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Conserved domains on  [gi|1771853516|ref|NP_001362583|]
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oxygen-regulated protein 1 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 392-510 1.99e-60

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


:

Pssm-ID: 238854  Cd Length: 120  Bit Score: 202.40  E-value: 1.99e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  392 TIYEVNVATGELWNAGTVANVYISIHGEKGDTGSRQLFRSKSSFNFLRGQTDTFFLEAVHLGDLCKIVIGHDGLGPGNGW 471
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1771853516  472 FLDDVVIKDPTTNYEYAFFCHRWLDQGEDDCKIVRELYA 510
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYP 119
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1247-1369 9.93e-52

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


:

Pssm-ID: 238854  Cd Length: 120  Bit Score: 177.75  E-value: 9.93e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1247 VLYEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQSkNNEIKFQRGQVDIFSIKAVSLGKLKKVLISHDGTGPGNG 1326
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKS-NNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1771853516 1327 WFLGSIVVKseDEDSSEEVLFLCNRWLDEYQDDGKTQRELLAE 1369
Cdd:cd01756     80 WFLDKVEIR--EPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 982-1101 5.36e-49

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


:

Pssm-ID: 238854  Cd Length: 120  Bit Score: 169.66  E-value: 5.36e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  982 VRYQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKSNMQVKFQRGQIDKFQVAAVSLGKLQKVLLRCEASDKSQYW 1061
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1771853516 1062 YCEQVIVREPGTTSESIFTCQRWLPFmSQGIIHSEIELYL 1101
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDK-DEDDGQIVRELYP 119
DCX1_RP1 cd17145
Doublecortin-like domain 1 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also ...
 36-114 4.08e-48

Doublecortin-like domain 1 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also termed oxygen-regulated protein 1, is a member of the doublecortin (DCX) family. Its DCX domains occur in double tandem repeats. RP1 is associated with retinitis pigmentosa, which is a type of inherited blindness. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The RP1 protein is expressed in photoreceptors and is required for correct stacking of outer segment discs. It interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


:

Pssm-ID: 340665  Cd Length: 79  Bit Score: 165.76  E-value: 4.08e-48
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853516   36 KRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSRKVPLPFGVRNISTPRGRHSITRLEELEDGESYLCSHGRKVQP 114
Cdd:cd17145      1 KRVCFYKSGDPQFGGLRMVVNSRSFKTFDALLDNLSKKVPLPFGVRNITTPRGVHHITSLEDLEDGKSYICSHQKKVKP 79
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 539-666 7.68e-47

FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ORP1, also called retinitis pigmentosa 1 protein, or retinitis pigmentosa RP1 protein, is a microtubule-associated protein that regulates the stability and length of the microtubule-based axoneme of photoreceptors. It is required for the differentiation of photoreceptor cells. It plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme. Members in this family may contain one or two fibroblast growth factor (FGF) domain(s) in the middle region. The FGF domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


:

Pssm-ID: 466998  Cd Length: 128  Bit Score: 163.90  E-value: 7.68e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  539 KGNTLQFYNKLTGGFVRLHPDGTVDAIGEKTDKYGVFDVIFNKRNICIFQSHEMRHLSLALDNGIVTGMVSGEATTELRV 618
Cdd:cd23312      2 DGNVVQLYSKLTGQALRVKPDGSVDATGDKKDKFAYFRVHKVKGNIRIFQSVANPGYFLAIDDGKVDGNGKGGEDCEFRV 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1771853516  619 LYQPNRCALLESALVPGHTVVFDRHGKIADASSAGYAnLSKEFVIFVK 666
Cdd:cd23312     82 RVQPDRSVTLESVKNPGQFVGFNPDGKPRDPRGTGDG-PNAQFYVYVK 128
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 674-795 4.41e-43

FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ORP1, also called retinitis pigmentosa 1 protein, or retinitis pigmentosa RP1 protein, is a microtubule-associated protein that regulates the stability and length of the microtubule-based axoneme of photoreceptors. It is required for the differentiation of photoreceptor cells. It plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme. Members in this family may contain one or two fibroblast growth factor (FGF) domain(s) in the middle region. The FGF domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


:

Pssm-ID: 466998  Cd Length: 128  Bit Score: 153.12  E-value: 4.41e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  674 VVLLATSL-CQALCLQPDGSCTGVGSQSEK-SYWKVHKISSGICMFESVKNAQMYLRIKDGRCDGTGTGDVDCHFKIKKN 751
Cdd:cd23312      5 VVQLYSKLtGQALRVKPDGSVDATGDKKDKfAYFRVHKVKGNIRIFQSVANPGYFLAIDDGKVDGNGKGGEDCEFRVRVQ 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1771853516  752 lKNASISLESTKSPGLFVGLQSDGQAKPMIYTKDE-NVCFYPQVI 795
Cdd:cd23312     85 -PDRSVTLESVKNPGQFVGFNPDGKPRDPRGTGDGpNAQFYVYVK 128
DCX2_RP1 cd17147
Dublecortin-like domain 2 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also termed ...
 154-229 9.86e-43

Dublecortin-like domain 2 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also termed oxygen-regulated protein 1, is a member of doublecortin (DCX) superfamily that contains double tandem repeats of the DCX domains. RP1 is associated with retinitis pigmentosa, which is a type of inherited blindness. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The RP1 protein is expressed in photoreceptors that is required for correct stacking of outer segment discs. RP1 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


:

Pssm-ID: 340667  Cd Length: 76  Bit Score: 150.29  E-value: 9.86e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853516  154 RSLVVFRNGDPKTRRAVLLSRRVTQSFEAFLQHLTEVMQRPVVKLYATDGRRVPSLQAVILSSGAVVAAGREPFKP 229
Cdd:cd17147      1 RKLIVFKNGDPGFKHTLILNKKTTQSFEALLDHVSELMQFPVVKLYTTDGRRVDSLQALILSSGAVVAAGREPFKP 76
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 265-381 4.86e-35

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


The actual alignment was detected with superfamily member cd01756:

Pssm-ID: 412108  Cd Length: 120  Bit Score: 129.98  E-value: 4.86e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  265 NWKVFIITSDLPDAGTSSQIYIILYGQHRSSAPIYLY-GTDGARFQVGHEDIFTITVGDIGALFKIRIGHTNSGSSPSWH 343
Cdd:cd01756      2 TYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKkSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWF 81

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1771853516  344 CKEIQLHNMNSGKQFYVPVQRWLARDQEDGEICREFPL 381
Cdd:cd01756     82 LDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYP 119
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 1121-1235 9.74e-34

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


The actual alignment was detected with superfamily member cd01756:

Pssm-ID: 412108  Cd Length: 120  Bit Score: 126.13  E-value: 9.74e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1121 WKVTIVTGDLENAGTTATVFLYVYGETKCSGPIILG-SGKHQLFNPNTADIFKINLKDIGEIYKIRIGHDNTGKNPRWYL 1199
Cdd:cd01756      3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKkSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFL 82

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1771853516 1200 EEVRLENIATYELFCLPVDSWIAENENDGDLWKEIP 1235
Cdd:cd01756     83 DKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELY 118
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 858-972 1.61e-25

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


The actual alignment was detected with superfamily member cd01756:

Pssm-ID: 412108  Cd Length: 120  Bit Score: 102.63  E-value: 1.61e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  858 WKVLVLTG---NTGTQANVTLWVYGDKGVTGPISLRKDSSEQLFLPGHEDEFQVEIRNTGNIYKIRIGHDGTSEQPEWNL 934
Cdd:cd01756      3 YEVTVKTGdvkGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFL 82

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1771853516  935 QRVTMQHMKSKKILDFAANVWLSRIQADGDVVCELPVV 972
Cdd:cd01756     83 DKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
 
Name Accession Description Interval E-value
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 392-510 1.99e-60

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 202.40  E-value: 1.99e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  392 TIYEVNVATGELWNAGTVANVYISIHGEKGDTGSRQLFRSKSSFNFLRGQTDTFFLEAVHLGDLCKIVIGHDGLGPGNGW 471
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1771853516  472 FLDDVVIKDPTTNYEYAFFCHRWLDQGEDDCKIVRELYA 510
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYP 119
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1247-1369 9.93e-52

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 177.75  E-value: 9.93e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1247 VLYEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQSkNNEIKFQRGQVDIFSIKAVSLGKLKKVLISHDGTGPGNG 1326
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKS-NNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1771853516 1327 WFLGSIVVKseDEDSSEEVLFLCNRWLDEYQDDGKTQRELLAE 1369
Cdd:cd01756     80 WFLDKVEIR--EPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 982-1101 5.36e-49

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 169.66  E-value: 5.36e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  982 VRYQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKSNMQVKFQRGQIDKFQVAAVSLGKLQKVLLRCEASDKSQYW 1061
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1771853516 1062 YCEQVIVREPGTTSESIFTCQRWLPFmSQGIIHSEIELYL 1101
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDK-DEDDGQIVRELYP 119
DCX1_RP1 cd17145
Doublecortin-like domain 1 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also ...
 36-114 4.08e-48

Doublecortin-like domain 1 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also termed oxygen-regulated protein 1, is a member of the doublecortin (DCX) family. Its DCX domains occur in double tandem repeats. RP1 is associated with retinitis pigmentosa, which is a type of inherited blindness. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The RP1 protein is expressed in photoreceptors and is required for correct stacking of outer segment discs. It interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340665  Cd Length: 79  Bit Score: 165.76  E-value: 4.08e-48
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853516   36 KRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSRKVPLPFGVRNISTPRGRHSITRLEELEDGESYLCSHGRKVQP 114
Cdd:cd17145      1 KRVCFYKSGDPQFGGLRMVVNSRSFKTFDALLDNLSKKVPLPFGVRNITTPRGVHHITSLEDLEDGKSYICSHQKKVKP 79
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 539-666 7.68e-47

FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ORP1, also called retinitis pigmentosa 1 protein, or retinitis pigmentosa RP1 protein, is a microtubule-associated protein that regulates the stability and length of the microtubule-based axoneme of photoreceptors. It is required for the differentiation of photoreceptor cells. It plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme. Members in this family may contain one or two fibroblast growth factor (FGF) domain(s) in the middle region. The FGF domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466998  Cd Length: 128  Bit Score: 163.90  E-value: 7.68e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  539 KGNTLQFYNKLTGGFVRLHPDGTVDAIGEKTDKYGVFDVIFNKRNICIFQSHEMRHLSLALDNGIVTGMVSGEATTELRV 618
Cdd:cd23312      2 DGNVVQLYSKLTGQALRVKPDGSVDATGDKKDKFAYFRVHKVKGNIRIFQSVANPGYFLAIDDGKVDGNGKGGEDCEFRV 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1771853516  619 LYQPNRCALLESALVPGHTVVFDRHGKIADASSAGYAnLSKEFVIFVK 666
Cdd:cd23312     82 RVQPDRSVTLESVKNPGQFVGFNPDGKPRDPRGTGDG-PNAQFYVYVK 128
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 674-795 4.41e-43

FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ORP1, also called retinitis pigmentosa 1 protein, or retinitis pigmentosa RP1 protein, is a microtubule-associated protein that regulates the stability and length of the microtubule-based axoneme of photoreceptors. It is required for the differentiation of photoreceptor cells. It plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme. Members in this family may contain one or two fibroblast growth factor (FGF) domain(s) in the middle region. The FGF domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466998  Cd Length: 128  Bit Score: 153.12  E-value: 4.41e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  674 VVLLATSL-CQALCLQPDGSCTGVGSQSEK-SYWKVHKISSGICMFESVKNAQMYLRIKDGRCDGTGTGDVDCHFKIKKN 751
Cdd:cd23312      5 VVQLYSKLtGQALRVKPDGSVDATGDKKDKfAYFRVHKVKGNIRIFQSVANPGYFLAIDDGKVDGNGKGGEDCEFRVRVQ 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1771853516  752 lKNASISLESTKSPGLFVGLQSDGQAKPMIYTKDE-NVCFYPQVI 795
Cdd:cd23312     85 -PDRSVTLESVKNPGQFVGFNPDGKPRDPRGTGDGpNAQFYVYVK 128
DCX2_RP1 cd17147
Dublecortin-like domain 2 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also termed ...
 154-229 9.86e-43

Dublecortin-like domain 2 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also termed oxygen-regulated protein 1, is a member of doublecortin (DCX) superfamily that contains double tandem repeats of the DCX domains. RP1 is associated with retinitis pigmentosa, which is a type of inherited blindness. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The RP1 protein is expressed in photoreceptors that is required for correct stacking of outer segment discs. RP1 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340667  Cd Length: 76  Bit Score: 150.29  E-value: 9.86e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853516  154 RSLVVFRNGDPKTRRAVLLSRRVTQSFEAFLQHLTEVMQRPVVKLYATDGRRVPSLQAVILSSGAVVAAGREPFKP 229
Cdd:cd17147      1 RKLIVFKNGDPGFKHTLILNKKTTQSFEALLDHVSELMQFPVVKLYTTDGRRVDSLQALILSSGAVVAAGREPFKP 76
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 265-381 4.86e-35

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 129.98  E-value: 4.86e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  265 NWKVFIITSDLPDAGTSSQIYIILYGQHRSSAPIYLY-GTDGARFQVGHEDIFTITVGDIGALFKIRIGHTNSGSSPSWH 343
Cdd:cd01756      2 TYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKkSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWF 81

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1771853516  344 CKEIQLHNMNSGKQFYVPVQRWLARDQEDGEICREFPL 381
Cdd:cd01756     82 LDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYP 119
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1121-1235 9.74e-34

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 126.13  E-value: 9.74e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1121 WKVTIVTGDLENAGTTATVFLYVYGETKCSGPIILG-SGKHQLFNPNTADIFKINLKDIGEIYKIRIGHDNTGKNPRWYL 1199
Cdd:cd01756      3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKkSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFL 82

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1771853516 1200 EEVRLENIATYELFCLPVDSWIAENENDGDLWKEIP 1235
Cdd:cd01756     83 DKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELY 118
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 31-118 1.02e-32

Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the Doublecortin gene product. Proposed to bind tubulin. Doublecortin (DCX) is mutated in human X-linked neuronal migration defects.


Pssm-ID: 214711  Cd Length: 89  Bit Score: 121.98  E-value: 1.02e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516    31 HPVVAKRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSR--KVPLPFGVRNISTPRGRHsITRLEELEDGESYLCSH 108
Cdd:smart00537    1 SLVKPKRIRFYRNGDRFFKGVRLVVNRKRFKSFEALLQDLTEvvKLDLPHGVRKLYTLDGKK-VTSLDELEDGGSYVASG 79

                            90
                    ....*....|
gi 1771853516   109 GRKVQPVDLD 118
Cdd:smart00537   80 TEAFKKVDYG 89
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 858-972 1.61e-25

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 102.63  E-value: 1.61e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  858 WKVLVLTG---NTGTQANVTLWVYGDKGVTGPISLRKDSSEQLFLPGHEDEFQVEIRNTGNIYKIRIGHDGTSEQPEWNL 934
Cdd:cd01756      3 YEVTVKTGdvkGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFL 82

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1771853516  935 QRVTMQHMKSKKILDFAANVWLSRIQADGDVVCELPVV 972
Cdd:cd01756     83 DKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1249-1363 2.28e-19

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 84.79  E-value: 2.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1249 YEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQSKNneiKFQRGQVDIFSIKA-VSLGKLKKVLISHDGTGPGNGW 1327
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNP---DFERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1771853516 1328 FLGSIVVKSEDEDSSeEVLFLCNRWLDEYQDDGKTQ 1363
Cdd:pfam01477   78 FLKSITVEVPGETGG-KYTFPCNSWVYGSKKYKETR 112
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 149-233 3.30e-19

Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the Doublecortin gene product. Proposed to bind tubulin. Doublecortin (DCX) is mutated in human X-linked neuronal migration defects.


Pssm-ID: 214711  Cd Length: 89  Bit Score: 83.46  E-value: 3.30e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516   149 MPRPPRSLVVFRNGDPKTR-RAVLLSRRVTQSFEAFLQHLTEV--MQRP--VVKLYATDGRRVPSLQAVIlSSGAVVAAG 223
Cdd:smart00537    1 SLVKPKRIRFYRNGDRFFKgVRLVVNRKRFKSFEALLQDLTEVvkLDLPhgVRKLYTLDGKKVTSLDELE-DGGSYVASG 79

                            90
                    ....*....|
gi 1771853516   224 REPFKPGNYD 233
Cdd:smart00537   80 TEAFKKVDYG 89
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 394-500 3.08e-18

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 81.71  E-value: 3.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  394 YEVNVATGELWNAGTVANVYISIHGEKGDTGSRQLFRSKSSFNflRGQTDTF-FLEAVHLGDLCKIVIGHDGLGPGNGWF 472
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPDFE--RGAEDSFeIDTDWDVGAILKINLHWDNNGLSDEWF 78

                           90       100
                   ....*....|....*....|....*....
gi 1771853516  473 LDDVVIKDP-TTNYEYAFFCHRWLDQGED 500
Cdd:pfam01477   79 LKSITVEVPgETGGKYTFPCNSWVYGSKK 107
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 266-370 1.88e-17

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 79.40  E-value: 1.88e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  266 WKVFIITSDLPDAGTSSQIYIILYGQHRSSAPIYLYgTDGARFQVGHEDIFTITVG-DIGALFKIRIGHTNSGSSPSWHC 344
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEIT-LDNPDFERGAEDSFEIDTDwDVGAILKINLHWDNNGLSDEWFL 79

                           90       100
                   ....*....|....*....|....*..
gi 1771853516  345 KEIQLH-NMNSGKQFYVPVQRWLARDQ 370
Cdd:pfam01477   80 KSITVEvPGETGGKYTFPCNSWVYGSK 106
DCX pfam03607
Doublecortin;
54-111 1.99e-17

Doublecortin;


Pssm-ID: 460986  Cd Length: 60  Bit Score: 77.49  E-value: 1.99e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516   54 VVNPRSFKSFDALLDNLSRKVP-LPFG-VRNISTPRGrHSITRLEELEDGESYLCSHGRK 111
Cdd:pfam03607    1 VVNKRRFRSFDALLDELTEKVVkLPFGaVRKLYTLDG-KRVTSLDELEDGGVYVAAGREK 59
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 984-1085 1.40e-15

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 74.00  E-value: 1.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  984 YQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKSNMqvKFQRGQIDKFQV-AAVSLGKLQKVLLRCEASDKSQYWY 1062
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNP--DFERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDEWF 78

                           90       100
                   ....*....|....*....|....
gi 1771853516 1063 CEQVIVREPGTT-SESIFTCQRWL 1085
Cdd:pfam01477   79 LKSITVEVPGETgGKYTFPCNSWV 102
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1121-1224 5.84e-14

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 69.21  E-value: 5.84e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  1121 WKVTIVTGDLENAGTTATVFLYVYGETKCSGPIILGSGKHQLFNPNTADIFKINLK-DIGEIYKIRIGHDNtgKNPRWYL 1199
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVDeDFGELGAVKIKNEH--RHPEWFL 80

                            90       100
                    ....*....|....*....|....*
gi 1771853516  1200 EEVRLENIATYELFCLPVDSWIAEN 1224
Cdd:smart00308   81 KSITVKDLPTGGKYHFPCNSWVYPD 105
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1121-1229 9.66e-13

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 65.92  E-value: 9.66e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1121 WKVTIVTGDLENAGTTATVFLYVYGE--TKCSGPIILGSGKhqlFNPNTADIFKINLK-DIGEIYKIRIGHDNTGKNPRW 1197
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKvgESAQLEITLDNPD---FERGAEDSFEIDTDwDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1771853516 1198 YLEEVRLENIATYE---LFClpVDSWIAENENDGD 1229
Cdd:pfam01477   78 FLKSITVEVPGETGgkyTFP--CNSWVYGSKKYKE 110
DCX pfam03607
Doublecortin;
171-227 3.59e-11

Doublecortin;


Pssm-ID: 460986  Cd Length: 60  Bit Score: 59.77  E-value: 3.59e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853516  171 LLSRRVTQSFEAFLQHLTEVMQR----PVVKLYATDGRRVPSLQAvILSSGAVVAAGREPF 227
Cdd:pfam03607    1 VVNKRRFRSFDALLDELTEKVVKlpfgAVRKLYTLDGKRVTSLDE-LEDGGVYVAAGREKF 60
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1249-1356 8.48e-10

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 57.27  E-value: 8.48e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  1249 YEIRIYTGTMTGAETESNVFINLIGTRGDSGKRrlHQSKNNEIKFQRGQVDIFSIK-AVSLGKLKKVLISHDGTGPgnGW 1327
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKES--KLDYLFKGIFARGSTYEFTFDvDEDFGELGAVKIKNEHRHP--EW 78

                            90       100
                    ....*....|....*....|....*....
gi 1771853516  1328 FLGSIVVKSEDEDSseEVLFLCNRWLDEY 1356
Cdd:smart00308   79 FLKSITVKDLPTGG--KYHFPCNSWVYPD 105
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 858-958 2.44e-09

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 56.29  E-value: 2.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  858 WKVLVLTGNT---GTQANVTLWVYGDKGVTGPISLRKDSSEqlFLPGHEDEFQVEIR-NTGNIYKIRIGHDGTSEQPEWN 933
Cdd:pfam01477    1 YQVKVVTGDElgaGTDADVYISLYGKVGESAQLEITLDNPD--FERGAEDSFEIDTDwDVGAILKINLHWDNNGLSDEWF 78

                           90       100
                   ....*....|....*....|....*.
gi 1771853516  934 LQRVT-MQHMKSKKILDFAANVWLSR 958
Cdd:pfam01477   79 LKSITvEVPGETGGKYTFPCNSWVYG 104
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
983-1085 3.92e-08

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 52.64  E-value: 3.92e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516   983 RYQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKsNMQVKFQRGQIDKFQVA-AVSLGKLQKVLLRCEASDKSqyW 1061
Cdd:smart00308    2 KYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDY-LFKGIFARGSTYEFTFDvDEDFGELGAVKIKNEHRHPE--W 78

                            90       100
                    ....*....|....*....|....
gi 1771853516  1062 YCEQVIVREPGTTSESIFTCQRWL 1085
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWV 102
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
392-496 6.31e-08

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 51.87  E-value: 6.31e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516   392 TIYEVNVATGELWNAGTVANVYISIHGEKGDTG-SRQLFRSKSSFNflRGQTDTFFLE-AVHLGDLCKIVIGHDGLGPgn 469
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKeSKLDYLFKGIFA--RGSTYEFTFDvDEDFGELGAVKIKNEHRHP-- 76

                            90       100
                    ....*....|....*....|....*..
gi 1771853516   470 GWFLDDVVIKDPTTNYEYAFFCHRWLD 496
Cdd:smart00308   77 EWFLKSITVKDLPTGGKYHFPCNSWVY 103
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
266-366 1.14e-07

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 51.10  E-value: 1.14e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516   266 WKVFIITSDLPDAGTSSQIYIILYGQH---RSSAPIYLYGTDGARfqvGHEDIFTITV-GDIGALFKIRIghTNSGSSPS 341
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEgdgKESKLDYLFKGIFAR---GSTYEFTFDVdEDFGELGAVKI--KNEHRHPE 77

                            90       100
                    ....*....|....*....|....*
gi 1771853516   342 WHCKEIQLHNMNSGKQFYVPVQRWL 366
Cdd:smart00308   78 WFLKSITVKDLPTGGKYHFPCNSWV 102
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
858-957 3.11e-04

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 41.47  E-value: 3.11e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516   858 WKVLVLTGN---TGTQANVTLWVYG---DKGVTGPISLRKdsseQLFLPG--HEDEFQVEIrNTGNIYKIRIGHDGTseQ 929
Cdd:smart00308    3 YKVTVTTGGldfAGTTASVSLSLVGaegDGKESKLDYLFK----GIFARGstYEFTFDVDE-DFGELGAVKIKNEHR--H 75

                            90       100
                    ....*....|....*....|....*...
gi 1771853516   930 PEWNLQRVTMQHMKSKKILDFAANVWLS 957
Cdd:smart00308   76 PEWFLKSITVKDLPTGGKYHFPCNSWVY 103
FGF pfam00167
Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in ...
 544-578 1.25e-03

Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in growth and differentiation in a wide range of contexts. They are found in a wide range of organizms, from nematodes to humans. Most share an internal core region of high similarity, conserved residues in which are involved in binding with their receptors. On binding, they cause dimerization of their tyrosine kinase receptors leading to intracellular signalling. There are currently four known tyrosine kinase receptors for fibroblast growth factors. These receptors can each bind several different members of this family. Members of this family have a beta trefoil structure. Most have N-terminal signal peptides and are secreted. A few lack signal sequences but are secreted anyway; still others also lack the signal peptide but are found on the cell surface and within the extracellular matrix. A third group remain intracellular. They have central roles in development, regulating cell proliferation, migration and differentiation. On the other hand, they are important in tissue repair following injury in adult organizms.


Pssm-ID: 425498  Cd Length: 124  Bit Score: 40.22  E-value: 1.25e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1771853516  544 QFYNKLTGGFVRLHPDGTVDAIGEKTDKYGVFDVI 578
Cdd:pfam00167    4 RLYCRTGGFHLQILPDGKVDGTGEDGSPYSILEIE 38
 
Name Accession Description Interval E-value
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 392-510 1.99e-60

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 202.40  E-value: 1.99e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  392 TIYEVNVATGELWNAGTVANVYISIHGEKGDTGSRQLFRSKSSFNFLRGQTDTFFLEAVHLGDLCKIVIGHDGLGPGNGW 471
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1771853516  472 FLDDVVIKDPTTNYEYAFFCHRWLDQGEDDCKIVRELYA 510
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYP 119
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1247-1369 9.93e-52

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 177.75  E-value: 9.93e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1247 VLYEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQSkNNEIKFQRGQVDIFSIKAVSLGKLKKVLISHDGTGPGNG 1326
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKS-NNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1771853516 1327 WFLGSIVVKseDEDSSEEVLFLCNRWLDEYQDDGKTQRELLAE 1369
Cdd:cd01756     80 WFLDKVEIR--EPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 982-1101 5.36e-49

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 169.66  E-value: 5.36e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  982 VRYQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKSNMQVKFQRGQIDKFQVAAVSLGKLQKVLLRCEASDKSQYW 1061
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1771853516 1062 YCEQVIVREPGTTSESIFTCQRWLPFmSQGIIHSEIELYL 1101
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDK-DEDDGQIVRELYP 119
DCX1_RP1 cd17145
Doublecortin-like domain 1 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also ...
 36-114 4.08e-48

Doublecortin-like domain 1 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also termed oxygen-regulated protein 1, is a member of the doublecortin (DCX) family. Its DCX domains occur in double tandem repeats. RP1 is associated with retinitis pigmentosa, which is a type of inherited blindness. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The RP1 protein is expressed in photoreceptors and is required for correct stacking of outer segment discs. It interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340665  Cd Length: 79  Bit Score: 165.76  E-value: 4.08e-48
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853516   36 KRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSRKVPLPFGVRNISTPRGRHSITRLEELEDGESYLCSHGRKVQP 114
Cdd:cd17145      1 KRVCFYKSGDPQFGGLRMVVNSRSFKTFDALLDNLSKKVPLPFGVRNITTPRGVHHITSLEDLEDGKSYICSHQKKVKP 79
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 539-666 7.68e-47

FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ORP1, also called retinitis pigmentosa 1 protein, or retinitis pigmentosa RP1 protein, is a microtubule-associated protein that regulates the stability and length of the microtubule-based axoneme of photoreceptors. It is required for the differentiation of photoreceptor cells. It plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme. Members in this family may contain one or two fibroblast growth factor (FGF) domain(s) in the middle region. The FGF domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466998  Cd Length: 128  Bit Score: 163.90  E-value: 7.68e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  539 KGNTLQFYNKLTGGFVRLHPDGTVDAIGEKTDKYGVFDVIFNKRNICIFQSHEMRHLSLALDNGIVTGMVSGEATTELRV 618
Cdd:cd23312      2 DGNVVQLYSKLTGQALRVKPDGSVDATGDKKDKFAYFRVHKVKGNIRIFQSVANPGYFLAIDDGKVDGNGKGGEDCEFRV 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1771853516  619 LYQPNRCALLESALVPGHTVVFDRHGKIADASSAGYAnLSKEFVIFVK 666
Cdd:cd23312     82 RVQPDRSVTLESVKNPGQFVGFNPDGKPRDPRGTGDG-PNAQFYVYVK 128
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 674-795 4.41e-43

FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ORP1, also called retinitis pigmentosa 1 protein, or retinitis pigmentosa RP1 protein, is a microtubule-associated protein that regulates the stability and length of the microtubule-based axoneme of photoreceptors. It is required for the differentiation of photoreceptor cells. It plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme. Members in this family may contain one or two fibroblast growth factor (FGF) domain(s) in the middle region. The FGF domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466998  Cd Length: 128  Bit Score: 153.12  E-value: 4.41e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  674 VVLLATSL-CQALCLQPDGSCTGVGSQSEK-SYWKVHKISSGICMFESVKNAQMYLRIKDGRCDGTGTGDVDCHFKIKKN 751
Cdd:cd23312      5 VVQLYSKLtGQALRVKPDGSVDATGDKKDKfAYFRVHKVKGNIRIFQSVANPGYFLAIDDGKVDGNGKGGEDCEFRVRVQ 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1771853516  752 lKNASISLESTKSPGLFVGLQSDGQAKPMIYTKDE-NVCFYPQVI 795
Cdd:cd23312     85 -PDRSVTLESVKNPGQFVGFNPDGKPRDPRGTGDGpNAQFYVYVK 128
DCX2_RP1 cd17147
Dublecortin-like domain 2 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also termed ...
 154-229 9.86e-43

Dublecortin-like domain 2 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also termed oxygen-regulated protein 1, is a member of doublecortin (DCX) superfamily that contains double tandem repeats of the DCX domains. RP1 is associated with retinitis pigmentosa, which is a type of inherited blindness. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The RP1 protein is expressed in photoreceptors that is required for correct stacking of outer segment discs. RP1 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340667  Cd Length: 76  Bit Score: 150.29  E-value: 9.86e-43
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853516  154 RSLVVFRNGDPKTRRAVLLSRRVTQSFEAFLQHLTEVMQRPVVKLYATDGRRVPSLQAVILSSGAVVAAGREPFKP 229
Cdd:cd17147      1 RKLIVFKNGDPGFKHTLILNKKTTQSFEALLDHVSELMQFPVVKLYTTDGRRVDSLQALILSSGAVVAAGREPFKP 76
DCX1_RP_like cd16110
Doublecortin-like domain 1 found in retinitis pigmentosa (RP)-like protein; RP-like protein ...
 36-110 2.99e-41

Doublecortin-like domain 1 found in retinitis pigmentosa (RP)-like protein; RP-like protein family is part of doublecortin (DCX) family. It has double tandem DCX repeats that are associated with retinitis pigmentosa. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. RP-like proteins are colocalized to the photoreceptor and share a function in outer segment disc morphogenesis.


Pssm-ID: 340527  Cd Length: 75  Bit Score: 145.90  E-value: 2.99e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771853516   36 KRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSRKVPLPFGVRNISTPRGRHSITRLEELEDGESYLCSHGR 110
Cdd:cd16110      1 KNVTFYKDGDVHFSGVRVAINPRRYRTFDALLDELSRKVPLPFGVRSITTPRGRHSITSLEQLEDGGKYVCSSKR 75
DCX1_RP1L1 cd17146
Doublecortin-like domain 1 found in retinitis pigmentosa 1-like 1 (RP1L1) protein; RP1L1 is a ...
 36-114 3.02e-40

Doublecortin-like domain 1 found in retinitis pigmentosa 1-like 1 (RP1L1) protein; RP1L1 is a member of the doublecortin (DCX) family. Its DCX domains occur in double tandem repeats. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX-domain of RP1L1 localizes to the photoreceptor and is genetically associated with retinitis pigmentosa.


Pssm-ID: 340666  Cd Length: 79  Bit Score: 143.05  E-value: 3.02e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853516   36 KRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSRKVPLPFGVRNISTPRGRHSITRLEELEDGESYLCSHGRKVQP 114
Cdd:cd17146      1 KKITFYKSGDPQFGGVKMAVNKRTFKSFSALLDDLSQRVPLPFGVRTITTPRGTHSISRLEQLEDGGCYLCSDKKYVKP 79
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 265-381 4.86e-35

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 129.98  E-value: 4.86e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  265 NWKVFIITSDLPDAGTSSQIYIILYGQHRSSAPIYLY-GTDGARFQVGHEDIFTITVGDIGALFKIRIGHTNSGSSPSWH 343
Cdd:cd01756      2 TYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKkSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWF 81

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1771853516  344 CKEIQLHNMNSGKQFYVPVQRWLARDQEDGEICREFPL 381
Cdd:cd01756     82 LDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYP 119
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1121-1235 9.74e-34

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 126.13  E-value: 9.74e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1121 WKVTIVTGDLENAGTTATVFLYVYGETKCSGPIILG-SGKHQLFNPNTADIFKINLKDIGEIYKIRIGHDNTGKNPRWYL 1199
Cdd:cd01756      3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKkSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFL 82

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1771853516 1200 EEVRLENIATYELFCLPVDSWIAENENDGDLWKEIP 1235
Cdd:cd01756     83 DKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELY 118
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 31-118 1.02e-32

Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the Doublecortin gene product. Proposed to bind tubulin. Doublecortin (DCX) is mutated in human X-linked neuronal migration defects.


Pssm-ID: 214711  Cd Length: 89  Bit Score: 121.98  E-value: 1.02e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516    31 HPVVAKRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSR--KVPLPFGVRNISTPRGRHsITRLEELEDGESYLCSH 108
Cdd:smart00537    1 SLVKPKRIRFYRNGDRFFKGVRLVVNRKRFKSFEALLQDLTEvvKLDLPHGVRKLYTLDGKK-VTSLDELEDGGSYVASG 79

                            90
                    ....*....|
gi 1771853516   109 GRKVQPVDLD 118
Cdd:smart00537   80 TEAFKKVDYG 89
DCX2_RP_like cd17070
Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein ...
 154-222 4.77e-26

Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein family is part of doublecortin (DCX) superfamily with double tandem DCX repeats that are associated with retinitis pigmentosa. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. RP-like proteins are colocalized to the photoreceptor and share a function in outer segment disc morphogenesis.


Pssm-ID: 340590  Cd Length: 69  Bit Score: 102.32  E-value: 4.77e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853516  154 RSLVVFRNGDPKTRRAVLLSRRVTQSFEAFLQHLTEVMQRPVVKLYATDGRRVPSLQAVILSSGAVVAA 222
Cdd:cd17070      1 KVITVISNGDPHSRHTILLNRRTTQSFEQVLQDLSELLKGPVRKLYTTDGKKVESLSALFHGPDEYVAA 69
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 858-972 1.61e-25

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 102.63  E-value: 1.61e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  858 WKVLVLTG---NTGTQANVTLWVYGDKGVTGPISLRKDSSEQLFLPGHEDEFQVEIRNTGNIYKIRIGHDGTSEQPEWNL 934
Cdd:cd01756      3 YEVTVKTGdvkGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWFL 82

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1771853516  935 QRVTMQHMKSKKILDFAANVWLSRIQADGDVVCELPVV 972
Cdd:cd01756     83 DKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 394-510 4.64e-24

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 98.50  E-value: 4.64e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  394 YEVNVATGELWNAGTVANVYISIHGEKGDTGSRqLFRSKSSFNFLRGQTDTFFLE-AVHLGDLCKIVIGHDGLGPGNGWF 472
Cdd:cd01752      3 YLVTVFTGWRRGAGTTAKVTITLYGAEGESEPH-HLRDPEKPIFERGSVDSFLLTtPFPLGELQSIRLWHDNSGLSPSWY 81

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1771853516  473 LDDVVIKDPTTNYEYAFFCHRWLDQGEDDCKIVRELYA 510
Cdd:cd01752     82 LSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPV 119
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 278-380 1.95e-23

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 96.58  E-value: 1.95e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  278 AGTSSQIYIILYGQHRSSAPIYLYGTDGARFQVGHEDIFTITV-GDIGALFKIRIGHTNSGSSPSWHCKEIQLHNMNSGK 356
Cdd:cd01752     15 AGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTpFPLGELQSIRLWHDNSGLSPSWYLSRVIVRDLQTGK 94

                           90       100
                   ....*....|....*....|....
gi 1771853516  357 QFYVPVQRWLARDQEDGEICREFP 380
Cdd:cd01752     95 KWFFLCNDWLSVEEGDGTVERTFP 118
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 1248-1369 3.87e-22

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 93.11  E-value: 3.87e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1248 LYEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQSKNNeiKFQRGQVDIFSIK-AVSLGKLKKVLISHDGTGPGNG 1326
Cdd:cd01752      2 LYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKP--IFERGSVDSFLLTtPFPLGELQSIRLWHDNSGLSPS 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1771853516 1327 WFLGSIVVKseDEDSSEEVLFLCNRWLDEYQDDGKTQRELLAE 1369
Cdd:cd01752     80 WYLSRVIVR--DLQTGKKWFFLCNDWLSVEEGDGTVERTFPVA 120
DCX cd01617
Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin ...
 36-108 1.08e-21

Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin (DCX) is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX gene family consists of eleven paralogs in human and mouse, and its DCX protein domains can occur in double tandem or as single DCX repeats. Proteins with DCX tandem domains in general have roles in microtubule (MT) regulation and signal transduction such as X-linked doublecortin (DCX), retinitis pigmentosa-1 (RP1) and doublecortin-like kinase (DCLK). Single DCX repeat proteins are normally localized to actin-rich subcellular structures, or the nucleus such as DCDC2. DCX is not only a unique MAP in terms of structure, it also interacts with multiple additional proteins. Mutations in human DCX genes are associated with abnormal neuronal migration, epilepsy, and mental retardation.


Pssm-ID: 340456  Cd Length: 73  Bit Score: 89.98  E-value: 1.08e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853516   36 KRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSRKVPL-PFGVRNISTPRGRHsITRLEELEDGESYLCSH 108
Cdd:cd01617      1 KRITVFRNGDKNFKGVKVLVKPRRFRTFDQLLDELTEKLGLpTGGVRKLYTPSGKL-VKSLSDLEDGESYVVCG 73
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 1123-1236 2.18e-21

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 90.80  E-value: 2.18e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1123 VTIVTGDLENAGTTATVFLYVYGETKCSGPIILGSGKHQLFNPNTADIFKIN-LKDIGEIYKIRIGHDNTGKNPRWYLEE 1201
Cdd:cd01752      5 VTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTtPFPLGELQSIRLWHDNSGLSPSWYLSR 84

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1771853516 1202 VRLENIATYELFCLPVDSWIAENENDGDLWKEIPI 1236
Cdd:cd01752     85 VIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPV 119
DCX2_RP1L1 cd17148
Dublecortin-like domain 2 found in retinitis pigmentosa 1-like 1 (RP1L1) protein; RP1L1 is a ...
 154-229 2.58e-21

Dublecortin-like domain 2 found in retinitis pigmentosa 1-like 1 (RP1L1) protein; RP1L1 is a member of doublecortin (DCX) family. Its protein domains occur in tandem repeats. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX-domain of RP1L1 localizes to the photoreceptor and is genetically associated with retinitis pigmentosa.


Pssm-ID: 340668  Cd Length: 76  Bit Score: 89.06  E-value: 2.58e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853516  154 RSLVVFRNGDPKTRRAVLLSRRVTQSFEAFLQHLTEVMQRPVVKLYATDGRRVPSLQAVILSSGAVVAAGREPFKP 229
Cdd:cd17148      1 KKITLVKNGDPDVRRSIILNRRNARNLRTFLDEISDLLQFPVKKLYTLEGRKIDSIQALLHCPSVLVCVGREPFKP 76
DCX1 cd16109
Dublecortin-like domain 1; Members of the doublecortin (DCX) gene family are ...
 35-107 8.02e-21

Dublecortin-like domain 1; Members of the doublecortin (DCX) gene family are microtubule-associated proteins (MAPs). Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX gene family consists of eleven paralogs in human and mouse, and its protein domains can occur in double tandem or single repeats. The family represents the first repeat of the DCX domain which has a stable ubiquitin-like tertiary fold. Proteins with DCX double tandem domains in general have roles in microtubule (MT) regulation and signal transduction such as X-linked doublecortin (DCX), retinitis pigmentosa-1 (RP1) and doublecortin-like kinase (DCLK).


Pssm-ID: 340526  Cd Length: 85  Bit Score: 88.12  E-value: 8.02e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853516   35 AKRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSR----KVPLPFGVRNISTPRGRHSITRLEELEDGESYLCS 107
Cdd:cd16109      2 AKKVRFYRNGDRFFKGIVYAVSSERFRSFEALLADLTRslsdNVNLPQGVRTIFTIDGSRKITSLDELEDGESYVCA 78
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1249-1363 2.28e-19

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 84.79  E-value: 2.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1249 YEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQSKNneiKFQRGQVDIFSIKA-VSLGKLKKVLISHDGTGPGNGW 1327
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNP---DFERGAEDSFEIDTdWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1771853516 1328 FLGSIVVKSEDEDSSeEVLFLCNRWLDEYQDDGKTQ 1363
Cdd:pfam01477   78 FLKSITVEVPGETGG-KYTFPCNSWVYGSKKYKETR 112
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 149-233 3.30e-19

Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the Doublecortin gene product. Proposed to bind tubulin. Doublecortin (DCX) is mutated in human X-linked neuronal migration defects.


Pssm-ID: 214711  Cd Length: 89  Bit Score: 83.46  E-value: 3.30e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516   149 MPRPPRSLVVFRNGDPKTR-RAVLLSRRVTQSFEAFLQHLTEV--MQRP--VVKLYATDGRRVPSLQAVIlSSGAVVAAG 223
Cdd:smart00537    1 SLVKPKRIRFYRNGDRFFKgVRLVVNRKRFKSFEALLQDLTEVvkLDLPhgVRKLYTLDGKKVTSLDELE-DGGSYVASG 79

                            90
                    ....*....|
gi 1771853516   224 REPFKPGNYD 233
Cdd:smart00537   80 TEAFKKVDYG 89
DCX1_DCDC2_like cd17071
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2) and ...
 36-104 1.67e-18

Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2) and similar proteins; DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340591  Cd Length: 80  Bit Score: 81.11  E-value: 1.67e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516   36 KRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSRKVPLPFG-VRNISTPRGRHSITRLEELEDGESY 104
Cdd:cd17071      1 KIIVVYKNGDPFFPGKKFVVNERQVRTFDAFLNEVTSGIKAPFGaVRSIYTPTGGHRVKDLDSLQNGGVY 70
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 394-500 3.08e-18

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 81.71  E-value: 3.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  394 YEVNVATGELWNAGTVANVYISIHGEKGDTGSRQLFRSKSSFNflRGQTDTF-FLEAVHLGDLCKIVIGHDGLGPGNGWF 472
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPDFE--RGAEDSFeIDTDWDVGAILKINLHWDNNGLSDEWF 78

                           90       100
                   ....*....|....*....|....*....
gi 1771853516  473 LDDVVIKDP-TTNYEYAFFCHRWLDQGED 500
Cdd:pfam01477   79 LKSITVEVPgETGGKYTFPCNSWVYGSKK 107
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 394-501 3.87e-18

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


Pssm-ID: 238061  Cd Length: 116  Bit Score: 81.62  E-value: 3.87e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  394 YEVNVATGELWNAGTVANVYISIHGEKGDTGsrQLFRSKSSFNFLRGQTDTFFLEA-VHLGDLCKIVIGHDGLGPGNGWF 472
Cdd:cd00113      3 YTVTIKTGDKKGAGTDSNISLALYGENGNSS--DIPILDGPGSFERGSTDTFQIDLkLDIGDITKVYLRRDGSGLSDGWY 80

                           90       100
                   ....*....|....*....|....*....
gi 1771853516  473 LDDVVIKDPTTNYEYAFFCHRWLDQGEDD 501
Cdd:cd00113     81 CESITVQALGTKKVYTFPVNRWVLGGKWY 109
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 1119-1221 1.60e-17

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


Pssm-ID: 238061  Cd Length: 116  Bit Score: 79.69  E-value: 1.60e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1119 GDWKVTIVTGDLENAGTTATVFLYVYGETKCSGPIILgSGKHQLFNPNTADIFKINLK-DIGEIYKIRIGHDNTGKNPRW 1197
Cdd:cd00113      1 CRYTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPI-LDGPGSFERGSTDTFQIDLKlDIGDITKVYLRRDGSGLSDGW 79

                           90       100
                   ....*....|....*....|....
gi 1771853516 1198 YLEEVRLENIATYELFCLPVDSWI 1221
Cdd:cd00113     80 YCESITVQALGTKKVYTFPVNRWV 103
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 266-370 1.88e-17

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 79.40  E-value: 1.88e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  266 WKVFIITSDLPDAGTSSQIYIILYGQHRSSAPIYLYgTDGARFQVGHEDIFTITVG-DIGALFKIRIGHTNSGSSPSWHC 344
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEIT-LDNPDFERGAEDSFEIDTDwDVGAILKINLHWDNNGLSDEWFL 79

                           90       100
                   ....*....|....*....|....*..
gi 1771853516  345 KEIQLH-NMNSGKQFYVPVQRWLARDQ 370
Cdd:pfam01477   80 KSITVEvPGETGGKYTFPCNSWVYGSK 106
DCX pfam03607
Doublecortin;
54-111 1.99e-17

Doublecortin;


Pssm-ID: 460986  Cd Length: 60  Bit Score: 77.49  E-value: 1.99e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516   54 VVNPRSFKSFDALLDNLSRKVP-LPFG-VRNISTPRGrHSITRLEELEDGESYLCSHGRK 111
Cdd:pfam03607    1 VVNKRRFRSFDALLDELTEKVVkLPFGaVRKLYTLDG-KRVTSLDELEDGGVYVAAGREK 59
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 265-366 4.06e-17

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


Pssm-ID: 238061  Cd Length: 116  Bit Score: 78.53  E-value: 4.06e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  265 NWKVFIITSDLPDAGTSSQIYIILYGQHRSSAPIYLygTDG-ARFQVGHEDIFTITVG-DIGALFKIRIGHTNSGSSPSW 342
Cdd:cd00113      2 RYTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPI--LDGpGSFERGSTDTFQIDLKlDIGDITKVYLRRDGSGLSDGW 79

                           90       100
                   ....*....|....*....|....
gi 1771853516  343 HCKEIQLHNMNSGKQFYVPVQRWL 366
Cdd:cd00113     80 YCESITVQALGTKKVYTFPVNRWV 103
DCX1_DCLK2 cd17141
Dublecortin-like domain 1 found in doublecortin-like kinase 2 (DCLK2); DCLK2 is a member of ...
 35-107 1.25e-16

Dublecortin-like domain 1 found in doublecortin-like kinase 2 (DCLK2); DCLK2 is a member of doublecortin (DCX) protein superfamily that functions as a microtubule-associated protein (MAP), and contains two conserved tubulin binding domains, which typically occur in tandem. The DCX domain has a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier (Ubiquitination) in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. In addition to microtubule binding domains, DCLK encodes a serine/threonine kinase-domain that is similar to Ca/calmodulin-dependent (Cam) protein kinases. Molecular actions of DCX members are less well characterized and it shows that DCLK2 members regulate cyclic AMP signaling. Unlike DCX, this DCLK has varying levels of expression throughout embryonic and adult life.


Pssm-ID: 340661  Cd Length: 85  Bit Score: 76.10  E-value: 1.25e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853516   35 AKRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSR----KVPLPFGVRNISTPRGRHSITRLEELEDGESYLCS 107
Cdd:cd17141      2 AKKVRFYRNGDRYFKGLVYAVSSDRFRSFDALLMELTRslsdNVNLPQGVRTIYTIDGSKKITSLDELLEGESYVCA 78
DCX1_DCX cd16112
Dublecortin-like domain 1 found in neuronal migration protein doublecortin (DCX); DCX, also ...
 35-116 2.81e-16

Dublecortin-like domain 1 found in neuronal migration protein doublecortin (DCX); DCX, also termed doublin or lissencephalin-X (Lis-XDCX), is a microtubule-associated protein (MAP). It belongs to the doublecortin (DCX) family, has double tandem DCX repeats, and is expressed in migrating neurons. Structure studies show that the N-terminal DCX domain has a stable ubiquitin-like fold. DCX is not only a unique MAP in terms of structure, it also interacts with multiple additional proteins. Mutations in the human DCX genes are associated with abnormal neuronal migration, epilepsy, and mental retardation.


Pssm-ID: 340529  Cd Length: 89  Bit Score: 75.34  E-value: 2.81e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516   35 AKRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSRK----VPLPFGVRNISTPRGRHSITRLEELEDGESYLCSHGR 110
Cdd:cd16112      2 AKKVRFYRNGDRYFKGIVYAVSSDRFRSFDALLADLTRSlsdnINLPQGVRYIYTIDGSRKIGSMDELEEGESYVCSSDN 81


                   ....*.
gi 1771853516  111 KVQPVD 116
Cdd:cd16112     82 FFKKVE 87
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 983-1085 3.44e-16

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 76.16  E-value: 3.44e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  983 RYQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKSNMQVkFQRGQIDKFQVA-AVSLGKLQKVLLRCEASDKSQYW 1061
Cdd:cd01752      2 LYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPI-FERGSVDSFLLTtPFPLGELQSIRLWHDNSGLSPSW 80

                           90       100
                   ....*....|....*....|....
gi 1771853516 1062 YCEQVIVREPGTTSESIFTCQRWL 1085
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWL 104
DCX1_DCLK1 cd17140
Dublecortin-like domain 1 found in doublecortin-like kinase 1 (DCLK1); DCLK1 is a member of ...
 35-107 1.20e-15

Dublecortin-like domain 1 found in doublecortin-like kinase 1 (DCLK1); DCLK1 is a member of doublecortin (DCX) protein superfamily that functions as a microtubule-associated protein (MAP), and contains two conserved tubulin binding domains. The DCX domain has a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. In addition to microtubule-binding domains, DCLK encodes a serine/threonine kinase domain that is similar to Ca/calmodulin-dependent (Cam) protein kinases. DCLK1 appears to regulate cyclic AMP signaling and is involved in neuronal migration, retrograde transport, neuronal apoptosis and neurogenesis. Unlike DCX, this DCLK has varying levels of expression throughout embryonic and adult life.


Pssm-ID: 340660  Cd Length: 89  Bit Score: 73.50  E-value: 1.20e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1771853516   35 AKRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSR----KVPLPFGVRNISTPRGRHSITRLEELEDGESYLCS 107
Cdd:cd17140      2 AKKVRFYRNGDRYFKGIVYAISPDRFRSFEALLADLTRtlsdNVNLPQGVRTIYTIDGLKKISSLDQLVEGESYVCG 78
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 984-1085 1.40e-15

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 74.00  E-value: 1.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  984 YQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKSNMqvKFQRGQIDKFQV-AAVSLGKLQKVLLRCEASDKSQYWY 1062
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNP--DFERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDEWF 78

                           90       100
                   ....*....|....*....|....
gi 1771853516 1063 CEQVIVREPGTT-SESIFTCQRWL 1085
Cdd:pfam01477   79 LKSITVEVPGETgGKYTFPCNSWV 102
DCX1_DCDC2 cd17149
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is ...
 36-105 1.95e-15

Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340669  Cd Length: 80  Bit Score: 72.50  E-value: 1.95e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853516   36 KRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSRKVPLPFG-VRNISTPRGRHSITRLEELEDGESYL 105
Cdd:cd17149      1 KNVLVYRNGDPFYAGRRLVINEKRVSSFEVFLKEVTGGVQAPFGaVRNIYTPRGGHRVRSLEQLQSGEQYV 71
DCX1_DCDC2C cd17151
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2C (DCDC2C); DCDC2 ...
 36-111 8.01e-15

Dublecortin-like domain 1 found in doublecortin domain-containing protein 2C (DCDC2C); DCDC2 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340671  Cd Length: 79  Bit Score: 70.59  E-value: 8.01e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853516   36 KRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSRKVPLPFGVRNISTPRGRHSITRLEELEDGESYLCSHGRK 111
Cdd:cd17151      1 KTILVYRNGDPFYQAHKVVIHRRRVKTFDALLRQLTETVKVPFGVRCLYTPRNGHRVKGLDDLQGGGKYVAAGRER 76
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 857-957 1.02e-14

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


Pssm-ID: 238061  Cd Length: 116  Bit Score: 71.60  E-value: 1.02e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  857 EWKVLVLTGN---TGTQANVTLWVYGDKGVTGPISLRKDSSEqlFLPGHEDEFQVEIR-NTGNIYKIRIGHDGTSEQPEW 932
Cdd:cd00113      2 RYTVTIKTGDkkgAGTDSNISLALYGENGNSSDIPILDGPGS--FERGSTDTFQIDLKlDIGDITKVYLRRDGSGLSDGW 79

                           90       100
                   ....*....|....*....|....*
gi 1771853516  933 NLQRVTMQHMKSKKILDFAANVWLS 957
Cdd:cd00113     80 YCESITVQALGTKKVYTFPVNRWVL 104
DCX1_DCDC2B cd17150
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2B (DCDC2B); DCDC2 ...
 36-105 1.50e-14

Dublecortin-like domain 1 found in doublecortin domain-containing protein 2B (DCDC2B); DCDC2 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340670  Cd Length: 79  Bit Score: 69.83  E-value: 1.50e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516   36 KRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSRKVPLPFGVRNISTPRGRHSITRLEELEDGESYL 105
Cdd:cd17150      1 KNVVVYRNGDPFFTGRKFVVNQRQFLTFEAFLNEVTSNIQAPVAVRNLYTPREGHRVTELGDLQNGGHYV 70
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 983-1086 5.01e-14

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


Pssm-ID: 238061  Cd Length: 116  Bit Score: 69.68  E-value: 5.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  983 RYQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKSNmqVKFQRGQIDKFQVAA-VSLGKLQKVLLRCEASDKSQYW 1061
Cdd:cd00113      2 RYTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILDGP--GSFERGSTDTFQIDLkLDIGDITKVYLRRDGSGLSDGW 79

                           90       100
                   ....*....|....*....|....*
gi 1771853516 1062 YCEQVIVREPGTTSESIFTCQRWLP 1086
Cdd:cd00113     80 YCESITVQALGTKKVYTFPVNRWVL 104
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 860-971 5.56e-14

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 69.61  E-value: 5.56e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  860 VLVLTG---NTGTQANVTLWVYGDKGVTGPISLRkDSSEQLFLPGHEDEFQVEI-RNTGNIYKIRIGHDGTSEQPEWNLQ 935
Cdd:cd01752      5 VTVFTGwrrGAGTTAKVTITLYGAEGESEPHHLR-DPEKPIFERGSVDSFLLTTpFPLGELQSIRLWHDNSGLSPSWYLS 83

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1771853516  936 RVTMQHMKSKKILDFAANVWLSRIQADGDVVCELPV 971
Cdd:cd01752     84 RVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPV 119
DCX cd01617
Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin ...
 154-222 5.56e-14

Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin (DCX) is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX gene family consists of eleven paralogs in human and mouse, and its DCX protein domains can occur in double tandem or as single DCX repeats. Proteins with DCX tandem domains in general have roles in microtubule (MT) regulation and signal transduction such as X-linked doublecortin (DCX), retinitis pigmentosa-1 (RP1) and doublecortin-like kinase (DCLK). Single DCX repeat proteins are normally localized to actin-rich subcellular structures, or the nucleus such as DCDC2. DCX is not only a unique MAP in terms of structure, it also interacts with multiple additional proteins. Mutations in human DCX genes are associated with abnormal neuronal migration, epilepsy, and mental retardation.


Pssm-ID: 340456  Cd Length: 73  Bit Score: 68.03  E-value: 5.56e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1771853516  154 RSLVVFRNGDPKTRRA-VLLSRRVTQSFEAFLQHLTEVMQ---RPVVKLYATDGRRVPSLQAVILSSGAVVAA 222
Cdd:cd01617      1 KRITVFRNGDKNFKGVkVLVKPRRFRTFDQLLDELTEKLGlptGGVRKLYTPSGKLVKSLSDLEDGESYVVCG 73
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1121-1224 5.84e-14

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 69.21  E-value: 5.84e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  1121 WKVTIVTGDLENAGTTATVFLYVYGETKCSGPIILGSGKHQLFNPNTADIFKINLK-DIGEIYKIRIGHDNtgKNPRWYL 1199
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVDeDFGELGAVKIKNEH--RHPEWFL 80

                            90       100
                    ....*....|....*....|....*
gi 1771853516  1200 EEVRLENIATYELFCLPVDSWIAEN 1224
Cdd:smart00308   81 KSITVKDLPTGGKYHFPCNSWVYPD 105
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 1249-1364 2.07e-13

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


Pssm-ID: 238061  Cd Length: 116  Bit Score: 68.13  E-value: 2.07e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1249 YEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQsknNEIKFQRGQVDIFSIKA-VSLGKLKKVLISHDGTGPGNGW 1327
Cdd:cd00113      3 YTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILD---GPGSFERGSTDTFQIDLkLDIGDITKVYLRRDGSGLSDGW 79

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1771853516 1328 FLGSIVVKSedEDSSEEVLFLCNRWLDEYQDDGKTQR 1364
Cdd:cd00113     80 YCESITVQA--LGTKKVYTFPVNRWVLGGKWYTSVRS 114
beta-trefoil_FGF cd00058
FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) ...
 541-664 3.24e-13

FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) superfamily; The FGF superfamily includes FGF1-23 and similar proteins. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. They play essential roles in patterning and differentiation during vertebrate embryogenesis and have neurotrophic activities. FGFs have a high affinity for heparan sulfate proteoglycans and require heparan sulfate to activate one of four cell surface FGF receptors. Upon binding to FGF, the receptors dimerize, and their intracellular tyrosine kinase domains become active. The structure of FGFs is typical of the beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466989  Cd Length: 127  Bit Score: 67.61  E-value: 3.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  541 NTLQFYNKlTGGFVRLHPDGTVDAIGEKTDKYGVFDVIFNKRNICIFQSHEmRHLSLALD-NGIVTGMVSGEATTELRVL 619
Cdd:cd00058      1 RLVRLYSR-TGYFLQILPDGTVNGTKDENSPYAILELQSVGTGLVRIKGVK-TGRYLAMDkNGKLYGTKKPTEDCVFKET 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1771853516  620 YQPNRCALLESALVP----GHTVVFDRHGKIADASSAGYANLSKEFVIF 664
Cdd:cd00058     79 LEENGYNTYSSYKYYhtrkGWYLAIKKNGKPKRGKKTKPGQKSTQFLPL 127
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1121-1229 9.66e-13

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 65.92  E-value: 9.66e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1121 WKVTIVTGDLENAGTTATVFLYVYGE--TKCSGPIILGSGKhqlFNPNTADIFKINLK-DIGEIYKIRIGHDNTGKNPRW 1197
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKvgESAQLEITLDNPD---FERGAEDSFEIDTDwDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1771853516 1198 YLEEVRLENIATYE---LFClpVDSWIAENENDGD 1229
Cdd:pfam01477   78 FLKSITVEVPGETGgkyTFP--CNSWVYGSKKYKE 110
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 394-501 1.38e-11

PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains consists of an eight stranded beta-barrel. In RabIP1 this domain may participate in lipid-mediated modulation of Rab6IP1's function via it's generally proposed function of mediating interaction with lipids or membrane bound proteins.


Pssm-ID: 238855  Cd Length: 114  Bit Score: 62.56  E-value: 1.38e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  394 YEVNVATGE-LWNAGTVANVYISIHGEKGDTGSRQLFRSKSSFNFlrgqtdtfflEAVHLGDLCKIVIGHDGLGPGNGWF 472
Cdd:cd01757      3 YHVVIVPSKkLGGSMFTANPWICVSGELGETPPLQIPKNSLEMTF----------DCQNLGKLTTVQIGHDNSGLLAKWL 72

                           90       100
                   ....*....|....*....|....*....
gi 1771853516  473 LDDVVIKDPTTNYEYAFFCHRWLDQGEDD 501
Cdd:cd01757     73 VEYVMVRNEITGHTYKFPCGRWLGEGVDD 101
DCX pfam03607
Doublecortin;
171-227 3.59e-11

Doublecortin;


Pssm-ID: 460986  Cd Length: 60  Bit Score: 59.77  E-value: 3.59e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853516  171 LLSRRVTQSFEAFLQHLTEVMQR----PVVKLYATDGRRVPSLQAvILSSGAVVAAGREPF 227
Cdd:pfam03607    1 VVNKRRFRSFDALLDELTEKVVKlpfgAVRKLYTLDGKRVTSLDE-LEDGGVYVAAGREKF 60
DCX1_DCDC2 cd17149
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is ...
 154-228 7.56e-10

Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340669  Cd Length: 80  Bit Score: 56.71  E-value: 7.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  154 RSLVVFRNGDP--KTRRAVLLSRRVTqSFEAFLQHLTEVMQRP---VVKLYAT-DGRRVPSLQAvILSSGAVVAAGREPF 227
Cdd:cd17149      1 KNVLVYRNGDPfyAGRRLVINEKRVS-SFEVFLKEVTGGVQAPfgaVRNIYTPrGGHRVRSLEQ-LQSGEQYVAAGRERF 78


                   .
gi 1771853516  228 K 228
Cdd:cd17149     79 K 79
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1249-1356 8.48e-10

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 57.27  E-value: 8.48e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  1249 YEIRIYTGTMTGAETESNVFINLIGTRGDSGKRrlHQSKNNEIKFQRGQVDIFSIK-AVSLGKLKKVLISHDGTGPgnGW 1327
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKES--KLDYLFKGIFARGSTYEFTFDvDEDFGELGAVKIKNEHRHP--EW 78

                            90       100
                    ....*....|....*....|....*....
gi 1771853516  1328 FLGSIVVKSEDEDSseEVLFLCNRWLDEY 1356
Cdd:smart00308   79 FLKSITVKDLPTGG--KYHFPCNSWVYPD 105
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 1120-1228 9.60e-10

PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains consists of an eight stranded beta-barrel. In RabIP1 this domain may participate in lipid-mediated modulation of Rab6IP1's function via it's generally proposed function of mediating interaction with lipids or membrane bound proteins.


Pssm-ID: 238855  Cd Length: 114  Bit Score: 57.55  E-value: 9.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1120 DWKVTIVTGD-LENAGTTATVFLYVYGETKCSGPIILgsgkhqlfNPNTADiFKINLKDIGEIYKIRIGHDNTGKNPRWY 1198
Cdd:cd01757      2 PYHVVIVPSKkLGGSMFTANPWICVSGELGETPPLQI--------PKNSLE-MTFDCQNLGKLTTVQIGHDNSGLLAKWL 72

                           90       100       110
                   ....*....|....*....|....*....|
gi 1771853516 1199 LEEVRLENIATYELFCLPVDSWIAENENDG 1228
Cdd:cd01757     73 VEYVMVRNEITGHTYKFPCGRWLGEGVDDG 102
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 982-1085 9.67e-10

PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they catalyze enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins. Both types of enzymes are cytosolic but need this domain to access their sequestered membrane or micelle bound substrates.


Pssm-ID: 238851  Cd Length: 113  Bit Score: 57.32  E-value: 9.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  982 VRYQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLykSNMQVKFQRGQIDKFQV-AAVSLGKLQKVLLRceasdKSQY 1060
Cdd:cd01753      1 AEYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLL--DRPGYDFERGAVDEYKVkVPEDLGELLLVRLR-----KRKY 73

                           90       100       110
                   ....*....|....*....|....*....|
gi 1771853516 1061 -----WYCEQVIVREPGTTsESIFTCQRWL 1085
Cdd:cd01753     74 llfdaWFCNYITVTGPGGD-EYHFPCYRWI 102
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 1247-1356 1.22e-09

PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they catalyze enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins. Both types of enzymes are cytosolic but need this domain to access their sequestered membrane or micelle bound substrates.


Pssm-ID: 238851  Cd Length: 113  Bit Score: 56.93  E-value: 1.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1247 VLYEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQSKNNeikFQRGQVDIFSIKA-VSLGKL------KKVLISHD 1319
Cdd:cd01753      1 AEYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRPGYD---FERGAVDEYKVKVpEDLGELllvrlrKRKYLLFD 77

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1771853516 1320 gtgpgnGWFLGSIVVKSEDEDsseEVLFLCNRWLDEY 1356
Cdd:cd01753     78 ------AWFCNYITVTGPGGD---EYHFPCYRWIEGY 105
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 858-958 2.44e-09

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 56.29  E-value: 2.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  858 WKVLVLTGNT---GTQANVTLWVYGDKGVTGPISLRKDSSEqlFLPGHEDEFQVEIR-NTGNIYKIRIGHDGTSEQPEWN 933
Cdd:pfam01477    1 YQVKVVTGDElgaGTDADVYISLYGKVGESAQLEITLDNPD--FERGAEDSFEIDTDwDVGAILKINLHWDNNGLSDEWF 78

                           90       100
                   ....*....|....*....|....*.
gi 1771853516  934 LQRVT-MQHMKSKKILDFAANVWLSR 958
Cdd:pfam01477   79 LKSITvEVPGETGGKYTFPCNSWVYG 104
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 394-496 4.11e-09

PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they catalyze enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins. Both types of enzymes are cytosolic but need this domain to access their sequestered membrane or micelle bound substrates.


Pssm-ID: 238851  Cd Length: 113  Bit Score: 55.78  E-value: 4.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  394 YEVNVATGELWNAGTVANVYISIHGEKGDtgSRQLFRSKSSFNFLRGQTDTFFLEA-VHLGDLCKIVIGHDGLGPGNGWF 472
Cdd:cd01753      3 YKVTVATGSSLFAGTDDYIYLTLVGTAGE--SEKQLLDRPGYDFERGAVDEYKVKVpEDLGELLLVRLRKRKYLLFDAWF 80

                           90       100
                   ....*....|....*....|....
gi 1771853516  473 LDDVVIKDPTTNYeYAFFCHRWLD 496
Cdd:cd01753     81 CNYITVTGPGGDE-YHFPCYRWIE 103
DCX1_DCDC2C cd17151
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2C (DCDC2C); DCDC2 ...
 154-228 4.27e-09

Dublecortin-like domain 1 found in doublecortin domain-containing protein 2C (DCDC2C); DCDC2 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340671  Cd Length: 79  Bit Score: 54.41  E-value: 4.27e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853516  154 RSLVVFRNGDP-KTRRAVLLSRRVTQSFEAFLQHLTEVMQRP--VVKLYA-TDGRRVPSLQAvILSSGAVVAAGREPFK 228
Cdd:cd17151      1 KTILVYRNGDPfYQAHKVVIHRRRVKTFDALLRQLTETVKVPfgVRCLYTpRNGHRVKGLDD-LQGGGKYVAAGRERFK 78
DCX1_DCDC2_like cd17071
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2) and ...
 154-229 2.15e-08

Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2) and similar proteins; DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340591  Cd Length: 80  Bit Score: 52.61  E-value: 2.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  154 RSLVVFRNGDP-KTRRAVLLSRRVTQSFEAFLQHLTEVMQ---RPVVKLY-ATDGRRVPSLQAvILSSGAVVAAGREPFK 228
Cdd:cd17071      1 KIIVVYKNGDPfFPGKKFVVNERQVRTFDAFLNEVTSGIKapfGAVRSIYtPTGGHRVKDLDS-LQNGGVYVAAGSERFK 79


                   .
gi 1771853516  229 P 229
Cdd:cd17071     80 K 80
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
983-1085 3.92e-08

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 52.64  E-value: 3.92e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516   983 RYQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKsNMQVKFQRGQIDKFQVA-AVSLGKLQKVLLRCEASDKSqyW 1061
Cdd:smart00308    2 KYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDY-LFKGIFARGSTYEFTFDvDEDFGELGAVKIKNEHRHPE--W 78

                            90       100
                    ....*....|....*....|....
gi 1771853516  1062 YCEQVIVREPGTTSESIFTCQRWL 1085
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWV 102
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
392-496 6.31e-08

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 51.87  E-value: 6.31e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516   392 TIYEVNVATGELWNAGTVANVYISIHGEKGDTG-SRQLFRSKSSFNflRGQTDTFFLE-AVHLGDLCKIVIGHDGLGPgn 469
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKeSKLDYLFKGIFA--RGSTYEFTFDvDEDFGELGAVKIKNEHRHP-- 76

                            90       100
                    ....*....|....*....|....*..
gi 1771853516   470 GWFLDDVVIKDPTTNYEYAFFCHRWLD 496
Cdd:smart00308   77 EWFLKSITVKDLPTGGKYHFPCNSWVY 103
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
266-366 1.14e-07

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 51.10  E-value: 1.14e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516   266 WKVFIITSDLPDAGTSSQIYIILYGQH---RSSAPIYLYGTDGARfqvGHEDIFTITV-GDIGALFKIRIghTNSGSSPS 341
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEgdgKESKLDYLFKGIFAR---GSTYEFTFDVdEDFGELGAVKI--KNEHRHPE 77

                            90       100
                    ....*....|....*....|....*
gi 1771853516   342 WHCKEIQLHNMNSGKQFYVPVQRWL 366
Cdd:smart00308   78 WFLKSITVKDLPTGGKYHFPCNSWV 102
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 1123-1221 5.08e-07

Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates. This subfamily contains Toxoplasma gondii Scavenger protein TgSR1.


Pssm-ID: 239228  Cd Length: 109  Bit Score: 49.38  E-value: 5.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1123 VTIVTGDLENAGTTATVFLYVYGETKCSGPIILgsgkHQLFNPNTADIFKINLKDIGEIYKIRIGhdNTGKNPRWYLEEV 1202
Cdd:cd02899      5 ASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTL----SQGFYPGSLKRIRFRAADVGDINAIILS--NTALNDPWYCDYV 78

                           90       100
                   ....*....|....*....|.
gi 1771853516 1203 RlenIATYE--LFCLPVDSWI 1221
Cdd:cd02899     79 R---IKSEDgkVFAFNVKRWI 96
DCX_DCLK3 cd16111
Doublecortin-like domain found in doublecortin-like kinase 3 (DCLK3); DCLK3 is a member of ...
 153-226 9.19e-07

Doublecortin-like domain found in doublecortin-like kinase 3 (DCLK3); DCLK3 is a member of doublecortin (DCX) protein family. It functions as a microtubule-associated protein (MAP). DCLK3 contains only one N-terminal doublecortin domain (DCX), unlike DCLK1 and DCLK2 which each have two conserved DCX domains. The DCX domain has a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. In addition to microtubule binding domains, DCLK3 has a serine/threonine kinase domain that is similar to Ca/calmodulin-dependent (Cam) protein kinases.


Pssm-ID: 340528  Cd Length: 85  Bit Score: 48.20  E-value: 9.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  153 PRSLVVFRNGD-PKTRRAVLLSRRVTQSFEAFLQHLTEVMQRP------VVKLYATDGRRVPSLQAVILSSGAVVAAGRE 225
Cdd:cd16111      2 PKVITVVRNGGqPRTKITILLNRRSVQTFEQLMADISEALGFPrwkndrVRKLYSLRGREVRSVSDFFREDDVFIATGRE 81


                   .
gi 1771853516  226 P 226
Cdd:cd16111     82 Q 82
DCX2 cd17069
Dublecortin-like domain 2; Members in doublecortin (DCX) gene family are ...
 153-227 1.01e-06

Dublecortin-like domain 2; Members in doublecortin (DCX) gene family are microtubule-associated proteins (MAPs). Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX gene family consists of eleven paralogs in human and mouse, and its protein domains can occur in double tandem or as a single repeat. The first repeat of DCX domain has a stable ubiquitin-like tertiary fold. Proteins with DCX double tandem domains in general have roles in microtubule (MT) regulation and signal transduction such as X-linked doublecortin (DCX), retinitis pigmentosa-1 (RP1) and doublecortin-like kinase (DCLK).


Pssm-ID: 340589  Cd Length: 84  Bit Score: 47.76  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  153 PRSLVVFRNGdPKTRRAV--LLSRRVTQSFEAFLQHLTEVMQR---PVVKLYATDGRRVPSLQAVILSSGAVVAAGREPF 227
Cdd:cd17069      4 PKLVTVIRNG-TKPRKAVriLLNKKTAHSFEQVLTDITEAIKLdsgAVRKLFTLDGRQVTCLQDFFGDDDVFIAYGPEKF 82
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 393-478 1.79e-06

PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of its members are stress induced. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238852  Cd Length: 129  Bit Score: 48.69  E-value: 1.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  393 IYEVNVATGELWNAGTVANVYISIHGEKGDTGS-------RQLFRSKSSFnFLRGQTDTFFLEAVHL-GDLCKIVIGHDG 464
Cdd:cd01754      2 VYTIYVQTGSIWKAGTDSRISLQIYDADGPGLRianleawGGLMGAGHDY-FERGNLDRFSGRGPCLpSPPCWMNLTSDG 80

                           90
                   ....*....|....
gi 1771853516  465 LGPGNGWFLDDVVI 478
Cdd:cd01754     81 TGNHPGWYVNYVEV 94
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 984-1087 2.27e-06

Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates. This subfamily contains Toxoplasma gondii Scavenger protein TgSR1.


Pssm-ID: 239228  Cd Length: 109  Bit Score: 47.84  E-value: 2.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  984 YQVDVYTGQLKHAETESEVFLCLFGERGDSGLRQLYKSnmqvkFQRGQIDKFQVAAVSLGKLQKVLLRCEASDKSqyWYC 1063
Cdd:cd02899      3 YTASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTLSQG-----FYPGSLKRIRFRAADVGDINAIILSNTALNDP--WYC 75

                           90       100
                   ....*....|....*....|....*.
gi 1771853516 1064 EQVIVREPGTTSeSIFTCQRWL--PF 1087
Cdd:cd02899     76 DYVRIKSEDGKV-FAFNVKRWIgyPY 100
DCX1_DCDC2B cd17150
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2B (DCDC2B); DCDC2 ...
 154-228 3.18e-06

Dublecortin-like domain 1 found in doublecortin domain-containing protein 2B (DCDC2B); DCDC2 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340670  Cd Length: 79  Bit Score: 46.33  E-value: 3.18e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853516  154 RSLVVFRNGDP-KTRRAVLLSRRVTQSFEAFLQHLTEVMQRPVV--KLYAT-DGRRVPSLqAVILSSGAVVAAGREPFK 228
Cdd:cd17150      1 KNVVVYRNGDPfFTGRKFVVNQRQFLTFEAFLNEVTSNIQAPVAvrNLYTPrEGHRVTEL-GDLQNGGHYVAAGFERFK 78
DCX2_DCX cd17142
Dublecortin-like domain 2 found in neuronal migration protein doublecortin (DCX); DCX, also ...
 153-228 1.64e-05

Dublecortin-like domain 2 found in neuronal migration protein doublecortin (DCX); DCX, also termed doublin or lissencephalin-X (Lis-XDCX), is a microtubule-associated protein (MAP). It belongs to the doublecortin (DCX) family, has double tandem DCX repeats, and is expressed in migrating neurons. Structure studies show that the N-terminal DCX domain has a stable ubiquitin-like fold. DCX is not only a unique MAP in terms of its structure, but also interacts with multiple additional proteins. Mutations in the human DCX genes are associated with abnormal neuronal migration, epilepsy, and mental retardation.


Pssm-ID: 340662  Cd Length: 84  Bit Score: 44.65  E-value: 1.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  153 PRSLVVFRNG-DPKTRRAVLLSRRVTQSFEAFLQHLTEVMQRP---VVKLYATDGRRVPSLQAVILSSGAVVAAGREPFK 228
Cdd:cd17142      4 PKLVTIIRSGvKPRKAVRVLLNKKTAHSFEQVLTDITEAIKLEtgvVKKLYTLDGKQVTCLHDFFGDDDVFIACGPEKFR 83
DCX2_DCDC2_like cd16113
Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is ...
 35-104 1.75e-05

Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of a ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340530  Cd Length: 74  Bit Score: 44.10  E-value: 1.75e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1771853516   35 AKRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSRKVPLPFG-VRNISTPRGrHSITRLEELEDGESY 104
Cdd:cd16113      1 PKTIHVFPNGDLLHPPSKVLLTKRRLPNWDTVLEEVTEKVKLQTGaVRKLYTLDG-KRISDPDELVNGGQY 70
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 1248-1353 2.08e-05

PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of its members are stress induced. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238852  Cd Length: 129  Bit Score: 45.61  E-value: 2.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1248 LYEIRIYTGTMTGAETESNVFINLIGTRGDSGKRRLHQSKNNEIK-----FQRGQVDIFSIKAVSL-GKLKKVLISHDGT 1321
Cdd:cd01754      2 VYTIYVQTGSIWKAGTDSRISLQIYDADGPGLRIANLEAWGGLMGaghdyFERGNLDRFSGRGPCLpSPPCWMNLTSDGT 81

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1771853516 1322 GPGNGWFLGSIVVKSEDEDS-SEEVLFLCNRWL 1353
Cdd:cd01754     82 GNHPGWYVNYVEVTQAGQHApCMQHLFAVEQWL 114
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 984-1085 2.53e-05

PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains consists of an eight stranded beta-barrel. In RabIP1 this domain may participate in lipid-mediated modulation of Rab6IP1's function via it's generally proposed function of mediating interaction with lipids or membrane bound proteins.


Pssm-ID: 238855  Cd Length: 114  Bit Score: 44.84  E-value: 2.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  984 YQVDVYTGQ-LKHAETESEVFLCLFGERGDSGLRQLYKSNMQVKFQrgqidkfqvaAVSLGKLQKVLLRCEASDKSQYWY 1062
Cdd:cd01757      3 YHVVIVPSKkLGGSMFTANPWICVSGELGETPPLQIPKNSLEMTFD----------CQNLGKLTTVQIGHDNSGLLAKWL 72

                           90       100
                   ....*....|....*....|...
gi 1771853516 1063 CEQVIVREPGTTSESIFTCQRWL 1085
Cdd:cd01757     73 VEYVMVRNEITGHTYKFPCGRWL 95
DCX2_DCDC2_like cd16113
Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is ...
 153-223 4.27e-05

Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of a ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340530  Cd Length: 74  Bit Score: 42.95  E-value: 4.27e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771853516  153 PRSLVVFRNGDPKTR-RAVLLSRRVTQSFEAFLQHLTE---VMQRPVVKLYATDGRRVPSLqAVILSSGAVVAAG 223
Cdd:cd16113      1 PKTIHVFPNGDLLHPpSKVLLTKRRLPNWDTVLEEVTEkvkLQTGAVRKLYTLDGKRISDP-DELVNGGQYVAVG 74
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 268-368 8.41e-05

Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates. This subfamily contains Toxoplasma gondii Scavenger protein TgSR1.


Pssm-ID: 239228  Cd Length: 109  Bit Score: 43.22  E-value: 8.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  268 VFIITSDLPDAGTSSQIYIILYGQHRSSAPIYLYGTdgarFQVGHEDIFTITVGDIGALFKIRIghTNSGSSPSWHCKEI 347
Cdd:cd02899      5 ASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTLSQG----FYPGSLKRIRFRAADVGDINAIIL--SNTALNDPWYCDYV 78

                           90       100
                   ....*....|....*....|.
gi 1771853516  348 QLHNmNSGKQFYVPVQRWLAR 368
Cdd:cd02899     79 RIKS-EDGKVFAFNVKRWIGY 98
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 266-373 1.34e-04

PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains consists of an eight stranded beta-barrel. In RabIP1 this domain may participate in lipid-mediated modulation of Rab6IP1's function via it's generally proposed function of mediating interaction with lipids or membrane bound proteins.


Pssm-ID: 238855  Cd Length: 114  Bit Score: 42.91  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  266 WKVFIITSD-LPDAGTSSQIYIILYGQHRSSAPIylygtdgarfQVGHEDI-FTITVGDIGALFKIRIGHTNSGSSPSWH 343
Cdd:cd01757      3 YHVVIVPSKkLGGSMFTANPWICVSGELGETPPL----------QIPKNSLeMTFDCQNLGKLTTVQIGHDNSGLLAKWL 72

                           90       100       110
                   ....*....|....*....|....*....|
gi 1771853516  344 CKEIQLHNMNSGKQFYVPVQRWLARDQEDG 373
Cdd:cd01757     73 VEYVMVRNEITGHTYKFPCGRWLGEGVDDG 102
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 858-965 2.01e-04

PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains consists of an eight stranded beta-barrel. In RabIP1 this domain may participate in lipid-mediated modulation of Rab6IP1's function via it's generally proposed function of mediating interaction with lipids or membrane bound proteins.


Pssm-ID: 238855  Cd Length: 114  Bit Score: 42.14  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  858 WKVLVLT----GNTGTQANVTLWVYGDKGVTGPISLRKDSSEQLFlpghedefqvEIRNTGNIYKIRIGHDGTSEQPEWN 933
Cdd:cd01757      3 YHVVIVPskklGGSMFTANPWICVSGELGETPPLQIPKNSLEMTF----------DCQNLGKLTTVQIGHDNSGLLAKWL 72

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1771853516  934 LQRVTMQHMKSKKILDFAANVWLSRIQADGDV 965
Cdd:cd01757     73 VEYVMVRNEITGHTYKFPCGRWLGEGVDDGNG 104
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 266-366 2.50e-04

PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they catalyze enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins. Both types of enzymes are cytosolic but need this domain to access their sequestered membrane or micelle bound substrates.


Pssm-ID: 238851  Cd Length: 113  Bit Score: 41.91  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  266 WKVFIITSDLPDAGTSSQIYIILYGQHRSSAPIYLygtD--GARFQVGHEDIFTITVG-DIGALFKIRIGHTNSGSSPSW 342
Cdd:cd01753      3 YKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLL---DrpGYDFERGAVDEYKVKVPeDLGELLLVRLRKRKYLLFDAW 79

                           90       100
                   ....*....|....*....|....
gi 1771853516  343 HCKEIQLHNMNSGKQFYvPVQRWL 366
Cdd:cd01753     80 FCNYITVTGPGGDEYHF-PCYRWI 102
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
858-957 3.11e-04

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 41.47  E-value: 3.11e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516   858 WKVLVLTGN---TGTQANVTLWVYG---DKGVTGPISLRKdsseQLFLPG--HEDEFQVEIrNTGNIYKIRIGHDGTseQ 929
Cdd:smart00308    3 YKVTVTTGGldfAGTTASVSLSLVGaegDGKESKLDYLFK----GIFARGstYEFTFDVDE-DFGELGAVKIKNEHR--H 75

                            90       100
                    ....*....|....*....|....*...
gi 1771853516   930 PEWNLQRVTMQHMKSKKILDFAANVWLS 957
Cdd:smart00308   76 PEWFLKSITVKDLPTGGKYHFPCNSWVY 103
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 1247-1362 4.81e-04

PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains consists of an eight stranded beta-barrel. In RabIP1 this domain may participate in lipid-mediated modulation of Rab6IP1's function via it's generally proposed function of mediating interaction with lipids or membrane bound proteins.


Pssm-ID: 238855  Cd Length: 114  Bit Score: 41.37  E-value: 4.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516 1247 VLYEIRIYTGT-MTGAETESNVFINLIGTRGDSGKRrlhQSKNNEIKFqrgqvdIFSIKavSLGKLKKVLISHDGTGPGN 1325
Cdd:cd01757      1 MPYHVVIVPSKkLGGSMFTANPWICVSGELGETPPL---QIPKNSLEM------TFDCQ--NLGKLTTVQIGHDNSGLLA 69

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1771853516 1326 GWFLGSIVVKSEDEDSSEEvlFLCNRWLDEYQDDGKT 1362
Cdd:cd01757     70 KWLVEYVMVRNEITGHTYK--FPCGRWLGEGVDDGNG 104
FGF pfam00167
Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in ...
 544-578 1.25e-03

Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in growth and differentiation in a wide range of contexts. They are found in a wide range of organizms, from nematodes to humans. Most share an internal core region of high similarity, conserved residues in which are involved in binding with their receptors. On binding, they cause dimerization of their tyrosine kinase receptors leading to intracellular signalling. There are currently four known tyrosine kinase receptors for fibroblast growth factors. These receptors can each bind several different members of this family. Members of this family have a beta trefoil structure. Most have N-terminal signal peptides and are secreted. A few lack signal sequences but are secreted anyway; still others also lack the signal peptide but are found on the cell surface and within the extracellular matrix. A third group remain intracellular. They have central roles in development, regulating cell proliferation, migration and differentiation. On the other hand, they are important in tissue repair following injury in adult organizms.


Pssm-ID: 425498  Cd Length: 124  Bit Score: 40.22  E-value: 1.25e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1771853516  544 QFYNKLTGGFVRLHPDGTVDAIGEKTDKYGVFDVI 578
Cdd:pfam00167    4 RLYCRTGGFHLQILPDGKVDGTGEDGSPYSILEIE 38
DCX2_DCLK2 cd17144
Dublecortin-like domain 2 found in doublecortin-like kinase 2 (DCLK2); DCLK2 is a member of ...
 153-228 1.71e-03

Dublecortin-like domain 2 found in doublecortin-like kinase 2 (DCLK2); DCLK2 is a member of doublecortin (DCX) protein family that functions as a microtubule-associated protein (MAP), and contains two conserved tubulin binding domains, which typically occur in double tandem. The DCX domain has a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. In addition to microtubule binding domains, DCLK encodes a serine/threonine kinase-domain that is similar to Ca/calmodulin-dependent (Cam) protein kinases. DCLK2 members regulate cyclic AMP signaling. Unlike DCX, the DCLK has varying levels of expression throughout embryonic and adult life.


Pssm-ID: 340664  Cd Length: 84  Bit Score: 38.86  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  153 PRSLVVFRNG-DPKTRRAVLLSRRVTQSFEAFLQHLTEVMQRP---VVKLYATDGRRVPSLQAVILSSGAVVAAGREPFK 228
Cdd:cd17144      4 PKLVTVIRSGvKPRKAVRILLNKKTAHSFEQVLTDITEAIKLDsgvVKRLCTLDGKQVTCLQDFFGDDDVFIACGPEKYR 83
DCX2_DCDC2B cd17153
Doublecortin-like domain 2 found in doublecortin domain-containing protein 2B (DCDC2B); DCDC2 ...
 158-228 2.83e-03

Doublecortin-like domain 2 found in doublecortin domain-containing protein 2B (DCDC2B); DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of a ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340673  Cd Length: 80  Bit Score: 38.19  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  158 VFRNGD---PKTRraVLLSRRVTQSFEAFLQHLTEvmqrpVVKLYATDGRRVPSLQAVILSSGA-------VVAAGREPF 227
Cdd:cd17153      6 VFRNGDllsPPFR--LLIPKHMLQDWETILSLLTE-----KANLRTGAVRKLCTLDGVPLSSGKelvsgqyYVAVGSEKF 78


                   .
gi 1771853516  228 K 228
Cdd:cd17153     79 K 79
DCX2_DCLK1 cd17143
Dublecortin-like domain 2 found in doublecortin-like kinase 1 (DCLK1); DCLK1 is a member of ...
 153-228 5.37e-03

Dublecortin-like domain 2 found in doublecortin-like kinase 1 (DCLK1); DCLK1 is a member of doublecortin (DCX) protein family that functions as a microtubule-associated protein (MAP), and contains two conserved tubulin binding domains. The DCX domain has a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. In addition to microtubule binding domains, DCLK encodes a serine/threonine kinase-domain that is similar to Ca/calmodulin-dependent (Cam) protein kinases. DCLK1 appears to regulate cyclic AMP signaling and is involved in neuronal migration, retrograde transport, neuronal apoptosis and neurogenesis. Unlike DCX, the DCLK has varying levels of expression throughout embryonic and adult life.


Pssm-ID: 340663  Cd Length: 84  Bit Score: 37.24  E-value: 5.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  153 PRSLVVFRNG-DPKTRRAVLLSRRVTQSFEAFLQHLTEVMQR---PVVKLYATDGRRVPSLQAVILSSGAVVAAGREPFK 228
Cdd:cd17143      4 PKLVTIIRSGvKPRKAVRILLNKKTAHSFEQVLTDITDAIKLdsgVVKRLYTLDGKQVMCLQDFFGDDDIFIACGPEKFR 83
beta-trefoil_FGF4 cd23316
FGF domain, beta-trefoil fold, found in fibroblast growth factor 4 (FGF4) and similar proteins; ...
 689-778 7.05e-03

FGF domain, beta-trefoil fold, found in fibroblast growth factor 4 (FGF4) and similar proteins; FGF4, also called heparin secretory-transforming protein 1 (HST-1), or HSTF-1, or heparin-binding growth factor 4 (HBGF4), or transforming protein KS3, plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal limb and cardiac valve development during embryogenesis. It interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF4 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467002  Cd Length: 125  Bit Score: 37.94  E-value: 7.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  689 PDGSCTGVGSQSEKSYWKVHKISSGICMFESVKNAQMYLRIKDGRCDGTGTGDVDCHFKiKKNLKNASISLESTKSPGLF 768
Cdd:cd23316     19 PDGRINGVHNENRYSLLEISPVERGVVSIFGVKSGLFVAMNSKGKLYGSPFFNDECKFK-EILLPNNYNAYESRKYPGMY 97

                           90
                   ....*....|
gi 1771853516  769 VGLQSDGQAK 778
Cdd:cd23316     98 IALSKNGKTK 107
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 393-495 9.29e-03

Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates. This subfamily contains Toxoplasma gondii Scavenger protein TgSR1.


Pssm-ID: 239228  Cd Length: 109  Bit Score: 37.44  E-value: 9.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853516  393 IYEVNVATGELWNAGTVANVYISIHGEKGDTGSRQLFRSkssfnFLRGQTDTFFLEAVHLGDLCKIVIGHDGLgpGNGWF 472
Cdd:cd02899      2 TYTASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTLSQG-----FYPGSLKRIRFRAADVGDINAIILSNTAL--NDPWY 74

                           90       100
                   ....*....|....*....|...
gi 1771853516  473 LDDVVIKDpTTNYEYAFFCHRWL 495
Cdd:cd02899     75 CDYVRIKS-EDGKVFAFNVKRWI 96
 
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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