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Conserved domains on  [gi|2051959432|ref|XP_041909651|]
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protein piccolo isoform X8 [Corvus kubaryi]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
4528-4621 3.89e-48

PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RIM, RIM2, piccolo and related domains. RIM proteins and Gallus gallus protein piccolo (also called aczonin) are involved in neurotransmitter release at presynaptic active zones, the site of vesicle fusion. A protein complex containing RIM proteins positions synaptic vesicles containing synaptotagmin at the active zone. RIM proteins simultaneously activate docking and priming of synaptic vesicles and recruit Ca2+-channels to active zones, thereby connecting primed synaptic vesicles to Ca2+-channels. RIM binding to vesicular Rab proteins (Rab3 and Rab27 isoforms) mediates vesicle docking; RIM binding to Munc13 activates vesicle priming; RIM binding to the Ca2+-channel, both directly and indirectly via RIM-BP, recruits the Ca2+-channels. The RIM PDZ domain interacts with the C-termini of N- and P/Q-type voltage-gated Ca2+-channels. RIM1, RIM2 and piccolo also participate in regulated exocytosis through binding cAMP-GEFII (cAMP-binding protein-guanidine nucleotide exchange factor II). The piccolo PDZ domain binds cAMP-GEFII. RIM2 also plays a role in dendrite formation by melanocytes. Caenorhabditis elegans RIM (also known as unc-10) may be involved in the regulation of defecation and daumone response. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


:

Pssm-ID: 467198 [Multi-domain]  Cd Length: 95  Bit Score: 167.73  E-value: 3.89e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 4528 FPHTRLKLLRDPKDHTVSGNGLGIRVVGGKEIPgsSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEV 4607
Cdd:cd06714      2 FLIGRIILQRDPKDGSVSGNGLGLKVVGGKMTE--SGRLGAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEV 79
                           90
                   ....*....|....
gi 2051959432 4608 QSIIIQQSGEAEIC 4621
Cdd:cd06714     80 QDIISQSKGEVELV 93
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
456-517 1.47e-42

FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the first FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


:

Pssm-ID: 277313 [Multi-domain]  Cd Length: 62  Bit Score: 150.57  E-value: 1.47e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432  456 TFCPLCTTTELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRALGG 517
Cdd:cd15774      1 TICPLCKTTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
922-985 3.86e-42

FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the second FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


:

Pssm-ID: 277315 [Multi-domain]  Cd Length: 64  Bit Score: 149.45  E-value: 3.86e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051959432  922 MSCPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSGQLG 985
Cdd:cd15776      1 LLCPLCKTELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQLG 64
PHA03247 super family cl33720
large tegument protein UL36; Provisional
250-751 3.38e-20

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 100.40  E-value: 3.38e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  250 VQKPGHRQPADAKQEQVKQPPQPRGPQKSQPQPSE-----------PAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQA 318
Cdd:PHA03247  2582 VTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPlppdthapdppPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRV 2661
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  319 PPPTKPSSQ-QPGPAKQPLQQPARQGGP--VKPSSQQAGPPKQlSQQPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPV 395
Cdd:PHA03247  2662 SRPRRARRLgRAAQASSPPQRPRRRAARptVGSLTSLADPPPP-PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPA 2740
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  396 KQVPPQA-----GPTKP--PSQTAGPTKP-PAQQPGPTKPSGQQPGPEKPLEQKQAGASQPTESVSKKTFCPLCTTTELL 467
Cdd:PHA03247  2741 PPAVPAGpatpgGPARParPPTTAGPPAPaPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP 2820
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  468 LHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEwlclncqmqrALGGDLAagHGPGPQPPAPKQKTPI-PPSTAKPS 546
Cdd:PHA03247  2821 AASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV----------APGGDVR--RRPPSRSPAAKPAAPArPPVRRLAR 2888
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  547 PQPQPvqkkditskpdpsqladpkkpppQKKQTPLPGSPPVKSKQPRAEPTEISQQTRDATPKSDQVKPTQAE-DKQKQP 625
Cdd:PHA03247  2889 PAVSR-----------------------STESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRpQPPLAP 2945
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  626 SVQKPTADTVSTSAALEQKQDLAGPRPPTQQKVTDSPKPELAKPSQDTHPAEDKPDskpvPQVSRQKSDPKLASQPGARP 705
Cdd:PHA03247  2946 TTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSL----SRVSSWASSLALHEETDPPP 3021
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051959432  706 DAKAQKPVEPTQTKD---------DPKK--------LPTKPAPKPDTKAAPKGPQAGAGPKPG 751
Cdd:PHA03247  3022 VSLKQTLWPPDDTEDsdadslfdsDSERsdlealdpLPPEPHDPFAHEPDPATPEAGARESPS 3084
PTZ00121 super family cl31754
MAEBL; Provisional
1032-1745 2.01e-10

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.86  E-value: 2.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1032 AKPKEEPGIQKEAPKLQQGRleKTLSADKIQQGVQREDAKpKQGKLVKTPSADKIQRASQKEDPR-IQQTRLTKTAsydR 1110
Cdd:PTZ00121  1151 AKRVEIARKAEDARKAEEAR--KAEDAKKAEAARKAEEVR-KAEELRKAEDARKAEAARKAEEERkAEEARKAEDA---K 1224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1111 VLHEVQKEDEKLQEAKLAKTSSADKilhgVQKEDIKLQETKLAKIPSADKILQGiqKEDPKLQQMKMAKAL-SADKIQPA 1189
Cdd:PTZ00121  1225 KAEAVKKAEEAKKDAEEAKKAEEER----NNEEIRKFEEARMAHFARRQAAIKA--EEARKADELKKAEEKkKADEAKKA 1298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1190 VQKEDAQLQEVKLPKAASVDKIQHgiQKEDIKLQHEKIKKTRSVDKIQEEDQKEETKLQRGKLSKTPSANKIPATTTADQ 1269
Cdd:PTZ00121  1299 EEKKKADEAKKKAEEAKKADEAKK--KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1270 KKPLNTV----EEDKETVPPEKSTPHPEDKKEEITaeiKDHVAKQKAEvEAPYKGLQAKEQEDVKKEdlttgiSQEVLKT 1345
Cdd:PTZ00121  1377 KKKADAAkkkaEEKKKADEAKKKAEEDKKKADELK---KAAAAKKKAD-EAKKKAEEKKKADEAKKK------AEEAKKA 1446
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1346 EKAQEEEIPVQTAplprtdhvEAVREKIEkEDDKSDTSSSQqqkspqglsdtgyssdgissslgeipshipTDEKDLLKE 1425
Cdd:PTZ00121  1447 DEAKKKAEEAKKA--------EEAKKKAE-EAKKADEAKKK------------------------------AEEAKKADE 1487
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1426 SNKKdtiSQESPPSPSDLAKLESTVLSILEAQantlSDEKSAKSKELSETYGEQTKDQLKTKPLPVTPESYSSDEEDLKA 1505
Cdd:PTZ00121  1488 AKKK---AEEAKKKADEAKKAAEAKKKADEAK----KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1506 ---IKEGEGTIVEEGKGTASSQAD-------------YKEDHEGEDIPARRQQRYDSVEDSSESENSPVPRRKRRTSVGS 1569
Cdd:PTZ00121  1561 eekKKAEEAKKAEEDKNMALRKAEeakkaeearieevMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1570 SSSDEYKRDDSQGSGDEEDFIRKQIIEMSADEDASGSEddEFIRNQLKEISAAES-QKKEEVKSKAKGTAGKHRRMARKS 1648
Cdd:PTZ00121  1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE--EAKKAEEDEKKAAEAlKKEAEEAKKAEELKKKEAEEKKKA 1718
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1649 SAGYDEDAGRRHSWHDDDDEtfDESPEPKYRESKSQDGEELAISGGGGLRRFKTIELNSTITAKYSEVSEQQkgilyfDE 1728
Cdd:PTZ00121  1719 EELKKAEEENKIKAEEAKKE--AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE------DE 1790
                          730
                   ....*....|....*..
gi 2051959432 1729 EPELEMESLTDSPEDRS 1745
Cdd:PTZ00121  1791 KRRMEVDKKIKDIFDNF 1807
CCDC47 super family cl46382
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
3786-3849 4.12e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


The actual alignment was detected with superfamily member pfam07946:

Pssm-ID: 480722  Cd Length: 323  Bit Score: 42.94  E-value: 4.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051959432 3786 ARAKILQDIDRELDLVERESAKLRKKQAELDEEEKEIDaklrylEMGINRRKEALLKEREKRER 3849
Cdd:pfam07946  265 TREEEIEKIKKAAEEERAEEAQEKKEEAKKKEREEKLA------KLSPEEQRKYEEKERKKEQR 322
 
Name Accession Description Interval E-value
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
4528-4621 3.89e-48

PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RIM, RIM2, piccolo and related domains. RIM proteins and Gallus gallus protein piccolo (also called aczonin) are involved in neurotransmitter release at presynaptic active zones, the site of vesicle fusion. A protein complex containing RIM proteins positions synaptic vesicles containing synaptotagmin at the active zone. RIM proteins simultaneously activate docking and priming of synaptic vesicles and recruit Ca2+-channels to active zones, thereby connecting primed synaptic vesicles to Ca2+-channels. RIM binding to vesicular Rab proteins (Rab3 and Rab27 isoforms) mediates vesicle docking; RIM binding to Munc13 activates vesicle priming; RIM binding to the Ca2+-channel, both directly and indirectly via RIM-BP, recruits the Ca2+-channels. The RIM PDZ domain interacts with the C-termini of N- and P/Q-type voltage-gated Ca2+-channels. RIM1, RIM2 and piccolo also participate in regulated exocytosis through binding cAMP-GEFII (cAMP-binding protein-guanidine nucleotide exchange factor II). The piccolo PDZ domain binds cAMP-GEFII. RIM2 also plays a role in dendrite formation by melanocytes. Caenorhabditis elegans RIM (also known as unc-10) may be involved in the regulation of defecation and daumone response. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467198 [Multi-domain]  Cd Length: 95  Bit Score: 167.73  E-value: 3.89e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 4528 FPHTRLKLLRDPKDHTVSGNGLGIRVVGGKEIPgsSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEV 4607
Cdd:cd06714      2 FLIGRIILQRDPKDGSVSGNGLGLKVVGGKMTE--SGRLGAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEV 79
                           90
                   ....*....|....
gi 2051959432 4608 QSIIIQQSGEAEIC 4621
Cdd:cd06714     80 QDIISQSKGEVELV 93
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
456-517 1.47e-42

FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the first FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277313 [Multi-domain]  Cd Length: 62  Bit Score: 150.57  E-value: 1.47e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432  456 TFCPLCTTTELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRALGG 517
Cdd:cd15774      1 TICPLCKTTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
922-985 3.86e-42

FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the second FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277315 [Multi-domain]  Cd Length: 64  Bit Score: 149.45  E-value: 3.86e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051959432  922 MSCPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSGQLG 985
Cdd:cd15776      1 LLCPLCKTELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQLG 64
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
923-980 5.45e-37

Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. There are eight conserved cysteines, suggesting that it coordinates two zinc ligands.


Pssm-ID: 461722 [Multi-domain]  Cd Length: 60  Bit Score: 134.85  E-value: 5.45e-37
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2051959432  923 SCPLCK-TGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAM 980
Cdd:pfam05715    2 LCPLCKtTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
456-515 7.80e-37

Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. There are eight conserved cysteines, suggesting that it coordinates two zinc ligands.


Pssm-ID: 461722 [Multi-domain]  Cd Length: 60  Bit Score: 134.47  E-value: 7.80e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  456 TFCPLCTTTELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRAL 515
Cdd:pfam05715    1 TLCPLCKTTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
PHA03247 PHA03247
large tegument protein UL36; Provisional
250-751 3.38e-20

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 100.40  E-value: 3.38e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  250 VQKPGHRQPADAKQEQVKQPPQPRGPQKSQPQPSE-----------PAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQA 318
Cdd:PHA03247  2582 VTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPlppdthapdppPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRV 2661
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  319 PPPTKPSSQ-QPGPAKQPLQQPARQGGP--VKPSSQQAGPPKQlSQQPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPV 395
Cdd:PHA03247  2662 SRPRRARRLgRAAQASSPPQRPRRRAARptVGSLTSLADPPPP-PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPA 2740
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  396 KQVPPQA-----GPTKP--PSQTAGPTKP-PAQQPGPTKPSGQQPGPEKPLEQKQAGASQPTESVSKKTFCPLCTTTELL 467
Cdd:PHA03247  2741 PPAVPAGpatpgGPARParPPTTAGPPAPaPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP 2820
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  468 LHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEwlclncqmqrALGGDLAagHGPGPQPPAPKQKTPI-PPSTAKPS 546
Cdd:PHA03247  2821 AASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV----------APGGDVR--RRPPSRSPAAKPAAPArPPVRRLAR 2888
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  547 PQPQPvqkkditskpdpsqladpkkpppQKKQTPLPGSPPVKSKQPRAEPTEISQQTRDATPKSDQVKPTQAE-DKQKQP 625
Cdd:PHA03247  2889 PAVSR-----------------------STESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRpQPPLAP 2945
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  626 SVQKPTADTVSTSAALEQKQDLAGPRPPTQQKVTDSPKPELAKPSQDTHPAEDKPDskpvPQVSRQKSDPKLASQPGARP 705
Cdd:PHA03247  2946 TTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSL----SRVSSWASSLALHEETDPPP 3021
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051959432  706 DAKAQKPVEPTQTKD---------DPKK--------LPTKPAPKPDTKAAPKGPQAGAGPKPG 751
Cdd:PHA03247  3022 VSLKQTLWPPDDTEDsdadslfdsDSERsdlealdpLPPEPHDPFAHEPDPATPEAGARESPS 3084
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
169-597 5.08e-14

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 79.43  E-value: 5.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  169 NPFDLISDSDTTHEDAgrkqkvtpKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPK 248
Cdd:pfam03154  150 SPQDNESDSDSSAQQQ--------ILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQT 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  249 QVQKPGHRQPADAKQEQVKQPPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQ 328
Cdd:pfam03154  222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLT 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  329 PgpakqplqQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPT--K 406
Cdd:pfam03154  302 P--------QSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQshK 373
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  407 PPSQTAGPT---------KPPAQQPGPT----KPSGQQPGPEKPLEQKQAGASQPTESvskktfcPLCTTTEllLHTPEK 473
Cdd:pfam03154  374 HPPHLSGPSpfqmnsnlpPPPALKPLSSlsthHPPSAHPPPLQLMPQSQQLPPPPAQP-------PVLTQSQ--SLPPPA 444
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  474 ANYNTCTQCHTVVcSLCGFNPNPHITEISEWLCLNCQMQRAlggdlAAGHGPGPQPP---APKQKTPIPPSTAKPSPqpq 550
Cdd:pfam03154  445 ASHPPTSGLHQVP-SQSPFPQHPFVPGGPPPITPPSGPPTS-----TSSAMPGIQPPssaSVSSSGPVPAAVSCPLP--- 515
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 2051959432  551 PVQKKDitSKPDPSQladpkkpppqkkqtpLPGSPPVKSKQPRAEPT 597
Cdd:pfam03154  516 PVQIKE--EALDEAE---------------EPESPPPPPRSPSPEPT 545
PTZ00121 PTZ00121
MAEBL; Provisional
1032-1745 2.01e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.86  E-value: 2.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1032 AKPKEEPGIQKEAPKLQQGRleKTLSADKIQQGVQREDAKpKQGKLVKTPSADKIQRASQKEDPR-IQQTRLTKTAsydR 1110
Cdd:PTZ00121  1151 AKRVEIARKAEDARKAEEAR--KAEDAKKAEAARKAEEVR-KAEELRKAEDARKAEAARKAEEERkAEEARKAEDA---K 1224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1111 VLHEVQKEDEKLQEAKLAKTSSADKilhgVQKEDIKLQETKLAKIPSADKILQGiqKEDPKLQQMKMAKAL-SADKIQPA 1189
Cdd:PTZ00121  1225 KAEAVKKAEEAKKDAEEAKKAEEER----NNEEIRKFEEARMAHFARRQAAIKA--EEARKADELKKAEEKkKADEAKKA 1298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1190 VQKEDAQLQEVKLPKAASVDKIQHgiQKEDIKLQHEKIKKTRSVDKIQEEDQKEETKLQRGKLSKTPSANKIPATTTADQ 1269
Cdd:PTZ00121  1299 EEKKKADEAKKKAEEAKKADEAKK--KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1270 KKPLNTV----EEDKETVPPEKSTPHPEDKKEEITaeiKDHVAKQKAEvEAPYKGLQAKEQEDVKKEdlttgiSQEVLKT 1345
Cdd:PTZ00121  1377 KKKADAAkkkaEEKKKADEAKKKAEEDKKKADELK---KAAAAKKKAD-EAKKKAEEKKKADEAKKK------AEEAKKA 1446
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1346 EKAQEEEIPVQTAplprtdhvEAVREKIEkEDDKSDTSSSQqqkspqglsdtgyssdgissslgeipshipTDEKDLLKE 1425
Cdd:PTZ00121  1447 DEAKKKAEEAKKA--------EEAKKKAE-EAKKADEAKKK------------------------------AEEAKKADE 1487
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1426 SNKKdtiSQESPPSPSDLAKLESTVLSILEAQantlSDEKSAKSKELSETYGEQTKDQLKTKPLPVTPESYSSDEEDLKA 1505
Cdd:PTZ00121  1488 AKKK---AEEAKKKADEAKKAAEAKKKADEAK----KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1506 ---IKEGEGTIVEEGKGTASSQAD-------------YKEDHEGEDIPARRQQRYDSVEDSSESENSPVPRRKRRTSVGS 1569
Cdd:PTZ00121  1561 eekKKAEEAKKAEEDKNMALRKAEeakkaeearieevMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1570 SSSDEYKRDDSQGSGDEEDFIRKQIIEMSADEDASGSEddEFIRNQLKEISAAES-QKKEEVKSKAKGTAGKHRRMARKS 1648
Cdd:PTZ00121  1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE--EAKKAEEDEKKAAEAlKKEAEEAKKAEELKKKEAEEKKKA 1718
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1649 SAGYDEDAGRRHSWHDDDDEtfDESPEPKYRESKSQDGEELAISGGGGLRRFKTIELNSTITAKYSEVSEQQkgilyfDE 1728
Cdd:PTZ00121  1719 EELKKAEEENKIKAEEAKKE--AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE------DE 1790
                          730
                   ....*....|....*..
gi 2051959432 1729 EPELEMESLTDSPEDRS 1745
Cdd:PTZ00121  1791 KRRMEVDKKIKDIFDNF 1807
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
510-794 6.41e-09

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 62.09  E-value: 6.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  510 QMQRALGGDLAAGHGPGPQPPAPKQKTPIPPSTAKP--SPQPQPVQKK----DITSKPDPSQLADPKKPPPQKKQTPLPG 583
Cdd:NF033839   142 KFEKDSSSSSSSGSSTKPETPQPENPEHQKPTTPAPdtKPSPQPEGKKpsvpDINQEKEKAKLAVATYMSKILDDIQKHH 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  584 SPPVKSKQPRAEPTEISQQTRDATPKSDQVKPtqaeDKQKQPSVQKPTADTVSTSAALEQKQDLAGPRPPtqqkvtDSPK 663
Cdd:NF033839   222 LQKEKHRQIVALIKELDELKKQALSEIDNVNT----KVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEP------GNKK 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  664 PELAKPSQDTHPAEDKPDSKPVPQVSRQKSDPKLAS-QPGARPDAKAQKP-VEPTQTKDDPKKLPTKPAPKPDTKAAPKG 741
Cdd:NF033839   292 PSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKpKPEVKPQPEKPKPeVKPQLETPKPEVKPQPEKPKPEVKPQPEK 371
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2051959432  742 PQAGAGPKPGPAQPAPQPQPPQKTPEQSRRFSLNLGGItdapKPQPTTPQETV 794
Cdd:NF033839   372 PKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEV----KPQPEKPKPEV 420
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
191-435 7.87e-09

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 61.71  E-value: 7.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  191 TPKEQGKPEeqrspakhptqPQSPKPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPKQVQKPghrQPADAKQEQVKQPP 270
Cdd:NF033839   283 TPKEPGNKK-----------PSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKP---QPEKPKPEVKPQLE 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  271 QPRGPQKsqPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPlqQPARQGGPVKPSS 350
Cdd:NF033839   349 TPKPEVK--PQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKP--QPEKPKPEVKPQP 424
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  351 QQAGPPKQlsqqPGPEKPSAQQTgpakqpPQPGSGKPplqqtgpvkQVPPQAGPTKPPSQTAGPTKPPAQQPGPTKPSGQ 430
Cdd:NF033839   425 EKPKPEVK----PQPEKPKPEVK------PQPEKPKP---------EVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPD 485

                   ....*
gi 2051959432  431 QPGPE 435
Cdd:NF033839   486 NSKPQ 490
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
527-789 9.30e-08

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 58.24  E-value: 9.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  527 PQPPApKQKTPIPPSTAKPSPQPQpvqkkditSKPDPSQLADPKKPPPQKKQTPLPGSPPvkskQPRAEPTEISQQTRDA 606
Cdd:NF033839   284 PKEPG-NKKPSAPKPGMQPSPQPE--------KKEVKPEPETPKPEVKPQLEKPKPEVKP----QPEKPKPEVKPQLETP 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  607 TPKSDQVKPTQAEDKQKQPSVQKPTADTVSTSAALEQKQDLAGPRPPTQqkvtdsPKPELAKPSQDTHPAEDKPDSKPVP 686
Cdd:NF033839   351 KPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVK------PQPEKPKPEVKPQPEKPKPEVKPQP 424
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  687 QVSRQKSDPKLAS-QPGARPDAKAQKP-VEPTQTKDDPKKLPTKPAPKPDTKAAPKGPQAGAGPKPGPAQPAPQPQPPQK 764
Cdd:NF033839   425 EKPKPEVKPQPEKpKPEVKPQPEKPKPeVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPSTPNNLSK 504
                          250       260
                   ....*....|....*....|....*
gi 2051959432  765 TPEQSRRFSLNLGGITDAPKPQPTT 789
Cdd:NF033839   505 DKQPSNQASTNEKATNKPKKSLPST 529
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
169-457 2.48e-07

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 57.00  E-value: 2.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  169 NPFDLISDSDTTHEDAGRKQKVTPKeqGKPEEQRSPAKHPTQPQSPKPAVQQQGQQRPTLQ------------------Q 230
Cdd:COG5180    213 EPPDLTGGADHPRPEAASSPKVDPP--STSEARSRPATVDAQPEMRPPADAKERRRAAIGDtpaaeppglpvleagsepQ 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  231 TESSKPVPQQQQQPGEPKQVQK--------PGHRQPADAKQEQVKQPPQ---PRGPQKSQP-------QPSEPAKPVQQQ 292
Cdd:COG5180    291 SDAPEAETARPIDVKGVASAPPatrpvrppGGARDPGTPRPGQPTERPAgvpEAASDAGQPpsayppaEEAVPGKPLEQG 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  293 TSAKLSSGPTKPSPQQPDSAKTTS-----------QAPPPTKPSSQQPGPAKQPLQQPARQGGPVKPSSQQAGPPKQLSQ 361
Cdd:COG5180    371 APRPGSSGGDGAPFQPPNGAPQPGlgrrgapgppmGAGDLVQAALDGGGRETASLGGAAGGAGQGPKADFVPGDAESVSG 450
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  362 QPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPtkppsqtAGPTKPPAQQPGPTKPSGQQPGPEKPLEQK 441
Cdd:COG5180    451 PAGLADQAGAAASTAMADFVAPVTDATPVDVADVLGVRPDAIL-------GGNVAPASGLDAETRIIEAEGAPATEDFVA 523
                          330
                   ....*....|....*.
gi 2051959432  442 qAGASQPTESVSKKTF 457
Cdd:COG5180    524 -AELSELREAAEEKTG 538
PHA03247 PHA03247
large tegument protein UL36; Provisional
518-1030 2.35e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 2.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  518 DLAAGHGPGPQPPAPKQKTPIPPSTAKPSPQPQP------VQKKDitSKPD-PSQLA-------DPKKPPPQKKQTPLP- 582
Cdd:PHA03247  2542 ELASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPrpsepaVTSRA--RRPDaPPQSArprapvdDRGDPRGPAPPSPLPp 2619
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  583 --GSPPVKSKQPRAEPTEISQQTRDATPKSDQVKPTQAEDKQKQPSVQKPTADTVSTSAALEqkqdlaGPRPPTQQKvTD 660
Cdd:PHA03247  2620 dtHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQ------RPRRRAARP-TV 2692
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  661 SPKPELAKPsqdtHPAEDKPDSKPVPQVSRQKSDPKLASQPGARPDAKAQkPVEP-----TQTKDDPKKLPTKPAPK-PD 734
Cdd:PHA03247  2693 GSLTSLADP----PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAA-PAPPavpagPATPGGPARPARPPTTAgPP 2767
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  735 TKAAPKGPQAGAGPKPGPAQPAPQPQPPQKTPEQS-----------RRFSLNLGGITDAPKPQPTTPQETVTGKlfgfgA 803
Cdd:PHA03247  2768 APAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWdpadppaavlaPAAALPPAASPAGPLPPPTSAQPTAPPP-----P 2842
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  804 SFFSQASNLISTAGQPGSQTSgappaakqpqpppqppapqtapketgqaqppPKVVPVKKEAKPLTTEKSEPSKVdsvlt 883
Cdd:PHA03247  2843 PGPPPPSLPLGGSVAPGGDVR-------------------------------RRPPSRSPAAKPAAPARPPVRRL----- 2886
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  884 kgsdleKKPGLAKDSKPQAAEAKKPDGLLEPDKASQPEMSCPLCKTGLNIGSKDPPNfntcteckkvvcnlcgfNPMPHI 963
Cdd:PHA03247  2887 ------ARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP-----------------RPQPPL 2943
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051959432  964 AEVQEWLCLNCQTQRAMSGQLGDM--GKVPLPKTGPSQPTSKPPAPPQKQPMPAVSHSPQKTSTPPTLA 1030
Cdd:PHA03247  2944 APTTDPAGAGEPSGAVPQPWLGALvpGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLA 3012
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
4540-4611 1.23e-05

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 46.12  E-value: 1.23e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432 4540 KDHTVSGNGLGIRVVGGkeipGSSGEIGAYIAKILPGGNAEQTGkLIEGMQVLEWNGIPLTGKTYEEVQSII 4611
Cdd:pfam00595    3 TLEKDGRGGLGFSLKGG----SDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLAL 69
Amelin smart00817
Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin ...
300-422 1.44e-05

Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin precursor (Amelin) proteins. Matrix proteins of tooth enamel consist mainly of amelogenin but also of non-amelogenin proteins, which, although their volumetric percentage is low, have an important role in enamel mineralisation. One of the non-amelogenin proteins is ameloblastin, also known as amelin and sheathlin. Ameloblastin (AMBN) is one of the enamel sheath proteins which is though to have a role in determining the prismatic structure of growing enamel crystals.


Pssm-ID: 214832 [Multi-domain]  Cd Length: 411  Bit Score: 51.04  E-value: 1.44e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432   300 GPTKPSPQQPDSAKTTSQAPPPTKPSSQ--QPG--PAKQPLQQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGP 375
Cdd:smart00817   80 RPREHETQQYEYSLPVHPPPLPSQPSLQpqQPGlkPFLQPTALPTNQATPQKNGPQPPMHLGQPPLQQAELPMIPPQVAP 159
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 2051959432   376 AKQPPQPGSgkPPLQQTGPVKQVPPQAGPTKPpsqtAGPTKPPAQQP 422
Cdd:smart00817  160 SDKPPQTEL--PLYDFADPQNPLLFQIAHLMS----RGPMPQNKQQH 200
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
1023-1354 1.09e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 48.47  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1023 TSTPPTLAAAKPKEEPGIQKEAPKLQQGRLEKTLSADKIQQG---VQREDAKPKQGKLVKTPSADKIQRASQKEDPRIQQ 1099
Cdd:NF033838   168 TNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAkakVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKE 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1100 TRLTKTASYDR----------VLHEVQKEDEKLQEAKLAKTSSADKILHG-VQKEDIKLQETKlAKIPSADKILQGIQKE 1168
Cdd:NF033838   248 AVEKNVATSEQdkpkrrakrgVLGEPATPDKKENDAKSSDSSVGEETLPSpSLKPEKKVAEAE-KKVEEAKKKAKDQKEE 326
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1169 DPKLQQMKMAKALSADKIQPAVQKEDAQLQEVKlpKAASVDKIQHGIQKEDIKLQHEKIKKTRsVDKIQEEDQKEETKLQ 1248
Cdd:NF033838   327 DRRNYPTNTYKTLELEIAESDVKVKEAELELVK--EEAKEPRNEEKIKQAKAKVESKKAEATR-LEKIKTDRKKAEEEAK 403
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1249 RgklsKTPSANKIpATTTADQKKPLNTVEedketvpPEKSTPHPEDKKEEITAEIKDhvaKQKAEVEapykglQAKEQEd 1328
Cdd:NF033838   404 R----KAAEEDKV-KEKPAEQPQPAPAPQ-------PEKPAPKPEKPAEQPKAEKPA---DQQAEED------YARRSE- 461
                          330       340
                   ....*....|....*....|....*.
gi 2051959432 1329 vkkEDLTTGISQEVLKTEKAQEEEIP 1354
Cdd:NF033838   462 ---EEYNRLTQQQPPKTEKPAQPSTP 484
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
155-631 1.45e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 47.84  E-value: 1.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  155 ANPLSAVTSVVNKF--NPFDLISDSDTTHEDAGRKQKVTPKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGQQRPTLQQTE 232
Cdd:NF033839   130 MESQSKVDEAVSKFekDSSSSSSSGSSTKPETPQPENPEHQKPTTPAPDTKPSPQPEGKKPSVPDINQEKEKAKLAVATY 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  233 SSKPVPQQQQQPgepkqVQKPGHRQPADAKQEQVKQPPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSA 312
Cdd:NF033839   210 MSKILDDIQKHH-----LQKEKHRQIVALIKELDELKKQALSEIDNVNTKVEIENTVHKIFADMDAVVTKFKKGLTQDTP 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  313 KttsqapPPTKPSSQQPGPAKQPLQQParqggPVKPSSQQAGPPKQlSQQPGPEKPSAQQTgpakqpPQPGSGKPplqqt 392
Cdd:NF033839   285 K------EPGNKKPSAPKPGMQPSPQP-----EKKEVKPEPETPKP-EVKPQLEKPKPEVK------PQPEKPKP----- 341
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  393 gpvkQVPPQAGPTKPPSQTAGPTKPPAQQPGPTKPSGQ-QPGPEKPLEQKQAGASQPTESVSKKtfcplctttelllhtP 471
Cdd:NF033839   342 ----EVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEvKPQPETPKPEVKPQPEKPKPEVKPQ---------------P 402
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  472 EKANYNTCTQCHTvvcslcgfnPNPHITeisewlclncqmqralggdlaaghgPGPQPPAPKQKTPipPSTAKPSPQPQP 551
Cdd:NF033839   403 EKPKPEVKPQPEK---------PKPEVK-------------------------PQPEKPKPEVKPQ--PEKPKPEVKPQP 446
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  552 vqkkditSKPDPSQLADPKKPPPQKKQTPLPGSPPVKSKQPRAEPTEISQQTRDATPKSdqvkpTQAEDKQKQPSVQKPT 631
Cdd:NF033839   447 -------EKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPST-----PNNLSKDKQPSNQAST 514
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
527-798 3.29e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 46.69  E-value: 3.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  527 PQPPAPKQKTPIPPS-TAKPSPQPQPVQ--KKDITSKPDPSQLADPKKPPPQKKQTPLPGSPPVKSKQPRAEPTEISQQT 603
Cdd:NF033839   162 PQPENPEHQKPTTPApDTKPSPQPEGKKpsVPDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIVALIKELDELK 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  604 RDATPKSDQVKPtqaeDKQKQPSVQKPTADTVSTSAALEQKQDLAGPRPPtqqkvtDSPKPELAKPSQDTHPAEDKPDSK 683
Cdd:NF033839   242 KQALSEIDNVNT----KVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEP------GNKKPSAPKPGMQPSPQPEKKEVK 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  684 PVPQvsrqksdpklasqpgarpdakaqkpveptqtKDDPKKLPTKPAPKPDTKAAPKGPQAGAGPKPGPAQPAPQPQPPQ 763
Cdd:NF033839   312 PEPE-------------------------------TPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEK 360
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2051959432  764 KTPEQSRRfslnLGGITDAPKPQPTTPQETVTGKL 798
Cdd:NF033839   361 PKPEVKPQ----PEKPKPEVKPQPETPKPEVKPQP 391
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1086-1625 5.24e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 46.61  E-value: 5.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1086 IQRASQKEDPRIQQTRLTKTASYDRVLHEVQKEDEKLQEAKLAKTSSadKILHGVQKEDIKL---------------QET 1150
Cdd:COG5022    848 IQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSI--SSLKLVNLELESEiielkkslssdlienLEF 925
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1151 KLAKIPSADKILQGIQ-KEDPKLQQMKMAKALSadkiqpaVQKEDAQLQEVKLPKAASVDKiqHGIQKEDIKLQHEKIKK 1229
Cdd:COG5022    926 KTELIARLKKLLNNIDlEEGPSIEYVKLPELNK-------LHEVESKLKETSEEYEDLLKK--STILVREGNKANSELKN 996
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1230 TRsvdKIQEEDQKEETKLQRgKLSKTPSANKIPATTTADQKKplntveedKETVPPEKSTPHPEDKkeeitaeIKDHVAK 1309
Cdd:COG5022    997 FK---KELAELSKQYGALQE-STKQLKELPVEVAELQSASKI--------ISSESTELSILKPLQK-------LKGLLLL 1057
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1310 QKAEVEAPYKGLQ-AKEQEDV-KKEDLTTGISQEVLKTEKAQEEEIPVQTAPLPrtdhvEAVREKIEKEDDKSDTSSSqq 1387
Cdd:COG5022   1058 ENNQLQARYKALKlRRENSLLdDKQLYQLESTENLLKTINVKDLEVTNRNLVKP-----ANVLQFIVAQMIKLNLLQE-- 1130
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1388 qkspqglsdtgySSDGISSSLGEIPSHIPTDEKDLLKESNKKDTISQESPPSPSDLAKLestvlsileaqantlsDEKSA 1467
Cdd:COG5022   1131 ------------ISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAAL----------------SEKRL 1182
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1468 KSKELSETYGEQTKDQLKTKPLPVTPESYSSDEEDLKAIKEGEGtIVEEGKGTASSQaDYKEDHEGEDIPARRQQR--YD 1545
Cdd:COG5022   1183 YQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKL-ISEGWVPTEYST-SLKGFNNLNKKFDTPASMsnEK 1260
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1546 SVEDSSESENSpVPRRKRRTSVGSSSSDEYKRDDSQGSGDEEdFIRKQIIEMSADEDAS--GSEDDEFIRNQlkEISAAE 1623
Cdd:COG5022   1261 LLSLLNSIDNL-LSSYKLEEEVLPATINSLLQYINVGLFNAL-RTKASSLRWKSATEVNynSEELDDWCREF--EISDVD 1336

                   ..
gi 2051959432 1624 SQ 1625
Cdd:COG5022   1337 EE 1338
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
174-391 8.33e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 45.77  E-value: 8.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  174 ISDSDTTHEDAGRKQKVTPK---EQGKPEEQRSPAKHPTQPQSPKPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPKQV 250
Cdd:NF033838   243 AKLKEAVEKNVATSEQDKPKrraKRGVLGEPATPDKKENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAKD 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  251 QKPGHRQ--PA------------------DAKQEQVKQ-PPQPRGPQK-SQPQPSEPAKPVQQ------QTSAKLSSGPT 302
Cdd:NF033838   323 QKEEDRRnyPTntyktleleiaesdvkvkEAELELVKEeAKEPRNEEKiKQAKAKVESKKAEAtrlekiKTDRKKAEEEA 402
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  303 KPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPlQQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQP 382
Cdd:NF033838   403 KRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKP-EKPAEQPKAEKPADQQAEEDYARRSEEEYNRLTQQQPPKTEKPAQP 481

                   ....*....
gi 2051959432  383 GSGKPPLQQ 391
Cdd:NF033838   482 STPKTGWKQ 490
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1041-1631 1.51e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.96  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1041 QKEAPKLQQGRLEKTLSADKIQQGVQREDAKPKQGKLVKtpSADKIQR--ASQKEDPRIQQTRLTKTASYDRVLHEVQKE 1118
Cdd:pfam02463  224 EYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEK--EEEKLAQvlKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1119 DEKLQEAKlaktSSADKILHGVQKEDIKLQETKLAKIPSADKILQGIQKEDPKLQQMKMAKALSADKIQPAVQKEDAQLQ 1198
Cdd:pfam02463  302 LLKLERRK----VDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLA 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1199 EVKLPKAASV-DKIQHGIQKEdikLQHEKIKKTRSVDKI--QEEDQKEETKLQ----RGKLSKTPSANKIPATTTADQKK 1271
Cdd:pfam02463  378 KKKLESERLSsAAKLKEEELE---LKSEEEKEAQLLLELarQLEDLLKEEKKEeleiLEEEEESIELKQGKLTEEKEELE 454
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1272 PLNTVEEDKETVPPEKSTPHPEDK--KEEITAEIKDHVAKQKAEVEAPYKGLQAKEQEDVKKEDLTTGISQEVLKTEKAQ 1349
Cdd:pfam02463  455 KQELKLLKDELELKKSEDLLKETQlvKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDL 534
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1350 EEEIPVQTAPLPRTDHVEAVREKIEKEDDKSDTSSSQQQKSPQGLSDTGYSSDGISSSLGEIPSHIPTD-EKDLLKESNK 1428
Cdd:pfam02463  535 GVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILnLAQLDKATLE 614
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1429 KDTISQESPPSPSDLAKLESTVLSILEAQANTLSDEKSAKSKELSETYGEQTKDQLKTKPLPVTPESYSSDEEDLKAIKE 1508
Cdd:pfam02463  615 ADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEI 694
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1509 G---EGTIVEEGKGTASSQADYKEDHEGEDIPARRQQRydsvedsseseNSPVPRRKRRTSVGSSSSDEYKRDDSQGSGD 1585
Cdd:pfam02463  695 LrrqLEIKKKEQREKEELKKLKLEAEELLADRVQEAQD-----------KINEELKLLKQKIDEEEEEEEKSRLKKEEKE 763
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2051959432 1586 EEDFIRKQIIEMSADEDAS------GSEDDEFIRNQLKEISAAESQKKEEVK 1631
Cdd:pfam02463  764 EEKSELSLKEKELAEEREKteklkvEEEKEEKLKAQEEELRALEEELKEEAE 815
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
173-461 2.17e-03

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 44.15  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  173 LISDSDTTHedagrkQKVTPKEQGKPEEQRSpaKHPTQPQSPKPAVQQQgqqrPTLQQTESSkpVPQQQQQPGEPKQVQK 252
Cdd:cd22540    212 LVGTQDGAT------QLQLAAAPSKPSKKIR--KKSAQAAQPAVTVAEQ----VETVLIETT--ADNIIQAGNNLLIVQS 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  253 PGHRQPADAKQEQVKqppQPRGPQKSQPQPSEPAKPVQQQtSAKLSSGPTKP--SPQQPDSAKTTSQAPPPTkPSSQQPG 330
Cdd:cd22540    278 PGTGQPAVLQQVQVL---QPKQEQQVVQIPQQALRVVQAA-SATLPTVPQKPlqNIQIQNSEPTPTQVYIKT-PSGEVQT 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  331 PAKQPLQQPARQGGPVKPSSQQAGPPkqLSQQPGPEKPSAQQTGPAKQPPQPGSG-----KPPLQQTGPVKQVPPQAGpT 405
Cdd:cd22540    353 VLLQEAPAATATPSSSTSTVQQQVTA--NNGTGTSKPNYNVRKERTLPKIAPAGGiislnAAQLAAAAQAIQTINING-V 429
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051959432  406 KPPSQTAGPTKPPAQQPGPTKP--------SGQQPGP-EKPLEQKQAGASQPTESVSK-KTFCPLC 461
Cdd:cd22540    430 QVQGVPVTITNAGGQQQLTVQTvssnnltiSGLSPTQiQLQMEQALEIETQPGEKRRRmACTCPNC 495
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
3786-3849 4.12e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 42.94  E-value: 4.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051959432 3786 ARAKILQDIDRELDLVERESAKLRKKQAELDEEEKEIDaklrylEMGINRRKEALLKEREKRER 3849
Cdd:pfam07946  265 TREEEIEKIKKAAEEERAEEAQEKKEEAKKKEREEKLA------KLSPEEQRKYEEKERKKEQR 322
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
263-421 4.47e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 43.26  E-value: 4.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  263 QEQVKQPPQPRGPQKSQPQPSEPAKPVQQQtsaklssGPTKPSPQQPDSAKTTSQAPPPTKPSSQqpgPAKQPLQQPARQ 342
Cdd:TIGR01628  374 QFMQLQPRMRQLPMGSPMGGAMGQPPYYGQ-------GPQQQFNGQPLGWPRMSMMPTPMGPGGP---LRPNGLAPMNAV 443
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051959432  343 GGPvkPSSQQAGPPKqLSQQPGPEKPSAQQtgpakqppqpgsgkPPLQQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQ 421
Cdd:TIGR01628  444 RAP--SRNAQNAAQK-PPMQPVMYPPNYQS--------------LPLSQDLPQPQSTASQGGQNKKLAQVLASATPQMQ 505
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
251-696 5.74e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 5.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  251 QKPGHRQPADAKQEqVKQPPQPRGPQKSQP---QPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQ 327
Cdd:NF033839   165 ENPEHQKPTTPAPD-TKPSPQPEGKKPSVPdinQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIVALIKELDELKKQ 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  328 QPGPAKQPLQQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTgpaKQPPQPGSGKPPLQQTgPVKQVPPQAGPTKP 407
Cdd:NF033839   244 ALSEIDNVNTKVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGN---KKPSAPKPGMQPSPQP-EKKEVKPEPETPKP 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  408 PSQTAGPTKPPAQQPGPTKPSGQ-QPGPEKPLEQKQAGASQPTESVSKKtfcplctttelllhtPEKanyntctqchtvv 486
Cdd:NF033839   320 EVKPQLEKPKPEVKPQPEKPKPEvKPQLETPKPEVKPQPEKPKPEVKPQ---------------PEK------------- 371
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  487 cslcgfnPNPHITeisewlclncqmqralggdlaaghgpgPQPPAPKQKTPIPPSTAKPSPQPQPvqkkditSKPDPSQL 566
Cdd:NF033839   372 -------PKPEVK---------------------------PQPETPKPEVKPQPEKPKPEVKPQP-------EKPKPEVK 410
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  567 ADPKKPPPQKKQTPLPGSPPVKSKQPRAEPtEISQQTRDATPksdQVKPtqaedkqkQPSVQKPTADTVSTSAALEQKQD 646
Cdd:NF033839   411 PQPEKPKPEVKPQPEKPKPEVKPQPEKPKP-EVKPQPEKPKP---EVKP--------QPETPKPEVKPQPEKPKPEVKPQ 478
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 2051959432  647 LAGPRPPTQQkvtdsPKPELAKPSQDTHPAEDKPDSKPVPQVSRQKSDPK 696
Cdd:NF033839   479 PEKPKPDNSK-----PQADDKKPSTPNNLSKDKQPSNQASTNEKATNKPK 523
 
Name Accession Description Interval E-value
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
4528-4621 3.89e-48

PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RIM, RIM2, piccolo and related domains. RIM proteins and Gallus gallus protein piccolo (also called aczonin) are involved in neurotransmitter release at presynaptic active zones, the site of vesicle fusion. A protein complex containing RIM proteins positions synaptic vesicles containing synaptotagmin at the active zone. RIM proteins simultaneously activate docking and priming of synaptic vesicles and recruit Ca2+-channels to active zones, thereby connecting primed synaptic vesicles to Ca2+-channels. RIM binding to vesicular Rab proteins (Rab3 and Rab27 isoforms) mediates vesicle docking; RIM binding to Munc13 activates vesicle priming; RIM binding to the Ca2+-channel, both directly and indirectly via RIM-BP, recruits the Ca2+-channels. The RIM PDZ domain interacts with the C-termini of N- and P/Q-type voltage-gated Ca2+-channels. RIM1, RIM2 and piccolo also participate in regulated exocytosis through binding cAMP-GEFII (cAMP-binding protein-guanidine nucleotide exchange factor II). The piccolo PDZ domain binds cAMP-GEFII. RIM2 also plays a role in dendrite formation by melanocytes. Caenorhabditis elegans RIM (also known as unc-10) may be involved in the regulation of defecation and daumone response. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467198 [Multi-domain]  Cd Length: 95  Bit Score: 167.73  E-value: 3.89e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 4528 FPHTRLKLLRDPKDHTVSGNGLGIRVVGGKEIPgsSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEV 4607
Cdd:cd06714      2 FLIGRIILQRDPKDGSVSGNGLGLKVVGGKMTE--SGRLGAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEV 79
                           90
                   ....*....|....
gi 2051959432 4608 QSIIIQQSGEAEIC 4621
Cdd:cd06714     80 QDIISQSKGEVELV 93
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
456-517 1.47e-42

FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the first FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277313 [Multi-domain]  Cd Length: 62  Bit Score: 150.57  E-value: 1.47e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432  456 TFCPLCTTTELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRALGG 517
Cdd:cd15774      1 TICPLCKTTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
922-985 3.86e-42

FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the second FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277315 [Multi-domain]  Cd Length: 64  Bit Score: 149.45  E-value: 3.86e-42
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051959432  922 MSCPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSGQLG 985
Cdd:cd15776      1 LLCPLCKTELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQLG 64
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
923-980 5.45e-37

Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. There are eight conserved cysteines, suggesting that it coordinates two zinc ligands.


Pssm-ID: 461722 [Multi-domain]  Cd Length: 60  Bit Score: 134.85  E-value: 5.45e-37
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2051959432  923 SCPLCK-TGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAM 980
Cdd:pfam05715    2 LCPLCKtTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
456-515 7.80e-37

Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. There are eight conserved cysteines, suggesting that it coordinates two zinc ligands.


Pssm-ID: 461722 [Multi-domain]  Cd Length: 60  Bit Score: 134.47  E-value: 7.80e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  456 TFCPLCTTTELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRAL 515
Cdd:pfam05715    1 TLCPLCKTTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
FYVE2_BSN_PCLO cd15772
FYVE-related domain 2 found in protein bassoon and piccolo; This family includes protein ...
923-985 1.45e-36

FYVE-related domain 2 found in protein bassoon and piccolo; This family includes protein bassoon and piccolo. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Both bassoon and piccolo contain two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. Their FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. This model corresponds to the second FYVE-related domain.


Pssm-ID: 277311 [Multi-domain]  Cd Length: 64  Bit Score: 133.62  E-value: 1.45e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051959432  923 SCPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSGQLG 985
Cdd:cd15772      2 TCPLCKTELNVGSKEPPNYNTCTQCHTQVCNLCGFNPTPHLVEKKEWLCLNCQTQRLMSGGLG 64
FYVE1_BSN_PCLO cd15771
FYVE-related domain 1 found in protein bassoon and piccolo; This family includes protein ...
456-517 6.61e-35

FYVE-related domain 1 found in protein bassoon and piccolo; This family includes protein bassoon and piccolo. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Both bassoon and piccolo contain two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. Their FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. This model corresponds to the first FYVE-related domain.


Pssm-ID: 277310 [Multi-domain]  Cd Length: 61  Bit Score: 128.97  E-value: 6.61e-35
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432  456 TFCPLCTTTELLLHTPeKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRALGG 517
Cdd:cd15771      1 TLCPLCNTTELTLHVP-KPNFNTCTQCHTTVCNQCGFNPNPHLTEVKEWLCLNCQMQRALGM 61
FYVE2_BSN cd15775
FYVE-related domain 2 found in protein bassoon; Protein bassoon, also termed zinc finger ...
921-985 3.68e-33

FYVE-related domain 2 found in protein bassoon; Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Bassoon contains two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. This family corresponds to the second FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277314 [Multi-domain]  Cd Length: 65  Bit Score: 123.87  E-value: 3.68e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051959432  921 EMSCPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSGQLG 985
Cdd:cd15775      1 RVTCPLCKTELNVGSTEPPNYNTCTSCRTQVCNLCGFNPTPHLVEKNEWLCLNCQTQRLLEGSLG 65
FYVE1_BSN cd15773
FYVE-related domain 1 found in protein bassoon; Protein bassoon, also termed zinc finger ...
456-516 9.76e-31

FYVE-related domain 1 found in protein bassoon; Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Bassoon contains two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. This family corresponds to the first FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277312 [Multi-domain]  Cd Length: 64  Bit Score: 117.11  E-value: 9.76e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051959432  456 TFCPLCTTTELLlHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRALG 516
Cdd:cd15773      4 TLCPICNTTELT-SFPSQPNFNTCTQCHNKVCNQCGFNPNPHLTEVKEWLCLNCQMQRALG 63
FYVE_BSN_PCLO cd15751
FYVE-related domain found in protein bassoon and piccolo; This family includes protein bassoon ...
924-980 7.38e-27

FYVE-related domain found in protein bassoon and piccolo; This family includes protein bassoon and piccolo. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Both bassoon and piccolo contain two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. Their FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277290 [Multi-domain]  Cd Length: 62  Bit Score: 106.00  E-value: 7.38e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2051959432  924 CPLCK-TGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAM 980
Cdd:cd15751      3 CPLCGtSELPLGSKSPPNYNTCTDCKNRVCNQCGFNSTPPVTKVKEWLCLNCQKKRAL 60
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
924-982 4.94e-26

FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the first FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277313 [Multi-domain]  Cd Length: 62  Bit Score: 103.57  E-value: 4.94e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  924 CPLCK-TGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSG 982
Cdd:cd15774      3 CPLCKtTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
FYVE2_BSN_PCLO cd15772
FYVE-related domain 2 found in protein bassoon and piccolo; This family includes protein ...
458-519 9.10e-26

FYVE-related domain 2 found in protein bassoon and piccolo; This family includes protein bassoon and piccolo. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Both bassoon and piccolo contain two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. Their FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. This model corresponds to the second FYVE-related domain.


Pssm-ID: 277311 [Multi-domain]  Cd Length: 64  Bit Score: 102.80  E-value: 9.10e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432  458 CPLCTTtELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRALGGDL 519
Cdd:cd15772      3 CPLCKT-ELNVGSKEPPNYNTCTQCHTQVCNLCGFNPTPHLVEKKEWLCLNCQTQRLMSGGL 63
FYVE2_BSN cd15775
FYVE-related domain 2 found in protein bassoon; Protein bassoon, also termed zinc finger ...
455-520 1.42e-25

FYVE-related domain 2 found in protein bassoon; Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Bassoon contains two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. This family corresponds to the second FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277314 [Multi-domain]  Cd Length: 65  Bit Score: 102.30  E-value: 1.42e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051959432  455 KTFCPLCTTtELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRALGGDLA 520
Cdd:cd15775      1 RVTCPLCKT-ELNVGSTEPPNYNTCTSCRTQVCNLCGFNPTPHLVEKNEWLCLNCQTQRLLEGSLG 65
FYVE1_BSN_PCLO cd15771
FYVE-related domain 1 found in protein bassoon and piccolo; This family includes protein ...
924-982 2.05e-25

FYVE-related domain 1 found in protein bassoon and piccolo; This family includes protein bassoon and piccolo. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Both bassoon and piccolo contain two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. Their FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. This model corresponds to the first FYVE-related domain.


Pssm-ID: 277310 [Multi-domain]  Cd Length: 61  Bit Score: 101.62  E-value: 2.05e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2051959432  924 CPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAMSG 982
Cdd:cd15771      3 CPLCNTTELTLHVPKPNFNTCTQCHTTVCNQCGFNPNPHLTEVKEWLCLNCQMQRALGM 61
FYVE1_BSN cd15773
FYVE-related domain 1 found in protein bassoon; Protein bassoon, also termed zinc finger ...
924-980 2.47e-24

FYVE-related domain 1 found in protein bassoon; Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Bassoon contains two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. This family corresponds to the first FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277312 [Multi-domain]  Cd Length: 64  Bit Score: 99.00  E-value: 2.47e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2051959432  924 CPLCKTGLNIGSKDPPNFNTCTECKKVVCNLCGFNPMPHIAEVQEWLCLNCQTQRAM 980
Cdd:cd15773      6 CPICNTTELTSFPSQPNFNTCTQCHNKVCNQCGFNPNPHLTEVKEWLCLNCQMQRAL 62
FYVE_BSN_PCLO cd15751
FYVE-related domain found in protein bassoon and piccolo; This family includes protein bassoon ...
458-516 6.19e-24

FYVE-related domain found in protein bassoon and piccolo; This family includes protein bassoon and piccolo. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Both bassoon and piccolo contain two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. Their FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277290 [Multi-domain]  Cd Length: 62  Bit Score: 97.52  E-value: 6.19e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2051959432  458 CPLCTTTELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRALG 516
Cdd:cd15751      3 CPLCGTSELPLGSKSPPNYNTCTDCKNRVCNQCGFNSTPPVTKVKEWLCLNCQKKRALG 61
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
458-519 1.21e-23

FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Piccolo is a multi-domain protein containing two N-terminal FYVE zinc fingers, a polyproline tract, and a PDZ domain and two C-terminal C2 domains. This family corresponds to the second FYVE domain, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277315 [Multi-domain]  Cd Length: 64  Bit Score: 97.06  E-value: 1.21e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432  458 CPLCTTtELLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRALGGDL 519
Cdd:cd15776      3 CPLCKT-ELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQL 63
PHA03247 PHA03247
large tegument protein UL36; Provisional
250-751 3.38e-20

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 100.40  E-value: 3.38e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  250 VQKPGHRQPADAKQEQVKQPPQPRGPQKSQPQPSE-----------PAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQA 318
Cdd:PHA03247  2582 VTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPlppdthapdppPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRV 2661
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  319 PPPTKPSSQ-QPGPAKQPLQQPARQGGP--VKPSSQQAGPPKQlSQQPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPV 395
Cdd:PHA03247  2662 SRPRRARRLgRAAQASSPPQRPRRRAARptVGSLTSLADPPPP-PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPA 2740
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  396 KQVPPQA-----GPTKP--PSQTAGPTKP-PAQQPGPTKPSGQQPGPEKPLEQKQAGASQPTESVSKKTFCPLCTTTELL 467
Cdd:PHA03247  2741 PPAVPAGpatpgGPARParPPTTAGPPAPaPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP 2820
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  468 LHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEwlclncqmqrALGGDLAagHGPGPQPPAPKQKTPI-PPSTAKPS 546
Cdd:PHA03247  2821 AASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV----------APGGDVR--RRPPSRSPAAKPAAPArPPVRRLAR 2888
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  547 PQPQPvqkkditskpdpsqladpkkpppQKKQTPLPGSPPVKSKQPRAEPTEISQQTRDATPKSDQVKPTQAE-DKQKQP 625
Cdd:PHA03247  2889 PAVSR-----------------------STESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRpQPPLAP 2945
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  626 SVQKPTADTVSTSAALEQKQDLAGPRPPTQQKVTDSPKPELAKPSQDTHPAEDKPDskpvPQVSRQKSDPKLASQPGARP 705
Cdd:PHA03247  2946 TTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSL----SRVSSWASSLALHEETDPPP 3021
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051959432  706 DAKAQKPVEPTQTKD---------DPKK--------LPTKPAPKPDTKAAPKGPQAGAGPKPG 751
Cdd:PHA03247  3022 VSLKQTLWPPDDTEDsdadslfdsDSERsdlealdpLPPEPHDPFAHEPDPATPEAGARESPS 3084
PHA03247 PHA03247
large tegument protein UL36; Provisional
253-793 6.40e-19

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 96.16  E-value: 6.40e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  253 PGHRQPADAKQEQVKQPPQPRG----------PQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPT 322
Cdd:PHA03247  2512 PSRLAPAILPDEPVGEPVHPRMltwirgleelASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDA 2591
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  323 KPSSQQPGPAKQPLQQPARQGGPVK-PSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPPlQQTGPVKQVPPQ 401
Cdd:PHA03247  2592 PPQSARPRAPVDDRGDPRGPAPPSPlPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP-GRVSRPRRARRL 2670
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  402 AGPTKPPSQTAGPTKPPAQQP-GPTKPSGQQPGPEKPLEqkqagaSQPTESVSkktfcplctttelllhtpekanyntCT 480
Cdd:PHA03247  2671 GRAAQASSPPQRPRRRAARPTvGSLTSLADPPPPPPTPE------PAPHALVS-------------------------AT 2719
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  481 QCHTVVCSLCGFNPNPHITEISEwlclncqmqralggdlAAGHGP----GPQPPAPKQKTPIPPSTAKPSPQPQPVQKKd 556
Cdd:PHA03247  2720 PLPPGPAAARQASPALPAAPAPP----------------AVPAGPatpgGPARPARPPTTAGPPAPAPPAAPAAGPPRR- 2782
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  557 iTSKPDPSQLAdpkkpppqkKQTPLPGSPPVKSKQPRAEPTEISQQTRDATPKSDQVKPTQAedkqkQPSVQKPTADTVS 636
Cdd:PHA03247  2783 -LTRPAVASLS---------ESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSA-----QPTAPPPPPGPPP 2847
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  637 TSAALEQKQDLAGP---RPPTQQKVtdspkpelAKPSQDTHPAEDKPDSKPVPQVSRQKSDPKLASQPGARPDAKAQKPV 713
Cdd:PHA03247  2848 PSLPLGGSVAPGGDvrrRPPSRSPA--------AKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQP 2919
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  714 EPTQTKDDPKKLPTKPAPKPDTKAAPK-GPQAGAGPKPGPAQPAPQPQPPQKTPEQSRRFSLNLGGItdaPKPQPTTPQE 792
Cdd:PHA03247  2920 QPQPPPPPQPQPPPPPPPRPQPPLAPTtDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSR---EAPASSTPPL 2996

                   .
gi 2051959432  793 T 793
Cdd:PHA03247  2997 T 2997
PHA03247 PHA03247
large tegument protein UL36; Provisional
267-774 6.20e-18

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 92.69  E-value: 6.20e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  267 KQPPQPRGPQKSQPQPsepakpvqqqtsaklssGPTKPSPQQPDSAKTTSQaPPPTKPSSQQPGPAKQP--------LQQ 338
Cdd:PHA03247  2481 RRPAEARFPFAAGAAP-----------------DPGGGGPPDPDAPPAPSR-LAPAILPDEPVGEPVHPrmltwirgLEE 2542
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  339 PARQ--GGPVKPSSQQAGPPKQLSQQPgPEKPSAQQTGPAKQ--------PPQPGSGKPPLQQTGPVKQVPPQAGPtkPP 408
Cdd:PHA03247  2543 LASDdaGDPPPPLPPAAPPAAPDRSVP-PPRPAPRPSEPAVTsrarrpdaPPQSARPRAPVDDRGDPRGPAPPSPL--PP 2619
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  409 SQTAGPTKPPAQQPGPTKPSGQQPGPEKPLEQKQAGASQPTESVSKKTFCPLCTTTELllHTPEKANYNTCTQCHTVVCS 488
Cdd:PHA03247  2620 DTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAS--SPPQRPRRRAARPTVGSLTS 2697
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  489 LC-----GFNPNPHITEISEWLCLNCQMQRALGGDLAAGHGPGPQPPAPKQKTPI----PPSTAKPSPQPQPVQKKDITS 559
Cdd:PHA03247  2698 LAdppppPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparPARPPTTAGPPAPAPPAAPAA 2777
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  560 KPDPSqlADPKKPPPQKKQTPLPGSPPVKSKQPRAEPTEISQQTRDATPKSDQVKPTQAedkqkQPSVQKPTADTVSTSA 639
Cdd:PHA03247  2778 GPPRR--LTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSA-----QPTAPPPPPGPPPPSL 2850
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  640 ALEQKQDLAGP---RPPTQQ---KVTDSPKPELAKPSQDTHPAEDKPDSKPVPQVSRQKSdPKLASQPGARPDAKAQ--- 710
Cdd:PHA03247  2851 PLGGSVAPGGDvrrRPPSRSpaaKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQ-PQAPPPPQPQPQPPPPpqp 2929
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432  711 KPVEPTQTKDDPKKLP-TKPAPKPDTKAAPKGPQAGA-------GPKPGPAQPAPQPQPPQKTPEQSRRFSL 774
Cdd:PHA03247  2930 QPPPPPPPRPQPPLAPtTDPAGAGEPSGAVPQPWLGAlvpgrvaVPRFRVPQPAPSREAPASSTPPLTGHSL 3001
PHA03247 PHA03247
large tegument protein UL36; Provisional
198-452 7.53e-17

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 89.23  E-value: 7.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  198 PEEQRSPAKHPTQPQSPKPAVQQQGQQR-PTLQQTESSKPVPQQQQQPGEPKQVQKP----GHRQPADAKQEQVKQPPQP 272
Cdd:PHA03247  2704 PPPTPEPAPHALVSATPLPPGPAAARQAsPALPAAPAPPAVPAGPATPGGPARPARPpttaGPPAPAPPAAPAAGPPRRL 2783
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  273 RGPQKSQPQPSEPAKPVQQQTSAKLSSGPTkPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARQGGPVKPSS-- 350
Cdd:PHA03247  2784 TRPAVASLSESRESLPSPWDPADPPAAVLA-PAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGdv 2862
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  351 QQAGPPkqlsqQPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGPTKPSGQ 430
Cdd:PHA03247  2863 RRRPPS-----RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP 2937
                          250       260
                   ....*....|....*....|..
gi 2051959432  431 QPGPEKPLEQKQAGASQPTESV 452
Cdd:PHA03247  2938 RPQPPLAPTTDPAGAGEPSGAV 2959
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
330-722 5.64e-15

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 82.34  E-value: 5.64e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  330 GPAKQPLQQPARQGGPVkPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPTKPPS 409
Cdd:PRK07764   389 GGAGAPAAAAPSAAAAA-PAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPA 467
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  410 QTAGPTKPPAQQPGPTKPSGQQPGPEkPLEQKQAGASQPT--------------ESVSKKTFcplcTTTELLLHTPEKAN 475
Cdd:PRK07764   468 PAPAAAPEPTAAPAPAPPAAPAPAAA-PAAPAAPAAPAGAddaatlrerwpeilAAVPKRSR----KTWAILLPEATVLG 542
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  476 Y--NTCTQCHTVVCSLCGFNpNPHITE-----ISEWLCLNCQMQRALGGDLAAGHGPGPQPPAPKQKtpiPPSTAKPSPQ 548
Cdd:PRK07764   543 VrgDTLVLGFSTGGLARRFA-SPGNAEvlvtaLAEELGGDWQVEAVVGPAPGAAGGEGPPAPASSGP---PEEAARPAAP 618
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  549 PQPVQKKDitskPDPSQLADPKKPPPQKKQTPLPGSPPVKSKQPRAEPTEISQQ----TRDATPKSDQVKPTQAEDKQKQ 624
Cdd:PRK07764   619 AAPAAPAA----PAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGwpakAGGAAPAAPPPAPAPAAPAAPA 694
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  625 PSVQKPTADTVSTSAALEQKQDLAGPRPPTQQ------KVTDSPKPELAKPSQDTHPAEDKPDSKPVPQVSRQksDPKLA 698
Cdd:PRK07764   695 GAAPAQPAPAPAATPPAGQADDPAAQPPQAAQgasapsPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPA--AAPAA 772
                          410       420
                   ....*....|....*....|....
gi 2051959432  699 SQPGARPDAKAQKPVEPTQTKDDP 722
Cdd:PRK07764   773 APPPSPPSEEEEMAEDDAPSMDDE 796
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
4545-4620 3.24e-14

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467153 [Multi-domain]  Cd Length: 81  Bit Score: 70.65  E-value: 3.24e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051959432 4545 SGNGLGIRVVGGKEIPGssgeiGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSIIIQQSGEAEI 4620
Cdd:cd00136      8 PGGGLGFSIRGGKDGGG-----GIFVSRVEPGGPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELLKSAGGEVTL 78
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
169-597 5.08e-14

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 79.43  E-value: 5.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  169 NPFDLISDSDTTHEDAgrkqkvtpKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPK 248
Cdd:pfam03154  150 SPQDNESDSDSSAQQQ--------ILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQT 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  249 QVQKPGHRQPADAKQEQVKQPPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQ 328
Cdd:pfam03154  222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLT 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  329 PgpakqplqQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPT--K 406
Cdd:pfam03154  302 P--------QSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQshK 373
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  407 PPSQTAGPT---------KPPAQQPGPT----KPSGQQPGPEKPLEQKQAGASQPTESvskktfcPLCTTTEllLHTPEK 473
Cdd:pfam03154  374 HPPHLSGPSpfqmnsnlpPPPALKPLSSlsthHPPSAHPPPLQLMPQSQQLPPPPAQP-------PVLTQSQ--SLPPPA 444
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  474 ANYNTCTQCHTVVcSLCGFNPNPHITEISEWLCLNCQMQRAlggdlAAGHGPGPQPP---APKQKTPIPPSTAKPSPqpq 550
Cdd:pfam03154  445 ASHPPTSGLHQVP-SQSPFPQHPFVPGGPPPITPPSGPPTS-----TSSAMPGIQPPssaSVSSSGPVPAAVSCPLP--- 515
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 2051959432  551 PVQKKDitSKPDPSQladpkkpppqkkqtpLPGSPPVKSKQPRAEPT 597
Cdd:pfam03154  516 PVQIKE--EALDEAE---------------EPESPPPPPRSPSPEPT 545
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
199-447 1.97e-12

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 73.92  E-value: 1.97e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  199 EEQ-RSPAKHPTQPQSPKPAVQQQGQQRptlqqtesskpvpqqqqqPGEPKQVQKPGHRQPADAKQE-----------QV 266
Cdd:pfam09770   97 EEQvRFNRQQPAARAAQSSAQPPASSLP------------------QYQYASQQSQQPSKPVRTGYEkykepepipdlQV 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  267 KQ-----PPQPRGPQKSQPQPSEPAKPVQQQTS---------AKLSSGPTKPSPQQPDSAKTTSQAPPPTK-PSSQQPGP 331
Cdd:pfam09770  159 DAslwgvAPKKAAAPAPAPQPAAQPASLPAPSRkmmsleeveAAMRAQAKKPAQQPAPAPAQPPAAPPAQQaQQQQQFPP 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  332 AKQPLQQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQT 411
Cdd:pfam09770  239 QIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQILQNPNRLSAARVGYPQ 318
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2051959432  412 AGptkPPAQQPGPTKPSGQQPGPEKPLEQKQAGASQ 447
Cdd:pfam09770  319 NP---QPGVQPAPAHQAHRQQGSFGRQAPIITHPQQ 351
PDZ1_GgSTXBP4-like cd06692
PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, ...
4547-4615 2.29e-12

PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, and related domains. Gallus gallus STXBP4 isoform X1 contains 2 PDZ domains (PDZ1 and PDZ2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This STXBP4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467179 [Multi-domain]  Cd Length: 88  Bit Score: 65.71  E-value: 2.29e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051959432 4547 NGLGIRVVGGKEiPGSSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSIIIQQS 4615
Cdd:cd06692      8 KGLGIKIIGGYR-ENTGEEFGIFIKRILPGGLAATDGRLKEGDLILEVNGESLQGVTNERAVSILRSAS 75
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
253-453 3.43e-12

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 73.10  E-value: 3.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  253 PGHRQPADAKQEQVKQPPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPA 332
Cdd:PRK07764   592 PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  333 KQPLQQPARQGGPVKPSSQQAG---PPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPPlQQTGPVKQVPPQAGPTKPPS 409
Cdd:PRK07764   672 KAGGAAPAAPPPAPAPAAPAAPagaAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASA-PSPAADDPVPLPPEPDDPPD 750
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2051959432  410 QTAGPTKPPAQQPGPTKPSGQQPGPEKPLEQKQAGASQPTESVS 453
Cdd:PRK07764   751 PAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMD 794
PRK10263 PRK10263
DNA translocase FtsK; Provisional
208-790 7.61e-12

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 72.43  E-value: 7.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  208 PTQPQSPKPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPKQVQKPGHRQPADAKQEQVKQPPQPRGPQKSQPQPSEPAK 287
Cdd:PRK10263   339 PVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQ 418
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  288 PVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPssQQPGPAKQPlQQPARQggPVKPSSQQAGPPKQLSQQPGPEK 367
Cdd:PRK10263   419 PYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQST--FAPQSTYQT-EQTYQQ--PAAQEPLYQQPQPVEQQPVVEPE 493
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  368 PSAQQTGPAkqppqpgsgKPPLQQTGPVKQvpPQAGPTKPPSQTAGPTKPPAQQPGPTKPSGQQPGPEKPLEQKQAGASQ 447
Cdd:PRK10263   494 PVVEETKPA---------RPPLYYFEEVEE--KRAREREQLAAWYQPIPEPVKEPEPIKSSLKAPSVAAVPPVEAAAAVS 562
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  448 PTESVSKKTfcPLCTTTELLLHTPekanyntctqchtVVCSLCGFNPNPHITEisewlclncqmqralggdlaaghGPGP 527
Cdd:PRK10263   563 PLASGVKKA--TLATGAAATVAAP-------------VFSLANSGGPRPQVKE-----------------------GIGP 604
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  528 QPPAPKqKTPIPpstakpspqpqpvQKKDITSK--PDPSQLADPKKPPPQKKQTPLPGSppvkskQPRAEPTEISQQTRD 605
Cdd:PRK10263   605 QLPRPK-RIRVP-------------TRRELASYgiKLPSQRAAEEKAREAQRNQYDSGD------QYNDDEIDAMQQDEL 664
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  606 ATPKSDQVKPTQAEDKQKQPSVQKPTADTVSTSA-----ALEQKQDLAGPRP--------------PTQQKVTDSPKPEL 666
Cdd:PRK10263   665 ARQFAQTQQQRYGEQYQHDVPVNAEDADAAAEAElarqfAQTQQQRYSGEQPaganpfslddfefsPMKALLDDGPHEPL 744
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  667 AKPSqdTHPaEDKPDSKPVPQVSRQKSDPKLASQpgaRPDAKAQKPVEPTQTKDDPKKlPTKPAP---KPDTKAAPK--- 740
Cdd:PRK10263   745 FTPI--VEP-VQQPQQPVAPQQQYQQPQQPVAPQ---PQYQQPQQPVAPQPQYQQPQQ-PVAPQPqyqQPQQPVAPQpqy 817
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2051959432  741 -GPQAGAGPKPgpaQPAPQPQPPQKTPEQSRRFSLNLGGITDAPKPQPTTP 790
Cdd:PRK10263   818 qQPQQPVAPQP---QYQQPQQPVAPQPQDTLLHPLLMRNGDSRPLHKPTTP 865
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
256-448 1.24e-11

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 71.61  E-value: 1.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  256 RQPADAKQEQVKQPPQPRGPQKSQP--QPSEPAKPVQqqTSAKLSSGPTKPSPQQPDSA------KTTSQAPPPTKPSSQ 327
Cdd:pfam09770  105 QQPAARAAQSSAQPPASSLPQYQYAsqQSQQPSKPVR--TGYEKYKEPEPIPDLQVDASlwgvapKKAAAPAPAPQPAAQ 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  328 QPGP--------------------AKQPLQQPAR--QGGPVKPSSQQAGPPKQLSQQPGPekPSAQQTGPAKQPPQPGSG 385
Cdd:pfam09770  183 PASLpapsrkmmsleeveaamraqAKKPAQQPAPapAQPPAAPPAQQAQQQQQFPPQIQQ--QQQPQQQPQQPQQHPGQG 260
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  386 KPPLQQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGPTK-------------------PSGQQPGPEKPLEQKQAGAS 446
Cdd:pfam09770  261 HPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQilqnpnrlsaarvgypqnpQPGVQPAPAHQAHRQQGSFG 340

                   ..
gi 2051959432  447 QP 448
Cdd:pfam09770  341 RQ 342
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
195-448 2.44e-11

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 70.36  E-value: 2.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  195 QGKPEEQRSPAKHPTQPQspKPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPKQVQKPGHRQPADAKQEQvkQPPQPRG 274
Cdd:pfam03157  271 QWQQSGQGQQGYYPTSLQ--QPGQGQSGYYPTSQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQPGQGQQGQ--QPAQGQQ 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  275 PQKSQPQpsepAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPAR-QGGPVKPSSQQA 353
Cdd:pfam03157  347 PGQGQPG----YYPTSPQQPGQGQPGYYPTSQQQPQQGQQPEQGQQGQQQGQGQQGQQPGQGQQPGQgQPGYYPTSPQQS 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  354 GppkqlSQQPGPEKPSAQQTGpakQPPQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGPTKPSGQQPG 433
Cdd:pfam03157  423 G-----QGQPGYYPTSPQQSG---QGQQPGQGQQPGQEQPGQGQQPGQGQQGQQPGQPEQGQQPGQGQPGYYPTSPQQSG 494
                          250
                   ....*....|....*.
gi 2051959432  434 P-EKPLEQKQAGASQP 448
Cdd:pfam03157  495 QgQQLGQWQQQGQGQP 510
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
163-653 3.00e-11

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 70.04  E-value: 3.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  163 SVVNKFNPfdLISDSDTTHEDAGRKQK--VTPKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGQQRPTLQQTESSKPVPQQ 240
Cdd:pfam09606    2 SVVNKIEE--ALQQNGQTSTKNAREMEnhVFAKARTKDEYLGTVARLILHVRDMSKKAAQQQQPQGGQGNGGMGGGQQGM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  241 QQQPGEPKQVQKPGHRQPADAKQeqvkqPPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTT---SQ 317
Cdd:pfam09606   80 PDPINALQNLAGQGTRPQMMGPM-----GPGPGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRVGRMqpgGQ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  318 APPPTKPSSQQPGPAKQplQQPARQGGPVKPSS----------QQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQpgSGKP 387
Cdd:pfam09606  155 AGGMMQPSSGQPGSGTP--NQMGPNGGPGQGQAggmnggqqgpMGGQMPPQMGVPGMPGPADAGAQMGQQAQAN--GGMN 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  388 PLQQTG-----PVKQVPPQAGPTK--------PPSQTAG--PTKPPAQQPG-PTKPSGQQPGPEKPleqkQAGASQPTES 451
Cdd:pfam09606  231 PQQMGGapnqvAMQQQQPQQQGQQsqlgmginQMQQMPQgvGGGAGQGGPGqPMGPPGQQPGAMPN----VMSIGDQNNY 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  452 VSKKTFCPLCTTtELLLHTPEKANYNTCTQCHTVVCSLCGFN----------------------------PNPHITEISE 503
Cdd:pfam09606  307 QQQQTRQQQQQQ-GGNHPAAHQQQMNQSVGQGGQVVALGGLNhletwnpgnfgglganpmqrgqpgmmssPSPVPGQQVR 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  504 WLCLNCQMQRALGGDLAAGHGPGPQPPAPKQKTPIPPSTAKPSPQPQPVQKKDITSKPdPSQLADPKKPPPQKKQTPLPG 583
Cdd:pfam09606  386 QVTPNQFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQRTI-GQDSPGGSLNTPGQSAVNSPL 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  584 SP--------PVKSKQPRAEPTE--ISQQTRDATPKSDQVKPTQAEDKQKQPSVQKPTADTVSTSAALEqkQDLAGPRPP 653
Cdd:pfam09606  465 NPqeeqlyreKYRQLTKYIEPLKrmIAKMENDPGDIDKMNKMKRLLEILSNPSSRIPLETLQKCEAALE--NQMGTPREP 542
PHA03378 PHA03378
EBNA-3B; Provisional
259-455 1.51e-10

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 67.78  E-value: 1.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  259 ADAKQEQVKQPPQPRGPQKSQP------------QPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSS 326
Cdd:PHA03378   619 SAPRQWPMPLRPIPMRPLRMQPitfnvlvfptphQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPP 698
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  327 QQPGPAKQP------LQQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAkQPPQPGSGKPPlqqtgPVKQVPP 400
Cdd:PHA03378   699 RAPTPMRPPaappgrAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRA-RPPAAAPGRAR-----PPAAAPG 772
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2051959432  401 QAGPTKPPSQTAGPTKPPAQQPGPTKPSGQQPGPEKPLEQKQAGASQPTESVSKK 455
Cdd:PHA03378   773 APTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQ 827
PTZ00121 PTZ00121
MAEBL; Provisional
1032-1745 2.01e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.86  E-value: 2.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1032 AKPKEEPGIQKEAPKLQQGRleKTLSADKIQQGVQREDAKpKQGKLVKTPSADKIQRASQKEDPR-IQQTRLTKTAsydR 1110
Cdd:PTZ00121  1151 AKRVEIARKAEDARKAEEAR--KAEDAKKAEAARKAEEVR-KAEELRKAEDARKAEAARKAEEERkAEEARKAEDA---K 1224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1111 VLHEVQKEDEKLQEAKLAKTSSADKilhgVQKEDIKLQETKLAKIPSADKILQGiqKEDPKLQQMKMAKAL-SADKIQPA 1189
Cdd:PTZ00121  1225 KAEAVKKAEEAKKDAEEAKKAEEER----NNEEIRKFEEARMAHFARRQAAIKA--EEARKADELKKAEEKkKADEAKKA 1298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1190 VQKEDAQLQEVKLPKAASVDKIQHgiQKEDIKLQHEKIKKTRSVDKIQEEDQKEETKLQRGKLSKTPSANKIPATTTADQ 1269
Cdd:PTZ00121  1299 EEKKKADEAKKKAEEAKKADEAKK--KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1270 KKPLNTV----EEDKETVPPEKSTPHPEDKKEEITaeiKDHVAKQKAEvEAPYKGLQAKEQEDVKKEdlttgiSQEVLKT 1345
Cdd:PTZ00121  1377 KKKADAAkkkaEEKKKADEAKKKAEEDKKKADELK---KAAAAKKKAD-EAKKKAEEKKKADEAKKK------AEEAKKA 1446
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1346 EKAQEEEIPVQTAplprtdhvEAVREKIEkEDDKSDTSSSQqqkspqglsdtgyssdgissslgeipshipTDEKDLLKE 1425
Cdd:PTZ00121  1447 DEAKKKAEEAKKA--------EEAKKKAE-EAKKADEAKKK------------------------------AEEAKKADE 1487
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1426 SNKKdtiSQESPPSPSDLAKLESTVLSILEAQantlSDEKSAKSKELSETYGEQTKDQLKTKPLPVTPESYSSDEEDLKA 1505
Cdd:PTZ00121  1488 AKKK---AEEAKKKADEAKKAAEAKKKADEAK----KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1506 ---IKEGEGTIVEEGKGTASSQAD-------------YKEDHEGEDIPARRQQRYDSVEDSSESENSPVPRRKRRTSVGS 1569
Cdd:PTZ00121  1561 eekKKAEEAKKAEEDKNMALRKAEeakkaeearieevMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1570 SSSDEYKRDDSQGSGDEEDFIRKQIIEMSADEDASGSEddEFIRNQLKEISAAES-QKKEEVKSKAKGTAGKHRRMARKS 1648
Cdd:PTZ00121  1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE--EAKKAEEDEKKAAEAlKKEAEEAKKAEELKKKEAEEKKKA 1718
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1649 SAGYDEDAGRRHSWHDDDDEtfDESPEPKYRESKSQDGEELAISGGGGLRRFKTIELNSTITAKYSEVSEQQkgilyfDE 1728
Cdd:PTZ00121  1719 EELKKAEEENKIKAEEAKKE--AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE------DE 1790
                          730
                   ....*....|....*..
gi 2051959432 1729 EPELEMESLTDSPEDRS 1745
Cdd:PTZ00121  1791 KRRMEVDKKIKDIFDNF 1807
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
1199-1588 2.18e-10

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 67.76  E-value: 2.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1199 EVKLPKAASVDKIQhgiqKE--DIKLQHEKIKKTRSVDKIQEEDQKEETK-------------------------LQRGK 1251
Cdd:PTZ00108   969 NGKIKKYSDALDIL----KEfyLVRLDLYKKRKEYLLGKLERELARLSNKvrfikhvingelvitnakkkdlvkeLKKLG 1044
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1252 LSKTPSANKIPATTTADQKKplnTVEEDKETVPPEKSTPHPEDKKE----------EITAEIKDHVAKQKAEVEAPYKGL 1321
Cdd:PTZ00108  1045 YVRFKDIIKKKSEKITAEEE---EGAEEDDEADDEDDEEELGAAVSydyllsmpiwSLTKEKVEKLNAELEKKEKELEKL 1121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1322 QAKEQEDVKKEDLTTGIsqEVLKTEKAQEEEIPVQT--APLPRTDHVEAVREKIEKEDDKSDtsssqqqkspqgLSDTGY 1399
Cdd:PTZ00108  1122 KNTTPKDMWLEDLDKFE--EALEEQEEVEEKEIAKEqrLKSKTKGKASKLRKPKLKKKEKKK------------KKSSAD 1187
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1400 SSDGISSSLGeiPSHIPTDEKDLLKE-SNKKDTISQESPPSPSDLAKLESTVLSILEAQANTLSDEKSAKSKELSETYGE 1478
Cdd:PTZ00108  1188 KSKKASVVGN--SKRVDSDEKRKLDDkPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDL 1265
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1479 QTKDQLKTKPLPVTPESYSSDE-------EDLKAIKEGEGTIVEEGKGTASSQADYKEDHEGEDIPARRQQRYDSVEDSS 1551
Cdd:PTZ00108  1266 SKEGKPKNAPKRVSAVQYSPPPpskrpdgESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQAS 1345
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2051959432 1552 ESENSPVPRRKRRTSVGSSS-SDEYKRDDSQGSGDEED 1588
Cdd:PTZ00108  1346 ASQSSRLLRRPRKKKSDSSSeDDDDSEVDDSEDEDDED 1383
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
195-447 2.25e-10

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 67.28  E-value: 2.25e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  195 QGKPEEQRSPAKHPTQPQSPKPAVQ-QQGQQR--PTLQQTESSKPVPQQQQQPGEPKQVQKPGHRQP-----ADAKQEQV 266
Cdd:pfam03157  133 QGQQPGQGQQWYYPTSPQQPGQWQQpGQGQQGyyPTSPQQSGQRQQPGQGQQLRQGQQGQQSGQGQPgyyptSSQQPGQL 212
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  267 KQPPQPRGPQKSQpQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQP------LQQPA 340
Cdd:pfam03157  213 QQTGQGQQGQQPE-RGQQGQQPGQGQQPGQGQQGQQPGQPQQLGQGQQGYYPISPQQPRQWQQSGQGQQgyyptsLQQPG 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  341 RQGGPVKPSSQQAGPPKQLSQQPGPEKpSAQQTGPAKQPPQPGSGkpplqQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQ 420
Cdd:pfam03157  292 QGQSGYYPTSQQQAGQLQQEQQLGQEQ-QDQQPGQGRQGQQPGQG-----QQGQQPAQGQQPGQGQPGYYPTSPQQPGQG 365
                          250       260
                   ....*....|....*....|....*..
gi 2051959432  421 QPGPTKPSGQQPGPEKPLEQKQAGASQ 447
Cdd:pfam03157  366 QPGYYPTSQQQPQQGQQPEQGQQGQQQ 392
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
193-367 2.68e-10

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 66.98  E-value: 2.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  193 KEQGKPEEQRSPAKHPTQPQSPKPAVQQQGQQRPTLQQtesskpvPQQQQQPGEPKQVQKPGHRQPAdakqeQVKQPPQP 272
Cdd:pfam09770  204 RAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQ-------QQQQPQQQPQQPQQHPGQGHPV-----TILQRPQS 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  273 RGPQKSQPQPSEPAKPVQQQTSaklssgPTKPSP----QQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARQGGPVKP 348
Cdd:pfam09770  272 PQPDPAQPSIQPQAQQFHQQPP------PVPVQPtqilQNPNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPI 345
                          170
                   ....*....|....*....
gi 2051959432  349 SSQqagpPKQLSQQPGPEK 367
Cdd:pfam09770  346 ITH----PQQLAQLSEEEK 360
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
192-445 8.02e-10

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 65.35  E-value: 8.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  192 PKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGQQRPTLQQTESSkpvpQQQQQpgepkqvqkPGHRQPA--DAKQEQVKQp 269
Cdd:pfam03157  299 PTSQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQPGQGQQGQQP----AQGQQ---------PGQGQPGyyPTSPQQPGQ- 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  270 PQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSP---QQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARQGGPV 346
Cdd:pfam03157  365 GQPGYYPTSQQQPQQGQQPEQGQQGQQQGQGQQGQQPgqgQQPGQGQPGYYPTSPQQSGQGQPGYYPTSPQQSGQGQQPG 444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  347 KPSSQQAGPPKQlSQQPGpEKPSAQQTGPAKQPPQPGSGKP-----PLQQTGPVKQVPP--QAGPTKPPSQTAGPTKPPA 419
Cdd:pfam03157  445 QGQQPGQEQPGQ-GQQPG-QGQQGQQPGQPEQGQQPGQGQPgyyptSPQQSGQGQQLGQwqQQGQGQPGYYPTSPLQPGQ 522
                          250       260
                   ....*....|....*....|....*.
gi 2051959432  420 QQPGPTKPSGQQPGPEKPLEQKQAGA 445
Cdd:pfam03157  523 GQPGYYPTSPQQPGQGQQLGQLQQPT 548
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
265-418 8.26e-10

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 60.82  E-value: 8.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  265 QVKQPPQPRGPQKSQPQPSEpaKPVQQQTSAKLSSGPTKPSPQQPdsakttsqaPPPTKPSSQQPGPAKQPLQQPARQGG 344
Cdd:pfam15240   25 QEDSPSLISEEEGQSQQGGQ--GPQGPPPGGFPPQPPASDDPPGP---------PPPGGPQQPPPQGGKQKPQGPPPQGG 93
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051959432  345 PVKPSSQQAGPPkqlsQQPGPEKPSAQQTGPAKQPPQPGSGKPPL---QQTGPVKQVPPQAGPTKPPSQTAGPTKPP 418
Cdd:pfam15240   94 PRPPPGKPQGPP----PQGGNQQQGPPPPGKPQGPPPQGGGPPPQggnQQGPPPPPPGNPQGPPQRPPQPGNPQGPP 166
PTZ00121 PTZ00121
MAEBL; Provisional
1031-1598 1.08e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.55  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1031 AAKPKEEPGIQKEAPKLQQGRLEKTLSADKIQQGVQREDAKPKQGKLVKTPSADKiqrasQKEDPRIQQTRLTKTASYDR 1110
Cdd:PTZ00121  1436 AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKK-----KAEEAKKKADEAKKAAEAKK 1510
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1111 VLHEVQKEDEKLQEAKLAKTSSADKILHGVQKEDIKlqetKLAKIPSADKILQGiqKEDPKLQQMKMA---KALSADKIQ 1187
Cdd:PTZ00121  1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK----KADELKKAEELKKA--EEKKKAEEAKKAeedKNMALRKAE 1584
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1188 PAVQKEDAQLQEV-KLPKAASVDKIQHGIQKEDIKLQHEKIKKTRSVDKIQEEDQK--EETKLQRGKLSKTPSANKIPAT 1264
Cdd:PTZ00121  1585 EAKKAEEARIEEVmKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKkeAEEKKKAEELKKAEEENKIKAA 1664
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1265 TTADQKkplntvEEDKEtvppekstphpedKKEEITAEIKDhvaKQKAEveapyKGLQAKEQEDVKKEDLTTGISQEVLK 1344
Cdd:PTZ00121  1665 EEAKKA------EEDKK-------------KAEEAKKAEED---EKKAA-----EALKKEAEEAKKAEELKKKEAEEKKK 1717
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1345 TEKAQEEEipvqtapLPRTDHVEAVREKIEKEDDKSDTSSSQQQKSpqglSDTGYSSDGISSSLGEIPSHIPTDEKDLLK 1424
Cdd:PTZ00121  1718 AEELKKAE-------EENKIKAEEAKKEAEEDKKKAEEAKKDEEEK----KKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1425 ESNKKDTIsqesppspsdlaKLESTVLSILEAQANTL--SDEKSAKSKELSETYGEQTKDQLKTKPLPVTpesySSDE-E 1501
Cdd:PTZ00121  1787 EEDEKRRM------------EVDKKIKDIFDNFANIIegGKEGNLVINDSKEMEDSAIKEVADSKNMQLE----EADAfE 1850
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1502 DLKAIKEGEGTIVEEGKGTASSQADYKEDHEGEDIPARRQQRYDSVEDSSESENSPVPRRKRRTSVGSSSSDEYKRDDSQ 1581
Cdd:PTZ00121  1851 KHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAE 1930
                          570
                   ....*....|....*..
gi 2051959432 1582 GSgdeedfiRKQIIEMS 1598
Cdd:PTZ00121  1931 ET-------REEIIKIS 1940
PTZ00121 PTZ00121
MAEBL; Provisional
1033-1691 1.18e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.16  E-value: 1.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1033 KPKEEPGIQKEAPKLQQGRLEKTLSADKIQQG--VQREDAKPKQGKLVKTPSADKIQRASQKEDPRIQQTRLTKTAS-YD 1109
Cdd:PTZ00121  1249 RNNEEIRKFEEARMAHFARRQAAIKAEEARKAdeLKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEeAK 1328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1110 RVLHEVQKEDEKLQEAKLAKTSSADKILHGVQKEDIKLQETKLaKIPSADKILQGIQKedpKLQQMKMAKALSADKIQPA 1189
Cdd:PTZ00121  1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK-KKEEAKKKADAAKK---KAEEKKKADEAKKKAEEDK 1404
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1190 VQKEDAQLQEVKLPKAASVDKIQHGIQK-EDIKLQHEKIKKTRSVDKIQEEDQKEETKLQRGKLSKTPSANKIPATTTAD 1268
Cdd:PTZ00121  1405 KKADELKKAAAAKKKADEAKKKAEEKKKaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK 1484
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1269 QKKPLNTVEEDKETVPPEKSTPHPEDKKEEITAEIKDHVAKQKAEVEAPYKGLQAKEQEDVKKEDlttgisqEVLKTEKA 1348
Cdd:PTZ00121  1485 ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD-------ELKKAEEL 1557
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1349 QEEEipvqtaplprtdHVEAVREKIEKEDDKSDTSSSQQQKSPqglsdtgyssdgISSSLGEIPSHIPTDEKDLLKESNK 1428
Cdd:PTZ00121  1558 KKAE------------EKKKAEEAKKAEEDKNMALRKAEEAKK------------AEEARIEEVMKLYEEEKKMKAEEAK 1613
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1429 KdtiSQESPPSPSDLAKLESTVLSILEAQANTLSDEKSAKSKELSETYGEQTKDQLKTKplpvtpesyssDEEDLKAIKE 1508
Cdd:PTZ00121  1614 K---AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK-----------AEEDKKKAEE 1679
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1509 GEGTIVEEGKGTASSQADYKEDHEGEDIPARRQQRYDSVEDSSESENSpvprRKRRTSVGSSSSDEYKRDDSQGSGDEED 1588
Cdd:PTZ00121  1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE----NKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1589 fiRKQIIEMSADEDASGSEDDEFIRNQLKE-ISAAESQKKEEVKSKAKGTagkhrrmaRKSSAGYDEDAGRRHSWHDDDD 1667
Cdd:PTZ00121  1756 --KKKIAHLKKEEEKKAEEIRKEKEAVIEEeLDEEDEKRRMEVDKKIKDI--------FDNFANIIEGGKEGNLVINDSK 1825
                          650       660
                   ....*....|....*....|....
gi 2051959432 1668 ETFDESPEPKYRESKSQDGEELAI 1691
Cdd:PTZ00121  1826 EMEDSAIKEVADSKNMQLEEADAF 1849
PDZ3_PDZD2-PDZ1_hPro-IL-16-like cd06759
PDZ domain 3 of PDZ domain containing 2 (PDZD2), PDZ domain 1 of human pro-interleukin-16 ...
4546-4606 2.90e-09

PDZ domain 3 of PDZ domain containing 2 (PDZD2), PDZ domain 1 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family also includes the first PDZ domain (PDZ1) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16; 1332 amino-acid protein). Precursor IL-16 is cleaved to produce pro-IL-16 and mature IL-16 (derived from the C-terminal 121 AA). Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467240 [Multi-domain]  Cd Length: 87  Bit Score: 56.90  E-value: 2.90e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051959432 4546 GNGLGIRVVGGKEIPgsSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEE 4606
Cdd:cd06759     11 GKGLGFSIVGGRDSP--RGPMGIYVKTIFPGGAAAEDGRLKEGDEILEVNGESLQGLTHQE 69
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
4547-4617 3.18e-09

PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of human PTPN13, and related domains. PTPN13, also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1), negatively regulates FAS-mediated apoptosis and NGFR-mediated pro-apoptotic signaling, and may also regulate phosphoinositide 3-kinase (PI3K) signaling. It contains 5 PDZ domains; interaction partners of its second PDZ domain (PDZ2) include the Fas receptor (TNFRSF6) and thyroid receptor-interacting protein 6 (TRIP6). The second PDZ (PDZ2) domain, but not PDZ1 or PDZ3, of FRMPD2 binds to GluN2A and GluN2B, two subunits of N-methyl-d-aspartic acid (NMDA) receptors. Other binding partners of the FRMPDZ2 PDZ2 domain include NOD2, and catenin family members, delta catenin (CTNND2), armadillo repeat gene deleted in velo-cardio-facial syndrome (ARVCF) and p0071 (also known as plakophilin 4; PKP4). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467254 [Multi-domain]  Cd Length: 87  Bit Score: 56.45  E-value: 3.18e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051959432 4547 NGLGIRVVGGKEIPGSSGeiGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSiIIQQSGE 4617
Cdd:cd06792     12 GSLGISVTGGINTSVRHG--GIYVKSLVPGGAAEQDGRIQKGDRLLEVNGVSLEGVTHKQAVE-CLKNAGQ 79
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
4540-4611 4.70e-09

PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains, and is expressed at exceptionally high levels in the pancreas and certain cancer tissues such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467239 [Multi-domain]  Cd Length: 88  Bit Score: 56.21  E-value: 4.70e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051959432 4540 KDHTVSGN-GLGIRVVGGKeipGSS-GEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSII 4611
Cdd:cd06758      4 KMHLLKEKgGLGIQITGGK---GSKrGDIGIFVAGVEEGGSADRDGRLKKGDELLMINGQSLIGLSHQEAVAIL 74
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
250-688 5.80e-09

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 62.78  E-value: 5.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  250 VQKPGHRQPADAKQEQVKQPPQPRGPQKSQPQPSEPAkpvqqqtSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQP 329
Cdd:PTZ00449   489 IKKSKKKLAPIEEEDSDKHDEPPEGPEASGLPPKAPG-------DKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKP 561
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  330 GPAKQ--PLQQPA---RQGGPVKPSSQQAgpPKQLSQQPGPEKPSAQQTGPAKQPPQ----PGSGKPPLQQTGPVKQVPP 400
Cdd:PTZ00449   562 GPAKEhkPSKIPTlskKPEFPKDPKHPKD--PEEPKKPKRPRSAQRPTRPKSPKLPElldiPKSPKRPESPKSPKRPPPP 639
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  401 Q--AGPTKPPSQTAGPT-KPPAQQPGPTKPSGQqpgpEKPLEQKQAGASQPTESvskKTFCPLCTTTELLLHTPEKANYN 477
Cdd:PTZ00449   640 QrpSSPERPEGPKIIKSpKPPKSPKPPFDPKFK----EKFYDDYLDAAAKSKET---KTTVVLDESFESILKETLPETPG 712
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  478 TCTQCHTVVCSLCGFNPNPHITEISEwlclncqmqralggdlaaghgPGPQPPAPKQKTPIPPS-------TAKPSPQP- 549
Cdd:PTZ00449   713 TPFTTPRPLPPKLPRDEEFPFEPIGD---------------------PDAEQPDDIEFFTPPEEertffheTPADTPLPd 771
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  550 ---QPVQKKDITSKP-DPSQLADPKKPPPQKKQTPLPGSPPVKSKQPRAE---------PTEISQQTRDATPKSDQVKPT 616
Cdd:PTZ00449   772 ilaEEFKEEDIHAETgEPDEAMKRPDSPSEHEDKPPGDHPSLPKKRHRLDglalsttdlESDAGRIAKDASGKIVKLKRS 851
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  617 QAED--------KQKQPSVQKPTADTVSTSAALEQKQdlagprPPTQQKVTD----SPKPELAKPSQDTHPAE-DKPDSK 683
Cdd:PTZ00449   852 KSFDdlttveeaEEMGAEARKIVVDDDGTEADDEDTH------PPEEKHKSEvrrrRPPKKPSKPKKPSKPKKpKKPDSA 925

                   ....*
gi 2051959432  684 PVPQV 688
Cdd:PTZ00449   926 FIPSI 930
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
196-404 6.02e-09

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 62.75  E-value: 6.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  196 GKPEEQRSPAKHPTQPQSPKPAVQQQGQQRPTLQQTESskpvpqqqqqpgepkqvqkpghrqpadAKQEQVKQPPQPRGP 275
Cdd:pfam09770  164 GVAPKKAAAPAPAPQPAAQPASLPAPSRKMMSLEEVEA---------------------------AMRAQAKKPAQQPAP 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  276 Q-KSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPT---KPSSQQPGPAKQPLQQPARQGGPVKPSSQ 351
Cdd:pfam09770  217 ApAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTilqRPQSPQPDPAQPSIQPQAQQFHQQPPPVP 296
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2051959432  352 QAgpPKQLSQQPGpeKPSAQQTgPAKQPPQPGSGKPPLQQTGPVKQVPPQAGP 404
Cdd:pfam09770  297 VQ--PTQILQNPN--RLSAARV-GYPQNPQPGVQPAPAHQAHRQQGSFGRQAP 344
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
510-794 6.41e-09

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 62.09  E-value: 6.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  510 QMQRALGGDLAAGHGPGPQPPAPKQKTPIPPSTAKP--SPQPQPVQKK----DITSKPDPSQLADPKKPPPQKKQTPLPG 583
Cdd:NF033839   142 KFEKDSSSSSSSGSSTKPETPQPENPEHQKPTTPAPdtKPSPQPEGKKpsvpDINQEKEKAKLAVATYMSKILDDIQKHH 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  584 SPPVKSKQPRAEPTEISQQTRDATPKSDQVKPtqaeDKQKQPSVQKPTADTVSTSAALEQKQDLAGPRPPtqqkvtDSPK 663
Cdd:NF033839   222 LQKEKHRQIVALIKELDELKKQALSEIDNVNT----KVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEP------GNKK 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  664 PELAKPSQDTHPAEDKPDSKPVPQVSRQKSDPKLAS-QPGARPDAKAQKP-VEPTQTKDDPKKLPTKPAPKPDTKAAPKG 741
Cdd:NF033839   292 PSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKpKPEVKPQPEKPKPeVKPQLETPKPEVKPQPEKPKPEVKPQPEK 371
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2051959432  742 PQAGAGPKPGPAQPAPQPQPPQKTPEQSRRFSLNLGGItdapKPQPTTPQETV 794
Cdd:NF033839   372 PKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEV----KPQPEKPKPEV 420
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
191-435 7.87e-09

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 61.71  E-value: 7.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  191 TPKEQGKPEeqrspakhptqPQSPKPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPKQVQKPghrQPADAKQEQVKQPP 270
Cdd:NF033839   283 TPKEPGNKK-----------PSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKP---QPEKPKPEVKPQLE 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  271 QPRGPQKsqPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPlqQPARQGGPVKPSS 350
Cdd:NF033839   349 TPKPEVK--PQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKP--QPEKPKPEVKPQP 424
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  351 QQAGPPKQlsqqPGPEKPSAQQTgpakqpPQPGSGKPplqqtgpvkQVPPQAGPTKPPSQTAGPTKPPAQQPGPTKPSGQ 430
Cdd:NF033839   425 EKPKPEVK----PQPEKPKPEVK------PQPEKPKP---------EVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPD 485

                   ....*
gi 2051959432  431 QPGPE 435
Cdd:NF033839   486 NSKPQ 490
motB PRK05996
MotB family protein;
147-379 7.89e-09

MotB family protein;


Pssm-ID: 235665 [Multi-domain]  Cd Length: 423  Bit Score: 61.25  E-value: 7.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  147 MMPSFL-----SEANPLSAvTSVVNKFNPFDLiSDSDTThedagRK--QKVTPKEQGKPEEQRSPAKhPTQPQSPKPAVQ 219
Cdd:PRK05996    43 MMAFFLvmwliNAANEETK-AAVASYFNPIKL-TDRKPS-----EKglKDPVDGAEGEQKPGKSKFE-EDQRVEGSSAVT 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  220 QQGQQRPTLQQTESSKPVPQQQQQPGEPKQVQKPGHRQPADAKQEQvkqppqprGPQKSQPQ-----------PSEP--- 285
Cdd:PRK05996   115 GDDTTRTSGDQTNYSEADLFRNPYAVLAEIAQEVGQQANVSAKGDG--------GAAQSGPAtgadggeayrdPFDPdfw 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  286 AKPVQQQT-SAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSsqqpgPAKQPlQQPARQGGPVK--PSSQQAGPPKQLSQQ 362
Cdd:PRK05996   187 SKQVEVTTaGDLLPPGQAREQAQGAKSATAAPATVPQAAPL-----PQAQP-KKAATEEELIAdaKKAATGEPAANAAKA 260
                          250
                   ....*....|....*..
gi 2051959432  363 PGPEKPSAQQTGPAKQP 379
Cdd:PRK05996   261 AKPEPMPDDQQKEAEQL 277
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
4529-4611 2.50e-08

PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of MUPP1 and PDZ domain 6 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ7 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467159 [Multi-domain]  Cd Length: 96  Bit Score: 54.25  E-value: 2.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 4529 PHTRLKLLRDPkdhtvsGNGLGIRVVGGKEI---PGSSGEI-GAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTY 4604
Cdd:cd06671      1 PPRRVELWREP------GKSLGISIVGGRVMgsrLSNGEEIrGIFIKHVLEDSPAGRNGTLKTGDRILEVNGVDLRNATH 74

                   ....*..
gi 2051959432 4605 EEVQSII 4611
Cdd:cd06671     75 EEAVEAI 81
PTZ00121 PTZ00121
MAEBL; Provisional
1021-1811 2.65e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.93  E-value: 2.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1021 QKTSTPPTLAAAKPKEEPGIQKEAPKLQQGRleKTLSADKIQQGVQREDAKPKQGKLvKTPSADKIQRASQKEDPRiqQT 1100
Cdd:PTZ00121  1104 KKTETGKAEEARKAEEAKKKAEDARKAEEAR--KAEDARKAEEARKAEDAKRVEIAR-KAEDARKAEEARKAEDAK--KA 1178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1101 RLTKTASYDRVLHEVQKEDE--KLQEAKLA----KTSSADKILHGVQKEDIKLQETKLAKIPSADKILQgiQKEDPKLQQ 1174
Cdd:PTZ00121  1179 EAARKAEEVRKAEELRKAEDarKAEAARKAeeerKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEE--ERNNEEIRK 1256
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1175 MKMAKALSADKIQPAVQKEDAQLQEvKLPKAASVDKIQHGIQKEDIKLQHEKIKKTRSVDKIQEEDQK-EETKLQRGKLS 1253
Cdd:PTZ00121  1257 FEEARMAHFARRQAAIKAEEARKAD-ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKaEEAKKKADAAK 1335
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1254 KTPSANKipattTADQKKPLNTVEEDKETVPPEKSTPHPEDKKEEitAEIKDHVAKQKAEVEAPYKGLQAKEQEDVKKED 1333
Cdd:PTZ00121  1336 KKAEEAK-----KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE--AKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1334 lttgisqEVLKTEKAQE--EEIPVQTAPLPRTDHVEAVREKIEKEDD-KSDTSSSQQQKSPQGLSDTGYSSDGISSSlge 1410
Cdd:PTZ00121  1409 -------ELKKAAAAKKkaDEAKKKAEEKKKADEAKKKAEEAKKADEaKKKAEEAKKAEEAKKKAEEAKKADEAKKK--- 1478
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1411 ipshipTDEKDLLKESNKKdtiSQESPPSPSDLAKLESTVLSILEAQantlSDEKSAKSKELSETYGEQTKDQLKTKPLP 1490
Cdd:PTZ00121  1479 ------AEEAKKADEAKKK---AEEAKKKADEAKKAAEAKKKADEAK----KAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1491 VTPESYSSDEEDLKA---IKEGEGTIVEEGKGTASSQAD-------------YKEDHEGEDIPARRQQRYDSVEDSSESE 1554
Cdd:PTZ00121  1546 KKADELKKAEELKKAeekKKAEEAKKAEEDKNMALRKAEeakkaeearieevMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1555 NSPVPRRKRRTSVGSSSSDEYKRDDSQGSGDEEDFIRKQIIEMSADEDASGSEddEFIRNQLKEISAAES-QKKEEVKSK 1633
Cdd:PTZ00121  1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE--EAKKAEEDEKKAAEAlKKEAEEAKK 1703
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1634 AKGTAGKHRRMARKSSAGYDEDAGRRHSWHDDDDEtfDESPEPKYRESKSQDGEELAISGGGGLRRFKTIELNSTITAKY 1713
Cdd:PTZ00121  1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE--AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1714 SEVSEQQkgilyfDEEPELEMESLTDSPEDRSR------GEGSSSLHAS--SFTPGTSPTSVSSLDEDSDSSPSHKKLGG 1785
Cdd:PTZ00121  1782 EEELDEE------DEKRRMEVDKKIKDIFDNFAniieggKEGNLVINDSkeMEDSAIKEVADSKNMQLEEADAFEKHKFN 1855
                          810       820
                   ....*....|....*....|....*...
gi 2051959432 1786 ESKQQRKARHRTHGPLLPT--IEDSSEE 1811
Cdd:PTZ00121  1856 KNNENGEDGNKEADFNKEKdlKEDDEEE 1883
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
187-457 4.51e-08

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 59.70  E-value: 4.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  187 KQKVTPKEQGKPEEQRSPAKHPTQ----PQSPKPAVQQQGQQRPTlQQTESSKPVPQQQQQPGEPKQvQKPG---HRQPA 259
Cdd:PTZ00449   493 KKKLAPIEEEDSDKHDEPPEGPEAsglpPKAPGDKEGEEGEHEDS-KESDEPKEGGKPGETKEGEVG-KKPGpakEHKPS 570
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  260 -----DAKQEQVKQPPQPRGPQ--KSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSS-QQPGP 331
Cdd:PTZ00449   571 kiptlSKKPEFPKDPKHPKDPEepKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSpERPEG 650
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  332 AKQPL--QQPARQGGPVKPS---------SQQAGPPKQlSQQPGPEKPSAQQTGPAKQPPQPGSgkpPLQQTGPvkqVPP 400
Cdd:PTZ00449   651 PKIIKspKPPKSPKPPFDPKfkekfyddyLDAAAKSKE-TKTTVVLDESFESILKETLPETPGT---PFTTPRP---LPP 723
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2051959432  401 QAgPTKPPSQTAGPTKPPAQQPGPTKPSgqQPGPEKPLEQKQAGASQPTESVSKKTF 457
Cdd:PTZ00449   724 KL-PRDEEFPFEPIGDPDAEQPDDIEFF--TPPEEERTFFHETPADTPLPDILAEEF 777
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
203-409 5.60e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 59.61  E-value: 5.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  203 SPAKHPTQPQSPKPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPKQVQKPGHRQPAdAKQEQVKQPPQPRGPQKSQPQP 282
Cdd:PRK07764   592 PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVA-APEHHPKHVAVPDASDGGDGWP 670
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  283 SEPAKPVQQQTSAklSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARQGGPVKPSSQQAGPPKQLSQQ 362
Cdd:PRK07764   671 AKAGGAAPAAPPP--APAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDP 748
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2051959432  363 PGPEKP--SAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPTKPPS 409
Cdd:PRK07764   749 PDPAGApaQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDED 797
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
527-789 9.30e-08

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 58.24  E-value: 9.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  527 PQPPApKQKTPIPPSTAKPSPQPQpvqkkditSKPDPSQLADPKKPPPQKKQTPLPGSPPvkskQPRAEPTEISQQTRDA 606
Cdd:NF033839   284 PKEPG-NKKPSAPKPGMQPSPQPE--------KKEVKPEPETPKPEVKPQLEKPKPEVKP----QPEKPKPEVKPQLETP 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  607 TPKSDQVKPTQAEDKQKQPSVQKPTADTVSTSAALEQKQDLAGPRPPTQqkvtdsPKPELAKPSQDTHPAEDKPDSKPVP 686
Cdd:NF033839   351 KPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVK------PQPEKPKPEVKPQPEKPKPEVKPQP 424
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  687 QVSRQKSDPKLAS-QPGARPDAKAQKP-VEPTQTKDDPKKLPTKPAPKPDTKAAPKGPQAGAGPKPGPAQPAPQPQPPQK 764
Cdd:NF033839   425 EKPKPEVKPQPEKpKPEVKPQPEKPKPeVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPSTPNNLSK 504
                          250       260
                   ....*....|....*....|....*
gi 2051959432  765 TPEQSRRFSLNLGGITDAPKPQPTT 789
Cdd:NF033839   505 DKQPSNQASTNEKATNKPKKSLPST 529
PHA03378 PHA03378
EBNA-3B; Provisional
179-451 9.77e-08

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 58.93  E-value: 9.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  179 TTHEDAGRKQKVTPKEQGKPEEQRSPAKHPTQPQSP-KPAVQQQGQQRPTlqQTESSKPVPQQQQQPGEPKQVQKPGHRQ 257
Cdd:PHA03378   678 PTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRaQRPAAATGRARPP--AAAPGRARPPAAAPGRARPPAAAPGRAR 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  258 PADAKQEQVKQPPQPRGPQKSQPQPSEPAKPVQQQTSAklssgptkPSPQQpdsakttsqaPPPTKPSSQQPGPakqplQ 337
Cdd:PHA03378   756 PPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGA--------PTPQP----------PPQAGPTSMQLMP-----R 812
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  338 QPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSA-QQTGPAKQPPQPGSGKPPLQQTGPV--------KQVPPQAGPTKPP 408
Cdd:PHA03378   813 AAPGQQGPTKQILRQLLTGGVKRGRPSLKKPAAlERQAAAGPTPSPGSGTSDKIVQAPVfyppvlqpIQVMRQLGSVRAA 892
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2051959432  409 SQTAGPtKPPAQQPGPTKPSGQQPgPEKPLEQKQAGASQPTES 451
Cdd:PHA03378   893 AASTVT-QAPTEYTGERRGVGPMH-PTDIPPSKRAKTDAYVES 933
PDZ3_MAGI-1_3-like cd06733
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
4547-4607 1.37e-07

PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467215 [Multi-domain]  Cd Length: 85  Bit Score: 51.84  E-value: 1.37e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051959432 4547 NGLGIRVVGGKEiPGSSGEIGAyiakILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEV 4607
Cdd:cd06733     11 TGFGFRILGGTE-EGSQVSIGA----IVPGGAADLDGRLRTGDELLSVDGVNVVGASHHKV 66
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
4547-4610 1.44e-07

PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Par3 (or PAR3 or Par-3, also known as Atypical PKC isotype-specific-interacting protein, ASIP, Drosophila Bazooka) and related domains. Par3 is a scaffold protein involved in organizing cell polarity across animals. Par3 binds numerous molecules both for its recruitment to one pole of the cell and for downstream contributions to polarized cell function. It regulates cell polarity by targeting the Par complex proteins Par6 and atypical protein kinase C (aPKC) to specific cortical sites. Physical interactions between Par3 and the Par complex include Par3 PDZ domain 1 binding to the Par6 PDZ domain, Par3 PDZ domain 1 and PDZ domain 3 binding the Par6's PDZ-binding motif, and an interaction with an undefined region of aPKC that requires both Par3 PDZ2 and PDZ3. The PDZ domains of Par3 have also been implicated as potential phosphoinositide signaling integrators, since its second PDZ domain binds to phosphoinositides, and the third PDZ interacts with phosphoinositide phosphatase PTEN. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par3 family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467271 [Multi-domain]  Cd Length: 93  Bit Score: 52.26  E-value: 1.44e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051959432 4547 NGLGIRVVGGKEIPGSSGEIgaYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSI 4610
Cdd:cd23058     15 EGLGFSITSRDNPTGGSGPI--YIKNILPKGAAIQDGRLKAGDRLLEVNGVDVTGKTQEEVVSL 76
PHA03378 PHA03378
EBNA-3B; Provisional
192-449 1.57e-07

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 58.15  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  192 PKEQGKPEEQRSPAKHPtQPQSPKPAVQQQGQQ-------RPTLQQTESSKPVPQQQQQPGEPKQVQKPGHRQPADAKQE 264
Cdd:PHA03378   609 PTTQSHIPETSAPRQWP-MPLRPIPMRPLRMQPitfnvlvFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPI 687
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  265 Q----VKQPPqPRGPQKSQPqPSEPAKPVQQQTSAklsSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPa 340
Cdd:PHA03378   688 QwapgTMQPP-PRAPTPMRP-PAAPPGRAQRPAAA---TGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAP- 761
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  341 rqgGPVKPSSQQAGPPKQLSQQPGPEKPSAQ-QTGPAKQPPqPGSGKPPLQQTGPvkQVPPQAGPTKPPSQTAGPTKPPA 419
Cdd:PHA03378   762 ---GRARPPAAAPGAPTPQPPPQAPPAPQQRpRGAPTPQPP-PQAGPTSMQLMPR--AAPGQQGPTKQILRQLLTGGVKR 835
                          250       260       270
                   ....*....|....*....|....*....|.
gi 2051959432  420 QQPGPTKPS-GQQPGPEKPLEQKQAGASQPT 449
Cdd:PHA03378   836 GRPSLKKPAaLERQAAAGPTPSPGSGTSDKI 866
PRK10263 PRK10263
DNA translocase FtsK; Provisional
309-794 1.75e-07

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 58.17  E-value: 1.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  309 PDSAKTTSQAPPPTKPSSQQPGPAKQPLQqparqgGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPP 388
Cdd:PRK10263   336 PVEPVTQTPPVASVDVPPAQPTVAWQPVP------GPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYA 409
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  389 LQQTGPVKQ---VPPQAGPTKPPSQTAGPTKPPAQQPGPTKPSGQQPGPEkPLEQKQAGASQPtesvskktfcplcTTTE 465
Cdd:PRK10263   410 PAAEQPAQQpyyAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQ-STYQTEQTYQQP-------------AAQE 475
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  466 LLLHTPEKANYNTCTQCHTVVCSLCGFNPNPHITEisewlclNCQMQRALGGD-LAAGHGPGPQPpaPKQKTPIPPSTAK 544
Cdd:PRK10263   476 PLYQQPQPVEQQPVVEPEPVVEETKPARPPLYYFE-------EVEEKRAREREqLAAWYQPIPEP--VKEPEPIKSSLKA 546
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  545 PSPQPQPVQKKDITSKPDPSQLADPKKPPPQKKQTPLPGSPPVKSKQPRAE-----------PTEISQQTRDATPKSDQV 613
Cdd:PRK10263   547 PSVAAVPPVEAAAAVSPLASGVKKATLATGAAATVAAPVFSLANSGGPRPQvkegigpqlprPKRIRVPTRRELASYGIK 626
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  614 KPTQ--AEDKQKQPS-VQKPTADTVSTSAALEQKQD-LAGPRPPTQQK----------------VTDSPKPELAK---PS 670
Cdd:PRK10263   627 LPSQraAEEKAREAQrNQYDSGDQYNDDEIDAMQQDeLARQFAQTQQQrygeqyqhdvpvnaedADAAAEAELARqfaQT 706
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  671 QDTHPAEDKP-----------DSKPVPQ-VSRQKSDPKLAsqPGARPDAKAQKPVEPTQTKDDPKklptKPAPKPDTKAA 738
Cdd:PRK10263   707 QQQRYSGEQPaganpfslddfEFSPMKAlLDDGPHEPLFT--PIVEPVQQPQQPVAPQQQYQQPQ----QPVAPQPQYQQ 780
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2051959432  739 PKGPQAgAGPKPGPAQPAPQPQPPQKTPEQSRrfslnlggitdAPKPQPTTPQETV 794
Cdd:PRK10263   781 PQQPVA-PQPQYQQPQQPVAPQPQYQQPQQPV-----------APQPQYQQPQQPV 824
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
208-451 1.76e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 57.69  E-value: 1.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  208 PTQPQSPKPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPKQVQKPGHRQPADAKQEQVKQPPQPRGPQKSQPQPSEPAK 287
Cdd:PRK07764   423 PAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAA 502
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  288 PVQQQTSAKL----------------------------------------SSGPTKPSPQQPDSAK-------------- 313
Cdd:PRK07764   503 PAGADDAATLrerwpeilaavpkrsrktwaillpeatvlgvrgdtlvlgfSTGGLARRFASPGNAEvlvtalaeelggdw 582
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  314 -------TTSQAPPPTKPSSQQPGPAKQPLQQPARQGGPVKPS----SQQAGPPKQLSQQPGPEKPSAQQTGPAK---QP 379
Cdd:PRK07764   583 qveavvgPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAapapAGAAAAPAEASAAPAPGVAAPEHHPKHVavpDA 662
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432  380 PQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGPTKPSGQQPGPEKPLEQKQAGASQPTES 451
Cdd:PRK07764   663 SDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPA 734
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
4548-4616 1.97e-07

PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1-7 (also known as MAGUK p55 subfamily members 1-7), and related domains. MPPs comprise a subfamily of a larger group of multidomain proteins, namely, membrane-associated guanylate kinases (MAGUKs). MPPs form diverse protein complexes at the cell membranes, which are involved in a wide range of cellular processes, including establishing proper cell structure, polarity and cell adhesion. MPPs have only one PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467208 [Multi-domain]  Cd Length: 80  Bit Score: 51.11  E-value: 1.97e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051959432 4548 GLGIRVVGGKEIpgssgeigayIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSIIIQQSG 4616
Cdd:cd06726     14 GATIKMEEDSVI----------VARILHGGMAHRSGLLHVGDEILEINGIPVSGKTVDELQKLLSSLSG 72
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
270-669 2.03e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 57.87  E-value: 2.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  270 PQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKT--TSQAPPPTKPSSQQPGPAKQPlqQPARQggPVK 347
Cdd:PHA03307    63 DRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTppGPSSPDPPPPTPPPASPPPSP--APDLS--EML 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  348 PSSQQAGPPKQLSQQPGPEKPSAQQTGPAkqppQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGPTKP 427
Cdd:PHA03307   139 RPVGSPGPPPAASPPAAGASPAAVASDAA----SSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPIS 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  428 SGQQPGPEKPLEQKQAGASQpTESVSKKTFCPLCTTTELllhtpekanyNTCTQCHTVVCSLCGfnpnpHITEISEWLCL 507
Cdd:PHA03307   215 ASASSPAPAPGRSAADDAGA-SSSDSSSSESSGCGWGPE----------NECPLPRPAPITLPT-----RIWEASGWNGP 278
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  508 NCQMQRALGGDLAAGHGPGPQPPAPKQ--KTPIPPSTAKPSPQPQPVQKKDITSKPDPSQLADPKKPPPQKKQTPLPGSP 585
Cdd:PHA03307   279 SSRPGPASSSSSPRERSPSPSPSSPGSgpAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPP 358
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  586 PV----KSKQPRAEPTEISQQTRDATPKSDQVKPTQAEDKQKQpsvQKPTADTVSTSAALEQKQDLAGPRPPTQQK---V 658
Cdd:PHA03307   359 PAdpssPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRR---DATGRFPAGRPRPSPLDAGAASGAFYARYPlltP 435
                          410
                   ....*....|.
gi 2051959432  659 TDSPKPELAKP 669
Cdd:PHA03307   436 SGEPWPGSPPP 446
PHA03377 PHA03377
EBNA-3C; Provisional
209-451 2.17e-07

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 57.76  E-value: 2.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  209 TQPQSPKPAV---QQQGQQRPTLQQTESSKPVPQQQQQPGEPKQVQK--------PGHRQPADAKQEQVKQPPQPRGpQK 277
Cdd:PHA03377   640 EQSTGPKPKSfweMRAGRDGSGIQQEPSSRRQPATQSTPPRPSWLPSvfvlpsvdAGRAQPSEESHLSSMSPTQPIS-HE 718
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  278 SQPQPSEPakpvqqQTSAKLSSGP---TKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQP---LQQPARQGGPVKPSSQ 351
Cdd:PHA03377   719 EQPRYEDP------DDPLDLSLHPdqaPPPSHQAPYSGHEEPQAQQAPYPGYWEPRPPQAPylgYQEPQAQGVQVSSYPG 792
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  352 QAGPPKQLSQQPGPEKPSAqqtgPAKQPPQPGSGKPPLQQTGPvkQVPPQAGPTKPPSQTAGPTKPPAQ-QPGPTKPSgQ 430
Cdd:PHA03377   793 YAGPWGLRAQHPRYRHSWA----YWSQYPGHGHPQGPWAPRPP--HLPPQWDGSAGHGQDQVSQFPHLQsETGPPRLQ-L 865
                          250       260
                   ....*....|....*....|.
gi 2051959432  431 QPGPEKPLEQKQAGASQPTES 451
Cdd:PHA03377   866 SQVPQLPYSQTLVSSSAPSWS 886
PDZ1_FRMPD2-like cd23071
PDZ domain 1 of FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ ...
4532-4617 2.28e-07

PDZ domain 1 of FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of FRMPD2 (also known as PDZ domain-containing protein 4, and related domains. FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467284 [Multi-domain]  Cd Length: 92  Bit Score: 51.34  E-value: 2.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 4532 RLKLLRDPKdhtvsgNGLGIRVVGGKEIpgSSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSiI 4611
Cdd:cd23071      4 CVTLKRDPK------RGFGFVIVGGENT--GKLDLGIFIASIIPGGPAEKDGRIKPGGRLISLNNISLEGVTFNTAVK-I 74

                   ....*.
gi 2051959432 4612 IQQSGE 4617
Cdd:cd23071     75 LQNSPD 80
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
211-447 2.39e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 57.47  E-value: 2.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  211 PQSPKPAVQQQGQQRPTLQQTESSKPVpqqqqqpgepkqvQKPGHRQP---ADAKQEQVKQPPQPRGPQKSQPQPSEPAK 287
Cdd:pfam03154  310 PPGPSPAAPGQSQQRIHTPPSQSQLQS-------------QQPPREQPlppAPLSMPHIKPPPTTPIPQLPNPQSHKHPP 376
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  288 PVQQQTSAKLSSGPTKPSPQQPDSAKTTSQaPPPTKPSSQQPGPAKQPLQQPARQGgPVKPSSQQAGPPKQLSQQPGPEK 367
Cdd:pfam03154  377 HLSGPSPFQMNSNLPPPPALKPLSSLSTHH-PPSAHPPPLQLMPQSQQLPPPPAQP-PVLTQSQSLPPPAASHPPTSGLH 454
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  368 PSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQTA----GP-------TKPPAQ----------QPGPTK 426
Cdd:pfam03154  455 QVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASvsssGPvpaavscPLPPVQikeealdeaeEPESPP 534
                          250       260
                   ....*....|....*....|.
gi 2051959432  427 PSGQQPGPEKPLEQKQAGASQ 447
Cdd:pfam03154  535 PPPRSPSPEPTVVNTPSHASQ 555
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
169-457 2.48e-07

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 57.00  E-value: 2.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  169 NPFDLISDSDTTHEDAGRKQKVTPKeqGKPEEQRSPAKHPTQPQSPKPAVQQQGQQRPTLQ------------------Q 230
Cdd:COG5180    213 EPPDLTGGADHPRPEAASSPKVDPP--STSEARSRPATVDAQPEMRPPADAKERRRAAIGDtpaaeppglpvleagsepQ 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  231 TESSKPVPQQQQQPGEPKQVQK--------PGHRQPADAKQEQVKQPPQ---PRGPQKSQP-------QPSEPAKPVQQQ 292
Cdd:COG5180    291 SDAPEAETARPIDVKGVASAPPatrpvrppGGARDPGTPRPGQPTERPAgvpEAASDAGQPpsayppaEEAVPGKPLEQG 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  293 TSAKLSSGPTKPSPQQPDSAKTTS-----------QAPPPTKPSSQQPGPAKQPLQQPARQGGPVKPSSQQAGPPKQLSQ 361
Cdd:COG5180    371 APRPGSSGGDGAPFQPPNGAPQPGlgrrgapgppmGAGDLVQAALDGGGRETASLGGAAGGAGQGPKADFVPGDAESVSG 450
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  362 QPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPtkppsqtAGPTKPPAQQPGPTKPSGQQPGPEKPLEQK 441
Cdd:COG5180    451 PAGLADQAGAAASTAMADFVAPVTDATPVDVADVLGVRPDAIL-------GGNVAPASGLDAETRIIEAEGAPATEDFVA 523
                          330
                   ....*....|....*.
gi 2051959432  442 qAGASQPTESVSKKTF 457
Cdd:COG5180    524 -AELSELREAAEEKTG 538
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
251-448 2.57e-07

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 57.19  E-value: 2.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  251 QKPGHRQPADAKQEQVKQP------PQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQqPDSAKTTSQAPPPTKP 324
Cdd:PRK12323   367 QSGGGAGPATAAAAPVAQPapaaaaPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPA-PEALAAARQASARGPG 445
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  325 SSQQPGPAkqPLQQPARQGGPvkPSSQQAGPPKQLSQQPGPEKPSAqQTGPAKQPPQPGSGKPP-LQQTGPVKQVPPQAG 403
Cdd:PRK12323   446 GAPAPAPA--PAAAPAAAARP--AAAGPRPVAAAAAAAPARAAPAA-APAPADDDPPPWEELPPeFASPAPAQPDAAPAG 520
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2051959432  404 PTKPPSQTAGPTKPPAQQPGPTKPSGQQPGPEKPLEQKQAGASQP 448
Cdd:PRK12323   521 WVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRP 565
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
287-456 2.90e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 56.80  E-value: 2.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  287 KPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPgPAKQPLQQPARQggPVKPSSQQAGPPKQLSQQPGPE 366
Cdd:PRK07994   360 HPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPP-PASAPQQAPAVP--LPETTSQLLAARQQLQRAQGAT 436
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  367 KPsaqqtgPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGPTKPsgqqPGPEKPLEQKQAGAS 446
Cdd:PRK07994   437 KA------KKSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKK----EPVATPKALKKALEH 506
                          170
                   ....*....|
gi 2051959432  447 QPTESVSKKT 456
Cdd:PRK07994   507 EKTPELAAKL 516
PRK10263 PRK10263
DNA translocase FtsK; Provisional
141-440 3.58e-07

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 57.02  E-value: 3.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  141 EDQKPSMMPSFLSEANPLSAVTSVVnkfnPFDLISDSDTTHEDAGRKQKV---TPKEQGKPEEQrspAKHPTQPQSPKP- 216
Cdd:PRK10263   538 EPIKSSLKAPSVAAVPPVEAAAAVS----PLASGVKKATLATGAAATVAApvfSLANSGGPRPQ---VKEGIGPQLPRPk 610
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  217 --------AVQQQGQQRPTLQQTESSKPVPQQQQQPGEPKQVQKPGHRQPADAKQEQVKQPPQPRgpQKSQPQPSEPAKP 288
Cdd:PRK10263   611 rirvptrrELASYGIKLPSQRAAEEKAREAQRNQYDSGDQYNDDEIDAMQQDELARQFAQTQQQR--YGEQYQHDVPVNA 688
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  289 VQQQTSAKL-------SSGPTKPSPQQPDSAKTTSQAP---PPTK------PSSQQPGPAKQPLQQPARQGGPVKP--SS 350
Cdd:PRK10263   689 EDADAAAEAelarqfaQTQQQRYSGEQPAGANPFSLDDfefSPMKallddgPHEPLFTPIVEPVQQPQQPVAPQQQyqQP 768
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  351 QQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSG-KPPLQQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGPT--KP 427
Cdd:PRK10263   769 QQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQyQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDTllHP 848
                          330
                   ....*....|...
gi 2051959432  428 SGQQPGPEKPLEQ 440
Cdd:PRK10263   849 LLMRNGDSRPLHK 861
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
195-442 4.26e-07

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 56.49  E-value: 4.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  195 QGKPEEQRSPAK--HPTQPQSPKPAvQQQGQQRPTLQQTESSKPVPQQQQQPGEPKQVQKPGH-----RQPADAKQEQVK 267
Cdd:pfam03157  451 QEQPGQGQQPGQgqQGQQPGQPEQG-QQPGQGQPGYYPTSPQQSGQGQQLGQWQQQGQGQPGYyptspLQPGQGQPGYYP 529
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  268 QPPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPP---TKPSSQQPGPAKQPLQQPARQGG 344
Cdd:pfam03157  530 TSPQQPGQGQQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQGQQPgqgQQPGQGQPGYYPTSPQQSGQGQQ 609
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  345 P---VKPSSQQAGPPKQLSQQPGpekpSAQQTGPAKQPPQPGSGKPPLQ-------QTGPVKQVPPQAGPTKPPSQTAGP 414
Cdd:pfam03157  610 PgqwQQPGQGQPGYYPTSSLQLG----QGQQGYYPTSPQQPGQGQQPGQwqqsgqgQQGYYPTSPQQSGQAQQPGQGQQP 685
                          250       260       270
                   ....*....|....*....|....*....|.
gi 2051959432  415 ---TKPPAQQPGPTKPSGQQPGPEKPLEQKQ 442
Cdd:pfam03157  686 gqwLQPGQGQQGYYPTSPQQPGQGQQLGQGQ 716
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
4531-4617 4.35e-07

PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], FRMPD2 (also known as PDZ domain-containing protein 4; PDZ domain-containing protein 5C), and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467180 [Multi-domain]  Cd Length: 92  Bit Score: 50.86  E-value: 4.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 4531 TRLKLLRDPKdhtvsgNGLGIRVVGGkEIPGSSgEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSi 4610
Cdd:cd06694      3 VIVTLKKDPQ------KGLGFTIVGG-ENSGSL-DLGIFVKSIIPGGPADKDGRIKPGDRIIAINGQSLEGKTHHAAVE- 73

                   ....*..
gi 2051959432 4611 IIQQSGE 4617
Cdd:cd06694     74 IIQNAPD 80
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
4546-4606 5.34e-07

PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila Dlg1, human Dlg1, 2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197; SAP-97), Dlg2 (also known as channel-associated protein of synapse-110; postsynaptic density protein 93, PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95; synapse-associated protein 90, SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling, regulating surface expression of NMDA receptors in dorsal horn neurons of the spinal cord; it interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. The Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development; postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467257 [Multi-domain]  Cd Length: 91  Bit Score: 50.43  E-value: 5.34e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051959432 4546 GNGLGIRVVGGKEipgssGEiGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEE 4606
Cdd:cd06795     11 STGLGFNIVGGED-----GE-GIFISFILAGGPADLSGELRRGDQILSVNGVDLRNATHEQ 65
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
306-428 7.63e-07

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 55.49  E-value: 7.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  306 PQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSG 385
Cdd:PRK14951   366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAV 445
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2051959432  386 K----PPLQQTGPVKQVPPQAGPtKPPSQTAGPTKPPAQQPGPTKPS 428
Cdd:PRK14951   446 AlapaPPAQAAPETVAIPVRVAP-EPAVASAAPAPAAAPAAARLTPT 491
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
4545-4620 8.46e-07

PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467176 [Multi-domain]  Cd Length: 102  Bit Score: 50.32  E-value: 8.46e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051959432 4545 SGNGLGIRVVGGKEipGSSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPL-TGKTYEEVQSIIIQQSGEAEI 4620
Cdd:cd06689     24 ESGGLGFSVVGLKS--ENRGELGIFVQEIQPGSVAARDGRLKENDQILAINGQPLdQSISHQQAIAILQQAKGSVEL 98
PHA03378 PHA03378
EBNA-3B; Provisional
290-750 1.18e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 55.07  E-value: 1.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  290 QQQTSAKLSSGPTKPSPQQPdsakTTSQAPPPTKPSSQQPGPAKQPLQQPARQ--GGPVKPSSQQAGPPKQLSQQPG--- 364
Cdd:PHA03378   431 RKKKAARTEQPRATPHSQAP----TVVLHRPPTQPLEGPTGPLSVQAPLEPWQplPHPQVTPVILHQPPAQGVQAHGsml 506
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  365 ----------------------PEKPSAQQTGPAK-------QPPQPGSGKPPLQQTGPVK-----QVPPQAGPTKP--- 407
Cdd:PHA03378   507 dllekddedmeqrvmatllppsPPQPRAGRRAPCVytedldiESDEPASTEPVHDQLLPAPglgplQIQPLTSPTTSqla 586
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  408 ---PS--QTAGPTKPPAQQPGPTKPSGQQPGPEKPLEQKQAGASQPTESVSKKTFcplcTTTELLLHTPEKANYNTCTQC 482
Cdd:PHA03378   587 ssaPSyaQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPI----TFNVLVFPTPHQPPQVEITPY 662
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  483 HTVVCSLCGFNPNPHITEISEWLCLNCQMQRALGGDLAAGHGPGPQ-PPAPKQK-----TPIPPSTAKPS----PQPQPV 552
Cdd:PHA03378   663 KPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAaPPGRAQRpaaatGRARPPAAAPGrarpPAAAPG 742
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  553 QKKDITSKPD--------PSQLADPKKPPPQKKQTPLPGSPPVKSKQPRAEPTeiSQQTRDATPKSDQVKPTQAEDKQ-- 622
Cdd:PHA03378   743 RARPPAAAPGrarppaaaPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPT--PQPPPQAGPTSMQLMPRAAPGQQgp 820
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  623 -KQPSVQKPTADTVSTSAALEQKQDLAGPRPPTQQkvtdsPKPELAKPSQDTH-PAEDKPDSKPVpQVSRQKSDPKLASQ 700
Cdd:PHA03378   821 tKQILRQLLTGGVKRGRPSLKKPAALERQAAAGPT-----PSPGSGTSDKIVQaPVFYPPVLQPI-QVMRQLGSVRAAAA 894
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2051959432  701 PGArPDAKAQKPVEPTQTKD-DPKKLPTKPAPKPDTKAAPKGPQAGAGPKP 750
Cdd:PHA03378   895 STV-TQAPTEYTGERRGVGPmHPTDIPPSKRAKTDAYVESQPPHGGQSHSF 944
PRK10263 PRK10263
DNA translocase FtsK; Provisional
188-714 1.22e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 55.09  E-value: 1.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  188 QKVTPKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGQ-QRP---------TLQQTESSKPVPQQQQQPGEPKQVQKPGHRQ 257
Cdd:PRK10263   361 QPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPlQQPvqpqqpyyaPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQ 440
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  258 PADAKQEQVKQPPQPRGPQKSQ------PQPSEPAKPVQQQTSAklssgPTKPSPQQPDSAKTTSQAPPPT--------- 322
Cdd:PRK10263   441 PVAGNAWQAEEQQSTFAPQSTYqteqtyQQPAAQEPLYQQPQPV-----EQQPVVEPEPVVEETKPARPPLyyfeeveek 515
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  323 -KPSSQQPGPAKQPLQQPARQGGPVKPS----SQQAGPPKQLSQQPGPEKPSAQQ----TGPAKQPPQPGSGkpPLQQTG 393
Cdd:PRK10263   516 rAREREQLAAWYQPIPEPVKEPEPIKSSlkapSVAAVPPVEAAAAVSPLASGVKKatlaTGAAATVAAPVFS--LANSGG 593
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  394 PVKQVPPQAGPTKP-PSQTAGPTKPPAQQPGPTKPSgQQPGPEKPLE----QKQAGASQPTESVSKktfcplctttellL 468
Cdd:PRK10263   594 PRPQVKEGIGPQLPrPKRIRVPTRRELASYGIKLPS-QRAAEEKAREaqrnQYDSGDQYNDDEIDA-------------M 659
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  469 HTPEKANYNTCTQCHTVVCSLCgfNPNPHITEISEwlclnCQMQRALGGDLAAGHGPGPQPPAPKQKTPIPPSTAKPSPq 548
Cdd:PRK10263   660 QQDELARQFAQTQQQRYGEQYQ--HDVPVNAEDAD-----AAAEAELARQFAQTQQQRYSGEQPAGANPFSLDDFEFSP- 731
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  549 pqpvQKKDITSKPDPSQLADPKKPPPQKKQTPLPGSPPVKSKQPRAEPTEISQQTRDATPKSDQVKPTQAEDKQKQPS-V 627
Cdd:PRK10263   732 ----MKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQqP 807
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  628 QKPTAdtvsTSAALEQKQDLAGPRPPTQQkvtdsPKPELAKPSQDT--HPAEDKP-DSKPVpqvsrQKSDPKLASQPGAR 704
Cdd:PRK10263   808 QQPVA----PQPQYQQPQQPVAPQPQYQQ-----PQQPVAPQPQDTllHPLLMRNgDSRPL-----HKPTTPLPSLDLLT 873
                          570
                   ....*....|
gi 2051959432  705 PDAKAQKPVE 714
Cdd:PRK10263   874 PPPSEVEPVD 883
PHA03269 PHA03269
envelope glycoprotein C; Provisional
304-434 1.35e-06

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 54.73  E-value: 1.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  304 PSPQQPDSAKT--TSQAPPPTKPSSQQPGPAKQPLQQPARqggpvKPSSQQAgPPKQLSQQPGPEKPSAQQtgpAKQPPQ 381
Cdd:PHA03269    27 PIPELHTSAATqkPDPAPAPHQAASRAPDPAVAPTSAASR-----KPDLAQA-PTPAASEKFDPAPAPHQA---ASRAPD 97
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2051959432  382 PGSGKPPLQQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGPTKPSGQQPGP 434
Cdd:PHA03269    98 PAVAPQLAAAPKPDAAEAFTSAAQAHEAPADAGTSAASKKPDPAAHTQHSPPP 150
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
251-769 1.49e-06

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 54.57  E-value: 1.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  251 QKPGH-RQPADAKQEQVKQPPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKP-SSQQ 328
Cdd:pfam03157  129 QRPGQgQQPGQGQQWYYPTSPQQPGQWQQPGQGQQGYYPTSPQQSGQRQQPGQGQQLRQGQQGQQSGQGQPGYYPtSSQQ 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  329 PGPakqpLQQPARQGGPVKPSSQQAGppkqlsQQPGPEkpsaQQTGPAKQPPQPGSGkpplQQTGPVKQVPPQAGPTKPP 408
Cdd:pfam03157  209 PGQ----LQQTGQGQQGQQPERGQQG------QQPGQG----QQPGQGQQGQQPGQP----QQLGQGQQGYYPISPQQPR 270
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  409 SQTAGPTKPPAQQPGPTKPSGQQPGPEKPLEQKQAGASQPTESVSKKTFCPLCTTTELLLHTPEKANYNTCTQchtvvcs 488
Cdd:pfam03157  271 QWQQSGQGQQGYYPTSLQQPGQGQSGYYPTSQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQPGQGQQGQQPAQ------- 343
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  489 lcGFNPnphiteisewlclncqmqralgGDLAAGHGP-GPQPPAPKQKTPIPPSTAKPSPQPQPVQKKDITSKPDPSQLA 567
Cdd:pfam03157  344 --GQQP----------------------GQGQPGYYPtSPQQPGQGQPGYYPTSQQQPQQGQQPEQGQQGQQQGQGQQGQ 399
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  568 DPKKPPPQKKQTP--LPGSPPVKSK-QPRAEPTEISQQTRDATPKSDQVKPTQAEDKQKQPSVQKPTADTVSTSAALEQK 644
Cdd:pfam03157  400 QPGQGQQPGQGQPgyYPTSPQQSGQgQPGYYPTSPQQSGQGQQPGQGQQPGQEQPGQGQQPGQGQQGQQPGQPEQGQQPG 479
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  645 QDLAGPRPPTQQKVTDSPKPELAKPSQDTHPAEdKPDSKPVPQVSRQKSDPKLASQPG-ARPDAKAQKPVEPTQTKDDPK 723
Cdd:pfam03157  480 QGQPGYYPTSPQQSGQGQQLGQWQQQGQGQPGY-YPTSPLQPGQGQPGYYPTSPQQPGqGQQLGQLQQPTQGQQGQQSGQ 558
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 2051959432  724 KLPTKPAPKPDTKAAPKGPQAGAGPKPGPAQPAPQPQPPQKTPEQS 769
Cdd:pfam03157  559 GQQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQS 604
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
253-620 1.96e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 54.22  E-value: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  253 PGHRQPADAKQEQVKQPPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPA 332
Cdd:PRK07764   394 PAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAA 473
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  333 KQPLQQPARQGGPVKPSSQQAGPPKQLSQQPGPE---------------------------KPSAQQTGPAKQPPQPGSG 385
Cdd:PRK07764   474 PEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADdaatlrerwpeilaavpkrsrktwailLPEATVLGVRGDTLVLGFS 553
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  386 KPPL------------------QQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGPT----KPSGQQPGPEKPLEQKQA 443
Cdd:PRK07764   554 TGGLarrfaspgnaevlvtalaEELGGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEaarpAAPAAPAAPAAPAPAGAA 633
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  444 GASQPTESVSKKTFCPLCTTTELLLHTPEKANyntctqchtvvcslcgfnpnphiteISEWlclncqmQRALGGDLAAGH 523
Cdd:PRK07764   634 AAPAEASAAPAPGVAAPEHHPKHVAVPDASDG-------------------------GDGW-------PAKAGGAAPAAP 681
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  524 GPGPQPPAPKQKTPIPPS--TAKPSPQPQPVQKKDITSKPDPSQLADPKKPPPQKKQTPLPGSP---PVKSKQPRAEPTE 598
Cdd:PRK07764   682 PPAPAPAAPAAPAGAAPAqpAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPddpPDPAGAPAQPPPP 761
                          410       420
                   ....*....|....*....|..
gi 2051959432  599 ISQQTRDATPKSDQVKPTQAED 620
Cdd:PRK07764   762 PAPAPAAAPAAAPPPSPPSEEE 783
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
4546-4616 2.08e-06

PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467155 [Multi-domain]  Cd Length: 80  Bit Score: 48.43  E-value: 2.08e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051959432 4546 GNGLGIRVVGGKeipgSSGEIgayIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSiIIQQSG 4616
Cdd:cd06667      9 GSGLGFGIVGGK----STGVV---VKTILPGGVADRDGRLRSGDHILQIGDTNLRGMGSEQVAQ-VLRQCG 71
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
274-742 2.11e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 54.39  E-value: 2.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  274 GPQKSQPQPSEPAKPVQQQTSaklSSGPTKPSPQQPDSakTTSQAPPPTKPSSQQPGPAKQPLQQPARQ----------- 342
Cdd:pfam03154   20 GRKKQTASPDGRASPTNEDLR---SSGRNSPSAASTSS--NDSKAESMKKSSKKIKEEAPSPLKSAKRQrekgasdteep 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  343 -------------GGPVKPSSQQ-------------AGPPKQLSQQ--------PGPE------KPSAQQTGPAKQPPQP 382
Cdd:pfam03154   95 eratakksktqeiSRPNSPSEGEgessdgrsvndegSSDPKDIDQDnrstspsiPSPQdnesdsDSSAQQQILQTQPPVL 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  383 GSGKPPLQQTGPVKQVPPQAGPTKPPSQTagPTKPPAQQPGPTKPSGQQPGPEKPLEQKQAGASQPTESVSKktfcPLCT 462
Cdd:pfam03154  175 QAQSGAASPPSPPPPGTTQAATAGPTPSA--PSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPS----PHPP 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  463 TTELllhTPEKANYNTCTQCHTVVCSLCGFNPNPHITEISEWLCLNCQMQRALGGDLAAGHGPGPQPPAPKQKTPIPPST 542
Cdd:pfam03154  249 LQPM---TQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRI 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  543 AKPSPQPQPVQKKDITSKPDPSQLAdPKKPPPQKKQTPLPGSP-PVKSKQPRAEPTEISQQTRDATPKSDQVKPTQAEDK 621
Cdd:pfam03154  326 HTPPSQSQLQSQQPPREQPLPPAPL-SMPHIKPPPTTPIPQLPnPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLST 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  622 QKQPSVQKPTADTVSTSAALeqkqdlagPRPPTQ-----QKVTDSPKPELAKPSQDTHPAedkPDSKPVPQVSRQKSDPK 696
Cdd:pfam03154  405 HHPPSAHPPPLQLMPQSQQL--------PPPPAQppvltQSQSLPPPAASHPPTSGLHQV---PSQSPFPQHPFVPGGPP 473
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  697 L------------ASQPGARPDAKAQK------------PVEPTQTKDDPKKLPTKPAPKPDTKAAPKGP 742
Cdd:pfam03154  474 PitppsgpptstsSAMPGIQPPSSASVsssgpvpaavscPLPPVQIKEEALDEAEEPESPPPPPRSPSPE 543
PHA03247 PHA03247
large tegument protein UL36; Provisional
518-1030 2.35e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 2.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  518 DLAAGHGPGPQPPAPKQKTPIPPSTAKPSPQPQP------VQKKDitSKPD-PSQLA-------DPKKPPPQKKQTPLP- 582
Cdd:PHA03247  2542 ELASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPrpsepaVTSRA--RRPDaPPQSArprapvdDRGDPRGPAPPSPLPp 2619
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  583 --GSPPVKSKQPRAEPTEISQQTRDATPKSDQVKPTQAEDKQKQPSVQKPTADTVSTSAALEqkqdlaGPRPPTQQKvTD 660
Cdd:PHA03247  2620 dtHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQ------RPRRRAARP-TV 2692
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  661 SPKPELAKPsqdtHPAEDKPDSKPVPQVSRQKSDPKLASQPGARPDAKAQkPVEP-----TQTKDDPKKLPTKPAPK-PD 734
Cdd:PHA03247  2693 GSLTSLADP----PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAA-PAPPavpagPATPGGPARPARPPTTAgPP 2767
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  735 TKAAPKGPQAGAGPKPGPAQPAPQPQPPQKTPEQS-----------RRFSLNLGGITDAPKPQPTTPQETVTGKlfgfgA 803
Cdd:PHA03247  2768 APAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWdpadppaavlaPAAALPPAASPAGPLPPPTSAQPTAPPP-----P 2842
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  804 SFFSQASNLISTAGQPGSQTSgappaakqpqpppqppapqtapketgqaqppPKVVPVKKEAKPLTTEKSEPSKVdsvlt 883
Cdd:PHA03247  2843 PGPPPPSLPLGGSVAPGGDVR-------------------------------RRPPSRSPAAKPAAPARPPVRRL----- 2886
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  884 kgsdleKKPGLAKDSKPQAAEAKKPDGLLEPDKASQPEMSCPLCKTGLNIGSKDPPNfntcteckkvvcnlcgfNPMPHI 963
Cdd:PHA03247  2887 ------ARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP-----------------RPQPPL 2943
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051959432  964 AEVQEWLCLNCQTQRAMSGQLGDM--GKVPLPKTGPSQPTSKPPAPPQKQPMPAVSHSPQKTSTPPTLA 1030
Cdd:PHA03247  2944 APTTDPAGAGEPSGAVPQPWLGALvpGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLA 3012
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
4548-4605 2.39e-06

PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Lin-7 (also known as LIN-7 or LIN7), and related domains. Lin-7 targets and organize protein complexes to epithelial and synaptic plasma membranes. There are three mammalian Lin-7 homologs: Lin-7A (protein lin-7 homolog A, also known as mammalian lin-seven protein 1 (MALS-1), vertebrate lin-7 homolog 1 (Veli-1), tax interaction protein 33); Lin-7B (also known as MALS-2, Veli-2); and Lin-7C (also known as MALS-3, Veli-3). Lin-7 is involved in localization of the Let-23 growth factor receptor to the basolateral membrane of epithelial cells, in tight junction localization of insulin receptor substrate p53 (IRSp53), in retaining gamma-aminobutyric (GABA) transporter (BGT-1) at the basolateral surface of epithelial cells, and in regulating recruitment of neurotransmitter receptors to the postsynaptic density (PSD). The Lin7 PDZ domain binds Let-23, BGT and beta-catenin, and NMDA (N-methyl-D-aspartate) receptor NR2B. Lin-7 also binds to the PDZ binding motif located in the C-terminal tail of Rhotekin, an effector protein for small GTPase Rho. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Lin-7-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467258 [Multi-domain]  Cd Length: 86  Bit Score: 48.59  E-value: 2.39e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2051959432 4548 GLGIRVVGGKEipgSSGEIgaYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYE 4605
Cdd:cd06796     13 GLGFNVMGGKE---QNSPI--YISRIIPGGVADRHGGLKRGDQLLSVNGVSVEGEHHE 65
Androgen_recep pfam02166
Androgen receptor;
250-417 2.66e-06

Androgen receptor;


Pssm-ID: 426632 [Multi-domain]  Cd Length: 501  Bit Score: 53.39  E-value: 2.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  250 VQKPGHRQPADAKQeqvKQPPQPRGPQKSQPQPSEPAKPVQQQTSaklssgptkpsPQQPDSAKTTSQAPPPTKPSSQQP 329
Cdd:pfam02166   29 IQNPGPRHPEAAGG---AAPPGARLQHQQQQQQQVPQQPQQQESS-----------PRQPQASVQPQQAGDDGSPPAHNR 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  330 GPAKQPLQQPARQGGPVKPSSQQAGPPkqlsqqpgpekpsaqQTGPAKQPPQPGSGKPPLQQTGpVKQVPPQAGPTKPPS 409
Cdd:pfam02166   95 GPAGYLALEDDEQPQPSQAQPAAECCP---------------ENGCVPEPGAAAAAGKGLPQQA-VAPAAPDDDDSAAPS 158
                          170
                   ....*....|
gi 2051959432  410 QTA--GPTKP 417
Cdd:pfam02166  159 TLSllGPSFP 168
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
4546-4607 2.83e-06

PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467185 [Multi-domain]  Cd Length: 98  Bit Score: 48.76  E-value: 2.83e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2051959432 4546 GNGLGIRVVGGkeIPGSSG------EIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEV 4607
Cdd:cd06701     14 GEKLGISIRGG--AKGHAGnpldptDEGIFISKINPDGAAARDGRLKVGQRILEVNGQSLLGATHQEA 79
PDZ_MPP3-MPP4-MPP7-like cd06799
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ...
4551-4616 2.83e-06

PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP3, MPP4, and MPP7, and related domains. MPP3 (also known as MAGUK p55 subfamily member 3, erythrocyte membrane protein p55, or EMP55), MPP4 (also known as MAGUK p55 subfamily member 4 or Discs large homolog 6), and MPP7 (also known as MAGUK p55 subfamily member 7) are membrane-associated guanylate kinase (MAGUK)-like proteins. MPP3 is part of a cell adhesion protein complex including tumor suppressor CADM1 and actin-binding protein 4.1B. Participation in the Crumbs cell polarity complex has also been demonstrated for MPP7 in epithelial cells, and for MPP3 and MPP4 in the retina. MPP4 is needed for proper localization of plasma membrane calcium ATPases and maintenance of calcium homeostasis at the rod photoreceptor synaptic terminals. Binding partners of the MPP3 PDZ domain include nectin-3, serotonin 5-hydroxytryptamine, 5-HT(2C) receptor, and a cell adhesion protein, TSLC1 (tumor suppressor in lung cancer 1); fragments of MPP4 having the PDZ domain bind CRB (PDZ-SH3-GUK) and GABA transporter GAT1 (PDZ-SH3). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467260 [Multi-domain]  Cd Length: 81  Bit Score: 48.01  E-value: 2.83e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051959432 4551 IRVVGGKEIPGS-------SGEIgaYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSIIIQQSG 4616
Cdd:cd06799      3 VRLVKNNEPLGAtikrdekTGAI--VVARIMRGGAADRSGLIHVGDELREVNGISVEGKDPEEVIQILANSQG 73
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
4546-4607 2.86e-06

PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNJ2BP, and related domains. SYNJ2BP (also known as mitochondrial outer membrane protein 25, OMP25) regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. Binding partners of the SYNJ2BP PDZ domain include activin type II receptors (ActR-II), and SYNJ2. SYNJ2BP interacts with the PDZ binding motif of the Notch Delta-like ligand 1 (DLL1) and DLL4, promoting Delta-Notch signaling, and inhibiting sprouting angiogenesis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNJ2BP-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467193 [Multi-domain]  Cd Length: 86  Bit Score: 48.06  E-value: 2.86e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432 4546 GNGLGIRVVGGKEIPGSSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEV 4607
Cdd:cd06709      9 PSGLGFNIVGGTDQPYIPNDSGIYVAKIKEDGAAAIDGRLQEGDKILEINGQSLENLTHQDA 70
dnaA PRK14086
chromosomal replication initiator protein DnaA;
275-436 3.02e-06

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 53.68  E-value: 3.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  275 PQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARQGgPVKPSSQQAG 354
Cdd:PRK14086    68 PIISETLSRELGRPIRIAITVDPSAGEPAPPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQ-DQLPTARPAY 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  355 PPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPPlqqTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGPTKPSGQQPGP 434
Cdd:PRK14086   147 PAYQQRPEPGAWPRAADDYGWQQQRLGFPPRAPY---ASPASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWDRPRR 223

                   ..
gi 2051959432  435 EK 436
Cdd:PRK14086   224 DR 225
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
4535-4616 3.12e-06

PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight junction (PATJ, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 12 of MUPP1, PDZ domain 10 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like PDZ12 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467163 [Multi-domain]  Cd Length: 86  Bit Score: 48.13  E-value: 3.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 4535 LLRDPKDhtvsgnGLGIRVVGGKeipGSS-GEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSIIIQ 4613
Cdd:cd06675      5 IKRGPQD------SLGISIAGGV---GSPlGDVPVFIAMIQPNGVAAQTGKLKVGDRIVSINGQSTDGLTHSEAVNLLKN 75

                   ...
gi 2051959432 4614 QSG 4616
Cdd:cd06675     76 ASG 78
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
270-460 3.44e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 53.70  E-value: 3.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  270 PQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAkttSQAPPPTKPSSQQPGPAKQPLQQ-----PARQGG 344
Cdd:PRK07003   412 PKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKAN---ARASADSRCDERDAQPPADSGSAsapasDAPPDA 488
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  345 PVKPSSQQAGPPKQLSQQPG-PEKPSAQQTG----------PAKQPPQPGSGKPPLQQTGPVKQV--------------- 398
Cdd:PRK07003   489 AFEPAPRAAAPSAATPAAVPdARAPAAASREdapaaaappaPEARPPTPAAAAPAARAGGAAAALdvlrnagmrvssdrg 568
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432  399 PPQAGPTKPPSQTAGPTKPPAQQP--------GPTKPSGQQPGPEKPLEQKQA--GASQPTESVSKKTFCPL 460
Cdd:PRK07003   569 ARAAAAAKPAAAPAAAPKPAAPRVavqvptprARAATGDAPPNGAARAEQAAEsrGAPPPWEDIPPDDYVPL 640
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
274-716 3.58e-06

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 53.38  E-value: 3.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  274 GPQKSQPQPSEPAKPVQqqTSAKLSSGPTKPSPQ--QPDSAKTTSQAPPPTkpssqqPGPAKQPLQQPARQGGPVKPSSQ 351
Cdd:pfam05109  441 APNTTTGLPSSTHVPTN--LTAPASTGPTVSTADvtSPTPAGTTSGASPVT------PSPSPRDNGTESKAPDMTSPTSA 512
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  352 QAGPpkqlsqqpgpeKPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQV-PPQAGPTKPPSQTAGPTkPPAQQP--GPTKPS 428
Cdd:pfam05109  513 VTTP-----------TPNATSPTPAVTTPTPNATSPTLGKTSPTSAVtTPTPNATSPTPAVTTPT-PNATIPtlGKTSPT 580
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  429 GQQPGPEKPLEQKQAGASQPTESVSKKTFCPlCTTTELLLHTPEKANYNTCTQCHTVV-CSLCGFNPNPhiTEISEWLCL 507
Cdd:pfam05109  581 SAVTTPTPNATSPTVGETSPQANTTNHTLGG-TSSTPVVTSPPKNATSAVTTGQHNITsSSTSSMSLRP--SSISETLSP 657
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  508 NCQmqralggDLAAGHGP---GPQPPAPKQKTPIPP--------STAKPSPQPQPVQKkdiTSKPDPSQLADPKKPPPQK 576
Cdd:pfam05109  658 STS-------DNSTSHMPlltSAHPTGGENITQVTPaststhhvSTSSPAPRPGTTSQ---ASGPGNSSTSTKPGEVNVT 727
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  577 KqtplpGSPPVKSKQPRAepteisqqtrdatpksdqvkptqaedkqkqPSVQKPTADTVSTSAAleQKQDLAGPRPPTQQ 656
Cdd:pfam05109  728 K-----GTPPKNATSPQA------------------------------PSGQKTAVPTVTSTGG--KANSTTGGKHTTGH 770
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  657 KVTDSPKPELAKPSQDTHPAEDKPDSKPVPQVSRQKSDPKLASQPGARPDAKAQKPVEPT 716
Cdd:pfam05109  771 GARTSTEPTTDYGGDSTTPRTRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPT 830
PHA03418 PHA03418
hypothetical E4 protein; Provisional
253-424 3.68e-06

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 51.28  E-value: 3.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  253 PGHRQPADAKQEQVKQPPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSakttSQAPPPTKPS-SQQPGP 331
Cdd:PHA03418    39 PHHPNPQEDPDKNPSPPPDPPLTPRPPAQPNGHNKPPVTKQPGGEGTEEDHQAPLAADA----DDDPRPGKRSkADEHGP 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  332 AkqplqqPAR-QGGPVKPSSQQAGPpkqlsqQPGPEKPSAQQTGPAKQPPQPG--SGKPPLQQTGPVKQVPPqagptkPP 408
Cdd:PHA03418   115 A------PGRaALAPFKLDLDQDPL------HGDPDPPPGATGGQGEEPPEGGeeSQPPLGEGEGAVEGHPP------PL 176
                          170
                   ....*....|....*.
gi 2051959432  409 sqtagptkPPAQQPGP 424
Cdd:PHA03418   177 --------PPAPEPKP 184
PDZ3_PTPN13_FRMPD2-like cd06695
PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ ...
4545-4623 4.40e-06

PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], FRMPD2 (also known as PDZ domain-containing protein 4; PDZ domain-containing protein 5C), and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 PDZ domains). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467181 [Multi-domain]  Cd Length: 90  Bit Score: 47.64  E-value: 4.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 4545 SGNGLGIRVVGGK-EIPGSSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSIIIQQSGEAE--IC 4621
Cdd:cd06695      9 GSSGLGFSFLGGEnNSPEDPFSGLVRIKKLFPGQPAAESGLIQEGDVILAVNGEPLKGLSYQEVLSLLRGAPPEVTllLC 88

                   ..
gi 2051959432 4622 GP 4623
Cdd:cd06695     89 RP 90
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
4533-4606 4.62e-06

PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Dlg1, human Dlg1,2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197 or SAP-97), Dlg2 (also known as channel-associated protein of synapse-110, postsynaptic density protein 93, or PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95, synapse-associated protein 90, or SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling. It regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord, and it also interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467207 [Multi-domain]  Cd Length: 85  Bit Score: 47.65  E-value: 4.62e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051959432 4533 LKLLRDPKdhtvsgnGLGIRVVGGK---EIPGSSGeigAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEE 4606
Cdd:cd06724      2 IKLVKGPK-------GLGFSIAGGVgnqHIPGDNG---IYVTKIIEGGAAQKDGRLQVGDKLLAVNDVSLEEVTHEE 68
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
175-442 5.22e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 53.15  E-value: 5.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  175 SDSDTTHEDAgrKQKVTPKEQGKPEEQRS--------------PAKHPTQPQSPKPAVQQQGQQRPtlQQTESSKpvpqq 240
Cdd:PTZ00449   528 EGEEGEHEDS--KESDEPKEGGKPGETKEgevgkkpgpakehkPSKIPTLSKKPEFPKDPKHPKDP--EEPKKPK----- 598
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  241 qQQPGEPKQVQKPGHRQPADAK-QEQVKQPPQPRGPqKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQP---------- 309
Cdd:PTZ00449   599 -RPRSAQRPTRPKSPKLPELLDiPKSPKRPESPKSP-KRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPfdpkfkekfy 676
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  310 DSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSgkPPL 389
Cdd:PTZ00449   677 DDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFT--PPE 754
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051959432  390 QQTGPVKQVP---PQAGPT----KPP---SQTAGPTKPPAQQPGPTKPSGQQPG--PEKPLEQKQ 442
Cdd:PTZ00449   755 EERTFFHETPadtPLPDILaeefKEEdihAETGEPDEAMKRPDSPSEHEDKPPGdhPSLPKKRHR 819
PDZ2_DLG5-like cd06765
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
4551-4611 5.55e-06

PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PSZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467246 [Multi-domain]  Cd Length: 77  Bit Score: 46.96  E-value: 5.55e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051959432 4551 IRVVGGKEiPGSSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSII 4611
Cdd:cd06765      2 INLSGQKD-SGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEALL 61
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
182-372 6.61e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 52.68  E-value: 6.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  182 EDAGRKQKVTPKEQGKPEEQRSPAK--HPTQPQSPKPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPKqvqkPGHRQPA 259
Cdd:PRK07764   599 GPPAPASSGPPEEAARPAAPAAPAApaAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD----GWPAKAG 674
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  260 DAKQEQVKQPPQPRGPQKSQPQPsePAKPVQQQTSAKLSSGPTKPSPQQPDSAktTSQAPPPTKPSSQQPGPAKQPLQQP 339
Cdd:PRK07764   675 GAAPAAPPPAPAPAAPAAPAGAA--PAQPAPAPAATPPAGQADDPAAQPPQAA--QGASAPSPAADDPVPLPPEPDDPPD 750
                          170       180       190
                   ....*....|....*....|....*....|...
gi 2051959432  340 ARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQ 372
Cdd:PRK07764   751 PAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
PHA03377 PHA03377
EBNA-3C; Provisional
202-737 6.71e-06

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 52.75  E-value: 6.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  202 RSPAKHPTQPQSPKPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPKQVQKPGHRQPADAKQEQVKQPPQPRGPQKSQPQ 281
Cdd:PHA03377   414 RKPRTLPWPTPKTHPVKRTLVKTSGRSDEAEQAQSTPERPGPSDQPSVPVEPAHLTPVEHTTVILHQPPQSPPTVAIKPA 493
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  282 PSEPAKP----------------VQQQTSAKLSSGPTKPSPQQPDSAKTTSQ-----APPPTKPSSQQPGPAKQPLQQPA 340
Cdd:PHA03377   494 PPPSRRRrgacvvydddiievidVETTEEEESVTQPAKPHRKVQDGFQRSGRrqkraTPPKVSPSDRGPPKASPPVMAPP 573
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  341 RQG----GPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGP-AKQPPQ--PGSGKPPLQQTGPVKQVPPQAGPTKPPS---- 409
Cdd:PHA03377   574 STGprvmATPSTGPRDMAPPSTGPRQQAKCKDGPPASGPhEKQPPSsaPRDMAPSVVRMFLRERLLEQSTGPKPKSfwem 653
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  410 ----QTAGPTKPPAQQPGPTkpsgQQPGPEKP--------LEQKQAGASQPTESVSKKTFCPLCTTTELLLHTPEKANYN 477
Cdd:PHA03377   654 ragrDGSGIQQEPSSRRQPA----TQSTPPRPswlpsvfvLPSVDAGRAQPSEESHLSSMSPTQPISHEEQPRYEDPDDP 729
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  478 TCTQCHTVVCSLcgfnPNPHiteisewlclncqmqralggDLAAGHG--PGPQPPAPKQKTPIPPSTAKPSPQPQPVQKK 555
Cdd:PHA03377   730 LDLSLHPDQAPP----PSHQ--------------------APYSGHEepQAQQAPYPGYWEPRPPQAPYLGYQEPQAQGV 785
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  556 DITSKPDPSqladpkkpppqkkqtplpGSPPVKSKQPRaepteiSQQTRDATPKSDQVKPTQAEDKQKQPSVqKPTADTV 635
Cdd:PHA03377   786 QVSSYPGYA------------------GPWGLRAQHPR------YRHSWAYWSQYPGHGHPQGPWAPRPPHL-PPQWDGS 840
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  636 STSAaleqkQDLAGPRPPTQQKvTDSPKPELAKPSQDTHPaeDKPDSKPVPqvsrqksdPKLASQPGArpdakaqkPVEP 715
Cdd:PHA03377   841 AGHG-----QDQVSQFPHLQSE-TGPPRLQLSQVPQLPYS--QTLVSSSAP--------SWSSPQPRA--------PIRP 896
                          570       580
                   ....*....|....*....|..
gi 2051959432  716 TqtkddPKKLPTKPAPKPDTKA 737
Cdd:PHA03377   897 I-----PTRFPPPPMPLQDSMA 913
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
265-404 7.69e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 52.09  E-value: 7.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  265 QVKQPPQPRGPQKSQPQPSEPAKP-VQQQTSAKLSSGPTKPSPQQPdsakTTSQAPPPTKPSSQQPgPAKQPLQQPARQG 343
Cdd:PRK14971   358 QLAQLTQKGDDASGGRGPKQHIKPvFTQPAAAPQPSAAAAASPSPS----QSSAAAQPSAPQSATQ-PAGTPPTVSVDPP 432
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432  344 GPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPPLQQ-TGPVKQVPPQAGP 404
Cdd:PRK14971   433 AAVPVNPPSTAPQAVRPAQFKEEKKIPVSKVSSLGPSTLRPIQEKAEQaTGNIKEAPTGTQK 494
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
4542-4617 7.79e-06

PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2) and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467166 [Multi-domain]  Cd Length: 82  Bit Score: 46.86  E-value: 7.79e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051959432 4542 HTVSGNGLGIRVVGGKEIPGssgeigAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSiIIQQSGE 4617
Cdd:cd06678      6 NKRDGEQLGIKLVRKKDEPG------VFILDLLEGGLAARDGRLKSDDRVLAINGQDLRHGTPEQAAQ-IIQASGE 74
PDZ13_MUPP1-like cd06676
PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
4548-4616 7.80e-06

PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 13 of MUPP1. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, PDZ9, and PDZ13. This MuPP1-like PDZ13 domain is therefore absent from PATJ. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ13 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467164 [Multi-domain]  Cd Length: 83  Bit Score: 46.95  E-value: 7.80e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051959432 4548 GLGIRVVGGKEIPgsSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSIIIQQSG 4616
Cdd:cd06676     10 GLGFSIVGGFGSP--HGDLPIYVKTVFEKGAAAEDGRLKRGDQILAVNGESLEGVTHEEAVNILKKTKG 76
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
67-451 9.53e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 52.08  E-value: 9.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432   67 PRGNLAGAEPPPMQRHPELDSSRHPRQPGKPPdpgppglsksrtvdvlkteQRAPGRSpsslslresksrtdfkedQKPS 146
Cdd:pfam03154  177 QSGAASPPSPPPPGTTQAATAGPTPSAPSVPP-------------------QGSPATS------------------QPPN 219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  147 MMPSFLSeanplsavtsvvnkfnPFDLISDSDTTHedagrkqkvtpkeqgkpeEQRSPAKHPTQPQSPKPAVQQQGQQRP 226
Cdd:pfam03154  220 QTQSTAA----------------PHTLIQQTPTLH------------------PQRLPSPHPPLQPMTQPPPPSQVSPQP 265
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  227 TLQQTESSKPVPQQQQQPGEPKQVQKPGHRQP----ADAKQEQVKQPPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPT 302
Cdd:pfam03154  266 LPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPfpltPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPL 345
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  303 KPSPQQPDSAKttsqaPPPTKPSSQQPGPakQPLQQPARQGGPVKPSSQQAGPP----KQLSQQPGPEKPSAQ----QTG 374
Cdd:pfam03154  346 PPAPLSMPHIK-----PPPTTPIPQLPNP--QSHKHPPHLSGPSPFQMNSNLPPppalKPLSSLSTHHPPSAHppplQLM 418
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  375 PAKQPPQPGSGKPP-LQQT----GPVKQVPPQAGPTKPPSQTAGPTKP--PAQQPGPTKPSGQQPGPEKPLEQKQAGASQ 447
Cdd:pfam03154  419 PQSQQLPPPPAQPPvLTQSqslpPPAASHPPTSGLHQVPSQSPFPQHPfvPGGPPPITPPSGPPTSTSSAMPGIQPPSSA 498

                   ....
gi 2051959432  448 PTES 451
Cdd:pfam03154  499 SVSS 502
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
516-750 1.06e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 52.16  E-value: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  516 GGDLAAGHGPGPQP---PAPKQKTPI----------PPSTAKPS--PQPQPVQKKDITSKPDPSQlADPKKPPPQKKQTP 580
Cdd:PRK07003   364 GGGAPGGGVPARVAgavPAPGARAAAavgasavpavTAVTGAAGaaLAPKAAAAAAATRAEAPPA-APAPPATADRGDDA 442
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  581 LPGSPPVKSKQPRAEPTEISQQTRDATPKSDQVK-----PTQAEDKQKQPSvqkPTADTVSTSAALEQKQ--DLAGPRPP 653
Cdd:PRK07003   443 ADGDAPVPAKANARASADSRCDERDAQPPADSGSasapaSDAPPDAAFEPA---PRAAAPSAATPAAVPDarAPAAASRE 519
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  654 TQQKVTDSPKPELAKPSqdthPAEDKPDSKP-----VPQVSRQkSDPKLASQPGARPDAKAQKPVEPTQTKDDPKKLPTK 728
Cdd:PRK07003   520 DAPAAAAPPAPEARPPT----PAAAAPAARAggaaaALDVLRN-AGMRVSSDRGARAAAAAKPAAAPAAAPKPAAPRVAV 594
                          250       260
                   ....*....|....*....|...
gi 2051959432  729 PAPKPDTKA-APKGPQAGAGPKP 750
Cdd:PRK07003   595 QVPTPRARAaTGDAPPNGAARAE 617
PRK14948 PRK14948
DNA polymerase III subunit gamma/tau;
257-428 1.11e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237862 [Multi-domain]  Cd Length: 620  Bit Score: 51.89  E-value: 1.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  257 QPADAKQEQVKQPPQPRGPQKSQPQPSEPAKPVQQ-QTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQ- 334
Cdd:PRK14948   366 SEIANASAPANPTPAPNPSPPPAPIQPSAPKTKQAaTTPSPPPAKASPPIPVPAEPTEPSPTPPANAANAPPSLNLEELw 445
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  335 -----PLQQPARQ--------------------------------------------GGPVKP--SSQQAGPPKQLSQQP 363
Cdd:PRK14948   446 qqilaKLELPSTRmllsqqaelvsldsnraviavspnwlgmvqsrkplleqafakvlGRSIKLnlESQSGSASNTAKTPP 525
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051959432  364 GPEKPSAQQ--TGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGPTKPS 428
Cdd:PRK14948   526 PPQKSPPPPapTPPLPQPTATAPPPTPPPPPPTATQASSNAPAQIPADSSPPPPIPEEPTPSPTKDS 592
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
4540-4611 1.23e-05

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 46.12  E-value: 1.23e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432 4540 KDHTVSGNGLGIRVVGGkeipGSSGEIGAYIAKILPGGNAEQTGkLIEGMQVLEWNGIPLTGKTYEEVQSII 4611
Cdd:pfam00595    3 TLEKDGRGGLGFSLKGG----SDQGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLAL 69
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
511-787 1.25e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.10  E-value: 1.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  511 MQRALGGDLAAGHGPGPQPPAPKQKTPIPPSTA-----------KPSPQPQPVQKKDITSKPD-------PSQLADPKKP 572
Cdd:PHA03307    99 SPAREGSPTPPGPSSPDPPPPTPPPASPPPSPApdlsemlrpvgSPGPPPAASPPAAGASPAAvasdaasSRQAALPLSS 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  573 PPQKKQTPLPGSPPVKSKQPRAEPT--------EISQQTRDATPKS--DQVKPTQAEDKQKQPSVQKPTADTVSTSAALE 642
Cdd:PHA03307   179 PEETARAPSSPPAEPPPSTPPAAASprpprrssPISASASSPAPAPgrSAADDAGASSSDSSSSESSGCGWGPENECPLP 258
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  643 QKQDLAGPRPPTQQKVTDSPKPELAKPSQDTHPAEDKPDSKPV-----PQVSRQKSDPKLASQPGARPDAKAQKPVEPTQ 717
Cdd:PHA03307   259 RPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSspgsgPAPSSPRASSSSSSSRESSSSSTSSSSESSRG 338
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  718 TKDDPKKLPTKPAPKPDTKAAPKGPQAGAGPKPGPAQPAPQPQPPQKTPEQSRRFSLNLGGITDAPKPQP 787
Cdd:PHA03307   339 AAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFP 408
PDZ3_Par3-like cd23059
PDZ domain 3 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
4548-4611 1.27e-05

PDZ domain 3 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Par3 (or PAR3 or Par-3, also known as Atypical PKC isotype-specific-interacting protein, ASIP, Drosophila Bazooka) and related domains. Par3 is a scaffold protein involved in organizing cell polarity across animals. Par3 binds numerous molecules both for its recruitment to one pole of the cell and for downstream contributions to polarized cell function. It regulates cell polarity by targeting the Par complex proteins Par6 and atypical protein kinase C (aPKC) to specific cortical sites. Physical interactions between Par-3 and the Par complex include Par3 PDZ domain 1 binding to the Par6 PDZ domain, Par3 PDZ domain 1 and PDZ domain 3 binding the Par6's PDZ-binding motif, and an interaction with an undefined region of aPKC that requires both Par3 PDZ2 and PDZ3. The PDZ domains of Par3 have also been implicated as potential phosphoinositide signaling integrators, since its second PDZ domain binds to phosphoinositides, and the third PDZ interacts with phosphoinositide phosphatase PTEN. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par3 family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467272 [Multi-domain]  Cd Length: 103  Bit Score: 46.89  E-value: 1.27e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051959432 4548 GLGIRVVG--GKEIPGSSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSII 4611
Cdd:cd23059     17 GLGVSVKGktSKEDNGGKADLGIFIKSIIHGGAASKDGRLRVNDQLIAVNGESLLGLTNSEAMETL 82
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
4534-4615 1.29e-05

PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467187 [Multi-domain]  Cd Length: 92  Bit Score: 46.49  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 4534 KLLRDpkdhtvsGNGLGIRVVGGKE-IPGSSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSIII 4612
Cdd:cd06703      6 TLIRD-------GKGLGFSIAGGKGsTPFRDGDEGIFISRITEGGAADRDGKLQVGDRVLSINGVDVTEARHDQAVALLT 78

                   ...
gi 2051959432 4613 QQS 4615
Cdd:cd06703     79 SSS 81
Amelin smart00817
Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin ...
300-422 1.44e-05

Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin precursor (Amelin) proteins. Matrix proteins of tooth enamel consist mainly of amelogenin but also of non-amelogenin proteins, which, although their volumetric percentage is low, have an important role in enamel mineralisation. One of the non-amelogenin proteins is ameloblastin, also known as amelin and sheathlin. Ameloblastin (AMBN) is one of the enamel sheath proteins which is though to have a role in determining the prismatic structure of growing enamel crystals.


Pssm-ID: 214832 [Multi-domain]  Cd Length: 411  Bit Score: 51.04  E-value: 1.44e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432   300 GPTKPSPQQPDSAKTTSQAPPPTKPSSQ--QPG--PAKQPLQQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGP 375
Cdd:smart00817   80 RPREHETQQYEYSLPVHPPPLPSQPSLQpqQPGlkPFLQPTALPTNQATPQKNGPQPPMHLGQPPLQQAELPMIPPQVAP 159
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 2051959432   376 AKQPPQPGSgkPPLQQTGPVKQVPPQAGPTKPpsqtAGPTKPPAQQP 422
Cdd:smart00817  160 SDKPPQTEL--PLYDFADPQNPLLFQIAHLMS----RGPMPQNKQQH 200
PDZ4_PDZD2-PDZ2_hPro-IL-16-like cd06760
PDZ domain 4 of PDZ domain containing 2 (PDZD2), PDZ domain 2 of human pro-interleukin-16 ...
4542-4620 1.67e-05

PDZ domain 4 of PDZ domain containing 2 (PDZD2), PDZ domain 2 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of PDZD2, also known as KIAA0300, PIN-1, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family also includes the second PDZ domain (PDZ2) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16; 1332 amino-acid protein). Precursor IL-16 is cleaved to produce pro-IL-16 and mature IL-16 (derived from the C-terminal 121 AA). Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467241 [Multi-domain]  Cd Length: 90  Bit Score: 46.11  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 4542 HTVSGNGLGIRVVGgkeIPGSSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSIIIQ-QSGEAEI 4620
Cdd:cd06760     10 NKEPGVGLGIGLCC---LPLENDIPGIFIHHLSPGSVAHMDGRLRRGDQILEINGTSLRNVTLNEAYAILSQcKPGPVTL 86
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
4548-4620 1.75e-05

PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GOPC and related domains. GOPC, also known as PIST (PDZ domain protein interacting specifically with TC10), FIG (fused in glioblastoma), and CAL (CFTR-associated ligand), regulates the trafficking of a wide array of proteins, including small GTPases, receptors, and cell surface molecules such as cadherin 23 and CFTR. It may regulate CFTR chloride currents and acid-sensing ASIC3 currents by modulating cell surface expression of both channels, and may play a role in autophagy. Interaction partners of the GOPC PDZ domains include: FZD5, FZD8, ASIC3, CFTR, MUC3, ARFRP1, Ggamma13, neuroligin, and Stargazin. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GOPC-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467261 [Multi-domain]  Cd Length: 83  Bit Score: 45.83  E-value: 1.75e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051959432 4548 GLGIRVVGGKE--IPgssgeigAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSIIIQQSGEAEI 4620
Cdd:cd06800     12 GLGISITGGKEhgVP-------ILISEIHEGQPADRCGGLYVGDAILSVNGIDLRDAKHKEAVTILSQQRGEITL 79
PDZ1_LNX1_2-like cd06677
PDZ domain 1 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
4549-4613 1.79e-05

PDZ domain 1 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2) and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467165 [Multi-domain]  Cd Length: 89  Bit Score: 46.08  E-value: 1.79e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2051959432 4549 LGIRVVGGKEIPgssgEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSIIIQ 4613
Cdd:cd06677     17 LGISIVGGNDTP----LINIVIQEVYRDGVIARDGRLLPGDQILEVNGVDISNVTHSQARSVLRQ 77
PDZ1_hSTXBP4-PDZ2_GgSTXBP4-like cd06698
PDZ1 domain of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus ...
4548-4611 1.85e-05

PDZ1 domain of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus uncharacterized STXBP4 isoform X1, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus uncharacterized STXBP4 isoform X1, and related domains. Human STXBP4 (also known as Synip) includes a single PDZ domain, a coiled-coil domain, and a WW domain (named for its two conserved tryptophans); Gallus gallus STXBP4 isoform X1 contains 2 PDZ domains (PDZ1 and PDZ2). Human STXBP4 plays a role in the translocation of transport vesicles from the cytoplasm to the plasma membrane: insulin induces the dissociation of the STXBP4 and STX4 complex liberating STX4 to interact with Vamp2, and to form the SNARE complex thereby promoting vesicle fusion. It may also play a role in the regulation of insulin release by pancreatic beta cells after stimulation by glucose. Human STXBP4 is also known to physically associate with a prominent isoform of TP63 (deltaNp63alpha 9) whose overexpression promotes squamous cell carcinoma development, and in doing so prevents degradation of this isoform by the Cdc20-APC/C complex, Itch, and RACK1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This STXBP4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467184 [Multi-domain]  Cd Length: 89  Bit Score: 46.14  E-value: 1.85e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051959432 4548 GLGIRVVGGKEIPGssgEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSII 4611
Cdd:cd06698     12 GLGLSIVGGINRPE---GPMVFIQEVIPGGDCYKDGRLRPGDQLVSINKESLIGVTLEEAKSIL 72
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
306-447 1.86e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 50.93  E-value: 1.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  306 PQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPArqggpvkPSSQqagpPKQLSQQPGPekPSAQQTGPAKQPPQPGSg 385
Cdd:PRK14971   363 TQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAA-------ASPS----PSQSSAAAQP--SAPQSATQPAGTPPTVS- 428
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051959432  386 kppLQQTGPVKQVPPQAGPtkppsQTAGPTKPPAQQPGPT-KPSGQQPGPEKPLEQKQAGASQ 447
Cdd:PRK14971   429 ---VDPPAAVPVNPPSTAP-----QAVRPAQFKEEKKIPVsKVSSLGPSTLRPIQEKAEQATG 483
PHA03247 PHA03247
large tegument protein UL36; Provisional
202-424 1.91e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  202 RSPAKHPTQPqsPKPAVQQQGqqRPTLQQTESSKPVPQQQQQPGEPKQVQKPGHRQPadakqeQVKQPPQPRGPQKSQPQ 281
Cdd:PHA03247  2869 RSPAAKPAAP--ARPPVRRLA--RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQP------QPPPPPQPQPPPPPPPR 2938
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  282 PSEPAKPvQQQTSAKLSSGPTKPSPQQ----PDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARQGGPVKPSS-----QQ 352
Cdd:PHA03247  2939 PQPPLAP-TTDPAGAGEPSGAVPQPWLgalvPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSlalheET 3017
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051959432  353 AGPPKQLSQQPGPekPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVP--PQAGPTKPPSQTAGPTKPPAQQPGP 424
Cdd:PHA03247  3018 DPPPVSLKQTLWP--PDDTEDSDADSLFDSDSERSDLEALDPLPPEPhdPFAHEPDPATPEAGARESPSSQFGP 3089
PHA03418 PHA03418
hypothetical E4 protein; Provisional
301-438 1.96e-05

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 49.35  E-value: 1.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  301 PTKPSPQQPdsaktTSQAPPPTKPSSQ-QPGPAKQPLQQPARQGGPV---KPSSQQAGPPKQLSQQP-GPEKPSAQQTGP 375
Cdd:PHA03418    34 PLLPAPHHP-----NPQEDPDKNPSPPpDPPLTPRPPAQPNGHNKPPvtkQPGGEGTEEDHQAPLAAdADDDPRPGKRSK 108
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  376 AKQP-PQPGSGKP-PLQQTgpVKQVPPQAGPTKPPSQTAGPTKPPAQ-----QPGPTKPSGQQPGPEKPL 438
Cdd:PHA03418   109 ADEHgPAPGRAALaPFKLD--LDQDPLHGDPDPPPGATGGQGEEPPEggeesQPPLGEGEGAVEGHPPPL 176
PDZ4_MUPP1-like cd06668
PDZ domain 4 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
4546-4611 2.21e-05

PDZ domain 4 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467156 [Multi-domain]  Cd Length: 88  Bit Score: 45.75  E-value: 2.21e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051959432 4546 GNGLGIRVVGGKEIpGSSGEigAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSII 4611
Cdd:cd06668     13 SSGLGISLEGTVDV-EVRGH--HYIRSILPEGPVGRNGKLFSGDELLEVNGIQLLGLSHKEVVSIL 75
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
4534-4607 2.40e-05

PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of syntrophins (including alpha-1-syntrophin, beta-1-syntrophin, beta-2-syntrophin, gamma-1-syntrophin, and gamma-2-syntrophin), and related domains. Syntrophins play a role in recruiting various signaling molecules into signaling complexes and help provide appropriate spatiotemporal regulation of signaling pathways. They function in cytoskeletal organization and maintenance; as components of the dystrophin-glycoprotein complex (DGC), they help maintain structural integrity of skeletal muscle fibers. They link voltage-gated sodium channels to the actin cytoskeleton and the extracellular matrix, and control the localization and activity of the actin reorganizing proteins such as PI3K, PI(3,4)P2 and TAPP1. Through association with various cytoskeletal proteins within the cells, they are involved in processes such as regulation of focal adhesions, myogenesis, calcium homeostasis, and cell migration. They also have roles in synapse formation and in the organization of utrophin, acetylcholine receptor, and acetylcholinesterase at the neuromuscular synapse. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This syntrophin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467262 [Multi-domain]  Cd Length: 83  Bit Score: 45.64  E-value: 2.40e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051959432 4534 KLLRDPkdhtvsGNGLGIRVVGGKE--IPgssgeigAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEV 4607
Cdd:cd06801      4 RVVKQD------VGGLGISIKGGAEhkMP-------ILISKIFKGQAADQTGQLFVGDAILSVNGENLEDATHDEA 66
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
170-459 2.45e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.94  E-value: 2.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  170 PFDLISDSDTTHEDAGRKQKVTPKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGQQRPTLQQT---ESSKPVPQQQQQPGE 246
Cdd:PHA03307   131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEpppSTPPAAASPRPPRRS 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  247 PKQVQKPGHRQPADAKQEQVKQPPQPRGPQKSQPQPSE-------PAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAP 319
Cdd:PHA03307   211 SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGwgpenecPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  320 PPTKPSSQQPGPAKQPLQQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPPLqQTGPVKQVP 399
Cdd:PHA03307   291 PRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPA-DPSSPRKRP 369
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  400 PQAGPTKPPSQTAGPTKPPAQQPGPTKPSGQQPGPEkPLEQKQAGASQPTESVSKKTFCP 459
Cdd:PHA03307   370 RPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATG-RFPAGRPRPSPLDAGAASGAFYA 428
PDZ_MPP5-like cd06798
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related ...
4570-4616 2.81e-05

PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP5, Drosophila Stardust, and related domains. MPP5 (also known as MAGUK p55 subfamily member 1, protein associated with Lin-7 1 or PALS1) and Drosophila Stardust are membrane-associated guanylate kinase (MAGUK)-like proteins that serve as signaling and scaffolding proteins, linking different proteins critical to the formation and maintenance of tight junctions (TJ) and apical-basal polarity. Apical-basal polarity determinants cluster in complexes; in particular, the Crumbs complex (Crb, MPP5, and PATJ) and the PAR/aPKC-complex (PAR-3, PAR-6, aPKC) determine the apical plasma membrane domain. Within the Crumbs complex, Crb is stabilized in the plasma membrane by MPP5, which in turn recruits PATJ and Lin-7 to the complex. MPP5 also links the Crumbs complex with the PAR/aPKC-complex. The Drosophila homolog of the Crumbs complex is the (CRB)-Stardust (Sdt)-Discs Lost (Dlt) complex. MPP5 also acts as an interaction partner for SARS-CoV envelope protein E, which results in delayed formation of TJs and dysregulation of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP5-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467259 [Multi-domain]  Cd Length: 79  Bit Score: 45.03  E-value: 2.81e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2051959432 4570 IAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSIIIQQSG 4616
Cdd:cd06798     25 ISRIVKGGAAEKSGLLHEGDEILEINGIEIRGKDVNEVCDLLADMHG 71
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
1424-1673 2.82e-05

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 50.82  E-value: 2.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1424 KESNKKDTISQESPPSPSDLAKLESTVLSILEAQANTLSDEKSAKSKELSETYGEQTKDQ--LKTKPLPVTPESYSSD-E 1500
Cdd:PTZ00108  1147 VEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKrkLDDKPDNKKSNSSGSDqE 1226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1501 EDLKAIKEGEGTIVEEGKGTASSQADYKEDHEGEDIPARRQQRYDSVEDSS-----ESENSPVPRRKRRTSVGSSSSDEY 1575
Cdd:PTZ00108  1227 DDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRvsavqYSPPPPSKRPDGESNGGSKPSSPT 1306
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1576 KRDDsqgsgdeEDFIRKQIIEMSADEDASgseddefirnqLKEISAAESQKKEEVKSKAKGTAGKHRRMARKSSAGYDED 1655
Cdd:PTZ00108  1307 KKKV-------KKRLEGSLAALKKKKKSE-----------KKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDD 1368
                          250
                   ....*....|....*...
gi 2051959432 1656 AGRRHSWHDDDDETFDES 1673
Cdd:PTZ00108  1369 DDSEVDDSEDEDDEDDED 1386
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
4546-4607 3.20e-05

PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of ZO-1, -2, -3 and related domains. Zonula occludens proteins (ZO-1, ZO-2, ZO-3) are multi-PDZ domain proteins involved in the maintenance and biogenesis of multi-protein networks at the cytoplasmic surface of intercellular contacts in epithelial and endothelial cells. They have three N-terminal PDZ domains, PDZ1-3, followed by a Src homology-3 (SH3) domain and a guanylate kinase (GuK)-like domain. Among protein-protein interactions for all ZO proteins is the binding of the first PDZ domain (PDZ1) to the C-termini of claudins , and the homo- and hetero-dimerization of ZO-proteins via their second PDZ domain (PDZ2), which takes place by symmetrical domain swapping of the first two beta-strands of PDZ2. At the cell level, ZO-1 and ZO-2 are involved in polarity maintenance, gene transcription, cell proliferation, and tumor cell metastasis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ZO family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467211 [Multi-domain]  Cd Length: 82  Bit Score: 45.25  E-value: 3.20e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432 4546 GNGLGIRVVGGKEIpgssgeiGAYIAKILPGGNAEQTGkLIEGMQVLEWNGIPLTGKTYEEV 4607
Cdd:cd06729     10 GGSVGLRLAGGNDV-------GIFVAGVQEGSPAEKQG-LQEGDQILKVNGVDFRNLTREEA 63
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
271-443 3.33e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 50.26  E-value: 3.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  271 QPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQP--------LQQPARQ 342
Cdd:PRK12323   364 RPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPapealaaaRQASARG 443
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  343 GGPVK---------PSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPP--QAGPTKPPSQT 411
Cdd:PRK12323   444 PGGAPapapapaaaPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPApaQPDAAPAGWVA 523
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2051959432  412 AGPTKPPAQQPGPTKPSGQQPGPEKPLEQKQA 443
Cdd:PRK12323   524 ESIPDPATADPDDAFETLAPAPAAAPAPRAAA 555
PHA03379 PHA03379
EBNA-3A; Provisional
196-445 3.55e-05

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 50.44  E-value: 3.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  196 GKPEEQRSPAKHPTQPQS--PKPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPKQVQKPGHRQPADAKQEQVKQPPQPR 273
Cdd:PHA03379   396 KLTERAREALEKASEPTYgtPRPPVEKPRPEVPQSLETATSHGSAQVPEPPPVHDLEPGPLHDQHSMAPCPVAQLPPGPL 475
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  274 gpQKSQPQPSEPAKPVQQQTSAKLSSGPTKP--SPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARqggPVKPSsq 351
Cdd:PHA03379   476 --QDLEPGDQLPGVVQDGRPACAPVPAPAGPivRPWEASLSQVPGVAFAPVMPQPMPVEPVPVPTVALER---PVCPA-- 548
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  352 qagPPKQLSQQPGpEKPSAQQTGPAKQPPqPGSGKPPlqqtGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGP-TKPSGQ 430
Cdd:PHA03379   549 ---PPLIAMQGPG-ETSGIVRVRERWRPA-PWTPNPP----RSPSQMSVRDRLARLRAEAQPYQASVEVQPPQlTQVSPQ 619
                          250
                   ....*....|....*..
gi 2051959432  431 QP--GPEKPLEQKQAGA 445
Cdd:PHA03379   620 QPmeYPLEPEQQMFPGS 636
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
4542-4617 5.14e-05

PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467186 [Multi-domain]  Cd Length: 89  Bit Score: 44.55  E-value: 5.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 4542 HTVSGNG-LGIRVVGGKE---IPGSSGEIGAYIAKILPGGNAEQTGKLIeGMQVLEWNGIPLTGKTYEEVQSIIIQQSGE 4617
Cdd:cd06702      4 HLVKAGGpLGLSIVGGSDhssHPFGVDEPGIFISKVIPDGAAAKSGLRI-GDRILSVNGKDLRHATHQEAVSALLSPGQE 82
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
292-422 5.43e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 49.39  E-value: 5.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  292 QTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPS----SQQPGPAKQPLQQPARQggpvkPSSQQAGPPKQLS-QQPGPE 366
Cdd:PRK14971   361 QLTQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAaaaaSPSPSQSSAAAQPSAPQ-----SATQPAGTPPTVSvDPPAAV 435
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2051959432  367 KPSAQQTGPAKQPPQPgsgkPPLQQTGPVKQVPPQAGPTKppsqtaGPTKPPAQQP 422
Cdd:PRK14971   436 PVNPPSTAPQAVRPAQ----FKEEKKIPVSKVSSLGPSTL------RPIQEKAEQA 481
PDZ_Radil-like cd06690
PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; ...
4546-4617 6.06e-05

PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Radil (also known as protein KIAA1849) and related domains. Radil is required for cell adhesion and migration of neural crest precursors during development. Radil is a component of a Rasip1-Radil-ARHGAP29 complex at endothelial cell-cell junctions. Rap1, via its effectors Radil and Rasip1 and their binding partner ArhGAP29, controls the endothelial barrier by decreasing Rho-mediated radial tension on cell-cell junctions. ArhGAP29 binds the Radil PDZ domain. The Radil PDZ domain also binds kinesin family protein 14 (KIF14); KIF14 negatively regulates Rap1-mediated inside-out integrin activation by tethering Radil on microtubules. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Radil-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467177 [Multi-domain]  Cd Length: 88  Bit Score: 44.59  E-value: 6.06e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432 4546 GNGLGIRVVGGKEIPGSSGeiGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSiIIQQSGE 4617
Cdd:cd06690     12 PKGLGLGLIDGLHTPLRSP--GIYIRTLVPDSPAARDGRLRLGDRILAVNGTSLVGADYQSAMD-LIRTSGD 80
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
253-439 6.36e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 49.46  E-value: 6.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  253 PGHRQPADAKQEQVKQPPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPA 332
Cdd:PRK07003   427 PAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAA 506
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  333 KQPLQQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPA----------------KQPPQPGSGKPPLQQTGPVK 396
Cdd:PRK07003   507 VPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAGGAAaaldvlrnagmrvssdRGARAAAAAKPAAAPAAAPK 586
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2051959432  397 QVPPQ-AGPTKPPSQTAGPTKPPAQQPGPTKPSGQQPGPEKPLE 439
Cdd:PRK07003   587 PAAPRvAVQVPTPRARAATGDAPPNGAARAEQAAESRGAPPPWE 630
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
4546-4616 6.49e-05

PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of afadin (AFDN, also known as ALL1-fused gene from chromosome 6 protein (AF6) and MLLT4), and related domains. AFDN belongs to the adhesion system, probably together with the E-cadherin-catenin system, that plays a role in the organization of homotypic, interneuronal, and heterotypic cell-cell adherens junctions. The AFDN PDZ domain interaction partners include poliovirus receptor-related protein PRR2/nectin, the junctional adhesion molecule (JAM), the breakpoint-cluster-region protein (BCR), connexin36 (Cx36), and a subset of Eph-related receptor tyrosine kinases; it can also bind low molecular weight ligands, in competition with a natural peptide ligand. Other AFDN-binding proteins have been identified. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This AFDN family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467251 [Multi-domain]  Cd Length: 89  Bit Score: 44.58  E-value: 6.49e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432 4546 GNGLGIRVVGGKeipGS-SGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSiIIQQSG 4616
Cdd:cd06789     12 GNGMGLSIVAAK---GAgQDKLGIYIKSVVKGGAADLDGRLQAGDQLLSVDGHSLVGLSQERAAE-LMTKTG 79
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
349-448 6.58e-05

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 46.57  E-value: 6.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  349 SSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPvKQVPPQAGPTKP--PSQTAGPTKPPAQQPGPTK 426
Cdd:pfam15240   28 SPSLISEEEGQSQQGGQGPQGPPPGGFPPQPPASDDPPGPPPPGGP-QQPPPQGGKQKPqgPPPQGGPRPPPGKPQGPPP 106
                           90       100
                   ....*....|....*....|....*.
gi 2051959432  427 PSGQQ----PGPEKPLEQKQAGASQP 448
Cdd:pfam15240  107 QGGNQqqgpPPPGKPQGPPPQGGGPP 132
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
263-410 6.94e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 49.09  E-value: 6.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  263 QEQVKQPPQPRGPQKSQPQPSEPAKPVQQQTSAklssgPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGpAKQPLQQPARQ 342
Cdd:PRK07994   362 AAPLPEPEVPPQSAAPAASAQATAAPTAAVAPP-----QAPAVPPPPASAPQQAPAVPLPETTSQLLA-ARQQLQRAQGA 435
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051959432  343 GGPVKPSSQQAGPPKQLSQ-----QPGPEKPSAQQTGPAKQPPQPGSGKPPlqqtgPVKQVPPQAGPTKPPSQ 410
Cdd:PRK07994   436 TKAKKSEPAAASRARPVNSalerlASVRPAPSALEKAPAKKEAYRWKATNP-----VEVKKEPVATPKALKKA 503
PHA03264 PHA03264
envelope glycoprotein D; Provisional
309-426 6.97e-05

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 48.85  E-value: 6.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  309 PDSAKTTSQAPPPTkPSSQQPGPAKQPLQQPARQGGPVKPssqqaGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPP 388
Cdd:PHA03264   256 PYFEESKGYEPPPA-PSGGSPAPPGDDRPEAKPEPGPVED-----GAPGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPA 329
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2051959432  389 lqqtgpvkqvPPQAGPTKPPSQTAGPTKPPA-QQPGPTK 426
Cdd:PHA03264   330 ----------PDADRPEGWPSLEAITFPPPTpATPAVPR 358
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
203-453 7.22e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.21  E-value: 7.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  203 SPAKHPTQPQSPKPAVQQQGQQRPTLQQTESSkpvpqqqqqpgepkQVQKPGHRQPADAKQEQVKQPPQPRGPQKSQPQP 282
Cdd:PRK07764   394 PAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAP--------------AAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPA 459
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  283 SEP-AKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQP-------------------------------- 329
Cdd:PRK07764   460 AAPsAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADdaatlrerwpeilaavpkrsrktwaillpeat 539
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  330 ---------------GPAKQPLQQP-----------ARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPG 383
Cdd:PRK07764   540 vlgvrgdtlvlgfstGGLARRFASPgnaevlvtalaEELGGDWQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPA 619
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  384 SGKPPLQQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGPTKPSGQQPGPEKPLEQKQAGASQPTESVS 453
Cdd:PRK07764   620 APAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAA 689
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
316-449 7.58e-05

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 46.18  E-value: 7.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  316 SQAPPPTKPSSQQPGPAKQPLQQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKP--PLQQTG 393
Cdd:pfam15240   14 SSAQSSSEDVSQEDSPSLISEEEGQSQQGGQGPQGPPPGGFPPQPPASDDPPGPPPPGGPQQPPPQGGKQKPqgPPPQGG 93
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051959432  394 P-----VKQVPPQAGPTKP--PSQTAGPTKPPAQQPGPTKPSGQQPGPEKPLEQKQAGASQPT 449
Cdd:pfam15240   94 PrpppgKPQGPPPQGGNQQqgPPPPGKPQGPPPQGGGPPPQGGNQQGPPPPPPGNPQGPPQRP 156
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
270-425 7.59e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 49.08  E-value: 7.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  270 PQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARQGGPVKPS 349
Cdd:PRK07003   383 PGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSR 462
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051959432  350 SQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGPT 425
Cdd:PRK07003   463 CDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPA 538
PRK10927 PRK10927
cell division protein FtsN;
260-405 9.51e-05

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 48.14  E-value: 9.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  260 DAKQEQVKQPPQPR--GPQKSQPQPSEPAKPVQQQTSAKLSSGPTKP-----SPQQPDSAKTT----SQAP--PPTKPSS 326
Cdd:PRK10927    90 ESRQPGVRAPTEPSagGEVKTPEQLTPEQRQLLEQMQADMRQQPTQLvevpwNEQTPEQRQQTlqrqRQAQqlAEQQRLA 169
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051959432  327 QQPGPAKQPLQQPARqggpvkpsSQQAGPPKQLSQQPGPeKPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPT 405
Cdd:PRK10927   170 QQSRTTEQSWQQQTR--------TSQAAPVQAQPRQSKP-ASTQQPYQDLLQTPAHTTAQSKPQQAAPVTRAADAPKPT 239
dnaA PRK14086
chromosomal replication initiator protein DnaA;
310-448 9.69e-05

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 48.67  E-value: 9.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  310 DSAKTTSQAPPPTKPSSQQPgpakqplQQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQP-PQPGSGKPP 388
Cdd:PRK14086    89 DPSAGEPAPPPPHARRTSEP-------ELPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARPAYPAYQQrPEPGAWPRA 161
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432  389 LQQTGPVKQV--PPQAGPTKPPSQTAGPTKPPAQQPGPTKPsgQQPGPEKPLEQKQAGASQP 448
Cdd:PRK14086   162 ADDYGWQQQRlgFPPRAPYASPASYAPEQERDREPYDAGRP--EYDQRRRDYDHPRPDWDRP 221
PDZ10_MUPP1-PDZ8_PATJ-like cd06673
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ...
4548-4607 9.87e-05

PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 10 of MUPP1, PDZ domain 8 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ10 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467161 [Multi-domain]  Cd Length: 86  Bit Score: 43.82  E-value: 9.87e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051959432 4548 GLGIRVVGGKEIPgssgeIGA-YIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEV 4607
Cdd:cd06673     14 GLGLSIVGGSDTL-----LGAiIIHEVYEDGAAAKDGRLWAGDQILEVNGEDLRKATHDEA 69
dnaA PRK14086
chromosomal replication initiator protein DnaA;
253-430 9.94e-05

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 48.67  E-value: 9.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  253 PGH-RQPADAKQeqvkqPPQPRGPQKSQPQPSEPAKpVQQQTSAKLSSGPTKPSPQQ-----PDSAKTTSQAPPPTKPSS 326
Cdd:PRK14086   119 EGYgGPRADDRP-----PGLPRQDQLPTARPAYPAY-QQRPEPGAWPRAADDYGWQQqrlgfPPRAPYASPASYAPEQER 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  327 QQPGPAKQPLQQPARQGGPVKPSSQQAGPPKQLSQQPGPEkpsaqqtgpakqppqPGSGKPPlqQTGPVKQVPPQAgpTK 406
Cdd:PRK14086   193 DREPYDAGRPEYDQRRRDYDHPRPDWDRPRRDRTDRPEPP---------------PGAGHVH--RGGPGPPERDDA--PV 253
                          170       180
                   ....*....|....*....|....*..
gi 2051959432  407 PPSQTAGPTKPPAQQ---PGPTKPSGQ 430
Cdd:PRK14086   254 VPIRPSAPGPLAAQPapaPGPGEPTAR 280
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
1023-1354 1.09e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 48.47  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1023 TSTPPTLAAAKPKEEPGIQKEAPKLQQGRLEKTLSADKIQQG---VQREDAKPKQGKLVKTPSADKIQRASQKEDPRIQQ 1099
Cdd:NF033838   168 TNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAkakVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKE 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1100 TRLTKTASYDR----------VLHEVQKEDEKLQEAKLAKTSSADKILHG-VQKEDIKLQETKlAKIPSADKILQGIQKE 1168
Cdd:NF033838   248 AVEKNVATSEQdkpkrrakrgVLGEPATPDKKENDAKSSDSSVGEETLPSpSLKPEKKVAEAE-KKVEEAKKKAKDQKEE 326
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1169 DPKLQQMKMAKALSADKIQPAVQKEDAQLQEVKlpKAASVDKIQHGIQKEDIKLQHEKIKKTRsVDKIQEEDQKEETKLQ 1248
Cdd:NF033838   327 DRRNYPTNTYKTLELEIAESDVKVKEAELELVK--EEAKEPRNEEKIKQAKAKVESKKAEATR-LEKIKTDRKKAEEEAK 403
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1249 RgklsKTPSANKIpATTTADQKKPLNTVEedketvpPEKSTPHPEDKKEEITAEIKDhvaKQKAEVEapykglQAKEQEd 1328
Cdd:NF033838   404 R----KAAEEDKV-KEKPAEQPQPAPAPQ-------PEKPAPKPEKPAEQPKAEKPA---DQQAEED------YARRSE- 461
                          330       340
                   ....*....|....*....|....*.
gi 2051959432 1329 vkkEDLTTGISQEVLKTEKAQEEEIP 1354
Cdd:NF033838   462 ---EEYNRLTQQQPPKTEKPAQPSTP 484
PHA03247 PHA03247
large tegument protein UL36; Provisional
254-474 1.18e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  254 GHRQPADAKqeqvKQPPQPRGPQKSQPQPsePAKPVQQQTSAKLSSGP-TKPSPqqPDSAKTTSQAPPPTKPS------- 325
Cdd:PHA03247   265 ADRAPETAR----GATGPPPPPEAAAPNG--AAAPPDGVWGAALAGAPlALPAP--PDPPPPAPAGDAEEEDDedgamev 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  326 -SQQPGP-AKQPLQQPARQGGPVKPSS------------QQAGPPKQLSQQ-PGPEKPSAQQTG----PAKQPPQPGSGK 386
Cdd:PHA03247   337 vSPLPRPrQHYPLGFPKRRRPTWTPPSsledlsagrhhpKRASLPTRKRRSaRHAATPFARGPGgddqTRPAAPVPASVP 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  387 PPLQQTGPVKQVPPQAGPTKP--PSQTAGPTKPPAQQPGPTKPSGQQPGPEKPLEQ--KQAGASQPTESvskktfcPLCT 462
Cdd:PHA03247   417 TPAPTPVPASAPPPPATPLPSaePGSDDGPAPPPERQPPAPATEPAPDDPDDATRKalDALRERRPPEP-------PGAD 489
                          250
                   ....*....|..
gi 2051959432  463 TTELLLHTPEKA 474
Cdd:PHA03247   490 LAELLGRHPDTA 501
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
269-422 1.23e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 48.05  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  269 PPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPS-PQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARQGgPVK 347
Cdd:PRK13108   282 PGALRGSEYVVDEALEREPAELAAAAVASAASAVGPVgPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDG-EST 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  348 PSSQQAGPPKQLSQQPG------PEKPSAQQTGPAKQPPQPgSGKPPLQQTGPVKQVP----PQAGPTKPPSQTAGPTKP 417
Cdd:PRK13108   361 PAVEETSEADIEREQPGdlagqaPAAHQVDAEAASAAPEEP-AALASEAHDETEPEVPekaaPIPDPAKPDELAVAGPGD 439

                   ....*
gi 2051959432  418 PAQQP 422
Cdd:PRK13108   440 DPAEP 444
PTZ00121 PTZ00121
MAEBL; Provisional
1114-1978 1.26e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1114 EVQKEDEKLQEAKlAKTSSADKILHGVQKEDIKLQETKlAKIPSADKILQGIQKEDPKLQQmKMAKALSADKIQPAVQKE 1193
Cdd:PTZ00121  1085 EDNRADEATEEAF-GKAEEAKKTETGKAEEARKAEEAK-KKAEDARKAEEARKAEDARKAE-EARKAEDAKRVEIARKAE 1161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1194 DAQLQEVKlPKAASVDKIQHGIQKEDIKlQHEKIKKTRSVDKIQEEDQKEETKlQRGKLSKTPSANKIPATTTADQKKpl 1273
Cdd:PTZ00121  1162 DARKAEEA-RKAEDAKKAEAARKAEEVR-KAEELRKAEDARKAEAARKAEEER-KAEEARKAEDAKKAEAVKKAEEAK-- 1236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1274 ntvEEDKETVPPEKSTPHPEDKKEEITAEIKDHVAKQKAEVEAPYKGLQAKEQEDVKKEDLTTGiSQEVLKTEKAQEEEI 1353
Cdd:PTZ00121  1237 ---KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK-AEEKKKADEAKKKAE 1312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1354 PVQTAplprtdhvEAVREKIEKEDDKSDTSssqqqkspqglsdtgyssdgissslgeipshiptdeKDLLKESNKKDTIS 1433
Cdd:PTZ00121  1313 EAKKA--------DEAKKKAEEAKKKADAA------------------------------------KKKAEEAKKAAEAA 1348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1434 QESPPSPSDLAKLESTvlsilEAQANTLSDEKSAKSKELSETYGEQTK--DQLKTKPlpvtpESYSSDEEDLKAiKEGEG 1511
Cdd:PTZ00121  1349 KAEAEAAADEAEAAEE-----KAEAAEKKKEEAKKKADAAKKKAEEKKkaDEAKKKA-----EEDKKKADELKK-AAAAK 1417
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1512 TIVEEGKGTAssqadyKEDHEGEDIPARRQQRYDSVEDSSESENSPVPRRKRRTSVGSSSSDEYKRDDSQGSGDEEDFIR 1591
Cdd:PTZ00121  1418 KKADEAKKKA------EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1592 KQIIEMSADEDASGSEDdefiRNQLKEISAAESQKKEEVKSKAKgtAGKHRRMARKSSAGYDEDAGRRHswhddddETFD 1671
Cdd:PTZ00121  1492 AEEAKKKADEAKKAAEA----KKKADEAKKAEEAKKADEAKKAE--EAKKADEAKKAEEKKKADELKKA-------EELK 1558
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1672 ESPEPKYRESKSQDGEElaisgggglrrfKTIELNSTITAKYSEVSEQQKGILYFDEEPELEMESLTDSPEDRSRGEgss 1751
Cdd:PTZ00121  1559 KAEEKKKAEEAKKAEED------------KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE--- 1623
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1752 slhassftpgtspTSVSSLDEDSDSSPSHKKLGGESKQQRKARHRTHGPLLPTIEDSseeeelREEEELLKEQEKQRELE 1831
Cdd:PTZ00121  1624 -------------ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA------KKAEEDKKKAEEAKKAE 1684
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1832 QQQRKSSSKKSKKDKDELRAQRRRERPKtppsnlspiEDASPTEELRQAAE-----MEELHRSSCSEYSPSIESEPEGFE 1906
Cdd:PTZ00121  1685 EDEKKAAEALKKEAEEAKKAEELKKKEA---------EEKKKAEELKKAEEenkikAEEAKKEAEEDKKKAEEAKKDEEE 1755
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2051959432 1907 ------ISPEKIIEVQKVYKLPTAVSLYSPTDEQPTGLPKEESGQKTLKSAEEVYEEMMHKSKSFqiSNENNEVFEKE 1978
Cdd:PTZ00121  1756 kkkiahLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLV--INDSKEMEDSA 1831
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
4542-4620 1.39e-04

PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of ZO-1, -2, -3 and related domains. Zonula occludens proteins (ZO-1, ZO-2, ZO-3) are multi-PDZ domain proteins involved in the maintenance and biogenesis of multi-protein networks at the cytoplasmic surface of intercellular contacts in epithelial and endothelial cells. They have three N-terminal PDZ domains, PDZ1-3, followed by a Src homology-3 (SH3) domain and a guanylate kinase (GuK)-like domain. Among protein-protein interactions for all ZO proteins is the binding of the first PDZ domain (PDZ1) to the C-termini of claudins, and the homo- and hetero-dimerization of ZO-proteins via their second PDZ domain (PDZ2), which takes place by symmetrical domain swapping of the first two beta-strands of PDZ2. At the cell level, ZO-1 and ZO-2 are involved in polarity maintenance, gene transcription, cell proliferation, and tumor cell metastasis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ZO family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467209 [Multi-domain]  Cd Length: 87  Bit Score: 43.42  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 4542 HTV-----SGNGLGIRVVGGKEIPG-SSGEIGAYIAKILPGGNAEqtGKLIEGMQVLEWNGIPLTGKTYEE-VQsiIIQQ 4614
Cdd:cd06727      1 HTVtlhraPGFGFGIAVSGGRDNPHfQSGDTSIVISDVLKGGPAE--GKLQENDRVVSVNGVSMENVEHSFaVQ--ILRK 76

                   ....*..
gi 2051959432 4615 SG-EAEI 4620
Cdd:cd06727     77 CGkTANI 83
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
155-631 1.45e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 47.84  E-value: 1.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  155 ANPLSAVTSVVNKF--NPFDLISDSDTTHEDAGRKQKVTPKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGQQRPTLQQTE 232
Cdd:NF033839   130 MESQSKVDEAVSKFekDSSSSSSSGSSTKPETPQPENPEHQKPTTPAPDTKPSPQPEGKKPSVPDINQEKEKAKLAVATY 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  233 SSKPVPQQQQQPgepkqVQKPGHRQPADAKQEQVKQPPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSA 312
Cdd:NF033839   210 MSKILDDIQKHH-----LQKEKHRQIVALIKELDELKKQALSEIDNVNTKVEIENTVHKIFADMDAVVTKFKKGLTQDTP 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  313 KttsqapPPTKPSSQQPGPAKQPLQQParqggPVKPSSQQAGPPKQlSQQPGPEKPSAQQTgpakqpPQPGSGKPplqqt 392
Cdd:NF033839   285 K------EPGNKKPSAPKPGMQPSPQP-----EKKEVKPEPETPKP-EVKPQLEKPKPEVK------PQPEKPKP----- 341
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  393 gpvkQVPPQAGPTKPPSQTAGPTKPPAQQPGPTKPSGQ-QPGPEKPLEQKQAGASQPTESVSKKtfcplctttelllhtP 471
Cdd:NF033839   342 ----EVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEvKPQPETPKPEVKPQPEKPKPEVKPQ---------------P 402
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  472 EKANYNTCTQCHTvvcslcgfnPNPHITeisewlclncqmqralggdlaaghgPGPQPPAPKQKTPipPSTAKPSPQPQP 551
Cdd:NF033839   403 EKPKPEVKPQPEK---------PKPEVK-------------------------PQPEKPKPEVKPQ--PEKPKPEVKPQP 446
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  552 vqkkditSKPDPSQLADPKKPPPQKKQTPLPGSPPVKSKQPRAEPTEISQQTRDATPKSdqvkpTQAEDKQKQPSVQKPT 631
Cdd:NF033839   447 -------EKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPST-----PNNLSKDKQPSNQAST 514
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
205-454 2.03e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 47.61  E-value: 2.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  205 AKHPTQPQSPKpavqqqgqqrptlqQTESSKPVPQQQQQPGEPKQVQKPGHRQPADAKQeqvkQPPQPRGPQKSQPQPSE 284
Cdd:PLN03209   321 AKIPSQRVPPK--------------ESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKA----VVPRPLSPYTAYEDLKP 382
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  285 PAKPVQQQTSAKlssgptKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARQGGPVKPSSQQAGPPKQLSQQPG 364
Cdd:PLN03209   383 PTSPIPTPPSSS------PASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYARYEDLKPPTSPSPT 456
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  365 PEKPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQTAgPTKPPAqQPGPTKPSGQQPGPEKPLEQKQAG 444
Cdd:PLN03209   457 APTGVSPSVSSTSSVPAVPDTAPATAATDAAAPPPANMRPLSPYAVYD-DLKPPT-SPSPAAPVGKVAPSSTNEVVKVGN 534
                          250
                   ....*....|
gi 2051959432  445 ASQPTESVSK 454
Cdd:PLN03209   535 SAPPTALADE 544
Med25_SD1 pfam11235
Mediator complex subunit 25 synapsin 1; The overall function of the full-length Med25 is ...
274-429 2.05e-04

Mediator complex subunit 25 synapsin 1; The overall function of the full-length Med25 is efficiently to coordinate the transcriptional activation of RAR/RXR (retinoic acid receptor/retinoic X receptor) in higher eukaryotic cells. Human Med25 consists of several domains with different binding properties, the N-terminal, VWA, domain, this SD1 - synapsin 1 - domain from residues 229-381, a PTOV(B) or ACID domain from 395-545, an SD2 domain from residues 564-645 and a C-terminal NR box-containing domain (646-650) from 646-747. This The function of the SD domains is unclear.


Pssm-ID: 463244 [Multi-domain]  Cd Length: 157  Bit Score: 44.77  E-value: 2.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  274 GP-QKSQPQPSEPAKPvqqqTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARQGGPVKPSSQQ 352
Cdd:pfam11235   10 GPlQSKQPVPLPPAAP----SGATLSAAPQQPLPPVPPQYQVPGNLSAAQVAAQNAVEAAKNQKAGLGPRFSPITPLQQA 85
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051959432  353 AgppkqlsqqPGPEKPSAQQTGPAKQPPQPGSGKPPlqqtgpvkqvPPQAGPTKPPSQTAGPTKPPAQQPGPTKPSG 429
Cdd:pfam11235   86 A---------PGVGPPFSQAPAPQLPPGPPGAPKPV----------PPASQPSLVSTVAPGSGLAPTAQPGAPSMAG 143
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
527-798 3.29e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 46.69  E-value: 3.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  527 PQPPAPKQKTPIPPS-TAKPSPQPQPVQ--KKDITSKPDPSQLADPKKPPPQKKQTPLPGSPPVKSKQPRAEPTEISQQT 603
Cdd:NF033839   162 PQPENPEHQKPTTPApDTKPSPQPEGKKpsVPDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIVALIKELDELK 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  604 RDATPKSDQVKPtqaeDKQKQPSVQKPTADTVSTSAALEQKQDLAGPRPPtqqkvtDSPKPELAKPSQDTHPAEDKPDSK 683
Cdd:NF033839   242 KQALSEIDNVNT----KVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEP------GNKKPSAPKPGMQPSPQPEKKEVK 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  684 PVPQvsrqksdpklasqpgarpdakaqkpveptqtKDDPKKLPTKPAPKPDTKAAPKGPQAGAGPKPGPAQPAPQPQPPQ 763
Cdd:NF033839   312 PEPE-------------------------------TPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEK 360
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2051959432  764 KTPEQSRRfslnLGGITDAPKPQPTTPQETVTGKL 798
Cdd:NF033839   361 PKPEVKPQ----PEKPKPEVKPQPETPKPEVKPQP 391
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
520-750 3.32e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.09  E-value: 3.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  520 AAGHGPGPQPPAPKQKTPIPPSTAKPSPQPQPVQKKDITSKPDPSQLADPKKPPPQKKQTPLPGSPPvkskqPRAEPtei 599
Cdd:PHA03307    61 ACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPP-----PSPAP--- 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  600 sqqtrDATPKSDQVKPTQAEDKQKQPSVQKPTADTVSTSAALEQKQDLAGPRPPTQQkvTDSPKPELAKPSQDTHPAEDK 679
Cdd:PHA03307   133 -----DLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETAR--APSSPPAEPPPSTPPAAASPR 205
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432  680 PDSKPVP-QVSRQKSDPKLASQPGARPDAKAQKPVEPTQTKDDPKKLPTKPAPKPDTKAAPKGPQAGAGPKP 750
Cdd:PHA03307   206 PPRRSSPiSASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNG 277
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
255-424 3.34e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 46.78  E-value: 3.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  255 HRQPADAKQEQVKQPPQPRGPQKSQPQPSEPAKPVQQQtsaklssgptkPSPQQPDSAKTTSQAPPPTKPSSQQPGpAKQ 334
Cdd:PRK07994   360 HPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAP-----------AVPPPPASAPQQAPAVPLPETTSQLLA-ARQ 427
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  335 PLQQPARQGGPVKPSSQQAGPPKQLsqqpgpekPSAQQTGPAKQP-PQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQTAG 413
Cdd:PRK07994   428 QLQRAQGATKAKKSEPAAASRARPV--------NSALERLASVRPaPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKA 499
                          170
                   ....*....|.
gi 2051959432  414 PTKPPAQQPGP 424
Cdd:PRK07994   500 LKKALEHEKTP 510
PHA03379 PHA03379
EBNA-3A; Provisional
202-587 3.40e-04

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 46.98  E-value: 3.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  202 RSPAKHPTQPQSPKPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPKQVQKPGHRQPADAKQEQVKQPPQPR-------- 273
Cdd:PHA03379   441 QVPEPPPVHDLEPGPLHDQHSMAPCPVAQLPPGPLQDLEPGDQLPGVVQDGRPACAPVPAPAGPIVRPWEASlsqvpgva 520
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  274 -GPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARQgGPVKPSSQQ 352
Cdd:PHA03379   521 fAPVMPQPMPVEPVPVPTVALERPVCPAPPLIAMQGPGETSGIVRVRERWRPAPWTPNPPRSPSQMSVRD-RLARLRAEA 599
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  353 AGPPKQLSQQPgPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAG-PTKPPSQTAGPTKPPAQQPGPTKP--SG 429
Cdd:PHA03379   600 QPYQASVEVQP-PQLTQVSPQQPMEYPLEPEQQMFPGSPFSQVADVMRAGGvPAMQPQYFDLPLQQPISQGAPLAPlrAS 678
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  430 QQPGPEKPLEQKQAGASQPTESVSKKT----FCPLCTTTELLLhtPEKANYNTCTQCHTVVcslcgfnpnphiTEISEWL 505
Cdd:PHA03379   679 MGPVPPVPATQPQYFDIPLTEPINQGAsaahFLPQQPMEGPLV--PERWMFQGATLSQSVR------------PGVAQSQ 744
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  506 CLNCQMQRALGGDLAAGHGPgPQPPAPKQKTP--IPPSTAKPSPQPQPVqkkditskpdPSQLADPKKPPPQKKQTPLPG 583
Cdd:PHA03379   745 YFDLPLTQPINHGAPAAHFL-HQPPMEGPWVPeqWMFQGAPPSQGTDVV----------QHQLDALGYVLHVLNHPGVPV 813

                   ....
gi 2051959432  584 SPPV 587
Cdd:PHA03379   814 SPAV 817
PDZ4_INAD-like cd23065
PDZ domain 4 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
4544-4620 3.65e-04

PDZ domain 4 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of INAD, and related domains. INAD assembles key enzymes of the Drosophila compound eye photo-transduction pathway into a supramolecular complex, supporting efficient and fast light signaling. It contains 5 PDZ domains arranged in tandem (PDZ1-PDZ5) which independently bind various proteins. INAD PDZ2 binds eye-specific protein kinase C, INAD PDZ3 binds transient receptor potential (TRP) channel, and INAD PDZ4,5 tandem binds NORPA (phospholipase Cbeta, PLCbeta). Mutations of the inaD gene that lead to disruption of each of these interactions impair fly photo signal transduction. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This INAD-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467278 [Multi-domain]  Cd Length: 82  Bit Score: 42.12  E-value: 3.65e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2051959432 4544 VSGNGLGIRVVGGKEipgsSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSIIIQQSGEAEI 4620
Cdd:cd23065      6 TDKSPLGVSVVGGKN----HVTTGCIITHIYPNSIVAADKRLKVFDQILDINGTKVHVMTTLKVHQLFHKTYEKAVT 78
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
346-436 3.73e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 46.73  E-value: 3.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  346 VKPSSQQAGPPKQLSQQPGPEKPsAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQ-AGPTKPPSQTAGPTKPPAQQPGP 424
Cdd:PRK14950   361 VPVPAPQPAKPTAAAPSPVRPTP-APSTRPKAAAAANIPPKEPVRETATPPPVPPRpVAPPVPHTPESAPKLTRAAIPVD 439
                           90
                   ....*....|..
gi 2051959432  425 TKPSGQQPGPEK 436
Cdd:PRK14950   440 EKPKYTPPAPPK 451
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
268-446 3.88e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 46.77  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  268 QPPQPRGPQKSQPQPSePAKPVQQQTSAKLSSGPTkPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARQGGPVK 347
Cdd:PRK07003   373 PARVAGAVPAPGARAA-AAVGASAVPAVTAVTGAA-GAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVP 450
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  348 PSSQQAGPPKQLSQQPGPEKPSAQQTGPAkqppqPGSGKPPLQQTGPVkqvPPQAGPTKPPSQTAGPTKPPAQQPGPTKP 427
Cdd:PRK07003   451 AKANARASADSRCDERDAQPPADSGSASA-----PASDAPPDAAFEPA---PRAAAPSAATPAAVPDARAPAAASREDAP 522
                          170       180
                   ....*....|....*....|
gi 2051959432  428 SGQ-QPGPEKPLEQKQAGAS 446
Cdd:PRK07003   523 AAAaPPAPEARPPTPAAAAP 542
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
4549-4620 4.07e-04

PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of LNX1 (also known as PDZ domain-containing RING finger protein 2, PDZRN2) and LNX2 (also known as PDZ domain-containing RING finger protein 1, PDZRN1), and related domains. LNX1 and LNX2 are Ring (Really Interesting New Gene) finger and PDZ domain-containing E3 ubiquitin ligases that bind to the cell fate determinant protein NUMB and mediate its ubiquitination. LNX1 can ubiquitinate a number of other ligands including PPFIA1, KLHL11, KIF7 and ERC2. LNX1 and LNX2 each have four PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This LNX family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467167 [Multi-domain]  Cd Length: 88  Bit Score: 42.24  E-value: 4.07e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432 4549 LGIRVVGGKEIPgsSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSIIIQQSGEAEI 4620
Cdd:cd06679     13 LGISVAGGRGSR--RGDLPIYVTNVQPDGCLGRDGRIKKGDVLLSINGISLTNLSHSEAVAVLKASAASSSI 82
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
267-463 4.11e-04

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 46.19  E-value: 4.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  267 KQPPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPtkPSPQQPDSAKTTSQAPPPTkpSSQQPGPAKQPLQQPARQGGPV 346
Cdd:pfam05539  166 KEPKTAVTTSKTTSWPTEVSHPTYPSQVTPQSQPA--TQGHQTATANQRLSSTEPV--GTQGTTTSSNPEPQTEPPPSQR 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  347 KPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQTA--------GPTKPP 418
Cdd:pfam05539  242 GPSGSPQHPPSTTSQDQSTTGDGQEHTQRRKTPPATSNRRSPHSTATPPPTTKRQETGRPTPRPTAttqsgsspPHSSPP 321
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2051959432  419 AQQPGPTKPSG------QQPGPEKPLeqKQAGASQPTESVSKKTFCPLCTT 463
Cdd:pfam05539  322 GVQANPTTQNLvdckelDPPKPNSIC--YGVGIYNEALPRGCDIVVPLCST 370
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
526-733 4.41e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 46.46  E-value: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  526 GPQPPAPKQKTPIPPStakPSPQPQPVQKKDITSKP-DPSQLADPKKPPPQKKQTPLPGSPP-VKSKQPRAEPTEISQQT 603
Cdd:PLN03209   338 GPKPVPTKPVTPEAPS---PPIEEEPPQPKAVVPRPlSPYTAYEDLKPPTSPIPTPPSSSPAsSKSVDAVAKPAEPDVVP 414
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  604 R-DATPKSDQVKPTQAEDKQ-------------KQPSVQKPTADT-------------------VSTSAALEQKQDLAGP 650
Cdd:PLN03209   415 SpGSASNVPEVEPAQVEAKKtrplspyaryedlKPPTSPSPTAPTgvspsvsstssvpavpdtaPATAATDAAAPPPANM 494
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  651 RPPTQQKVTDSPKPELAKPSQDTHPAEDKPDSKPVPQVSRQKSDPKLAS-QPGARPDakaQKPVEPTQTKDDPKKlPTKP 729
Cdd:PLN03209   495 RPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADeQHHAQPK---PRPLSPYTMYEDLKP-PTSP 570

                   ....
gi 2051959432  730 APKP 733
Cdd:PLN03209   571 TPSP 574
PDZ7_PDZD2-PDZ4_hPro-IL-16-like cd06763
PDZ domain 7 of PDZ domain containing 2 (PDZD2), PDZ domain 4 of human pro-interleukin-16 ...
4548-4611 4.47e-04

PDZ domain 7 of PDZ domain containing 2 (PDZD2), PDZ domain 4 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of PDZD2, also known as KIAA0300, PIN-1, PAPIN, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family include the PDZ domain of the secreted mature form of human interleukin-16 (IL-16); this is the fourth PDZ domain (PDZ4) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16). Precursor IL-16 is cleaved to produce pro-IL-16 and C-terminal mature IL-16. Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDZD2-like family PDZ7 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467244 [Multi-domain]  Cd Length: 86  Bit Score: 41.83  E-value: 4.47e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051959432 4548 GLGIRVVGGKEIPgsSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSII 4611
Cdd:cd06763     12 GLGFSLEGGKGSP--LGDRPLTIKRIFKGGAAEQSGVLQVGDEILQINGTSLQGLTRFEAWNII 73
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
270-404 4.52e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 46.63  E-value: 4.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  270 PQPRGPQKSQPQPSEPAKPVQQQTSAklSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPlqqPARQGGPVKPS 349
Cdd:PRK14951   366 PAAAAEAAAPAEKKTPARPEAAAPAA--APVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAP---AAAAPAAAPAA 440
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2051959432  350 SQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGP 404
Cdd:PRK14951   441 APAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEGD 495
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1086-1625 5.24e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 46.61  E-value: 5.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1086 IQRASQKEDPRIQQTRLTKTASYDRVLHEVQKEDEKLQEAKLAKTSSadKILHGVQKEDIKL---------------QET 1150
Cdd:COG5022    848 IQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSI--SSLKLVNLELESEiielkkslssdlienLEF 925
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1151 KLAKIPSADKILQGIQ-KEDPKLQQMKMAKALSadkiqpaVQKEDAQLQEVKLPKAASVDKiqHGIQKEDIKLQHEKIKK 1229
Cdd:COG5022    926 KTELIARLKKLLNNIDlEEGPSIEYVKLPELNK-------LHEVESKLKETSEEYEDLLKK--STILVREGNKANSELKN 996
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1230 TRsvdKIQEEDQKEETKLQRgKLSKTPSANKIPATTTADQKKplntveedKETVPPEKSTPHPEDKkeeitaeIKDHVAK 1309
Cdd:COG5022    997 FK---KELAELSKQYGALQE-STKQLKELPVEVAELQSASKI--------ISSESTELSILKPLQK-------LKGLLLL 1057
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1310 QKAEVEAPYKGLQ-AKEQEDV-KKEDLTTGISQEVLKTEKAQEEEIPVQTAPLPrtdhvEAVREKIEKEDDKSDTSSSqq 1387
Cdd:COG5022   1058 ENNQLQARYKALKlRRENSLLdDKQLYQLESTENLLKTINVKDLEVTNRNLVKP-----ANVLQFIVAQMIKLNLLQE-- 1130
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1388 qkspqglsdtgySSDGISSSLGEIPSHIPTDEKDLLKESNKKDTISQESPPSPSDLAKLestvlsileaqantlsDEKSA 1467
Cdd:COG5022   1131 ------------ISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAAL----------------SEKRL 1182
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1468 KSKELSETYGEQTKDQLKTKPLPVTPESYSSDEEDLKAIKEGEGtIVEEGKGTASSQaDYKEDHEGEDIPARRQQR--YD 1545
Cdd:COG5022   1183 YQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKL-ISEGWVPTEYST-SLKGFNNLNKKFDTPASMsnEK 1260
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1546 SVEDSSESENSpVPRRKRRTSVGSSSSDEYKRDDSQGSGDEEdFIRKQIIEMSADEDAS--GSEDDEFIRNQlkEISAAE 1623
Cdd:COG5022   1261 LLSLLNSIDNL-LSSYKLEEEVLPATINSLLQYINVGLFNAL-RTKASSLRWKSATEVNynSEELDDWCREF--EISDVD 1336

                   ..
gi 2051959432 1624 SQ 1625
Cdd:COG5022   1337 EE 1338
PHA03379 PHA03379
EBNA-3A; Provisional
525-750 5.65e-04

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 46.20  E-value: 5.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  525 PGP-QPPAPKQKTPIPPSTAKPSPQPQPVQKKDITSKPDPSQLADPKKPPPQKKQTPLPGSP-PVKS----KQPRAEPTE 598
Cdd:PHA03379   472 PGPlQDLEPGDQLPGVVQDGRPACAPVPAPAGPIVRPWEASLSQVPGVAFAPVMPQPMPVEPvPVPTvaleRPVCPAPPL 551
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  599 ISQQTRDATPKSDQVKPTQAedkqkqPSVQKPTAdtvstsaaleqkqdlagPRPPTQQKVTDSPKPELAKPSQDTHPAED 678
Cdd:PHA03379   552 IAMQGPGETSGIVRVRERWR------PAPWTPNP-----------------PRSPSQMSVRDRLARLRAEAQPYQASVEV 608
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  679 KPDSkpVPQVSRQksdpklasQPGARPDAKAQK--PVEPTQTKDDPKKLPTKPAPKPD----------TKAAPKGP-QAG 745
Cdd:PHA03379   609 QPPQ--LTQVSPQ--------QPMEYPLEPEQQmfPGSPFSQVADVMRAGGVPAMQPQyfdlplqqpiSQGAPLAPlRAS 678

                   ....*
gi 2051959432  746 AGPKP 750
Cdd:PHA03379   679 MGPVP 683
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
528-751 5.99e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.02  E-value: 5.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  528 QPPAPKQKTPIPPSTAKPSPQPQPVQKKDITSKPDPsqladpkkpppqkkqTPLPGSPPVKSKQPRAEPTEISQQTRdAT 607
Cdd:PRK12323   364 RPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAP---------------AAPPAAPAAAPAAAAAARAVAAAPAR-RS 427
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  608 PKSDQVKPTQAEDKQKQPSVQKPTADTVSTSAALEQKQdLAGPRPPTQQKVTDSPKPELAKPS----QDTHPAEDKPDSK 683
Cdd:PRK12323   428 PAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPA-AAGPRPVAAAAAAAPARAAPAAAPapadDDPPPWEELPPEF 506
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051959432  684 PVP-----------QVSRQKSDPKLASQPGARPDAKAQKPVEPTQTKDDPkkLPTKPAPKPDTKAAPKGPQAGAGPKPG 751
Cdd:PRK12323   507 ASPapaqpdaapagWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAA--TEPVVAPRPPRASASGLPDMFDGDWPA 583
Androgen_recep pfam02166
Androgen receptor;
304-437 6.83e-04

Androgen receptor;


Pssm-ID: 426632 [Multi-domain]  Cd Length: 501  Bit Score: 45.69  E-value: 6.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  304 PSPQQPDSAKttSQAPPPTKPSSQQPGPAKQPLQQPARQGGPVKPssQQAGPPKQlsqQPGPEKPSAQQTGPA------- 376
Cdd:pfam02166   32 PGPRHPEAAG--GAAPPGARLQHQQQQQQQVPQQPQQQESSPRQP--QASVQPQQ---AGDDGSPPAHNRGPAgylaled 104
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051959432  377 KQPPQPGSGKPPLQ---QTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGPTKPSGQQPGPEKP 437
Cdd:pfam02166  105 DEQPQPSQAQPAAEccpENGCVPEPGAAAAAGKGLPQQAVAPAAPDDDDSAAPSTLSLLGPSFP 168
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
254-412 7.02e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 7.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  254 GHRQPADAKQEQVKQPPqPRGPQKSQ----PQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSqAPPPTKPSSQQP 329
Cdd:PHA03307   773 ALLEPAEPQRGAGSSPP-VRAEAAFRrpgrLRRSGPAADAASRTASKRKSRSHTPDGGSESSGPARP-PGAAARPPPARS 850
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  330 GPAKQPLQQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPV-----------KQV 398
Cdd:PHA03307   851 SESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKLGPMppggpdprggfRRV 930
                          170
                   ....*....|....
gi 2051959432  399 PPQAGPTKPPSQTA 412
Cdd:PHA03307   931 PPGDLHTPAPSAAA 944
dnaA PRK14086
chromosomal replication initiator protein DnaA;
268-449 7.97e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 45.59  E-value: 7.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  268 QPPQPRGPQKSQPQ-PSEPAKPVQQQTSAKLSSGP--TKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPaRQGg 344
Cdd:PRK14086    96 APPPPHARRTSEPElPRPGRRPYEGYGGPRADDRPpgLPRQDQLPTARPAYPAYQQRPEPGAWPRAADDYGWQQQ-RLG- 173
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  345 pvKPSSQQAGPPKQLSQQPGPEKPSaqqtgPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGP 424
Cdd:PRK14086   174 --FPPRAPYASPASYAPEQERDREP-----YDAGRPEYDQRRRDYDHPRPDWDRPRRDRTDRPEPPPGAGHVHRGGPGPP 246
                          170       180
                   ....*....|....*....|....*
gi 2051959432  425 TKPSGQQPGPEKPLEQKQAGASQPT 449
Cdd:PRK14086   247 ERDDAPVVPIRPSAPGPLAAQPAPA 271
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
174-391 8.33e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 45.77  E-value: 8.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  174 ISDSDTTHEDAGRKQKVTPK---EQGKPEEQRSPAKHPTQPQSPKPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPKQV 250
Cdd:NF033838   243 AKLKEAVEKNVATSEQDKPKrraKRGVLGEPATPDKKENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAKD 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  251 QKPGHRQ--PA------------------DAKQEQVKQ-PPQPRGPQK-SQPQPSEPAKPVQQ------QTSAKLSSGPT 302
Cdd:NF033838   323 QKEEDRRnyPTntyktleleiaesdvkvkEAELELVKEeAKEPRNEEKiKQAKAKVESKKAEAtrlekiKTDRKKAEEEA 402
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  303 KPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPlQQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQP 382
Cdd:NF033838   403 KRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKP-EKPAEQPKAEKPADQQAEEDYARRSEEEYNRLTQQQPPKTEKPAQP 481

                   ....*....
gi 2051959432  383 GSGKPPLQQ 391
Cdd:NF033838   482 STPKTGWKQ 490
Amelin smart00817
Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin ...
192-435 8.63e-04

Ameloblastin precursor (Amelin); This family consists of several mammalian Ameloblastin precursor (Amelin) proteins. Matrix proteins of tooth enamel consist mainly of amelogenin but also of non-amelogenin proteins, which, although their volumetric percentage is low, have an important role in enamel mineralisation. One of the non-amelogenin proteins is ameloblastin, also known as amelin and sheathlin. Ameloblastin (AMBN) is one of the enamel sheath proteins which is though to have a role in determining the prismatic structure of growing enamel crystals.


Pssm-ID: 214832 [Multi-domain]  Cd Length: 411  Bit Score: 45.27  E-value: 8.63e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432   192 PKEQGKPEEQRSPAKHPTQPQSPKPAVQQQGQQRPTLQQTEsskpvpqqqqQPGEPKQVQKPGHRQPADAKQEQVKQPPQ 271
Cdd:smart00817   81 PREHETQQYEYSLPVHPPPLPSQPSLQPQQPGLKPFLQPTA----------LPTNQATPQKNGPQPPMHLGQPPLQQAEL 150
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432   272 PRGPQksQPQPSEpaKPVQQQTSAKLSSGPTKPSPQQpdSAKTTSQAPPPtKPSSQQPGPAKQPLQQPARQGgpvkpssq 351
Cdd:smart00817  151 PMIPP--QVAPSD--KPPQTELPLYDFADPQNPLLFQ--IAHLMSRGPMP-QNKQQHLYPGLFYMSYGANQL-------- 215
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432   352 qaGPPKQLSQQPGPEKPSAQQTGPAKQPPQPGSG-----------KPPLQQTGPVKQVPPQAGpTKPPSQTAG-PTKPPA 419
Cdd:smart00817  216 --GAPARLGAMSSEEMTGGRGAPHAYGALFPGLGgmrpglrgmpqNPAMQGDFTLEDDSPVAA-TKGPEKGEGgAQGSPI 292
                           250
                    ....*....|....*.
gi 2051959432   420 QQPGPTKPSGQQPGPE 435
Cdd:smart00817  293 PEAQGVDPENPALLSE 308
PDZ3_FL-whirlin-like cd06742
PDZ domain 3 of the full-length isoform of whirlin, PDZ domain 1 of the short isoform of ...
4549-4611 8.74e-04

PDZ domain 3 of the full-length isoform of whirlin, PDZ domain 1 of the short isoform of whirlin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of the full-length isoform of whirlin, PDZ domain 1 of the short isoform of whirlin, and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This whirlin family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467224 [Multi-domain]  Cd Length: 91  Bit Score: 41.19  E-value: 8.74e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051959432 4549 LGIRVVGGkeipGSSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSII 4611
Cdd:cd06742     13 LGIAIEGG----ANTKQPLPRVINIQRGGSAHNCGGLKVGHVILEVNGTSLRGLEHREAARLI 71
ECM1 pfam05782
Extracellular matrix protein 1 (ECM1); This family consists of several eukaryotic ...
269-394 9.64e-04

Extracellular matrix protein 1 (ECM1); This family consists of several eukaryotic extracellular matrix protein 1 (ECM1) sequences. ECM1 has been shown to regulate endochondral bone formation, stimulate the proliferation of endothelial cells and induce angiogenesis. Mutations in the ECM1 gene can cause lipoid proteinosis, a disorder which causes generalized thickening of skin, mucosae and certain viscera. Classical features include beaded eyelid papules and laryngeal infiltration leading to hoarseness.


Pssm-ID: 461739  Cd Length: 518  Bit Score: 45.22  E-value: 9.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  269 PPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTK--------PSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQpa 340
Cdd:pfam05782    9 PPQTRGLPVDHPDTSQHDPPFEGQSEVQPPPSQEAipvqeeelPPPQLPVEKKVDPPLPQEAIPLQEELPPPQLPIEQ-- 86
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2051959432  341 RQGGPVKPSSQQAGPPKQLSQQPGpekPSAQQTgpakqPPQPGSGKPPL--QQTGP 394
Cdd:pfam05782   87 KEIDPPFPQQEEITPSKQREEKPA---PLVGQG-----HPEPESWNPAQhcQQGRR 134
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
368-718 9.73e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 45.68  E-value: 9.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  368 PSAQQTGPAKqpPQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQTAGPTkpPAQQPGPTKPSGQQPGP-EKPLEQKQAGAS 446
Cdd:pfam05109  432 PTLNTTGFAA--PNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPT--PAGTTSGASPVTPSPSPrDNGTESKAPDMT 507
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  447 QPTESVSKKTfcPLCTTTELLLHTPeKANYNTCTQCHTvvcslcgfNPNPHITEISewlclncqmqralggdlaaghgPG 526
Cdd:pfam05109  508 SPTSAVTTPT--PNATSPTPAVTTP-TPNATSPTLGKT--------SPTSAVTTPT----------------------PN 554
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  527 PQPPAPKQKTPIP----PSTAKPSPQ-----PQPVQKKDITSKPDPsQLADPKKPPPQKKQTPLPGSPPvksKQPRAEPT 597
Cdd:pfam05109  555 ATSPTPAVTTPTPnatiPTLGKTSPTsavttPTPNATSPTVGETSP-QANTTNHTLGGTSSTPVVTSPP---KNATSAVT 630
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  598 EISQQTRDATPKSDQVKPTQAEDKQKQPSVQKPTADT-VSTSAALEQKQDLAGPRPP---TQQKVTDSPKPELAKPSQDT 673
Cdd:pfam05109  631 TGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMpLLTSAHPTGGENITQVTPAstsTHHVSTSSPAPRPGTTSQAS 710
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2051959432  674 HPAEDKPDSKPVPQVSRQKSDPKLASQPGArpdAKAQKPVEPTQT 718
Cdd:pfam05109  711 GPGNSSTSTKPGEVNVTKGTPPKNATSPQA---PSGQKTAVPTVT 752
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
261-455 9.81e-04

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 44.94  E-value: 9.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  261 AKQEQVKQPPQPRgpQKSQPQPSEPAKPVQQQTSAKLSSGPtkpspqqpdSAKTTSQAPPPTKPSSQQPGPAKQPLQQPA 340
Cdd:PTZ00436   173 ARKQELRKREKDR--ERARREDAAAAAAAKQKAAAKKAAAP---------SGKKSAKAAAPAKAAAAPAKAAAPPAKAAA 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  341 RQGGPVKPSSQQAGPPKQLSQQPG--PEKPSAQQTGPAKQ--PPQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQTAGptk 416
Cdd:PTZ00436   242 APAKAAAAPAKAAAPPAKAAAPPAkaAAPPAKAAAPPAKAaaPPAKAAAPPAKAAAAPAKAAAAPAKAAAAPAKAAA--- 318
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2051959432  417 PPAQQPGPTKPSGQQPGPEKPLEQKQAGASQPTESVSKK 455
Cdd:PTZ00436   319 PPAKAAAPPAKAATPPAKAAAPPAKAAAAPVGKKAGGKK 357
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
4545-4607 1.00e-03

PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 11 of MUPP1, PDZ domain 9 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ11 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467162 [Multi-domain]  Cd Length: 87  Bit Score: 41.11  E-value: 1.00e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051959432 4545 SGNGLGIRVVGGKEipgssgEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEV 4607
Cdd:cd06674     12 PGRGLGLSIVGKRN------DTGVFVSDIVKGGAADADGRLMQGDQILSVNGEDVRNASQEAA 68
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
252-353 1.01e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 45.15  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  252 KPGHRQPADAKQEQVKQPPQPRGPQKS-QPQPSEPAKPVQQQTSA-KLSSGPTKPSPQQPDSAkTTSQAPPPTKPSSQQP 329
Cdd:PRK14971   380 KPVFTQPAAAPQPSAAAAASPSPSQSSaAAQPSAPQSATQPAGTPpTVSVDPPAAVPVNPPST-APQAVRPAQFKEEKKI 458
                           90       100
                   ....*....|....*....|....
gi 2051959432  330 GPAKQPLQQPARQgGPVKPSSQQA 353
Cdd:PRK14971   459 PVSKVSSLGPSTL-RPIQEKAEQA 481
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
516-790 1.10e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  516 GGDLAAGHGPGPQPPAPKQkTPIPPSTAKPSPQPQPVQKKDITSKPDPSQLADPKKPPPQKKQTPLPGSPPVKSKQPRAE 595
Cdd:PRK07764   403 AAAPAAAPAPAAAAPAAAA-APAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPA 481
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  596 PTEISQQTRDATPKSDQVKPTQ------AEDKQKQPSV-QKPTADTVSTSAALEQKQDLAGPRPPT-------------- 654
Cdd:PRK07764   482 PAPPAAPAPAAAPAAPAAPAAPagaddaATLRERWPEIlAAVPKRSRKTWAILLPEATVLGVRGDTlvlgfstgglarrf 561
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  655 -QQKVTDSPKPELAKP---------SQDTHPAEDKPDSKPVPQVSR---QKSDPKLASQPGARPDAKAQK-PVEPTQTKD 720
Cdd:PRK07764   562 aSPGNAEVLVTALAEElggdwqveaVVGPAPGAAGGEGPPAPASSGppeEAARPAAPAAPAAPAAPAPAGaAAAPAEASA 641
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  721 DPkklPTKPAPKPDTKAAPKGPQAGAGPKPGPAQPAPQPQPPQKTPEQSRRFSLNLGGITDAPKPQPTTP 790
Cdd:PRK07764   642 AP---APGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAAT 708
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
4546-4607 1.12e-03

PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467253 [Multi-domain]  Cd Length: 89  Bit Score: 41.06  E-value: 1.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432 4546 GNGLGIRVVGGKEIPGSSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEV 4607
Cdd:cd06791     11 EQGLGITIAGYVGEKASGELSGIFVKSIIPGSAADQDGRIQVNDQIIAVDGVNLQGFTNQEA 72
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
4532-4615 1.24e-03

PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of harmonin isoforms a, b, and c, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This harmonin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467219 [Multi-domain]  Cd Length: 85  Bit Score: 40.70  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 4532 RLKLLRDPKDHtvsGNGLGIRVVGGKEIpgssgEIGAYIAKILPGGNAEQTGkLIEGMQVLEWNGIPLTGKTYEEVQSII 4611
Cdd:cd06737      1 KLRLVRLDRRG---PESLGFSVRGGLEH-----GCGLFVSHVSPGSQADNKG-LRVGDEIVRINGYSISQCTHEEVINLI 71

                   ....
gi 2051959432 4612 IQQS 4615
Cdd:cd06737     72 KTKK 75
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
282-434 1.26e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  282 PSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARQGGPVKPSSQQAGPPKQLSQ 361
Cdd:PHA03307   765 PAKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKSRSHTPDGGSESSGPARPPGAAAR 844
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051959432  362 QPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGPTKPSGQQPGP 434
Cdd:PHA03307   845 PPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKLGPMP 917
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
269-652 1.30e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  269 PPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTkPSSQQPGPAKQPLQQPARQGGPVKP 348
Cdd:PHA03307    19 EFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPP-PGPGTEAPANESRSTPTWSLSTLAP 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  349 -SSQQAGPPKQLSQQPGPEKPSAQQtgPAKQPPQPGSGKPPLQQTGPVKQVPPQ---AGPTKPPSQTAGPTKPPAQ---- 420
Cdd:PHA03307    98 aSPAREGSPTPPGPSSPDPPPPTPP--PASPPPSPAPDLSEMLRPVGSPGPPPAaspPAAGASPAAVASDAASSRQaalp 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  421 --------QPGPTKPSgqQPGPEKPLEQKQAGASQPTESVSKKTFCPlcttTELLLHTPEKANYNTCTQCHTVVCSLCGF 492
Cdd:PHA03307   176 lsspeetaRAPSSPPA--EPPPSTPPAAASPRPPRRSSPISASASSP----APAPGRSAADDAGASSSDSSSSESSGCGW 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  493 -----NPNPHITEISEwlcLNCQMQRALGGDLAAGHGPGPQPPAPKQKTPIP-PSTAKPSPQPQPVQKKDITSKPDPSQL 566
Cdd:PHA03307   250 gpeneCPLPRPAPITL---PTRIWEASGWNGPSSRPGPASSSSSPRERSPSPsPSSPGSGPAPSSPRASSSSSSSRESSS 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  567 ADPKKPPPQKKQTPLPGSPPVKSKQPRAEPTEisqqTRDATPKSDQVKPTQAEDKQKQPSVQKPTADTVSTSAALEQKQD 646
Cdd:PHA03307   327 SSTSSSSESSRGAAVSPGPSPSRSPSPSRPPP----PADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRD 402

                   ....*.
gi 2051959432  647 LAGPRP 652
Cdd:PHA03307   403 ATGRFP 408
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
4531-4611 1.37e-03

PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467285 [Multi-domain]  Cd Length: 92  Bit Score: 40.94  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 4531 TRLKLLRDPKdhtvsgNGLGIRVVGGkEIPGSSgEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSI 4610
Cdd:cd23072      3 TLVNLKKDAK------YGLGFQIVGG-EKSGRL-DLGIFISSITPGGPADLDGRLKPGDRLISVNDVSLEGLSHDAAVEI 74

                   .
gi 2051959432 4611 I 4611
Cdd:cd23072     75 L 75
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1041-1631 1.51e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.96  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1041 QKEAPKLQQGRLEKTLSADKIQQGVQREDAKPKQGKLVKtpSADKIQR--ASQKEDPRIQQTRLTKTASYDRVLHEVQKE 1118
Cdd:pfam02463  224 EYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEK--EEEKLAQvlKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1119 DEKLQEAKlaktSSADKILHGVQKEDIKLQETKLAKIPSADKILQGIQKEDPKLQQMKMAKALSADKIQPAVQKEDAQLQ 1198
Cdd:pfam02463  302 LLKLERRK----VDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLA 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1199 EVKLPKAASV-DKIQHGIQKEdikLQHEKIKKTRSVDKI--QEEDQKEETKLQ----RGKLSKTPSANKIPATTTADQKK 1271
Cdd:pfam02463  378 KKKLESERLSsAAKLKEEELE---LKSEEEKEAQLLLELarQLEDLLKEEKKEeleiLEEEEESIELKQGKLTEEKEELE 454
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1272 PLNTVEEDKETVPPEKSTPHPEDK--KEEITAEIKDHVAKQKAEVEAPYKGLQAKEQEDVKKEDLTTGISQEVLKTEKAQ 1349
Cdd:pfam02463  455 KQELKLLKDELELKKSEDLLKETQlvKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDL 534
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1350 EEEIPVQTAPLPRTDHVEAVREKIEKEDDKSDTSSSQQQKSPQGLSDTGYSSDGISSSLGEIPSHIPTD-EKDLLKESNK 1428
Cdd:pfam02463  535 GVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILnLAQLDKATLE 614
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1429 KDTISQESPPSPSDLAKLESTVLSILEAQANTLSDEKSAKSKELSETYGEQTKDQLKTKPLPVTPESYSSDEEDLKAIKE 1508
Cdd:pfam02463  615 ADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEI 694
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 1509 G---EGTIVEEGKGTASSQADYKEDHEGEDIPARRQQRydsvedsseseNSPVPRRKRRTSVGSSSSDEYKRDDSQGSGD 1585
Cdd:pfam02463  695 LrrqLEIKKKEQREKEELKKLKLEAEELLADRVQEAQD-----------KINEELKLLKQKIDEEEEEEEKSRLKKEEKE 763
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2051959432 1586 EEDFIRKQIIEMSADEDAS------GSEDDEFIRNQLKEISAAESQKKEEVK 1631
Cdd:pfam02463  764 EEKSELSLKEKELAEEREKteklkvEEEKEEKLKAQEEELRALEEELKEEAE 815
PHA03377 PHA03377
EBNA-3C; Provisional
262-768 1.52e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 45.04  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  262 KQEQVKQPPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPtkpspqqPDSAKTTSQAPPPtkPSSQQPGPAKQPLQQPAR 341
Cdd:PHA03377   442 EAEQAQSTPERPGPSDQPSVPVEPAHLTPVEHTTVILHQP-------PQSPPTVAIKPAP--PPSRRRRGACVVYDDDII 512
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  342 QGGPVKPSSQQAGppkqlSQQPGPEKPSAQQTGPAKQPPQPGSGKPPLQ--QTGPVKQVPPQAGP--TKPPSQTAGPTKP 417
Cdd:PHA03377   513 EVIDVETTEEEES-----VTQPAKPHRKVQDGFQRSGRRQKRATPPKVSpsDRGPPKASPPVMAPpsTGPRVMATPSTGP 587
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  418 PAQQPGPTKPSGQQPGPEKPleqkqaGASQPTESVSKKTFCPLCTTTELLLHTPEKANYNTctqchtvvcslcgFNPNPH 497
Cdd:PHA03377   588 RDMAPPSTGPRQQAKCKDGP------PASGPHEKQPPSSAPRDMAPSVVRMFLRERLLEQS-------------TGPKPK 648
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  498 iteiSEWlclncQMQralggdlAAGHGPGP-QPPAPKQKTPIPPSTAKPSPQPQPVQKKDI-TSKPDPSQLADPKKPPpq 575
Cdd:PHA03377   649 ----SFW-----EMR-------AGRDGSGIqQEPSSRRQPATQSTPPRPSWLPSVFVLPSVdAGRAQPSEESHLSSMS-- 710
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  576 kkqtplPGSPPVKSKQPRAE----PTEISQQTRDATPKSDQVKPTQAEDKQKQ----PSVQKPTADTVStsaaleqkqdL 647
Cdd:PHA03377   711 ------PTQPISHEEQPRYEdpddPLDLSLHPDQAPPPSHQAPYSGHEEPQAQqapyPGYWEPRPPQAP----------Y 774
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  648 AGPRPPTQQKVTDSPKPELAKP--SQDTHPAEDKP----DSKPV---PQVSRQKSDPKLASQ--PGARPDAKAQKPVEPT 716
Cdd:PHA03377   775 LGYQEPQAQGVQVSSYPGYAGPwgLRAQHPRYRHSwaywSQYPGhghPQGPWAPRPPHLPPQwdGSAGHGQDQVSQFPHL 854
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  717 QTKDDPKKLPTKPAPK------PDTKAAPK--GPQAGAGPKPgpaqpAPQPQPPQKTPEQ 768
Cdd:PHA03377   855 QSETGPPRLQLSQVPQlpysqtLVSSSAPSwsSPQPRAPIRP-----IPTRFPPPPMPLQ 909
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
4550-4611 1.81e-03

PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 PDZ domains). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDLIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467235 [Multi-domain]  Cd Length: 79  Bit Score: 39.82  E-value: 1.81e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051959432 4550 GIRVVGGKE--IPgssgeigAYIAKILPGGNAEQTGkLIEGMQVLEWNGIPLTGKTYEEVQSII 4611
Cdd:cd06753     11 GFRLQGGKDfnQP-------LTISRVTPGGKAAQAN-LRPGDVILAINGESTEGMTHLEAQNKI 66
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
528-735 1.82e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 44.68  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  528 QPPAPKQ-KTPIPPSTAKPSPQPQPVQKKDITSKPDPSQLADPKKPPPQKKQTPLPGSP--PVKSKQP-RAEPTEISQQT 603
Cdd:PTZ00449   578 KPEFPKDpKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPppPQRPSSPeRPEGPKIIKSP 657
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  604 RdaTPKSDQV------KPTQAEDKQKQPSVQKPTADTVSTSAALEQKQDLAGPRPPTQQKVTDSP-KPELAKPSQDTHPA 676
Cdd:PTZ00449   658 K--PPKSPKPpfdpkfKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPRPlPPKLPRDEEFPFEP 735
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  677 EDKPDSK----------PVPQVSRQKSDPKLASQPGARPD-AKAQKPVEPTQTKDDPKKLPTKPAPKPDT 735
Cdd:PTZ00449   736 IGDPDAEqpddiefftpPEEERTFFHETPADTPLPDILAEeFKEEDIHAETGEPDEAMKRPDSPSEHEDK 805
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
4535-4616 1.91e-03

PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5, and belongs to this MAGI1,2,3-like family. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467217 [Multi-domain]  Cd Length: 84  Bit Score: 40.25  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 4535 LLRDPKdhtvsGNGLGIRvvGGKEipgsSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEevQSI-IIQ 4613
Cdd:cd06735      6 LERGPK-----GFGFSIR--GGRE----YNNMPLYVLRLAEDGPAQRDGRLRVGDQILEINGESTQGMTHA--QAIeLIR 72

                   ...
gi 2051959432 4614 QSG 4616
Cdd:cd06735     73 SGG 75
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
525-688 1.96e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 44.47  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  525 PGPQPPAPKQKTPIPPSTAKPSPQPQPVQkkditsKPDPSQLADPKKPPPQKKQTPLPGSPPVKSKQPRAEPTeiSQQTR 604
Cdd:PRK07994   364 PLPEPEVPPQSAAPAASAQATAAPTAAVA------PPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQ--RAQGA 435
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  605 DATPKSdqvKPTQAEDKQKQPSVQKPTADTVSTSAALEQKQDLAGPRPPTQQKVTDSPKPELAKPSQDTHPAEDKPDSKP 684
Cdd:PRK07994   436 TKAKKS---EPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKALEHEKTPEL 512

                   ....
gi 2051959432  685 VPQV 688
Cdd:PRK07994   513 AAKL 516
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
203-343 2.04e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 44.38  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  203 SPAKHPTQPQspKPAVQQQGQQRPTLQQTesskpvpqqqqqpgepkqvqkpghrQPADAKQEQVKQPPQPRGPQKSQPQP 282
Cdd:PRK14971   370 SGGRGPKQHI--KPVFTQPAAAPQPSAAA-------------------------AASPSPSQSSAAAQPSAPQSATQPAG 422
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2051959432  283 SEPAKPVQQQTSAKLSSgPTKPSPQQPDSAKTTSQAPPPTKPSSQQPgPAKQPLQQPARQG 343
Cdd:PRK14971   423 TPPTVSVDPPAAVPVNP-PSTAPQAVRPAQFKEEKKIPVSKVSSLGP-STLRPIQEKAEQA 481
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
188-378 2.11e-03

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 44.18  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  188 QKVTPKEQGKPEEQRSPAK-HPTQPQSPKPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPKQVQKPGHRQPADAKQEQV 266
Cdd:PTZ00441   267 EGCTTHMVEECEEEECPVEpEPLPVPAPVPPTPEDDNPRPTDDEFAVPNFNEGLDVPDNPQDPVPPPNEGKDGNPNEENL 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  267 KQPPQPRGPQKSQPQPSEPAKPvQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARQGGPV 346
Cdd:PTZ00441   347 FPPGDDEVPDESNVPPNPPNVP-GGSNSEFSSDVENPPNPPNPDIPEQEPNIPEDSNKEVPEDVPMEPEDDRDNNFNEPK 425
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2051959432  347 KPSSQQAGPPKQLSqqPGPEKPSAQQTGPAKQ 378
Cdd:PTZ00441   426 KPENKGDGQNEPVI--PKPLDNERDQSNKNKQ 455
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
173-461 2.17e-03

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 44.15  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  173 LISDSDTTHedagrkQKVTPKEQGKPEEQRSpaKHPTQPQSPKPAVQQQgqqrPTLQQTESSkpVPQQQQQPGEPKQVQK 252
Cdd:cd22540    212 LVGTQDGAT------QLQLAAAPSKPSKKIR--KKSAQAAQPAVTVAEQ----VETVLIETT--ADNIIQAGNNLLIVQS 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  253 PGHRQPADAKQEQVKqppQPRGPQKSQPQPSEPAKPVQQQtSAKLSSGPTKP--SPQQPDSAKTTSQAPPPTkPSSQQPG 330
Cdd:cd22540    278 PGTGQPAVLQQVQVL---QPKQEQQVVQIPQQALRVVQAA-SATLPTVPQKPlqNIQIQNSEPTPTQVYIKT-PSGEVQT 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  331 PAKQPLQQPARQGGPVKPSSQQAGPPkqLSQQPGPEKPSAQQTGPAKQPPQPGSG-----KPPLQQTGPVKQVPPQAGpT 405
Cdd:cd22540    353 VLLQEAPAATATPSSSTSTVQQQVTA--NNGTGTSKPNYNVRKERTLPKIAPAGGiislnAAQLAAAAQAIQTINING-V 429
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2051959432  406 KPPSQTAGPTKPPAQQPGPTKP--------SGQQPGP-EKPLEQKQAGASQPTESVSK-KTFCPLC 461
Cdd:cd22540    430 QVQGVPVTITNAGGQQQLTVQTvssnnltiSGLSPTQiQLQMEQALEIETQPGEKRRRmACTCPNC 495
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
305-443 2.18e-03

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 42.08  E-value: 2.18e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432   305 SPQQPDSAKTTSQAPPPTKPsSQQPGPAKQPL-QQPARQggPVKPSSQqagppkqlsQQPGPEKPSAQQTGPakQPPQPG 383
Cdd:smart00818   43 SQQHPPTHTLQPHHHIPVLP-AQQPVVPQQPLmPVPGQH--SMTPTQH---------HQPNLPQPAQQPFQP--QPLQPP 108
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432   384 SGKPPLQQTGPVKQVPPQagptkpPSQTAGPTKPPAQQPGPTKpsgqqpgPEKPLEQKQA 443
Cdd:smart00818  109 QPQQPMQPQPPVHPIPPL------PPQPPLPPMFPMQPLPPLL-------PDLPLEAWPA 155
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
4573-4618 2.43e-03

PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467169 [Multi-domain]  Cd Length: 89  Bit Score: 39.91  E-value: 2.43e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2051959432 4573 ILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSIIIQQSGEA 4618
Cdd:cd06681     37 VRPGGPADREGTIKPGDRLLSVDGISLHGATHAEAMSILKQCGQEA 82
PRK12757 PRK12757
cell division protein FtsN; Provisional
341-456 2.59e-03

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 43.11  E-value: 2.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  341 RQGGPVKPSSQQAGPPKQLSQQPGPEKPS--AQQTGPAKQPPQPGSGKPPLQQTGPVKQV----PPQAGPTKPPSQTA-- 412
Cdd:PRK12757    58 RQIGVPTPTEPSAGGEVNSPTQLTDEQRQllEQMQADMRQQPTQLSEVPYNEQTPQVPRStvqiQQQAQQQQPPATTAqp 137
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2051959432  413 GPTKPPAQQPGPTKPSGQQPGPEKPLEQKQAGASQPTESVSKKT 456
Cdd:PRK12757   138 QPVTPPRQTTAPVQPQTPAPVRTQPAAPVTQAVEAPKVEAEKEK 181
PRK12757 PRK12757
cell division protein FtsN; Provisional
319-452 2.68e-03

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 43.11  E-value: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  319 PPPTKPSSQQPGPAKQPLQQPARQggpvKPSSQQAG---PPKQLSQQPGPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPV 395
Cdd:PRK12757    63 PTPTEPSAGGEVNSPTQLTDEQRQ----LLEQMQADmrqQPTQLSEVPYNEQTPQVPRSTVQIQQQAQQQQPPATTAQPQ 138
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051959432  396 KQVPPQAGPTKPPSQTAGPTKPPAQQPGPTKPSGQQPGPEKPLEQK---QAG---ASQPTESV 452
Cdd:PRK12757   139 PVTPPRQTTAPVQPQTPAPVRTQPAAPVTQAVEAPKVEAEKEKEQRwmvQCGsfkGTEQAESV 201
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
4531-4611 3.17e-03

PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of the full-length isoform of whirlin and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This whirlin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467222 [Multi-domain]  Cd Length: 82  Bit Score: 39.27  E-value: 3.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432 4531 TRLKLLRDPKDHTvsgnGLGIRVVGGKEipgsSGeIGAYIAKILPGGNAEQTGkLIEGMQVLEWNGIPLTGKTYEEVQSI 4610
Cdd:cd06740      1 VRQVTLKRSKSHE----GLGFSIRGGAE----HG-VGIYVSLVEPGSLAEKEG-LRVGDQILRVNDVSFEKVTHAEAVKI 70

                   .
gi 2051959432 4611 I 4611
Cdd:cd06740     71 L 71
PHA03269 PHA03269
envelope glycoprotein C; Provisional
600-738 3.22e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 43.56  E-value: 3.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  600 SQQTRDATPKSDQVKPTQAEDKQKQPSVQKPTAdtvstsaaleqkqdlagPRPPTQQKVTDSPKPELAKPSqdTHPAEDK 679
Cdd:PHA03269    21 NLNTNIPIPELHTSAATQKPDPAPAPHQAASRA-----------------PDPAVAPTSAASRKPDLAQAP--TPAASEK 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2051959432  680 PDSKPVP-QVSRQKSDPKLASQPGA--RPDAkAQKPVEPTQTKDDPKKLPTKPAPKPDTKAA 738
Cdd:PHA03269    82 FDPAPAPhQAASRAPDPAVAPQLAAapKPDA-AEAFTSAAQAHEAPADAGTSAASKKPDPAA 142
Not5 COG5665
CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];
587-749 3.38e-03

CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];


Pssm-ID: 444384 [Multi-domain]  Cd Length: 874  Bit Score: 43.88  E-value: 3.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  587 VKSKQPRAEPTEISQQTRDAT--PKSDQVKPTQAEDKQKQ-PSVQKPTADTVSTSAAleqkqdlAGPRPPTQQKVTDSPK 663
Cdd:COG5665    255 KSSQQPKSQPTSPSGGTTPPStnQLTTSNTPTSTAKAQPQpPTKKQPAKEPPSDTAS-------GNPSAPSVLINSDSPT 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  664 PELAKPSQDTHPAEDKPDSKP--VPQVSRQKS----DPKLASQPgARPDAKAQKPVEPtqtkDDPKKlPTKPAPKPDTKA 737
Cdd:COG5665    328 SEDPATASVPTTEETTAFTTPssVPSTPAEKDtpatDLATPVSP-TPPETSVDKKVSP----DSATS-STKSEKEGGTAS 401
                          170
                   ....*....|..
gi 2051959432  738 APKGPQAGAGPK 749
Cdd:COG5665    402 SPMPPNIAIGAK 413
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
318-459 3.42e-03

MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 42.67  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  318 APPPTKPSSQQPGPAKQPLQQParQGGP-VKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAkqppqPGSGKPPLQQTGPVK 396
Cdd:pfam15822    6 ALPEQSPAKTSAVSNPKPGQPP--QGWPgSNPWNNPSAPPAVPSGLPPSTAPSTVPFGPA-----PTGMYPSIPLTGPSP 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051959432  397 QVPPQAGPTKPPSQTAGPTKPPAQQPGPTkPSGQQPGPEKPLEQKQAGASQPTESVSKKTFCP 459
Cdd:pfam15822   79 GPPAPFPPSGPSCPPPGGPYPAPTVPGPG-PIGPYPTPNMPFPELPRPYGAPTDPAAAAPSGP 140
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
201-453 3.64e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 3.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  201 QRSPAKHPTQPQSPKPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPKQVQKPGHRQPADAKQEQVKQPPQPRGPQKSQP 280
Cdd:PRK07764   401 AAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAP 480
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  281 QPSEPAKPvQQQTSAKLSSGPTKPSPQQPDSA-----------------------KTTSQAPPPTKPS------------ 325
Cdd:PRK07764   481 APAPPAAP-APAAAPAAPAAPAAPAGADDAATlrerwpeilaavpkrsrktwailLPEATVLGVRGDTlvlgfstgglar 559
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  326 --SQQPGPA--KQPLQQ---------------PARQGGPVKPSSQQAGPPKQLSQ---QPGPEKPSAQQTGPAKQPPQPG 383
Cdd:PRK07764   560 rfASPGNAEvlVTALAEelggdwqveavvgpaPGAAGGEGPPAPASSGPPEEAARpaaPAAPAAPAAPAPAGAAAAPAEA 639
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2051959432  384 SGKPPLQQTGPVKQVPPQAGPT---KPPSQTAGPTKPPAQQPGPTKPSGQQPGPEKPLEQKQAGASQPTESVS 453
Cdd:PRK07764   640 SAAPAPGVAAPEHHPKHVAVPDasdGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAG 712
FimV COG3170
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];
198-435 3.69e-03

Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];


Pssm-ID: 442403 [Multi-domain]  Cd Length: 508  Bit Score: 43.24  E-value: 3.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  198 PEEQRSPAKHPTQ---PQSPKPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPKQVQKPGHRQPADAKQEQVKQPPQ--- 271
Cdd:COG3170    106 PPAYAAAAAAPAAapaPAPAAPAAAAAAADQPAAEAAPAASGEYYPVRPGDTLWSIAARPVRPSSGVSLDQMMVALYran 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  272 ------------PRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPpTKPSSQQPGPAKQPLQQP 339
Cdd:COG3170    186 pdafidgninrlKAGAVLRVPAAEEVAALSPAEARQEVQAQSADWAAYRARLAAAVEPAPA-AAAPAAPPAAAAAAGPVP 264
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  340 ARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQPgsgkppLQQTGPVKQVPPQAGPTKPPSQTAGPTKPPA 419
Cdd:COG3170    265 AAAEDTLSPEVTAAAAAEEADALPEAAAELAERLAALEAQLAE------LQRLLALKNPAPAAAVSAPAAAAAAATVEAA 338
                          250
                   ....*....|....*.
gi 2051959432  420 QQPGPTKPSGQQPGPE 435
Cdd:COG3170    339 APAAAAQPAAAAPAPA 354
PHA03269 PHA03269
envelope glycoprotein C; Provisional
270-376 3.75e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 43.56  E-value: 3.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  270 PQPRGPQKSQPQPSEPAKPVQQQTSAKL--SSGPTKPSPQQPDSAKTtsqappPTKPSSQQPGPAKQPLQQPARQGGP-V 346
Cdd:PHA03269    27 PIPELHTSAATQKPDPAPAPHQAASRAPdpAVAPTSAASRKPDLAQA------PTPAASEKFDPAPAPHQAASRAPDPaV 100
                           90       100       110
                   ....*....|....*....|....*....|
gi 2051959432  347 KPSSQQAGPPkqlsqQPGPEKPSAQQTGPA 376
Cdd:PHA03269   101 APQLAAAPKP-----DAAEAFTSAAQAHEA 125
PDZ1_Dlg1-2-4-like cd06723
PDZ domain 1 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
4546-4585 4.06e-03

PDZ domain 1 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Dlg1, human Dlg1,2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197 or SAP-97), Dlg2 (also known as channel-associated protein of synapse-110, postsynaptic density protein 93, or PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95, synapse-associated protein 90, or SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling. It regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord, and it also interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467206 [Multi-domain]  Cd Length: 89  Bit Score: 39.22  E-value: 4.06e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2051959432 4546 GNGLGIRVVGGKEIPGSSGEIGAYIAKILPGGNAEQTGKL 4585
Cdd:cd06723     10 NSGLGFSIAGGTDNPHIGDDPSIYITKIIPGGAAAADGRL 49
PRK10905 PRK10905
cell division protein DamX; Validated
257-433 4.06e-03

cell division protein DamX; Validated


Pssm-ID: 236792 [Multi-domain]  Cd Length: 328  Bit Score: 43.00  E-value: 4.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  257 QPADAKQEQVKQPPQPRGPQKSQpQPSEPAKPVQQQTSAKLSSGPTKP-SPQQPDSAKTTSQAPppTKPSSQQP-----G 330
Cdd:PRK10905    62 QTAGNTQQDVSLPPISSTPTQGQ-TPVATDGQQRVEVQGDLNNALTQPqNQQQLNNVAVNSTLP--TEPATVAPvrngnA 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  331 PAKQPLQQPARQGGPVKPSSQQAGPPkqlsqqpgPEKPSAQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQ 410
Cdd:PRK10905   139 SRQTAKTQTAERPATTRPARKQAVIE--------PKKPQATAKTEPKPVAQTPKRTEPAAPVASTKAPAATSTPAPKETA 210
                          170       180
                   ....*....|....*....|....*
gi 2051959432  411 TAGP--TKPPAQQPGPTKPSGQQPG 433
Cdd:PRK10905   211 TTAPvqTASPAQTTATPAAGGKTAG 235
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
3786-3849 4.12e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 42.94  E-value: 4.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051959432 3786 ARAKILQDIDRELDLVERESAKLRKKQAELDEEEKEIDaklrylEMGINRRKEALLKEREKRER 3849
Cdd:pfam07946  265 TREEEIEKIKKAAEEERAEEAQEKKEEAKKKEREEKLA------KLSPEEQRKYEEKERKKEQR 322
ECM1 pfam05782
Extracellular matrix protein 1 (ECM1); This family consists of several eukaryotic ...
318-435 4.21e-03

Extracellular matrix protein 1 (ECM1); This family consists of several eukaryotic extracellular matrix protein 1 (ECM1) sequences. ECM1 has been shown to regulate endochondral bone formation, stimulate the proliferation of endothelial cells and induce angiogenesis. Mutations in the ECM1 gene can cause lipoid proteinosis, a disorder which causes generalized thickening of skin, mucosae and certain viscera. Classical features include beaded eyelid papules and laryngeal infiltration leading to hoarseness.


Pssm-ID: 461739  Cd Length: 518  Bit Score: 43.29  E-value: 4.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  318 APPPTKPSSQQPgpakqPLQQP-ARQGGP-------VKPSSQQAGPPKQLSQQPGPEKPSAQQTGPakqpPQPGsGKPPL 389
Cdd:pfam05782    4 AAPPSPPQTRGL-----PVDHPdTSQHDPpfegqseVQPPPSQEAIPVQEEELPPPQLPVEKKVDP----PLPQ-EAIPL 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2051959432  390 QQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQPGPTKPSGQQPGPE 435
Cdd:pfam05782   74 QEELPPPQLPIEQKEIDPPFPQQEEITPSKQREEKPAPLVGQGHPE 119
Caprin-1_C pfam12287
Cytoplasmic activation/proliferation-associated protein-1 C term; This family of proteins is ...
308-409 4.26e-03

Cytoplasmic activation/proliferation-associated protein-1 C term; This family of proteins is found in eukaryotes. Proteins in this family are typically between 343 and 708 amino acids in length. This family is the C terminal region of caprin-1. Caprin-1 is a protein involved in regulating cellular proliferation. In mutated phenotypes, the G1 phase of the cell cycle is greatly lengthened, impairing normal proliferation. The C terminal region of caprin-1 contains RGG motifs which are characteriztic of RNA binding domains. It is possible that caprin-1 functions through an RNA binding mechanism.


Pssm-ID: 463522 [Multi-domain]  Cd Length: 320  Bit Score: 42.86  E-value: 4.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  308 QPDSAKTTSQAPPPTKPSSQQPGPAKQP----------LQQPAR-QGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPA 376
Cdd:pfam12287   25 PSDSAIVSAQPPSQSPDLSQMVCPPASPeqrlsqqsdvLQQPEQtQVSPVSPSSNACASSGSEYQFHTSEPPQPEAIDPI 104
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2051959432  377 ----KQPPQPGSGKPPLQQTGpvkqvPPQAGPTKPPS 409
Cdd:pfam12287  105 qssmSLPSELAPPSPPLSPAS-----QPQVFQSKPAS 136
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
263-421 4.47e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 43.26  E-value: 4.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  263 QEQVKQPPQPRGPQKSQPQPSEPAKPVQQQtsaklssGPTKPSPQQPDSAKTTSQAPPPTKPSSQqpgPAKQPLQQPARQ 342
Cdd:TIGR01628  374 QFMQLQPRMRQLPMGSPMGGAMGQPPYYGQ-------GPQQQFNGQPLGWPRMSMMPTPMGPGGP---LRPNGLAPMNAV 443
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051959432  343 GGPvkPSSQQAGPPKqLSQQPGPEKPSAQQtgpakqppqpgsgkPPLQQTGPVKQVPPQAGPTKPPSQTAGPTKPPAQQ 421
Cdd:TIGR01628  444 RAP--SRNAQNAAQK-PPMQPVMYPPNYQS--------------LPLSQDLPQPQSTASQGGQNKKLAQVLASATPQMQ 505
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
4548-4621 4.90e-03

PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467213 [Multi-domain]  Cd Length: 85  Bit Score: 39.12  E-value: 4.90e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2051959432 4548 GLGIRVVGGKEipgsSGEIgAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEV----QSIIIQQSGEAEIC 4621
Cdd:cd06731     12 GFGFTIIGGDE----PDEF-LQIKSVVPDGPAALDGKLRTGDVLVSVNDTCVLGYTHADVvklfQSIPIGQSVNLEVC 84
PRK11901 PRK11901
hypothetical protein; Reviewed
263-438 5.27e-03

hypothetical protein; Reviewed


Pssm-ID: 237015 [Multi-domain]  Cd Length: 327  Bit Score: 42.36  E-value: 5.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  263 QEQVKQPPQPRGPQKSQPQPSEPAKPvQQQTSAKLSSGPTKPSPQQPdsakttsqappptkPSSQQ----PGPAKQPLQQ 338
Cdd:PRK11901    91 NQSSPSAANNTSDGHDASGVKNTAPP-QDISAPPISPTPTQAAPPQT--------------PNGQQrielPGNISDALSQ 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  339 parQGGPVKPSSQQAGPPkqlsqqpgpekpsaQQTGPAKQPPQPGSGKPPLQQTGPVKQVPPQAGPTKPPSQTAGPTKPP 418
Cdd:PRK11901   156 ---QQGQVNAASQNAQGN--------------TSTLPTAPATVAPSKGAKVPATAETHPTPPQKPATKKPAVNHHKTATV 218
                          170       180
                   ....*....|....*....|
gi 2051959432  419 AQQPGPTKPSGQQPGPEKPL 438
Cdd:PRK11901   219 AVPPATSGKPKSGAASARAL 238
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
251-696 5.74e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.83  E-value: 5.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  251 QKPGHRQPADAKQEqVKQPPQPRGPQKSQP---QPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQ 327
Cdd:NF033839   165 ENPEHQKPTTPAPD-TKPSPQPEGKKPSVPdinQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIVALIKELDELKKQ 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  328 QPGPAKQPLQQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTgpaKQPPQPGSGKPPLQQTgPVKQVPPQAGPTKP 407
Cdd:NF033839   244 ALSEIDNVNTKVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGN---KKPSAPKPGMQPSPQP-EKKEVKPEPETPKP 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  408 PSQTAGPTKPPAQQPGPTKPSGQ-QPGPEKPLEQKQAGASQPTESVSKKtfcplctttelllhtPEKanyntctqchtvv 486
Cdd:NF033839   320 EVKPQLEKPKPEVKPQPEKPKPEvKPQLETPKPEVKPQPEKPKPEVKPQ---------------PEK------------- 371
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  487 cslcgfnPNPHITeisewlclncqmqralggdlaaghgpgPQPPAPKQKTPIPPSTAKPSPQPQPvqkkditSKPDPSQL 566
Cdd:NF033839   372 -------PKPEVK---------------------------PQPETPKPEVKPQPEKPKPEVKPQP-------EKPKPEVK 410
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  567 ADPKKPPPQKKQTPLPGSPPVKSKQPRAEPtEISQQTRDATPksdQVKPtqaedkqkQPSVQKPTADTVSTSAALEQKQD 646
Cdd:NF033839   411 PQPEKPKPEVKPQPEKPKPEVKPQPEKPKP-EVKPQPEKPKP---EVKP--------QPETPKPEVKPQPEKPKPEVKPQ 478
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 2051959432  647 LAGPRPPTQQkvtdsPKPELAKPSQDTHPAEDKPDSKPVPQVSRQKSDPK 696
Cdd:NF033839   479 PEKPKPDNSK-----PQADDKKPSTPNNLSKDKQPSNQASTNEKATNKPK 523
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
319-443 5.87e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.87  E-value: 5.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  319 PPPTKPSSQQPGPAKQPLQQPARQGGPVKPSSQQAGPPKQlSQQPGPEKPSAQQtGPAKQPPQPGSGKPPLQQTgPVKQV 398
Cdd:TIGR01628  380 PRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNGQPLGWPRM-SMMPTPMGPGGPL-RPNGLAPMNAVRAPSRNAQ-NAAQK 456
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2051959432  399 PPQAGPTKPPSQTAGPTKPPAQQP-------GPTKPSGQQPGPEKPLEQKQA 443
Cdd:TIGR01628  457 PPMQPVMYPPNYQSLPLSQDLPQPqstasqgGQNKKLAQVLASATPQMQKQV 508
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
290-377 7.06e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 42.96  E-value: 7.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  290 QQQTSAKLSSGPTKPSPQQPDSAKTTSQAPPPTKPSSQQPGPAKQPLQQPARQGGPVKPSSQQAGPPKQLSQQPGPEKPS 369
Cdd:PRK12270    34 ADYGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAV 113
                           90
                   ....*....|..
gi 2051959432  370 AQQT----GPAK 377
Cdd:PRK12270   114 EDEVtplrGAAA 125
PRK10927 PRK10927
cell division protein FtsN;
131-386 7.07e-03

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 41.97  E-value: 7.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  131 RESKSRTDFKEDQKPSMMPSFLSEAnplSAVtsVVNKFNPFDLISDSDTTHEDAGRKQKVT-------PKEQG---KPEE 200
Cdd:PRK10927    16 RRKKSTSRKKQRNLPAVSPAMVAIA---AAV--LVTFIGGLYFITHHKKEESETLQSQKVTgnglppkPEERWryiKELE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  201 QRSPA-KHPTQPQSP---KPAVQQQGQQRPTLQQTESSKPVPQQQQQPGEPKQvQKPGHRQ---------PADAKQEQVK 267
Cdd:PRK10927    91 SRQPGvRAPTEPSAGgevKTPEQLTPEQRQLLEQMQADMRQQPTQLVEVPWNE-QTPEQRQqtlqrqrqaQQLAEQQRLA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  268 QPPQprgpqksqpqpsEPAKPVQQQTsaklSSGPTKPSPQQPDsakttsqapPPTKPSSQQpgPAKQPLQQPARQGGpvK 347
Cdd:PRK10927   170 QQSR------------TTEQSWQQQT----RTSQAAPVQAQPR---------QSKPASTQQ--PYQDLLQTPAHTTA--Q 220
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2051959432  348 PSSQQAGPpkqLSQQPGPEKPSAQQTGPAKQPPQPGSGK 386
Cdd:PRK10927   221 SKPQQAAP---VTRAADAPKPTAEKKDERRWMVQCGSFR 256
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
263-364 8.46e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.10  E-value: 8.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  263 QEQVKQPPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKtTSQAPPPTKPSSQQPgPAKQPLQQPAR- 341
Cdd:TIGR01628  406 QQQFNGQPLGWPRMSMMPTPMGPGGPLRPNGLAPMNAVRAPSRNAQNAAQK-PPMQPVMYPPNYQSL-PLSQDLPQPQSt 483
                           90       100
                   ....*....|....*....|....*..
gi 2051959432  342 --QGGPVKPSSQ--QAGPPKQLSQQPG 364
Cdd:TIGR01628  484 asQGGQNKKLAQvlASATPQMQKQVLG 510
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
176-382 9.09e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.22  E-value: 9.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  176 DSDTTHEDAGRKQKVTPKEQGKPEEQRSPAKHPTQ----------------PQSPKPAVQQQGQQRPTLQQTESSKPVPQ 239
Cdd:PLN03209   332 ESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVvprplspytayedlkpPTSPIPTPPSSSPASSKSVDAVAKPAEPD 411
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  240 QQQQPGEPKQV--QKPGhrqPADAKQEQvKQPPQPRGPQKSQPQPSEPAKPVQQQTSAKLSSGPTKPSPQQPDSAKTTSQ 317
Cdd:PLN03209   412 VVPSPGSASNVpeVEPA---QVEAKKTR-PLSPYARYEDLKPPTSPSPTAPTGVSPSVSSTSSVPAVPDTAPATAATDAA 487
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2051959432  318 APPPTKPSSQQPGPAKQPLQ-----QPARQGGPVKPSSQQAGPPKQLSQQPGPEKPSAQQTGPAKQPPQP 382
Cdd:PLN03209   488 APPPANMRPLSPYAVYDDLKpptspSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQPKPRPLSP 557
PDZ1_Par3-like cd06691
PDZ domain 1 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
4543-4610 9.37e-03

PDZ domain 1 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Par3 (or PAR3 or Par-3, also known as Atypical PKC isotype-specific-interacting protein, ASIP) and related domains; Drosophila bazooka PDZ1 belongs to a different PDZ family. Par3 is a scaffold protein involved in organizing cell polarity across animals. Par3 binds numerous molecules both for its recruitment to one pole of the cell and for downstream contributions to polarized cell function. It regulates cell polarity by targeting the Par complex proteins Par6 and atypical protein kinase C (aPKC) to specific cortical sites. Physical interactions between Par3 and the Par complex include: Par-3 PDZ domain 1 binding to the Par6 PDZ domain, Par3 PDZ domain 1 and PDZ domain 3 binding the Par6's PDZ-binding motif, and an interaction with an undefined region of aPKC that requires both Par3 PDZ2 and PDZ3. The PDZ domains of Par3 have also been implicated as potential phosphoinositide signaling integrators, since its second PDZ domain binds to phosphoinositides, and the third PDZ interacts with phosphoinositide phosphatase PTEN. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par3 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467178 [Multi-domain]  Cd Length: 98  Bit Score: 38.75  E-value: 9.37e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2051959432 4543 TVSGNG--LGIRVVggkeiP----GSSGEIGAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSI 4610
Cdd:cd06691      9 ELSNDGgpLGIHVV-----PfsssLSGRTLGLLIRGIEEGSRAERDGRFQENDCIVEINGVDLIDKSFEQAQDI 77
PDZ1_APBA1_3-like cd06720
PDZ domain 1 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, ...
4546-4611 9.91e-03

PDZ domain 1 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, APBA3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of APBA1, APBA2, APBA3, and related domains. The APBA/X11/Mint protein family includes three members: neuron specific APBA1 (also known as X11alpha and Mint1) and APBA2 (also known as X11beta and Mint2), and the ubiquitously expressed APBA3 (also known as (X12gamma and Mint3). They are involved in regulating neuronal signaling, trafficking and plasticity. They contain two PDZ domains (PDZ1 and PDZ2) which bind a variety of proteins: Arf GTPases (APBA1 and APBA2 PDZ2) and neurexin (APBA1 and APBA2 PDZ1 and 2), which are involved in vesicle docking and exocytosis; alpha1B subunit of N-type Ca2+ channel (APBA1 PDZ1) that is involved in ion channels; KIF17 (APBA1 PDZ1) that is involved in transport and traffic; and Alzheimer's disease related proteins such as APP (APBA3 PDZ2), CCS (APBA1 PDZ2), NF-kappa-B/p65 (APBA2 PDZ2), presenilin-1 (APBA1 and APBA2 PDZ1 and PDZ2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This APBA1,2,3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467203 [Multi-domain]  Cd Length: 86  Bit Score: 38.01  E-value: 9.91e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2051959432 4546 GNGLGIRVVG---GKEIPGssgeigAYIAKILPGGNAEQTGKLIEGMQVLEWNGIPLTGKTYEEVQSII 4611
Cdd:cd06720     10 GEILGVVIVEsgwGSLLPT------VVVANMMPGGPAARSGKLNIGDQIMSINGTSLVGLPLSTCQAII 72
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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