRTATPTDRGCSKNTGARFLMVGVGLSFLFFWFLMLVVLLYFLVGGNTYTLV 497
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005686841 161 CQSWENGELFEFADTPGNLPpSMNLSQLL--GLRKNISIHQAYQQCKEGAALWTVLQLNDSYDLEEHLDINQYTNKLRQE 238
Cdd:pfam05478 498 CAPWENNELFRFLDTPGLLP-EIDLSRYLpgGLKPNLTISQAYSACKANQSIFTVLRLNNIYDISKLLNISVYTEEIQQE 576
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005686841 239 LQSLKVDTQSLDLLSSAARRDLEALQSSGLQRIHYPDFLVQIQRPVVKTSMEQLAQELQGLAQAQDNSVLGQRLQEEAQG 318
Cdd:pfam05478 577 LENLKVDLSNIDLLTPEERRDLEALRESGLSTIHYSLYLQQLCKPFTKVNLLTLADKLEGLANSLPNGNLKVSLQNEAQD 656
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005686841 319 LRNLHQEKVVPQQSLVAKLNLSVRALESSAPNLQLETSDVLANVTYLKGELPAWAARILRNVSECFLAREMGYFSQYVAW 398
Cdd:pfam05478 657 LRAIHQEFVLPLQSLVAKLNQSVKELDSSNNDLNNSITNLLDAVERAENFLPNNGSSIINNESENLLDRIMGYFEQYIDW 736
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005686841 399 VREEVTQRIATCQPLSGALDNSRVILCDMMADPWNAFWFCLAWCTFFLIPSIIFAVKTSKYFR 461
Cdd:pfam05478 737 VIEEVTENVGHCKPLAYAYDSGVVLLCDRLVDPINAFWFGLGWCTLLLLPSIIFAVKLAKYYR 799
 
Name Accession Description Interval E-value
Prominin pfam05478
Prominin; The prominins are an emerging family of proteins that among the multispan membrane ...
1-461 0e+00

Prominin; The prominins are an emerging family of proteins that among the multispan membrane proteins display a novel topology. Mouse prominin and human prominin (mouse)-like 1 (PROML1) are predicted to contain five membrane spanning domains, with an N-terminal domain exposed to the extracellular space followed by four, alternating small cytoplasmic and large extracellular, loops and a cytoplasmic C-terminal domain. The exact function of prominin is unknown although in humans defects in PROM1, the gene coding for prominin, cause retinal degeneration.


Pssm-ID: 461660 [Multi-domain]  Cd Length: 799  Bit Score: 680.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005686841   1 MVQEENSTFNALPALAAMQTSSVVQELKKAVAQQPEGVRTLAEGFPgLEAASRWAQALQEVEESSRPYLQEVQRYETYRW 80
Cdd:pfam05478 339 IVQEGLDRFNNIPEKVKNQTAGVVPPLKRALAQIREQIRTLATDIP-RDALSAVSSDIHNTERSSRTFLDVVEKYGSYRW 417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005686841  81 IVGCVLCSVVLFVVLCNLLGLNLGIWGLSARDDPSHPEAKGEAGARFLMAGVGLSFLFAAPLILLVFATFLVGGNVQTLV 160
Cdd:pfam05478 418 LIGLILCSLILLIVVCLLLGLLCGICGLRRTATPTDRGCSKNTGARFLMVGVGLSFLFFWFLMLVVLLYFLVGGNTYTLV 497
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005686841 161 CQSWENGELFEFADTPGNLPpSMNLSQLL--GLRKNISIHQAYQQCKEGAALWTVLQLNDSYDLEEHLDINQYTNKLRQE 238
Cdd:pfam05478 498 CAPWENNELFRFLDTPGLLP-EIDLSRYLpgGLKPNLTISQAYSACKANQSIFTVLRLNNIYDISKLLNISVYTEEIQQE 576
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005686841 239 LQSLKVDTQSLDLLSSAARRDLEALQSSGLQRIHYPDFLVQIQRPVVKTSMEQLAQELQGLAQAQDNSVLGQRLQEEAQG 318
Cdd:pfam05478 577 LENLKVDLSNIDLLTPEERRDLEALRESGLSTIHYSLYLQQLCKPFTKVNLLTLADKLEGLANSLPNGNLKVSLQNEAQD 656
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005686841 319 LRNLHQEKVVPQQSLVAKLNLSVRALESSAPNLQLETSDVLANVTYLKGELPAWAARILRNVSECFLAREMGYFSQYVAW 398
Cdd:pfam05478 657 LRAIHQEFVLPLQSLVAKLNQSVKELDSSNNDLNNSITNLLDAVERAENFLPNNGSSIINNESENLLDRIMGYFEQYIDW 736
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005686841 399 VREEVTQRIATCQPLSGALDNSRVILCDMMADPWNAFWFCLAWCTFFLIPSIIFAVKTSKYFR 461
Cdd:pfam05478 737 VIEEVTENVGHCKPLAYAYDSGVVLLCDRLVDPINAFWFGLGWCTLLLLPSIIFAVKLAKYYR 799
 
Name Accession Description Interval E-value
Prominin pfam05478
Prominin; The prominins are an emerging family of proteins that among the multispan membrane ...
1-461 0e+00

Prominin; The prominins are an emerging family of proteins that among the multispan membrane proteins display a novel topology. Mouse prominin and human prominin (mouse)-like 1 (PROML1) are predicted to contain five membrane spanning domains, with an N-terminal domain exposed to the extracellular space followed by four, alternating small cytoplasmic and large extracellular, loops and a cytoplasmic C-terminal domain. The exact function of prominin is unknown although in humans defects in PROM1, the gene coding for prominin, cause retinal degeneration.


Pssm-ID: 461660 [Multi-domain]  Cd Length: 799  Bit Score: 680.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005686841   1 MVQEENSTFNALPALAAMQTSSVVQELKKAVAQQPEGVRTLAEGFPgLEAASRWAQALQEVEESSRPYLQEVQRYETYRW 80
Cdd:pfam05478 339 IVQEGLDRFNNIPEKVKNQTAGVVPPLKRALAQIREQIRTLATDIP-RDALSAVSSDIHNTERSSRTFLDVVEKYGSYRW 417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005686841  81 IVGCVLCSVVLFVVLCNLLGLNLGIWGLSARDDPSHPEAKGEAGARFLMAGVGLSFLFAAPLILLVFATFLVGGNVQTLV 160
Cdd:pfam05478 418 LIGLILCSLILLIVVCLLLGLLCGICGLRRTATPTDRGCSKNTGARFLMVGVGLSFLFFWFLMLVVLLYFLVGGNTYTLV 497
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005686841 161 CQSWENGELFEFADTPGNLPpSMNLSQLL--GLRKNISIHQAYQQCKEGAALWTVLQLNDSYDLEEHLDINQYTNKLRQE 238
Cdd:pfam05478 498 CAPWENNELFRFLDTPGLLP-EIDLSRYLpgGLKPNLTISQAYSACKANQSIFTVLRLNNIYDISKLLNISVYTEEIQQE 576
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005686841 239 LQSLKVDTQSLDLLSSAARRDLEALQSSGLQRIHYPDFLVQIQRPVVKTSMEQLAQELQGLAQAQDNSVLGQRLQEEAQG 318
Cdd:pfam05478 577 LENLKVDLSNIDLLTPEERRDLEALRESGLSTIHYSLYLQQLCKPFTKVNLLTLADKLEGLANSLPNGNLKVSLQNEAQD 656
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005686841 319 LRNLHQEKVVPQQSLVAKLNLSVRALESSAPNLQLETSDVLANVTYLKGELPAWAARILRNVSECFLAREMGYFSQYVAW 398
Cdd:pfam05478 657 LRAIHQEFVLPLQSLVAKLNQSVKELDSSNNDLNNSITNLLDAVERAENFLPNNGSSIINNESENLLDRIMGYFEQYIDW 736
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005686841 399 VREEVTQRIATCQPLSGALDNSRVILCDMMADPWNAFWFCLAWCTFFLIPSIIFAVKTSKYFR 461
Cdd:pfam05478 737 VIEEVTENVGHCKPLAYAYDSGVVLLCDRLVDPINAFWFGLGWCTLLLLPSIIFAVKLAKYYR 799
 
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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