NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1681348841|ref|NP_001357850|]
View 

oxygen-regulated protein 1 isoform 3 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 395-513 2.48e-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: 201.63  E-value: 2.48e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  395 TTYKVYITTGELWNSGTIANVYLSIYGEKGDTGSRKLFRSKNSSKFLRGQVDTFFLEAVNLGDLCKIVIGHDGLGQGNGW 474
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1681348841  475 FLEDVVVRDPTTNHEYAFFCHRWLDEGEDDGKIVREMYA 513
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYP 119
DCX1_RP1 cd17145
Doublecortin-like domain 1 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also ...
 35-113 3.89e-47

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: 162.68  E-value: 3.89e-47
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681348841   35 KRISFYKSGDPQFGGVRVVVNPRSFKTFDALLDSLSRKVPLPFGVRNISTPRGRHSITRLEELEDGKSYVCSHNKKVLP 113
Cdd:cd17145      1 KRVCFYKSGDPQFGGLRMVVNSRSFKTFDALLDNLSKKVPLPFGVRNITTPRGVHHITSLEDLEDGKSYICSHQKKVKP 79
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 973-1092 4.82e-43

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: 152.32  E-value: 4.82e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  973 VRYHVDVYTGQLKQAKTESEVSLCLYGERGDSGLRLLHRSNMPVRFQRGQIDAFQIEAVSLGNLQKALLHCEASDKSQYW 1052
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1681348841 1053 YCEKIIVKDPGSSSESIFTCERWIPFmSEGLMHSEIELYC 1092
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDK-DEDDGQIVRELYP 119
DCX2_RP1 cd17147
Dublecortin-like domain 2 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also termed ...
 157-232 1.08e-40

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: 144.13  E-value: 1.08e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681348841  157 RRLVVFRNGDPKNKHVVLLSRRITQSFEAFLQYLTQVMQCPVAKLYATDGRKVPSLQAVILSSGAVVAAGREPFKP 232
Cdd:cd17147      1 RKLIVFKNGDPGFKHTLILNKKTTQSFEALLDHVSELMQFPVVKLYTTDGRRVDSLQALILSSGAVVAAGREPFKP 76
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 673-794 1.10e-40

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: 146.18  E-value: 1.10e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  673 VVILATSL-CQALCLQPNGTCTGAGNQSEQ-SHWRVHRISSGICMFESVKTARMYLRIKDGYCNGMGTGDTDCHFKIKKN 750
Cdd:cd23312      5 VVQLYSKLtGQALRVKPDGSVDATGDKKDKfAYFRVHKVKGNIRIFQSVANPGYFLAIDDGKVDGNGKGGEDCEFRVRVQ 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1681348841  751 lENASISLESLKSPGLFVGLQPDGQAKPVIYTKDE-SVCFYPRVI 794
Cdd:cd23312     85 -PDRSVTLESVKNPGQFVGFNPDGKPRDPRGTGDGpNAQFYVYVK 128
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 542-665 5.97e-40

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: 143.87  E-value: 5.97e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  542 KGNTLQFYNKLSGGFVRLHPDGTVDAAGEQTDRYGLFDVIFNKGNICVFQSHEMRHLSLNFDN----GMVGGGGHSELQV 617
Cdd:cd23312      2 DGNVVQLYSKLTGQALRVKPDGSVDATGDKKDKFAYFRVHKVKGNIRIFQSVANPGYFLAIDDgkvdGNGKGGEDCEFRV 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1681348841  618 IYQPNRCVLLESVLLPGHTLTVDRHGKVTDESSAGYaELSKEFLVFVK 665
Cdd:cd23312     82 RVQPDRSVTLESVKNPGQFVGFNPDGKPRDPRGTGD-GPNAQFYVYVK 128
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 268-383 6.66e-31

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: 117.66  E-value: 6.66e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  268 NWKVSINTSDFPNAGTSSQIYIVLYGHCRSSAPIYLYGRDGT-RFQDGHEDNFTIMVGDIGTPFKIRVGHTNSGHSPSWH 346
Cdd:cd01756      2 TYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKnKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWF 81

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1681348841  347 CKRIELQNMNSGEKFYIPVQRWLAQEQEDGEICREFP 383
Cdd:cd01756     82 LDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELY 118
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 848-963 6.05e-28

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: 109.18  E-value: 6.05e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  848 KWKVLVVTG---NTGTQANVTLWVYGYEGVTGPISLTKDSQEKLFLPGQTDEFQVVLRGIGEIYKIRIGHDGTGGQPEWT 924
Cdd:cd01756      2 TYEVTVKTGdvkGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWF 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1681348841  925 LQRVTMENVKSKKTLHFVANVCLSRNQADGDIVCELPVM 963
Cdd:cd01756     82 LDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 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 ...
 395-513 2.48e-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: 201.63  E-value: 2.48e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  395 TTYKVYITTGELWNSGTIANVYLSIYGEKGDTGSRKLFRSKNSSKFLRGQVDTFFLEAVNLGDLCKIVIGHDGLGQGNGW 474
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1681348841  475 FLEDVVVRDPTTNHEYAFFCHRWLDEGEDDGKIVREMYA 513
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYP 119
DCX1_RP1 cd17145
Doublecortin-like domain 1 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also ...
 35-113 3.89e-47

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: 162.68  E-value: 3.89e-47
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681348841   35 KRISFYKSGDPQFGGVRVVVNPRSFKTFDALLDSLSRKVPLPFGVRNISTPRGRHSITRLEELEDGKSYVCSHNKKVLP 113
Cdd:cd17145      1 KRVCFYKSGDPQFGGLRMVVNSRSFKTFDALLDNLSKKVPLPFGVRNITTPRGVHHITSLEDLEDGKSYICSHQKKVKP 79
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 973-1092 4.82e-43

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: 152.32  E-value: 4.82e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  973 VRYHVDVYTGQLKQAKTESEVSLCLYGERGDSGLRLLHRSNMPVRFQRGQIDAFQIEAVSLGNLQKALLHCEASDKSQYW 1052
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1681348841 1053 YCEKIIVKDPGSSSESIFTCERWIPFmSEGLMHSEIELYC 1092
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDK-DEDDGQIVRELYP 119
DCX2_RP1 cd17147
Dublecortin-like domain 2 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also termed ...
 157-232 1.08e-40

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: 144.13  E-value: 1.08e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681348841  157 RRLVVFRNGDPKNKHVVLLSRRITQSFEAFLQYLTQVMQCPVAKLYATDGRKVPSLQAVILSSGAVVAAGREPFKP 232
Cdd:cd17147      1 RKLIVFKNGDPGFKHTLILNKKTTQSFEALLDHVSELMQFPVVKLYTTDGRRVDSLQALILSSGAVVAAGREPFKP 76
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 673-794 1.10e-40

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: 146.18  E-value: 1.10e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  673 VVILATSL-CQALCLQPNGTCTGAGNQSEQ-SHWRVHRISSGICMFESVKTARMYLRIKDGYCNGMGTGDTDCHFKIKKN 750
Cdd:cd23312      5 VVQLYSKLtGQALRVKPDGSVDATGDKKDKfAYFRVHKVKGNIRIFQSVANPGYFLAIDDGKVDGNGKGGEDCEFRVRVQ 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1681348841  751 lENASISLESLKSPGLFVGLQPDGQAKPVIYTKDE-SVCFYPRVI 794
Cdd:cd23312     85 -PDRSVTLESVKNPGQFVGFNPDGKPRDPRGTGDGpNAQFYVYVK 128
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 542-665 5.97e-40

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: 143.87  E-value: 5.97e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  542 KGNTLQFYNKLSGGFVRLHPDGTVDAAGEQTDRYGLFDVIFNKGNICVFQSHEMRHLSLNFDN----GMVGGGGHSELQV 617
Cdd:cd23312      2 DGNVVQLYSKLTGQALRVKPDGSVDATGDKKDKFAYFRVHKVKGNIRIFQSVANPGYFLAIDDgkvdGNGKGGEDCEFRV 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1681348841  618 IYQPNRCVLLESVLLPGHTLTVDRHGKVTDESSAGYaELSKEFLVFVK 665
Cdd:cd23312     82 RVQPDRSVTLESVKNPGQFVGFNPDGKPRDPRGTGD-GPNAQFYVYVK 128
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 30-117 3.54e-31

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: 117.36  E-value: 3.54e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841    30 HPVVAKRISFYKSGDPQFGGVRVVVNPRSFKTFDALLDSLSR--KVPLPFGVRNISTPRGRHsITRLEELEDGKSYVCSH 107
Cdd:smart00537    1 SLVKPKRIRFYRNGDRFFKGVRLVVNRKRFKSFEALLQDLTEvvKLDLPHGVRKLYTLDGKK-VTSLDELEDGGSYVASG 79

                            90
                    ....*....|
gi 1681348841   108 NKKVLPVDLD 117
Cdd:smart00537   80 TEAFKKVDYG 89
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 268-383 6.66e-31

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: 117.66  E-value: 6.66e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  268 NWKVSINTSDFPNAGTSSQIYIVLYGHCRSSAPIYLYGRDGT-RFQDGHEDNFTIMVGDIGTPFKIRVGHTNSGHSPSWH 346
Cdd:cd01756      2 TYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKnKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWF 81

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1681348841  347 CKRIELQNMNSGEKFYIPVQRWLAQEQEDGEICREFP 383
Cdd:cd01756     82 LDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELY 118
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 848-963 6.05e-28

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: 109.18  E-value: 6.05e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  848 KWKVLVVTG---NTGTQANVTLWVYGYEGVTGPISLTKDSQEKLFLPGQTDEFQVVLRGIGEIYKIRIGHDGTGGQPEWT 924
Cdd:cd01756      2 TYEVTVKTGdvkGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWF 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1681348841  925 LQRVTMENVKSKKTLHFVANVCLSRNQADGDIVCELPVM 963
Cdd:cd01756     82 LDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 152-236 1.10e-24

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: 98.87  E-value: 1.10e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841   152 MLRAPRRLVVFRNGDP-KNKHVVLLSRRITQSFEAFLQYLTQV--MQCP--VAKLYATDGRKVPSLQAVIlSSGAVVAAG 226
Cdd:smart00537    1 SLVKPKRIRFYRNGDRfFKGVRLVVNRKRFKSFEALLQDLTEVvkLDLPhgVRKLYTLDGKKVTSLDELE-DGGSYVASG 79

                            90
                    ....*....|
gi 1681348841   227 REPFKPGNYD 236
Cdd:smart00537   80 TEAFKKVDYG 89
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 397-503 3.00e-22

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: 92.88  E-value: 3.00e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  397 YKVYITTGELWNSGTIANVYLSIYGEKGDTGSRKLFRSKNSskFLRGQVDTF-FLEAVNLGDLCKIVIGHDGLGQGNGWF 475
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPD--FERGAEDSFeIDTDWDVGAILKINLHWDNNGLSDEWF 78

                           90       100
                   ....*....|....*....|....*....
gi 1681348841  476 LEDVVVRDP-TTNHEYAFFCHRWLDEGED 503
Cdd:pfam01477   79 LKSITVEVPgETGGKYTFPCNSWVYGSKK 107
DCX pfam03607
Doublecortin;
53-110 4.24e-19

Doublecortin;


Pssm-ID: 460986  Cd Length: 60  Bit Score: 81.72  E-value: 4.24e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841   53 VVNPRSFKTFDALLDSLSRKVP-LPFG-VRNISTPRGrHSITRLEELEDGKSYVCSHNKK 110
Cdd:pfam03607    1 VVNKRRFRSFDALLDELTEKVVkLPFGaVRKLYTLDG-KRVTSLDELEDGGVYVAAGREK 59
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 269-373 1.21e-16

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: 76.70  E-value: 1.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  269 WKVSINTSDFPNAGTSSQIYIVLYGHCRSSAPIYLYgRDGTRFQDGHEDNFTIMVG-DIGTPFKIRVGHTNSGHSPSWHC 347
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEIT-LDNPDFERGAEDSFEIDTDwDVGAILKINLHWDNNGLSDEWFL 79

                           90       100
                   ....*....|....*....|....*..
gi 1681348841  348 KRIELQ-NMNSGEKFYIPVQRWLAQEQ 373
Cdd:pfam01477   80 KSITVEvPGETGGKYTFPCNSWVYGSK 106
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 975-1076 2.12e-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: 73.23  E-value: 2.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  975 YHVDVYTGQLKQAKTESEVSLCLYGERGDSGLRLLHRSNMPvrFQRGQIDAFQI-EAVSLGNLQKALLHCEASDKSQYWY 1053
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPD--FERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDEWF 78

                           90       100
                   ....*....|....*....|....
gi 1681348841 1054 CEKIIVKDPGSS-SESIFTCERWI 1076
Cdd:pfam01477   79 LKSITVEVPGETgGKYTFPCNSWV 102
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 849-944 5.44e-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: 66.30  E-value: 5.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  849 WKVLVVTGNT---GTQANVTLWVYGYEGVTGPISLTKDSQEklFLPGQTDEFQVVLR-GIGEIYKIRIGHDGTGGQPEWT 924
Cdd:pfam01477    1 YQVKVVTGDElgaGTDADVYISLYGKVGESAQLEITLDNPD--FERGAEDSFEIDTDwDVGAILKINLHWDNNGLSDEWF 78

                           90       100
                   ....*....|....*....|.
gi 1681348841  925 LQRVTME-NVKSKKTLHFVAN 944
Cdd:pfam01477   79 LKSITVEvPGETGGKYTFPCN 99
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
848-944 1.21e-10

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 59.58  E-value: 1.21e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841   848 KWKVLVVTGN---TGTQANVTLWVYGYEGVTGPISLtkDSQEK-LFLPGQTDEFQV-VLRGIGEIYKIRIGHDGtgGQPE 922
Cdd:smart00308    2 KYKVTVTTGGldfAGTTASVSLSLVGAEGDGKESKL--DYLFKgIFARGSTYEFTFdVDEDFGELGAVKIKNEH--RHPE 77

                            90       100
                    ....*....|....*....|..
gi 1681348841   923 WTLQRVTMENVKSKKTLHFVAN 944
Cdd:smart00308   78 WFLKSITVKDLPTGGKYHFPCN 99
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
397-500 1.72e-10

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 58.81  E-value: 1.72e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841   397 YKVYITTGELWNSGTIANVYLSIYGEKGDTGSRKL-FRSKNSskFLRGQVDTFFLE-AVNLGDLCKIVIGHDglGQGNGW 474
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLdYLFKGI--FARGSTYEFTFDvDEDFGELGAVKIKNE--HRHPEW 78

                            90       100
                    ....*....|....*....|....*.
gi 1681348841   475 FLEDVVVRDPTTNHEYAFFCHRWLDE 500
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVYP 104
DCX pfam03607
Doublecortin;
174-230 2.15e-10

Doublecortin;


Pssm-ID: 460986  Cd Length: 60  Bit Score: 57.07  E-value: 2.15e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681348841  174 LLSRRITQSFEAFLQYLTQVMQC----PVAKLYATDGRKVPSLQAvILSSGAVVAAGREPF 230
Cdd:pfam03607    1 VVNKRRFRSFDALLDELTEKVVKlpfgAVRKLYTLDGKRVTSLDE-LEDGGVYVAAGREKF 60
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
974-1076 1.78e-09

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 56.11  E-value: 1.78e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841   974 RYHVDVYTGQLKQAKTESEVSLCLYGERGDSGLR---LLHRsnmpVRFQRGQIDAFQIE-AVSLGNLQKALLHCEASDKS 1049
Cdd:smart00308    2 KYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESkldYLFK----GIFARGSTYEFTFDvDEDFGELGAVKIKNEHRHPE 77

                            90       100
                    ....*....|....*....|....*..
gi 1681348841  1050 qyWYCEKIIVKDPGSSSESIFTCERWI 1076
Cdd:smart00308   78 --WFLKSITVKDLPTGGKYHFPCNSWV 102
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
269-369 8.35e-09

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 54.18  E-value: 8.35e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841   269 WKVSINTSDFPNAGTSSQIYIVLYG-HCRS--SAPIYLYGRDGTRfqdGHEDNFTIMV-GDIGTPFKIRVghTNSGHSPS 344
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGaEGDGkeSKLDYLFKGIFAR---GSTYEFTFDVdEDFGELGAVKI--KNEHRHPE 77

                            90       100
                    ....*....|....*....|....*
gi 1681348841   345 WHCKRIELQNMNSGEKFYIPVQRWL 369
Cdd:smart00308   78 WFLKSITVKDLPTGGKYHFPCNSWV 102
FGF pfam00167
Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in ...
 547-581 1.07e-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: 1.07e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1681348841  547 QFYNKLSGGFVRLHPDGTVDAAGEQTDRYGLFDVI 581
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 ...
 395-513 2.48e-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: 201.63  E-value: 2.48e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  395 TTYKVYITTGELWNSGTIANVYLSIYGEKGDTGSRKLFRSKNSSKFLRGQVDTFFLEAVNLGDLCKIVIGHDGLGQGNGW 474
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1681348841  475 FLEDVVVRDPTTNHEYAFFCHRWLDEGEDDGKIVREMYA 513
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYP 119
DCX1_RP1 cd17145
Doublecortin-like domain 1 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also ...
 35-113 3.89e-47

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: 162.68  E-value: 3.89e-47
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681348841   35 KRISFYKSGDPQFGGVRVVVNPRSFKTFDALLDSLSRKVPLPFGVRNISTPRGRHSITRLEELEDGKSYVCSHNKKVLP 113
Cdd:cd17145      1 KRVCFYKSGDPQFGGLRMVVNSRSFKTFDALLDNLSKKVPLPFGVRNITTPRGVHHITSLEDLEDGKSYICSHQKKVKP 79
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 973-1092 4.82e-43

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: 152.32  E-value: 4.82e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  973 VRYHVDVYTGQLKQAKTESEVSLCLYGERGDSGLRLLHRSNMPVRFQRGQIDAFQIEAVSLGNLQKALLHCEASDKSQYW 1052
Cdd:cd01756      1 VTYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGW 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1681348841 1053 YCEKIIVKDPGSSSESIFTCERWIPFmSEGLMHSEIELYC 1092
Cdd:cd01756     81 FLDKVEIREPGTGDEYTFPCNRWLDK-DEDDGQIVRELYP 119
DCX1_RP_like cd16110
Doublecortin-like domain 1 found in retinitis pigmentosa (RP)-like protein; RP-like protein ...
 35-109 2.36e-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: 2.36e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681348841   35 KRISFYKSGDPQFGGVRVVVNPRSFKTFDALLDSLSRKVPLPFGVRNISTPRGRHSITRLEELEDGKSYVCSHNK 109
Cdd:cd16110      1 KNVTFYKDGDVHFSGVRVAINPRRYRTFDALLDELSRKVPLPFGVRSITTPRGRHSITSLEQLEDGGKYVCSSKR 75
DCX2_RP1 cd17147
Dublecortin-like domain 2 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also termed ...
 157-232 1.08e-40

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: 144.13  E-value: 1.08e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681348841  157 RRLVVFRNGDPKNKHVVLLSRRITQSFEAFLQYLTQVMQCPVAKLYATDGRKVPSLQAVILSSGAVVAAGREPFKP 232
Cdd:cd17147      1 RKLIVFKNGDPGFKHTLILNKKTTQSFEALLDHVSELMQFPVVKLYTTDGRRVDSLQALILSSGAVVAAGREPFKP 76
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 673-794 1.10e-40

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: 146.18  E-value: 1.10e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  673 VVILATSL-CQALCLQPNGTCTGAGNQSEQ-SHWRVHRISSGICMFESVKTARMYLRIKDGYCNGMGTGDTDCHFKIKKN 750
Cdd:cd23312      5 VVQLYSKLtGQALRVKPDGSVDATGDKKDKfAYFRVHKVKGNIRIFQSVANPGYFLAIDDGKVDGNGKGGEDCEFRVRVQ 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1681348841  751 lENASISLESLKSPGLFVGLQPDGQAKPVIYTKDE-SVCFYPRVI 794
Cdd:cd23312     85 -PDRSVTLESVKNPGQFVGFNPDGKPRDPRGTGDGpNAQFYVYVK 128
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 542-665 5.97e-40

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: 143.87  E-value: 5.97e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  542 KGNTLQFYNKLSGGFVRLHPDGTVDAAGEQTDRYGLFDVIFNKGNICVFQSHEMRHLSLNFDN----GMVGGGGHSELQV 617
Cdd:cd23312      2 DGNVVQLYSKLTGQALRVKPDGSVDATGDKKDKFAYFRVHKVKGNIRIFQSVANPGYFLAIDDgkvdGNGKGGEDCEFRV 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1681348841  618 IYQPNRCVLLESVLLPGHTLTVDRHGKVTDESSAGYaELSKEFLVFVK 665
Cdd:cd23312     82 RVQPDRSVTLESVKNPGQFVGFNPDGKPRDPRGTGD-GPNAQFYVYVK 128
DCX1_RP1L1 cd17146
Doublecortin-like domain 1 found in retinitis pigmentosa 1-like 1 (RP1L1) protein; RP1L1 is a ...
 35-113 5.99e-39

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: 139.19  E-value: 5.99e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681348841   35 KRISFYKSGDPQFGGVRVVVNPRSFKTFDALLDSLSRKVPLPFGVRNISTPRGRHSITRLEELEDGKSYVCSHNKKVLP 113
Cdd:cd17146      1 KKITFYKSGDPQFGGVKMAVNKRTFKSFSALLDDLSQRVPLPFGVRTITTPRGTHSISRLEQLEDGGCYLCSDKKYVKP 79
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 30-117 3.54e-31

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: 117.36  E-value: 3.54e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841    30 HPVVAKRISFYKSGDPQFGGVRVVVNPRSFKTFDALLDSLSR--KVPLPFGVRNISTPRGRHsITRLEELEDGKSYVCSH 107
Cdd:smart00537    1 SLVKPKRIRFYRNGDRFFKGVRLVVNRKRFKSFEALLQDLTEvvKLDLPHGVRKLYTLDGKK-VTSLDELEDGGSYVASG 79

                            90
                    ....*....|
gi 1681348841   108 NKKVLPVDLD 117
Cdd:smart00537   80 TEAFKKVDYG 89
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 268-383 6.66e-31

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: 117.66  E-value: 6.66e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  268 NWKVSINTSDFPNAGTSSQIYIVLYGHCRSSAPIYLYGRDGT-RFQDGHEDNFTIMVGDIGTPFKIRVGHTNSGHSPSWH 346
Cdd:cd01756      2 TYEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKnKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWF 81

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1681348841  347 CKRIELQNMNSGEKFYIPVQRWLAQEQEDGEICREFP 383
Cdd:cd01756     82 LDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELY 118
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 848-963 6.05e-28

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: 109.18  E-value: 6.05e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  848 KWKVLVVTG---NTGTQANVTLWVYGYEGVTGPISLTKDSQEKLFLPGQTDEFQVVLRGIGEIYKIRIGHDGTGGQPEWT 924
Cdd:cd01756      2 TYEVTVKTGdvkGAGTDANVFITLYGENGDTGKRKLKKSNNKNKFERGQTDKFTVEAVDLGKLKKIRIGHDNSGLGAGWF 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1681348841  925 LQRVTMENVKSKKTLHFVANVCLSRNQADGDIVCELPVM 963
Cdd:cd01756     82 LDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
 152-236 1.10e-24

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: 98.87  E-value: 1.10e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841   152 MLRAPRRLVVFRNGDP-KNKHVVLLSRRITQSFEAFLQYLTQV--MQCP--VAKLYATDGRKVPSLQAVIlSSGAVVAAG 226
Cdd:smart00537    1 SLVKPKRIRFYRNGDRfFKGVRLVVNRKRFKSFEALLQDLTEVvkLDLPhgVRKLYTLDGKKVTSLDELE-DGGSYVASG 79

                            90
                    ....*....|
gi 1681348841   227 REPFKPGNYD 236
Cdd:smart00537   80 TEAFKKVDYG 89
DCX2_RP_like cd17070
Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein ...
 157-225 1.83e-24

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: 97.70  E-value: 1.83e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681348841  157 RRLVVFRNGDPKNKHVVLLSRRITQSFEAFLQYLTQVMQCPVAKLYATDGRKVPSLQAVILSSGAVVAA 225
Cdd:cd17070      1 KVITVISNGDPHSRHTILLNRRTTQSFEQVLQDLSELLKGPVRKLYTTDGKKVESLSALFHGPDEYVAA 69
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 397-505 2.46e-22

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: 93.17  E-value: 2.46e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  397 YKVYITTGELWNSGTIANVYLSIYGEKGDTGsrKLFRSKNSSKFLRGQVDTFFLEA-VNLGDLCKIVIGHDGLGQGNGWF 475
Cdd:cd00113      3 YTVTIKTGDKKGAGTDSNISLALYGENGNSS--DIPILDGPGSFERGSTDTFQIDLkLDIGDITKVYLRRDGSGLSDGWY 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 1681348841  476 LEDVVVRDPTTNHEYAFFCHRWLDEGEDDG 505
Cdd:cd00113     81 CESITVQALGTKKVYTFPVNRWVLGGKWYT 110
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 397-503 3.00e-22

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: 92.88  E-value: 3.00e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  397 YKVYITTGELWNSGTIANVYLSIYGEKGDTGSRKLFRSKNSskFLRGQVDTF-FLEAVNLGDLCKIVIGHDGLGQGNGWF 475
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPD--FERGAEDSFeIDTDWDVGAILKINLHWDNNGLSDEWF 78

                           90       100
                   ....*....|....*....|....*....
gi 1681348841  476 LEDVVVRDP-TTNHEYAFFCHRWLDEGED 503
Cdd:pfam01477   79 LKSITVEVPgETGGKYTFPCNSWVYGSKK 107
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 397-513 3.47e-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: 92.72  E-value: 3.47e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  397 YKVYITTGELWNSGTIANVYLSIYGEKGDTGSRkLFRSKNSSKFLRGQVDTFFLE-AVNLGDLCKIVIGHDGLGQGNGWF 475
Cdd:cd01752      3 YLVTVFTGWRRGAGTTAKVTITLYGAEGESEPH-HLRDPEKPIFERGSVDSFLLTtPFPLGELQSIRLWHDNSGLSPSWY 81

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1681348841  476 LEDVVVRDPTTNHEYAFFCHRWLDEGEDDGKIVREMYA 513
Cdd:cd01752     82 LSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPV 119
DCX2_RP1L1 cd17148
Dublecortin-like domain 2 found in retinitis pigmentosa 1-like 1 (RP1L1) protein; RP1L1 is a ...
 157-232 4.38e-22

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: 90.98  E-value: 4.38e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681348841  157 RRLVVFRNGDPKNKHVVLLSRRITQSFEAFLQYLTQVMQCPVAKLYATDGRKVPSLQAVILSSGAVVAAGREPFKP 232
Cdd:cd17148      1 KKITLVKNGDPDVRRSIILNRRNARNLRTFLDEISDLLQFPVKKLYTLEGRKIDSIQALLHCPSVLVCVGREPFKP 76
DCX cd01617
Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin ...
 35-107 1.76e-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: 89.21  E-value: 1.76e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681348841   35 KRISFYKSGDPQFGGVRVVVNPRSFKTFDALLDSLSRKVPL-PFGVRNISTPRGRHsITRLEELEDGKSYVCSH 107
Cdd:cd01617      1 KRITVFRNGDKNFKGVKVLVKPRRFRTFDQLLDELTEKLGLpTGGVRKLYTPSGKL-VKSLSDLEDGESYVVCG 73
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 281-384 3.37e-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: 90.03  E-value: 3.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  281 AGTSSQIYIVLYGHCRSSAPIYLYGRDGTRFQDGHEDNFTI-MVGDIGTPFKIRVGHTNSGHSPSWHCKRIELQNMNSGE 359
Cdd:cd01752     15 AGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLtTPFPLGELQSIRLWHDNSGLSPSWYLSRVIVRDLQTGK 94

                           90       100
                   ....*....|....*....|....*
gi 1681348841  360 KFYIPVQRWLAQEQEDGEICREFPI 384
Cdd:cd01752     95 KWFFLCNDWLSVEEGDGTVERTFPV 119
DCX1 cd16109
Dublecortin-like domain 1; Members of the doublecortin (DCX) gene family are ...
 34-108 4.45e-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: 88.51  E-value: 4.45e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681348841   34 AKRISFYKSGDPQFGGVRVVVNPRSFKTFDALLDSLSR----KVPLPFGVRNISTPRGRHSITRLEELEDGKSYVCSHN 108
Cdd:cd16109      2 AKKVRFYRNGDRFFKGIVYAVSSERFRSFEALLADLTRslsdNVNLPQGVRTIFTIDGSRKITSLDELEDGESYVCAST 80
DCX1_DCDC2_like cd17071
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2) and ...
 35-110 7.88e-21

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: 87.66  E-value: 7.88e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681348841   35 KRISFYKSGDPQFGGVRVVVNPRSFKTFDALLDSLSRKVPLPFG-VRNISTPRGRHSITRLEELEDGKSYVCSHNKK 110
Cdd:cd17071      1 KIIVVYKNGDPFFPGKKFVVNERQVRTFDAFLNEVTSGIKAPFGaVRSIYTPTGGHRVKDLDSLQNGGVYVAAGSER 77
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 974-1075 2.41e-20

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: 87.72  E-value: 2.41e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  974 RYHVDVYTGQLKQAKTESEVSLCLYGERGDSGLRLLHRSNMPVrFQRGQIDAFQIE-AVSLGNLQKALLHCEASDKSQYW 1052
Cdd:cd01752      2 LYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPI-FERGSVDSFLLTtPFPLGELQSIRLWHDNSGLSPSW 80

                           90       100
                   ....*....|....*....|...
gi 1681348841 1053 YCEKIIVKDPGSSSESIFTCERW 1075
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDW 103
DCX pfam03607
Doublecortin;
53-110 4.24e-19

Doublecortin;


Pssm-ID: 460986  Cd Length: 60  Bit Score: 81.72  E-value: 4.24e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841   53 VVNPRSFKTFDALLDSLSRKVP-LPFG-VRNISTPRGrHSITRLEELEDGKSYVCSHNKK 110
Cdd:pfam03607    1 VVNKRRFRSFDALLDELTEKVVkLPFGaVRKLYTLDG-KRVTSLDELEDGGVYVAAGREK 59
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 848-962 1.46e-17

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: 79.63  E-value: 1.46e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  848 KWKVLVVTG---NTGTQANVTLWVYGYEGVTGPISLTkDSQEKLFLPGQTDEFQV-VLRGIGEIYKIRIGHDGTGGQPEW 923
Cdd:cd01752      2 LYLVTVFTGwrrGAGTTAKVTITLYGAEGESEPHHLR-DPEKPIFERGSVDSFLLtTPFPLGELQSIRLWHDNSGLSPSW 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1681348841  924 TLQRVTMENVKSKKTLHFVANVCLSRNQADGDIVCELPV 962
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPV 119
DCX1_DCLK2 cd17141
Dublecortin-like domain 1 found in doublecortin-like kinase 2 (DCLK2); DCLK2 is a member of ...
 34-109 2.47e-17

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: 77.64  E-value: 2.47e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841   34 AKRISFYKSGDPQFGGVRVVVNPRSFKTFDALL----DSLSRKVPLPFGVRNISTPRGRHSITRLEELEDGKSYVCSHNK 109
Cdd:cd17141      2 AKKVRFYRNGDRYFKGLVYAVSSDRFRSFDALLmeltRSLSDNVNLPQGVRTIYTIDGSKKITSLDELLEGESYVCASNE 81
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 267-369 7.54e-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: 77.38  E-value: 7.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  267 GNWKVSINTSDFPNAGTSSQIYIVLYGHCRSSAPIYLYGrDGTRFQDGHEDNFTIMVG-DIGTPFKIRVGHTNSGHSPSW 345
Cdd:cd00113      1 CRYTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILD-GPGSFERGSTDTFQIDLKlDIGDITKVYLRRDGSGLSDGW 79

                           90       100
                   ....*....|....*....|....
gi 1681348841  346 HCKRIELQNMNSGEKFYIPVQRWL 369
Cdd:cd00113     80 YCESITVQALGTKKVYTFPVNRWV 103
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 269-373 1.21e-16

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: 76.70  E-value: 1.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  269 WKVSINTSDFPNAGTSSQIYIVLYGHCRSSAPIYLYgRDGTRFQDGHEDNFTIMVG-DIGTPFKIRVGHTNSGHSPSWHC 347
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEIT-LDNPDFERGAEDSFEIDTDwDVGAILKINLHWDNNGLSDEWFL 79

                           90       100
                   ....*....|....*....|....*..
gi 1681348841  348 KRIELQ-NMNSGEKFYIPVQRWLAQEQ 373
Cdd:pfam01477   80 KSITVEvPGETGGKYTFPCNSWVYGSK 106
DCX1_DCDC2C cd17151
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2C (DCDC2C); DCDC2 ...
 35-104 1.93e-16

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: 75.21  E-value: 1.93e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841   35 KRISFYKSGDPQFGGVRVVVNPRSFKTFDALLDSLSRKVPLPFGVRNISTPRGRHSITRLEELEDGKSYV 104
Cdd:cd17151      1 KTILVYRNGDPFYQAHKVVIHRRRVKTFDALLRQLTETVKVPFGVRCLYTPRNGHRVKGLDDLQGGGKYV 70
DCX1_DCDC2B cd17150
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2B (DCDC2B); DCDC2 ...
 35-104 4.50e-16

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: 74.07  E-value: 4.50e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841   35 KRISFYKSGDPQFGGVRVVVNPRSFKTFDALLDSLSRKVPLPFGVRNISTPRGRHSITRLEELEDGKSYV 104
Cdd:cd17150      1 KNVVVYRNGDPFFTGRKFVVNQRQFLTFEAFLNEVTSNIQAPVAVRNLYTPREGHRVTELGDLQNGGHYV 70
DCX1_DCX cd16112
Dublecortin-like domain 1 found in neuronal migration protein doublecortin (DCX); DCX, also ...
 34-111 8.40e-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: 73.80  E-value: 8.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841   34 AKRISFYKSGDPQFGGVRVVVNPRSFKTFDALL----DSLSRKVPLPFGVRNISTPRGRHSITRLEELEDGKSYVC-SHN 108
Cdd:cd16112      2 AKKVRFYRNGDRYFKGIVYAVSSDRFRSFDALLadltRSLSDNINLPQGVRYIYTIDGSRKIGSMDELEEGESYVCsSDN 81


                   ....*
gi 1681348841  109 --KKV 111
Cdd:cd16112     82 ffKKV 86
DCX1_DCDC2 cd17149
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is ...
 35-104 1.55e-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: 1.55e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681348841   35 KRISFYKSGDPQFGGVRVVVNPRSFKTFDALLDSLSRKVPLPFG-VRNISTPRGRHSITRLEELEDGKSYV 104
Cdd:cd17149      1 KNVLVYRNGDPFYAGRRLVINEKRVSSFEVFLKEVTGGVQAPFGaVRNIYTPRGGHRVRSLEQLQSGEQYV 71
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 975-1076 2.12e-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: 73.23  E-value: 2.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  975 YHVDVYTGQLKQAKTESEVSLCLYGERGDSGLRLLHRSNMPvrFQRGQIDAFQI-EAVSLGNLQKALLHCEASDKSQYWY 1053
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPD--FERGAEDSFEIdTDWDVGAILKINLHWDNNGLSDEWF 78

                           90       100
                   ....*....|....*....|....
gi 1681348841 1054 CEKIIVKDPGSS-SESIFTCERWI 1076
Cdd:pfam01477   79 LKSITVEVPGETgGKYTFPCNSWV 102
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 848-944 3.40e-15

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: 72.76  E-value: 3.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  848 KWKVLVVTGN---TGTQANVTLWVYGYEGVTGPISLTKDSQEklFLPGQTDEFQVVLRG-IGEIYKIRIGHDGTGGQPEW 923
Cdd:cd00113      2 RYTVTIKTGDkkgAGTDSNISLALYGENGNSSDIPILDGPGS--FERGSTDTFQIDLKLdIGDITKVYLRRDGSGLSDGW 79

                           90       100
                   ....*....|....*....|.
gi 1681348841  924 TLQRVTMENVKSKKTLHFVAN 944
Cdd:cd00113     80 YCESITVQALGTKKVYTFPVN 100
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 397-505 3.40e-15

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: 72.57  E-value: 3.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  397 YKVYITTGE-LWNSGTIANVYLSIYGEKGDTGSRKLfrSKNSSKFlrgqvdTFflEAVNLGDLCKIVIGHDGLGQGNGWF 475
Cdd:cd01757      3 YHVVIVPSKkLGGSMFTANPWICVSGELGETPPLQI--PKNSLEM------TF--DCQNLGKLTTVQIGHDNSGLLAKWL 72

                           90       100       110
                   ....*....|....*....|....*....|
gi 1681348841  476 LEDVVVRDPTTNHEYAFFCHRWLDEGEDDG 505
Cdd:cd01757     73 VEYVMVRNEITGHTYKFPCGRWLGEGVDDG 102
DCX1_DCLK1 cd17140
Dublecortin-like domain 1 found in doublecortin-like kinase 1 (DCLK1); DCLK1 is a member of ...
 34-106 6.67e-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: 71.19  E-value: 6.67e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681348841   34 AKRISFYKSGDPQFGGVRVVVNPRSFKTFDALLDSLSR----KVPLPFGVRNISTPRGRHSITRLEELEDGKSYVCS 106
Cdd:cd17140      2 AKKVRFYRNGDRYFKGIVYAISPDRFRSFEALLADLTRtlsdNVNLPQGVRTIYTIDGLKKISSLDQLVEGESYVCG 78
DCX cd01617
Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin ...
 157-225 1.86e-13

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: 66.48  E-value: 1.86e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681348841  157 RRLVVFRNGDPKNKHV-VLLSRRITQSFEAFLQYLTQVMQC---PVAKLYATDGRKVPSLQAVILSSGAVVAA 225
Cdd:cd01617      1 KRITVFRNGDKNFKGVkVLVKPRRFRTFDQLLDELTEKLGLptgGVRKLYTPSGKLVKSLSDLEDGESYVVCG 73
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 974-1077 2.17e-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: 67.75  E-value: 2.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  974 RYHVDVYTGQLKQAKTESEVSLCLYGERGDSGLRLLHRSnmPVRFQRGQIDAFQIEA-VSLGNLQKALLHCEASDKSQYW 1052
Cdd:cd00113      2 RYTVTIKTGDKKGAGTDSNISLALYGENGNSSDIPILDG--PGSFERGSTDTFQIDLkLDIGDITKVYLRRDGSGLSDGW 79

                           90       100
                   ....*....|....*....|....*
gi 1681348841 1053 YCEKIIVKDPGSSSESIFTCERWIP 1077
Cdd:cd00113     80 YCESITVQALGTKKVYTFPVNRWVL 104
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 849-944 5.44e-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: 66.30  E-value: 5.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  849 WKVLVVTGNT---GTQANVTLWVYGYEGVTGPISLTKDSQEklFLPGQTDEFQVVLR-GIGEIYKIRIGHDGTGGQPEWT 924
Cdd:pfam01477    1 YQVKVVTGDElgaGTDADVYISLYGKVGESAQLEITLDNPD--FERGAEDSFEIDTDwDVGAILKINLHWDNNGLSDEWF 78

                           90       100
                   ....*....|....*....|.
gi 1681348841  925 LQRVTME-NVKSKKTLHFVAN 944
Cdd:pfam01477   79 LKSITVEvPGETGGKYTFPCN 99
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
848-944 1.21e-10

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 59.58  E-value: 1.21e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841   848 KWKVLVVTGN---TGTQANVTLWVYGYEGVTGPISLtkDSQEK-LFLPGQTDEFQV-VLRGIGEIYKIRIGHDGtgGQPE 922
Cdd:smart00308    2 KYKVTVTTGGldfAGTTASVSLSLVGAEGDGKESKL--DYLFKgIFARGSTYEFTFdVDEDFGELGAVKIKNEH--RHPE 77

                            90       100
                    ....*....|....*....|..
gi 1681348841   923 WTLQRVTMENVKSKKTLHFVAN 944
Cdd:smart00308   78 WFLKSITVKDLPTGGKYHFPCN 99
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
397-500 1.72e-10

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 58.81  E-value: 1.72e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841   397 YKVYITTGELWNSGTIANVYLSIYGEKGDTGSRKL-FRSKNSskFLRGQVDTFFLE-AVNLGDLCKIVIGHDglGQGNGW 474
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLdYLFKGI--FARGSTYEFTFDvDEDFGELGAVKIKNE--HRHPEW 78

                            90       100
                    ....*....|....*....|....*.
gi 1681348841   475 FLEDVVVRDPTTNHEYAFFCHRWLDE 500
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVYP 104
DCX pfam03607
Doublecortin;
174-230 2.15e-10

Doublecortin;


Pssm-ID: 460986  Cd Length: 60  Bit Score: 57.07  E-value: 2.15e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681348841  174 LLSRRITQSFEAFLQYLTQVMQC----PVAKLYATDGRKVPSLQAvILSSGAVVAAGREPF 230
Cdd:pfam03607    1 VVNKRRFRSFDALLDELTEKVVKlpfgAVRKLYTLDGKRVTSLDE-LEDGGVYVAAGREKF 60
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 973-1076 8.19e-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: 8.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  973 VRYHVDVYTGQLKQAKTESEVSLCLYGERGDSGLRLLhrSNMPVRFQRGQIDAFQIEA-VSLGNLQKALLHceasdKSQY 1051
Cdd:cd01753      1 AEYKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLL--DRPGYDFERGAVDEYKVKVpEDLGELLLVRLR-----KRKY 73

                           90       100       110
                   ....*....|....*....|....*....|
gi 1681348841 1052 -----WYCEKIIVKDPGsSSESIFTCERWI 1076
Cdd:cd01753     74 llfdaWFCNYITVTGPG-GDEYHFPCYRWI 102
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
974-1076 1.78e-09

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 56.11  E-value: 1.78e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841   974 RYHVDVYTGQLKQAKTESEVSLCLYGERGDSGLR---LLHRsnmpVRFQRGQIDAFQIE-AVSLGNLQKALLHCEASDKS 1049
Cdd:smart00308    2 KYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESkldYLFK----GIFARGSTYEFTFDvDEDFGELGAVKIKNEHRHPE 77

                            90       100
                    ....*....|....*....|....*..
gi 1681348841  1050 qyWYCEKIIVKDPGSSSESIFTCERWI 1076
Cdd:smart00308   78 --WFLKSITVKDLPTGGKYHFPCNSWV 102
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 396-481 4.55e-09

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: 55.62  E-value: 4.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  396 TYKVYITTGELWNSGTIANVYLSIYGEKGDTGSRKLFRS------KNSSKFLRGQVDTFFLEAVNL-GDLCKIVIGHDGL 468
Cdd:cd01754      2 VYTIYVQTGSIWKAGTDSRISLQIYDADGPGLRIANLEAwgglmgAGHDYFERGNLDRFSGRGPCLpSPPCWMNLTSDGT 81

                           90
                   ....*....|...
gi 1681348841  469 GQGNGWFLEDVVV 481
Cdd:cd01754     82 GNHPGWYVNYVEV 94
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 396-499 5.83e-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: 55.01  E-value: 5.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  396 TYKVYITTGELWNSGTIANVYLSIYGEKGDtgSRKLFRSKNSSKFLRGQVDTFfleAVNLG-DLCKIVIG---------H 465
Cdd:cd01753      2 EYKVTVATGSSLFAGTDDYIYLTLVGTAGE--SEKQLLDRPGYDFERGAVDEY---KVKVPeDLGELLLVrlrkrkyllF 76

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1681348841  466 DglgqgnGWFLEDVVVRDPTTNHeYAFFCHRWLD 499
Cdd:cd01753     77 D------AWFCNYITVTGPGGDE-YHFPCYRWIE 103
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
269-369 8.35e-09

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 54.18  E-value: 8.35e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841   269 WKVSINTSDFPNAGTSSQIYIVLYG-HCRS--SAPIYLYGRDGTRfqdGHEDNFTIMV-GDIGTPFKIRVghTNSGHSPS 344
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGaEGDGkeSKLDYLFKGIFAR---GSTYEFTFDVdEDFGELGAVKI--KNEHRHPE 77

                            90       100
                    ....*....|....*....|....*
gi 1681348841   345 WHCKRIELQNMNSGEKFYIPVQRWL 369
Cdd:smart00308   78 WFLKSITVKDLPTGGKYHFPCNSWV 102
DCX1_DCDC2C cd17151
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2C (DCDC2C); DCDC2 ...
 157-231 2.22e-08

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: 52.10  E-value: 2.22e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681348841  157 RRLVVFRNGDP-KNKHVVLLSRRITQSFEAFLQYLTQVMQCP--VAKLYA-TDGRKVPSLQAvILSSGAVVAAGREPFK 231
Cdd:cd17151      1 KTILVYRNGDPfYQAHKVVIHRRRVKTFDALLRQLTETVKVPfgVRCLYTpRNGHRVKGLDD-LQGGGKYVAAGRERFK 78
DCX1_DCDC2_like cd17071
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2) and ...
 157-232 5.85e-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: 51.07  E-value: 5.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  157 RRLVVFRNGDP--KNKHVVLLSRRItQSFEAFLQYLTQVMQCP---VAKLY-ATDGRKVPSLQAvILSSGAVVAAGREPF 230
Cdd:cd17071      1 KIIVVYKNGDPffPGKKFVVNERQV-RTFDAFLNEVTSGIKAPfgaVRSIYtPTGGHRVKDLDS-LQNGGVYVAAGSERF 78


                   ..
gi 1681348841  231 KP 232
Cdd:cd17071     79 KK 80
DCX1_DCDC2 cd17149
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is ...
 161-231 1.38e-07

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: 49.77  E-value: 1.38e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681348841  161 VFRNGDP--KNKHVVLLSRRITqSFEAFLQYLTQVMQCP---VAKLYAT-DGRKVPSLQAvILSSGAVVAAGREPFK 231
Cdd:cd17149      5 VYRNGDPfyAGRRLVINEKRVS-SFEVFLKEVTGGVQAPfgaVRNIYTPrGGHRVRSLEQ-LQSGEQYVAAGRERFK 79
beta-trefoil_FGF cd00058
FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) ...
 544-663 1.43e-07

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: 51.43  E-value: 1.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  544 NTLQFYNKlSGGFVRLHPDGTVDAAGEQTDRYGLFDVIFNKGNICVFQSHE-MRHLSLNfDNG----MVGGGGHSELQVI 618
Cdd:cd00058      1 RLVRLYSR-TGYFLQILPDGTVNGTKDENSPYAILELQSVGTGLVRIKGVKtGRYLAMD-KNGklygTKKPTEDCVFKET 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1681348841  619 YQPNRCVLLESVLLP----GHTLTVDRHGKVTDESSAGYAELSKEFLVF 663
Cdd:cd00058     79 LEENGYNTYSSYKYYhtrkGWYLAIKKNGKPKRGKKTKPGQKSTQFLPL 127
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 975-1078 1.24e-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: 48.23  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  975 YHVDVYTGQLKQAKTESEVSLCLYGERGDSGLRLLHRSNMPVRFQRgqidaFQIEAVSLGNLQKALLHCEASDKSqyWYC 1054
Cdd:cd02899      3 YTASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTLSQGFYPGSLKR-----IRFRAADVGDINAIILSNTALNDP--WYC 75

                           90       100
                   ....*....|....*....|....*..
gi 1681348841 1055 EKIIVK-DPGSSseSIFTCERWI--PF 1078
Cdd:cd02899     76 DYVRIKsEDGKV--FAFNVKRWIgyPY 100
DCX2_DCDC2_like cd16113
Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is ...
 34-104 2.79e-06

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: 46.03  E-value: 2.79e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681348841   34 AKRISFYKSGDPQFGGVRVVVNPRSFKTFDALLDSLSRKVPLPFG-VRNISTPRGrHSITRLEELEDGKSYV 104
Cdd:cd16113      1 PKTIHVFPNGDLLHPPSKVLLTKRRLPNWDTVLEEVTEKVKLQTGaVRKLYTLDG-KRISDPDELVNGGQYV 71
DCX1_DCDC2B cd17150
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2B (DCDC2B); DCDC2 ...
 157-231 5.42e-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: 45.56  E-value: 5.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  157 RRLVVFRNGDP--KNKHVVLLSRRITqSFEAFLQYLTQVMQCPVA--KLYAT-DGRKVPSLqAVILSSGAVVAAGREPFK 231
Cdd:cd17150      1 KNVVVYRNGDPffTGRKFVVNQRQFL-TFEAFLNEVTSNIQAPVAvrNLYTPrEGHRVTEL-GDLQNGGHYVAAGFERFK 78
DCX_DCLK3 cd16111
Doublecortin-like domain found in doublecortin-like kinase 3 (DCLK3); DCLK3 is a member of ...
 156-229 9.01e-06

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: 45.12  E-value: 9.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  156 PRRLVVFRNGD-PKNKHVVLLSRRITQSFEAFLQYLTQVMQCP------VAKLYATDGRKVPSLQAVILSSGAVVAAGRE 228
Cdd:cd16111      2 PKVITVVRNGGqPRTKITILLNRRSVQTFEQLMADISEALGFPrwkndrVRKLYSLRGREVRSVSDFFREDDVFIATGRE 81


                   .
gi 1681348841  229 P 229
Cdd:cd16111     82 Q 82
DCX2_DCX cd17142
Dublecortin-like domain 2 found in neuronal migration protein doublecortin (DCX); DCX, also ...
 156-231 3.47e-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: 43.50  E-value: 3.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  156 PRRLVVFRNG-DPKNKHVVLLSRRITQSFEAFLQYLTQVMQCP---VAKLYATDGRKVPSLQAVILSSGAVVAAGREPFK 231
Cdd:cd17142      4 PKLVTIIRSGvKPRKAVRVLLNKKTAHSFEQVLTDITEAIKLEtgvVKKLYTLDGKQVTCLHDFFGDDDVFIACGPEKFR 83
DCX2 cd17069
Dublecortin-like domain 2; Members in doublecortin (DCX) gene family are ...
 156-230 6.84e-05

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: 42.37  E-value: 6.84e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681348841  156 PRRLVVFRNGDPKNKHV-VLLSRRITQSFEAFLQYLTQVMQC---PVAKLYATDGRKVPSLQAVILSSGAVVAAGREPF 230
Cdd:cd17069      4 PKLVTVIRNGTKPRKAVrILLNKKTAHSFEQVLTDITEAIKLdsgAVRKLFTLDGRQVTCLQDFFGDDDVFIAYGPEKF 82
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 849-941 1.28e-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: 42.53  E-value: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  849 WKVLVVT----GNTGTQANVTLWVYGYEGVTGPISLTKDSQEKLFLpgqtdefqvvLRGIGEIYKIRIGHDGTGGQPEWT 924
Cdd:cd01757      3 YHVVIVPskklGGSMFTANPWICVSGELGETPPLQIPKNSLEMTFD----------CQNLGKLTTVQIGHDNSGLLAKWL 72

                           90
                   ....*....|....*..
gi 1681348841  925 LQRVTMENVKSKKTLHF 941
Cdd:cd01757     73 VEYVMVRNEITGHTYKF 89
DCX2_DCDC2_like cd16113
Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is ...
 156-226 5.25e-04

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: 39.48  E-value: 5.25e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681348841  156 PRRLVVFRNGDPKNKHV-VLLSRRITQSFEAFLQYLT---QVMQCPVAKLYATDGRKVPSLqAVILSSGAVVAAG 226
Cdd:cd16113      1 PKTIHVFPNGDLLHPPSkVLLTKRRLPNWDTVLEEVTekvKLQTGAVRKLYTLDGKRISDP-DELVNGGQYVAVG 74
FGF pfam00167
Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in ...
 547-581 1.07e-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: 1.07e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1681348841  547 QFYNKLSGGFVRLHPDGTVDAAGEQTDRYGLFDVI 581
Cdd:pfam00167    4 RLYCRTGGFHLQILPDGKVDGTGEDGSPYSILEIE 38
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 271-369 1.82e-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: 38.98  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  271 VSINTSDFPNAGTSSQIYIVLYGHCRSSAPIYLYgrdgTRFQDGHEDNFTIMVGDIGTPFKIRVghTNSGHSPSWHCKRI 350
Cdd:cd02899      5 ASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTLS----QGFYPGSLKRIRFRAADVGDINAIIL--SNTALNDPWYCDYV 78

                           90
                   ....*....|....*....
gi 1681348841  351 ELQNmNSGEKFYIPVQRWL 369
Cdd:cd02899     79 RIKS-EDGKVFAFNVKRWI 96
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 269-369 2.98e-03

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: 38.44  E-value: 2.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  269 WKVSINTSDFPNAGTSSQIYIVLYGHCRSSAPIYLyGRDGTRFQDGHEDNFTIMVG-DIGTPFKIRVGHTNSGHSPSWHC 347
Cdd:cd01753      3 YKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLL-DRPGYDFERGAVDEYKVKVPeDLGELLLVRLRKRKYLLFDAWFC 81

                           90       100
                   ....*....|....*....|..
gi 1681348841  348 KRIELQNMNsGEKFYIPVQRWL 369
Cdd:cd01753     82 NYITVTGPG-GDEYHFPCYRWI 102
PLAT_SR cd02899
Scavenger receptor protein. A subfamily of PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) ...
 396-498 4.40e-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: 37.83  E-value: 4.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  396 TYKVYITTGELWNSGTIANVYLSIYGEKGDTGSRKLFRSknsskFLRGQVDTFFLEAVNLGDLCKIVIGHDGLgqGNGWF 475
Cdd:cd02899      2 TYTASVQTGKDKEAGTNGTIEITLLGSSGRSNPKTLSQG-----FYPGSLKRIRFRAADVGDINAIILSNTAL--NDPWY 74

                           90       100
                   ....*....|....*....|...
gi 1681348841  476 LEDVVVRDpTTNHEYAFFCHRWL 498
Cdd:cd02899     75 CDYVRIKS-EDGKVFAFNVKRWI 96
DCX2_DCDC5 cd17157
Doublecortin-like domain 2 found in doublecortin domain-containing protein 5 (DCDC5); DCDC5 is ...
 157-226 6.01e-03

Doublecortin-like domain 2 found in doublecortin domain-containing protein 5 (DCDC5); DCDC5 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. 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. DCDC5 is expressed during mitosis and involved in coordinating late cytokinesis. DCDC5 interacts with cytoplasmic dynein and Rab8, as well as with the Rab8 nucleotide exchange factor Rabin8.


Pssm-ID: 340677  Cd Length: 86  Bit Score: 36.94  E-value: 6.01e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681348841  157 RRLVVFRNGDPKNKHVVLLSrriTQSFEAFLQYLTQVMQ--CPVAKLYATDGRKVPSLQAVILSSGAVVAAG 226
Cdd:cd17157      1 RRILVFKNGDGSEGYEIVAD---LDEFEQFLDACTSKLNlgSPARVLYDWEGKEIKDLSEAPKLDKCLQNSS 69
KHA cd17073
KHA, dimerization domain of potassium ion channel, similar to doublecortin-like domain, found ...
 157-206 7.25e-03

KHA, dimerization domain of potassium ion channel, similar to doublecortin-like domain, found in potassium channel tetramerization domain containing 9 (KCTD9) and similar proteins; This family corresponds to KHA, the tetramerization domain of eukaryotic voltage-dependent potassium ion-channel proteins, mainly found in vertebrates KCTD9 and plants AKT proteins. In plants the domain lies at the C-terminus whereas in many chordates it lies at the N-terminus. KHA shows high sequence similarity with doublecortin-like domain, which has a stable ubiquitin-like tertiary fold. KCTD9, also termed BTB/POZ domain-containing protein 9, belongs to the KCTD protein family, which corresponds to potassium channel tetramerization domain proteins, a class of BTB-domain-containing proteins. It is involved in potassium channel formation. Moreover, KCTD9 contributes to liver injury through NK cell activation during hepatitis B virus (HBV)-induced acute-on-chronic liver failure. AKT proteins play crucial roles in K+ uptake and translocation in plant cells.


Pssm-ID: 340593  Cd Length: 65  Bit Score: 36.04  E-value: 7.25e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1681348841  157 RRLVVFRNGDPKNKHVVLLsrriTQSFEAFLQYLTQVMQCPVAKLYATDG 206
Cdd:cd17073      1 KRVTVFVNGSSSGGKVIAL----PSTLSELLKIASEKLGIPAKRLYTGSG 46
DCX2_DCLK1 cd17143
Dublecortin-like domain 2 found in doublecortin-like kinase 1 (DCLK1); DCLK1 is a member of ...
 156-231 7.61e-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: 36.86  E-value: 7.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681348841  156 PRRLVVFRNG-DPKNKHVVLLSRRITQSFEAFLQYLTQVMQC---PVAKLYATDGRKVPSLQAVILSSGAVVAAGREPFK 231
Cdd:cd17143      4 PKLVTIIRSGvKPRKAVRILLNKKTAHSFEQVLTDITDAIKLdsgVVKRLYTLDGKQVMCLQDFFGDDDIFIACGPEKFR 83
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH