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Conserved domains on  [gi|2069550323|ref|XP_042325158|]
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protein piccolo isoform X3 [Sceloporus undulatus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 4793-4927 1.59e-66

C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology and do not bind Ca2+.


:

Pssm-ID: 175997 [Multi-domain]  Cd Length: 125  Bit Score: 221.74  E-value: 1.59e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4793 ITGEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRgqvmvvqnaSVENKRRTKYVQKSLNPEWNQT 4872
Cdd:cd04031      1 ITGRIQIQLWYDKVTSQLIVTVLQARDLPPRDDGSLRNPYVKVYLLPDR---------SEKSKRRTKTVKKTLNPEWNQT 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2069550323 4873 VIYKNISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELsSSSQLDNTPRWYTLK 4927
Cdd:cd04031     72 FEYSNVRRETLKERTLEVTVWDYDRDGENDFLGEVVIDL-ADALLDDEPHWYPLQ 125
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 4592-4687 1.22e-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: 169.27  E-value: 1.22e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4592 FPHARLKLPRDPKDHSVSGNGLGIRIVGGKEIPgtNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEV 4671
Cdd:cd06714      2 FLIGRIILQRDPKDGSVSGNGLGLKVVGGKMTE--SGRLGAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEV 79

                           90
                   ....*....|....*.
gi 2069550323 4672 QSIISQQSGEAEICVR 4687
Cdd:cd06714     80 QDIISQSKGEVELVVS 95
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 430-491 2.84e-43

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: 152.88  E-value: 2.84e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069550323  430 TFCPLCTTTELLLHTPEKANYNTCTQCQTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALGG 491
Cdd:cd15774      1 TICPLCKTTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 902-965 7.20e-41

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: 145.98  E-value: 7.20e-41
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069550323  902 SACPLCKTELNVGSKDPPNYNTCTECKNVVCNLCGFNPMPHITEVQEWLCLNCQTKRALSGQLG 965
Cdd:cd15776      1 LLCPLCKTELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQLG 64
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 5137-5262 1.91e-15

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


The actual alignment was detected with superfamily member cd04030:

Pssm-ID: 472691 [Multi-domain]  Cd Length: 127  Bit Score: 75.77  E-value: 1.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5137 GEIKIALkkEMKTDGEQLIVEILQCRNITykFKSPDHLPDLYVKLYVvnLATQKRVIKKKTRVCRHDREPSFNETFRFSL 5216
Cdd:cd04030      3 GRIQLTI--RYSSQRQKLIVTVHKCRNLP--PCDSSDIPDPYVRLYL--LPDKSKSTRRKTSVKKDNLNPVFDETFEFPV 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5217 SPTGHSLQILLVS--NGGKFM--KKTLIGEAYIWLDKVDLRKRIVNWHKL 5262
Cdd:cd04030     77 SLEELKRRTLDVAvkNSKSFLsrEKKLLGQVLIDLSDLDLSKGFTQWYDL 126
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 23-433 5.46e-11

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 69.97  E-value: 5.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323   23 PSEGPRLPSGEAPDLSQLSE--AERRQIAAVLSRAQDPS--PRHAQldsshhPRQPGKPPDSGP-PTLSKSRTVDTLKTE 97
Cdd:PHA03247  2552 PPPLPPAAPPAAPDRSVPPPrpAPRPSEPAVTSRARRPDapPQSAR------PRAPVDDRGDPRgPAPPSPLPPDTHAPD 2625

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323   98 QRVPGRSPSSISLRQSTSrtdfkedqKPSMMPSFLSDANPFGAVTSVVNKFNPFDLISDSDTAQ----EEASKKQKPIQK 173
Cdd:PHA03247  2626 PPPPSPSPAANEPDPHPP--------PTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQrprrRAARPTVGSLTS 2697

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  174 EQDKPGQQKGPSKQPVQQQS--PKPTGPQQGSVKPAPQKTAPPKQVVPQQQQQQQQQQQQPGVPKQAQKPGPGQQAGPQS 251
Cdd:PHA03247  2698 LADPPPPPPTPEPAPHALVSatPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA 2777

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  252 eeakkqqGAPKTQPQQSESTKTPPQQQQQSPAKPPPQQPGTARASPQQANASKTSSQVPTPTKATVAQQGISTGKQPSQQ 331
Cdd:PHA03247  2778 -------GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSL 2850

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  332 -------PGGPT--KPAPQSAGANKQATQQQGSAAKPAPQQTGPTKQQLQQPGEPAKPSAQQAGPTKQPQHQAEPtKPTG 402
Cdd:PHA03247  2851 plggsvaPGGDVrrRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPP-PPQP 2929

                          410       420       430
                   ....*....|....*....|....*....|.
gi 2069550323  403 QKPGPVQQKPEASPPQASQPGGSASKKTFCP 433
Cdd:PHA03247  2930 QPPPPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 329-730 6.14e-10

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 66.50  E-value: 6.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  329 SQQPGGPTKPAPqsAGANKQATQQQGSAAKPAPQQTGPTKQ-QLQQPGEPAKPSAQQA--GPTKQPQHQAEPTK--PTGQ 403
Cdd:PHA03247  2545 SDDAGDPPPPLP--PAAPPAAPDRSVPPPRPAPRPSEPAVTsRARRPDAPPQSARPRApvDDRGDPRGPAPPSPlpPDTH 2622

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  404 KPGPVQQKPEASPPQASQPGGSASKKTFCPLCTTTELLLHTPEKANyntcTQCQTVVCSLCGFNPNPhiteikewlclnc 483
Cdd:PHA03247  2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRAR----RLGRAAQASSPPQRPRR------------- 2685

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  484 qmqRALGGDLG--------PAPGPGPQSSAPKQKMAAPTTAGKPPPQAQQPTQKKESTVK--PDATQSPEHKKPPPPQTK 553
Cdd:PHA03247  2686 ---RAARPTVGsltsladpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPavPAGPATPGGPARPARPPT 2762

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  554 QPTIPSSTPEKAKPPAPE-----------TQQTESTPKSDQTKPAPAEDKQKQPHVQKPISDVVPKPSEFDTKQDSPGPK 622
Cdd:PHA03247  2763 TAGPPAPAPPAAPAAGPPrrltrpavaslSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPP 2842

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  623 PAPVQQKVvhPQGSEVAK----SSEDTPQDKTVPPDTKTSPQVSRqksdpklVSQPgsgidtKVQKQTEPVEGKGDLKKM 698
Cdd:PHA03247  2843 PGPPPPSL--PLGGSVAPggdvRRRPPSRSPAAKPAAPARPPVRR-------LARP------AVSRSTESFALPPDQPER 2907

                          410       420       430
                   ....*....|....*....|....*....|....
gi 2069550323  699 QPQ-MSPKPDAKQAQKPQQATVGPKP-TQSQPKA 730
Cdd:PHA03247  2908 PPQpQAPPPPQPQPQPPPPPQPQPPPpPPPRPQP 2941
PTZ00121 super family cl31754
MAEBL; Provisional
 989-1732 5.82e-09

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 5.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  989 QVKSAETPQQQKaSARPAQNEKRGPDIQKEDPASQQGKPAKAISADKIQEiVQKEHTTPQQEKLPKTISADKLSQSISGE 1068
Cdd:PTZ00121  1132 EARKAEDARKAE-EARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEA-ARKAEEVRKAEELRKAEDARKAEAARKAE 1209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1069 D----SEIQKG----KIGKPPSADQVPKEEAKVvRKSSADKLLEIVQKKEPKELEHVSDNIQIQKEDPKVQQIRLSKPPS 1140
Cdd:PTZ00121  1210 EerkaEEARKAedakKAEAVKKAEEAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1141 ---ADQIRKEDPKVQQVKLSKtpSADQIRKED---PKVQQVKlTKAPSADQIRKEDPKIQQVKLAKAPSADQiqedpKLQ 1214
Cdd:PTZ00121  1289 kkkADEAKKAEEKKKADEAKK--KAEEAKKADeakKKAEEAK-KKADAAKKKAEEAKKAAEAAKAEAEAAAD-----EAE 1360

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1215 QGKfvKTPSADKIRQEDPKIHQEKLTKvpSDSEIKKVDPKIQQAKLAKiPSADHIQKEDSKLFKAKIVKTAS-----ADQ 1289
Cdd:PTZ00121  1361 AAE--EKAEAAEKKKEEAKKKADAAKK--KAEEKKKADEAKKKAEEDK-KKADELKKAAAAKKKADEAKKKAeekkkADE 1435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1290 LPKD-NKFQEMELANIPVEDYISSKTIHDQTQVARRKEDDTKFP----LSRESLHLAESRQKVAGEQFDEEKiEPKVLPK 1364
Cdd:PTZ00121  1436 AKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAeeakKADEAKKKAEEAKKKADEAKKAAE-AKKKADE 1514

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1365 TRQQEDIKREDLMMDIPESISKDQ-KSPKEETSAPPV----PLPKPDHVEAIREKAEKEDDKSDASSSQQQKSPqglsdt 1439
Cdd:PTZ00121  1515 AKKAEEAKKADEAKKAEEAKKADEaKKAEEKKKADELkkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK------ 1588

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1440 gyssdgISSSLGEIPSLIQSEEKDVLKESCKKEilsqESSPTSPSDLAKLES-----TVLSILEAQASTLAEEKSGKSKD 1514
Cdd:PTZ00121  1589 ------AEEARIEEVMKLYEEEKKMKAEEAKKA----EEAKIKAEELKKAEEekkkvEQLKKKEAEEKKKAEELKKAEEE 1658

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1515 IYGVYSEHSRVPHKTKTQlgAPESYSADEEDLAKQNIQGKyggAPEEGDKQDILSQKSYKGKTDTREDASARRQRYDSV- 1593
Cdd:PTZ00121  1659 NKIKAAEEAKKAEEDKKK--AEEAKKAEEDEKKAAEALKK---EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAe 1733

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1594 -------EDSSESENSPVPQRKRRTSVGSSSSDDYKAEDSPGSG--------DDEDFIRKQIMEMSADEDASGSE----- 1653
Cdd:PTZ00121  1734 eakkeaeEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeavieeelDEEDEKRRMEVDKKIKDIFDNFAniieg 1813

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1654 ----------DDEFIRNQLKEISITDSHKKEEMKNKKGIPGKHKRMTRKSSTGyEDDTSRRHSWHDDDDETFDESPEPKY 1723
Cdd:PTZ00121  1814 gkegnlvindSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNK-EADFNKEKDLKEDDEEEIEEADEIEK 1892


                   ....*....
gi 2069550323 1724 RETKSQDSE 1732
Cdd:PTZ00121  1893 IDKDDIERE 1901
CCDC47 super family cl46382
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 3856-3919 5.42e-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: 42.55  E-value: 5.42e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069550323 3856 ARAKILQDIDRELDLVERESAKLRKKQAELDEEEKEIDaklrylEMGINRRKEALLKEREKRER 3919
Cdd:pfam07946  265 TREEEIEKIKKAAEEERAEEAQEKKEEAKKKEREEKLA------KLSPEEQRKYEEKERKKEQR 322
 
Name Accession Description Interval E-value
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 4793-4927 1.59e-66

C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology and do not bind Ca2+.


Pssm-ID: 175997 [Multi-domain]  Cd Length: 125  Bit Score: 221.74  E-value: 1.59e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4793 ITGEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRgqvmvvqnaSVENKRRTKYVQKSLNPEWNQT 4872
Cdd:cd04031      1 ITGRIQIQLWYDKVTSQLIVTVLQARDLPPRDDGSLRNPYVKVYLLPDR---------SEKSKRRTKTVKKTLNPEWNQT 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2069550323 4873 VIYKNISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELsSSSQLDNTPRWYTLK 4927
Cdd:cd04031     72 FEYSNVRRETLKERTLEVTVWDYDRDGENDFLGEVVIDL-ADALLDDEPHWYPLQ 125
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 4592-4687 1.22e-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: 169.27  E-value: 1.22e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4592 FPHARLKLPRDPKDHSVSGNGLGIRIVGGKEIPgtNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEV 4671
Cdd:cd06714      2 FLIGRIILQRDPKDGSVSGNGLGLKVVGGKMTE--SGRLGAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEV 79

                           90
                   ....*....|....*.
gi 2069550323 4672 QSIISQQSGEAEICVR 4687
Cdd:cd06714     80 QDIISQSKGEVELVVS 95
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 430-491 2.84e-43

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: 152.88  E-value: 2.84e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069550323  430 TFCPLCTTTELLLHTPEKANYNTCTQCQTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALGG 491
Cdd:cd15774      1 TICPLCKTTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 902-965 7.20e-41

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: 145.98  E-value: 7.20e-41
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069550323  902 SACPLCKTELNVGSKDPPNYNTCTECKNVVCNLCGFNPMPHITEVQEWLCLNCQTKRALSGQLG 965
Cdd:cd15776      1 LLCPLCKTELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQLG 64
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
 902-960 1.52e-38

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: 139.47  E-value: 1.52e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  902 SACPLCK-TELNVGSKDPPNYNTCTECKNVVCNLCGFNPMPHITEVQEWLCLNCQTKRAL 960
Cdd:pfam05715    1 TLCPLCKtTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
 430-489 1.81e-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: 136.39  E-value: 1.81e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  430 TFCPLCTTTELLLHTPEKANYNTCTQCQTVVCSLCGFNPNPHITEIKEWLCLNCQMQRAL 489
Cdd:pfam05715    1 TLCPLCKTTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
C2 pfam00168
C2 domain;
4808-4926 5.45e-31

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 119.35  E-value: 5.45e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4808 GNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGrgqvmvvqnasvENKRRTKYVQKSLNPEWNQTVIYkniSMEQLKKKT 4887
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNGTSDPYVKVYLLDG------------KQKKKTKVVKNTLNPVWNETFTF---SVPDPENAV 65

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2069550323 4888 LEVTVWDYDRFSSNDFLGEVLIELSSSSQLDNTPRWYTL 4926
Cdd:pfam00168   66 LEIEVYDYDRFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 4810-4923 1.36e-26

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 106.80  E-value: 1.36e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  4810 LIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQvmvvqnasvenKRRTKYVQKSLNPEWNQTVIYKNISMEqlkKKTLE 4889
Cdd:smart00239    2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKE-----------KKKTKVVKNTLNPVWNETFEFEVPPPE---LAELE 67

                            90       100       110
                    ....*....|....*....|....*....|....
gi 2069550323  4890 VTVWDYDRFSSNDFLGEVLIELSSSSQLDNTPRW 4923
Cdd:smart00239   68 IEVYDKDRFGRDDFIGQVTIPLSDLLLGGRHEKL 101
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 5137-5262 1.91e-15

C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins are uncharacterized human proteins. They were compiled by the Kazusa mammalian cDNA project which identified more than 2000 human genes. They are identified by 4 digit codes that precede the KIAA designation. Many KIAA genes are still functionally uncharacterized including KIAA1228. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175996 [Multi-domain]  Cd Length: 127  Bit Score: 75.77  E-value: 1.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5137 GEIKIALkkEMKTDGEQLIVEILQCRNITykFKSPDHLPDLYVKLYVvnLATQKRVIKKKTRVCRHDREPSFNETFRFSL 5216
Cdd:cd04030      3 GRIQLTI--RYSSQRQKLIVTVHKCRNLP--PCDSSDIPDPYVRLYL--LPDKSKSTRRKTSVKKDNLNPVFDETFEFPV 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5217 SPTGHSLQILLVS--NGGKFM--KKTLIGEAYIWLDKVDLRKRIVNWHKL 5262
Cdd:cd04030     77 SLEELKRRTLDVAvkNSKSFLsrEKKLLGQVLIDLSDLDLSKGFTQWYDL 126
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 5153-5259 5.52e-14

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 70.98  E-value: 5.52e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  5153 QLIVEILQCRNITYKFKSpdHLPDLYVKLYVVNlatqKRVIKKKTRVCRHDREPSFNETFRFSLSPTGHSLQILLVSNGG 5232
Cdd:smart00239    1 TLTVKIISARNLPPKDKG--GKSDPYVKVSLDG----DPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDKD 74

                            90       100
                    ....*....|....*....|....*..
gi 2069550323  5233 KFMKKTLIGEAYIWLDKVDLRKRIVNW 5259
Cdd:smart00239   75 RFGRDDFIGQVTIPLSDLLLGGRHEKL 101
C2 pfam00168
C2 domain;
5153-5262 2.07e-13

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 69.27  E-value: 2.07e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5153 QLIVEILQCRNITYKFKSPdhLPDLYVKLYVvnlatQKRVIKKKTRVCRHDREPSFNETFRFSLSPTGHSLQILLVSNGG 5232
Cdd:pfam00168    2 RLTVTVIEAKNLPPKDGNG--TSDPYVKVYL-----LDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDYD 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 2069550323 5233 KFMKKTLIGEAYIWLDKVDLRKRIVNWHKL 5262
Cdd:pfam00168   75 RFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 4609-4687 1.43e-11

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 63.55  E-value: 1.43e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069550323  4609 SGNGLGIRIVGGKEIPGtngeiGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEAEICVR 4687
Cdd:smart00228   10 GGGGLGFSLVGGKDEGG-----GVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
PHA03247 PHA03247
large tegument protein UL36; Provisional
 23-433 5.46e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 69.97  E-value: 5.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323   23 PSEGPRLPSGEAPDLSQLSE--AERRQIAAVLSRAQDPS--PRHAQldsshhPRQPGKPPDSGP-PTLSKSRTVDTLKTE 97
Cdd:PHA03247  2552 PPPLPPAAPPAAPDRSVPPPrpAPRPSEPAVTSRARRPDapPQSAR------PRAPVDDRGDPRgPAPPSPLPPDTHAPD 2625

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323   98 QRVPGRSPSSISLRQSTSrtdfkedqKPSMMPSFLSDANPFGAVTSVVNKFNPFDLISDSDTAQ----EEASKKQKPIQK 173
Cdd:PHA03247  2626 PPPPSPSPAANEPDPHPP--------PTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQrprrRAARPTVGSLTS 2697

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  174 EQDKPGQQKGPSKQPVQQQS--PKPTGPQQGSVKPAPQKTAPPKQVVPQQQQQQQQQQQQPGVPKQAQKPGPGQQAGPQS 251
Cdd:PHA03247  2698 LADPPPPPPTPEPAPHALVSatPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA 2777

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  252 eeakkqqGAPKTQPQQSESTKTPPQQQQQSPAKPPPQQPGTARASPQQANASKTSSQVPTPTKATVAQQGISTGKQPSQQ 331
Cdd:PHA03247  2778 -------GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSL 2850

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  332 -------PGGPT--KPAPQSAGANKQATQQQGSAAKPAPQQTGPTKQQLQQPGEPAKPSAQQAGPTKQPQHQAEPtKPTG 402
Cdd:PHA03247  2851 plggsvaPGGDVrrRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPP-PPQP 2929

                          410       420       430
                   ....*....|....*....|....*....|.
gi 2069550323  403 QKPGPVQQKPEASPPQASQPGGSASKKTFCP 433
Cdd:PHA03247  2930 QPPPPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 159-465 2.47e-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: 2.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  159 TAQEEASKKQKPIQKEQDKPGQQKGPSKQPVQQQSPK-------PTGPQQ---GSVKPAPQKTAPPKQVVPQQQQQQQQQ 228
Cdd:pfam03157  443 PGQGQQPGQEQPGQGQQPGQGQQGQQPGQPEQGQQPGqgqpgyyPTSPQQsgqGQQLGQWQQQGQGQPGYYPTSPLQPGQ 522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  229 QQQPGVPKQAQKPGPGQQAGPQSEEAKKQQGAPKTQPQQSESTKTPPQQQQQSPAKPPPQ----------QPGTARASPQ 298
Cdd:pfam03157  523 GQPGYYPTSPQQPGQGQQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQGQQpgqgqqpgqgQPGYYPTSPQ 602

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  299 QANASKTSSQVPTPTKATVAQQGISTgKQPSQQPGGPTKPAPQSAGANKQATQQQGSAA------KPAPQQTGPTKQ--Q 370
Cdd:pfam03157  603 QSGQGQQPGQWQQPGQGQPGYYPTSS-LQLGQGQQGYYPTSPQQPGQGQQPGQWQQSGQgqqgyyPTSPQQSGQAQQpgQ 681

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  371 LQQPGEPAKPSAQQAG--PTKQPQHQAEPTKPTGQKPGPVQQKPEASPPQASQPGGSASKKTFCPLCTTTELLLHTPEKA 448
Cdd:pfam03157  682 GQQPGQWLQPGQGQQGyyPTSPQQPGQGQQLGQGQQSGQGQQGYYPTSPGQGQQSGQGQQGYDSPYHVSAEHQAASLKVA 761

                          330
                   ....*....|....*..
gi 2069550323  449 NYNTCTQCQTVVCSLCG 465
Cdd:pfam03157  762 KAQQLAAQLPAMCRLEG 778
PHA03247 PHA03247
large tegument protein UL36; Provisional
 329-730 6.14e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 66.50  E-value: 6.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  329 SQQPGGPTKPAPqsAGANKQATQQQGSAAKPAPQQTGPTKQ-QLQQPGEPAKPSAQQA--GPTKQPQHQAEPTK--PTGQ 403
Cdd:PHA03247  2545 SDDAGDPPPPLP--PAAPPAAPDRSVPPPRPAPRPSEPAVTsRARRPDAPPQSARPRApvDDRGDPRGPAPPSPlpPDTH 2622

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  404 KPGPVQQKPEASPPQASQPGGSASKKTFCPLCTTTELLLHTPEKANyntcTQCQTVVCSLCGFNPNPhiteikewlclnc 483
Cdd:PHA03247  2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRAR----RLGRAAQASSPPQRPRR------------- 2685

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  484 qmqRALGGDLG--------PAPGPGPQSSAPKQKMAAPTTAGKPPPQAQQPTQKKESTVK--PDATQSPEHKKPPPPQTK 553
Cdd:PHA03247  2686 ---RAARPTVGsltsladpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPavPAGPATPGGPARPARPPT 2762

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  554 QPTIPSSTPEKAKPPAPE-----------TQQTESTPKSDQTKPAPAEDKQKQPHVQKPISDVVPKPSEFDTKQDSPGPK 622
Cdd:PHA03247  2763 TAGPPAPAPPAAPAAGPPrrltrpavaslSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPP 2842

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  623 PAPVQQKVvhPQGSEVAK----SSEDTPQDKTVPPDTKTSPQVSRqksdpklVSQPgsgidtKVQKQTEPVEGKGDLKKM 698
Cdd:PHA03247  2843 PGPPPPSL--PLGGSVAPggdvRRRPPSRSPAAKPAAPARPPVRR-------LARP------AVSRSTESFALPPDQPER 2907

                          410       420       430
                   ....*....|....*....|....*....|....
gi 2069550323  699 QPQ-MSPKPDAKQAQKPQQATVGPKP-TQSQPKA 730
Cdd:PHA03247  2908 PPQpQAPPPPQPQPQPPPPPQPQPPPpPPPRPQP 2941
PTZ00121 PTZ00121
MAEBL; Provisional
 989-1732 5.82e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 5.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  989 QVKSAETPQQQKaSARPAQNEKRGPDIQKEDPASQQGKPAKAISADKIQEiVQKEHTTPQQEKLPKTISADKLSQSISGE 1068
Cdd:PTZ00121  1132 EARKAEDARKAE-EARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEA-ARKAEEVRKAEELRKAEDARKAEAARKAE 1209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1069 D----SEIQKG----KIGKPPSADQVPKEEAKVvRKSSADKLLEIVQKKEPKELEHVSDNIQIQKEDPKVQQIRLSKPPS 1140
Cdd:PTZ00121  1210 EerkaEEARKAedakKAEAVKKAEEAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1141 ---ADQIRKEDPKVQQVKLSKtpSADQIRKED---PKVQQVKlTKAPSADQIRKEDPKIQQVKLAKAPSADQiqedpKLQ 1214
Cdd:PTZ00121  1289 kkkADEAKKAEEKKKADEAKK--KAEEAKKADeakKKAEEAK-KKADAAKKKAEEAKKAAEAAKAEAEAAAD-----EAE 1360

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1215 QGKfvKTPSADKIRQEDPKIHQEKLTKvpSDSEIKKVDPKIQQAKLAKiPSADHIQKEDSKLFKAKIVKTAS-----ADQ 1289
Cdd:PTZ00121  1361 AAE--EKAEAAEKKKEEAKKKADAAKK--KAEEKKKADEAKKKAEEDK-KKADELKKAAAAKKKADEAKKKAeekkkADE 1435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1290 LPKD-NKFQEMELANIPVEDYISSKTIHDQTQVARRKEDDTKFP----LSRESLHLAESRQKVAGEQFDEEKiEPKVLPK 1364
Cdd:PTZ00121  1436 AKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAeeakKADEAKKKAEEAKKKADEAKKAAE-AKKKADE 1514

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1365 TRQQEDIKREDLMMDIPESISKDQ-KSPKEETSAPPV----PLPKPDHVEAIREKAEKEDDKSDASSSQQQKSPqglsdt 1439
Cdd:PTZ00121  1515 AKKAEEAKKADEAKKAEEAKKADEaKKAEEKKKADELkkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK------ 1588

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1440 gyssdgISSSLGEIPSLIQSEEKDVLKESCKKEilsqESSPTSPSDLAKLES-----TVLSILEAQASTLAEEKSGKSKD 1514
Cdd:PTZ00121  1589 ------AEEARIEEVMKLYEEEKKMKAEEAKKA----EEAKIKAEELKKAEEekkkvEQLKKKEAEEKKKAEELKKAEEE 1658

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1515 IYGVYSEHSRVPHKTKTQlgAPESYSADEEDLAKQNIQGKyggAPEEGDKQDILSQKSYKGKTDTREDASARRQRYDSV- 1593
Cdd:PTZ00121  1659 NKIKAAEEAKKAEEDKKK--AEEAKKAEEDEKKAAEALKK---EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAe 1733

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1594 -------EDSSESENSPVPQRKRRTSVGSSSSDDYKAEDSPGSG--------DDEDFIRKQIMEMSADEDASGSE----- 1653
Cdd:PTZ00121  1734 eakkeaeEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeavieeelDEEDEKRRMEVDKKIKDIFDNFAniieg 1813

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1654 ----------DDEFIRNQLKEISITDSHKKEEMKNKKGIPGKHKRMTRKSSTGyEDDTSRRHSWHDDDDETFDESPEPKY 1723
Cdd:PTZ00121  1814 gkegnlvindSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNK-EADFNKEKDLKEDDEEEIEEADEIEK 1892


                   ....*....
gi 2069550323 1724 RETKSQDSE 1732
Cdd:PTZ00121  1893 IDKDDIERE 1901
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
4808-4916 4.13e-08

Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 60.16  E-value: 4.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4808 GNLIIHILQARNLAPRDNNGYSDPFVKVYLlpgrgqvmvvQNASVenkRRTKYVQKSLNPEWNQTVIyknisMEQLKKKT 4887
Cdd:COG5038   1040 GYLTIMLRSGENLPSSDENGYSDPFVKLFL----------NEKSV---YKTKVVKKTLNPVWNEEFT-----IEVLNRVK 1101

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2069550323 4888 --LEVTVWDYDRFSSNDFLGEVLIELSSSSQ 4916
Cdd:COG5038   1102 dvLTINVNDWDSGEKNDLLGTAEIDLSKLEP 1132
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 992-1294 1.54e-07

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 57.87  E-value: 1.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  992 SAETPQQQKASARPAQNEKRGPDIQKEDPASQQgKPAKAISADKIQEIVQ-KEHTTPQQEKLPKtisadklsqsisgEDS 1070
Cdd:NF040676   142 SSTAPTEKKADEKTKQVAKVQKSVKAKEEAKTQ-KVAKAKETTKAQEIVKpKEEVKVQEVVKPK-------------EEP 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1071 EIQKgkIGKPpsadqvpKEEAKV---VRKSSADKLLEIVQkkePKELEHVSDNIQIqKEDPKVQQIrlSKPpsadqirKE 1147
Cdd:NF040676   208 KVQE--IVKP-------KEEVKVqeeVKPKEEEKVQEIVK---PKEEAKVQEEVKV-KEEAKVQEI--AKA-------KE 265

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1148 DPKVQQV-KLSKTPSADQIRKEDPKVQQVKLTKApsadqirKEDPKIQQVklAKAPSADQIQEDPKLQQgkfvkTPSADK 1226
Cdd:NF040676   266 EAKAQEIaKAKEEAKAQEIAKAKEEAKAQEIAKA-------KEEEKAQEI--AKAKEEAKAREIAKAKE-----EEKARE 331

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069550323 1227 IRQEDPKIHQEKLTKVPSDSEIKKVDpKIQQAKLAKIPSADHIQKEDSKLfkaKIVKTA-SADqlPKDN 1294
Cdd:NF040676   332 IAKAKEEAKAREIAKAKEEAKAREIA-KAKEEERAKEASKNNIQSAKREL---TVVATAyTAD--PSEN 394
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 189-806 2.46e-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: 57.65  E-value: 2.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  189 VQQQSPKPTGPQQGSVKPApqktappkqvvpQQQQQQQQQQQQPGVPKQAQKPGPGQQAGPQSEEAKKQQGAPKTQPQQS 268
Cdd:pfam03157  106 LQRYYPGVTSPQQVSYYPG------------QASPQRPGQGQQPGQGQQWYYPTSPQQPGQWQQPGQGQQGYYPTSPQQS 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  269 ----ESTKTPPQQQQQSPAKPPPQQPGTARASPQQANASKTSSQVPTPTKATVAQQGISTGK-------QPSQQPGGPTK 337
Cdd:pfam03157  174 gqrqQPGQGQQLRQGQQGQQSGQGQPGYYPTSSQQPGQLQQTGQGQQGQQPERGQQGQQPGQgqqpgqgQQGQQPGQPQQ 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  338 PAPQSAGANKQATQQQGSAAKPAPQQTGPTKQQLQQPGEPAK----PSAQQAGPTKQPQHQAEPTK-------PTGQKPG 406
Cdd:pfam03157  254 LGQGQQGYYPISPQQPRQWQQSGQGQQGYYPTSLQQPGQGQSgyypTSQQQAGQLQQEQQLGQEQQdqqpgqgRQGQQPG 333

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  407 PVQQKPEasPPQASQPGgsASKKTFCPlctTTELLLHTPEKANYNTCTQCQTvvcslcgfnpnphiteikewlclncQMQ 486
Cdd:pfam03157  334 QGQQGQQ--PAQGQQPG--QGQPGYYP---TSPQQPGQGQPGYYPTSQQQPQ-------------------------QGQ 381

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  487 RALGGDLGPAPGPGPQSSAPkqkmaapttaGKPPPQAQQPTQKKESTVKPDATQSPEHKKPPPPQTKQPTIPSSTPEKAK 566
Cdd:pfam03157  382 QPEQGQQGQQQGQGQQGQQP----------GQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSPQQSGQGQQPGQGQQPGQ 451

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  567 PPAPETQQtestPKSDQTKPAPAEDKQKQPHVQKpisdvvpKPSEFDTKQDSPGPKPAPVQQKvVHPQGSEVAKSSEDTP 646
Cdd:pfam03157  452 EQPGQGQQ----PGQGQQGQQPGQPEQGQQPGQG-------QPGYYPTSPQQSGQGQQLGQWQ-QQGQGQPGYYPTSPLQ 519

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  647 QDKTVPPDTKTSPQVSRQKSDPKLVSQPGSGID----TKVQKQTEPVEGKGDLKKMQPQMSPKPDakQAQKPQQATVGPK 722
Cdd:pfam03157  520 PGQGQPGYYPTSPQQPGQGQQLGQLQQPTQGQQgqqsGQGQQGQQPGQGQQGQQPGQGQQGQQPG--QGQQPGQGQPGYY 597

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  723 PTQSQPKATQSQPPAQPQQSQKAPEQSSRFSLNIG----GFTDSSKSQPTTPQERVTGKLFGFGASIFNQASNLISTAGQ 798
Cdd:pfam03157  598 PTSPQQSGQGQQPGQWQQPGQGQPGYYPTSSLQLGqgqqGYYPTSPQQPGQGQQPGQWQQSGQGQQGYYPTSPQQSGQAQ 677


                   ....*...
gi 2069550323  799 QGAQPQGP 806
Cdd:pfam03157  678 QPGQGQQP 685
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 4604-4681 6.97e-07

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 49.97  E-value: 6.97e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069550323 4604 KDHSVSGNGLGIRIVGGKEipgtNGEIGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGE 4681
Cdd:pfam00595    3 TLEKDGRGGLGFSLKGGSD----QGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGK 75
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 507-769 1.60e-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: 44.76  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  507 KQKMAAPTTAGKPPPQAQQPTQKKE-STVKPDATQSPEHKKPPppqtkqptiPSSTPEKAKP---PAPETQQTESTPKSD 582
Cdd:NF033839   289 NKKPSAPKPGMQPSPQPEKKEVKPEpETPKPEVKPQLEKPKPE---------VKPQPEKPKPevkPQLETPKPEVKPQPE 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  583 QTKPapaedkQKQPHVQKPISDVVPKPS----EFDTKQDSPGP--KPAPVQQKV-VHPQGSevAKSSEDTPQDKTVPPDT 655
Cdd:NF033839   360 KPKP------EVKPQPEKPKPEVKPQPEtpkpEVKPQPEKPKPevKPQPEKPKPeVKPQPE--KPKPEVKPQPEKPKPEV 431

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  656 KTSPqvsrQKSDPKLVSQP-GSGIDTKVQKQTEPVEGKGDLKKMQPQMSPKPDAkqaqkpqqatvgPKPTQSQPKAtQSQ 734
Cdd:NF033839   432 KPQP----EKPKPEVKPQPeKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEK------------PKPDNSKPQA-DDK 494

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2069550323  735 PPAQPQQSQKAPEQSSRFSLNIGGFTDSSKSQPTT 769
Cdd:NF033839   495 KPSTPNNLSKDKQPSNQASTNEKATNKPKKSLPST 529
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 3856-3919 5.42e-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: 42.55  E-value: 5.42e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069550323 3856 ARAKILQDIDRELDLVERESAKLRKKQAELDEEEKEIDaklrylEMGINRRKEALLKEREKRER 3919
Cdd:pfam07946  265 TREEEIEKIKKAAEEERAEEAQEKKEEAKKKEREEKLA------KLSPEEQRKYEEKERKKEQR 322
 
Name Accession Description Interval E-value
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 4793-4927 1.59e-66

C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology and do not bind Ca2+.


Pssm-ID: 175997 [Multi-domain]  Cd Length: 125  Bit Score: 221.74  E-value: 1.59e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4793 ITGEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRgqvmvvqnaSVENKRRTKYVQKSLNPEWNQT 4872
Cdd:cd04031      1 ITGRIQIQLWYDKVTSQLIVTVLQARDLPPRDDGSLRNPYVKVYLLPDR---------SEKSKRRTKTVKKTLNPEWNQT 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2069550323 4873 VIYKNISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELsSSSQLDNTPRWYTLK 4927
Cdd:cd04031     72 FEYSNVRRETLKERTLEVTVWDYDRDGENDFLGEVVIDL-ADALLDDEPHWYPLQ 125
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
 4592-4687 1.22e-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: 169.27  E-value: 1.22e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4592 FPHARLKLPRDPKDHSVSGNGLGIRIVGGKEIPgtNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEV 4671
Cdd:cd06714      2 FLIGRIILQRDPKDGSVSGNGLGLKVVGGKMTE--SGRLGAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEV 79

                           90
                   ....*....|....*.
gi 2069550323 4672 QSIISQQSGEAEICVR 4687
Cdd:cd06714     80 QDIISQSKGEVELVVS 95
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 430-491 2.84e-43

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: 152.88  E-value: 2.84e-43
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069550323  430 TFCPLCTTTELLLHTPEKANYNTCTQCQTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALGG 491
Cdd:cd15774      1 TICPLCKTTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 902-965 7.20e-41

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: 145.98  E-value: 7.20e-41
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069550323  902 SACPLCKTELNVGSKDPPNYNTCTECKNVVCNLCGFNPMPHITEVQEWLCLNCQTKRALSGQLG 965
Cdd:cd15776      1 LLCPLCKTELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQLG 64
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
 902-960 1.52e-38

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: 139.47  E-value: 1.52e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  902 SACPLCK-TELNVGSKDPPNYNTCTECKNVVCNLCGFNPMPHITEVQEWLCLNCQTKRAL 960
Cdd:pfam05715    1 TLCPLCKtTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
FYVE2_BSN_PCLO cd15772
FYVE-related domain 2 found in protein bassoon and piccolo; This family includes protein ...
 902-965 4.19e-38

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: 138.24  E-value: 4.19e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069550323  902 SACPLCKTELNVGSKDPPNYNTCTECKNVVCNLCGFNPMPHITEVQEWLCLNCQTKRALSGQLG 965
Cdd:cd15772      1 VTCPLCKTELNVGSKEPPNYNTCTQCHTQVCNLCGFNPTPHLVEKKEWLCLNCQTQRLMSGGLG 64
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
 430-489 1.81e-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: 136.39  E-value: 1.81e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  430 TFCPLCTTTELLLHTPEKANYNTCTQCQTVVCSLCGFNPNPHITEIKEWLCLNCQMQRAL 489
Cdd:pfam05715    1 TLCPLCKTTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
FYVE1_BSN_PCLO cd15771
FYVE-related domain 1 found in protein bassoon and piccolo; This family includes protein ...
 430-491 3.49e-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: 129.74  E-value: 3.49e-35
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069550323  430 TFCPLCTTTELLLHTPeKANYNTCTQCQTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALGG 491
Cdd:cd15771      1 TLCPLCNTTELTLHVP-KPNFNTCTQCHTTVCNQCGFNPNPHLTEVKEWLCLNCQMQRALGM 61
FYVE2_BSN cd15775
FYVE-related domain 2 found in protein bassoon; Protein bassoon, also termed zinc finger ...
 904-965 5.94e-34

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: 126.57  E-value: 5.94e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069550323  904 CPLCKTELNVGSKDPPNYNTCTECKNVVCNLCGFNPMPHITEVQEWLCLNCQTKRALSGQLG 965
Cdd:cd15775      4 CPLCKTELNVGSTEPPNYNTCTSCRTQVCNLCGFNPTPHLVEKNEWLCLNCQTQRLLEGSLG 65
C2A_SLP cd08521
C2 domain first repeat present in Synaptotagmin-like proteins; All Slp members basically share ...
 4795-4926 2.83e-33

C2 domain first repeat present in Synaptotagmin-like proteins; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike the case in Slp3 and Slp4/granuphilin in which their C2A domains are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp3 and Slp4/granuphilin promote dense-core vesicle exocytosis. Slp5 mRNA has been shown to be restricted to human placenta and liver suggesting a role in Rab27A-dependent membrane trafficking in specific tissues. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176056 [Multi-domain]  Cd Length: 123  Bit Score: 126.60  E-value: 2.83e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4795 GEIQLQVNYDKHLGNLIIHILQARNLAPRDN-NGYSDPFVKVYLLPGRgqvmvvqnaSVENKRRTKYVQKSLNPEWNQTV 4873
Cdd:cd08521      1 GEIEFSLSYNYKTGSLEVHIKECRNLAYADEkKKRSNPYVKVYLLPDK---------SKQSKRKTSVKKNTTNPVFNETL 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2069550323 4874 IYKnISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSSSQLDNTPRWYTL 4926
Cdd:cd08521     72 KYH-ISKSQLETRTLQLSVWHHDRFGRNTFLGEVEIPLDSWDLDSQQSEWYPL 123
C2 pfam00168
C2 domain;
4808-4926 5.45e-31

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 119.35  E-value: 5.45e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4808 GNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGrgqvmvvqnasvENKRRTKYVQKSLNPEWNQTVIYkniSMEQLKKKT 4887
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNGTSDPYVKVYLLDG------------KQKKKTKVVKNTLNPVWNETFTF---SVPDPENAV 65

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2069550323 4888 LEVTVWDYDRFSSNDFLGEVLIELSSSSQLDNTPRWYTL 4926
Cdd:pfam00168   66 LEIEVYDYDRFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
FYVE1_BSN cd15773
FYVE-related domain 1 found in protein bassoon; Protein bassoon, also termed zinc finger ...
 430-490 1.88e-30

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: 116.34  E-value: 1.88e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069550323  430 TFCPLCTTTELLlHTPEKANYNTCTQCQTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALG 490
Cdd:cd15773      4 TLCPICNTTELT-SFPSQPNFNTCTQCHNKVCNQCGFNPNPHLTEVKEWLCLNCQMQRALG 63
FYVE_BSN_PCLO cd15751
FYVE-related domain found in protein bassoon and piccolo; This family includes protein bassoon ...
 902-960 5.29e-30

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: 114.86  E-value: 5.29e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  902 SACPLCK-TELNVGSKDPPNYNTCTECKNVVCNLCGFNPMPHITEVQEWLCLNCQTKRAL 960
Cdd:cd15751      1 SACPLCGtSELPLGSKSPPNYNTCTDCKNRVCNQCGFNSTPPVTKVKEWLCLNCQKKRAL 60
C2B_SLP_1-2-3-4 cd04020
C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically ...
 4808-4913 5.34e-29

C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike the case in Slp3 and Slp4/granuphilin in which their C2A domains are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp3 and Slp4/granuphilin promote dense-core vesicle exocytosis. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175987 [Multi-domain]  Cd Length: 162  Bit Score: 115.88  E-value: 5.34e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4808 GNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRgqvmvvqnaSVENKRRTKYVQKSLNPEWNQTVIYKNISMEQLKKKT 4887
Cdd:cd04020     27 GELHVWVKEAKNLPALKSGGTSDSFVKCYLLPDK---------SKKSKQKTPVVKKSVNPVWNHTFVYDGVSPEDLSQAC 97

                           90       100
                   ....*....|....*....|....*.
gi 2069550323 4888 LEVTVWDYDRFSSNDFLGEVLIELSS 4913
Cdd:cd04020     98 LELTVWDHDKLSSNDFLGGVRLGLGT 123
C2B_Rabphilin_Doc2 cd08384
C2 domain second repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
 4797-4924 8.29e-29

C2 domain second repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons and in neuroendrocrine cells, while Doc2 is found not only in the brain but in tissues, including mast cells, chromaffin cells, and osteoblasts. Rabphilin and Doc2s share highly homologous tandem C2 domains, although their N-terminal structures are completely different: rabphilin contains an N-terminal Rab-binding domain (RBD),7 whereas Doc2 contains an N-terminal Munc13-1-interacting domain (MID). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176030 [Multi-domain]  Cd Length: 133  Bit Score: 114.37  E-value: 8.29e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4797 IQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPgrgqvmvvqNASVENKRRTKYVQKSLNPEWNQTVIYK 4876
Cdd:cd08384      2 ILVSLMYNTQRRGLIVGIIRCVNLAAMDANGYSDPFVKLYLKP---------DAGKKSKHKTQVKKKTLNPEFNEEFFYD 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2069550323 4877 nISMEQLKKKTLEVTVWDYDRFSSNDFLGEVliELSSSSQLDNTPRWY 4924
Cdd:cd08384     73 -IKHSDLAKKTLEITVWDKDIGKSNDYIGGL--QLGINAKGERLRHWL 117
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
 4795-4932 1.90e-28

C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha and gamma. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1(alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 175992 [Multi-domain]  Cd Length: 131  Bit Score: 113.13  E-value: 1.90e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4795 GEIQLQVNYDKhlGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPgrgqvmvvqNASVENKRRTKYVQKSLNPEWNQTVI 4874
Cdd:cd04026      2 GRIYLKISVKD--NKLTVEVREAKNLIPMDPNGLSDPYVKLKLIP---------DPKNETKQKTKTIKKTLNPVWNETFT 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4875 YkNISMEQlKKKTLEVTVWDYDRFSSNDFLGEVLIELsssSQLDNTPR--WYTLKEQSES 4932
Cdd:cd04026     71 F-DLKPAD-KDRRLSIEVWDWDRTTRNDFMGSLSFGV---SELIKMPVdgWYKLLNQEEG 125
C2A_Rabphilin_Doc2 cd04035
C2 domain first repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
 4795-4912 2.63e-28

C2 domain first repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons and in neuroendrocrine cells, while Doc2 is found not only in the brain but in tissues, including mast cells, chromaffin cells, and osteoblasts. Rabphilin and Doc2s share highly homologous tandem C2 domains, although their N-terminal structures are completely different: rabphilin contains an N-terminal Rab-binding domain (RBD),7 whereas Doc2 contains an N-terminal Munc13-1-interacting domain (MID). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176000 [Multi-domain]  Cd Length: 123  Bit Score: 112.38  E-value: 2.63e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4795 GEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGrgqvmvvqnASVENKRRTKYVQKSLNPEWNQTVI 4874
Cdd:cd04035      2 GTLEFTLLYDPANSALHCTIIRAKGLKAMDANGLSDPYVKLNLLPG---------ASKATKLRTKTVHKTRNPEFNETLT 72

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2069550323 4875 YKNISMEQLKKKTLEVTVWDYDRFsSNDFLGEVLIELS 4912
Cdd:cd04035     73 YYGITEEDIQRKTLRLLVLDEDRF-GNDFLGETRIPLK 109
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 904-962 3.38e-28

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: 110.12  E-value: 3.38e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  904 CPLCK-TELNVGSKDPPNYNTCTECKNVVCNLCGFNPMPHITEVQEWLCLNCQTKRALSG 962
Cdd:cd15774      3 CPLCKtTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
C2A_SLP-1_2 cd08393
C2 domain first repeat present in Synaptotagmin-like proteins 1 and 2; All Slp members ...
 4795-4927 7.25e-28

C2 domain first repeat present in Synaptotagmin-like proteins 1 and 2; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike Slp3 and Slp4/granuphilin which are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176039 [Multi-domain]  Cd Length: 125  Bit Score: 111.37  E-value: 7.25e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4795 GEIQLQVNYDKHLGNLIIHILQARNLAPRD-NNGYSDPFVKVYLLPGRgqvmvvqnaSVENKRRTKYVQKSLNPEWNQTV 4873
Cdd:cd08393      2 GSVQFALDYDPKLRELHVHVIQCQDLAAADpKKQRSDPYVKTYLLPDK---------SNRGKRKTSVKKKTLNPVFNETL 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2069550323 4874 IYKnISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSSSQLDNTPRWYTLK 4927
Cdd:cd08393     73 RYK-VEREELPTRVLNLSVWHRDSLGRNSFLGEVEVDLGSWDWSNTQPTWYPLQ 125
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 4810-4926 1.17e-27

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 109.85  E-value: 1.17e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4810 LIIHILQARNLAPRDNNGYSDPFVKVYLLPGRgqvmvvqnasvenKRRTKYVQKSLNPEWNQTViykNISMEQLKKKTLE 4889
Cdd:cd00030      1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQ-------------KFKTKVVKNTLNPVWNETF---EFPVLDPESDTLT 64

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2069550323 4890 VTVWDYDRFSSNDFLGEVLIELSS-SSQLDNTPRWYTL 4926
Cdd:cd00030     65 VEVWDKDRFSKDDFLGEVEIPLSElLDSGKEGELWLPL 102
C2A_Synaptotagmin-7 cd08386
C2A domain first repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 4795-4912 1.99e-27

C2A domain first repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 7, a member of class 2 synaptotagmins, is located in presynaptic plasma membranes in neurons, dense-core vesicles in endocrine cells, and lysosomes in fibroblasts. It has been shown to play a role in regulation of Ca2+-dependent lysosomal exocytosis in fibroblasts and may also function as a vesicular Ca2+-sensor. It is distinguished from the other synaptotagmins by having over 12 splice forms. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176032 [Multi-domain]  Cd Length: 125  Bit Score: 110.11  E-value: 1.99e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4795 GEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGqvmvvqnasveNKRRTKYVQKSLNPEWNQTVI 4874
Cdd:cd08386      3 GRIQFSVSYDFQESTLTLKILKAVELPAKDFSGTSDPFVKIYLLPDKK-----------HKLETKVKRKNLNPHWNETFL 71

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2069550323 4875 YKNISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELS 4912
Cdd:cd08386     72 FEGFPYEKLQQRVLYLQVLDYDRFSRNDPIGEVSLPLN 109
C2B_PI3K_class_II cd08381
C2 domain second repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are ...
 4794-4927 2.27e-27

C2 domain second repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a N-terminal C2 domain, a PIK domain, and a kinase catalytic domain. Unlike class I and class III, class II PI3Ks have additionally a PX domain and a C-terminal C2 domain containing a nuclear localization signal both of which bind phospholipids though in a slightly different fashion. PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176027 [Multi-domain]  Cd Length: 122  Bit Score: 109.69  E-value: 2.27e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4794 TGEIQLQVNYDKhlGNLIIHILQARNLAPRDNNgYSDPFVKVYLLPgrgqvmvvqNASVENKRRTKYVQKSLNPEWNQTV 4873
Cdd:cd08381      1 GGQVKLSISYKN--GTLFVMVMHAKNLPLLDGS-DPDPYVKTYLLP---------DPQKTTKRKTKVVRKTRNPTFNEML 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2069550323 4874 IYKNISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSSSQLDNTPRWYTLK 4927
Cdd:cd08381     69 VYDGLPVEDLQQRVLQVSVWSHDSLVENEFLGGVCIPLKKLDLSQETEKWYPLG 122
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 4810-4923 1.36e-26

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 106.80  E-value: 1.36e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  4810 LIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQvmvvqnasvenKRRTKYVQKSLNPEWNQTVIYKNISMEqlkKKTLE 4889
Cdd:smart00239    2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKE-----------KKKTKVVKNTLNPVWNETFEFEVPPPE---LAELE 67

                            90       100       110
                    ....*....|....*....|....*....|....
gi 2069550323  4890 VTVWDYDRFSSNDFLGEVLIELSSSSQLDNTPRW 4923
Cdd:smart00239   68 IEVYDKDRFGRDDFIGQVTIPLSDLLLGGRHEKL 101
FYVE1_BSN_PCLO cd15771
FYVE-related domain 1 found in protein bassoon and piccolo; This family includes protein ...
 904-962 1.95e-26

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: 104.70  E-value: 1.95e-26
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2069550323  904 CPLCKTELNVGSKDPPNYNTCTECKNVVCNLCGFNPMPHITEVQEWLCLNCQTKRALSG 962
Cdd:cd15771      3 CPLCNTTELTLHVPKPNFNTCTQCHTTVCNQCGFNPNPHLTEVKEWLCLNCQMQRALGM 61
FYVE2_BSN_PCLO cd15772
FYVE-related domain 2 found in protein bassoon and piccolo; This family includes protein ...
 432-494 4.11e-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: 103.96  E-value: 4.11e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069550323  432 CPLCTTtELLLHTPEKANYNTCTQCQTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALGGDLG 494
Cdd:cd15772      3 CPLCKT-ELNVGSKEPPNYNTCTQCHTQVCNLCGFNPTPHLVEKKEWLCLNCQTQRLMSGGLG 64
C2A_Synaptotagmin-1-5-6-9-10 cd08385
C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a ...
 4795-4923 6.91e-26

C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 1, a member of class 1 synaptotagmins, is located in the brain and endocranium and localized to the synaptic vesicles and secretory granules. It functions as a Ca2+ sensor for fast exocytosis as do synaptotagmins 5, 6, and 10. It is distinguished from the other synaptotagmins by having an N-glycosylated N-terminus. Synaptotagmins 5, 6, and 10, members of class 3 synaptotagmins, are located primarily in the brain and localized to the active zone and plasma membrane. They is distinguished from the other synaptotagmins by having disulfide bonds at its N-terminus. Synaptotagmin 6 also regulates the acrosome reaction, a unique Ca2+-regulated exocytosis, in sperm. Synaptotagmin 9, a class 5 synaptotagmins, is located in the brain and localized to the synaptic vesicles. It is thought to be a Ca2+-sensor for dense-core vesicle exocytosis. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176031 [Multi-domain]  Cd Length: 124  Bit Score: 105.42  E-value: 6.91e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4795 GEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRgqvmvvqnasvENKRRTKYVQKSLNPEWNQTVI 4874
Cdd:cd08385      3 GKLQFSLDYDFQSNQLTVGIIQAADLPAMDMGGTSDPYVKVYLLPDK-----------KKKFETKVHRKTLNPVFNETFT 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2069550323 4875 YKnISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSSSQLDNTPRW 4923
Cdd:cd08385     72 FK-VPYSELGNKTLVFSVYDFDRFSKHDLIGEVRVPLLTVDLGHVTEEW 119
FYVE2_BSN cd15775
FYVE-related domain 2 found in protein bassoon; Protein bassoon, also termed zinc finger ...
 429-494 1.46e-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: 102.69  E-value: 1.46e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069550323  429 KTFCPLCTTtELLLHTPEKANYNTCTQCQTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALGGDLG 494
Cdd:cd15775      1 RVTCPLCKT-ELNVGSTEPPNYNTCTSCRTQVCNLCGFNPTPHLVEKNEWLCLNCQTQRLLEGSLG 65
FYVE1_BSN cd15773
FYVE-related domain 1 found in protein bassoon; Protein bassoon, also termed zinc finger ...
 900-960 1.86e-25

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: 102.08  E-value: 1.86e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069550323  900 PTSA-CPLCKTELNVGSKDPPNYNTCTECKNVVCNLCGFNPMPHITEVQEWLCLNCQTKRAL 960
Cdd:cd15773      1 PSSTlCPICNTTELTSFPSQPNFNTCTQCHNKVCNQCGFNPNPHLTEVKEWLCLNCQMQRAL 62
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
 432-494 2.07e-25

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: 102.07  E-value: 2.07e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069550323  432 CPLCTTtELLLHTPEKANYNTCTQCQTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALGGDLG 494
Cdd:cd15776      3 CPLCKT-ELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQLG 64
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 4794-4927 3.92e-25

C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins are uncharacterized human proteins. They were compiled by the Kazusa mammalian cDNA project which identified more than 2000 human genes. They are identified by 4 digit codes that precede the KIAA designation. Many KIAA genes are still functionally uncharacterized including KIAA1228. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175996 [Multi-domain]  Cd Length: 127  Bit Score: 103.51  E-value: 3.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4794 TGEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRgqvmvvqnaSVENKRRTKYVQKSLNPEWNQTV 4873
Cdd:cd04030      2 LGRIQLTIRYSSQRQKLIVTVHKCRNLPPCDSSDIPDPYVRLYLLPDK---------SKSTRRKTSVKKDNLNPVFDETF 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2069550323 4874 IYkNISMEQLKKKTLEVTVWDYDRFSS--NDFLGEVLIELSSSSQLDNTPRWYTLK 4927
Cdd:cd04030     73 EF-PVSLEELKRRTLDVAVKNSKSFLSreKKLLGQVLIDLSDLDLSKGFTQWYDLT 127
FYVE_BSN_PCLO cd15751
FYVE-related domain found in protein bassoon and piccolo; This family includes protein bassoon ...
 432-490 7.82e-25

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: 100.22  E-value: 7.82e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2069550323  432 CPLCTTTELLLHTPEKANYNTCTQCQTVVCSLCGFNPNPHITEIKEWLCLNCQMQRALG 490
Cdd:cd15751      3 CPLCGTSELPLGSKSPPNYNTCTDCKNRVCNQCGFNSTPPVTKVKEWLCLNCQKKRALG 61
C2A_SLP-4_5 cd04029
C2 domain first repeat present in Synaptotagmin-like proteins 4 and 5; All Slp members ...
 4794-4913 1.85e-24

C2 domain first repeat present in Synaptotagmin-like proteins 4 and 5; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. SHD of Slp (except for the Slp4-SHD) function as a specific Rab27A/B-binding domain. In addition to Slp, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp4/granuphilin promotes dense-core vesicle exocytosis. The C2A domain of Slp4 is Ca2+ dependent. Slp5 mRNA has been shown to be restricted to human placenta and liver suggesting a role in Rab27A-dependent membrane trafficking in specific tissues. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 175995 [Multi-domain]  Cd Length: 125  Bit Score: 101.75  E-value: 1.85e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4794 TGEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGY-SDPFVKVYLLPGRgqvmvvqnaSVENKRRTKYVQKSLNPEWNQT 4872
Cdd:cd04029      1 SGEILFSLSYDYKTQSLNVHVKECRNLAYGDEAKKrSNPYVKTYLLPDK---------SRQSKRKTSIKRNTTNPVYNET 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2069550323 4873 VIYKnISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSS 4913
Cdd:cd04029     72 LKYS-ISHSQLETRTLQLSVWHYDRFGRNTFLGEVEIPLDS 111
C2B_Synaptotagmin-7 cd08405
C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 4795-4927 1.22e-22

C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 7, a member of class 2 synaptotagmins, is located in presynaptic plasma membranes in neurons, dense-core vesicles in endocrine cells, and lysosomes in fibroblasts. It has been shown to play a role in regulation of Ca2+-dependent lysosomal exocytosis in fibroblasts and may also function as a vesicular Ca2+-sensor. It is distinguished from the other synaptotagmins by having over 12 splice forms. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176050 [Multi-domain]  Cd Length: 136  Bit Score: 96.72  E-value: 1.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4795 GEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQVmvvqnasveNKRRTKYVQKSLNPEWNQTVI 4874
Cdd:cd08405      2 GELLLSLCYNPTANRITVNIIKARNLKAMDINGTSDPYVKVWLMYKDKRV---------EKKKTVIKKRTLNPVFNESFI 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069550323 4875 YkNISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLI-------ELSSSSQLDNTPR-----WYTLK 4927
Cdd:cd08405     73 F-NIPLERLRETTLIITVMDKDRLSRNDLIGKIYLgwksgglELKHWKDMLSKPRqpvaqWHRLK 136
C2A_Synaptotagmin-8 cd08387
C2A domain first repeat present in Synaptotagmin 8; Synaptotagmin is a membrane-trafficking ...
 4794-4927 2.11e-22

C2A domain first repeat present in Synaptotagmin 8; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176033 [Multi-domain]  Cd Length: 124  Bit Score: 95.55  E-value: 2.11e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4794 TGEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRgqvmvvqnasvENKRRTKYVQKSLNPEWNQTV 4873
Cdd:cd08387      2 RGELHFSLEYDKDMGILNVKLIQARNLQPRDFSGTADPYCKVRLLPDR-----------SNTKQSKIHKKTLNPEFDESF 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2069550323 4874 IYKnISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSSSQLDNTPRWYTLK 4927
Cdd:cd08387     71 VFE-VPPQELPKRTLEVLLYDFDQFSRDECIGVVELPLAEVDLSEKLDLWRKIQ 123
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 4795-4926 3.64e-22

C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 95.34  E-value: 3.64e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4795 GEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQVmvvqnasveNKRRTKYVQKSLNPEWNQTVI 4874
Cdd:cd00276      1 GELLLSLSYLPTAERLTVVVLKARNLPPSDGKGLSDPYVKVSLLQGGKKL---------KKKKTSVKKGTLNPVFNEAFS 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069550323 4875 YkNISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLI-ELSSSSQLD------NTPR-----WYTL 4926
Cdd:cd00276     72 F-DVPAEQLEEVSLVITVVDKDSVGRNEVIGQVVLgPDSGGEELEhwnemlASPRkpiarWHKL 134
C2B_Synaptotagmin-1 cd08402
C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking ...
 4795-4927 9.11e-22

C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 1, a member of the class 1 synaptotagmins, is located in the brain and endocranium and localized to the synaptic vesicles and secretory granules. It functions as a Ca2+ sensor for fast exocytosis. It, like synaptotagmin-2, has an N-glycosylated N-terminus. Synaptotagmin 4, a member of class 4 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmin-11, has an Asp to Ser substitution in its C2A domain. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176047 [Multi-domain]  Cd Length: 136  Bit Score: 94.39  E-value: 9.11e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4795 GEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQVmvvqnasveNKRRTKYVQKSLNPEWNQTVI 4874
Cdd:cd08402      2 GDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRL---------KKKKTTIKKRTLNPYYNESFS 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069550323 4875 YKnISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLI-------ELSSSSQLDNTPR-----WYTLK 4927
Cdd:cd08402     73 FE-VPFEQIQKVHLIVTVLDYDRIGKNDPIGKVVLgcnatgaELRHWSDMLASPRrpiaqWHTLQ 136
C2B_Munc13-like cd04009
C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are ...
 4795-4913 1.75e-19

C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175976 [Multi-domain]  Cd Length: 133  Bit Score: 87.68  E-value: 1.75e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4795 GEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQVMVVqnasvenKRRTKYVQKSLNPEWNQTvI 4874
Cdd:cd04009      3 GVLTVKAYYRASEQSLRVEILNARNLLPLDSNGSSDPFVKVELLPRHLFPDVP-------TPKTQVKKKTLFPLFDES-F 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2069550323 4875 YKNISMEQLKKK--TLEVTVWDYDRFSSNDFLGEVLIELSS 4913
Cdd:cd04009     75 EFNVPPEQCSVEgaLLLFTVKDYDLLGSNDFEGEAFLPLND 115
C2A_Synaptotagmin-15-17 cd08390
C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a ...
 4795-4912 2.78e-18

C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. It is thought to be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues and is Ca2+ independent. Human synaptotagmin 15 has 2 alternatively spliced forms that encode proteins with different C-termini. The larger, SYT15a, contains a N-terminal TM region, a putative fatty-acylation site, and 2 tandem C terminal C2 domains. The smaller, SYT15b, lacks the C-terminal portion of the second C2 domain. Unlike most other synaptotagmins it is nearly absent in the brain and rather is found in the heart, lungs, skeletal muscle, and testis. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176036 [Multi-domain]  Cd Length: 123  Bit Score: 83.85  E-value: 2.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4795 GEIQLQVNYDKHLGNLIIHILQARNLAPRD-NNGYSDPFVKVYLLPGRGQVmvvqnasvenkRRTKYVQKSLNPEWNQTV 4873
Cdd:cd08390      1 GRLWFSVQYDLEEEQLTVSLIKARNLPPRTkDVAHCDPFVKVCLLPDERRS-----------LQSKVKRKTQNPNFDETF 69

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2069550323 4874 IYKnISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELS 4912
Cdd:cd08390     70 VFQ-VSFKELQRRTLRLSVYDVDRFSRHCIIGHVLFPLK 107
C2A_Synaptotagmin-like cd04024
C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 4808-4927 4.85e-17

C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 175990 [Multi-domain]  Cd Length: 128  Bit Score: 80.55  E-value: 4.85e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4808 GNLIIHILQARNLAPRD--NNGYSDPFVKVYLlpgrGqvmvvqnasvENKRRTKYVQKSLNPEWNqtvIYKNISMEQLKK 4885
Cdd:cd04024      1 GVLRVHVVEAKDLAAKDrsGKGKSDPYAILSV----G----------AQRFKTQTIPNTLNPKWN---YWCEFPIFSAQN 63

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2069550323 4886 KTLEVTVWDYDRFSSNDFLGEVLIELSSS---SQLDNTPRWYTLK 4927
Cdd:cd04024     64 QLLKLILWDKDRFAGKDYLGEFDIALEEVfadGKTGQSDKWITLK 108
C2A_Synaptotagmin-4-11 cd08388
C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a ...
 4795-4913 8.13e-17

C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmins 4 and 11, class 4 synaptotagmins, are located in the brain. Their functions are unknown. They are distinguished from the other synaptotagmins by having and Asp to Ser substitution in their C2A domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176034 [Multi-domain]  Cd Length: 128  Bit Score: 79.70  E-value: 8.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4795 GEIQLQVNYDKHLGNLIIHILQARNLAPRD-NNGYSDPFVKVYLLPGRgqvmvvqnasvENKRRTKYVQKSLNPEWNQTV 4873
Cdd:cd08388      3 GTLFFSLRYNSEKKALLVNIIECRDLPAMDeQSGTSDPYVKLQLLPEK-----------EHKVKTRVLRKTRNPVYDETF 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2069550323 4874 IYKNISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSS 4913
Cdd:cd08388     72 TFYGIPYNQLQDLSLHFAVLSFDRYSRDDVIGEVVCPLAG 111
C2D_Tricalbin-like cd04040
C2 domain fourth repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 4810-4913 1.10e-15

C2 domain fourth repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the fifth C2 repeat, C2E, and has a type-II topology.


Pssm-ID: 176005 [Multi-domain]  Cd Length: 115  Bit Score: 76.07  E-value: 1.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4810 LIIHILQARNLAPRDNNGYSDPFVKVYLlpgrgqvmvvqnasvENKR--RTKYVQKSLNPEWNQTViykNISMEQLKKKT 4887
Cdd:cd04040      1 LTVDVISAENLPSADRNGKSDPFVKFYL---------------NGEKvfKTKTIKKTLNPVWNESF---EVPVPSRVRAV 62

                           90       100
                   ....*....|....*....|....*.
gi 2069550323 4888 LEVTVWDYDRFSSNDFLGEVLIELSS 4913
Cdd:cd04040     63 LKVEVYDWDRGGKDDLLGSAYIDLSD 88
C2D_Ferlin cd04017
C2 domain fourth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 4812-4927 1.35e-15

C2 domain fourth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the fourth C2 repeat, C2D, and has a type-II topology.


Pssm-ID: 175984 [Multi-domain]  Cd Length: 135  Bit Score: 76.43  E-value: 1.35e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4812 IHILQARNLAPRDNNGYSDPFVKVYLLpGRGQvmvvqnasvenkrRTKYVQKSLNPEWNQTVIYKNISMEQLKKKTLE-- 4889
Cdd:cd04017      5 AYIYQARDLLAADKSGLSDPFARVSFL-NQSQ-------------ETEVIKETLSPTWDQTLIFDEVELYGSPEEIAQnp 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2069550323 4890 ----VTVWDYDRFSSNDFLGEVLI--ELSSSSQLDNTP--RWYTLK 4927
Cdd:cd04017     71 plvvVELFDQDSVGKDEFLGRSVAkpLVKLDLEEDFPPklQWFPIY 116
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 4609-4687 1.89e-15

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: 74.12  E-value: 1.89e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069550323 4609 SGNGLGIRIVGGKEIPGtngeiGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEAEICVR 4687
Cdd:cd00136      8 PGGGLGFSIRGGKDGGG-----GIFVSRVEPGGPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELLKSAGGEVTLTVR 81
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
 5137-5262 1.91e-15

C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins are uncharacterized human proteins. They were compiled by the Kazusa mammalian cDNA project which identified more than 2000 human genes. They are identified by 4 digit codes that precede the KIAA designation. Many KIAA genes are still functionally uncharacterized including KIAA1228. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175996 [Multi-domain]  Cd Length: 127  Bit Score: 75.77  E-value: 1.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5137 GEIKIALkkEMKTDGEQLIVEILQCRNITykFKSPDHLPDLYVKLYVvnLATQKRVIKKKTRVCRHDREPSFNETFRFSL 5216
Cdd:cd04030      3 GRIQLTI--RYSSQRQKLIVTVHKCRNLP--PCDSSDIPDPYVRLYL--LPDKSKSTRRKTSVKKDNLNPVFDETFEFPV 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5217 SPTGHSLQILLVS--NGGKFM--KKTLIGEAYIWLDKVDLRKRIVNWHKL 5262
Cdd:cd04030     77 SLEELKRRTLDVAvkNSKSFLsrEKKLLGQVLIDLSDLDLSKGFTQWYDL 126
C2B_RIM1alpha cd04028
C2 domain second repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 5133-5267 2.69e-15

C2 domain second repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology and do not bind Ca2+.


Pssm-ID: 175994 [Multi-domain]  Cd Length: 146  Bit Score: 76.27  E-value: 2.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5133 TQVMGEIKIALkkeMKTDGeQLIVEILQCRNITYKFKSpDHLPDLYVKLYVvnLATQKRVIKKKTRVCRHDREPSFNETF 5212
Cdd:cd04028     14 SPSMGDIQLGL---YDKKG-QLEVEVIRARGLVQKPGS-KVLPAPYVKVYL--LEGKKCIAKKKTKIARKTLDPLYQQQL 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2069550323 5213 RFSLSPTGHSLQILLVSNGGKFMKKTLIGEAYIWLDKVDLRKRIVNWHKLLVSST 5267
Cdd:cd04028     87 VFDVSPTGKTLQVIVWGDYGRMDKKVFMGVAQILLDDLDLSNLVIGWYKLFPTSS 141
C2E_Ferlin cd04037
C2 domain fifth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 4812-4911 3.36e-15

C2 domain fifth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the fifth C2 repeat, C2E, and has a type-II topology.


Pssm-ID: 176002 [Multi-domain]  Cd Length: 124  Bit Score: 74.89  E-value: 3.36e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4812 IHILQARNLAPRDNNGYSDPFVKvyllpgrgqvmvVQNASVENKRRTKYVQKSLNPEWNQTVIYK-NISMEqlkkKTLEV 4890
Cdd:cd04037      4 VYVVRARNLQPKDPNGKSDPYLK------------IKLGKKKINDRDNYIPNTLNPVFGKMFELEaTLPGN----SILKI 67

                           90       100
                   ....*....|....*....|.
gi 2069550323 4891 TVWDYDRFSSNDFLGEVLIEL 4911
Cdd:cd04037     68 SVMDYDLLGSDDLIGETVIDL 88
C2B_RasA1_RasA4 cd04025
C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase ...
 4813-4926 6.90e-15

C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase activating protein 1s ), Ras-specific GAP members, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. Both proteins contain two C2 domains, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) zinc binding domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175991 [Multi-domain]  Cd Length: 123  Bit Score: 74.06  E-value: 6.90e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4813 HILQARNLAPRDNNGYSDPFVKVYLlpgRGQVmvvqnasvenkRRTKYVQKSLNPEWNQTVIYKnisMEQLKKKTLEVTV 4892
Cdd:cd04025      5 HVLEARDLAPKDRNGTSDPFVRVFY---NGQT-----------LETSVVKKSCYPRWNEVFEFE---LMEGADSPLSVEV 67

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2069550323 4893 WDYDRFSSNDFLGEVLIELSSSSQLDNTPRWYTL 4926
Cdd:cd04025     68 WDWDLVSKNDFLGKVVFSIQTLQQAKQEEGWFRL 101
C2C_MCTP_PRT cd08377
C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 4808-4930 1.53e-14

C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); MCTPs are involved in Ca2+ signaling at the membrane. The cds in this family contain multiple C2 domains as well as a C-terminal PRT domain. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 176023 [Multi-domain]  Cd Length: 119  Bit Score: 73.10  E-value: 1.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4808 GNLIIHILQARNLAPRDNNGYSDPFVkvyllpgrgqVMVVQNASVenkrRTKYVQKSLNPEWNQTVIY--KNISmeqlkk 4885
Cdd:cd08377      1 GFLQVKVIRASGLAAADIGGKSDPFC----------VLELVNARL----QTHTIYKTLNPEWNKIFTFpiKDIH------ 60

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2069550323 4886 KTLEVTVWDYDRFSSNDFLGEVLIELSSSSqlDNTPRWYTLKEQS 4930
Cdd:cd08377     61 DVLEVTVYDEDKDKKPEFLGKVAIPLLSIK--NGERKWYALKDKK 103
C2A_MCTP_PRT_plant cd04022
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 4810-4930 1.62e-14

C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset; MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 175989 [Multi-domain]  Cd Length: 127  Bit Score: 73.14  E-value: 1.62e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4810 LIIHILQARNLAPRDNNGYSDPFVKVYLLpgrGQvmvvqnasvenKRRTKYVQKSLNPEWNQTVIYKNISMEQLKKKTLE 4889
Cdd:cd04022      2 LVVEVVDAQDLMPKDGQGSSSAYVELDFD---GQ-----------KKRTRTKPKDLNPVWNEKLVFNVSDPSRLSNLVLE 67

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2069550323 4890 VTVWDYDRFS-SNDFLGEVLIELSS-SSQLDNTPRWYTLKEQS 4930
Cdd:cd04022     68 VYVYNDRRSGrRRSFLGRVRISGTSfVPPSEAVVQRYPLEKRG 110
C2B_RasGAP cd08675
C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
 4810-4935 2.29e-14

C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. The proteins here all contain two tandem C2 domains, a Ras-GAP domain, and a pleckstrin homology (PH)-like domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 176057 [Multi-domain]  Cd Length: 137  Bit Score: 73.18  E-value: 2.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4810 LIIHILQARNLAPRdNNGYSDPFVKVYLLPGRGQVMvvqnasvenkRRTKYVQKSLNPEWNQTVIY------------KN 4877
Cdd:cd08675      1 LSVRVLECRDLALK-SNGTCDPFARVTLNYSSKTDT----------KRTKVKKKTNNPRFDEAFYFeltigfsyekksFK 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2069550323 4878 ISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSSSQLDNTPRWYTLKEQSESIDH 4935
Cdd:cd08675     70 VEEEDLEKSELRVELWHASMVSGDDFLGEVRIPLQGLQQAGSHQAWYFLQPREAPGTR 127
C2B_RIM1alpha cd04028
C2 domain second repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 4792-4934 3.95e-14

C2 domain second repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology and do not bind Ca2+.


Pssm-ID: 175994 [Multi-domain]  Cd Length: 146  Bit Score: 72.81  E-value: 3.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4792 PITGEIQLQVNYDKhlGNLIIHILQARNLAPRDNNGY-SDPFVKVYLLPGRgqvmvvqnASVEnKRRTKYVQKSLNPEWN 4870
Cdd:cd04028     15 PSMGDIQLGLYDKK--GQLEVEVIRARGLVQKPGSKVlPAPYVKVYLLEGK--------KCIA-KKKTKIARKTLDPLYQ 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069550323 4871 QTVIYKnismEQLKKKTLEVTVW-DYDRFSSNDFLGEVLIELSSSSQLDNTPRWYTLKEQSESID 4934
Cdd:cd04028     84 QQLVFD----VSPTGKTLQVIVWgDYGRMDKKVFMGVAQILLDDLDLSNLVIGWYKLFPTSSLVD 144
PDZ1_GgSTXBP4-like cd06692
PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, ...
 4611-4691 5.15e-14

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: 70.33  E-value: 5.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4611 NGLGIRIVGGKEiPGTNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSgeAEICVRLDI 4690
Cdd:cd06692      8 KGLGIKIIGGYR-ENTGEEFGIFIKRILPGGLAATDGRLKEGDLILEVNGESLQGVTNERAVSILRSAS--ASNHMSLLI 84


                   .
gi 2069550323 4691 S 4691
Cdd:cd06692     85 A 85
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 5153-5259 5.52e-14

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 70.98  E-value: 5.52e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  5153 QLIVEILQCRNITYKFKSpdHLPDLYVKLYVVNlatqKRVIKKKTRVCRHDREPSFNETFRFSLSPTGHSLQILLVSNGG 5232
Cdd:smart00239    1 TLTVKIISARNLPPKDKG--GKSDPYVKVSLDG----DPKEKKKTKVVKNTLNPVWNETFEFEVPPPELAELEIEVYDKD 74

                            90       100
                    ....*....|....*....|....*..
gi 2069550323  5233 KFMKKTLIGEAYIWLDKVDLRKRIVNW 5259
Cdd:smart00239   75 RFGRDDFIGQVTIPLSDLLLGGRHEKL 101
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
 5152-5262 5.86e-14

C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 71.85  E-value: 5.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5152 EQLIVEILQCRNItyKFKSPDHLPDLYVKLYVVNLAtqKRVIKKKTRVCRHDREPSFNETFRFSLSPT---GHSLQILLV 5228
Cdd:cd00276     14 ERLTVVVLKARNL--PPSDGKGLSDPYVKVSLLQGG--KKLKKKKTSVKKGTLNPVFNEAFSFDVPAEqleEVSLVITVV 89

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2069550323 5229 SNgGKFMKKTLIGEAYI-----------WLDKVD-LRKRIVNWHKL 5262
Cdd:cd00276     90 DK-DSVGRNEVIGQVVLgpdsggeelehWNEMLAsPRKPIARWHKL 134
C2A_SLP cd08521
C2 domain first repeat present in Synaptotagmin-like proteins; All Slp members basically share ...
 5137-5262 8.31e-14

C2 domain first repeat present in Synaptotagmin-like proteins; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike the case in Slp3 and Slp4/granuphilin in which their C2A domains are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp3 and Slp4/granuphilin promote dense-core vesicle exocytosis. Slp5 mRNA has been shown to be restricted to human placenta and liver suggesting a role in Rab27A-dependent membrane trafficking in specific tissues. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176056 [Multi-domain]  Cd Length: 123  Bit Score: 71.13  E-value: 8.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5137 GEIKIALKKEMKTDGeqLIVEILQCRNITYKfKSPDHLPDLYVKLYVvnLATQKRVIKKKTRVCRHDREPSFNETFRFSL 5216
Cdd:cd08521      1 GEIEFSLSYNYKTGS--LEVHIKECRNLAYA-DEKKKRSNPYVKVYL--LPDKSKQSKRKTSVKKNTTNPVFNETLKYHI 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2069550323 5217 SPTGHSLQILLVS--NGGKFMKKTLIGEAYIWLDKVDLRKRIVNWHKL 5262
Cdd:cd08521     76 SKSQLETRTLQLSvwHHDRFGRNTFLGEVEIPLDSWDLDSQQSEWYPL 123
C2B_Synaptotagmin-4 cd08404
C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking ...
 4795-4915 8.89e-14

C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 4, a member of class 4 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmin-11, has an Asp to Ser substitution in its C2A domain. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176049 [Multi-domain]  Cd Length: 136  Bit Score: 71.30  E-value: 8.89e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4795 GEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQVmvvqnasveNKRRTKYVQKSLNPEWNQTVI 4874
Cdd:cd08404      2 GELLLSLCYQPTTNRLTVVVLKARHLPKMDVSGLADPYVKVNLYYGKKRI---------SKKKTHVKKCTLNPVFNESFV 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2069550323 4875 YkNISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSSS 4915
Cdd:cd08404     73 F-DIPSEELEDISVEFLVLDSDRVTKNEVIGRLVLGPKASG 112
C2 pfam00168
C2 domain;
5153-5262 2.07e-13

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 69.27  E-value: 2.07e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5153 QLIVEILQCRNITYKFKSPdhLPDLYVKLYVvnlatQKRVIKKKTRVCRHDREPSFNETFRFSLSPTGHSLQILLVSNGG 5232
Cdd:pfam00168    2 RLTVTVIEAKNLPPKDGNG--TSDPYVKVYL-----LDGKQKKKTKVVKNTLNPVWNETFTFSVPDPENAVLEIEVYDYD 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 2069550323 5233 KFMKKTLIGEAYIWLDKVDLRKRIVNWHKL 5262
Cdd:pfam00168   75 RFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 5154-5262 7.98e-13

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 67.48  E-value: 7.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5154 LIVEILQCRNITYKFKSpdHLPDLYVKLYVVNlatqkrVIKKKTRVCRHDREPSFNETFRFSLSPTGHSLQILLVSNGGK 5233
Cdd:cd00030      1 LRVTVIEARNLPAKDLN--GKSDPYVKVSLGG------KQKFKTKVVKNTLNPVWNETFEFPVLDPESDTLTVEVWDKDR 72

                           90       100       110
                   ....*....|....*....|....*....|
gi 2069550323 5234 FMKKTLIGEAYIWLDKV-DLRKRIVNWHKL 5262
Cdd:cd00030     73 FSKDDFLGEVEIPLSELlDSGKEGELWLPL 102
C2A_fungal cd04041
C2 domain first repeat; fungal group; C2 domains were first identified in Protein Kinase C ...
 4808-4930 1.44e-12

C2 domain first repeat; fungal group; C2 domains were first identified in Protein Kinase C (PKC). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176006 [Multi-domain]  Cd Length: 111  Bit Score: 67.29  E-value: 1.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4808 GNLIIHILQARNLAPRDNN-GYSDPFVKVYLlpgrgqvmvvqNASVENKRRTKYVQKSLNPEWNQTVIYKNISMEQLKKK 4886
Cdd:cd04041      1 GVLVVTIHRATDLPKADFGtGSSDPYVTASF-----------AKFGKPLYSTRIIRKDLNPVWEETWFVLVTPDEVKAGE 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2069550323 4887 TLEVTVWDYDRFSSNDFLGEVLIELSSssqLDNTPRWYTLKEQS 4930
Cdd:cd04041     70 RLSCRLWDSDRFTADDRLGRVEIDLKE---LIEDRNWMGRREDG 110
C2A_SLP-3 cd08392
C2 domain first repeat present in Synaptotagmin-like protein 3; All Slp members basically ...
 4794-4927 1.85e-12

C2 domain first repeat present in Synaptotagmin-like protein 3; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. SHD of Slp (except for the Slp4-SHD) function as a specific Rab27A/B-binding domain. In addition to Slp, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. Little is known about the expression or localization of Slp3. The C2A domain of Slp3 is Ca2+ dependent. It has been demonstrated that Slp3 promotes dense-core vesicle exocytosis. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176038 [Multi-domain]  Cd Length: 128  Bit Score: 67.55  E-value: 1.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4794 TGEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYS-DPFVKVYLLPGRgqvmvvqnaSVENKRRTKYVQKSLNPEWNQT 4872
Cdd:cd08392      1 TGEIEFALHYNFRTSCLEITIKACRNLAYGDEKKKKcHPYVKVCLLPDK---------SHNSKRKTAVKKGTVNPVFNET 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2069550323 4873 VIYKnISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSSSQLDNTP---RWYTLK 4927
Cdd:cd08392     72 LKYV-VEADLLSSRQLQVSVWHSRTLKRRVFLGEVLIPLADWDFEDTDSqrfLWYPLN 128
C2A_MCTP_PRT cd04042
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 4810-4935 4.26e-12

C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); MCTPs are involved in Ca2+ signaling at the membrane. MCTP is composed of a variable N-terminal sequence, three C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176007 [Multi-domain]  Cd Length: 121  Bit Score: 66.15  E-value: 4.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4810 LIIHILQARNLAPRDNNGYSDPFVKVYLlpgrGQVMVVqnasvenkrRTKYVQKSLNPEWNQTVIyknISMEQLKKKtLE 4889
Cdd:cd04042      2 LDIHLKEGRNLAARDRGGTSDPYVKFKY----GGKTVY---------KSKTIYKNLNPVWDEKFT---LPIEDVTQP-LY 64

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2069550323 4890 VTVWDYDRFSSNDFLGEVLIELSSSSQldNTPRWYTLKEQSESIDH 4935
Cdd:cd04042     65 IKVFDYDRGLTDDFMGSAFVDLSTLEL--NKPTEVKLKLEDPNSDE 108
C2B_Synaptotagmin-17 cd08410
C2 domain second repeat present in Synaptotagmin 17; Synaptotagmin is a membrane-trafficking ...
 4795-4914 6.54e-12

C2 domain second repeat present in Synaptotagmin 17; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176055 [Multi-domain]  Cd Length: 135  Bit Score: 66.07  E-value: 6.54e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4795 GEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRgqvmvvqnaSVENKRRTKYVQKSLNPEWNQTVI 4874
Cdd:cd08410      1 GELLLSLNYLPSAGRLNVDIIRAKQLLQTDMSQGSDPFVKIQLVHGL---------KLIKTKKTSCMRGTIDPFYNESFS 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2069550323 4875 YKnISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSS 4914
Cdd:cd08410     72 FK-VPQEELENVSLVFTVYGHNVKSSNDFIGRIVIGQYSS 110
C2B_Synaptotagmin-3-5-6-9-10 cd08403
C2 domain second repeat present in Synaptotagmins 3, 5, 6, 9, and 10; Synaptotagmin is a ...
 4795-4905 6.97e-12

C2 domain second repeat present in Synaptotagmins 3, 5, 6, 9, and 10; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 3, a member of class 3 synaptotagmins, is located in the brain and localized to the active zone and plasma membrane. It functions as a Ca2+ sensor for fast exocytosis. It, along with synaptotagmins 5,6, and 10, has disulfide bonds at its N-terminus. Synaptotagmin 9, a class 5 synaptotagmins, is located in the brain and localized to the synaptic vesicles. It is thought to be a Ca2+-sensor for dense-core vesicle exocytosis. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176048 [Multi-domain]  Cd Length: 134  Bit Score: 65.99  E-value: 6.97e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4795 GEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLpGRGQVMvvqnasveNKRRTKYVQKSLNPEWNQTVI 4874
Cdd:cd08403      1 GELMFSLCYLPTAGRLTLTIIKARNLKAMDITGFSDPYVKVSLM-CEGRRL--------KKKKTSVKKNTLNPTYNEALV 71

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2069550323 4875 YkNISMEQLKKKTLEVTVWDYDRFSSNDFLG 4905
Cdd:cd08403     72 F-DVPPENVDNVSLIIAVVDYDRVGHNELIG 101
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 4609-4687 1.43e-11

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 63.55  E-value: 1.43e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069550323  4609 SGNGLGIRIVGGKEIPGtngeiGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEAEICVR 4687
Cdd:smart00228   10 GGGGLGFSLVGGKDEGG-----GVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
C2A_Munc13-like cd08676
C2 domain first repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are ...
 4810-4926 1.65e-11

C2 domain first repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176058 [Multi-domain]  Cd Length: 153  Bit Score: 65.47  E-value: 1.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4810 LIIHILQARNLAPRDNNGYSDPFVKVYLLPG---------------RGQVMVVQNASVENKRRTKYVQKSLNPEWNQTVI 4874
Cdd:cd08676     30 LKVTVIEAKGLLAKDVNGFSDPYCMLGIVPAsrernsekskkrkshRKKAVLKDTVPAKSIKVTEVKPQTLNPVWNETFR 109

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2069550323 4875 YKnisMEQLKKKTLEVTVWDYDrfssNDFLGEVLIELSSSSQlDNTPRWYTL 4926
Cdd:cd08676    110 FE---VEDVSNDQLHLDIWDHD----DDFLGCVNIPLKDLPS-CGLDSWFKL 153
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
 4808-4937 1.81e-11

C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains either the first or third repeat in Synaptotagmin-like proteins with a type-I topology.


Pssm-ID: 176037 [Multi-domain]  Cd Length: 121  Bit Score: 64.24  E-value: 1.81e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4808 GNLIIHILQARNLAPRDNN------GYSDPFVKVyllpgrgQVMvvqnasvENKRRTKYVQKSLNPEWNQT---VIYkni 4878
Cdd:cd08391      1 GVLRIHVIEAQDLVAKDKFvgglvkGKSDPYVIV-------RVG-------AQTFKSKVIKENLNPKWNEVyeaVVD--- 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2069550323 4879 smeQLKKKTLEVTVWDYDRfSSNDFLGEVLIELSSSSQLDNTPRWYTLkeqsESIDHGK 4937
Cdd:cd08391     64 ---EVPGQELEIELFDEDP-DKDDFLGRLSIDLGSVEKKGFIDEWLPL----EDVKSGR 114
C2B_MCTP_PRT_plant cd08378
C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 4833-4926 2.89e-11

C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset; MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176024 [Multi-domain]  Cd Length: 121  Bit Score: 63.87  E-value: 2.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4833 VKVYLLPGRGQVMVVQNASVENKRRTKYVQKSLNPEWNQTVIyknISMEQLKKKTLEVTVWDYDrFSSNDFLGEVLIELS 4912
Cdd:cd08378      7 VKARGLPANSNDPVVEVKLGNYKGSTKAIERTSNPEWNQVFA---FSKDRLQGSTLEVSVWDKD-KAKDDFLGGVCFDLS 82

                           90       100
                   ....*....|....*....|.
gi 2069550323 4913 S-------SSQLdnTPRWYTL 4926
Cdd:cd08378     83 EvptrvppDSPL--APQWYRL 101
C2B_PI3K_class_II cd08381
C2 domain second repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are ...
 5175-5262 3.07e-11

C2 domain second repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a N-terminal C2 domain, a PIK domain, and a kinase catalytic domain. Unlike class I and class III, class II PI3Ks have additionally a PX domain and a C-terminal C2 domain containing a nuclear localization signal both of which bind phospholipids though in a slightly different fashion. PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176027 [Multi-domain]  Cd Length: 122  Bit Score: 63.85  E-value: 3.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5175 PDLYVKLYVvnLATQKRVIKKKTRVCRHDREPSFNETFRFSLSP----TGHSLQiLLVSNGGKFMKKTLIGEAYIWLDKV 5250
Cdd:cd08381     33 PDPYVKTYL--LPDPQKTTKRKTKVVRKTRNPTFNEMLVYDGLPvedlQQRVLQ-VSVWSHDSLVENEFLGGVCIPLKKL 109

                           90
                   ....*....|..
gi 2069550323 5251 DLRKRIVNWHKL 5262
Cdd:cd08381    110 DLSQETEKWYPL 121
C2_ArfGAP cd04038
C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating ...
 4807-4911 3.46e-11

C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating protein which regulates the ADP ribosylation factor Arf, a member of the Ras superfamily of GTP-binding proteins. The GTP-bound form of Arf is involved in Golgi morphology and is involved in recruiting coat proteins. ArfGAP is responsible for the GDP-bound form of Arf which is necessary for uncoating the membrane and allowing the Golgi to fuse with an acceptor compartment. These proteins contain an N-terminal ArfGAP domain containing the characteristic zinc finger motif (Cys-x2-Cys-x(16,17)-x2-Cys) and C-terminal C2 domain. C2 domains were first identified in Protein Kinase C (PKC). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176003 [Multi-domain]  Cd Length: 145  Bit Score: 64.27  E-value: 3.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4807 LGNLIIHILQARNLAPRDNNGySDPFVkvyllpgrgqVMVVQNASVenkrRTKYVQKSLNPEWNQ--TVIYKNIsMEQLK 4884
Cdd:cd04038      1 LGLLKVRVVRGTNLAVRDFTS-SDPYV----------VLTLGNQKV----KTRVIKKNLNPVWNEelTLSVPNP-MAPLK 64

                           90       100
                   ....*....|....*....|....*..
gi 2069550323 4885 kktleVTVWDYDRFSSNDFLGEVLIEL 4911
Cdd:cd04038     65 -----LEVFDKDTFSKDDSMGEAEIDL 86
C2B_MCTP_PRT cd08376
C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 4812-4913 5.40e-11

C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); MCTPs are involved in Ca2+ signaling at the membrane. MCTP is composed of a variable N-terminal sequence, three C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176022 [Multi-domain]  Cd Length: 116  Bit Score: 62.66  E-value: 5.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4812 IHILQARNLAPRDNNGYSDPFVKVYLlpgRGQvmvvqnasvenKRRTKYVQKSLNPEWnqtviyknisMEQL-------K 4884
Cdd:cd08376      4 IVLVEGKNLPPMDDNGLSDPYVKFRL---GNE-----------KYKSKVCSKTLNPQW----------LEQFdlhlfddQ 59

                           90       100
                   ....*....|....*....|....*....
gi 2069550323 4885 KKTLEVTVWDYDRFSSNDFLGEVLIELSS 4913
Cdd:cd08376     60 SQILEIEVWDKDTGKKDEFIGRCEIDLSA 88
PHA03247 PHA03247
large tegument protein UL36; Provisional
 23-433 5.46e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 69.97  E-value: 5.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323   23 PSEGPRLPSGEAPDLSQLSE--AERRQIAAVLSRAQDPS--PRHAQldsshhPRQPGKPPDSGP-PTLSKSRTVDTLKTE 97
Cdd:PHA03247  2552 PPPLPPAAPPAAPDRSVPPPrpAPRPSEPAVTSRARRPDapPQSAR------PRAPVDDRGDPRgPAPPSPLPPDTHAPD 2625

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323   98 QRVPGRSPSSISLRQSTSrtdfkedqKPSMMPSFLSDANPFGAVTSVVNKFNPFDLISDSDTAQ----EEASKKQKPIQK 173
Cdd:PHA03247  2626 PPPPSPSPAANEPDPHPP--------PTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQrprrRAARPTVGSLTS 2697

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  174 EQDKPGQQKGPSKQPVQQQS--PKPTGPQQGSVKPAPQKTAPPKQVVPQQQQQQQQQQQQPGVPKQAQKPGPGQQAGPQS 251
Cdd:PHA03247  2698 LADPPPPPPTPEPAPHALVSatPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAA 2777

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  252 eeakkqqGAPKTQPQQSESTKTPPQQQQQSPAKPPPQQPGTARASPQQANASKTSSQVPTPTKATVAQQGISTGKQPSQQ 331
Cdd:PHA03247  2778 -------GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSL 2850

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  332 -------PGGPT--KPAPQSAGANKQATQQQGSAAKPAPQQTGPTKQQLQQPGEPAKPSAQQAGPTKQPQHQAEPtKPTG 402
Cdd:PHA03247  2851 plggsvaPGGDVrrRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPP-PPQP 2929

                          410       420       430
                   ....*....|....*....|....*....|.
gi 2069550323  403 QKPGPVQQKPEASPPQASQPGGSASKKTFCP 433
Cdd:PHA03247  2930 QPPPPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960
C2_Intersectin cd08375
C2 domain present in Intersectin; A single instance of the C2 domain is located C terminally ...
 4808-4913 1.73e-10

C2 domain present in Intersectin; A single instance of the C2 domain is located C terminally in the intersectin protein. Intersectin functions as a scaffolding protein, providing a link between the actin cytoskeleton and the components of endocytosis and plays a role in signal transduction. In addition to C2, intersectin contains several additional domains including: Eps15 homology domains, SH3 domains, a RhoGEF domain, and a PH domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. The members here have topology I.


Pssm-ID: 176021 [Multi-domain]  Cd Length: 136  Bit Score: 62.02  E-value: 1.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4808 GNLIIHILQARNLAPRDNNGYSDPFVKVyllpgrgqVMVVQnasvenKRRTKYVQKSLNPEWNQTVIYKNISMEQlkkKT 4887
Cdd:cd08375     15 GRLMVVIVEGRDLKPCNSNGKSDPYCEV--------SMGSQ------EHKTKVVSDTLNPKWNSSMQFFVKDLEQ---DV 77

                           90       100
                   ....*....|....*....|....*.
gi 2069550323 4888 LEVTVWDYDRFSSNDFLGEVLIELSS 4913
Cdd:cd08375     78 LCITVFDRDFFSPDDFLGRTEIRVAD 103
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 ...
 4610-4687 2.15e-10

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: 59.98  E-value: 2.15e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069550323 4610 GNGLGIRIVGGKEIPgtNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEE-VQSIISQQSGEAEICVR 4687
Cdd:cd06759     11 GKGLGFSIVGGRDSP--RGPMGIYVKTIFPGGAAAEDGRLKEGDEILEVNGESLQGLTHQEaIQKFKQIKKGLVVLTVR 87
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 159-465 2.47e-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: 2.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  159 TAQEEASKKQKPIQKEQDKPGQQKGPSKQPVQQQSPK-------PTGPQQ---GSVKPAPQKTAPPKQVVPQQQQQQQQQ 228
Cdd:pfam03157  443 PGQGQQPGQEQPGQGQQPGQGQQGQQPGQPEQGQQPGqgqpgyyPTSPQQsgqGQQLGQWQQQGQGQPGYYPTSPLQPGQ 522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  229 QQQPGVPKQAQKPGPGQQAGPQSEEAKKQQGAPKTQPQQSESTKTPPQQQQQSPAKPPPQ----------QPGTARASPQ 298
Cdd:pfam03157  523 GQPGYYPTSPQQPGQGQQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQGQQpgqgqqpgqgQPGYYPTSPQ 602

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  299 QANASKTSSQVPTPTKATVAQQGISTgKQPSQQPGGPTKPAPQSAGANKQATQQQGSAA------KPAPQQTGPTKQ--Q 370
Cdd:pfam03157  603 QSGQGQQPGQWQQPGQGQPGYYPTSS-LQLGQGQQGYYPTSPQQPGQGQQPGQWQQSGQgqqgyyPTSPQQSGQAQQpgQ 681

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  371 LQQPGEPAKPSAQQAG--PTKQPQHQAEPTKPTGQKPGPVQQKPEASPPQASQPGGSASKKTFCPLCTTTELLLHTPEKA 448
Cdd:pfam03157  682 GQQPGQWLQPGQGQQGyyPTSPQQPGQGQQLGQGQQSGQGQQGYYPTSPGQGQQSGQGQQGYDSPYHVSAEHQAASLKVA 761

                          330
                   ....*....|....*..
gi 2069550323  449 NYNTCTQCQTVVCSLCG 465
Cdd:pfam03157  762 KAQQLAAQLPAMCRLEG 778
PHA03247 PHA03247
large tegument protein UL36; Provisional
 329-730 6.14e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 66.50  E-value: 6.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  329 SQQPGGPTKPAPqsAGANKQATQQQGSAAKPAPQQTGPTKQ-QLQQPGEPAKPSAQQA--GPTKQPQHQAEPTK--PTGQ 403
Cdd:PHA03247  2545 SDDAGDPPPPLP--PAAPPAAPDRSVPPPRPAPRPSEPAVTsRARRPDAPPQSARPRApvDDRGDPRGPAPPSPlpPDTH 2622

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  404 KPGPVQQKPEASPPQASQPGGSASKKTFCPLCTTTELLLHTPEKANyntcTQCQTVVCSLCGFNPNPhiteikewlclnc 483
Cdd:PHA03247  2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRAR----RLGRAAQASSPPQRPRR------------- 2685

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  484 qmqRALGGDLG--------PAPGPGPQSSAPKQKMAAPTTAGKPPPQAQQPTQKKESTVK--PDATQSPEHKKPPPPQTK 553
Cdd:PHA03247  2686 ---RAARPTVGsltsladpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPavPAGPATPGGPARPARPPT 2762

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  554 QPTIPSSTPEKAKPPAPE-----------TQQTESTPKSDQTKPAPAEDKQKQPHVQKPISDVVPKPSEFDTKQDSPGPK 622
Cdd:PHA03247  2763 TAGPPAPAPPAAPAAGPPrrltrpavaslSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPP 2842

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  623 PAPVQQKVvhPQGSEVAK----SSEDTPQDKTVPPDTKTSPQVSRqksdpklVSQPgsgidtKVQKQTEPVEGKGDLKKM 698
Cdd:PHA03247  2843 PGPPPPSL--PLGGSVAPggdvRRRPPSRSPAAKPAAPARPPVRR-------LARP------AVSRSTESFALPPDQPER 2907

                          410       420       430
                   ....*....|....*....|....*....|....
gi 2069550323  699 QPQ-MSPKPDAKQAQKPQQATVGPKP-TQSQPKA 730
Cdd:PHA03247  2908 PPQpQAPPPPQPQPQPPPPPQPQPPPpPPPRPQP 2941
C2_Kibra cd08680
C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador ...
 4797-4926 8.69e-10

C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador (Sav)/Warts (Wts)/Hippo (Hpo) (SWH) signaling network, which limits tissue growth by inhibiting cell proliferation and promoting apoptosis. The core of the pathway consists of a MST and LATS family kinase cascade that ultimately phosphorylates and inactivates the YAP/Yorkie (Yki) transcription coactivator. The FERM domain proteins Merlin (Mer) and Expanded (Ex) are part of the upstream regulation controlling pathway mechanism. Kibra colocalizes and associates with Mer and Ex and is thought to transduce an extracellular signal via the SWH network. The apical scaffold machinery that contains Hpo, Wts, and Ex recruits Yki to the apical membrane facilitating its inhibitory phosphorlyation by Wts. Since Kibra associates with Ex and is apically located it is hypothesized that KIBRA is part of the scaffold, helps in the Hpo/Wts complex, and helps recruit Yki for inactivation that promotes SWH pathway activity. Kibra contains two amino-terminal WW domains, an internal C2-like domain, and a carboxy-terminal glutamic acid-rich stretch. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176062  Cd Length: 124  Bit Score: 59.55  E-value: 8.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4797 IQLQVNYDKHLGNLIIHILQARNLA---PRDNngySDPFVKVYLLPGrgqvmvvqNASVENKRRTKYVQKSLNPEWNqTV 4873
Cdd:cd08680      3 VQIGLRYDSGDSSLVISVEQLRNLSalsIPEN---SKVYVRVALLPC--------SSSTSCLFRTKALEDQDKPVFN-EV 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2069550323 4874 IYKNISMEQLKKKTLEVTVWDYDRFSSNDFLGEV---LIELSSSSqlDNTPRWYTL 4926
Cdd:cd08680     71 FRVPISSTKLYQKTLQVDVCSVGPDQQEECLGGAqisLADFESSE--EMSTKWYNL 124
C2B_Munc13 cd04027
C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins; C2-like domains are ...
 4810-4931 1.34e-09

C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 175993 [Multi-domain]  Cd Length: 127  Bit Score: 59.12  E-value: 1.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4810 LIIHILQARNLAPRDNNGYSDPFVKVyllpgrgQVMVVqnasvenKRRTKYVQKSLNPEWNQTVIYK-NISMEQLKkktl 4888
Cdd:cd04027      3 ISITVVCAQGLIAKDKTGTSDPYVTV-------QVGKT-------KKRTKTIPQNLNPVWNEKFHFEcHNSSDRIK---- 64

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2069550323 4889 eVTVWDYD---------RFS--SNDFLGEVLIELSS-SSQLDntpRWYTLKEQSE 4931
Cdd:cd04027     65 -VRVWDEDddiksrlkqKFTreSDDFLGQTIIEVRTlSGEMD---VWYNLEKRTD 115
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 305-671 1.84e-09

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 64.62  E-value: 1.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  305 TSSQVPTPTKATVAQQGISTGKQPSQQPGGPTKPAPQSAGANKQATQQQGSAAKPAPQQTGPTKQQLQQPGEPAKPSAQQ 384
Cdd:PRK07764   387 VAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQP 466

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  385 A---GPTKQPQHQAEPTKPTGQKPGPVQQKP-EASPPQASQPG--------------GSASKKTFCPLctTTELLLHTPE 446
Cdd:PRK07764   467 ApapAAAPEPTAAPAPAPPAAPAPAAAPAAPaAPAAPAGADDAatlrerwpeilaavPKRSRKTWAIL--LPEATVLGVR 544

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  447 KanyntctqcQTVVCslcGF-NPN-------PHITE-----IKEWLCLNCQMQRALGGDLG------------------- 494
Cdd:PRK07764   545 G---------DTLVL---GFsTGGlarrfasPGNAEvlvtaLAEELGGDWQVEAVVGPAPGaaggegppapassgppeea 612

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  495 --PAPGPGPQSSAPKQKMAAPTTAGKPPPQAQQPTQKKESTVKPDATQSPEHKKPPPPQTKQPTIPSSTPEKAKPPAPET 572
Cdd:PRK07764   613 arPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAA 692

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  573 QQTEST----PKSDQTKPAPAEDKQKQPHVQKPIS---------DVVPKPSEFDTKQDSPGPKPAPVQQKVVHPQGSEVA 639
Cdd:PRK07764   693 PAGAAPaqpaPAPAATPPAGQADDPAAQPPQAAQGasapspaadDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAA 772

                          410       420       430
                   ....*....|....*....|....*....|..
gi 2069550323  640 KSSEDTPQDKTVPPDTKTSPQVSRQKSDPKLV 671
Cdd:PRK07764   773 APPPSPPSEEEEMAEDDAPSMDDEDRRDAEEV 804
C2A_SLP-4_5 cd04029
C2 domain first repeat present in Synaptotagmin-like proteins 4 and 5; All Slp members ...
 5137-5262 2.09e-09

C2 domain first repeat present in Synaptotagmin-like proteins 4 and 5; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. SHD of Slp (except for the Slp4-SHD) function as a specific Rab27A/B-binding domain. In addition to Slp, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp4/granuphilin promotes dense-core vesicle exocytosis. The C2A domain of Slp4 is Ca2+ dependent. Slp5 mRNA has been shown to be restricted to human placenta and liver suggesting a role in Rab27A-dependent membrane trafficking in specific tissues. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 175995 [Multi-domain]  Cd Length: 125  Bit Score: 58.60  E-value: 2.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5137 GEIKIALKKEMKTDGeqLIVEILQCRNITYKFKSpDHLPDLYVKLYVvnLATQKRVIKKKTRVCRHDREPSFNETFRFSL 5216
Cdd:cd04029      2 GEILFSLSYDYKTQS--LNVHVKECRNLAYGDEA-KKRSNPYVKTYL--LPDKSRQSKRKTSIKRNTTNPVYNETLKYSI 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2069550323 5217 SPT---GHSLQiLLVSNGGKFMKKTLIGEAYIWLDKVDLRKRIVNWHKL 5262
Cdd:cd04029     77 SHSqleTRTLQ-LSVWHYDRFGRNTFLGEVEIPLDSWNFDSQHEECLPL 124
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
 4593-4675 2.57e-09

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: 57.33  E-value: 2.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4593 PHARLKLPRDPkdhsvsGNGLGIRIVGGKEIPG--TNGEI--GAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTY 4668
Cdd:cd06671      1 PPRRVELWREP------GKSLGISIVGGRVMGSrlSNGEEirGIFIKHVLEDSPAGRNGTLKTGDRILEVNGVDLRNATH 74


                   ....*..
gi 2069550323 4669 EEVQSII 4675
Cdd:cd06671     75 EEAVEAI 81
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 159-423 3.22e-09

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: 63.81  E-value: 3.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  159 TAQEEASKKQKPIQKEQDKPGQQKGPSKQPVQQQSPK-------PTGPQQgSVKPAPQKTAPPKQVVPQQQQQQQQQQQQ 231
Cdd:pfam03157  372 TSQQQPQQGQQPEQGQQGQQQGQGQQGQQPGQGQQPGqgqpgyyPTSPQQ-SGQGQPGYYPTSPQQSGQGQQPGQGQQPG 450

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  232 PGVPKQAQKPGPGQQAG----PQSEE--AKKQQGAPKTQPQQS----------ESTKTPPQQQQQSPAKPPPQQPGTARA 295
Cdd:pfam03157  451 QEQPGQGQQPGQGQQGQqpgqPEQGQqpGQGQPGYYPTSPQQSgqgqqlgqwqQQGQGQPGYYPTSPLQPGQGQPGYYPT 530

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  296 SPQQANASKTSSQVPTPTKATVAQQgiSTGKQPSQQPGGPTKPAPQSAGankQATQQQGSAAKPAPQQTGPTKQQLQQPG 375
Cdd:pfam03157  531 SPQQPGQGQQLGQLQQPTQGQQGQQ--SGQGQQGQQPGQGQQGQQPGQG---QQGQQPGQGQQPGQGQPGYYPTSPQQSG 605

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2069550323  376 EPAKPSAQQAGPTKQPQHQAEPTKPTGQKPGPVQQKPEASPPQASQPG 423
Cdd:pfam03157  606 QGQQPGQWQQPGQGQPGYYPTSSLQLGQGQQGYYPTSPQQPGQGQQPG 653
C2_KIAA0528-like cd08688
C2 domain found in the Human KIAA0528 cDNA clone; The members of this CD are named after the ...
 4812-4913 3.39e-09

C2 domain found in the Human KIAA0528 cDNA clone; The members of this CD are named after the Human KIAA0528 cDNA clone. All members here contain a single C2 repeat. No other information on this protein is currently known. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176070 [Multi-domain]  Cd Length: 110  Bit Score: 57.32  E-value: 3.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4812 IHILQARNLAPRD-NNGYSDPFVKVYLlpgrgqvmvvqnASVENKrrTKYVQKSLNPEWNQTVIYKNISMEQLKKKTLEV 4890
Cdd:cd08688      3 VRVVAARDLPVMDrSSDLTDAFVEVKF------------GSTTYK--TDVVKKSLNPVWNSEWFRFEVDDEELQDEPLQI 68

                           90       100
                   ....*....|....*....|...
gi 2069550323 4891 TVWDYDRFSSNDFLGEVLIELSS 4913
Cdd:cd08688     69 RVMDHDTYSANDAIGKVYIDLNP 91
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 4597-4686 4.88e-09

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: 56.12  E-value: 4.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4597 LKLPRDPKdhsvsgnGLGIRIVGGK---EIPGTNGeigAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQS 4673
Cdd:cd06724      2 IKLVKGPK-------GLGFSIAGGVgnqHIPGDNG---IYVTKIIEGGAAQKDGRLQVGDKLLAVNDVSLEEVTHEEAVA 71

                           90
                   ....*....|...
gi 2069550323 4674 IISQQSGEAEICV 4686
Cdd:cd06724     72 ALKNTSDVVYLKV 84
PTZ00121 PTZ00121
MAEBL; Provisional
 989-1732 5.82e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 5.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  989 QVKSAETPQQQKaSARPAQNEKRGPDIQKEDPASQQGKPAKAISADKIQEiVQKEHTTPQQEKLPKTISADKLSQSISGE 1068
Cdd:PTZ00121  1132 EARKAEDARKAE-EARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEA-ARKAEEVRKAEELRKAEDARKAEAARKAE 1209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1069 D----SEIQKG----KIGKPPSADQVPKEEAKVvRKSSADKLLEIVQKKEPKELEHVSDNIQIQKEDPKVQQIRLSKPPS 1140
Cdd:PTZ00121  1210 EerkaEEARKAedakKAEAVKKAEEAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1141 ---ADQIRKEDPKVQQVKLSKtpSADQIRKED---PKVQQVKlTKAPSADQIRKEDPKIQQVKLAKAPSADQiqedpKLQ 1214
Cdd:PTZ00121  1289 kkkADEAKKAEEKKKADEAKK--KAEEAKKADeakKKAEEAK-KKADAAKKKAEEAKKAAEAAKAEAEAAAD-----EAE 1360

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1215 QGKfvKTPSADKIRQEDPKIHQEKLTKvpSDSEIKKVDPKIQQAKLAKiPSADHIQKEDSKLFKAKIVKTAS-----ADQ 1289
Cdd:PTZ00121  1361 AAE--EKAEAAEKKKEEAKKKADAAKK--KAEEKKKADEAKKKAEEDK-KKADELKKAAAAKKKADEAKKKAeekkkADE 1435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1290 LPKD-NKFQEMELANIPVEDYISSKTIHDQTQVARRKEDDTKFP----LSRESLHLAESRQKVAGEQFDEEKiEPKVLPK 1364
Cdd:PTZ00121  1436 AKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAeeakKADEAKKKAEEAKKKADEAKKAAE-AKKKADE 1514

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1365 TRQQEDIKREDLMMDIPESISKDQ-KSPKEETSAPPV----PLPKPDHVEAIREKAEKEDDKSDASSSQQQKSPqglsdt 1439
Cdd:PTZ00121  1515 AKKAEEAKKADEAKKAEEAKKADEaKKAEEKKKADELkkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK------ 1588

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1440 gyssdgISSSLGEIPSLIQSEEKDVLKESCKKEilsqESSPTSPSDLAKLES-----TVLSILEAQASTLAEEKSGKSKD 1514
Cdd:PTZ00121  1589 ------AEEARIEEVMKLYEEEKKMKAEEAKKA----EEAKIKAEELKKAEEekkkvEQLKKKEAEEKKKAEELKKAEEE 1658

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1515 IYGVYSEHSRVPHKTKTQlgAPESYSADEEDLAKQNIQGKyggAPEEGDKQDILSQKSYKGKTDTREDASARRQRYDSV- 1593
Cdd:PTZ00121  1659 NKIKAAEEAKKAEEDKKK--AEEAKKAEEDEKKAAEALKK---EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAe 1733

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1594 -------EDSSESENSPVPQRKRRTSVGSSSSDDYKAEDSPGSG--------DDEDFIRKQIMEMSADEDASGSE----- 1653
Cdd:PTZ00121  1734 eakkeaeEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeavieeelDEEDEKRRMEVDKKIKDIFDNFAniieg 1813

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1654 ----------DDEFIRNQLKEISITDSHKKEEMKNKKGIPGKHKRMTRKSSTGyEDDTSRRHSWHDDDDETFDESPEPKY 1723
Cdd:PTZ00121  1814 gkegnlvindSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNK-EADFNKEKDLKEDDEEEIEEADEIEK 1892


                   ....*....
gi 2069550323 1724 RETKSQDSE 1732
Cdd:PTZ00121  1893 IDKDDIERE 1901
C2A_Synaptotagmin-14_16 cd08389
C2A domain first repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are ...
 4795-4927 7.93e-09

C2A domain first repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are membrane-trafficking proteins in specific tissues outside the brain. Both of these contain C-terminal tandem C2 repeats, but only Synaptotagmin 14 has an N-terminal transmembrane domain and a putative fatty-acylation site. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium and this is indeed the case here. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176035 [Multi-domain]  Cd Length: 124  Bit Score: 56.87  E-value: 7.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4795 GEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQvmvvqnasvenKRRTKyVQKSLNPEWNQTVI 4874
Cdd:cd08389      3 GDLDVAFEYDPSARKLTVTVIRAQDIPTKDRGGASSWQVHLVLLPSKKQ-----------RAKTK-VQRGPNPVFNETFT 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2069550323 4875 YKNISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSSSQLDNTPRWYTLK 4927
Cdd:cd08389     71 FSRVEPEELNNMALRFRLYGVERMRKERLIGEKVVPLSQLNLEGETTVWLTLE 123
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 241-427 1.12e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 61.93  E-value: 1.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  241 PGPGQQAGPQSEEAKKQQGAPKTQPQQSESTKTPPQQQQQSPAKPPPQQPGTARASPQQANASKTSSQVPTPTKATVAQQ 320
Cdd:PRK07764   591 APGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWP 670

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  321 GISTGKQPSQQPGGPTKPAPQSAGANKQATQQQGSAAKPAPQQtgPTKQQLQQPGEPAKPSAQQAGPTKQPQHQAEPTKP 400
Cdd:PRK07764   671 AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQ--ADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDP 748

                          170       180
                   ....*....|....*....|....*..
gi 2069550323  401 TGQKPGPVQQKPEASPPQASQPGGSAS 427
Cdd:PRK07764   749 PDPAGAPAQPPPPPAPAPAAAPAAAPP 775
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
 4604-4680 1.29e-08

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: 55.05  E-value: 1.29e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069550323 4604 KDHSVSGN-GLGIRIVGGKeipGTN-GEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSG 4680
Cdd:cd06758      4 KMHLLKEKgGLGIQITGGK---GSKrGDIGIFVAGVEEGGSADRDGRLKKGDELLMINGQSLIGLSHQEAVAILRSSAS 79
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
 4810-4914 2.41e-08

C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated 4 (NEDD4) and NEDD4-like (NEDD4L/NEDD42); Nedd4 and Nedd4-2 are two of the nine members of the Human Nedd4 family. All vertebrates appear to have both Nedd4 and Nedd4-2 genes. They are thought to participate in the regulation of epithelial Na+ channel (ENaC) activity. They also have identical specificity for ubiquitin conjugating enzymes (E2). Nedd4 and Nedd4-2 are composed of a C2 domain, 2-4 WW domains, and a ubiquitin ligase Hect domain. Their WW domains can bind PPxY (PY) or LPSY motifs, and in vitro studies suggest that WW3 and WW4 of both proteins bind PY motifs in the key substrates, with WW3 generally exhibiting higher affinity. Most Nedd4 family members, especially Nedd4-2, also have multiple splice variants, which might play different roles in regulating their substrates. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175999 [Multi-domain]  Cd Length: 133  Bit Score: 55.82  E-value: 2.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4810 LIIHILQARNLAPRDNNGYSDPFVKVYLLPGrgqvmvvQNASVENKRRTKYVQKSLNPEWNQTVIYK-NISMEQLKkktL 4888
Cdd:cd04033      2 LRVKVLAGIDLAKKDIFGASDPYVKISLYDP-------DGNGEIDSVQTKTIKKTLNPKWNEEFFFRvNPREHRLL---F 71

                           90       100
                   ....*....|....*....|....*.
gi 2069550323 4889 EvtVWDYDRFSSNDFLGEVLIELSSS 4914
Cdd:cd04033     72 E--VFDENRLTRDDFLGQVEVPLNNL 95
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
 4611-4677 2.41e-08

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: 54.14  E-value: 2.41e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069550323 4611 NGLGIRIVGGKEIPGTNGeiGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQ 4677
Cdd:cd06792     12 GSLGISVTGGINTSVRHG--GIYVKSLVPGGAAEQDGRIQKGDRLLEVNGVSLEGVTHKQAVECLKN 76
C2A_Synaptotagmin-15-17 cd08390
C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a ...
 5146-5262 2.78e-08

C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. It is thought to be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues and is Ca2+ independent. Human synaptotagmin 15 has 2 alternatively spliced forms that encode proteins with different C-termini. The larger, SYT15a, contains a N-terminal TM region, a putative fatty-acylation site, and 2 tandem C terminal C2 domains. The smaller, SYT15b, lacks the C-terminal portion of the second C2 domain. Unlike most other synaptotagmins it is nearly absent in the brain and rather is found in the heart, lungs, skeletal muscle, and testis. Synaptotagmin 17 is located in the brain, kidney, and prostate and is thought to be a peripheral membrane protein. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176036 [Multi-domain]  Cd Length: 123  Bit Score: 55.34  E-value: 2.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5146 EMKTDGEQLIVEILQCRNITYKFKSPDHlPDLYVKLYVvnLATQKRVikKKTRVCRHDREPSFNETFRFSLSPT---GHS 5222
Cdd:cd08390      8 QYDLEEEQLTVSLIKARNLPPRTKDVAH-CDPFVKVCL--LPDERRS--LQSKVKRKTQNPNFDETFVFQVSFKelqRRT 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2069550323 5223 LQILLVSNgGKFMKKTLIGEAYIWLDKVDLRKRIVNWHKL 5262
Cdd:cd08390     83 LRLSVYDV-DRFSRHCIIGHVLFPLKDLDLVKGGVVWRDL 121
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 4610-4686 2.82e-08

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: 54.28  E-value: 2.82e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069550323 4610 GNGLGIRIVGGKeipgtNGEiGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEAEICV 4686
Cdd:cd06795     11 STGLGFNIVGGE-----DGE-GIFISFILAGGPADLSGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTIIA 81
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 4612-4687 3.08e-08

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: 53.98  E-value: 3.08e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069550323 4612 GLGIRIVGGKEipgTNGEIgaYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEAEICVR 4687
Cdd:cd06796     13 GLGFNVMGGKE---QNSPI--YISRIIPGGVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKLVVR 83
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 168-637 4.03e-08

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: 60.02  E-value: 4.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  168 QKPIQKEQDKPGQqkGPSKQPVQQQSPKPTGPQQGSVKPApqKTAPPKQVVPQQQQQQQQQQQQPGVPKQAQKPGPGQQA 247
Cdd:pfam09606   80 PDPINALQNLAGQ--GTRPQMMGPMGPGPGGPMGQQMGGP--GTASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPGGQA 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  248 GPQSEEAKKQQGapKTQPQQsestktppqqqqqspakpppqqpgtaraspQQANASKTSSQVPTPTkatVAQQGISTGKQ 327
Cdd:pfam09606  156 GGMMQPSSGQPG--SGTPNQ------------------------------MGPNGGPGQGQAGGMN---GGQQGPMGGQM 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  328 PSQQpGGPTKPAPQSAGAnkQATQQQGSAAKPAPQQTGPTKQQLQQPGEPAKPSAQQA---------GPTKQPQHQAEPT 398
Cdd:pfam09606  201 PPQM-GVPGMPGPADAGA--QMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSqlgmginqmQQMPQGVGGGAGQ 277

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  399 KPTGQKPGPVQQKPEASPPQASqpggsaskktfcplctttelllhtPEKANYNTCTQCQTVVCSLCGFNPNPHITEIkew 478
Cdd:pfam09606  278 GGPGQPMGPPGQQPGAMPNVMS------------------------IGDQNNYQQQQTRQQQQQQGGNHPAAHQQQM--- 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  479 lclNCQMQRalGGDLGPAPGpgpqssapkQKMAAPTTAGKPPPQAQQPTQKKESTVKPdaTQSPEHKKPPPPQTKQPTIP 558
Cdd:pfam09606  331 ---NQSVGQ--GGQVVALGG---------LNHLETWNPGNFGGLGANPMQRGQPGMMS--SPSPVPGQQVRQVTPNQFMR 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  559 SSTPEKAKPPAPETQQTESTPKSdQTKPAPAEDKQKQPHVQKPIsdvvpkPSEFDTKQDSPG-PKPAPVQQKVVHPQGSE 637
Cdd:pfam09606  395 QSPQPSVPSPQGPGSQPPQSHPG-GMIPSPALIPSPSPQMSQQP------AQQRTIGQDSPGgSLNTPGQSAVNSPLNPQ 467
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
4808-4916 4.13e-08

Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 60.16  E-value: 4.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4808 GNLIIHILQARNLAPRDNNGYSDPFVKVYLlpgrgqvmvvQNASVenkRRTKYVQKSLNPEWNQTVIyknisMEQLKKKT 4887
Cdd:COG5038   1040 GYLTIMLRSGENLPSSDENGYSDPFVKLFL----------NEKSV---YKTKVVKKTLNPVWNEEFT-----IEVLNRVK 1101

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2069550323 4888 --LEVTVWDYDRFSSNDFLGEVLIELSSSSQ 4916
Cdd:COG5038   1102 dvLTINVNDWDSGEKNDLLGTAEIDLSKLEP 1132
PDZ1_FRMPD2-like cd23071
PDZ domain 1 of FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ ...
 4596-4680 5.62e-08

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: 53.27  E-value: 5.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4596 RLKLPRDPKdhsvsgNGLGIRIVGGKEIpgTNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTY------- 4668
Cdd:cd23071      4 CVTLKRDPK------RGFGFVIVGGENT--GKLDLGIFIASIIPGGPAEKDGRIKPGGRLISLNNISLEGVTFntavkil 75

                           90
                   ....*....|....*.
gi 2069550323 4669 ----EEVQSIISQQSG 4680
Cdd:cd23071     76 qnspDEVELIISQPKD 91
PTZ00121 PTZ00121
MAEBL; Provisional
 989-1383 5.65e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.77  E-value: 5.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  989 QVKSAETPQQQKASARPAQNEKRGPDIQKEDPASQQGKPAKAISADKIQEIVQKEHTTPQQEKL----PKTISADKLSQS 1064
Cdd:PTZ00121  1501 EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKkaeeAKKAEEDKNMAL 1580

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1065 ISGEDS-EIQKGKIGKPPSA-DQVPKEEAKVVRKSSADKL-LEIVQKKEPKELEHVSDNIQIQKEDPKVQQIRlsKPPSA 1141
Cdd:PTZ00121  1581 RKAEEAkKAEEARIEEVMKLyEEEKKMKAEEAKKAEEAKIkAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK--KAEEE 1658

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1142 DQIRKEDPKVQQVKLSKtpSADQIRKEdpkvQQVKLTKAPSADQIRKEDPKIQQVKLAKAPSADQIQEDPKLQQGKFVKT 1221
Cdd:PTZ00121  1659 NKIKAAEEAKKAEEDKK--KAEEAKKA----EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA 1732

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1222 PSADKIRQEDPKihqeKLTKVPSDSEIKKvdpKIQQAKLAKIPSADHIQKEDSKLFKAKIVKTASADQLPKDNK------ 1295
Cdd:PTZ00121  1733 EEAKKEAEEDKK----KAEEAKKDEEEKK---KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKikdifd 1805

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1296 ----FQEMELANIPV-----EDYISS-KTIHDQTQVARRKEDDT---KFPLSRESLHLAESRQKVAGEQFDEEKIEPKVL 1362
Cdd:PTZ00121  1806 nfanIIEGGKEGNLVindskEMEDSAiKEVADSKNMQLEEADAFekhKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIE 1885

                          410       420
                   ....*....|....*....|.
gi 2069550323 1363 pKTRQQEDIKREDLMMDIPES 1383
Cdd:PTZ00121  1886 -EADEIEKIDKDDIEREIPNN 1905
C2_Rab11-FIP_classI cd08682
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ...
 4814-4927 6.17e-08

C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit various effector proteins to organelles and vesicles. Rab11-family interacting proteins (FIPs) are involved in mediating the role of Rab11. FIPs can be divided into three classes: class I FIPs (Rip11a, Rip11b, RCP, and FIP2) which contain a C2 domain after N-terminus of the protein, class II FIPs (FIP3 and FIP4) which contain two EF-hands and a proline rich region, and class III FIPs (FIP1) which exhibits no homology to known protein domains. All FIP proteins contain a highly conserved, 20-amino acid motif at the C-terminus of the protein, known as Rab11/25 binding domain (RBD). Class I FIPs are thought to bind to endocytic membranes via their C2 domain, which interacts directly with phospholipids. Class II FIPs do not have any membrane binding domains leaving much to speculate about the mechanism involving FIP3 and FIP4 interactions with endocytic membranes. The members in this CD are class I FIPs. The exact function of the Rab11 and FIP interaction is unknown, but there is speculation that it involves the role of forming a targeting complex that recruits a group of proteins involved in membrane transport to organelles. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176064 [Multi-domain]  Cd Length: 126  Bit Score: 54.38  E-value: 6.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4814 ILQARNLAPRDNNGYSDPFVKVYLlpGRgqvmvvqnasveNKRRTKYVQKSLNPEWNQTVIYK--NISMEQLKKKTLEVT 4891
Cdd:cd08682      5 VLQARGLLCKGKSGTNDAYVIIQL--GK------------EKYSTSVKEKTTSPVWKEECSFElpGLLSGNGNRATLQLT 70

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2069550323 4892 VWDYDRFSSNDFLGEVLIELSSSSQLDNTPR--WYTLK 4927
Cdd:cd08682     71 VMHRNLLGLDKFLGQVSIPLNDLDEDKGRRRtrWFKLE 108
C2B_Copine cd04047
C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
 4815-4918 6.50e-08

C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176012 [Multi-domain]  Cd Length: 110  Bit Score: 53.72  E-value: 6.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4815 LQARNLAPRDNNGYSDPFVKVYLLPGRGQ-VMVvqnasvenkRRTKYVQKSLNPEWNQTviykNISMEQL----KKKTLE 4889
Cdd:cd04047      7 FSGKKLDKKDFFGKSDPFLEISRQSEDGTwVLV---------YRTEVIKNTLNPVWKPF----TIPLQKLcngdYDRPIK 73

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2069550323 4890 VTVWDYDRFSSNDFLGEV---LIELSSSSQLD 4918
Cdd:cd04047     74 IEVYDYDSSGKHDLIGEFettLDELLKSSPLE 105
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
 4612-4686 7.30e-08

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: 52.76  E-value: 7.30e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069550323 4612 GLGIRIVGGKE--IPgtngeigAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEAEICV 4686
Cdd:cd06800     12 GLGISITGGKEhgVP-------ILISEIHEGQPADRCGGLYVGDAILSVNGIDLRDAKHKEAVTILSQQRGEITLEV 81
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
 4812-4929 7.83e-08

C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176008 [Multi-domain]  Cd Length: 126  Bit Score: 54.19  E-value: 7.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4812 IHILQARNLAPRDNNGYSDPFVkvyllpgrgqVMVVQNASVENKrRTKYVQKSLNPEWNQTViykNISMEQLKKKTLEVT 4891
Cdd:cd04043      5 IRIVRAENLKADSSNGLSDPYV----------TLVDTNGKRRIA-KTRTIYDTLNPRWDEEF---ELEVPAGEPLWISAT 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2069550323 4892 VWDYDRFSSNDFLGEVLIELSSSSQLDN-TPR--WYTLKEQ 4929
Cdd:cd04043     71 VWDRSFVGKHDLCGRASLKLDPKRFGDDgLPReiWLDLDTQ 111
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
 5137-5219 9.01e-08

C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha and gamma. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1(alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 175992 [Multi-domain]  Cd Length: 131  Bit Score: 54.19  E-value: 9.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5137 GEIKIalkkEMKTDGEQLIVEILQCRNITYKfkSPDHLPDLYVKLYVvnLATQKRVIKKKTRVCRHDREPSFNETFRFSL 5216
Cdd:cd04026      2 GRIYL----KISVKDNKLTVEVREAKNLIPM--DPNGLSDPYVKLKL--IPDPKNETKQKTKTIKKTLNPVWNETFTFDL 73


                   ...
gi 2069550323 5217 SPT 5219
Cdd:cd04026     74 KPA 76
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 238-424 1.04e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 58.84  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  238 AQKPGPGQQAGPQSEEAKKQQGAPKTQPQQSEST---KTPPQQQQQSPAKPPPQQPGTARASPQQANASKTSSQV--PTP 312
Cdd:PRK07764   604 ASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAeasAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPaaPPP 683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  313 TKATVAQQGISTGKQPSQQPGGPTKPAPQSAGANKQATQQQGSAAKPAPQQTGPTKQQLQQPGEPAKPSAQQAGPTkQPQ 392
Cdd:PRK07764   684 APAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPP-PPP 762

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2069550323  393 HQAEPTKPTGQKPGPVQQKPEASPPQASQPGG 424
Cdd:PRK07764   763 APAPAAAPAAAPPPSPPSEEEEMAEDDAPSMD 794
C2B_Synaptotagmin-12 cd08406
C2 domain second repeat present in Synaptotagmin 12; Synaptotagmin is a membrane-trafficking ...
 4795-4914 1.05e-07

C2 domain second repeat present in Synaptotagmin 12; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 12, a member of class 6 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmins 8 and 13, do not have any consensus Ca2+ binding sites. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176051 [Multi-domain]  Cd Length: 136  Bit Score: 54.03  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4795 GEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLpgrgqvmvvQNASVENKRRTKYVQKSLNPEWNQTVI 4874
Cdd:cd08406      2 GEILLSLSYLPTAERLTVVVVKARNLVWDNGKTTADPFVKVYLL---------QDGRKISKKKTSVKRDDTNPIFNEAMI 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2069550323 4875 YkNISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSS 4914
Cdd:cd08406     73 F-SVPAIVLQDLSLRVTVAESTEDGKTPNVGHVIIGPAAS 111
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 4610-4686 1.21e-07

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: 52.26  E-value: 1.21e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069550323 4610 GNGLGIRIVGGKE-IPGTNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEAEICV 4686
Cdd:cd06703     11 GKGLGFSIAGGKGsTPFRDGDEGIFISRITEGGAADRDGKLQVGDRVLSINGVDVTEARHDQAVALLTSSSPTITLVV 88
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
 4634-4680 1.22e-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: 51.88  E-value: 1.22e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2069550323 4634 IAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSG 4680
Cdd:cd06726     26 VARILHGGMAHRSGLLHVGDEILEINGIPVSGKTVDELQKLLSSLSG 72
PDZ3_MAGI-1_3-like cd06733
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 4611-4687 1.38e-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: 52.23  E-value: 1.38e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069550323 4611 NGLGIRIVGGKEiPGTNGEIGAyiakILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQ--QSGEAEICVR 4687
Cdd:cd06733     11 TGFGFRILGGTE-EGSQVSIGA----IVPGGAADLDGRLRTGDELLSVDGVNVVGASHHKVVDLMGNaaRNGQVNLTVR 84
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 992-1294 1.54e-07

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 57.87  E-value: 1.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  992 SAETPQQQKASARPAQNEKRGPDIQKEDPASQQgKPAKAISADKIQEIVQ-KEHTTPQQEKLPKtisadklsqsisgEDS 1070
Cdd:NF040676   142 SSTAPTEKKADEKTKQVAKVQKSVKAKEEAKTQ-KVAKAKETTKAQEIVKpKEEVKVQEVVKPK-------------EEP 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1071 EIQKgkIGKPpsadqvpKEEAKV---VRKSSADKLLEIVQkkePKELEHVSDNIQIqKEDPKVQQIrlSKPpsadqirKE 1147
Cdd:NF040676   208 KVQE--IVKP-------KEEVKVqeeVKPKEEEKVQEIVK---PKEEAKVQEEVKV-KEEAKVQEI--AKA-------KE 265

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1148 DPKVQQV-KLSKTPSADQIRKEDPKVQQVKLTKApsadqirKEDPKIQQVklAKAPSADQIQEDPKLQQgkfvkTPSADK 1226
Cdd:NF040676   266 EAKAQEIaKAKEEAKAQEIAKAKEEAKAQEIAKA-------KEEEKAQEI--AKAKEEAKAREIAKAKE-----EEKARE 331

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069550323 1227 IRQEDPKIHQEKLTKVPSDSEIKKVDpKIQQAKLAKIPSADHIQKEDSKLfkaKIVKTA-SADqlPKDN 1294
Cdd:NF040676   332 IAKAKEEAKAREIAKAKEEAKAREIA-KAKEEERAKEASKNNIQSAKREL---TVVATAyTAD--PSEN 394
C2_fungal_Inn1p-like cd08681
C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 ...
 4808-4931 1.82e-07

C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 associates with the contractile actomyosin ring at the end of mitosis and is needed for cytokinesis. The C2 domain of Inn1, located at the N-terminus, is required for ingression of the plasma membrane. The C-terminus is relatively unstructured and contains eight PXXP motifs that are thought to mediate interaction of Inn1 with other proteins with SH3 domains in the cytokinesis proteins Hof1 (an F-BAR protein) and Cyk3 (whose overexpression can restore primary septum formation in Inn1Delta cells) as well as recruiting Inn1 to the bud-neck by binding to Cyk3. Inn1 and Cyk3 appear to cooperate in activating chitin synthase Chs2 for primary septum formation, which allows coordination of actomyosin ring contraction with ingression of the cleavage furrow. It is thought that the C2 domain of Inn1 helps to preserve the link between the actomyosin ring and the plasma membrane, contributing both to membrane ingression, as well as to stability of the contracting ring. Additionally, Inn1 might induce curvature of the plasma membrane adjacent to the contracting ring, thereby promoting ingression of the membrane. It has been shown that the C2 domain of human synaptotagmin induces curvature in target membranes and thereby contributes to fusion of these membranes with synaptic vesicles. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176063 [Multi-domain]  Cd Length: 118  Bit Score: 52.64  E-value: 1.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4808 GNLIIHILQARNLAPRDNNGYSDPFVKVYLlpgrGQVmvvqnasvenKRRTKYVQKS-LNPEWNQTVIYkNISMEqlKKK 4886
Cdd:cd08681      1 GTLVVVVLKARNLPNKRKLDKQDPYCVLRI----GGV----------TKKTKTDFRGgQHPEWDEELRF-EITED--KKP 63

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2069550323 4887 TLEVTVWDyDRFSSNDFLGEVLIELSSSSQLDNTPRWYTLKEQSE 4931
Cdd:cd08681     64 ILKVAVFD-DDKRKPDLIGDTEVDLSPALKEGEFDDWYELTLKGR 107
PHA03247 PHA03247
large tegument protein UL36; Provisional
 174-666 1.83e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.41  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  174 EQDKPGQQKGPSKQPVQQQSPKPTGPQQGSVKPAPQKTAPPKQVVPQQQQQQQQQQQQPGVPKQAQKPGPGQQAGPQSEE 253
Cdd:PHA03247  2594 QSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA 2673

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  254 AKKQQGAPKTQPQQSESTKTPPQQQQQSPAKPPpqqpgtarasPQQANASKTSSQVPTPTKATVAQQG---ISTGKQPSQ 330
Cdd:PHA03247  2674 AQASSPPQRPRRRAARPTVGSLTSLADPPPPPP----------TPEPAPHALVSATPLPPGPAAARQAspaLPAAPAPPA 2743

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  331 QPGGPTKPAPQSAGANKQATQQQGSAAKPAPQQTGPTKQQLQQPGEPAKPSAQQA-GPTKQPQHQAEPTKPTGQKPGPVQ 409
Cdd:PHA03247  2744 VPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLpSPWDPADPPAAVLAPAAALPPAAS 2823

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  410 QKPEASPPQASQPggSASKKTFCPLCTTTelllhtpekanyntctqcqtvvcSLCGfnpnphiteikeWLclncqmqrAL 489
Cdd:PHA03247  2824 PAGPLPPPTSAQP--TAPPPPPGPPPPSL-----------------------PLGG------------SV--------AP 2858

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  490 GGDLGPAPGPGPQSSAPkqkmAAPTtagkpppqaqqpTQKKESTVKPDATQSPEhkkppppqtkQPTIPSSTPEKAKPPA 569
Cdd:PHA03247  2859 GGDVRRRPPSRSPAAKP----AAPA------------RPPVRRLARPAVSRSTE----------SFALPPDQPERPPQPQ 2912

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  570 PETQQTESTPKSDQTKPAPAEDKQKQPHVQ-KPISDVVPKPSEFDTKQDSPGPKPAPVQQKVVHPQGSEVAKSSEdTPQD 648
Cdd:PHA03247  2913 APPPPQPQPQPPPPPQPQPPPPPPPRPQPPlAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSRE-APAS 2991

                          490
                   ....*....|....*...
gi 2069550323  649 KTVPPDTKTSPQVSRQKS 666
Cdd:PHA03247  2992 STPPLTGHSLSRVSSWAS 3009
C2B_Synaptotagmin-7 cd08405
C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
 5154-5262 2.34e-07

C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 7, a member of class 2 synaptotagmins, is located in presynaptic plasma membranes in neurons, dense-core vesicles in endocrine cells, and lysosomes in fibroblasts. It has been shown to play a role in regulation of Ca2+-dependent lysosomal exocytosis in fibroblasts and may also function as a vesicular Ca2+-sensor. It is distinguished from the other synaptotagmins by having over 12 splice forms. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176050 [Multi-domain]  Cd Length: 136  Bit Score: 53.19  E-value: 2.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5154 LIVEILQCRNItyKFKSPDHLPDLYVKLYVvnLATQKRVIKKKTRVCRHDREPSFNETFRFSLsPTgHSLQ----ILLVS 5229
Cdd:cd08405     17 ITVNIIKARNL--KAMDINGTSDPYVKVWL--MYKDKRVEKKKTVIKKRTLNPVFNESFIFNI-PL-ERLRettlIITVM 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2069550323 5230 NGGKFMKKTLIGEAYI-----------WLDKV-DLRKRIVNWHKL 5262
Cdd:cd08405     91 DKDRLSRNDLIGKIYLgwksgglelkhWKDMLsKPRQPVAQWHRL 135
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 189-806 2.46e-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: 57.65  E-value: 2.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  189 VQQQSPKPTGPQQGSVKPApqktappkqvvpQQQQQQQQQQQQPGVPKQAQKPGPGQQAGPQSEEAKKQQGAPKTQPQQS 268
Cdd:pfam03157  106 LQRYYPGVTSPQQVSYYPG------------QASPQRPGQGQQPGQGQQWYYPTSPQQPGQWQQPGQGQQGYYPTSPQQS 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  269 ----ESTKTPPQQQQQSPAKPPPQQPGTARASPQQANASKTSSQVPTPTKATVAQQGISTGK-------QPSQQPGGPTK 337
Cdd:pfam03157  174 gqrqQPGQGQQLRQGQQGQQSGQGQPGYYPTSSQQPGQLQQTGQGQQGQQPERGQQGQQPGQgqqpgqgQQGQQPGQPQQ 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  338 PAPQSAGANKQATQQQGSAAKPAPQQTGPTKQQLQQPGEPAK----PSAQQAGPTKQPQHQAEPTK-------PTGQKPG 406
Cdd:pfam03157  254 LGQGQQGYYPISPQQPRQWQQSGQGQQGYYPTSLQQPGQGQSgyypTSQQQAGQLQQEQQLGQEQQdqqpgqgRQGQQPG 333

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  407 PVQQKPEasPPQASQPGgsASKKTFCPlctTTELLLHTPEKANYNTCTQCQTvvcslcgfnpnphiteikewlclncQMQ 486
Cdd:pfam03157  334 QGQQGQQ--PAQGQQPG--QGQPGYYP---TSPQQPGQGQPGYYPTSQQQPQ-------------------------QGQ 381

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  487 RALGGDLGPAPGPGPQSSAPkqkmaapttaGKPPPQAQQPTQKKESTVKPDATQSPEHKKPPPPQTKQPTIPSSTPEKAK 566
Cdd:pfam03157  382 QPEQGQQGQQQGQGQQGQQP----------GQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSPQQSGQGQQPGQGQQPGQ 451

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  567 PPAPETQQtestPKSDQTKPAPAEDKQKQPHVQKpisdvvpKPSEFDTKQDSPGPKPAPVQQKvVHPQGSEVAKSSEDTP 646
Cdd:pfam03157  452 EQPGQGQQ----PGQGQQGQQPGQPEQGQQPGQG-------QPGYYPTSPQQSGQGQQLGQWQ-QQGQGQPGYYPTSPLQ 519

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  647 QDKTVPPDTKTSPQVSRQKSDPKLVSQPGSGID----TKVQKQTEPVEGKGDLKKMQPQMSPKPDakQAQKPQQATVGPK 722
Cdd:pfam03157  520 PGQGQPGYYPTSPQQPGQGQQLGQLQQPTQGQQgqqsGQGQQGQQPGQGQQGQQPGQGQQGQQPG--QGQQPGQGQPGYY 597

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  723 PTQSQPKATQSQPPAQPQQSQKAPEQSSRFSLNIG----GFTDSSKSQPTTPQERVTGKLFGFGASIFNQASNLISTAGQ 798
Cdd:pfam03157  598 PTSPQQSGQGQQPGQWQQPGQGQPGYYPTSSLQLGqgqqGYYPTSPQQPGQGQQPGQWQQSGQGQQGYYPTSPQQSGQAQ 677


                   ....*...
gi 2069550323  799 QGAQPQGP 806
Cdd:pfam03157  678 QPGQGQQP 685
PDZ_MPP3-MPP4-MPP7-like cd06799
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ...
 4615-4680 2.59e-07

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: 51.09  E-value: 2.59e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069550323 4615 IRIVGGKEIPG----TNGEIGA-YIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSG 4680
Cdd:cd06799      3 VRLVKNNEPLGatikRDEKTGAiVVARIMRGGAADRSGLIHVGDELREVNGISVEGKDPEEVIQILANSQG 73
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
 4610-4671 3.22e-07

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: 51.14  E-value: 3.22e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069550323 4610 GNGLGIRIVGGKEIPGTNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEV 4671
Cdd:cd06709      9 PSGLGFNIVGGTDQPYIPNDSGIYVAKIKEDGAAAIDGRLQEGDKILEINGQSLENLTHQDA 70
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 4609-4686 4.17e-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: 51.09  E-value: 4.17e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069550323 4609 SGNGLGIRIVGGKEipGTNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPL-TAKTYEEVQSIISQQSGEAEICV 4686
Cdd:cd06689     24 ESGGLGFSVVGLKS--ENRGELGIFVQEIQPGSVAARDGRLKENDQILAINGQPLdQSISHQQAIAILQQAKGSVELVV 100
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 4611-4674 4.39e-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: 50.72  E-value: 4.39e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069550323 4611 NGLGIRIVGGKEIPGTNGEIgaYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSI 4674
Cdd:cd23058     15 EGLGFSITSRDNPTGGSGPI--YIKNILPKGAAIQDGRLKAGDRLLEVNGVDVTGKTQEEVVSL 76
C2B_Synaptotagmin-15 cd08409
C2 domain second repeat present in Synaptotagmin 15; Synaptotagmin is a membrane-trafficking ...
 4794-4909 4.47e-07

C2 domain second repeat present in Synaptotagmin 15; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. It is thought to be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues and is Ca2+ independent. Human synaptotagmin 15 has 2 alternatively spliced forms that encode proteins with different C-termini. The larger, SYT15a, contains a N-terminal TM region, a putative fatty-acylation site, and 2 tandem C terminal C2 domains. The smaller, SYT15b, lacks the C-terminal portion of the second C2 domain. Unlike most other synaptotagmins it is nearly absent in the brain and rather is found in the heart, lungs, skeletal muscle, and testis. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176054 [Multi-domain]  Cd Length: 137  Bit Score: 52.34  E-value: 4.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4794 TGEIQLQVNYDKHLGNLIIHILQARNLAPRDNNGySDPFVKVYLLPGRGQVmvvqnasveNKRRTKYVQKSLNPEWNQTV 4873
Cdd:cd08409      1 LGDIQISLTYNPTLNRLTVVVLRARGLRQLDHAH-TSVYVKVSLMIHNKVV---------KTKKTEVVDGAASPSFNESF 70

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2069550323 4874 IYKnISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLI 4909
Cdd:cd08409     71 SFK-VTSRQLDTASLSLSVMQSGGVRKSKLLGRVVL 105
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
 4596-4680 4.76e-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: 4.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4596 RLKLPRDPKdhsvsgNGLGIRIVGGkEIPGTnGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTY------- 4668
Cdd:cd06694      4 IVTLKKDPQ------KGLGFTIVGG-ENSGS-LDLGIFVKSIIPGGPADKDGRIKPGDRIIAINGQSLEGKTHhaaveii 75

                           90
                   ....*....|....*.
gi 2069550323 4669 ----EEVQSIISQQSG 4680
Cdd:cd06694     76 qnapDKVELIISQPKS 91
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
 4609-4694 5.12e-07

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: 50.36  E-value: 5.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4609 SGNGLGIRIVGGKEipgtngEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEaeicVRL 4688
Cdd:cd06674     12 PGRGLGLSIVGKRN------DTGVFVSDIVKGGAADADGRLMQGDQILSVNGEDVRNASQEAAAALLKCAQGK----VRL 81


                   ....*.
gi 2069550323 4689 DISMLS 4694
Cdd:cd06674     82 EVGRLK 87
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 172-423 5.18e-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: 5.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  172 QKEQDKPG------QQKGPSKQPVQQQSPKP--TGPQQGSVKPAPQKTAPPKQVVPQQQQQQQQQQQQPGVPKqAQKPGP 243
Cdd:pfam03157  157 QPGQGQQGyyptspQQSGQRQQPGQGQQLRQgqQGQQSGQGQPGYYPTSSQQPGQLQQTGQGQQGQQPERGQQ-GQQPGQ 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  244 GQQAG---------PQSEEAKKQQGAPKTQPQQ----SESTKTPPQQQQQSPAKPPPQQPGTARASPQQANASKTSSQVP 310
Cdd:pfam03157  236 GQQPGqgqqgqqpgQPQQLGQGQQGYYPISPQQprqwQQSGQGQQGYYPTSLQQPGQGQSGYYPTSQQQAGQLQQEQQLG 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  311 TPTKATVAQQGI--------------STGKQPSQQPGGPTKPAPQSAGANKQ-----ATQQQGSAAKPAPQQTGPTK--- 368
Cdd:pfam03157  316 QEQQDQQPGQGRqgqqpgqgqqgqqpAQGQQPGQGQPGYYPTSPQQPGQGQPgyyptSQQQPQQGQQPEQGQQGQQQgqg 395

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069550323  369 QQLQQPGEPAKPSAQQAG--PTK-----QPQHQAEPTKP----TGQKPGPVQQKPEASPPQASQPG 423
Cdd:pfam03157  396 QQGQQPGQGQQPGQGQPGyyPTSpqqsgQGQPGYYPTSPqqsgQGQQPGQGQQPGQEQPGQGQQPG 461
PDZ1_LNX1_2-like cd06677
PDZ domain 1 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 4613-4677 5.28e-07

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: 50.71  E-value: 5.28e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069550323 4613 LGIRIVGGKEIPgtngEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQ 4677
Cdd:cd06677     17 LGISIVGGNDTP----LINIVIQEVYRDGVIARDGRLLPGDQILEVNGVDISNVTHSQARSVLRQ 77
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 1381-1634 5.53e-07

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 56.59  E-value: 5.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1381 PESISKDQKSPKEETSAPPvPLPKPdhveaIREKAEKEDDKSDASSSQQQKSPQGlsdTGYSSDGISSSLGEIPSLIQSE 1460
Cdd:PTZ00108  1149 EKEIAKEQRLKSKTKGKAS-KLRKP-----KLKKKEKKKKKSSADKSKKASVVGN---SKRVDSDEKRKLDDKPDNKKSN 1219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1461 EKDVLKESCKKEILSQESSPTSPSDLAKLESTVLSILEAQASTLAEEKSGKSKDIYGVYSEHSRVPHKTKTQLGAPESYS 1540
Cdd:PTZ00108  1220 SSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGG 1299

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1541 ADEEDLAKQNIQgkyggapeegdKQDILSQKSYKGKTDTREDASARRQRYDSVEDSSESENSPVPQRKRRTSVGSSS-SD 1619
Cdd:PTZ00108  1300 SKPSSPTKKKVK-----------KRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSeDD 1368

                          250
                   ....*....|....*
gi 2069550323 1620 DYKAEDSPGSGDDED 1634
Cdd:PTZ00108  1369 DDSEVDDSEDEDDED 1383
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 159-423 5.93e-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: 56.11  E-value: 5.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  159 TAQEEASKKQKPIQKEQDKPGQQKGPSKQPVQQ-QSPKPTGPQQGSVKPAPQKTAPPKQVVPQQQQQQQQQQQQPGVPKQ 237
Cdd:pfam03157  300 TSQQQAGQLQQEQQLGQEQQDQQPGQGRQGQQPgQGQQGQQPAQGQQPGQGQPGYYPTSPQQPGQGQPGYYPTSQQQPQQ 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  238 AQKPGPGQQAGPQSEEAKKQQGAPKTQPQQSEstktppqqqqqspakpppqqPGTARASPQQANASKTSSQVPTPTKATV 317
Cdd:pfam03157  380 GQQPEQGQQGQQQGQGQQGQQPGQGQQPGQGQ--------------------PGYYPTSPQQSGQGQPGYYPTSPQQSGQ 439

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  318 AQQGISTGKQPSQQPGGPTKPA-------PQSAGANKQATQQQGSAAKPAPQQTGPTKQ--QLQQPGEPAK----PSAQQ 384
Cdd:pfam03157  440 GQQPGQGQQPGQEQPGQGQQPGqgqqgqqPGQPEQGQQPGQGQPGYYPTSPQQSGQGQQlgQWQQQGQGQPgyypTSPLQ 519

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2069550323  385 AGPTKQPQHQAEPTKP-TGQKPGPVQQKPEASPPQASQPG 423
Cdd:pfam03157  520 PGQGQPGYYPTSPQQPgQGQQLGQLQQPTQGQQGQQSGQG 559
PHA03247 PHA03247
large tegument protein UL36; Provisional
 188-726 6.26e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.49  E-value: 6.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  188 PVQQQSPKPTGPQQGS--VKP-APQKTAPPKQVVPQQQQQQQQQQQQPGVPKQAQKPGPGQQAGPQSEEAKKQQGAPKTQ 264
Cdd:PHA03247  2569 PPPRPAPRPSEPAVTSraRRPdAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPP 2648

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  265 PQQSESTKTPPQQQQQSPAKPPPQQPGtARASPQQ--------ANASKTSSQVPTPTKATvaqqgistgKQPSQQPGGPT 336
Cdd:PHA03247  2649 PERPRDDPAPGRVSRPRRARRLGRAAQ-ASSPPQRprrraarpTVGSLTSLADPPPPPPT---------PEPAPHALVSA 2718

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  337 KPAPQSAGANKQATQQQGSAAKPAPQQTGPTkqqlqQPGEPAKPSAQQ--AGPTKQPQHQAEPTKPTGQKPGPVQQKPEA 414
Cdd:PHA03247  2719 TPLPPGPAAARQASPALPAAPAPPAVPAGPA-----TPGGPARPARPPttAGPPAPAPPAAPAAGPPRRLTRPAVASLSE 2793

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  415 SPPQASQPGGSASKKTFCPLCTTTELLLHTPEKANYNTCTQCQTVVCSLCGFNPNPhiteikewlclncqmqRALGGDLG 494
Cdd:PHA03247  2794 SRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPS----------------LPLGGSVA 2857

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  495 PApGPGPQSSAPKQKMAAPTTAGKPPPQAQQPTQKKESTvKPDATQSPEHKKPPPPQTKQPTIPSSTPEKAKPPAPETQQ 574
Cdd:PHA03247  2858 PG-GDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRST-ESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  575 TESTPKSDQTKPAPAEDKQKQPHVQKP-ISDVVPKPSEFDTKQDSPGPKPAPVQQKVVHPQ-----------GSEVAKSS 642
Cdd:PHA03247  2936 PPRPQPPLAPTTDPAGAGEPSGAVPQPwLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLtghslsrvsswASSLALHE 3015

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  643 EDTP------QDKTVPPDTKTSPQVSRQKSDPKLVSQpgSGIDTKVQKQTEPVEGKGDlkkmqpqmsPKPDAKQAQKPQQ 716
Cdd:PHA03247  3016 ETDPppvslkQTLWPPDDTEDSDADSLFDSDSERSDL--EALDPLPPEPHDPFAHEPD---------PATPEAGARESPS 3084

                          570
                   ....*....|
gi 2069550323  717 ATVGPKPTQS 726
Cdd:PHA03247  3085 SQFGPPPLSA 3094
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 4604-4681 6.97e-07

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 49.97  E-value: 6.97e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069550323 4604 KDHSVSGNGLGIRIVGGKEipgtNGEIGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGE 4681
Cdd:pfam00595    3 TLEKDGRGGLGFSLKGGSD----QGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGK 75
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 ...
 4606-4687 7.00e-07

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: 50.35  E-value: 7.00e-07
                           10        20        30        40        50        60        70        80
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gi 2069550323 4606 HSVSGNGLGIRIVGgkeIPGTNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQ-QSGEAEI 4684
Cdd:cd06760     10 NKEPGVGLGIGLCC---LPLENDIPGIFIHHLSPGSVAHMDGRLRRGDQILEINGTSLRNVTLNEAYAILSQcKPGPVTL 86


                   ...
gi 2069550323 4685 CVR 4687
Cdd:cd06760     87 IIS 89
C2A_SLP-3 cd08392
C2 domain first repeat present in Synaptotagmin-like protein 3; All Slp members basically ...
 5136-5262 7.85e-07

C2 domain first repeat present in Synaptotagmin-like protein 3; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. SHD of Slp (except for the Slp4-SHD) function as a specific Rab27A/B-binding domain. In addition to Slp, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. Little is known about the expression or localization of Slp3. The C2A domain of Slp3 is Ca2+ dependent. It has been demonstrated that Slp3 promotes dense-core vesicle exocytosis. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176038 [Multi-domain]  Cd Length: 128  Bit Score: 51.37  E-value: 7.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5136 MGEIKIALKKEMKTdgEQLIVEILQCRNITY-KFKSPDHLPdlYVKLYVvnLATQKRVIKKKTRVCRHDREPSFNETFRF 5214
Cdd:cd08392      1 TGEIEFALHYNFRT--SCLEITIKACRNLAYgDEKKKKCHP--YVKVCL--LPDKSHNSKRKTAVKKGTVNPVFNETLKY 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2069550323 5215 SLSPTGHSLQILLVS--NGGKFMKKTLIGEAYIWLDKVDLRKRIV---NWHKL 5262
Cdd:cd08392     75 VVEADLLSSRQLQVSvwHSRTLKRRVFLGEVLIPLADWDFEDTDSqrfLWYPL 127
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 4606-4691 7.93e-07

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: 49.94  E-value: 7.93e-07
                           10        20        30        40        50        60        70        80
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gi 2069550323 4606 HSVSGNGLGIRIVGGKEIPGTngeigaYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIIsQQSGEaeiC 4685
Cdd:cd06678      6 NKRDGEQLGIKLVRKKDEPGV------FILDLLEGGLAARDGRLKSDDRVLAINGQDLRHGTPEQAAQII-QASGE---R 75


                   ....*.
gi 2069550323 4686 VRLDIS 4691
Cdd:cd06678     76 VHFVVS 81
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 4606-4687 8.87e-07

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: 49.95  E-value: 8.87e-07
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gi 2069550323 4606 HSVSGNG-LGIRIVGGKEIP----GTNgEIGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSG 4680
Cdd:cd06702      4 HLVKAGGpLGLSIVGGSDHSshpfGVD-EPGIFISKVIPDGAAAKSG-LRIGDRILSVNGKDLRHATHQEAVSALLSPGQ 81


                   ....*..
gi 2069550323 4681 EAEICVR 4687
Cdd:cd06702     82 EIKLLVR 88
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 4809-4913 9.96e-07

C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is present in cPLA2 which releases arachidonic acid from membranes initiating the biosynthesis of potent inflammatory mediators such as prostaglandins, leukotrienes, and platelet-activating factor. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members of this cd have a type-II topology.


Pssm-ID: 176001 [Multi-domain]  Cd Length: 119  Bit Score: 50.72  E-value: 9.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4809 NLIIHILQARNLAPRDNNGYSDPFVKVYLlPgrgqvmvvqNASVENKRrTKYVQKSLNPEWNQTVIY------KNIsmeq 4882
Cdd:cd04036      1 LLTVRVLRATNITKGDLLSTPDCYVELWL-P---------TASDEKKR-TKTIKNSINPVWNETFEFriqsqvKNV---- 65

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2069550323 4883 lkkktLEVTVWDYDRFSSnDFLGEVLIELSS 4913
Cdd:cd04036     66 -----LELTVMDEDYVMD-DHLGTVLFDVSK 90
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 4610-4686 1.02e-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: 49.92  E-value: 1.02e-06
                           10        20        30        40        50        60        70        80
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gi 2069550323 4610 GNGLGIRIVGG-KEIPGTNGEI---GAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEAEIC 4685
Cdd:cd06701     14 GEKLGISIRGGaKGHAGNPLDPtdeGIFISKINPDGAAARDGRLKVGQRILEVNGQSLLGATHQEAVRILRSVGDTLTLL 93


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gi 2069550323 4686 V 4686
Cdd:cd06701     94 V 94
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
 4610-4687 1.03e-06

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: 49.49  E-value: 1.03e-06
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                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4610 GNGLGIRIVGGKE--IPgtngeigAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEAEICVR 4687
Cdd:cd06801     10 VGGLGISIKGGAEhkMP-------ILISKIFKGQAADQTGQLFVGDAILSVNGENLEDATHDEAVQALKNAGDEVTLTVK 82
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
 4809-4913 1.11e-06

C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2) to d-myo-inositol-1,4,5-trisphosphate (1,4,5-IP3) and sn-1,2-diacylglycerol (DAG). 1,4,5-IP3 and DAG are second messengers in eukaryotic signal transduction cascades. PLC is composed of a N-terminal PH domain followed by a series of EF hands, a catalytic TIM barrel and a C-terminal C2 domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-II topology.


Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 50.62  E-value: 1.11e-06
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gi 2069550323 4809 NLIIHILQARNL--APRDNNGYSDPFVKVYllpgrgqvMVVQNASVENKRRTKYVQK-SLNPEWNQT----VIYKNISMe 4881
Cdd:cd00275      3 TLTIKIISGQQLpkPKGDKGSIVDPYVEVE--------IHGLPADDSAKFKTKVVKNnGFNPVWNETfefdVTVPELAF- 73

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2069550323 4882 qlkkktLEVTVWDYDRFsSNDFLGEVLIELSS 4913
Cdd:cd00275     74 ------LRFVVYDEDSG-DDDFLGQACLPLDS 98
PDZ13_MUPP1-like cd06676
PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
 4612-4686 1.36e-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: 49.26  E-value: 1.36e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069550323 4612 GLGIRIVGGKEIPgtNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEAEICV 4686
Cdd:cd06676     10 GLGFSIVGGFGSP--HGDLPIYVKTVFEKGAAAEDGRLKRGDQILAVNGESLEGVTHEEAVNILKKTKGTVTLTV 82
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 4610-4691 1.54e-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: 48.82  E-value: 1.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4610 GNGLGIRIVGGKEIpgtngeiGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEaeicVRLD 4689
Cdd:cd06667      9 GSGLGFGIVGGKST-------GVVVKTILPGGVADRDGRLRSGDHILQIGDTNLRGMGSEQVAQVLRQCGSH----VRLV 77


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gi 2069550323 4690 IS 4691
Cdd:cd06667     78 VA 79
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
 4599-4686 2.14e-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: 48.90  E-value: 2.14e-06
                           10        20        30        40        50        60        70        80
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gi 2069550323 4599 LPRDPKDhsvsgnGLGIRIVGGKEIPgtNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQ 4678
Cdd:cd06675      5 IKRGPQD------SLGISIAGGVGSP--LGDVPVFIAMIQPNGVAAQTGKLKVGDRIVSINGQSTDGLTHSEAVNLLKNA 76


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gi 2069550323 4679 SGEAEICV 4686
Cdd:cd06675     77 SGTIILQV 84
PRK11901 PRK11901
hypothetical protein; Reviewed
 303-430 2.37e-06

hypothetical protein; Reviewed


Pssm-ID: 237015 [Multi-domain]  Cd Length: 327  Bit Score: 53.15  E-value: 2.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  303 SKTSSQVPTPTKATVAQQGISTGKQP---SQQP--GGPTKPAPQSAGANKQA-----------TQQQG-----SAAKPAP 361
Cdd:PRK11901    91 NQSSPSAANNTSDGHDASGVKNTAPPqdiSAPPisPTPTQAAPPQTPNGQQRielpgnisdalSQQQGqvnaaSQNAQGN 170

                           90       100       110       120       130       140       150
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gi 2069550323  362 QQTGPTKQQLQQPGEPAKPSAQQAGPTKQPQHQAEPTKPTGQKPGP-VQQKPEASP-PQASQPGGSASKKT 430
Cdd:PRK11901   171 TSTLPTAPATVAPSKGAKVPATAETHPTPPQKPATKKPAVNHHKTAtVAVPPATSGkPKSGAASARALSSA 241
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 4610-4677 3.87e-06

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: 48.05  E-value: 3.87e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069550323 4610 GNGLGIRIVGGKeipGTNGE-IGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQ 4677
Cdd:cd06789     12 GNGMGLSIVAAK---GAGQDkLGIYIKSVVKGGAADLDGRLQAGDQLLSVDGHSLVGLSQERAAELMTK 77
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 4610-4681 6.04e-06

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: 47.18  E-value: 6.04e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069550323 4610 GNGLGIRIVGGKEIpgtngeiGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTAKTYEE-VQSIISQQSGE 4681
Cdd:cd06729     10 GGSVGLRLAGGNDV-------GIFVAGVQEGSPAEKQG-LQEGDQILKVNGVDFRNLTREEaVLFLLDLPKGE 74
C2A_Synaptotagmin-1-5-6-9-10 cd08385
C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a ...
 5152-5263 8.70e-06

C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 1, a member of class 1 synaptotagmins, is located in the brain and endocranium and localized to the synaptic vesicles and secretory granules. It functions as a Ca2+ sensor for fast exocytosis as do synaptotagmins 5, 6, and 10. It is distinguished from the other synaptotagmins by having an N-glycosylated N-terminus. Synaptotagmins 5, 6, and 10, members of class 3 synaptotagmins, are located primarily in the brain and localized to the active zone and plasma membrane. They is distinguished from the other synaptotagmins by having disulfide bonds at its N-terminus. Synaptotagmin 6 also regulates the acrosome reaction, a unique Ca2+-regulated exocytosis, in sperm. Synaptotagmin 9, a class 5 synaptotagmins, is located in the brain and localized to the synaptic vesicles. It is thought to be a Ca2+-sensor for dense-core vesicle exocytosis. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176031 [Multi-domain]  Cd Length: 124  Bit Score: 48.03  E-value: 8.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5152 EQLIVEILQCRNitykfkspdhLP--------DLYVKLYVvnLATQKRviKKKTRVCRHDREPSFNETFRFSLSPTGHSL 5223
Cdd:cd08385     16 NQLTVGIIQAAD----------LPamdmggtsDPYVKVYL--LPDKKK--KFETKVHRKTLNPVFNETFTFKVPYSELGN 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2069550323 5224 QILLVS--NGGKFMKKTLIGEAYIWLDKVDLRKRIVNWHKLL 5263
Cdd:cd08385     82 KTLVFSvyDFDRFSKHDLIGEVRVPLLTVDLGHVTEEWRDLE 123
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 319-424 8.82e-06

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 49.27  E-value: 8.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  319 QQGISTGKQPSQQPGGPTKPAPQSAGANKQATQQQGSAAKPA------PQQTGPTKQQLQQPGEPAKPSAQQAGPTKQPQ 392
Cdd:pfam15240   57 QPPASDDPPGPPPPGGPQQPPPQGGKQKPQGPPPQGGPRPPPgkpqgpPPQGGNQQQGPPPPGKPQGPPPQGGGPPPQGG 136

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2069550323  393 HQAEPTKPtgqKPGPvQQKPEASPPQASQPGG 424
Cdd:pfam15240  137 NQQGPPPP---PPGN-PQGPPQRPPQPGNPQG 164
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
 4606-4687 1.00e-05

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: 46.88  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4606 HSVSGNGLGIRIVGGKEIPG-TNGEIGAYIAKILPGGSAEqtGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEAEI 4684
Cdd:cd06727      6 HRAPGFGFGIAVSGGRDNPHfQSGDTSIVISDVLKGGPAE--GKLQENDRVVSVNGVSMENVEHSFAVQILRKCGKTANI 83


                   ...
gi 2069550323 4685 CVR 4687
Cdd:cd06727     84 TVK 86
PDZ10_MUPP1-PDZ8_PATJ-like cd06673
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ...
 4612-4677 1.11e-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: 46.52  E-value: 1.11e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069550323 4612 GLGIRIVGGKEIPgtngeIGA-YIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQ 4677
Cdd:cd06673     14 GLGLSIVGGSDTL-----LGAiIIHEVYEDGAAAKDGRLWAGDQILEVNGEDLRKATHDEAINVLRQ 75
C2B_Synaptotagmin-14_16 cd08408
C2 domain second repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are ...
 4796-4928 1.12e-05

C2 domain second repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are membrane-trafficking proteins in specific tissues outside the brain. Both of these contain C-terminal tandem C2 repeats, but only Synaptotagmin 14 has an N-terminal transmembrane domain and a putative fatty-acylation site. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium and this is indeed the case here. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176053 [Multi-domain]  Cd Length: 138  Bit Score: 48.13  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4796 EIQLQVNYDKHLGNLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQVMVVQNASVenkRRTKYvqkslNPEWNQTVIY 4875
Cdd:cd08408      3 ELLLGLEYNALTGRLSVEVIKGSNFKNLAMNKAPDTYVKLTLLNSDGQEISKSKTSI---RRGQP-----DPEFKETFVF 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2069550323 4876 KnISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSSSQlDNTPRWYTLKE 4928
Cdd:cd08408     75 Q-VALFQLSEVTLMFSVYNKRKMKRKEMIGWFSLGLNSSGE-EEEEHWNEMKE 125
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 291-427 1.13e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.91  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  291 GTARASPQQANASKTSSQVPTPTKATVAQQGISTGKQPSQQPGGPTKPAPQSAGANKQATQQQGSAAKPA--------PQ 362
Cdd:PRK07764   589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAvpdasdggDG 668

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069550323  363 QTGPTKQQLQQPGEPAKPSAQQAGPTKQPQHQAEPtKPTGQKPGPVQQKPEASPPQASQPGGSAS 427
Cdd:PRK07764   669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAP-APAATPPAGQADDPAAQPPQAAQGASAPS 732
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
296-414 1.15e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 51.70  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  296 SPQQANASKTSSQV--PTPTKATVAQQGISTGKQPSQQPGGPtkPAPQSAGANKQATQQQGSAAKPAPQQTGPTKQQLQQ 373
Cdd:PRK14971   374 GPKQHIKPVFTQPAaaPQPSAAAAASPSPSQSSAAAQPSAPQ--SATQPAGTPPTVSVDPPAAVPVNPPSTAPQAVRPAQ 451

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2069550323  374 PGEPAKPSAQQAG----PTKQPQHQAEPTKPTGQKPGPVQQKPEA 414
Cdd:PRK14971   452 FKEEKKIPVSKVSslgpSTLRPIQEKAEQATGNIKEAPTGTQKEI 496
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 297-422 1.22e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 52.01  E-value: 1.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  297 PQQANASKTSSQVPTPTKATV----AQQGISTGKQPSQQPGGPTKPAPQSAGANKQATQQQgsaAKPAPQQTGPTKQQLQ 372
Cdd:PRK10263   716 PAGANPFSLDDFEFSPMKALLddgpHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQP---QYQQPQQPVAPQPQYQ 792

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2069550323  373 QPGEPAKPSAQQAgptkQPQHQAEPtKPTGQKPgpvqQKPEASPPQASQP 422
Cdd:PRK10263   793 QPQQPVAPQPQYQ----QPQQPVAP-QPQYQQP----QQPVAPQPQYQQP 833
C2B_Synaptotagmin-12 cd08406
C2 domain second repeat present in Synaptotagmin 12; Synaptotagmin is a membrane-trafficking ...
 5152-5226 1.26e-05

C2 domain second repeat present in Synaptotagmin 12; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 12, a member of class 6 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmins 8 and 13, do not have any consensus Ca2+ binding sites. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176051 [Multi-domain]  Cd Length: 136  Bit Score: 47.86  E-value: 1.26e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069550323 5152 EQLIVEILQCRNITYKFKSPDHlpDLYVKLYVvnLATQKRVIKKKTRVCRHDREPSFNETFRFSLSPTghSLQIL 5226
Cdd:cd08406     15 ERLTVVVVKARNLVWDNGKTTA--DPFVKVYL--LQDGRKISKKKTSVKRDDTNPIFNEAMIFSVPAI--VLQDL 83
PDZ3_PTPN13_FRMPD2-like cd06695
PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ ...
 4609-4681 1.56e-05

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: 46.48  E-value: 1.56e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069550323 4609 SGNGLGIRIVGGK-EIPGTNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGE 4681
Cdd:cd06695      9 GSSGLGFSFLGGEnNSPEDPFSGLVRIKKLFPGQPAAESGLIQEGDVILAVNGEPLKGLSYQEVLSLLRGAPPE 82
C2_putative_Elicitor-responsive_gene cd04049
C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive ...
 4808-4911 1.82e-05

C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive proteins are triggered in response to specific elicitor molecules such as glycolproteins, peptides, carbohydrates and lipids. A host of defensive responses are also triggered resulting in localized cell death. Antimicrobial secondary metabolites, such as phytoalexins, or defense-related proteins, including pathogenesis-related (PR) proteins are also produced. There is a single C2 domain present here. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members have a type-II topology.


Pssm-ID: 176014 [Multi-domain]  Cd Length: 124  Bit Score: 47.33  E-value: 1.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4808 GNLIIHILQARNLAPRDNNGYSDPFVkvyLLPGRGQVmvvQNASV-ENKRRtkyvqkslNPEWNQTVIYkNISMEQLKKK 4886
Cdd:cd04049      1 GTLEVLLISAKGLQDTDFLGKIDPYV---IIQCRTQE---RKSKVaKGDGR--------NPEWNEKFKF-TVEYPGWGGD 65

                           90       100
                   ....*....|....*....|....*.
gi 2069550323 4887 T-LEVTVWDYDRFSSNDFLGEVLIEL 4911
Cdd:cd04049     66 TkLILRIMDKDNFSDDDFIGEATIHL 91
C2_PSD cd04039
C2 domain present in Phosphatidylserine decarboxylase (PSD); PSD is involved in the ...
 4808-4921 2.00e-05

C2 domain present in Phosphatidylserine decarboxylase (PSD); PSD is involved in the biosynthesis of aminophospholipid by converting phosphatidylserine (PtdSer) to phosphatidylethanolamine (PtdEtn). There is a single C2 domain present and it is thought to confer PtdSer binding motif that is common to PKC and synaptotagmin. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176004 [Multi-domain]  Cd Length: 108  Bit Score: 46.48  E-value: 2.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4808 GNLIIHILQARNLAPRDN---NGYS-DPFVKVYLlpgrgqvmvvqnasveNKR--RTKYVQKSLNPEWNQTVIYKNISME 4881
Cdd:cd04039      1 GVVFMEIKSITDLPPLKNmtrTGFDmDPFVIISF----------------GRRvfRTSWRRHTLNPVFNERLAFEVYPHE 64

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2069550323 4882 qlKKKTLEVTVWDYDRFSSNDFLGEVLIELSSSSQLDNTP 4921
Cdd:cd04039     65 --KNFDIQFKVLDKDKFSFNDYVATGSLSVQELLNAAPQP 102
PDZ_MPP5-like cd06798
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related ...
 4634-4680 2.21e-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: 45.80  E-value: 2.21e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2069550323 4634 IAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSG 4680
Cdd:cd06798     25 ISRIVKGGAAEKSGLLHEGDEILEINGIEIRGKDVNEVCDLLADMHG 71
C2B_Synaptotagmin-14_16 cd08408
C2 domain second repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are ...
 5154-5263 2.31e-05

C2 domain second repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are membrane-trafficking proteins in specific tissues outside the brain. Both of these contain C-terminal tandem C2 repeats, but only Synaptotagmin 14 has an N-terminal transmembrane domain and a putative fatty-acylation site. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium and this is indeed the case here. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176053 [Multi-domain]  Cd Length: 138  Bit Score: 47.36  E-value: 2.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5154 LIVEILQCRNitYKFKSPDHLPDLYVKLYVVNlATQKRVIKKKTRVCRHDREPSFNETFRFSLSPTGHSLQILLVS--NG 5231
Cdd:cd08408     17 LSVEVIKGSN--FKNLAMNKAPDTYVKLTLLN-SDGQEISKSKTSIRRGQPDPEFKETFVFQVALFQLSEVTLMFSvyNK 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2069550323 5232 GKFMKKTLIG------------EAYIWLDKVDLR-KRIVNWHKLL 5263
Cdd:cd08408     94 RKMKRKEMIGwfslglnssgeeEEEHWNEMKESKgQQVCRWHTLL 138
C2B_Synaptotagmin-1 cd08402
C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking ...
 5153-5262 2.50e-05

C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 1, a member of the class 1 synaptotagmins, is located in the brain and endocranium and localized to the synaptic vesicles and secretory granules. It functions as a Ca2+ sensor for fast exocytosis. It, like synaptotagmin-2, has an N-glycosylated N-terminus. Synaptotagmin 4, a member of class 4 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmin-11, has an Asp to Ser substitution in its C2A domain. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176047 [Multi-domain]  Cd Length: 136  Bit Score: 47.01  E-value: 2.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5153 QLIVEILQCRNItyKFKSPDHLPDLYVKLYVVNlaTQKRVIKKKTRVCRHDREPSFNETFRFSLSPtgHSLQ----ILLV 5228
Cdd:cd08402     16 KLTVVILEAKNL--KKMDVGGLSDPYVKIHLMQ--NGKRLKKKKTTIKKRTLNPYYNESFSFEVPF--EQIQkvhlIVTV 89

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2069550323 5229 SNGGKFMKKTLIGEAYI-----------WLDKVDLRKR-IVNWHKL 5262
Cdd:cd08402     90 LDYDRIGKNDPIGKVVLgcnatgaelrhWSDMLASPRRpIAQWHTL 135
PDZ4_MUPP1-like cd06668
PDZ domain 4 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 4633-4688 2.67e-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: 2.67e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2069550323 4633 YIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISqqsgEAEICVRL 4688
Cdd:cd06668     33 YIRSILPEGPVGRNGKLFSGDELLEVNGIQLLGLSHKEVVSILK----ELPPPVRL 84
C2A_Copine cd04048
C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
 4814-4913 2.95e-05

C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176013 [Multi-domain]  Cd Length: 120  Bit Score: 46.41  E-value: 2.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4814 ILQARNLAPRDNNGYSDPFVKVYLLPGRGQVMVvqnasveNKRRTKYVQKSLNPEWNQTVI--YkNISMEQlkkkTLEVT 4891
Cdd:cd04048      6 SISCRNLLDKDVLSKSDPFVVVYVKTGGSGQWV-------EIGRTEVIKNNLNPDFVTTFTvdY-YFEEVQ----KLRFE 73

                           90       100
                   ....*....|....*....|....*.
gi 2069550323 4892 VWDYD----RFSSNDFLGEVLIELSS 4913
Cdd:cd04048     74 VYDVDskskDLSDHDFLGEAECTLGE 99
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 291-422 3.55e-05

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: 50.42  E-value: 3.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  291 GTARASPQQANASKTSSQVPTPTKAT---------VAQQGISTGKQPSQQPGGPTKPAPQSAGANKQATQQQGSAAKPAP 361
Cdd:pfam09770  164 GVAPKKAAAPAPAPQPAAQPASLPAPsrkmmsleeVEAAMRAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQ 243

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069550323  362 QQTGPTKQQLQQPGEPAKPSAQQAGPTKQPQHQAEPTKPTGQKPGPVQQkpeasPPQASQP 422
Cdd:pfam09770  244 QQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQP-----PPVPVQP 299
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 155-626 3.86e-05

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: 50.54  E-value: 3.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  155 SDSDTAQEEASKKQKPIQKE-----------QDKPGQQKGPSKQPVQQQSPKPTGPQQGSVKPAPqkTAPPKQVVPQQQQ 223
Cdd:pfam03154  121 SDGRSVNDEGSSDPKDIDQDnrstspsipspQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPS--PPPPGTTQAATAG 198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  224 QQQQQQQQPGVPKQAQKPGPGQQAGPQSEEAKKQQGaPKTQPQQSESTKTPpqqqqqspakpppqqpgtARASPQQANAS 303
Cdd:pfam03154  199 PTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQT-PTLHPQRLPSPHPP------------------LQPMTQPPPPS 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  304 KTSSQ-VPTPTKATVAQQG---ISTGKQPSQQPGgptkpAPQSAGANKQATQQQGSAAkPAPQQTGPTKQQLQQPgePAK 379
Cdd:pfam03154  260 QVSPQpLPQPSLHGQMPPMphsLQTGPSHMQHPV-----PPQPFPLTPQSSQSQVPPG-PSPAAPGQSQQRIHTP--PSQ 331

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  380 PSAQQAGPTKQ----------PQHQAEPTKPTGQKPGPVQQKpeaSPPQASQPGGSASKKTFCP---LCTTTELLLHTPE 446
Cdd:pfam03154  332 SQLQSQQPPREqplppaplsmPHIKPPPTTPIPQLPNPQSHK---HPPHLSGPSPFQMNSNLPPppaLKPLSSLSTHHPP 408

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  447 KAnyntctqcqtvvcslcgfNPNPhiteikewLCLNCQMQralggdlgPAPGPGPQSSAPKQKMAAPTTAGKPPPQaqqp 526
Cdd:pfam03154  409 SA------------------HPPP--------LQLMPQSQ--------QLPPPPAQPPVLTQSQSLPPPAASHPPT---- 450

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  527 tqkkeSTVKPDATQSPEHKKPPPPQTKQPTIPSSTPEKAKPPAPETQQTESTPKSDQTKPAPAEDKQKQP--HVQKPISD 604
Cdd:pfam03154  451 -----SGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPpvQIKEEALD 525

                          490       500
                   ....*....|....*....|..
gi 2069550323  605 VVPKPSEFDTKQDSPGPKPAPV 626
Cdd:pfam03154  526 EAEEPESPPPPPRSPSPEPTVV 547
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 300-726 5.11e-05

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: 49.91  E-value: 5.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  300 ANASKTSSQVPTPTKATVAQQGISTGKQPSQQPGGPTKPAPQSAGANKqATQQQGSAAKP----APQQTGPTKQqlqqpg 375
Cdd:pfam05109  397 GTAPKTLIITRTATNATTTTHKVIFSKAPESTTTSPTLNTTGFAAPNT-TTGLPSSTHVPtnltAPASTGPTVS------ 469

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  376 epakpSAQQAGPTkqPQHQAEPTKPTGQKPGPVQQKPEASPPQASQPGGSASKKTfcPLCTTTELLLHTPeKANYNTCTQ 455
Cdd:pfam05109  470 -----TADVTSPT--PAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPT--PNATSPTPAVTTP-TPNATSPTL 539

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  456 CQTVVCSLCGfNPNPHITEikewlclncqmqralggdlgPAPG---PGPQSSAPKQKMAAPTTA-------------GKP 519
Cdd:pfam05109  540 GKTSPTSAVT-TPTPNATS--------------------PTPAvttPTPNATIPTLGKTSPTSAvttptpnatsptvGET 598

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  520 PPQAQQPTQKKESTVKPDATQSPEHKKPPPPQTKQPTIPSSTPEKAKPPAPETQQTESTPKSDQTKPAPAEDKQKQPHVQ 599
Cdd:pfam05109  599 SPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGG 678

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  600 KPISDVVP-KPSEFDTKQDSPGPKPAPVQQkVVHPQGSEVAKSSEDTPQDKTVPPDTKTSPQV-SRQKSD-PKLVSQPGS 676
Cdd:pfam05109  679 ENITQVTPaSTSTHHVSTSSPAPRPGTTSQ-ASGPGNSSTSTKPGEVNVTKGTPPKNATSPQApSGQKTAvPTVTSTGGK 757

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 2069550323  677 GIDTKVQKQTepvEGKGDLKKMQPQMSPKPDAKQAQKPQQATVGPKPTQS 726
Cdd:pfam05109  758 ANSTTGGKHT---TGHGARTSTEPTTDYGGDSTTPRTRYNATTYLPPSTS 804
C2B_Synaptotagmin-4 cd08404
C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking ...
 5137-5262 5.56e-05

C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 4, a member of class 4 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmin-11, has an Asp to Ser substitution in its C2A domain. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176049 [Multi-domain]  Cd Length: 136  Bit Score: 46.27  E-value: 5.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5137 GEIKIALKKEMKTDgeQLIVEILQCRNITykfKSPDHLP-DLYVKLYVvnLATQKRVIKKKTRVCRHDREPSFNETFRFS 5215
Cdd:cd08404      2 GELLLSLCYQPTTN--RLTVVVLKARHLP---KMDVSGLaDPYVKVNL--YYGKKRISKKKTHVKKCTLNPVFNESFVFD 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069550323 5216 L-SPTGHSLQI-LLVSNGGKFMKKTLIGEAYI-----------WLDKVD-LRKRIVNWHKL 5262
Cdd:cd08404     75 IpSEELEDISVeFLVLDSDRVTKNEVIGRLVLgpkasgsgghhWKEVCNpPRRQIAEWHML 135
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 296-630 6.08e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.78  E-value: 6.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  296 SPQQANASKTSSQVPTPTKATVAQQGISTGKQPSQQPGGPTKPAPQSAGANKQATQQQGSAAKPAPQQTGPTKQQlqQPG 375
Cdd:PHA03307    77 TEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAAS--PPA 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  376 EPAKPSAQQAGPTKQPQ--------HQAEPTKPTGQKPGPVQQKPEASPPQASQPGGSASKKTFCPLCTTT-ELLLHTPE 446
Cdd:PHA03307   155 AGASPAAVASDAASSRQaalplsspEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGrSAADDAGA 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  447 KANYNTCTQCQTVVCSLCGFNPNPHITEIKEwlcLNCQMQRALGGDLGPAPGPGPQSSAPKQK--MAAPTTAGKPPPQAQ 524
Cdd:PHA03307   235 SSSDSSSSESSGCGWGPENECPLPRPAPITL---PTRIWEASGWNGPSSRPGPASSSSSPRERspSPSPSSPGSGPAPSS 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  525 QPTQKKESTVKPDATQSPEhkkpPPPQTKQPTIPSSTPEKAKPPAPETQQTESTPKSDQTKPAPAEDKQ--KQPHVQKPI 602
Cdd:PHA03307   312 PRASSSSSSSRESSSSSTS----SSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSspAASAGRPTR 387

                          330       340
                   ....*....|....*....|....*...
gi 2069550323  603 SDVVPKPSEFDTKQDSPGPKPAPVQQKV 630
Cdd:PHA03307   388 RRARAAVAGRARRRDATGRFPAGRPRPS 415
C2B_RasA3 cd04010
C2 domain second repeat present in RAS p21 protein activator 3 (RasA3); RasA3 are members of ...
 4810-4931 7.62e-05

C2 domain second repeat present in RAS p21 protein activator 3 (RasA3); RasA3 are members of GTPase activating protein 1 (GAP1), a Ras-specific GAP, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. RasA3 contains an N-terminal C2 domain, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) zinc binding domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175977 [Multi-domain]  Cd Length: 148  Bit Score: 46.24  E-value: 7.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4810 LIIHILQARNLAPrdNNGYSDPFVKVYLL-PGRGQVMvvqnasvenkRRTKYVQKSLNPEWNQTVI------------YK 4876
Cdd:cd04010      2 LSVRVIECSDLAL--KNGTCDPYASVTLIySNKKQDT----------KRTKVKKKTNNPQFDEAFYfdvtidsspekkQF 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2069550323 4877 NISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSSSQLDNTPR-WYTLKEQSE 4931
Cdd:cd04010     70 EMPEEDAEKLELRVDLWHASMGGGDVFLGEVRIPLRGLDLQAGSHQaWYFLQPREE 125
C2A_Synaptotagmin-14_16 cd08389
C2A domain first repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are ...
 5152-5252 8.32e-05

C2A domain first repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are membrane-trafficking proteins in specific tissues outside the brain. Both of these contain C-terminal tandem C2 repeats, but only Synaptotagmin 14 has an N-terminal transmembrane domain and a putative fatty-acylation site. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium and this is indeed the case here. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176035 [Multi-domain]  Cd Length: 124  Bit Score: 45.31  E-value: 8.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5152 EQLIVEILQCRNITYKFKS-PDHlpdlyVKLYVVNLATQKRviKKKTRVcRHDREPSFNETFRFS-LSP---TGHSLQIL 5226
Cdd:cd08389     16 RKLTVTVIRAQDIPTKDRGgASS-----WQVHLVLLPSKKQ--RAKTKV-QRGPNPVFNETFTFSrVEPeelNNMALRFR 87

                           90       100
                   ....*....|....*....|....*.
gi 2069550323 5227 LVSNgGKFMKKTLIGEAYIWLDKVDL 5252
Cdd:cd08389     88 LYGV-ERMRKERLIGEKVVPLSQLNL 112
PDZ2_DLG5-like cd06765
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 4615-4676 8.73e-05

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: 43.87  E-value: 8.73e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069550323 4615 IRIVGGKEiPGTNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIIS 4676
Cdd:cd06765      2 INLSGQKD-SGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEALLR 62
C2_Perforin cd04032
C2 domain of Perforin; Perforin contains a single copy of a C2 domain in its C-terminus and ...
 4807-4915 9.10e-05

C2 domain of Perforin; Perforin contains a single copy of a C2 domain in its C-terminus and plays a role in lymphocyte-mediated cytotoxicity. Mutations in perforin leads to familial hemophagocytic lymphohistiocytosis type 2. The function of perforin is calcium dependent and the C2 domain is thought to confer this binding to target cell membranes. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175998 [Multi-domain]  Cd Length: 127  Bit Score: 45.33  E-value: 9.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4807 LGNLIIHILQARNLaprdnNG----YSDPFVKVYLlpgRGQVmvvqnasvenkRRTKYVQKSLNPEWNQTVIYKNISMEQ 4882
Cdd:cd04032     27 LATLTVTVLRATGL-----WGdyftSTDGYVKVFF---GGQE-----------KRTEVIWNNNNPRWNATFDFGSVELSP 87

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2069550323 4883 LKKKTLEVtvWDYDRFSSNDFLGEVLIELSSSS 4915
Cdd:cd04032     88 GGKLRFEV--WDRDNGWDDDLLGTCSVVPEAGV 118
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 4602-4678 9.51e-05

PDZ domain 3 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 3 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 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: 467248 [Multi-domain]  Cd Length: 82  Bit Score: 43.85  E-value: 9.51e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069550323 4602 DPKDHSV--SGNGLGIRIVGGKeipgtNGeiGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTAKTYEEVQSIISQQ 4678
Cdd:cd06767      2 EPRHVSIekGSEPLGISIVSGE-----NG--GIFVSSVTEGSLAHQAG-LEYGDQLLEVNGINLRNATEQQAALILRQC 72
PDZ1_hSTXBP4-PDZ2_GgSTXBP4-like cd06698
PDZ1 domain of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus ...
 4612-4675 1.03e-04

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: 44.22  E-value: 1.03e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069550323 4612 GLGIRIVGGKEIPGtngEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSII 4675
Cdd:cd06698     12 GLGLSIVGGINRPE---GPMVFIQEVIPGGDCYKDGRLRPGDQLVSINKESLIGVTLEEAKSIL 72
PRK10927 PRK10927
cell division protein FtsN;
293-429 1.14e-04

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 47.75  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  293 ARASPQQANASKTSSQVPTPTKATVAQQGISTGKQPSQQ---PGGPTKPAPQSAGANKQATQQQGSAAKPAPQQTGPTKQ 369
Cdd:PRK10927    98 APTEPSAGGEVKTPEQLTPEQRQLLEQMQADMRQQPTQLvevPWNEQTPEQRQQTLQRQRQAQQLAEQQRLAQQSRTTEQ 177

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069550323  370 QLQQPGEPAK--PSAQQAGPTKQPQHQA------EPTKPTGQKPGPVQQKPEASPPQASQPggSASKK 429
Cdd:PRK10927   178 SWQQQTRTSQaaPVQAQPRQSKPASTQQpyqdllQTPAHTTAQSKPQQAAPVTRAADAPKP--TAEKK 243
PHA03378 PHA03378
EBNA-3B; Provisional
 174-421 1.30e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 48.52  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  174 EQDKPGqqkgpSKQPVQQQSPKPTGPQQGSVKPAPQKTappkqvvpqqqqqqqQQQQQPGVPKQAQKPGPGQQAGPQSEE 253
Cdd:PHA03378   549 ESDEPA-----STEPVHDQLLPAPGLGPLQIQPLTSPT---------------TSQLASSAPSYAQTPWPVPHPSQTPEP 608

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  254 AKKQQGAPKT----------------------------------QPQQSESTKTPPQQQQQSPAKPPPQQPGTARASPQQ 299
Cdd:PHA03378   609 PTTQSHIPETsaprqwpmplrpipmrplrmqpitfnvlvfptphQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQ 688

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  300 A--NASKTSSQVPTPTKATVAQQGistgkqPSQQPGGPTKPAPQSAGANKQATQQQGSAAKPAPQQTGPTKQQLQQ--PG 375
Cdd:PHA03378   689 WapGTMQPPPRAPTPMRPPAAPPG------RAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAaaPG 762

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2069550323  376 EPAKPSAQQAGPTKQPQHQAEPTKPTGQKPGPVQQKPEASPPQASQ 421
Cdd:PHA03378   763 RARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQ 808
C2A_SLP-1_2 cd08393
C2 domain first repeat present in Synaptotagmin-like proteins 1 and 2; All Slp members ...
 5137-5262 1.33e-04

C2 domain first repeat present in Synaptotagmin-like proteins 1 and 2; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike Slp3 and Slp4/granuphilin which are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176039 [Multi-domain]  Cd Length: 125  Bit Score: 44.73  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5137 GEIKIALKKEMKTdgEQLIVEILQCRNITYKFKSPDHlPDLYVKLYVvnLATQKRVIKKKTRVCRHDREPSFNETFRFSL 5216
Cdd:cd08393      2 GSVQFALDYDPKL--RELHVHVIQCQDLAAADPKKQR-SDPYVKTYL--LPDKSNRGKRKTSVKKKTLNPVFNETLRYKV 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2069550323 5217 SPTGHSLQILLVS--NGGKFMKKTLIGEAYIWLDKVDLRKRIVNWHKL 5262
Cdd:cd08393     77 EREELPTRVLNLSvwHRDSLGRNSFLGEVEVDLGSWDWSNTQPTWYPL 124
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
243-433 1.41e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 48.33  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  243 PGQQAGPQSEEAKKQqgAPKTQPQQSESTKTPPQQQQQSPAKPPPQQPGTARASPQQANASKTSSQVPTPTKATVAQQGI 322
Cdd:PRK12323   365 PGQSGGGAGPATAAA--APVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASAR 442

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  323 STGKQPSQQPGGPTKPAPQS------------AGANKQATQQQGSAAKPAPQQTGPTKqqlQQPGEPAKPSAQQAGPTKQ 390
Cdd:PRK12323   443 GPGGAPAPAPAPAAAPAAAArpaaagprpvaaAAAAAPARAAPAAAPAPADDDPPPWE---ELPPEFASPAPAQPDAAPA 519

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2069550323  391 PQHQAEPTKPTGQKPGPVQQKPEASPPQASQPGGSASKKTFCP 433
Cdd:PRK12323   520 GWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVA 562
PDZ3_Par3-like cd23059
PDZ domain 3 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
 4612-4675 1.42e-04

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: 44.20  E-value: 1.42e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069550323 4612 GLGIRIVG--GKEIPGTNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSII 4675
Cdd:cd23059     17 GLGVSVKGktSKEDNGGKADLGIFIKSIIHGGAASKDGRLRVNDQLIAVNGESLLGLTNSEAMETL 82
PDZ1_Dlg1-2-4-like cd06723
PDZ domain 1 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
 4610-4649 1.47e-04

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: 43.46  E-value: 1.47e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2069550323 4610 GNGLGIRIVGGKEIPGTNGEIGAYIAKILPGGSAEQTGKL 4649
Cdd:cd06723     10 NSGLGFSIAGGTDNPHIGDDPSIYITKIIPGGAAAADGRL 49
C2B_Synaptotagmin-15 cd08409
C2 domain second repeat present in Synaptotagmin 15; Synaptotagmin is a membrane-trafficking ...
 5137-5262 1.61e-04

C2 domain second repeat present in Synaptotagmin 15; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. It is thought to be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues and is Ca2+ independent. Human synaptotagmin 15 has 2 alternatively spliced forms that encode proteins with different C-termini. The larger, SYT15a, contains a N-terminal TM region, a putative fatty-acylation site, and 2 tandem C terminal C2 domains. The smaller, SYT15b, lacks the C-terminal portion of the second C2 domain. Unlike most other synaptotagmins it is nearly absent in the brain and rather is found in the heart, lungs, skeletal muscle, and testis. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176054 [Multi-domain]  Cd Length: 137  Bit Score: 45.02  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5137 GEIKIALKKEMKTDgeQLIVEILQCRNItyKFKSPDHLpDLYVKlyvVNLATQKRVIK-KKTRVCRHDREPSFNETFRFS 5215
Cdd:cd08409      2 GDIQISLTYNPTLN--RLTVVVLRARGL--RQLDHAHT-SVYVK---VSLMIHNKVVKtKKTEVVDGAASPSFNESFSFK 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069550323 5216 LSPTGHSLQILLVS--NGGKFMKKTLIGEAYI-------------WLDKV-DLRKRIVNWHKL 5262
Cdd:cd08409     74 VTSRQLDTASLSLSvmQSGGVRKSKLLGRVVLgpfmyargkelehWNDMLsKPKELIKRWHAL 136
PDZ3_FL-whirlin-like cd06742
PDZ domain 3 of the full-length isoform of whirlin, PDZ domain 1 of the short isoform of ...
 4613-4677 1.79e-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: 43.50  E-value: 1.79e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069550323 4613 LGIRIVGGKeipGTNgEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQ 4677
Cdd:cd06742     13 LGIAIEGGA---NTK-QPLPRVINIQRGGSAHNCGGLKVGHVILEVNGTSLRGLEHREAARLIAE 73
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 80-438 1.86e-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: 47.99  E-value: 1.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323   80 SGPPTLSKSRTVD--TLKTEQRVPGRSPSSISLRQSTSRTDFKEDQKPSMMPSFLSDANPFGAVTSVVNKFNPFDLISDS 157
Cdd:pfam05109  398 TAPKTLIITRTATnaTTTTHKVIFSKAPESTTTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPT 477

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  158 DTAQEEASKKQKPIQKEQDKPGQQKGPS----KQPVQQQSPKPTGPQQGSVKPAPQKTAPPKQVVPQQQQQQQQQQQQPG 233
Cdd:pfam05109  478 PAGTTSGASPVTPSPSPRDNGTESKAPDmtspTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATS 557

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  234 VPKQAQKPGPGQQAGPQSeeakkqqgapKTQPQQSESTKTPPQQQQQSPAKPPPQQPGTARASPQQANASKTSSQVPTPT 313
Cdd:pfam05109  558 PTPAVTTPTPNATIPTLG----------KTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATS 627

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  314 KATVAQQGISTGKQPSQ--QPGGPTKPAPQSAGANKQATQQQGSAAKPapqqTGPTKQQLQQPGEPAKPSAQQAGPTKQP 391
Cdd:pfam05109  628 AVTTGQHNITSSSTSSMslRPSSISETLSPSTSDNSTSHMPLLTSAHP----TGGENITQVTPASTSTHHVSTSSPAPRP 703

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2069550323  392 QHQAEPTKP----TGQKPGPVQQKPEASPPQASQPGGSASKKTFCPLCTTT 438
Cdd:pfam05109  704 GTTSQASGPgnssTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTST 754
C2A_Synaptotagmin-4-11 cd08388
C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a ...
 5154-5252 2.34e-04

C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmins 4 and 11, class 4 synaptotagmins, are located in the brain. Their functions are unknown. They are distinguished from the other synaptotagmins by having and Asp to Ser substitution in their C2A domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176034 [Multi-domain]  Cd Length: 128  Bit Score: 44.26  E-value: 2.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5154 LIVEILQCRNITYKfKSPDHLPDLYVKLYVvnLATQKRviKKKTRVCRHDREPSFNETFRFSLSPTGH----SLQILLVS 5229
Cdd:cd08388     18 LLVNIIECRDLPAM-DEQSGTSDPYVKLQL--LPEKEH--KVKTRVLRKTRNPVYDETFTFYGIPYNQlqdlSLHFAVLS 92

                           90       100
                   ....*....|....*....|...
gi 2069550323 5230 NgGKFMKKTLIGEAYIWLDKVDL 5252
Cdd:cd08388     93 F-DRYSRDDVIGEVVCPLAGADL 114
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 1457-1718 2.39e-04

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 47.73  E-value: 2.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1457 IQSEEKDVLKESCKKEILSQESsPTSPSDLAKLESTVLSILEAQASTLAEEKSGKSKDIYGVYSEHSRVPHKtKTQLGAP 1536
Cdd:PTZ00108  1141 LEEQEEVEEKEIAKEQRLKSKT-KGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDD-KPDNKKS 1218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1537 ESYSADEEDLAKQNIQGKYGGAPEEGDKQDILSQKSY---KGKTDTREDASARRQRYDSVEDSSESENSPVPQRKRRTSV 1613
Cdd:PTZ00108  1219 NSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEdndEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNG 1298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1614 GSSSSDdykaedsPGSGDDEDFIRKQIMEMSADEDASgseddefirnqlKEISITDSHKKEEMKNKK---GIPGKHKRmT 1690
Cdd:PTZ00108  1299 GSKPSS-------PTKKKVKKRLEGSLAALKKKKKSE------------KKTARKKKSKTRVKQASAsqsSRLLRRPR-K 1358

                          250       260
                   ....*....|....*....|....*...
gi 2069550323 1691 RKSSTGYEDDTSRRHSWHDDDDETFDES 1718
Cdd:PTZ00108  1359 KKSDSSSEDDDDSEVDDSEDEDDEDDED 1386
PDZ_Radil-like cd06690
PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; ...
 4610-4681 3.05e-04

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: 42.66  E-value: 3.05e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069550323 4610 GNGLGIRIVGGKEIPGtnGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIIsQQSGE 4681
Cdd:cd06690     12 PKGLGLGLIDGLHTPL--RSPGIYIRTLVPDSPAARDGRLRLGDRILAVNGTSLVGADYQSAMDLI-RTSGD 80
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 4613-4687 3.11e-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: 42.62  E-value: 3.11e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069550323 4613 LGIRIVGGKEIPGtnGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEAEICVR 4687
Cdd:cd06679     13 LGISVAGGRGSRR--GDLPIYVTNVQPDGCLGRDGRIKKGDVLLSINGISLTNLSHSEAVAVLKASAASSSIVLK 85
PTZ00121 PTZ00121
MAEBL; Provisional
 989-1330 3.25e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 3.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  989 QVKSAETPQQQKASARPAQNEKRGPDIQKEDPASQQGKpAKAISADKIQEIVQKEHTTPQQEKLPKTISADKLSQSISGE 1068
Cdd:PTZ00121  1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK-AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1069 DSEIQKGKIGKPPSADQVPKEEAKVVRKSSADKLLEIVQKKEPKELEHVSDNIQIQKEDPKVQQirlskppsadqirKED 1148
Cdd:PTZ00121  1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE-------------EEK 1756

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1149 PKVQQVKLSKTPSADQIRKEDPKVQQvkltkapsaDQIRKEDPKIQQVKLAKapSADQIQEDPKLQQGKFVKTPSADKIR 1228
Cdd:PTZ00121  1757 KKIAHLKKEEEKKAEEIRKEKEAVIE---------EELDEEDEKRRMEVDKK--IKDIFDNFANIIEGGKEGNLVINDSK 1825

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 1229 Q-EDPKIHQEKLTKVPSDSEIKKVdpkiQQAKLAK--IPSADHIQKEDSKL-------FKAKIVKTASADQLPKDNKFQE 1298
Cdd:PTZ00121  1826 EmEDSAIKEVADSKNMQLEEADAF----EKHKFNKnnENGEDGNKEADFNKekdlkedDEEEIEEADEIEKIDKDDIERE 1901

                          330       340       350
                   ....*....|....*....|....*....|..
gi 2069550323 1299 MELANIPVEDYISSKTIHDQTQVARRKEDDTK 1330
Cdd:PTZ00121  1902 IPNNNMAGKNNDIIDDKLDKDEYIKRDAEETR 1933
PDZ4_GRIP1-2-like cd06686
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 4606-4690 3.47e-04

PDZ domain 4 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 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: 467174 [Multi-domain]  Cd Length: 99  Bit Score: 42.72  E-value: 3.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4606 HSVSGNGLGIRIVGGKEIPGTNGEiGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEAEIC 4685
Cdd:cd06686     13 RGDPLKGFGIQLQGGVFATETLSS-PPLISFIEPDSPAERCGVLQVGDRVLSINGIPTEDRTLEEANQLLRDSASKVTLE 91


                   ....*
gi 2069550323 4686 VRLDI 4690
Cdd:cd06686     92 IEFDV 96
C2B_SLP_1-2-3-4 cd04020
C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically ...
 5137-5215 3.58e-04

C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike the case in Slp3 and Slp4/granuphilin in which their C2A domains are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp3 and Slp4/granuphilin promote dense-core vesicle exocytosis. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175987 [Multi-domain]  Cd Length: 162  Bit Score: 44.24  E-value: 3.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5137 GEIKIALK----------KEMKTDGEQLIVEILQCRNITYKfKSPDHLpDLYVKLYVvnLATQKRVIKKKTRVCRHDREP 5206
Cdd:cd04020      2 GELKVALKyvppesegalKSKKPSTGELHVWVKEAKNLPAL-KSGGTS-DSFVKCYL--LPDKSKKSKQKTPVVKKSVNP 77


                   ....*....
gi 2069550323 5207 SFNETFRFS 5215
Cdd:cd04020     78 VWNHTFVYD 86
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 109-373 4.11e-04

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: 46.95  E-value: 4.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  109 SLRQSTSRTDFKEDQKPSMMPSFLSDANPFGA-----VTSVVNKFNPFDLISD--SDTAQEEASKKQKPIQKEQDKPGQQ 181
Cdd:pfam09770  103 NRQQPAARAAQSSAQPPASSLPQYQYASQQSQqpskpVRTGYEKYKEPEPIPDlqVDASLWGVAPKKAAAPAPAPQPAAQ 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  182 KGPSKQPVQQ-------------QSPKPTGPQQGSVKPAPQktappKQVVPQQQQQQQQQQQQPGVPKQAQKPGPGQQAG 248
Cdd:pfam09770  183 PASLPAPSRKmmsleeveaamraQAKKPAQQPAPAPAQPPA-----APPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHP 257

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  249 PQSEEAKKQQGAPKTQPQQSEstktppqqqqqspakpppqqpgtarasPQQANASKTSSQVPTPTKATVAQQGISTGKQP 328
Cdd:pfam09770  258 GQGHPVTILQRPQSPQPDPAQ---------------------------PSIQPQAQQFHQQPPPVPVQPTQILQNPNRLS 310

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2069550323  329 SQQPGGPTKPAPQSAGANKQ-ATQQQGSAAKPAPQQTGPtkQQLQQ 373
Cdd:pfam09770  311 AARVGYPQNPQPGVQPAPAHqAHRQQGSFGRQAPIITHP--QQLAQ 354
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 4609-4675 4.54e-04

PDZ domain 2 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 2 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 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: 467223 [Multi-domain]  Cd Length: 84  Bit Score: 41.87  E-value: 4.54e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069550323 4609 SGNGLGIRIVGGKEIpgtngEIGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTAKTYEEVQSII 4675
Cdd:cd06741     10 DGQSLGLMIRGGAEY-----GLGIYVTGVDPGSVAENAG-LKVGDQILEVNGRSFLDITHDEAVKIL 70
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 27-427 5.50e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.70  E-value: 5.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323   27 PRLPSGEAPDLSQLSEAERRQIAAVlSRAQDPSPRHAQLDSSHHPRQPGKPPDSGPP----TLSKSRTVDTLKTEQRVPG 102
Cdd:PHA03307    63 DRFEPPTGPPPGPGTEAPANESRST-PTWSLSTLAPASPAREGSPTPPGPSSPDPPPptppPASPPPSPAPDLSEMLRPV 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  103 RSPSSISLRQS----TSRTDFKEDQKPSMMPSFLSDANPfGAVTSVVNKFNPFDLISDSDTAQEEASKKQKPIQKEQDKP 178
Cdd:PHA03307   142 GSPGPPPAASPpaagASPAAVASDAASSRQAALPLSSPE-ETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSP 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  179 GQQKGPSkqpvqQQSPKPTGPQQGSVKPAPQKTAPPKQVVPQQQQQQQQQQQQPGVPKQAQKPGPGqqAGPQSEEAKKQQ 258
Cdd:PHA03307   221 APAPGRS-----AADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSR--PGPASSSSSPRE 293

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  259 GAPKTQPQQSEStktppqqqqqspakppPQQPGTARASPQQANASKTSSQVPTPTKATVAQQGISTGKQPSqQPGGPTKP 338
Cdd:PHA03307   294 RSPSPSPSSPGS----------------GPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPS-RSPSPSRP 356

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  339 APQSAGANKQAtQQQGSAAKPAPQQTgptkqqlqqPGEPAKPSAQ-QAGPTKQPQHQAEPTKPTGQKPGPVQQKPEASPP 417
Cdd:PHA03307   357 PPPADPSSPRK-RPRPSRAPSSPAAS---------AGRPTRRRARaAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAF 426

                          410
                   ....*....|
gi 2069550323  418 QASQPGGSAS 427
Cdd:PHA03307   427 YARYPLLTPS 436
C2C_Ferlin cd04018
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 4823-4916 5.96e-04

C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175985 [Multi-domain]  Cd Length: 151  Bit Score: 43.39  E-value: 5.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4823 RDNNGYSDPFVKVYLLpgrGQvmvvqnasvenKRRTKYVQKSLNPEWNQTVIYKNI--SMEQlkkkTLEVTVWDYDRFSS 4900
Cdd:cd04018     29 GEKKELVDPYVEVSFA---GQ-----------KVKTSVKKNSYNPEWNEQIVFPEMfpPLCE----RIKIQIRDWDRVGN 90

                           90
                   ....*....|....*.
gi 2069550323 4901 NDFLGEVLIELSSSSQ 4916
Cdd:cd04018     91 DDVIGTHFIDLSKISN 106
C2C_Tricalbin-like cd04045
C2 domain third repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 4808-4912 6.43e-04

C2 domain third repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 176010 [Multi-domain]  Cd Length: 120  Bit Score: 42.58  E-value: 6.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4808 GNLIIHILQARNLAPRDNNGYSDPFVKVYLlpgRGQVmvvqnasvenKRRTKYVQKSLNPEWNQtVIYKNIsMEQLKKKT 4887
Cdd:cd04045      1 GVLRLHIRKANDLKNLEGVGKIDPYVRVLV---NGIV----------KGRTVTISNTLNPVWDE-VLYVPV-TSPNQKIT 65

                           90       100
                   ....*....|....*....|....*
gi 2069550323 4888 LEvtVWDYDRFSSNDFLGEVLIELS 4912
Cdd:cd04045     66 LE--VMDYEKVGKDRSLGSVEINVS 88
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 4614-4681 7.22e-04

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: 41.36  E-value: 7.22e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4614 GIRIVGGKE--IPGTngeigayIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGE 4681
Cdd:cd06753     11 GFRLQGGKDfnQPLT-------ISRVTPGGKAAQAN-LRPGDVILAINGESTEGMTHLEAQNKIKAATGS 72
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 297-422 7.91e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 46.01  E-value: 7.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  297 PQQANASKTSSQVPTPT----KATVAQQGISTGKQPSQQPGGPTKPAPQSAGANKQATQQQGSAAKPAPQQtgptKQQLQ 372
Cdd:PRK07994   361 PAAPLPEPEVPPQSAAPaasaQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQR----AQGAT 436

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2069550323  373 QPGEPAKPSAQQAGPTKQPQHQAEPTKPTGQKPGPVQQKPEASPPQASQP 422
Cdd:PRK07994   437 KAKKSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNP 486
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 4610-4671 9.29e-04

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: 41.45  E-value: 9.29e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069550323 4610 GNGLGIRIVG--GKeipGTNGEI-GAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEV 4671
Cdd:cd06791     11 EQGLGITIAGyvGE---KASGELsGIFVKSIIPGSAADQDGRIQVNDQIIAVDGVNLQGFTNQEA 72
C2F_Ferlin cd08374
C2 domain sixth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
 4881-4926 1.02e-03

C2 domain sixth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the sixth C2 repeat, C2E, and has a type-II topology.


Pssm-ID: 176020  Cd Length: 133  Bit Score: 42.27  E-value: 1.02e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2069550323 4881 EQLKKKTLEVTVWDYDRFSSNDFLGEVLIELSSSSQLDNTPRWYTL 4926
Cdd:cd08374     88 EYKIPPKLTLQVWDNDKFSPDDFLGSLELDLSILPRPAKTSKKCGL 133
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 ...
 4612-4687 1.17e-03

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: 41.06  E-value: 1.17e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069550323 4612 GLGIRIVGGKEIPGTNGEIgaYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSII-SQQSGEAEICVR 4687
Cdd:cd06763     12 GLGFSLEGGKGSPLGDRPL--TIKRIFKGGAAEQSGVLQVGDEILQINGTSLQGLTRFEAWNIIkSLPEGPVTLLIR 86
C2_Smurf-like cd08382
C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 ...
 4814-4922 1.17e-03

C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 domain is found in Smurf proteins, C2-WW-HECT-domain E3s, which play an important role in the downregulation of the TGF-beta signaling pathway. Smurf proteins also regulate cell shape, motility, and polarity by degrading small guanosine triphosphatases (GTPases). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have type-II topology.


Pssm-ID: 176028 [Multi-domain]  Cd Length: 123  Bit Score: 41.91  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4814 ILQARNLAPRDNNGYSDPFVKVyllpgrgqvmvvqnaSV--ENKRRTKYVQKSLNPEWNQTviYK-NISmeqlKKKTLEV 4890
Cdd:cd08382      6 VLCADGLAKRDLFRLPDPFAVI---------------TVdgGQTHSTDVAKKTLDPKWNEH--FDlTVG----PSSIITI 64

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2069550323 4891 TVWDYDRFSSND--FLGEVLIELSSSSQLDNTPR 4922
Cdd:cd08382     65 QVFDQKKFKKKDqgFLGCVRIRANAVLPLKDTGY 98
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
 4597-4677 1.40e-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: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4597 LKLPRDPKdhsvsgNGLGIRIVGGkEIPGTNgEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTY-------- 4668
Cdd:cd23072      5 VNLKKDAK------YGLGFQIVGG-EKSGRL-DLGIFISSITPGGPADLDGRLKPGDRLISVNDVSLEGLSHdaaveilq 76

                           90
                   ....*....|..
gi 2069550323 4669 ---EEVQSIISQ 4677
Cdd:cd23072     77 napEDVTLVVSQ 88
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 28-403 1.46e-03

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 44.95  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323   28 RLPSGEAPDLSQLSEAERRQIAA--VLSRAqdpsPRHAQLDSSHHPRQPGKPPDSGPPTLSKSR-TVDTLKTEQRVPGRS 104
Cdd:pfam17823   85 EVTAEHTPHGTDLSEPATREGAAdgAASRA----LAAAASSSPSSAAQSLPAAIAALPSEAFSApRAAACRANASAAPRA 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  105 P--SSISLRQSTSRTDFKEDQKPSMMPSFLSDANPFGAVTSVVNKFNPFDLISDSDTAQEEASKKQKPIQKEQDKPgqqk 182
Cdd:pfam17823  161 AiaAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGISTAATATGHPAAGTALAAVGNSSP---- 236

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  183 gpSKQPVQQQSPKPTGPQQGSVKPAPQKTAPPKQVVPQQQQQQQQQQQQPGVPKQAQKPGPGQQAGPQSEEAKKQqgAPK 262
Cdd:pfam17823  237 --AAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQ--VST 312

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  263 TQPQQS---ESTKTPPQQQQQSPAKPPPQQPGTARASPQQANASK-TSSQVPTPTKATVAQ-QGISTGKQPS-----QQP 332
Cdd:pfam17823  313 DQPVHNtagEPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAQAKEpSASPVPVLHTSMIPEvEATSPTTQPSpllptQGA 392

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069550323  333 GGPTKPapqsagankQATQQQGSAAKPAPQQTGPTKQQLQQPGEPAKPSAQqagPTKQPQHQAEPTKPTGQ 403
Cdd:pfam17823  393 AGPGIL---------LAPEQVATEATAGTASAGPTPRSSGDPKTLAMASCQ---LSTQGQYLVVTTDPLTP 451
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 4596-4679 1.47e-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: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4596 RLKLPRDPKDHsvsGNGLGIRIVGGKEIpGTngeiGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTAKTYEEVQSII 4675
Cdd:cd06737      1 KLRLVRLDRRG---PESLGFSVRGGLEH-GC----GLFVSHVSPGSQADNKG-LRVGDEIVRINGYSISQCTHEEVINLI 71


                   ....
gi 2069550323 4676 SQQS 4679
Cdd:cd06737     72 KTKK 75
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 328-417 1.50e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 44.80  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  328 PSQQPGGPTKPAPqsagANKQATQQQGSAAKPAPQQTGPTKQQLQQPGEPAKPSAQQAGPTKQPQHQAEPTKPTGQKPgp 407
Cdd:PRK14950   364 PAPQPAKPTAAAP----SPVRPTPAPSTRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRAAIP-- 437

                           90
                   ....*....|
gi 2069550323  408 VQQKPEASPP 417
Cdd:PRK14950   438 VDEKPKYTPP 447
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 507-769 1.60e-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: 44.76  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  507 KQKMAAPTTAGKPPPQAQQPTQKKE-STVKPDATQSPEHKKPPppqtkqptiPSSTPEKAKP---PAPETQQTESTPKSD 582
Cdd:NF033839   289 NKKPSAPKPGMQPSPQPEKKEVKPEpETPKPEVKPQLEKPKPE---------VKPQPEKPKPevkPQLETPKPEVKPQPE 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  583 QTKPapaedkQKQPHVQKPISDVVPKPS----EFDTKQDSPGP--KPAPVQQKV-VHPQGSevAKSSEDTPQDKTVPPDT 655
Cdd:NF033839   360 KPKP------EVKPQPEKPKPEVKPQPEtpkpEVKPQPEKPKPevKPQPEKPKPeVKPQPE--KPKPEVKPQPEKPKPEV 431

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  656 KTSPqvsrQKSDPKLVSQP-GSGIDTKVQKQTEPVEGKGDLKKMQPQMSPKPDAkqaqkpqqatvgPKPTQSQPKAtQSQ 734
Cdd:NF033839   432 KPQP----EKPKPEVKPQPeKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEK------------PKPDNSKPQA-DDK 494

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2069550323  735 PPAQPQQSQKAPEQSSRFSLNIGGFTDSSKSQPTT 769
Cdd:NF033839   495 KPSTPNNLSKDKQPSNQASTNEKATNKPKKSLPST 529
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
 4609-4675 1.72e-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: 40.42  E-value: 1.72e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069550323 4609 SGNGLGIRIVGGKEipgtNGeIGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTAKTYEEVQSII 4675
Cdd:cd06740     11 SHEGLGFSIRGGAE----HG-VGIYVSLVEPGSLAEKEG-LRVGDQILRVNDVSFEKVTHAEAVKIL 71
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
 4609-4682 1.93e-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: 40.29  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4609 SGNGLGIRIVGG------KEIPGTngeigayIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEA 4682
Cdd:cd06681     10 EGNSFGFVIRGGahedrnKSRPLT-------VTHVRPGGPADREGTIKPGDRLLSVDGISLHGATHAEAMSILKQCGQEA 82
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 325-430 1.96e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  325 GKQPSQQPGGPTKPAPQSAGANKQATQQQGSAAKPAPQqtgptkqqlqqpgEPAKPSAQQAGPTKQPQHQAEPTKPTGQK 404
Cdd:PRK07764   384 RLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAA-------------APAPAAAPQPAPAPAPAPAPPSPAGNAPA 450

                           90       100
                   ....*....|....*....|....*.
gi 2069550323  405 PGPVQQKPEASPPQASQPGGSASKKT 430
Cdd:PRK07764   451 GGAPSPPPAAAPSAQPAPAPAAAPEP 476
PDZ4_INAD-like cd23065
PDZ domain 4 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
 4608-4686 2.01e-03

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: 40.19  E-value: 2.01e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069550323 4608 VSGNGLGIRIVGGKEIPGTngeiGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEAEICV 4686
Cdd:cd23065      6 TDKSPLGVSVVGGKNHVTT----GCIITHIYPNSIVAADKRLKVFDQILDINGTKVHVMTTLKVHQLFHKTYEKAVTLV 80
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 325-434 2.32e-03

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: 44.64  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  325 GKQPSQQPGGPTKPAPQSAGANKQAT----------------QQQGSAAKPAPQQTGPTKQQLQQPGEPAKPSAQQAGPT 388
Cdd:pfam09770  164 GVAPKKAAAPAPAPQPAAQPASLPAPsrkmmsleeveaamraQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQ 243

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2069550323  389 KQPQHQAEPTKPTGQKPGPVQ--QKPEASPPQASQPGGSASKKTFCPL 434
Cdd:pfam09770  244 QQPQQQPQQPQQHPGQGHPVTilQRPQSPQPDPAQPSIQPQAQQFHQQ 291
PDZ2-PDZRN4-like cd06716
PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 4629-4679 2.43e-03

PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PDZRN4, PDZRN3-B, and related domains. PDZRN4 (also known as ligand of numb protein X 4, and SEMACAP3-like protein) contains an N-terminal RING domain and two tandem repeat PDZ domains. It is involved in the progression of cancer, including human liver cancer and breast cancer, and may contribute to the tumorigenesis of rectal adenocarcinoma. Danio rerio PDZRN3-B may participate in neurogenesis: the first PDZ domain of Danio rerio Pdzrn3 interacts with Kidins220 (Kinase D-interacting substrate 220 kD, also named Ankyrin Repeat-Rich Membrane Spanning), a crucial mediator of signal transduction in neural tissues. 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 PDZRN4-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: 467200 [Multi-domain]  Cd Length: 88  Bit Score: 39.95  E-value: 2.43e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2069550323 4629 EIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLtaKTYEEVQSIISQQS 4679
Cdd:cd06716     30 DTGIYVSEVDPNSIAAKDGRIREGDQILQINGVDV--QNREEAIALLSEEE 78
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
238-428 2.51e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 44.46  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  238 AQKPGPGQQAGPqseeAKKQQGAPKTQPQQSESTKTPPQQQQQSPAKPPPQQPGTARASPQQANASKTSSQVPTPTKATV 317
Cdd:PRK07003   357 AFEPAVTGGGAP----GGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAP 432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  318 AQQG-ISTGKQPSQQPGGPTKPAPQSAGANKQATQQQgSAAKPAPQQTGPTKQQLQQPGEPAKPSAQQAGPTKQPqhQAE 396
Cdd:PRK07003   433 PATAdRGDDAADGDAPVPAKANARASADSRCDERDAQ-PPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAA--VPD 509

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2069550323  397 PTKPTGQKPGPVQQKPEASPPQASQPGGSASK 428
Cdd:PRK07003   510 ARAPAAASREDAPAAAAPPAPEARPPTPAAAA 541
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
183-425 2.57e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 44.46  E-value: 2.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  183 GPSKQPVQQQSPKPTGPQQGSVKPAPQKTAPPKQVVPQQQQQQQQQQQQPGVPKQAQKPGPGQQAGPQSEEAKKQQGAPK 262
Cdd:PRK07003   372 VPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPA 451

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  263 TQPQQSESTKTPPQQQQQSPAKPPPQQPGTARASPQQANASKTSSQVPTPTKATVAQQGISTGKQPSqqpggPTKPAPQS 342
Cdd:PRK07003   452 KANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASR-----EDAPAAAA 526

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  343 AGAnKQATQQQGSAAKPAPQQTGP--------------TKQQLQQPGEPAKPSAQQAGPTKQPQHQAE---PTKPTGQKP 405
Cdd:PRK07003   527 PPA-PEARPPTPAAAAPAARAGGAaaaldvlrnagmrvSSDRGARAAAAAKPAAAPAAAPKPAAPRVAvqvPTPRARAAT 605

                          250       260
                   ....*....|....*....|
gi 2069550323  406 GPVQQKPEASPPQASQPGGS 425
Cdd:PRK07003   606 GDAPPNGAARAEQAAESRGA 625
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
 5135-5215 2.75e-03

C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology and do not bind Ca2+.


Pssm-ID: 175997 [Multi-domain]  Cd Length: 125  Bit Score: 41.08  E-value: 2.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 5135 VMGEIKIALKKEMKTdgEQLIVEILQCRNItykfKSPDH--LPDLYVKLYVVNLATQKRviKKKTRVCRHDREPSFNETF 5212
Cdd:cd04031      1 ITGRIQIQLWYDKVT--SQLIVTVLQARDL----PPRDDgsLRNPYVKVYLLPDRSEKS--KRRTKTVKKTLNPEWNQTF 72


                   ...
gi 2069550323 5213 RFS 5215
Cdd:cd04031     73 EYS 75
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
 4807-4913 2.79e-03

C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176009 [Multi-domain]  Cd Length: 124  Bit Score: 41.00  E-value: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4807 LGNLIIHILQARNLAPRDN-NGYSDPFVKVyllpgrgqvmvvqnaSVENKR---RTKYVQKSLNPEWNQTviyKNISMEQ 4882
Cdd:cd04044      1 IGVLAVTIKSARGLKGSDIiGGTVDPYVTF---------------SISNRRelaRTKVKKDTSNPVWNET---KYILVNS 62

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2069550323 4883 LKKKtLEVTVWDYDRFSSNDFLGEVLIELSS 4913
Cdd:cd04044     63 LTEP-LNLTVYDFNDKRKDKLIGTAEFDLSS 92
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
 4613-4686 2.94e-03

PDZ domain 4 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 4 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 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: 467168 [Multi-domain]  Cd Length: 89  Bit Score: 40.02  E-value: 2.94e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069550323 4613 LGIRIVGGKEipGTNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEAEICV 4686
Cdd:cd06680     13 LGFSIVGGYE--ESHGNQPFFVKSIVPGTPAYNDGRLKCGDIILAVNGVSTVGMSHAALVPLLKEQRGRVTLTV 84
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 4612-4672 3.08e-03

PDZ domain 1 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 1 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 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: 467188 [Multi-domain]  Cd Length: 87  Bit Score: 39.95  E-value: 3.08e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069550323 4612 GLGIRIVGGK-EIPGTNGEIGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLT-AKTYEEVQ 4672
Cdd:cd06704     11 GLGISIAGGKgSTPYKGDDEGIFISRVTEGGPAAKAG-VRVGDKLLEVNGVDLVdADHHEAVE 72
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
 5153-5218 3.15e-03

C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is present in cPLA2 which releases arachidonic acid from membranes initiating the biosynthesis of potent inflammatory mediators such as prostaglandins, leukotrienes, and platelet-activating factor. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members of this cd have a type-II topology.


Pssm-ID: 176001 [Multi-domain]  Cd Length: 119  Bit Score: 40.71  E-value: 3.15e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069550323 5153 QLIVEILQCRNIT-YKFKSPdhlPDLYVKLYVVNLATQKrvikKKTRVCRHDREPSFNETFRFSLSP 5218
Cdd:cd04036      1 LLTVRVLRATNITkGDLLST---PDCYVELWLPTASDEK----KRTKTIKNSINPVWNETFEFRIQS 60
motB PRK05996
MotB family protein;
293-428 3.17e-03

MotB family protein;


Pssm-ID: 235665 [Multi-domain]  Cd Length: 423  Bit Score: 43.53  E-value: 3.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  293 ARASPQQANAS-KTSSQVPTPTKATVAQQGIS----------TGKQPSQQPGGPTKPAPqsagANKQATQQQGSAAKPA- 360
Cdd:PRK05996   145 AQEVGQQANVSaKGDGGAAQSGPATGADGGEAyrdpfdpdfwSKQVEVTTAGDLLPPGQ----AREQAQGAKSATAAPAt 220

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069550323  361 PQQTGPTKQqlQQPGEPAKPSAQQAGPTKQPQHQAEPTKPTGQKPGPVQQKPEASPPQA-----SQPGGSASK 428
Cdd:PRK05996   221 VPQAAPLPQ--AQPKKAATEEELIADAKKAATGEPAANAAKAAKPEPMPDDQQKEAEQLqaaiaQAIGGVAGK 291
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 4613-4661 3.47e-03

PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa. PDZD7 also forms homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the second PDZ domain of the canonical isoform of PDZD7- isoform 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 PDZD7-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: 467270 [Multi-domain]  Cd Length: 85  Bit Score: 39.68  E-value: 3.47e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2069550323 4613 LGIRIVGGKEIPgtngeIGAYIAKILPGGSAEQTGkLMEGMQVLEWNGI 4661
Cdd:cd10834     15 LGFNIRGGSEYG-----LGIYVSKVDPGGLAEQNG-IKVGDQILAVNGV 57
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 304-429 3.64e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 43.70  E-value: 3.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  304 KTSSQVPTPTKATVAQQGIStgkqpsQQPGGPTKPAPQSAGANKQATQQQGSAAKPAPQQTGPTKQQLQQPgePAKPSAQ 383
Cdd:PRK07994   362 AAPLPEPEVPPQSAAPAASA------QATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAAR--QQLQRAQ 433

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2069550323  384 QAGPTKQPqhqaEPTKPTGQKPGPVQQKPEASPPQASQPGGSASKK 429
Cdd:PRK07994   434 GATKAKKS----EPAAASRARPVNSALERLASVRPAPSALEKAPAK 475
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 329-416 3.98e-03

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 43.73  E-value: 3.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  329 SQQPGGPTKPAPQSAGANKQATQQQGSAAKPAPQQTGPTKQQLQQPGEPAKPSAQQAGPTKQPqhqAEPTKPTGQKPGPV 408
Cdd:PRK12270    35 DYGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPA---APPAAAAAAAPAAA 111


                   ....*...
gi 2069550323  409 QQKPEASP 416
Cdd:PRK12270   112 AVEDEVTP 119
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 4612-4691 4.05e-03

PDZ domain 5 of Danio rerio tyrosine-protein 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 5 of Danio rerio Ptpn13, and related domains. Protein-tyrosine phosphatases (PTPs) dephosphorylate phosphotyrosyl residues in proteins that are phosphorylated by protein tyrosine kinases (PTKs). Danio rerio Ptpn13 is a classical non-receptor-like PTP. 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 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: 467273 [Multi-domain]  Cd Length: 80  Bit Score: 39.26  E-value: 4.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4612 GLGIRIVGGkeipgtNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQQSGEaeicVRLDIS 4691
Cdd:cd23060     11 GLGFSLVGG------EGGSGIFVKSISPGGVADRDGRLQVGDRLLQVNGESVIGLSHSKAVNILRKAKGT----VQLTVS 80
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 292-422 4.21e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 43.70  E-value: 4.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  292 TARASPQQANASKTSSQVPTPTKATVAQQGISTGKQPSQQPGGPTKPAPQsAGANKQATQQQGSAAKPAPQQTGPTKqQL 371
Cdd:PRK07994   375 AAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLA-ARQQLQRAQGATKAKKSEPAAASRAR-PV 452

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2069550323  372 QQPGEPAKPSAQQAGPTKQPQHQAEPTKPTGQKPGPVQQKPEASPPQASQP 422
Cdd:PRK07994   453 NSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKA 503
PHA03378 PHA03378
EBNA-3B; Provisional
 292-458 4.33e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.52  E-value: 4.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  292 TARASPQQANASKTSSQVPTPTKATVAQQGISTGKQPSQQPGgptkPAPQSAGANKQATQQQGSAAKPAPQQ---TGPTK 368
Cdd:PHA03378   721 TGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPG----RARPPAAAPGAPTPQPPPQAPPAPQQrprGAPTP 796

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  369 QQLQQPGepakPSAQQAGPtKQPQHQAEPTKPT-------GQKPG-PVQQKPEASPPQAS-----QPGGSASKKT----- 430
Cdd:PHA03378   797 QPPPQAG----PTSMQLMP-RAAPGQQGPTKQIlrqlltgGVKRGrPSLKKPAALERQAAagptpSPGSGTSDKIvqapv 871

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2069550323  431 -FCPLCTTTELL--LHTPEKANYNTCTQCQT 458
Cdd:PHA03378   872 fYPPVLQPIQVMrqLGSVRAAAASTVTQAPT 902
PDZ3_PDZD7-like cd06751
PDZ domain 3 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 4613-4677 4.55e-03

PDZ domain 3 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of the Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa and can also form homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the third PDZ domain of the canonical isoform of PDZD7- isoform 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 PDZD7-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: 467233 [Multi-domain]  Cd Length: 89  Bit Score: 39.34  E-value: 4.55e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069550323 4613 LGIRIVGGKEipgTNGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIISQ 4677
Cdd:cd06751     13 LGISISGGIE---SKVQPVVKIEKIFPGGAAALSGNLKAGYELVSVDGESLQQVTHQQAVDIIRR 74
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 316-455 4.79e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 43.18  E-value: 4.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  316 TVAQQGISTGKQPSQQPGGP--TKPAPQSAGANKQATQQQGSAAKPAPQQTGPTKQQLQQPGEPAKPSAQQAGPTKQPqH 393
Cdd:PHA03269    11 TIACINLIIANLNTNIPIPElhTSAATQKPDPAPAPHQAASRAPDPAVAPTSAASRKPDLAQAPTPAASEKFDPAPAP-H 89

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069550323  394 QAEPTKPtgqKPGPVQQKPEASPPQASQPGGSASKKTFCPLCTTTELLLHTPEKANYNTCTQ 455
Cdd:PHA03269    90 QAASRAP---DPAVAPQLAAAPKPDAAEAFTSAAQAHEAPADAGTSAASKKPDPAAHTQHSP 148
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
177-423 5.19e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.33  E-value: 5.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  177 KPGQQKGPSKQPVQQQSPKPTgpqqgsvkPAPqktappkqvvpqqqqqqqqqqqqpgvPKQAQKPGPGQQAGPQSEEAKK 256
Cdd:PRK12323   364 RPGQSGGGAGPATAAAAPVAQ--------PAP--------------------------AAAAPAAAAPAPAAPPAAPAAA 409

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  257 QQGAPKTQPQQSESTKTPPQQQQQSPAKPPPQQPGTARASPQQANASKTSSQVPTPTKATVAQQGISTGKQPSQQPGGPT 336
Cdd:PRK12323   410 PAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAP 489

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  337 KPAPQSAGANKQATqqqGSAAKPAPQQTGPTKQQLQQPGEPaKPSAQQAGPTKQPQHQAEPTKPTGQKPGPVQQKPEASP 416
Cdd:PRK12323   490 APADDDPPPWEELP---PEFASPAPAQPDAAPAGWVAESIP-DPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRP 565


                   ....*..
gi 2069550323  417 PQASQPG 423
Cdd:PRK12323   566 PRASASG 572
PHA03377 PHA03377
EBNA-3C; Provisional
 293-440 5.28e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 43.50  E-value: 5.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  293 ARASPQQANASKTSSQVPTPTKATVAQQGISTGKQPSQQPGG-PTKPAPQSAGANKQA----------------TQQQGS 355
Cdd:PHA03377   446 AQSTPERPGPSDQPSVPVEPAHLTPVEHTTVILHQPPQSPPTvAIKPAPPPSRRRRGAcvvydddiievidvetTEEEES 525

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  356 AAKPA-----PQQTGPTKQQLQQPGEPAKPSAQQAGPTKQPQHQAEPTKPTGQKPGPVQQKPEASPPQASQPGGSASKKT 430
Cdd:PHA03377   526 VTQPAkphrkVQDGFQRSGRRQKRATPPKVSPSDRGPPKASPPVMAPPSTGPRVMATPSTGPRDMAPPSTGPRQQAKCKD 605

                          170
                   ....*....|
gi 2069550323  431 FCPLCTTTEL 440
Cdd:PHA03377   606 GPPASGPHEK 615
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 3856-3919 5.42e-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: 42.55  E-value: 5.42e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069550323 3856 ARAKILQDIDRELDLVERESAKLRKKQAELDEEEKEIDaklrylEMGINRRKEALLKEREKRER 3919
Cdd:pfam07946  265 TREEEIEKIKKAAEEERAEEAQEKKEEAKKKEREEKLA------KLSPEEQRKYEEKERKKEQR 322
C2A_RasGAP cd08383
C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
 4810-4926 5.71e-03

C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. The proteins here all contain either a single C2 domain or two tandem C2 domains, a Ras-GAP domain, and a pleckstrin homology (PH)-like domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 176029 [Multi-domain]  Cd Length: 117  Bit Score: 39.94  E-value: 5.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4810 LIIHILQARNLAPRdnnGYSDPFVKVYLlpgrGQVMVVqnasvenkrRTKYVQKsLNPEWNQTVIYKNISMEqLKKKTLE 4889
Cdd:cd08383      2 LRLRILEAKNLPSK---GTRDPYCTVSL----DQVEVA---------RTKTVEK-LNPFWGEEFVFDDPPPD-VTFFTLS 63

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2069550323 4890 VTVWDYDRFSSNDFLGEVLIelsssSQLDN---TPRWYTL 4926
Cdd:cd08383     64 FYNKDKRSKDRDIVIGKVAL-----SKLDLgqgKDEWFPL 98
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
4807-4913 5.96e-03

Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 43.21  E-value: 5.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4807 LGNLIIHILQARNLAPRDN--NGYSDPFVkVYLLPGRGqvmvvqnasvenKRRTKYVQKSLNPEWNQTvIYknISMEQLK 4884
Cdd:COG5038    435 IGVVEVKIKSAEGLKKSDStiNGTVDPYI-TVTFSDRV------------IGKTRVKKNTLNPVWNET-FY--ILLNSFT 498

                           90       100
                   ....*....|....*....|....*....
gi 2069550323 4885 KKtLEVTVWDYDRFSSNDFLGEVLIELSS 4913
Cdd:COG5038    499 DP-LNLSLYDFNSFKSDKVVGSTQLDLAL 526
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 159-726 6.11e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.15  E-value: 6.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  159 TAQEEASKKQKPIQKEQDKPGQQKgPSKQPVQQQSPKPtGPQQG--SVKPAPQKTAPPKQVVPQQqqqqqqqqqqpgvpk 236
Cdd:PRK10263   328 TATQSWAAPVEPVTQTPPVASVDV-PPAQPTVAWQPVP-GPQTGepVIAPAPEGYPQQSQYAQPA--------------- 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  237 qAQKPGPGQQ-AGPQSEEAKKQQGAPKTQPQQSESTKTPPQQQQQSPAKPPPQQPGTARASPQQANASktssqvptptka 315
Cdd:PRK10263   391 -VQYNEPLQQpVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFA------------ 457

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  316 tvaqqgistgKQPSQQPGGP-TKPAPQSAGANKQATQQQGSAAKPAP--QQTGPTKQQLQQPGE----PAKPSAQQAG-- 386
Cdd:PRK10263   458 ----------PQSTYQTEQTyQQPAAQEPLYQQPQPVEQQPVVEPEPvvEETKPARPPLYYFEEveekRAREREQLAAwy 527

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  387 -PTKQPQHQAEPTKPTGQKPGPVQQKPEASPPQASQPGGSASKKTfcpLCTTTELLLHTPekanyntctqcqtVVCSLCG 465
Cdd:PRK10263   528 qPIPEPVKEPEPIKSSLKAPSVAAVPPVEAAAAVSPLASGVKKAT---LATGAAATVAAP-------------VFSLANS 591

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  466 FNPNPHITE-IKEWLCLNCQMQRALGGDLGPAPGPGPQSSAPKQKMAA----PTTAGKPPPQAQQPTQKKESTVKPDATQ 540
Cdd:PRK10263   592 GGPRPQVKEgIGPQLPRPKRIRVPTRRELASYGIKLPSQRAAEEKAREaqrnQYDSGDQYNDDEIDAMQQDELARQFAQT 671

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  541 SP----EHKKPPPPQTKQPTIPSSTPEKAKPPAPETQQTESTPKSDQTKPAPAEDKQKQPhvQKPISDVVPKPSEFdtkq 616
Cdd:PRK10263   672 QQqrygEQYQHDVPVNAEDADAAAEAELARQFAQTQQQRYSGEQPAGANPFSLDDFEFSP--MKALLDDGPHEPLF---- 745

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  617 dSPGPKPAPVQQKVVHPQGSEVAKSSEDTPQDKTVPPDTKTSPQVSRQKSDPKLVSQPgsgidtKVQKQTEPVEGKGDLK 696
Cdd:PRK10263   746 -TPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQP------QYQQPQQPVAPQPQYQ 818

                          570       580       590
                   ....*....|....*....|....*....|
gi 2069550323  697 KMQPQMSPKPdakQAQKPQQaTVGPKPTQS 726
Cdd:PRK10263   819 QPQQPVAPQP---QYQQPQQ-PVAPQPQDT 844
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 299-719 6.44e-03

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: 43.22  E-value: 6.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  299 QANASkTSSQVPTPT-----KATVAQQGISTGKQPSQQPGGPTKPAPQSAGANKQATQQQG---SAAKPAPQQTGPTKQQ 370
Cdd:pfam03154  139 QDNRS-TSPSIPSPQdnesdSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGptpSAPSVPPQGSPATSQP 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  371 LQQPGEPAKP-SAQQAGPTKQPQHQAEPTKPTGQKPGPVqqKPEASPPQASQPGgsaskktfcplctttelLLHTPekan 449
Cdd:pfam03154  218 PNQTQSTAAPhTLIQQTPTLHPQRLPSPHPPLQPMTQPP--PPSQVSPQPLPQP-----------------SLHGQ---- 274

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  450 yntctqcqtvvcslcgFNPNPHITEIKEWLclncqmqraLGGDLGPAPGPGPQSSAPKQKMAAPTTAgkpppqaqqPTQK 529
Cdd:pfam03154  275 ----------------MPPMPHSLQTGPSH---------MQHPVPPQPFPLTPQSSQSQVPPGPSPA---------APGQ 320

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  530 KESTVKPDATQSPEHKKPPPPQTKQPTIPSSTPEKAKPPA------PETQQTESTPKSDQTKPAPAEDKQKQPHVQKPIS 603
Cdd:pfam03154  321 SQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTtpipqlPNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLS 400

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  604 DVvpkpsefdTKQDSPGPKPAPVQqkvVHPQGSEVAKSSEDTP---QDKTVPPDTKTSPQVSRQKSDPklvSQPGSGIDT 680
Cdd:pfam03154  401 SL--------STHHPPSAHPPPLQ---LMPQSQQLPPPPAQPPvltQSQSLPPPAASHPPTSGLHQVP---SQSPFPQHP 466

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2069550323  681 KVQKQTEPVegkgdLKKMQPQMSPKPDAKQAQKPQQATV 719
Cdd:pfam03154  467 FVPGGPPPI-----TPPSGPPTSTSSAMPGIQPPSSASV 500
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
326-430 6.58e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 42.84  E-value: 6.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  326 KQPSQQPGGPTKPApqsagANKQATQQQGSAAkPAPQQtgptkqqlqQPGEPAKPSAQQAGPTKQPQHQAEPTKPTgQKP 405
Cdd:PRK14971   369 ASGGRGPKQHIKPV-----FTQPAAAPQPSAA-AAASP---------SPSQSSAAAQPSAPQSATQPAGTPPTVSV-DPP 432

                           90       100
                   ....*....|....*....|....*
gi 2069550323  406 GPVQQKPEASPPQASQPGGSASKKT 430
Cdd:PRK14971   433 AAVPVNPPSTAPQAVRPAQFKEEKK 457
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
238-427 7.32e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.91  E-value: 7.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  238 AQKPGPGQQAGPQSEEAKKQQGAPKTQPQQSESTKTPPQQQQQSPAKPPPQQPGTARASPQQANASKTSSQVPTPTKATV 317
Cdd:PRK07003   380 VPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASA 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  318 AQQGISTGKQPSQQPGGPTKPAPQSAGAnkqatqqqgSAAKPAPQQTGPTKQQLQQPGEPAKPSAQQAGptKQPQHQAEP 397
Cdd:PRK07003   460 DSRCDERDAQPPADSGSASAPASDAPPD---------AAFEPAPRAAAPSAATPAAVPDARAPAAASRE--DAPAAAAPP 528

                          170       180       190
                   ....*....|....*....|....*....|
gi 2069550323  398 TkPTGQKPGPVQQKPeasppqASQPGGSAS 427
Cdd:PRK07003   529 A-PEARPPTPAAAAP------AARAGGAAA 551
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 291-423 7.62e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.78  E-value: 7.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  291 GTARASPQQANASKTSSQVPTPTKATVAQQgiSTGKQPSQQPGGPTKPAPQS-AGANKQATQQQGSAAKPAPQQTGPTKQ 369
Cdd:PRK14951   368 AAAEAAAPAEKKTPARPEAAAPAAAPVAQA--AAAPAPAAAPAAAASAPAAPpAAAPPAPVAAPAAAAPAAAPAAAPAAV 445

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2069550323  370 QLQQPgepakPSAQQAGPTKQPQHQAEPTKPTGQKPGPVQQKPEASPPQASQPG 423
Cdd:PRK14951   446 ALAPA-----PPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEG 494
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
 4599-4680 8.99e-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: 38.33  E-value: 8.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323 4599 LPRDPKdhsvsGNGLGIRivGGKEIpgtnGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTAKTYEEVQSIIsQQ 4678
Cdd:cd06735      6 LERGPK-----GFGFSIR--GGREY----NNMPLYVLRLAEDGPAQRDGRLRVGDQILEINGESTQGMTHAQAIELI-RS 73


                   ..
gi 2069550323 4679 SG 4680
Cdd:cd06735     74 GG 75
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 157-413 9.42e-03

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: 42.33  E-value: 9.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  157 SDTAQEEASK--KQKPIQKEQDKPGQQKGPSKQPVQQQSPKPTGPQQgSVKPAPQKTAPPKQVVPQQQQQQQQQQQQPGV 234
Cdd:pfam09770   92 SDAIEEEQVRfnRQQPAARAAQSSAQPPASSLPQYQYASQQSQQPSK-PVRTGYEKYKEPEPIPDLQVDASLWGVAPKKA 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  235 PKQAQKPGPGQQAGPQS---------EE--------AKKQQGAPKTQPQQSESTKTPPQQQQQSPAKPPPQQPGTARASP 297
Cdd:pfam09770  171 AAPAPAPQPAAQPASLPapsrkmmslEEveaamraqAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQP 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069550323  298 QQanasktssqvptptkatvAQQGISTGKQPSQQPGGPTKPAPQSAGANKQATQQQGSAAKPAPQQtgPTkQQLQQPGEP 377
Cdd:pfam09770  251 QQ------------------PQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQ--PT-QILQNPNRL 309

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2069550323  378 AK-----PSAQQAGPTKQPQHQAEPTKPTGQKPGPVQQKPE 413
Cdd:pfam09770  310 SAarvgyPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITHPQ 350
 
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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