NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|150170670|ref|NP_055325|]
View 

protein piccolo isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
4694-4826 1.72e-63

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: 212.88  E-value: 1.72e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4694 ITGEIQLQINYD--LGNLIIHILQARNLVPRDNNGYSDPFVKVYLLPGRgqvmvvqnaSAEYKRRTKHVQKSLNPEWNQT 4771
Cdd:cd04031     1 ITGRIQIQLWYDkvTSQLIVTVLQARDLPPRDDGSLRNPYVKVYLLPDR---------SEKSKRRTKTVKKTLNPEWNQT 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 150170670 4772 VIYKSISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLsSTSHLDNTPRWYPLK 4826
Cdd:cd04031    72 FEYSNVRRETLKERTLEVTVWDYDRDGENDFLGEVVIDL-ADALLDDEPHWYPLQ 125
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
4492-4587 4.09e-49

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: 170.81  E-value: 4.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4492 FPHARIKITRDSKDHTVSGNGLGIRIVGGKEIPghSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEV 4571
Cdd:cd06714     2 FLIGRIILQRDPKDGSVSGNGLGLKVVGGKMTE--SGRLGAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEV 79
                          90
                  ....*....|....*.
gi 150170670 4572 QSIISQQSGEAEICVR 4587
Cdd:cd06714    80 QDIISQSKGEVELVVS 95
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
587-648 1.73e-42

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


:

Pssm-ID: 277313 [Multi-domain]  Cd Length: 62  Bit Score: 150.57  E-value: 1.73e-42
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150170670  587 TICPLCNTTELLLHVPEKANFNTCTECQTTVCSLCGFNPNPHLTEVKEWLCLNCQMKRALGG 648
Cdd:cd15774     1 TICPLCKTTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
1057-1120 5.89e-42

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


:

Pssm-ID: 277315 [Multi-domain]  Cd Length: 64  Bit Score: 149.06  E-value: 5.89e-42
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670 1057 STCPLCKTELNIGSKDPPNFNTCTECKNQVCNLCGFNPTPHLTEIQEWLCLNCQTQRAISGQLG 1120
Cdd:cd15776     1 LLCPLCKTELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQLG 64
PHA03247 super family cl33720
large tegument protein UL36; Provisional
308-905 6.88e-27

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 122.35  E-value: 6.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  308 QPTPgKPPAQQPGHEKSQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEK-PSSEQP 386
Cdd:PHA03247 2572 RPAP-RPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPpTVPPPE 2650
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  387 GPKALAQPPGV-----GKTPAQQPGPAKPPTQqvgtPKPLAQQPG---LQSPAKAPGPTKTPVQQPGPgKIPAQQAGPGK 458
Cdd:PHA03247 2651 RPRDDPAPGRVsrprrARRLGRAAQASSPPQR----PRRRAARPTvgsLTSLADPPPPPPTPEPAPHA-LVSATPLPPGP 2725
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  459 TSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSqqPGSTKPPPQQPGPAKPSPqqPGSTKPPSQqPGSAK 538
Cdd:PHA03247 2726 AAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA--PAPPAAPAAGPPRRLTRP--AVASLSESR-ESLPS 2800
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  539 PSAQQPSPAKPSAQQSTKPVSQTGSGkPLQPPTVSPSAKQPPSQGLPKTICPLCNTTelllhvpekanfntctecqttvc 618
Cdd:PHA03247 2801 PWDPADPPAAVLAPAAALPPAASPAG-PLPPPTSAQPTAPPPPPGPPPPSLPLGGSV----------------------- 2856
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  619 slcgfnpnphltevkewlclncqmkrALGGDLAPVPSSPQPKLKTAPVTTTSAVSKSSPQPQQtSPKKDAAPKQDLSKAP 698
Cdd:PHA03247 2857 --------------------------APGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSR-STESFALPPDQPERPP 2909
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  699 EPKKPPPlvkqptlhgsPSAKAKQPPEADSLSKPAPPKEPSVPSEQDKAPVADDKPKQPKMVKPTTDLVSSSSATTKPDI 778
Cdd:PHA03247 2910 QPQAPPP----------PQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRV 2979
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  779 PSSKVQSQAEEKTTPPLKTDSAKPSQSFPPTgekvSPFDSKAIPRPASDSKIISHPGPSSESKGQKQVDpvqkkEEPKKA 858
Cdd:PHA03247 2980 PQPAPSREAPASSTPPLTGHSLSRVSSWASS----LALHEETDPPPVSLKQTLWPPDDTEDSDADSLFD-----SDSERS 3050
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|..
gi 150170670  859 QTK-MSPKPDAKPMPKGSPTPPGPRPTAGQTVPTPQQSPKPQEQ----SRRF 905
Cdd:PHA03247 3051 DLEaLDPLPPEPHDPFAHEPDPATPEAGARESPSSQFGPPPLSAnaalSRRY 3102
PTZ00121 super family cl31754
MAEBL; Provisional
1157-1700 1.93e-10

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.86  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1157 VKKQEQEVKTEAEkvilEKVKETLSMEKIPPMVTTDQKQEESKLEKDKASALQEKKPLPEEKKLiPEEEKIRSEEKKPLL 1236
Cdd:PTZ00121 1320 AKKKAEEAKKKAD----AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK-ADAAKKKAEEKKKAD 1394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1237 EEKKPTPEDKKLLPEAKTSAPEEQKHDLLKSQvqiAEEKLEGRVAPKTVQEGKQP-QTKMEGLPSGTPQSLPKEDDKTTK 1315
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKK---AEEKKKADEAKKKAEEAKKAdEAKKKAEEAKKAEEAKKKAEEAKK 1471
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1316 TIKEQPQPPCTAKPDQVEPGKEKTEKEDDKSDTSSSQQPKSPQGL-SDTGYSSDGI--------------------SSSL 1374
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKkAEEAKKADEAkkaeeakkadeakkaeekkkADEL 1551
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1375 GEIPSLIPTDEKDILKGLKKDSFSQESSPSSPSDLAKLESTVLSILEAQASTLADEKSE--KKTQPHEVSPEQPKDQEKT 1452
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEeaKKAEEAKIKAEELKKAEEE 1631
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1453 QSLSETLEITISEEEIKESQEERKDTFKK-DSQQDIPSSKDHKEKSEfvddiTTRREPYDSVEESSESENSPvPQRKRRT 1531
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKiKAAEEAKKAEEDKKKAE-----EAKKAEEDEKKAAEALKKEA-EEAKKAE 1705
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1532 SVGSSSSDEYKQEDSQGSGEEEDFIRKQIIEMSADEDASGSED---DEFIRNQLKEISSSTESQKKEETKGKGKITAGKH 1608
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEakkDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1609 RRltrksstsidEDAGRRHSWHDEDDEAFDESPELK------------YRETKSQESEELVVTGGGGLRRFKTIELNSTI 1676
Cdd:PTZ00121 1786 DE----------EDEKRRMEVDKKIKDIFDNFANIIeggkegnlvindSKEMEDSAIKEVADSKNMQLEEADAFEKHKFN 1855
                         570       580       590
                  ....*....|....*....|....*....|
gi 150170670 1677 ADKYSAESSQ------KKTSLYFDEEPELE 1700
Cdd:PTZ00121 1856 KNNENGEDGNkeadfnKEKDLKEDDEEEIE 1885
kgd super family cl39092
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
947-1027 1.90e-05

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


The actual alignment was detected with superfamily member PRK12270:

Pssm-ID: 476867 [Multi-domain]  Cd Length: 1228  Bit Score: 51.43  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  947 STAGQPGPHSQSGPGAPMKQAPAPSQPPTSQGPPKSTGQAPPAPAKsipvKKETKAPAAEKLEPKAEQAPTVKRTETEKK 1026
Cdd:PRK12270   43 APTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAA----AAAAAAAPAAPPAAAAAAAPAAAAVEDEVT 118

                  .
gi 150170670 1027 P 1027
Cdd:PRK12270  119 P 119
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
32-411 7.34e-05

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.21  E-value: 7.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   32 PSHTAIPAGMEADLSQLSEEERRQIAAVMSRAQGLPKGSVPPAAAESPSMHRKQELDSSHPPKQSGRPPDPGRPAQPGLS 111
Cdd:PRK07764  427 AAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGA 506
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  112 ksRTTDTFRSE-----QKLPGRSPSTISLKESKSR------TDLKEEHKSSMMPGFLSEVNALSAVSSVVnkfnpfdlis 180
Cdd:PRK07764  507 --DDAATLRERwpeilAAVPKRSRKTWAILLPEATvlgvrgDTLVLGFSTGGLARRFASPGNAEVLVTAL---------- 574
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  181 dseasQEETTKKQKVVQKEQGKPEGiikPPLQQQPPKPIPKQQGPGRDPLQQDGTPKSISSQQPEKikSQPPGTGKPIQG 260
Cdd:PRK07764  575 -----AEELGGDWQVEAVVGPAPGA---AGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGA--AAAPAEASAAPA 644
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  261 PTQTPQTDHAKLPLQRDASRPQTKQADIVRGESVKPSLPSPSKPPIQQPTPGKPPAQQPgheKSQPGPAKPPAQPSGLTK 340
Cdd:PRK07764  645 PGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAP---APAATPPAGQADDPAAQP 721
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150170670  341 PLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQqtgsekPSSEQPGPKALAQPPGVGKTPAQQPGPAKPP 411
Cdd:PRK07764  722 PQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAP------AQPPPPPAPAPAAAPAAAPPPSPPSEEEEMA 786
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
3460-3965 9.36e-05

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 49.31  E-value: 9.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3460 RRRRTKKSVDTSVQTDDEDQDEW---------DMPTRSRRKARVGKY--------GDSMTEADKTKPLSKVSSIAVQTVA 3522
Cdd:PRK10263  258 MGRQTDAALFSGKRMDDDEEITYtargvaadpDDVLFSGNRATQPEYdeydpllnGAPITEPVAVAAAATTATQSWAAPV 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3523 EISVQTEPVGTIRTPSIRARVDAKVEIIKHISAPEktykggslgCQTEADSDTQSPQYLSATSPPKDK-KRPTPLEIGYS 3601
Cdd:PRK10263  338 EPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPV---------IAPAPEGYPQQSQYAQPAVQYNEPlQQPVQPQQPYY 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3602 SHLRADSTVQLAPSPPKSPKVLYSPISPLSPGKALESAFVPYEKPLPDDisPQKVLHPDMAKVPPASPKTAKMMQRSMSD 3681
Cdd:PRK10263  409 APAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFA--PQSTYQTEQTYQQPAAQEPLYQQPQPVEQ 486
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3682 PKPLSPT--ADES--SRAPFQYTEGYTTKGSQTMTSSGA-----QKKVKRTLPN------------PPPEEIST------ 3734
Cdd:PRK10263  487 QPVVEPEpvVEETkpARPPLYYFEEVEEKRAREREQLAAwyqpiPEPVKEPEPIksslkapsvaavPPVEAAAAvsplas 566
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3735 ----GTQSTFSTMGTVSRRRICRTNTMARAKILQDIDRELDLVERESAKLRKKQAELD--------EEEKEIDAKLRYLE 3802
Cdd:PRK10263  567 gvkkATLATGAAATVAAPVFSLANSGGPRPQVKEGIGPQLPRPKRIRVPTRRELASYGiklpsqraAEEKAREAQRNQYD 646
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3803 MGINRRK---EALLKEREKRERAYLQ-------------GVAEDRDYMSDSEVSSTRPTRIESQHGIERPRTAPQTEFSQ 3866
Cdd:PRK10263  647 SGDQYNDdeiDAMQQDELARQFAQTQqqrygeqyqhdvpVNAEDADAAAEAELARQFAQTQQQRYSGEQPAGANPFSLDD 726
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3867 F-----------------IPPQTQTESQlvPPTSPYTQYQYSSPALPTQAPTSYTQ-QSHFEQQTLYHQQVSPYQTQPTF 3928
Cdd:PRK10263  727 FefspmkallddgpheplFTPIVEPVQQ--PQQPVAPQQQYQQPQQPVAPQPQYQQpQQPVAPQPQYQQPQQPVAPQPQY 804
                         570       580       590
                  ....*....|....*....|....*....|....*..
gi 150170670 3929 QavatmsftpQVQPTPTPQPSYQLPSQMMVIQQKPRQ 3965
Cdd:PRK10263  805 Q---------QPQQPVAPQPQYQQPQQPVAPQPQYQQ 832
 
Name Accession Description Interval E-value
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
4694-4826 1.72e-63

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: 212.88  E-value: 1.72e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4694 ITGEIQLQINYD--LGNLIIHILQARNLVPRDNNGYSDPFVKVYLLPGRgqvmvvqnaSAEYKRRTKHVQKSLNPEWNQT 4771
Cdd:cd04031     1 ITGRIQIQLWYDkvTSQLIVTVLQARDLPPRDDGSLRNPYVKVYLLPDR---------SEKSKRRTKTVKKTLNPEWNQT 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 150170670 4772 VIYKSISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLsSTSHLDNTPRWYPLK 4826
Cdd:cd04031    72 FEYSNVRRETLKERTLEVTVWDYDRDGENDFLGEVVIDL-ADALLDDEPHWYPLQ 125
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
4492-4587 4.09e-49

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: 170.81  E-value: 4.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4492 FPHARIKITRDSKDHTVSGNGLGIRIVGGKEIPghSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEV 4571
Cdd:cd06714     2 FLIGRIILQRDPKDGSVSGNGLGLKVVGGKMTE--SGRLGAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEV 79
                          90
                  ....*....|....*.
gi 150170670 4572 QSIISQQSGEAEICVR 4587
Cdd:cd06714    80 QDIISQSKGEVELVVS 95
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
587-648 1.73e-42

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


Pssm-ID: 277313 [Multi-domain]  Cd Length: 62  Bit Score: 150.57  E-value: 1.73e-42
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150170670  587 TICPLCNTTELLLHVPEKANFNTCTECQTTVCSLCGFNPNPHLTEVKEWLCLNCQMKRALGG 648
Cdd:cd15774     1 TICPLCKTTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
1057-1120 5.89e-42

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


Pssm-ID: 277315 [Multi-domain]  Cd Length: 64  Bit Score: 149.06  E-value: 5.89e-42
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670 1057 STCPLCKTELNIGSKDPPNFNTCTECKNQVCNLCGFNPTPHLTEIQEWLCLNCQTQRAISGQLG 1120
Cdd:cd15776     1 LLCPLCKTELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQLG 64
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
1057-1115 1.66e-39

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: 142.17  E-value: 1.66e-39
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  1057 STCPLCK-TELNIGSKDPPNFNTCTECKNQVCNLCGFNPTPHLTEIQEWLCLNCQTQRAI 1115
Cdd:pfam05715    1 TLCPLCKtTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
587-646 3.00e-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: 135.62  E-value: 3.00e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   587 TICPLCNTTELLLHVPEKANFNTCTECQTTVCSLCGFNPNPHLTEVKEWLCLNCQMKRAL 646
Cdd:pfam05715    1 TLCPLCKTTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
C2 pfam00168
C2 domain;
4707-4825 4.82e-32

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 122.43  E-value: 4.82e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  4707 GNLIIHILQARNLVPRDNNGYSDPFVKVYLLPGrgqvmvvqnasaEYKRRTKHVQKSLNPEWNQTVIYkSISMEQlkKKT 4786
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNGTSDPYVKVYLLDG------------KQKKKTKVVKNTLNPVWNETFTF-SVPDPE--NAV 65
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 150170670  4787 LEVTVWDYDRFSSNDFLGEVLIDLSSTSHLDNTPRWYPL 4825
Cdd:pfam00168   66 LEIEVYDYDRFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
4709-4822 3.27e-27

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: 108.34  E-value: 3.27e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   4709 LIIHILQARNLVPRDNNGYSDPFVKVYLLPGRGQvmvvqnasaeyKRRTKHVQKSLNPEWNQTVIYKSISMEqlkKKTLE 4788
Cdd:smart00239    2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKE-----------KKKTKVVKNTLNPVWNETFEFEVPPPE---LAELE 67
                            90       100       110
                    ....*....|....*....|....*....|....
gi 150170670   4789 VTVWDYDRFSSNDFLGEVLIDLSSTSHLDNTPRW 4822
Cdd:smart00239   68 IEVYDKDRFGRDDFIGQVTIPLSDLLLGGRHEKL 101
PHA03247 PHA03247
large tegument protein UL36; Provisional
308-905 6.88e-27

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 122.35  E-value: 6.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  308 QPTPgKPPAQQPGHEKSQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEK-PSSEQP 386
Cdd:PHA03247 2572 RPAP-RPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPpTVPPPE 2650
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  387 GPKALAQPPGV-----GKTPAQQPGPAKPPTQqvgtPKPLAQQPG---LQSPAKAPGPTKTPVQQPGPgKIPAQQAGPGK 458
Cdd:PHA03247 2651 RPRDDPAPGRVsrprrARRLGRAAQASSPPQR----PRRRAARPTvgsLTSLADPPPPPPTPEPAPHA-LVSATPLPPGP 2725
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  459 TSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSqqPGSTKPPPQQPGPAKPSPqqPGSTKPPSQqPGSAK 538
Cdd:PHA03247 2726 AAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA--PAPPAAPAAGPPRRLTRP--AVASLSESR-ESLPS 2800
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  539 PSAQQPSPAKPSAQQSTKPVSQTGSGkPLQPPTVSPSAKQPPSQGLPKTICPLCNTTelllhvpekanfntctecqttvc 618
Cdd:PHA03247 2801 PWDPADPPAAVLAPAAALPPAASPAG-PLPPPTSAQPTAPPPPPGPPPPSLPLGGSV----------------------- 2856
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  619 slcgfnpnphltevkewlclncqmkrALGGDLAPVPSSPQPKLKTAPVTTTSAVSKSSPQPQQtSPKKDAAPKQDLSKAP 698
Cdd:PHA03247 2857 --------------------------APGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSR-STESFALPPDQPERPP 2909
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  699 EPKKPPPlvkqptlhgsPSAKAKQPPEADSLSKPAPPKEPSVPSEQDKAPVADDKPKQPKMVKPTTDLVSSSSATTKPDI 778
Cdd:PHA03247 2910 QPQAPPP----------PQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRV 2979
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  779 PSSKVQSQAEEKTTPPLKTDSAKPSQSFPPTgekvSPFDSKAIPRPASDSKIISHPGPSSESKGQKQVDpvqkkEEPKKA 858
Cdd:PHA03247 2980 PQPAPSREAPASSTPPLTGHSLSRVSSWASS----LALHEETDPPPVSLKQTLWPPDDTEDSDADSLFD-----SDSERS 3050
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|..
gi 150170670  859 QTK-MSPKPDAKPMPKGSPTPPGPRPTAGQTVPTPQQSPKPQEQ----SRRF 905
Cdd:PHA03247 3051 DLEaLDPLPPEPHDPFAHEPDPATPEAGARESPSSQFGPPPLSAnaalSRRY 3102
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
226-575 1.84e-18

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: 94.06  E-value: 1.84e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   226 GRDPLQQDGTPKSISSQQPEKIKSQPPGTGKPIQGPTQTPQTDHAKLPLQRDASRPQTKQADIVRGESVKPSLPSPSKPP 305
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPP 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   306 IQQPTPGKPPAQQPGHEKSQP---GPAKPPAQPSGLTKPLAQQPGtvkpPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPS 382
Cdd:pfam03154  249 LQPMTQPPPPSQVSPQPLPQPslhGQMPPMPHSLQTGPSHMQHPV----PPQPFPLTPQSSQSQVPPGPSPAAPGQSQQR 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   383 SEQPGPKALAQPPgvgKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKtpVQQPGPGKIPAQQAGPGKTSAQ 462
Cdd:pfam03154  325 IHTPPSQSQLQSQ---QPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPH--LSGPSPFQMNSNLPPPPALKPL 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   463 QTGPTK-PPSQLPGPAKPPPQ----QPGPAKPP--------PQQPGSAKPPSQ-QPGSTKPP-PQQP-GPAKPSPQQPGS 526
Cdd:pfam03154  400 SSLSTHhPPSAHPPPLQLMPQsqqlPPPPAQPPvltqsqslPPPAASHPPTSGlHQVPSQSPfPQHPfVPGGPPPITPPS 479
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150170670   527 TKPPS--------QQPGSAKPSAQQPSPAKPSA-----QQSTKPVSQTGSGKPLQPPTVSPS 575
Cdd:pfam03154  480 GPPTStssampgiQPPSSASVSSSGPVPAAVSCplppvQIKEEALDEAEEPESPPPPPRSPS 541
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
270-585 3.41e-12

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 72.79  E-value: 3.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  270 AKLPLQRDASRPQTKQADIVRGESVKPSLPSPSKPPIQQPTPgKPPAQQPGHEKSQPGPAKPPAQPSGLTKPLAQQPGTV 349
Cdd:COG5180   146 AGVALAAALLQRSDPILAKDPDGDSASTLPPPAEKLDKVLTE-PRDALKDSPEKLDRPKVEVKDEAQEEPPDLTGGADHP 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  350 KPPVQPPGTTKPPAQPLGPAKPPaqqTGSEKPSSEQPGPKALAQPPGVGKTPAQQPgpakpptqqvgtpkplaqqPGLQS 429
Cdd:COG5180   225 RPEAASSPKVDPPSTSEARSRPA---TVDAQPEMRPPADAKERRRAAIGDTPAAEP-------------------PGLPV 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  430 PAKAPGPTKTPVQQPGPGKIpaqQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPG--PAKPPPQQPGSAKPPSQQPGST 507
Cdd:COG5180   283 LEAGSEPQSDAPEAETARPI---DVKGVASAPPATRPVRPPGGARDPGTPRPGQPTerPAGVPEAASDAGQPPSAYPPAE 359
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670  508 KPPPQQPGPA-KPSPQQPGSTKPPSQqPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPSQGLP 585
Cdd:COG5180   360 EAVPGKPLEQgAPRPGSSGGDGAPFQ-PPNGAPQPGLGRRGAPGPPMGAGDLVQAALDGGGRETASLGGAAGGAGQGPK 437
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
4509-4587 4.99e-12

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: 64.71  E-value: 4.99e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670   4509 SGNGLGIRIVGGKEIPGhsgeiGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGEAEICVR 4587
Cdd:smart00228   10 GGGGLGFSLVGGKDEGG-----GVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
337-582 1.01e-10

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: 68.26  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  337 GLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSE-KPSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQqv 415
Cdd:NF033839  278 GLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEvKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVK-- 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  416 gtPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPgKTSAQQTGPTKPPSQLPGPAKPPPQqpgpAKPPPQQPG 495
Cdd:NF033839  356 --PQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKP-KPEVKPQPEKPKPEVKPQPEKPKPE----VKPQPEKPK 428
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  496 SAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQStKPvsQTGSGKPLQPPTVSPS 575
Cdd:NF033839  429 PEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNS-KP--QADDKKPSTPNNLSKD 505

                  ....*..
gi 150170670  576 aKQPPSQ 582
Cdd:NF033839  506 -KQPSNQ 511
PTZ00121 PTZ00121
MAEBL; Provisional
1157-1700 1.93e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.86  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1157 VKKQEQEVKTEAEkvilEKVKETLSMEKIPPMVTTDQKQEESKLEKDKASALQEKKPLPEEKKLiPEEEKIRSEEKKPLL 1236
Cdd:PTZ00121 1320 AKKKAEEAKKKAD----AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK-ADAAKKKAEEKKKAD 1394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1237 EEKKPTPEDKKLLPEAKTSAPEEQKHDLLKSQvqiAEEKLEGRVAPKTVQEGKQP-QTKMEGLPSGTPQSLPKEDDKTTK 1315
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKK---AEEKKKADEAKKKAEEAKKAdEAKKKAEEAKKAEEAKKKAEEAKK 1471
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1316 TIKEQPQPPCTAKPDQVEPGKEKTEKEDDKSDTSSSQQPKSPQGL-SDTGYSSDGI--------------------SSSL 1374
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKkAEEAKKADEAkkaeeakkadeakkaeekkkADEL 1551
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1375 GEIPSLIPTDEKDILKGLKKDSFSQESSPSSPSDLAKLESTVLSILEAQASTLADEKSE--KKTQPHEVSPEQPKDQEKT 1452
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEeaKKAEEAKIKAEELKKAEEE 1631
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1453 QSLSETLEITISEEEIKESQEERKDTFKK-DSQQDIPSSKDHKEKSEfvddiTTRREPYDSVEESSESENSPvPQRKRRT 1531
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKiKAAEEAKKAEEDKKKAE-----EAKKAEEDEKKAAEALKKEA-EEAKKAE 1705
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1532 SVGSSSSDEYKQEDSQGSGEEEDFIRKQIIEMSADEDASGSED---DEFIRNQLKEISSSTESQKKEETKGKGKITAGKH 1608
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEakkDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1609 RRltrksstsidEDAGRRHSWHDEDDEAFDESPELK------------YRETKSQESEELVVTGGGGLRRFKTIELNSTI 1676
Cdd:PTZ00121 1786 DE----------EDEKRRMEVDKKIKDIFDNFANIIeggkegnlvindSKEMEDSAIKEVADSKNMQLEEADAFEKHKFN 1855
                         570       580       590
                  ....*....|....*....|....*....|
gi 150170670 1677 ADKYSAESSQ------KKTSLYFDEEPELE 1700
Cdd:PTZ00121 1856 KNNENGEDGNkeadfnKEKDLKEDDEEEIE 1885
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
4705-4815 1.18e-09

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 65.17  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4705 DLGNLIIHILQARNLVPRDNNGYSDPFVKVYLlpgrgqvmvvqnaSAEYKRRTKHVQKSLNPEWNQtviykSISMEQLKK 4784
Cdd:COG5038  1038 NSGYLTIMLRSGENLPSSDENGYSDPFVKLFL-------------NEKSVYKTKVVKKTLNPVWNE-----EFTIEVLNR 1099
                          90       100       110
                  ....*....|....*....|....*....|...
gi 150170670 4785 KT--LEVTVWDYDRFSSNDFLGEVLIDLSSTSH 4815
Cdd:COG5038  1100 VKdvLTINVNDWDSGEKNDLLGTAEIDLSKLEP 1132
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
322-583 8.23e-09

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 61.46  E-value: 8.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  322 EKSQPGPAKP--------PAQPSGLTKPlaQQPGTVKPPVQPPGTTKP-----PAQPLGPAKPPAQQtGSEKPSSE--QP 386
Cdd:NF038329  118 EKGEPGPAGPagpageqgPRGDRGETGP--AGPAGPPGPQGERGEKGPagpqgEAGPQGPAGKDGEA-GAKGPAGEkgPQ 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  387 GPKALAQPPGvGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPT-----KTPVQQPGPGKIPAQQAGPGKT-- 459
Cdd:NF038329  195 GPRGETGPAG-EQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTgedgpQGPDGPAGKDGPRGDRGEAGPDgp 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  460 --SAQQTGPTKPPSQ--------LPGPAKPPPQQPGPAKP-------PPQQPGSAKPPSQ--QPGstKPPPQQPG-PAKP 519
Cdd:NF038329  274 dgKDGERGPVGPAGKdgqngkdgLPGKDGKDGQNGKDGLPgkdgkdgQPGKDGLPGKDGKdgQPG--KPAPKTPEvPQKP 351
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150170670  520 SpQQPGSTKPPsQQPGSAKPSAqqPSPAKPSAQQSTKPvsQTGSGKPL-QPPTVSPSAKQPPSQG 583
Cdd:NF038329  352 D-TAPHTPKTP-QIPGQSKDVT--PAPQNPSNRGLNKP--QTQGGNQLaKTPAAHDTHRQLPATG 410
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
307-550 1.54e-08

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 60.94  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  307 QQPTPGKPPAQQPGHEKSQPGPAKPPAQPSgltkplaQQPGTVKPPVQP-PGTTKPPAQPlGPAKPPAQQtgseKPSSEQ 385
Cdd:NF033839  304 QPEKKEVKPEPETPKPEVKPQLEKPKPEVK-------PQPEKPKPEVKPqLETPKPEVKP-QPEKPKPEV----KPQPEK 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  386 PGPKALAQPPGVGKTPAQQPGPAKPPTQqvgtPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPgKTSAQQTG 465
Cdd:NF033839  372 PKPEVKPQPETPKPEVKPQPEKPKPEVK----PQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKP-KPEVKPQP 446
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  466 PTKPPSQLPGPAKPPPQ-QPGPAKPPPQqpgsAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQP 544
Cdd:NF033839  447 EKPKPEVKPQPETPKPEvKPQPEKPKPE----VKPQPEKPKPDNSKPQADDKKPSTPNNLSKDKQPSNQASTNEKATNKP 522

                  ....*.
gi 150170670  545 SPAKPS 550
Cdd:NF033839  523 KKSLPS 528
PHA03247 PHA03247
large tegument protein UL36; Provisional
823-1389 1.65e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.41  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  823 RPAsDSKIISHPGPSSESKGQKQVDPVQKKEEPKKAQTKMSPKPDAKPMP-----------------KGSPTPP----GP 881
Cdd:PHA03247 2482 RPA-EARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVHprmltwirgleelasddAGDPPPPlppaAP 2560
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  882 RPTAGQTVPTPQQSPKPQEQSRRfslnlgsitdAPKSQPTTPQETVTGKlfgfgasifsqasnliSTAGQPGPHSQSGPG 961
Cdd:PHA03247 2561 PAAPDRSVPPPRPAPRPSEPAVT----------SRARRPDAPPQSARPR----------------APVDDRGDPRGPAPP 2614
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  962 APMKQAPAPSQPPTSQGPPKSTGQAPPAPAKSIPVKKETKAPAAEKLEPKaeqaptvKRTETEKKPP----PIKDSKSLT 1037
Cdd:PHA03247 2615 SPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRP-------RRARRLGRAAqassPPQRPRRRA 2687
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1038 AEPQKAVLpTKLEKSPKPESTCPLCKTELNIGSKDPPNFNTCTecknqvcnlcGFNPTPHLTEIQEwlclncQTQRAISG 1117
Cdd:PHA03247 2688 ARPTVGSL-TSLADPPPPPPTPEPAPHALVSATPLPPGPAAAR----------QASPALPAAPAPP------AVPAGPAT 2750
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1118 QLGDIRKM-PPAPSGPKASPMPVPTESSSQKTAVPPQVklvkkqeQEVKTEAEKVILEKVKETLSMEKIPPMVTTDQKQE 1196
Cdd:PHA03247 2751 PGGPARPArPPTTAGPPAPAPPAAPAAGPPRRLTRPAV-------ASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS 2823
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1197 ESKLEKDKASALQEKKPLPEEkkliPEEEKIRSE---------EKKPLLEEKKPTPEDKKLLPEAKTSAPEEQKHDLLKS 1267
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPPG----PPPPSLPLGgsvapggdvRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFA 2899
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1268 QVQIAEEKLEGRVAPKTVQEGKQPQTKMEGLPSGTPQSLPKEDDKTTKTIKEQPQPPCTAK--------PDQVEPGKEKT 1339
Cdd:PHA03247 2900 LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPqpwlgalvPGRVAVPRFRV 2979
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|
gi 150170670 1340 EKEDDKSDTSSSQQPkSPQGLSDTGYSSDGISSSLGEIPSLIPTDEKDIL 1389
Cdd:PHA03247 2980 PQPAPSREAPASSTP-PLTGHSLSRVSSWASSLALHEETDPPPVSLKQTL 3028
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
453-557 1.89e-07

trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia intracellular motility A), WP_004266405.1-like proteins in Burkholderia mallei or B. pseudomallei. The term BimA has also been used for WP_011205626.1-like homologs that have a very different N-terminal half.


Pssm-ID: 468913 [Multi-domain]  Cd Length: 382  Bit Score: 56.83  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  453 QAGPGKTSAQQTGPTKPPSQLPGPakPPPQQPGPAKPPPQQPGSAKPPSqqPGSTKPPPQQPGPAKPSPQQPgSTKPPSQ 532
Cdd:NF040983   69 QIKKGDFKLKPVGDRTLPNKVPPP--PPPPPPPPPPPPTPPPPPPPPPP--PPPPSPPPPPPPSPPPSPPPP-TTTPPTR 143
                          90       100
                  ....*....|....*....|....*
gi 150170670  533 QPgsakPSAQQPSPAKPSAQQSTKP 557
Cdd:NF040983  144 TT----PSTTTPTPSMHPIQPTQLP 164
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
4502-4581 1.92e-07

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 51.51  E-value: 1.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  4502 DSKDHTVSGNGLGIRIVGGKEipghSGEIGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGE 4581
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSD----QGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGK 75
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
416-586 3.21e-07

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: 56.70  E-value: 3.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  416 GTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKP----------PSQLPGPAKPPPQ-QP 484
Cdd:NF033839  288 GNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPevkpqletpkPEVKPQPEKPKPEvKP 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  485 GPAKPPPQ---QPGSAKPPSQQPGSTKPPPQQPGPAKPSPQ-QPGSTKP-PSQQPGSAKPSAQ-QPSPAKPSAQQSTKPV 558
Cdd:NF033839  368 QPEKPKPEvkpQPETPKPEVKPQPEKPKPEVKPQPEKPKPEvKPQPEKPkPEVKPQPEKPKPEvKPQPEKPKPEVKPQPE 447
                         170       180
                  ....*....|....*....|....*...
gi 150170670  559 SQTGSGKPlQPPTVSPSAKQPPSQGLPK 586
Cdd:NF033839  448 KPKPEVKP-QPETPKPEVKPQPEKPKPE 474
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
458-563 6.10e-07

trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia intracellular motility A), WP_004266405.1-like proteins in Burkholderia mallei or B. pseudomallei. The term BimA has also been used for WP_011205626.1-like homologs that have a very different N-terminal half.


Pssm-ID: 468913 [Multi-domain]  Cd Length: 382  Bit Score: 55.29  E-value: 6.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  458 KTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQpgSTKPPSQQP--G 535
Cdd:NF040983   83 RTLPNKVPPPPPPPPPPPPPPPTPPPPPPPPPPPPPPSPPPPPPPSPPPSPPPPTTTPPTRTTPST--TTPTPSMHPiqP 160
                          90       100
                  ....*....|....*....|....*...
gi 150170670  536 SAKPSAQQPSPAKPSAQQSTKPVSQTGS 563
Cdd:NF040983  161 TQLPSIPNATPTSGSATNVTINFNSTGA 188
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
331-591 5.39e-06

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


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 52.62  E-value: 5.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  331 PPAQPSGLTKPLAQQPGTVKPPVQppgttKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQ--PGPA 408
Cdd:cd22540    39 PPAVEAAVTPPAPPQPTPRKLVPI-----KPAPLPLGPGKNSIGFLSAKGNIIQLQGSQLSSSAPGGQQVFAIQnpTMII 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  409 KPPTQQVGTPKPLAQQPGLQspakapgptkTPVQQPGPGKIpaqQAGPGKTSAQ----QTGPTKPPSQLPGPAKPPPQQP 484
Cdd:cd22540   114 KGSQTRSSTNQQYQISPQIQ----------AAGQINNSGQI---QIIPGTNQAIitpvQVLQQPQQAHKPVPIKPAPLQT 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  485 GPA-KPPPQQPGSA--KPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQT 561
Cdd:cd22540   181 SNTnSASLQVPGNVikLQSGGNVALTLPVNNLVGTQDGATQLQLAAAPSKPSKKIRKKSAQAAQPAVTVAEQVETVLIET 260
                         250       260       270
                  ....*....|....*....|....*....|
gi 150170670  562 GSGKPLQPPTvSPSAKQPPSQGLPKTICPL 591
Cdd:cd22540   261 TADNIIQAGN-NLLIVQSPGTGQPAVLQQV 289
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
947-1027 1.90e-05

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 51.43  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  947 STAGQPGPHSQSGPGAPMKQAPAPSQPPTSQGPPKSTGQAPPAPAKsipvKKETKAPAAEKLEPKAEQAPTVKRTETEKK 1026
Cdd:PRK12270   43 APTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAA----AAAAAAAPAAPPAAAAAAAPAAAAVEDEVT 118

                  .
gi 150170670 1027 P 1027
Cdd:PRK12270  119 P 119
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
461-552 3.98e-05

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 49.62  E-value: 3.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  461 AQQTGPTKPPSQlpgpakPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPA-KPSPQQPGSTKPPSQQPGSAKP 539
Cdd:NF041121   12 AAQMGRAAAPPS------PEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLpAPYPGSLAPPPPPPPGPAGAAP 85
                          90
                  ....*....|....*
gi 150170670  540 SAQQP--SPAKPSAQ 552
Cdd:NF041121   86 GAALPvrVPAPPALP 100
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
375-533 5.76e-05

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 49.42  E-value: 5.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   375 QTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPaKPPTQQVGTPKPLAQQPGLQSPAKAPGPtktPVQQPGPGKiPAQQA 454
Cdd:TIGR01628  379 QPRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNG-QPLGWPRMSMMPTPMGPGGPLRPNGLAP---MNAVRAPSR-NAQNA 453
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670   455 gpgktsaqqtgptkppsqlpgpAKPPPQQPGPAkPPPQQPGSAKPPSQQPGSTkppPQQPGPAKPSPQQPGSTkPPSQQ 533
Cdd:TIGR01628  454 ----------------------AQKPPMQPVMY-PPNYQSLPLSQDLPQPQST---ASQGGQNKKLAQVLASA-TPQMQ 505
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
32-411 7.34e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.21  E-value: 7.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   32 PSHTAIPAGMEADLSQLSEEERRQIAAVMSRAQGLPKGSVPPAAAESPSMHRKQELDSSHPPKQSGRPPDPGRPAQPGLS 111
Cdd:PRK07764  427 AAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGA 506
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  112 ksRTTDTFRSE-----QKLPGRSPSTISLKESKSR------TDLKEEHKSSMMPGFLSEVNALSAVSSVVnkfnpfdlis 180
Cdd:PRK07764  507 --DDAATLRERwpeilAAVPKRSRKTWAILLPEATvlgvrgDTLVLGFSTGGLARRFASPGNAEVLVTAL---------- 574
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  181 dseasQEETTKKQKVVQKEQGKPEGiikPPLQQQPPKPIPKQQGPGRDPLQQDGTPKSISSQQPEKikSQPPGTGKPIQG 260
Cdd:PRK07764  575 -----AEELGGDWQVEAVVGPAPGA---AGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGA--AAAPAEASAAPA 644
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  261 PTQTPQTDHAKLPLQRDASRPQTKQADIVRGESVKPSLPSPSKPPIQQPTPGKPPAQQPgheKSQPGPAKPPAQPSGLTK 340
Cdd:PRK07764  645 PGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAP---APAATPPAGQADDPAAQP 721
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150170670  341 PLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQqtgsekPSSEQPGPKALAQPPGVGKTPAQQPGPAKPP 411
Cdd:PRK07764  722 PQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAP------AQPPPPPAPAPAAAPAAAPPPSPPSEEEEMA 786
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
339-810 7.98e-05

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: 49.00  E-value: 7.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  339 TKPLAQQPGTVKP--PVQPPGTTKPPAQPLGPaKPPAQQTGSEKpssEQPGPKALAQPPGVGKTPAQQPGPAKPPTQQVG 416
Cdd:NF033839  157 TKPETPQPENPEHqkPTTPAPDTKPSPQPEGK-KPSVPDINQEK---EKAKLAVATYMSKILDDIQKHHLQKEKHRQIVA 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  417 TPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQ-QPGPAKPPPQQPG 495
Cdd:NF033839  233 LIKELDELKKQALSEIDNVNTKVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGmQPSPQPEKKEVKP 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  496 SAKPPSQQpgsTKPPPQQPGP-AKPSPQQPGSTKPPsqQPGSAKPSAQqPSPAKPSAQQSTKPVSQTGSGKPlQPPTVSP 574
Cdd:NF033839  313 EPETPKPE---VKPQLEKPKPeVKPQPEKPKPEVKP--QLETPKPEVK-PQPEKPKPEVKPQPEKPKPEVKP-QPETPKP 385
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  575 SAKQPPSQGLPkticplcnttelllhvpekanfntctecqttvcslcgfnpnphltevkewlclncqmkralggDLAPVP 654
Cdd:NF033839  386 EVKPQPEKPKP---------------------------------------------------------------EVKPQP 402
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  655 SSPQPKLKTAPVTttsavSKSSPQPQQTSPKKDAAPKQDlskapepkkppplvkqptlhgSPSAKAKQPPEAdslSKPAP 734
Cdd:NF033839  403 EKPKPEVKPQPEK-----PKPEVKPQPEKPKPEVKPQPE---------------------KPKPEVKPQPEK---PKPEV 453
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670  735 PKEPSVPSEQDKAPVADDKPK-QPKMVKPTTDLVSSSSATTKPDIPSSKVQSQAEEKTTPPLKTDSAKPSQSFPPTG 810
Cdd:NF033839  454 KPQPETPKPEVKPQPEKPKPEvKPQPEKPKPDNSKPQADDKKPSTPNNLSKDKQPSNQASTNEKATNKPKKSLPSTG 530
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
436-527 8.65e-05

trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia intracellular motility A), WP_004266405.1-like proteins in Burkholderia mallei or B. pseudomallei. The term BimA has also been used for WP_011205626.1-like homologs that have a very different N-terminal half.


Pssm-ID: 468913 [Multi-domain]  Cd Length: 382  Bit Score: 48.36  E-value: 8.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  436 PTKTPVQQPGPGKIPaqqagPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPqqpgSAKPPSQQPGSTKPPPQQPG 515
Cdd:NF040983   86 PNKVPPPPPPPPPPP-----PPPPTPPPPPPPPPPPPPPSPPPPPPPSPPPSPPPP----TTTPPTRTTPSTTTPTPSMH 156
                          90
                  ....*....|....
gi 150170670  516 PAKPS--PQQPGST 527
Cdd:NF040983  157 PIQPTqlPSIPNAT 170
PRK10263 PRK10263
DNA translocase FtsK; Provisional
3460-3965 9.36e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 49.31  E-value: 9.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3460 RRRRTKKSVDTSVQTDDEDQDEW---------DMPTRSRRKARVGKY--------GDSMTEADKTKPLSKVSSIAVQTVA 3522
Cdd:PRK10263  258 MGRQTDAALFSGKRMDDDEEITYtargvaadpDDVLFSGNRATQPEYdeydpllnGAPITEPVAVAAAATTATQSWAAPV 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3523 EISVQTEPVGTIRTPSIRARVDAKVEIIKHISAPEktykggslgCQTEADSDTQSPQYLSATSPPKDK-KRPTPLEIGYS 3601
Cdd:PRK10263  338 EPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPV---------IAPAPEGYPQQSQYAQPAVQYNEPlQQPVQPQQPYY 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3602 SHLRADSTVQLAPSPPKSPKVLYSPISPLSPGKALESAFVPYEKPLPDDisPQKVLHPDMAKVPPASPKTAKMMQRSMSD 3681
Cdd:PRK10263  409 APAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFA--PQSTYQTEQTYQQPAAQEPLYQQPQPVEQ 486
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3682 PKPLSPT--ADES--SRAPFQYTEGYTTKGSQTMTSSGA-----QKKVKRTLPN------------PPPEEIST------ 3734
Cdd:PRK10263  487 QPVVEPEpvVEETkpARPPLYYFEEVEEKRAREREQLAAwyqpiPEPVKEPEPIksslkapsvaavPPVEAAAAvsplas 566
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3735 ----GTQSTFSTMGTVSRRRICRTNTMARAKILQDIDRELDLVERESAKLRKKQAELD--------EEEKEIDAKLRYLE 3802
Cdd:PRK10263  567 gvkkATLATGAAATVAAPVFSLANSGGPRPQVKEGIGPQLPRPKRIRVPTRRELASYGiklpsqraAEEKAREAQRNQYD 646
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3803 MGINRRK---EALLKEREKRERAYLQ-------------GVAEDRDYMSDSEVSSTRPTRIESQHGIERPRTAPQTEFSQ 3866
Cdd:PRK10263  647 SGDQYNDdeiDAMQQDELARQFAQTQqqrygeqyqhdvpVNAEDADAAAEAELARQFAQTQQQRYSGEQPAGANPFSLDD 726
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3867 F-----------------IPPQTQTESQlvPPTSPYTQYQYSSPALPTQAPTSYTQ-QSHFEQQTLYHQQVSPYQTQPTF 3928
Cdd:PRK10263  727 FefspmkallddgpheplFTPIVEPVQQ--PQQPVAPQQQYQQPQQPVAPQPQYQQpQQPVAPQPQYQQPQQPVAPQPQY 804
                         570       580       590
                  ....*....|....*....|....*....|....*..
gi 150170670 3929 QavatmsftpQVQPTPTPQPSYQLPSQMMVIQQKPRQ 3965
Cdd:PRK10263  805 Q---------QPQQPVAPQPQYQQPQQPVAPQPQYQQ 832
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
716-1072 1.50e-04

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 48.23  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  716 PSAKAKQPPEADSLSKPAPPKEPSVPSEQDKAPVADDKPKQPK--------MVKPTTDLVSSSSATTKPDIPSSKVQSQA 787
Cdd:NF033839  159 PETPQPENPEHQKPTTPAPDTKPSPQPEGKKPSVPDINQEKEKaklavatyMSKILDDIQKHHLQKEKHRQIVALIKELD 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  788 EEKTTPPLKTDSAKPSQSFPPTGEKVSPfDSKAIPRPASDSKIISHPGPsseskgqkqvdPVQKKEEPKKAQTKMSPKPD 867
Cdd:NF033839  239 ELKKQALSEIDNVNTKVEIENTVHKIFA-DMDAVVTKFKKGLTQDTPKE-----------PGNKKPSAPKPGMQPSPQPE 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  868 AKPmPKGSPTPPGPRPTAGQTVPTPQQSPKPQEQSRRFSLNLGSITDAPKSQPTTPQETVTGKLFGFGASIfsqasnlis 947
Cdd:NF033839  307 KKE-VKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEV--------- 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  948 tagQPGPHSQSGPGAPMKQAPAPSQPPTsqgPPKSTGQAPPAPAKSIPVKKETKAPAAEKLEPKAEQAPTVKRTETEKKP 1027
Cdd:NF033839  377 ---KPQPETPKPEVKPQPEKPKPEVKPQ---PEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPK 450
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 150170670 1028 PPIKdsksltAEPQKAvlptKLEKSPKPESTCPLCKTELNIGSKD 1072
Cdd:NF033839  451 PEVK------PQPETP----KPEVKPQPEKPKPEVKPQPEKPKPD 485
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
660-1055 5.42e-04

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 46.30  E-value: 5.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  660 KLKTAPVTTTSAVSKSSPQPQQTSPKKDAAPKQDLSKapepkkppplvkqptlhgSPSAKAKQPPEADSLSKPAPPKePS 739
Cdd:NF033839  145 KDSSSSSSSGSSTKPETPQPENPEHQKPTTPAPDTKP------------------SPQPEGKKPSVPDINQEKEKAK-LA 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  740 VPSEQDKapVADDKPKQPKMVKPTTDLVSsssatTKPDIPSSKVQSQAEEKTTPPLKTDSAKPSQSFPPTGEKVSPFDSK 819
Cdd:NF033839  206 VATYMSK--ILDDIQKHHLQKEKHRQIVA-----LIKELDELKKQALSEIDNVNTKVEIENTVHKIFADMDAVVTKFKKG 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  820 AIPRPAS--DSKIISHPGPSSESKGQKQVDPVQKKEEPKKAQTKMSPKpdaKPMPKGSPTPPGPRPTAGQTVPTPQQSPK 897
Cdd:NF033839  279 LTQDTPKepGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLE---KPKPEVKPQPEKPKPEVKPQLETPKPEVK 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  898 PQEQSRRFSLNLGSITDAP--KSQPTTPQETVTGKLFGFGASIfsqasnlistagQPGPHSQSGPGAPMKQAPAPSQPPT 975
Cdd:NF033839  356 PQPEKPKPEVKPQPEKPKPevKPQPETPKPEVKPQPEKPKPEV------------KPQPEKPKPEVKPQPEKPKPEVKPQ 423
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  976 SQGPPKSTGQAPPAPAKSIPVKKETKAPA--AEKLEPKAEQAPTVKRTETEKKPPPIK---DSKSLTAEPQKAVLPTKLE 1050
Cdd:NF033839  424 PEKPKPEVKPQPEKPKPEVKPQPEKPKPEvkPQPETPKPEVKPQPEKPKPEVKPQPEKpkpDNSKPQADDKKPSTPNNLS 503

                  ....*
gi 150170670 1051 KSPKP 1055
Cdd:NF033839  504 KDKQP 508
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
651-1047 5.42e-04

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 46.30  E-value: 5.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  651 APVPSSPQPKLKTAPVTTTsavsKSSPQPQQTSPKK-DAAPKQDLSKAPEPKKPPPLVKQPTLHGSPSAKAKQP----PE 725
Cdd:NF033839  161 TPQPENPEHQKPTTPAPDT----KPSPQPEGKKPSVpDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIvaliKE 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  726 ADSLSKPAPPKEPSV-----PSEQDKAPVADDKPKQPKMVKPTTDLVSSSSATTKPDIPSSKVQSQAEEKTtPPLKTDSA 800
Cdd:NF033839  237 LDELKKQALSEIDNVntkveIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEK-KEVKPEPE 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  801 KPSQSFPPTGEKVSPfdsKAIPRPAsdskiishpGPSSESKGQKQVDPVQKKEEPKKAQTKMSPKPDaKPMPKGSPTPPG 880
Cdd:NF033839  316 TPKPEVKPQLEKPKP---EVKPQPE---------KPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPE-KPKPEVKPQPET 382
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  881 PRPTAGQTVPTPQQSPKPQEQSRRFSLNLGSITDAP--KSQPTTPQETVtgklfgfgasifsqasnlistagQPGPHSQS 958
Cdd:NF033839  383 PKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPevKPQPEKPKPEV-----------------------KPQPEKPK 439
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  959 GPGAPMKQAPAPSQPPTSQGPPKSTGQAPPAPAKSIPVKKETKAPAAEKLEPKAEQAPTVKRTETEKKPPPIKDSKSLTA 1038
Cdd:NF033839  440 PEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPSTPNNLSKDKQPSNQASTNEKAT 519

                  ....*....
gi 150170670 1039 EPQKAVLPT 1047
Cdd:NF033839  520 NKPKKSLPS 528
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
449-524 8.05e-04

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 45.38  E-value: 8.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670  449 IPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQP 524
Cdd:NF041121   15 MGRAAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPGAALP 90
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
1154-1558 1.18e-03

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


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 45.39  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1154 VKLVKKQeQEVKTE---AEKVILEKVKETLSMEKippmvttdQKQEESKLEKDKASALQEKKPLPEEKKLIPEEEKiRSE 1230
Cdd:NF033838   87 VALNKKL-SDIKTEylyELNVLKEKSEAELTSKT--------KKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEK-KAK 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1231 EKKPLLEEKKPTPEDKKLLPEAKTSAPEEQKHDLLKSQVQIAEEKLEGRV--APKTVQEGKQPQTKMEGLPsgTPQSLPK 1308
Cdd:NF033838  157 DQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIkqAKAKVESKKAEATRLEKIK--TDREKAE 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1309 EDDKTTKTIKEQpqppctakpDQVEPGKEKTEKEDDKSDT--SSSQQPKSPQGLSDTGYSSDgisSSLGE----IPSLIP 1382
Cdd:NF033838  235 EEAKRRADAKLK---------EAVEKNVATSEQDKPKRRAkrGVLGEPATPDKKENDAKSSD---SSVGEetlpSPSLKP 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1383 tdEKDILKGLKK-DSFSQESSPSSPSDLAKLESTVLSILEAQastLADEKSEKKTQPHEVSPE---QPKDQEKTQSLSET 1458
Cdd:NF033838  303 --EKKVAEAEKKvEEAKKKAKDQKEEDRRNYPTNTYKTLELE---IAESDVKVKEAELELVKEeakEPRNEEKIKQAKAK 377
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1459 LEitiseeeIKESQEERKDTFKKDSQQdipSSKDHKEKSEFVDDIttrrepydSVEESSESENSPVPQRKRRTSVGSSSS 1538
Cdd:NF033838  378 VE-------SKKAEATRLEKIKTDRKK---AEEEAKRKAAEEDKV--------KEKPAEQPQPAPAPQPEKPAPKPEKPA 439
                         410       420
                  ....*....|....*....|
gi 150170670 1539 DEYKQEDSQGSGEEEDFIRK 1558
Cdd:NF033838  440 EQPKAEKPADQQAEEDYARR 459
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1127-1363 1.51e-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: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1127 PAPSGPKASPMPVPTESSSQKTAVPPQVKLVKKQEQEVKTEAEKVILEKVKETlsmEKIPPMVTTDQKQEESKLEKDKAS 1206
Cdd:NF033839  284 PKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQP---EKPKPEVKPQLETPKPEVKPQPEK 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1207 ALQEKKPLPEEKK-LIPEEEKIRSEEKKPLLEEKKP--TPEDKKLLPEAKtsaPEEQKHdllKSQVQIAEEKLEGRVAPK 1283
Cdd:NF033839  361 PKPEVKPQPEKPKpEVKPQPETPKPEVKPQPEKPKPevKPQPEKPKPEVK---PQPEKP---KPEVKPQPEKPKPEVKPQ 434
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1284 TVQEGKQPQTKMEG-LPSGTPQslPKEDDKTTKTIKEQPQPPCTAKPDQVEPGKEKTEKEDDK-SDTSSSQQPKSPQGLS 1361
Cdd:NF033839  435 PEKPKPEVKPQPEKpKPEVKPQ--PETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKpSTPNNLSKDKQPSNQA 512

                  ..
gi 150170670 1362 DT 1363
Cdd:NF033839  513 ST 514
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
1134-1261 2.62e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.68  E-value: 2.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  1134 ASPMPVPTESSSQKTAVPPQVKLVKKQEQEVKTEAEKVILEKVKETLSMEKIPPMVTTDQKQEESKLEKDKASAL-QEKK 1212
Cdd:TIGR02794   25 HSVKPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAaEKAA 104
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 150170670  1213 PLPEEKKLIPEEEKIRSEEKKP-LLEEKKPTPE---DKKLLPEAKTSAPEEQK 1261
Cdd:TIGR02794  105 KQAEQAAKQAEEKQKQAEEAKAkQAAEAKAKAEaeaERKAKEEAAKQAEEEAK 157
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
3758-3821 3.97e-03

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


Pssm-ID: 462322  Cd Length: 323  Bit Score: 42.94  E-value: 3.97e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670  3758 ARAKILQDIDRELDLVERESAKLRKKQAELDEEEKEIDaklrylEMGINRRKEALLKEREKRER 3821
Cdd:pfam07946  265 TREEEIEKIKKAAEEERAEEAQEKKEEAKKKEREEKLA------KLSPEEQRKYEEKERKKEQR 322
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1142-1309 4.37e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 43.10  E-value: 4.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1142 ESSSQKTAVPPQVKLVKKQEQEVKTEAEkvILEKVKETLSMEKIPPMVTT--------------DQKQEESKLEKDKASA 1207
Cdd:COG3064     3 EALEEKAAEAAAQERLEQAEAEKRAAAE--AEQKAKEEAEEERLAELEAKrqaeeeareakaeaEQRAAELAAEAAKKLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1208 LQEKKPLPEEKKLIPEEEKIRSEEKKPLLEEKKPTPEDKKLLPEAKTSAPEEQKHDLLKSQVQIAEEKLEGRVAPKTVQE 1287
Cdd:COG3064    81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAA 160
                         170       180
                  ....*....|....*....|..
gi 150170670 1288 GKQPQTKMEGLPSGTPQSLPKE 1309
Cdd:COG3064   161 AAAAAAAAAAAARAAAGAAAAL 182
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
382-500 7.26e-03

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


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 40.54  E-value: 7.26e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670    382 SSEQPGPKALAQPPGVGKTPAQQPGpakPPTQqvgtpkPLAQQPGLQSpakapgptKTPVQQPGPGKIPAQQAGPGKTSA 461
Cdd:smart00818   43 SQQHPPTHTLQPHHHIPVLPAQQPV---VPQQ------PLMPVPGQHS--------MTPTQHHQPNLPQPAQQPFQPQPL 105
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 150170670    462 QQTGPTKPPSQLPGPAKPPPQQPGPAKPP--PQQPGSAKPP 500
Cdd:smart00818  106 QPPQPQQPMQPQPPVHPIPPLPPQPPLPPmfPMQPLPPLLP 146
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
835-1065 8.76e-03

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.45  E-value: 8.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  835 GPSSESKGQKQVDPVQKKEEPKKAQTKMSPKPDAKPMPKGSPTPPgPRPTAGQTVPTPQ--------------QSPKPQE 900
Cdd:NF033839  146 DSSSSSSSGSSTKPETPQPENPEHQKPTTPAPDTKPSPQPEGKKP-SVPDINQEKEKAKlavatymskilddiQKHHLQK 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  901 QSRRFSLNLGSITDAPKSQPTTPQETV---------TGKLFGFGASIFSQASNLIS--TAGQPGPHSQSGPGAPMKQAPA 969
Cdd:NF033839  225 EKHRQIVALIKELDELKKQALSEIDNVntkveientVHKIFADMDAVVTKFKKGLTqdTPKEPGNKKPSAPKPGMQPSPQ 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  970 PSQPPTSQGPPKSTGQAPPAPAKSIPVKK---ETKAPA--AEKLEPKAEQAPTVKRTETEKKPPPIKDSKSLTAEPQKAv 1044
Cdd:NF033839  305 PEKKEVKPEPETPKPEVKPQLEKPKPEVKpqpEKPKPEvkPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETP- 383
                         250       260
                  ....*....|....*....|.
gi 150170670 1045 lptKLEKSPKPESTCPLCKTE 1065
Cdd:NF033839  384 ---KPEVKPQPEKPKPEVKPQ 401
 
Name Accession Description Interval E-value
C2A_RIM1alpha cd04031
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
4694-4826 1.72e-63

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: 212.88  E-value: 1.72e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4694 ITGEIQLQINYD--LGNLIIHILQARNLVPRDNNGYSDPFVKVYLLPGRgqvmvvqnaSAEYKRRTKHVQKSLNPEWNQT 4771
Cdd:cd04031     1 ITGRIQIQLWYDkvTSQLIVTVLQARDLPPRDDGSLRNPYVKVYLLPDR---------SEKSKRRTKTVKKTLNPEWNQT 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 150170670 4772 VIYKSISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLsSTSHLDNTPRWYPLK 4826
Cdd:cd04031    72 FEYSNVRRETLKERTLEVTVWDYDRDGENDFLGEVVIDL-ADALLDDEPHWYPLQ 125
PDZ_RIM-like cd06714
PDZ domain of Rab3-interacting molecule 1 (RIM), RIM2, piccolo and related domains; PDZ ...
4492-4587 4.09e-49

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: 170.81  E-value: 4.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4492 FPHARIKITRDSKDHTVSGNGLGIRIVGGKEIPghSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEV 4571
Cdd:cd06714     2 FLIGRIILQRDPKDGSVSGNGLGLKVVGGKMTE--SGRLGAYVTKVKPGSVADTVGHLREGDEVLEWNGISLQGKTFEEV 79
                          90
                  ....*....|....*.
gi 150170670 4572 QSIISQQSGEAEICVR 4587
Cdd:cd06714    80 QDIISQSKGEVELVVS 95
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
587-648 1.73e-42

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


Pssm-ID: 277313 [Multi-domain]  Cd Length: 62  Bit Score: 150.57  E-value: 1.73e-42
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150170670  587 TICPLCNTTELLLHVPEKANFNTCTECQTTVCSLCGFNPNPHLTEVKEWLCLNCQMKRALGG 648
Cdd:cd15774     1 TICPLCKTTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
1057-1120 5.89e-42

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


Pssm-ID: 277315 [Multi-domain]  Cd Length: 64  Bit Score: 149.06  E-value: 5.89e-42
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670 1057 STCPLCKTELNIGSKDPPNFNTCTECKNQVCNLCGFNPTPHLTEIQEWLCLNCQTQRAISGQLG 1120
Cdd:cd15776     1 LLCPLCKTELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQLG 64
FYVE2_BSN_PCLO cd15772
FYVE-related domain 2 found in protein bassoon and piccolo; This family includes protein ...
1057-1120 2.04e-41

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: 147.48  E-value: 2.04e-41
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670 1057 STCPLCKTELNIGSKDPPNFNTCTECKNQVCNLCGFNPTPHLTEIQEWLCLNCQTQRAISGQLG 1120
Cdd:cd15772     1 VTCPLCKTELNVGSKEPPNYNTCTQCHTQVCNLCGFNPTPHLVEKKEWLCLNCQTQRLMSGGLG 64
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
1057-1115 1.66e-39

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: 142.17  E-value: 1.66e-39
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  1057 STCPLCK-TELNIGSKDPPNFNTCTECKNQVCNLCGFNPTPHLTEIQEWLCLNCQTQRAI 1115
Cdd:pfam05715    1 TLCPLCKtTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
FYVE1_BSN_PCLO cd15771
FYVE-related domain 1 found in protein bassoon and piccolo; This family includes protein ...
587-648 1.30e-38

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: 139.37  E-value: 1.30e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150170670  587 TICPLCNTTELLLHVPeKANFNTCTECQTTVCSLCGFNPNPHLTEVKEWLCLNCQMKRALGG 648
Cdd:cd15771     1 TLCPLCNTTELTLHVP-KPNFNTCTQCHTTVCNQCGFNPNPHLTEVKEWLCLNCQMQRALGM 61
zf-piccolo pfam05715
Piccolo Zn-finger; This (predicted) Zinc finger is found in the bassoon and piccolo proteins. ...
587-646 3.00e-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: 135.62  E-value: 3.00e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   587 TICPLCNTTELLLHVPEKANFNTCTECQTTVCSLCGFNPNPHLTEVKEWLCLNCQMKRAL 646
Cdd:pfam05715    1 TLCPLCKTTELNVGSKEPPNYNTCTECKSQVCNLCGFNPTPHLTEKKEWLCLNCQTQRAL 60
FYVE2_BSN cd15775
FYVE-related domain 2 found in protein bassoon; Protein bassoon, also termed zinc finger ...
1056-1120 6.63e-36

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: 131.96  E-value: 6.63e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150170670 1056 ESTCPLCKTELNIGSKDPPNFNTCTECKNQVCNLCGFNPTPHLTEIQEWLCLNCQTQRAISGQLG 1120
Cdd:cd15775     1 RVTCPLCKTELNVGSTEPPNYNTCTSCRTQVCNLCGFNPTPHLVEKNEWLCLNCQTQRLLEGSLG 65
C2 pfam00168
C2 domain;
4707-4825 4.82e-32

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 122.43  E-value: 4.82e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  4707 GNLIIHILQARNLVPRDNNGYSDPFVKVYLLPGrgqvmvvqnasaEYKRRTKHVQKSLNPEWNQTVIYkSISMEQlkKKT 4786
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNGTSDPYVKVYLLDG------------KQKKKTKVVKNTLNPVWNETFTF-SVPDPE--NAV 65
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 150170670  4787 LEVTVWDYDRFSSNDFLGEVLIDLSSTSHLDNTPRWYPL 4825
Cdd:pfam00168   66 LEIEVYDYDRFGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2A_SLP cd08521
C2 domain first repeat present in Synaptotagmin-like proteins; All Slp members basically share ...
4696-4825 2.93e-31

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: 120.82  E-value: 2.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4696 GEIQLQINYDL--GNLIIHILQARNLVPRDN-NGYSDPFVKVYLLPGRgqvmvvqnaSAEYKRRTKHVQKSLNPEWNQTV 4772
Cdd:cd08521     1 GEIEFSLSYNYktGSLEVHIKECRNLAYADEkKKRSNPYVKVYLLPDK---------SKQSKRKTSVKKNTTNPVFNETL 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 150170670 4773 IYKsISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSTShLDNT-PRWYPL 4825
Cdd:cd08521    72 KYH-ISKSQLETRTLQLSVWHHDRFGRNTFLGEVEIPLDSWD-LDSQqSEWYPL 123
FYVE1_BSN cd15773
FYVE-related domain 1 found in protein bassoon; Protein bassoon, also termed zinc finger ...
587-647 1.43e-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: 116.72  E-value: 1.43e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150170670  587 TICPLCNTTELLlHVPEKANFNTCTECQTTVCSLCGFNPNPHLTEVKEWLCLNCQMKRALG 647
Cdd:cd15773     4 TLCPICNTTELT-SFPSQPNFNTCTQCHNKVCNQCGFNPNPHLTEVKEWLCLNCQMQRALG 63
C2_PKC_alpha_gamma cd04026
C2 domain in Protein Kinase C (PKC) alpha and gamma; A single C2 domain is found in PKC alpha ...
4696-4804 3.36e-29

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: 115.05  E-value: 3.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4696 GEIQLQINYDLGNLIIHILQARNLVPRDNNGYSDPFVKVYLLPgrgqvmvvqNASAEYKRRTKHVQKSLNPEWNQTVIYK 4775
Cdd:cd04026     2 GRIYLKISVKDNKLTVEVREAKNLIPMDPNGLSDPYVKLKLIP---------DPKNETKQKTKTIKKTLNPVWNETFTFD 72
                          90       100
                  ....*....|....*....|....*....
gi 150170670 4776 sISMEQlKKKTLEVTVWDYDRFSSNDFLG 4804
Cdd:cd04026    73 -LKPAD-KDRRLSIEVWDWDRTTRNDFMG 99
FYVE_BSN_PCLO cd15751
FYVE-related domain found in protein bassoon and piccolo; This family includes protein bassoon ...
1057-1114 1.26e-28

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: 111.00  E-value: 1.26e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670 1057 STCPLCK-TELNIGSKDPPNFNTCTECKNQVCNLCGFNPTPHLTEIQEWLCLNCQTQRA 1114
Cdd:cd15751     1 SACPLCGtSELPLGSKSPPNYNTCTDCKNRVCNQCGFNSTPPVTKVKEWLCLNCQKKRA 59
C2B_SLP_1-2-3-4 cd04020
C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically ...
4686-4812 1.84e-28

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: 114.34  E-value: 1.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4686 GTKVVSHPITGEIQlqinydlgnliIHILQARNLVPRDNNGYSDPFVKVYLLPGRgqvmvvqnaSAEYKRRTKHVQKSLN 4765
Cdd:cd04020    17 GALKSKKPSTGELH-----------VWVKEAKNLPALKSGGTSDSFVKCYLLPDK---------SKKSKQKTPVVKKSVN 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 150170670 4766 PEWNQTVIYKSISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSS 4812
Cdd:cd04020    77 PVWNHTFVYDGVSPEDLSQACLELTVWDHDKLSSNDFLGGVRLGLGT 123
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
4709-4825 2.17e-28

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: 111.78  E-value: 2.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4709 LIIHILQARNLVPRDNNGYSDPFVKVYLLPGRgqvmvvqnasaeyKRRTKHVQKSLNPEWNQTVIyksISMEQLKKKTLE 4788
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQ-------------KFKTKVVKNTLNPVWNETFE---FPVLDPESDTLT 64
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150170670 4789 VTVWDYDRFSSNDFLGEVLIDLSS-TSHLDNTPRWYPL 4825
Cdd:cd00030    65 VEVWDKDRFSKDDFLGEVEIPLSElLDSGKEGELWLPL 102
C2B_PI3K_class_II cd08381
C2 domain second repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are ...
4695-4826 4.90e-28

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: 111.62  E-value: 4.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4695 TGEIQLQINYDLGNLIIHILQARNLVPRDNNgYSDPFVKVYLLPgrgqvmvvqNASAEYKRRTKHVQKSLNPEWNQTVIY 4774
Cdd:cd08381     1 GGQVKLSISYKNGTLFVMVMHAKNLPLLDGS-DPDPYVKTYLLP---------DPQKTTKRKTKVVRKTRNPTFNEMLVY 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 150170670 4775 KSISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSTSHLDNTPRWYPLK 4826
Cdd:cd08381    71 DGLPVEDLQQRVLQVSVWSHDSLVENEFLGGVCIPLKKLDLSQETEKWYPLG 122
C2A_SLP-1_2 cd08393
C2 domain first repeat present in Synaptotagmin-like proteins 1 and 2; All Slp members ...
4696-4826 1.36e-27

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: 110.60  E-value: 1.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4696 GEIQLQINYD--LGNLIIHILQARNLVPRD-NNGYSDPFVKVYLLPGRgqvmvvqnaSAEYKRRTKHVQKSLNPEWNQTV 4772
Cdd:cd08393     2 GSVQFALDYDpkLRELHVHVIQCQDLAAADpKKQRSDPYVKTYLLPDK---------SNRGKRKTSVKKKTLNPVFNETL 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 150170670 4773 IYKsISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSTSHLDNTPRWYPLK 4826
Cdd:cd08393    73 RYK-VEREELPTRVLNLSVWHRDSLGRNSFLGEVEVDLGSWDWSNTQPTWYPLQ 125
FYVE1_PCLO cd15774
FYVE-related domain 1 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
1059-1117 1.39e-27

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: 108.19  E-value: 1.39e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1059 CPLCK-TELNIGSKDPPNFNTCTECKNQVCNLCGFNPTPHLTEIQEWLCLNCQTQRAISG 1117
Cdd:cd15774     3 CPLCKtTELLLHTPEKANYNTCTQCQTTVCSLCGFNPNPHITEKKEWLCLNCQMQRALGG 62
C2B_Rabphilin_Doc2 cd08384
C2 domain second repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
4697-4812 1.55e-27

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: 110.52  E-value: 1.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4697 EIQLQINYDLGNLIIHILQARNLVPRDNNGYSDPFVKVYLLPgrgqvmvvqNASAEYKRRTKHVQKSLNPEWNQTVIYKs 4776
Cdd:cd08384     3 LVSLMYNTQRRGLIVGIIRCVNLAAMDANGYSDPFVKLYLKP---------DAGKKSKHKTQVKKKTLNPEFNEEFFYD- 72
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 150170670 4777 ISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSS 4812
Cdd:cd08384    73 IKHSDLAKKTLEITVWDKDIGKSNDYIGGLQLGINA 108
FYVE1_BSN_PCLO cd15771
FYVE-related domain 1 found in protein bassoon and piccolo; This family includes protein ...
1059-1117 2.03e-27

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: 107.78  E-value: 2.03e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670 1059 CPLCKTELNIGSKDPPNFNTCTECKNQVCNLCGFNPTPHLTEIQEWLCLNCQTQRAISG 1117
Cdd:cd15771     3 CPLCNTTELTLHVPKPNFNTCTQCHTTVCNQCGFNPNPHLTEVKEWLCLNCQMQRALGM 61
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
4709-4822 3.27e-27

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: 108.34  E-value: 3.27e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   4709 LIIHILQARNLVPRDNNGYSDPFVKVYLLPGRGQvmvvqnasaeyKRRTKHVQKSLNPEWNQTVIYKSISMEqlkKKTLE 4788
Cdd:smart00239    2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKE-----------KKKTKVVKNTLNPVWNETFEFEVPPPE---LAELE 67
                            90       100       110
                    ....*....|....*....|....*....|....
gi 150170670   4789 VTVWDYDRFSSNDFLGEVLIDLSSTSHLDNTPRW 4822
Cdd:smart00239   68 IEVYDKDRFGRDDFIGQVTIPLSDLLLGGRHEKL 101
PHA03247 PHA03247
large tegument protein UL36; Provisional
308-905 6.88e-27

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 122.35  E-value: 6.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  308 QPTPgKPPAQQPGHEKSQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEK-PSSEQP 386
Cdd:PHA03247 2572 RPAP-RPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPpTVPPPE 2650
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  387 GPKALAQPPGV-----GKTPAQQPGPAKPPTQqvgtPKPLAQQPG---LQSPAKAPGPTKTPVQQPGPgKIPAQQAGPGK 458
Cdd:PHA03247 2651 RPRDDPAPGRVsrprrARRLGRAAQASSPPQR----PRRRAARPTvgsLTSLADPPPPPPTPEPAPHA-LVSATPLPPGP 2725
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  459 TSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSqqPGSTKPPPQQPGPAKPSPqqPGSTKPPSQqPGSAK 538
Cdd:PHA03247 2726 AAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPA--PAPPAAPAAGPPRRLTRP--AVASLSESR-ESLPS 2800
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  539 PSAQQPSPAKPSAQQSTKPVSQTGSGkPLQPPTVSPSAKQPPSQGLPKTICPLCNTTelllhvpekanfntctecqttvc 618
Cdd:PHA03247 2801 PWDPADPPAAVLAPAAALPPAASPAG-PLPPPTSAQPTAPPPPPGPPPPSLPLGGSV----------------------- 2856
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  619 slcgfnpnphltevkewlclncqmkrALGGDLAPVPSSPQPKLKTAPVTTTSAVSKSSPQPQQtSPKKDAAPKQDLSKAP 698
Cdd:PHA03247 2857 --------------------------APGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSR-STESFALPPDQPERPP 2909
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  699 EPKKPPPlvkqptlhgsPSAKAKQPPEADSLSKPAPPKEPSVPSEQDKAPVADDKPKQPKMVKPTTDLVSSSSATTKPDI 778
Cdd:PHA03247 2910 QPQAPPP----------PQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRV 2979
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  779 PSSKVQSQAEEKTTPPLKTDSAKPSQSFPPTgekvSPFDSKAIPRPASDSKIISHPGPSSESKGQKQVDpvqkkEEPKKA 858
Cdd:PHA03247 2980 PQPAPSREAPASSTPPLTGHSLSRVSSWASS----LALHEETDPPPVSLKQTLWPPDDTEDSDADSLFD-----SDSERS 3050
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|..
gi 150170670  859 QTK-MSPKPDAKPMPKGSPTPPGPRPTAGQTVPTPQQSPKPQEQ----SRRF 905
Cdd:PHA03247 3051 DLEaLDPLPPEPHDPFAHEPDPATPEAGARESPSSQFGPPPLSAnaalSRRY 3102
FYVE1_BSN cd15773
FYVE-related domain 1 found in protein bassoon; Protein bassoon, also termed zinc finger ...
1055-1115 1.11e-26

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: 105.55  E-value: 1.11e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150170670 1055 PEST-CPLCKTELNIGSKDPPNFNTCTECKNQVCNLCGFNPTPHLTEIQEWLCLNCQTQRAI 1115
Cdd:cd15773     1 PSSTlCPICNTTELTSFPSQPNFNTCTQCHNKVCNQCGFNPNPHLTEVKEWLCLNCQMQRAL 62
C2A_Synaptotagmin-7 cd08386
C2A domain first repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
4696-4826 1.93e-26

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: 107.03  E-value: 1.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4696 GEIQLQINYDLGN--LIIHILQARNLVPRDNNGYSDPFVKVYLLPGRGQvmvvqnasaeyKRRTKHVQKSLNPEWNQTVI 4773
Cdd:cd08386     3 GRIQFSVSYDFQEstLTLKILKAVELPAKDFSGTSDPFVKIYLLPDKKH-----------KLETKVKRKNLNPHWNETFL 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 150170670 4774 YKSISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSTSHLDNTPRWYPLK 4826
Cdd:cd08386    72 FEGFPYEKLQQRVLYLQVLDYDRFSRNDPIGEVSLPLNKVDLTEEQTFWKDLK 124
C2A_Rabphilin_Doc2 cd04035
C2 domain first repeat present in Rabphilin and Double C2 domain; Rabphilin is found neurons ...
4696-4811 2.26e-26

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: 106.98  E-value: 2.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4696 GEIQLQINYDLGNLIIH--ILQARNLVPRDNNGYSDPFVKVYLLPGrgqvmvvqnASAEYKRRTKHVQKSLNPEWNQTVI 4773
Cdd:cd04035     2 GTLEFTLLYDPANSALHctIIRAKGLKAMDANGLSDPYVKLNLLPG---------ASKATKLRTKTVHKTRNPEFNETLT 72
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150170670 4774 YKSISMEQLKKKTLEVTVWDYDRFsSNDFLGEVLIDLS 4811
Cdd:cd04035    73 YYGITEEDIQRKTLRLLVLDEDRF-GNDFLGETRIPLK 109
FYVE_BSN_PCLO cd15751
FYVE-related domain found in protein bassoon and piccolo; This family includes protein bassoon ...
587-647 5.83e-26

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: 103.30  E-value: 5.83e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150170670  587 TICPLCNTTELLLHVPEKANFNTCTECQTTVCSLCGFNPNPHLTEVKEWLCLNCQMKRALG 647
Cdd:cd15751     1 SACPLCGTSELPLGSKSPPNYNTCTDCKNRVCNQCGFNSTPPVTKVKEWLCLNCQKKRALG 61
C2A_Synaptotagmin-1-5-6-9-10 cd08385
C2A domain first repeat present in Synaptotagmins 1, 5, 6, 9, and 10; Synaptotagmin is a ...
4696-4822 7.70e-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: 7.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4696 GEIQLQINYDL--GNLIIHILQARNLVPRDNNGYSDPFVKVYLLPGRGQvmvvqnasaeyKRRTKHVQKSLNPEWNQTVI 4773
Cdd:cd08385     3 GKLQFSLDYDFqsNQLTVGIIQAADLPAMDMGGTSDPYVKVYLLPDKKK-----------KFETKVHRKTLNPVFNETFT 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 150170670 4774 YKsISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSTSHLDNTPRW 4822
Cdd:cd08385    72 FK-VPYSELGNKTLVFSVYDFDRFSKHDLIGEVRVPLLTVDLGHVTEEW 119
PHA03247 PHA03247
large tegument protein UL36; Provisional
224-585 8.02e-26

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 118.89  E-value: 8.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  224 GPGRDPLQQDGTPKSISSQQPEKIKSQPPGTGKPIQGPTQTPqtdhaklPLQRDASRPQTKQADIVRGESVKPSLPSPSK 303
Cdd:PHA03247 2606 GDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVP-------PPERPRDDPAPGRVSRPRRARRLGRAAQASS 2678
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  304 PPIQQPTPGKPPAQQPGHEKSQPGPAKPPAQPsgltKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAkPPAQQTGSEKPSs 383
Cdd:PHA03247 2679 PPQRPRRRAARPTVGSLTSLADPPPPPPTPEP----APHALVSATPLPPGPAAARQASPALPAAPA-PPAVPAGPATPG- 2752
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  384 eqpGPKALAQPPgvgkTPAQQPGPAkPPTQQVGTPKPLAQQPGLQSPAKA---------PGPTKTPVQQPGPGKIPAQQA 454
Cdd:PHA03247 2753 ---GPARPARPP----TTAGPPAPA-PPAAPAAGPPRRLTRPAVASLSESreslpspwdPADPPAAVLAPAAALPPAASP 2824
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  455 GPG---KTSAQQTGPTKPPSQLP------------------GPAKPPPQQPG------------PAKPPPQQPGSAKPPS 501
Cdd:PHA03247 2825 AGPlppPTSAQPTAPPPPPGPPPpslplggsvapggdvrrrPPSRSPAAKPAaparppvrrlarPAVSRSTESFALPPDQ 2904
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  502 QQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQP-P 580
Cdd:PHA03247 2905 PERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPaP 2984

                  ....*
gi 150170670  581 SQGLP 585
Cdd:PHA03247 2985 SREAP 2989
C2C_KIAA1228 cd04030
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ...
4695-4826 9.43e-26

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: 105.05  E-value: 9.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4695 TGEIQLQINYDLGN--LIIHILQARNLVPRDNNGYSDPFVKVYLLPGRgqvmvvqnaSAEYKRRTKHVQKSLNPEWNQTV 4772
Cdd:cd04030     2 LGRIQLTIRYSSQRqkLIVTVHKCRNLPPCDSSDIPDPYVRLYLLPDK---------SKSTRRKTSVKKDNLNPVFDETF 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670 4773 IYkSISMEQLKKKTLEVTVWDYDRFSS--NDFLGEVLIDLsstSHLDNTPR---WYPLK 4826
Cdd:cd04030    73 EF-PVSLEELKRRTLDVAVKNSKSFLSreKKLLGQVLIDL---SDLDLSKGftqWYDLT 127
FYVE2_BSN_PCLO cd15772
FYVE-related domain 2 found in protein bassoon and piccolo; This family includes protein ...
587-650 1.72e-25

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


Pssm-ID: 277311 [Multi-domain]  Cd Length: 64  Bit Score: 102.03  E-value: 1.72e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670  587 TICPLCNTtELLLHVPEKANFNTCTECQTTVCSLCGFNPNPHLTEVKEWLCLNCQMKRALGGDL 650
Cdd:cd15772     1 VTCPLCKT-ELNVGSKEPPNYNTCTQCHTQVCNLCGFNPTPHLVEKKEWLCLNCQTQRLMSGGL 63
FYVE2_BSN cd15775
FYVE-related domain 2 found in protein bassoon; Protein bassoon, also termed zinc finger ...
586-651 1.16e-24

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: 99.99  E-value: 1.16e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670  586 KTICPLCNTtELLLHVPEKANFNTCTECQTTVCSLCGFNPNPHLTEVKEWLCLNCQMKRALGGDLA 651
Cdd:cd15775     1 RVTCPLCKT-ELNVGSTEPPNYNTCTSCRTQVCNLCGFNPTPHLVEKNEWLCLNCQTQRLLEGSLG 65
PHA03247 PHA03247
large tegument protein UL36; Provisional
225-585 1.21e-24

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 115.04  E-value: 1.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  225 PGRDPLQQDGTPKSISSQQPEKIKSQPPGTGKPIQGPTQtpqtdhaklPLQRDASRPQTKQADivrgeSVKPSLPSPSKP 304
Cdd:PHA03247 2647 PPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRR---------RAARPTVGSLTSLAD-----PPPPPPTPEPAP 2712
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  305 PIQQPTPGKPPAQQPGHEKSQPGPAKP--PAQPSGltkplAQQPGTVKPPVQPPGTTKP--PAQPLGPAKPPAQQTGSEK 380
Cdd:PHA03247 2713 HALVSATPLPPGPAAARQASPALPAAPapPAVPAG-----PATPGGPARPARPPTTAGPpaPAPPAAPAAGPPRRLTRPA 2787
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  381 PSSEQPGPKALAQPPGVGKTPAQQPGP--AKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPG---PGKIPAQQAG 455
Cdd:PHA03247 2788 VASLSESRESLPSPWDPADPPAAVLAPaaALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGsvaPGGDVRRRPP 2867
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  456 PGKTSAQQTGPTKPPSQ-------------LPGPAKPPPQQPGPAKPPPQQPgsaKPPSQQPGSTKPPPQQPGPAKPSPQ 522
Cdd:PHA03247 2868 SRSPAAKPAAPARPPVRrlarpavsrstesFALPPDQPERPPQPQAPPPPQP---QPQPPPPPQPQPPPPPPPRPQPPLA 2944
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150170670  523 qpgstkPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPlQPPTVSPSAKQPPSQGLP 585
Cdd:PHA03247 2945 ------PTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQP-APSREAPASSTPPLTGHS 3000
FYVE2_PCLO cd15776
FYVE-related domain 2 found in protein piccolo; Protein piccolo, also termed aczonin, is a ...
589-650 2.69e-24

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: 98.99  E-value: 2.69e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150170670  589 CPLCNTtELLLHVPEKANFNTCTECQTTVCSLCGFNPNPHLTEVKEWLCLNCQMKRALGGDL 650
Cdd:cd15776     3 CPLCKT-ELNIGSKDPPNFNTCTECKKTVCNLCGFNPTPHLTEVKEWLCLNCQTQRAMSGQL 63
PHA03247 PHA03247
large tegument protein UL36; Provisional
311-1037 2.78e-24

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 113.88  E-value: 2.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  311 PGKPPAQQPGHEKSqPGPAKPPAQPSGLTKPLAQQPgtvkPPVQPPGTTKPPAQPLGPAKPPAQQT---GSEKPSSEQPG 387
Cdd:PHA03247 2475 PGAPVYRRPAEARF-PFAAGAAPDPGGGGPPDPDAP----PAPSRLAPAILPDEPVGEPVHPRMLTwirGLEELASDDAG 2549
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  388 PKAlaqPPGVGKTPAQQPGPAKPPTQqvgtPKPLAQQPGLQSPAKAPGptktpvqqpgpgkIPAQQAGPgktsaqqTGPT 467
Cdd:PHA03247 2550 DPP---PPLPPAAPPAAPDRSVPPPR----PAPRPSEPAVTSRARRPD-------------APPQSARP-------RAPV 2602
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  468 KPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPG---STKPPPQQPGPAkPSPQQPGSTKPPSQQPGSAKPSAQQP 544
Cdd:PHA03247 2603 DDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPhppPTVPPPERPRDD-PAPGRVSRPRRARRLGRAAQASSPPQ 2681
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  545 SPAKPSAQQSTKPVsqTGSGKPLQPPTVSPSAKQPPSQGLPKTICPLCNTTELLLHVPEKANFNTCTECQTTVcslcgfN 624
Cdd:PHA03247 2682 RPRRRAARPTVGSL--TSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPG------G 2753
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  625 PNPHLTevkewlclncqmKRALGGDLAPVP-----SSPQPKLKTAPVTTTSAVSKSSPQPQQTSPKKDAAPkqdlskape 699
Cdd:PHA03247 2754 PARPAR------------PPTTAGPPAPAPpaapaAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVL--------- 2812
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  700 pkkppPLVKQPTLHGSPSAKAKQPPEADSLSkPAPPKEPSVPSEQDKAPVAddkpkqpkmvkPTTDLVSSSSATTKPDIP 779
Cdd:PHA03247 2813 -----APAAALPPAASPAGPLPPPTSAQPTA-PPPPPGPPPPSLPLGGSVA-----------PGGDVRRRPPSRSPAAKP 2875
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  780 SSKVQSQAEEKTTPPLktdsAKPSQSFPptgekvSPFDSKAIPRPASdskiishPGPSSESKGQKQVDPVQKKEEPKKAQ 859
Cdd:PHA03247 2876 AAPARPPVRRLARPAV----SRSTESFA------LPPDQPERPPQPQ-------APPPPQPQPQPPPPPQPQPPPPPPPR 2938
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  860 TKMSPKPDAKPMPKGSPTPPGPRPTAGQTVPTPQQSPKPQEQSRRFSLnlgsitDAPKSQPTTPQEtvtgklfgfgasif 939
Cdd:PHA03247 2939 PQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSR------EAPASSTPPLTG-------------- 2998
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  940 SQASNLISTAGQPGPHSQSGPG-APMKQAPAPSQPPTSQGPPKSTGQAPPAPAKSI--PVKKETKAPAAEKLEPKAEQAP 1016
Cdd:PHA03247 2999 HSLSRVSSWASSLALHEETDPPpVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEAldPLPPEPHDPFAHEPDPATPEAG 3078
                         730       740
                  ....*....|....*....|.
gi 150170670 1017 TVKRTETEKKPPPIKDSKSLT 1037
Cdd:PHA03247 3079 ARESPSSQFGPPPLSANAALS 3099
PHA03378 PHA03378
EBNA-3B; Provisional
313-553 7.09e-24

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 111.70  E-value: 7.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  313 KPPAQQPGHEKSQPGPAKPPAQPSGLTKPLAQQPGTVKP-------PVQPPGTTkpPAQPLGPAKPPAQQTGSEKPSSEQ 385
Cdd:PHA03378  552 EPASTEPVHDQLLPAPGLGPLQIQPLTSPTTSQLASSAPsyaqtpwPVPHPSQT--PEPPTTQSHIPETSAPRQWPMPLR 629
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  386 PGPKALA----------------QPPGVGKTPAQ----QPG--PAKPPTQQVGTPKPLAQQPG-LQSPAKAPGPTKTPVQ 442
Cdd:PHA03378  630 PIPMRPLrmqpitfnvlvfptphQPPQVEITPYKptwtQIGhiPYQPSPTGANTMLPIQWAPGtMQPPPRAPTPMRPPAA 709
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  443 QPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGstKPPPQQPGPAKPSPQ 522
Cdd:PHA03378  710 PPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPG--APTPQPPPQAPPAPQ 787
                         250       260       270
                  ....*....|....*....|....*....|.
gi 150170670  523 QPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQ 553
Cdd:PHA03378  788 QRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQ 818
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
4696-4825 4.28e-23

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: 98.04  E-value: 4.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4696 GEIQLQINY--DLGNLIIHILQARNLVPRDNNGYSDPFVKVYLLPGRGQVmvvqnasaeYKRRTKHVQKSLNPEWNQTVI 4773
Cdd:cd00276     1 GELLLSLSYlpTAERLTVVVLKARNLPPSDGKGLSDPYVKVSLLQGGKKL---------KKKKTSVKKGTLNPVFNEAFS 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150170670 4774 YKsISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSTSH--------LDNtPR-----WYPL 4825
Cdd:cd00276    72 FD-VPAEQLEEVSLVITVVDKDSVGRNEVIGQVVLGPDSGGEelehwnemLAS-PRkpiarWHKL 134
C2A_SLP-4_5 cd04029
C2 domain first repeat present in Synaptotagmin-like proteins 4 and 5; All Slp members ...
4695-4825 4.64e-23

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: 97.51  E-value: 4.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4695 TGEIQLQINYD--LGNLIIHILQARNLVPRDNNGY-SDPFVKVYLLPGRgqvmvvqnaSAEYKRRTKHVQKSLNPEWNQT 4771
Cdd:cd04029     1 SGEILFSLSYDykTQSLNVHVKECRNLAYGDEAKKrSNPYVKTYLLPDK---------SRQSKRKTSIKRNTTNPVYNET 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 150170670 4772 VIYkSISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSTSHLDNTPRWYPL 4825
Cdd:cd04029    72 LKY-SISHSQLETRTLQLSVWHYDRFGRNTFLGEVEIPLDSWNFDSQHEECLPL 124
PHA03247 PHA03247
large tegument protein UL36; Provisional
233-747 4.10e-22

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 106.56  E-value: 4.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  233 DGTPKSISSQQPEKIKSQPPGTGKPIQGPTQTPqtdhaklPLQRDASRPQTKQADIVRGESVKPSLPSPSKppiQQPTPG 312
Cdd:PHA03247 2590 DAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTH-------APDPPPPSPSPAANEPDPHPPPTVPPPERPR---DDPAPG 2659
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  313 KppAQQPGHEKSQPGPAKPPAQPSGLTKPLAQQP-GTVKPPVQPPgttkPPAQPLGPAkPPAQQTGSEKPSSEQPGPKAL 391
Cdd:PHA03247 2660 R--VSRPRRARRLGRAAQASSPPQRPRRRAARPTvGSLTSLADPP----PPPPTPEPA-PHALVSATPLPPGPAAARQAS 2732
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  392 AQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPgPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPS 471
Cdd:PHA03247 2733 PALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAP-AAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAV 2811
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  472 QLPGPAKPPPQQPGPAKPPPQQPGSAKPPsqqPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPgSAKPSAQQPSP----A 547
Cdd:PHA03247 2812 LAPAAALPPAASPAGPLPPPTSAQPTAPP---PPPGPPPPSLPLGGSVAPGGDVRRRPPSRSP-AAKPAAPARPPvrrlA 2887
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  548 KPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPSQGLPKTICPLCNTTELLLHVPEKANFNTCTECQTTvcslcGFNPNP 627
Cdd:PHA03247 2888 RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPS-----GAVPQP 2962
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  628 HLTEVKEWLCLNCQMKRALGGDLAPVPSSPQPKLKTAPVTTTSAVSKSSPQPQQTSPKKdAAPKQDLSKAPEPKKPPPLV 707
Cdd:PHA03247 2963 WLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPP-VSLKQTLWPPDDTEDSDADS 3041
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 150170670  708 KQPTLHGSPSAKAKQPPEADSLSKPAPPKEPSVPSEQDKA 747
Cdd:PHA03247 3042 LFDSDSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARE 3081
C2A_Synaptotagmin-8 cd08387
C2A domain first repeat present in Synaptotagmin 8; Synaptotagmin is a membrane-trafficking ...
4695-4826 1.41e-20

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: 90.54  E-value: 1.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4695 TGEIQLQINYD--LGNLIIHILQARNLVPRDNNGYSDPFVKVYLLPGRGQVmvvqnasaeykRRTKHVQKSLNPEWNQTV 4772
Cdd:cd08387     2 RGELHFSLEYDkdMGILNVKLIQARNLQPRDFSGTADPYCKVRLLPDRSNT-----------KQSKIHKKTLNPEFDESF 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 150170670 4773 IYkSISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSTSHLDNTPRWYPLK 4826
Cdd:cd08387    71 VF-EVPPQELPKRTLEVLLYDFDQFSRDECIGVVELPLAEVDLSEKLDLWRKIQ 123
C2B_Synaptotagmin-1 cd08402
C2 domain second repeat present in Synaptotagmin 1; Synaptotagmin is a membrane-trafficking ...
4696-4813 1.27e-19

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: 88.23  E-value: 1.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4696 GEIQLQINY--DLGNLIIHILQARNLVPRDNNGYSDPFVKVYLLPGRGQVMvvqnasaeyKRRTKHVQKSLNPEWNQTVI 4773
Cdd:cd08402     2 GDICFSLRYvpTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLK---------KKKTTIKKRTLNPYYNESFS 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 150170670 4774 YKsISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSST 4813
Cdd:cd08402    73 FE-VPFEQIQKVHLIVTVLDYDRIGKNDPIGKVVLGCNAT 111
C2B_Synaptotagmin-7 cd08405
C2 domain second repeat present in Synaptotagmin 7; Synaptotagmin is a membrane-trafficking ...
4696-4808 1.77e-19

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: 87.47  E-value: 1.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4696 GEIQLQINYD--LGNLIIHILQARNLVPRDNNGYSDPFVKVYLLPGRGQVmvvqnasaeYKRRTKHVQKSLNPEWNQTVI 4773
Cdd:cd08405     2 GELLLSLCYNptANRITVNIIKARNLKAMDINGTSDPYVKVWLMYKDKRV---------EKKKTVIKKRTLNPVFNESFI 72
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 150170670 4774 YkSISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLI 4808
Cdd:cd08405    73 F-NIPLERLRETTLIITVMDKDRLSRNDLIGKIYL 106
PHA03247 PHA03247
large tegument protein UL36; Provisional
446-1046 2.94e-19

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 97.32  E-value: 2.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  446 PGKiPAQQAGPGKTSAQQTGPTKPPSQLPGP---AKPPPQQPGPAKPPPQQPGSAKPPSQ-----------QPGSTKPPP 511
Cdd:PHA03247 2475 PGA-PVYRRPAEARFPFAAGAAPDPGGGGPPdpdAPPAPSRLAPAILPDEPVGEPVHPRMltwirgleelaSDDAGDPPP 2553
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  512 QQPgPAKPSPQQPGSTKPPSQQPGSAKPSAQQ--------PSPAKPSAqqstkPVSQTGSGKPLQPPTVSPSAKQPPSQG 583
Cdd:PHA03247 2554 PLP-PAAPPAAPDRSVPPPRPAPRPSEPAVTSrarrpdapPQSARPRA-----PVDDRGDPRGPAPPSPLPPDTHAPDPP 2627
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  584 LPkticplcnttelllhvpekanfntctecqttvcslcgfNPNPHLTEvkewlclncqmkrALGGDLAPVPSSPQPKLKT 663
Cdd:PHA03247 2628 PP--------------------------------------SPSPAANE-------------PDPHPPPTVPPPERPRDDP 2656
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  664 APvtttSAVSKSSPQPQQTSPKKDAAPKQDLSKAPEPKKPpplvkqptlhGSPSAKAKQPPEADSLSKPAPPKEPSVPSE 743
Cdd:PHA03247 2657 AP----GRVSRPRRARRLGRAAQASSPPQRPRRRAARPTV----------GSLTSLADPPPPPPTPEPAPHALVSATPLP 2722
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  744 QDKAPVADDKPKQPkmVKPTTDLVSSSSAT-TKPDIPSSKVQSQAEEKTTPPLKTDSAKPSQSFPPTGEKVSP-FDSKAI 821
Cdd:PHA03247 2723 PGPAAARQASPALP--AAPAPPAVPAGPATpGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSEsRESLPS 2800
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  822 PRPASDSKIISHPGPSSESKGQKQVDPVQKKEEPKKAQTKMSPKPDAKPMP-KGSPTPPGP---RPTAGQTVPTPQQSPK 897
Cdd:PHA03247 2801 PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPlGGSVAPGGDvrrRPPSRSPAAKPAAPAR 2880
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  898 PqeQSRRFSLNLGSITDAPKSQPTTPQEtvtgklfgfgasifsqasNLISTAGQPGPHSQSGPGAPMKQAPAPSQPPTSQ 977
Cdd:PHA03247 2881 P--PVRRLARPAVSRSTESFALPPDQPE------------------RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ 2940
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670  978 GPPKSTGQAPPAPAKSIPVkketKAPAAEKLEPKAEQAPtvkRTETEKKPPPIKDSKSLTAEPQKAVLP 1046
Cdd:PHA03247 2941 PPLAPTTDPAGAGEPSGAV----PQPWLGALVPGRVAVP---RFRVPQPAPSREAPASSTPPLTGHSLS 3002
C2B_Munc13-like cd04009
C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are ...
4709-4812 3.67e-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: 86.52  E-value: 3.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4709 LIIHILQARNLVPRDNNGYSDPFVKVYLLPGRGQVMVVqnasaeyKRRTKHVQKSLNPEWNQTvIYKSISMEQLKKK--T 4786
Cdd:cd04009    18 LRVEILNARNLLPLDSNGSSDPFVKVELLPRHLFPDVP-------TPKTQVKKKTLFPLFDES-FEFNVPPEQCSVEgaL 89
                          90       100
                  ....*....|....*....|....*.
gi 150170670 4787 LEVTVWDYDRFSSNDFLGEVLIDLSS 4812
Cdd:cd04009    90 LLFTVKDYDLLGSNDFEGEAFLPLND 115
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
226-575 1.84e-18

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: 94.06  E-value: 1.84e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   226 GRDPLQQDGTPKSISSQQPEKIKSQPPGTGKPIQGPTQTPQTDHAKLPLQRDASRPQTKQADIVRGESVKPSLPSPSKPP 305
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPP 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   306 IQQPTPGKPPAQQPGHEKSQP---GPAKPPAQPSGLTKPLAQQPGtvkpPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPS 382
Cdd:pfam03154  249 LQPMTQPPPPSQVSPQPLPQPslhGQMPPMPHSLQTGPSHMQHPV----PPQPFPLTPQSSQSQVPPGPSPAAPGQSQQR 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   383 SEQPGPKALAQPPgvgKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKtpVQQPGPGKIPAQQAGPGKTSAQ 462
Cdd:pfam03154  325 IHTPPSQSQLQSQ---QPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPH--LSGPSPFQMNSNLPPPPALKPL 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   463 QTGPTK-PPSQLPGPAKPPPQ----QPGPAKPP--------PQQPGSAKPPSQ-QPGSTKPP-PQQP-GPAKPSPQQPGS 526
Cdd:pfam03154  400 SSLSTHhPPSAHPPPLQLMPQsqqlPPPPAQPPvltqsqslPPPAASHPPTSGlHQVPSQSPfPQHPfVPGGPPPITPPS 479
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150170670   527 TKPPS--------QQPGSAKPSAQQPSPAKPSA-----QQSTKPVSQTGSGKPLQPPTVSPS 575
Cdd:pfam03154  480 GPPTStssampgiQPPSSASVSSSGPVPAAVSCplppvQIKEEALDEAEEPESPPPPPRSPS 541
C2D_Tricalbin-like cd04040
C2 domain fourth repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
4709-4828 4.04e-18

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: 83.00  E-value: 4.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4709 LIIHILQARNLVPRDNNGYSDPFVKVYLlpgrgqvmvvqNASAEYKrrTKHVQKSLNPEWNQTViykSISMEQLKKKTLE 4788
Cdd:cd04040     1 LTVDVISAENLPSADRNGKSDPFVKFYL-----------NGEKVFK--TKTIKKTLNPVWNESF---EVPVPSRVRAVLK 64
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 150170670 4789 VTVWDYDRFSSNDFLGEVLIDLSSTSHLDNTPRWYPLKEQ 4828
Cdd:cd04040    65 VEVYDWDRGGKDDLLGSAYIDLSDLEPEETTELTLPLDGQ 104
C2A_Synaptotagmin-like cd04024
C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
4707-4826 3.08e-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: 80.93  E-value: 3.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4707 GNLIIHILQARNLVPRD--NNGYSDPFVKVYLlpgrgqvmvvqnasAEYKRRTKHVQKSLNPEWNqtvIYKSISMEQLKK 4784
Cdd:cd04024     1 GVLRVHVVEAKDLAAKDrsGKGKSDPYAILSV--------------GAQRFKTQTIPNTLNPKWN---YWCEFPIFSAQN 63
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 150170670 4785 KTLEVTVWDYDRFSSNDFLGEVLIDLSSTSHLDNT---PRWYPLK 4826
Cdd:cd04024    64 QLLKLILWDKDRFAGKDYLGEFDIALEEVFADGKTgqsDKWITLK 108
C2A_Synaptotagmin-15-17 cd08390
C2A domain first repeat present in Synaptotagmins 15 and 17; Synaptotagmin is a ...
4696-4816 3.40e-17

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: 80.76  E-value: 3.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4696 GEIQLQINYDLG--NLIIHILQARNLVPRD-NNGYSDPFVKVYLLPGRGQVmvvqnasaeykRRTKHVQKSLNPEWNQTV 4772
Cdd:cd08390     1 GRLWFSVQYDLEeeQLTVSLIKARNLPPRTkDVAHCDPFVKVCLLPDERRS-----------LQSKVKRKTQNPNFDETF 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 150170670 4773 IYKsISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLI-----DLSSTSHL 4816
Cdd:cd08390    70 VFQ-VSFKELQRRTLRLSVYDVDRFSRHCIIGHVLFplkdlDLVKGGVV 117
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
187-586 6.72e-17

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: 88.47  E-value: 6.72e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   187 EETTKKQKVVQKEQGKPEGIIKPPLQQQPPKPIPKQQGPGRDplQQDGTP-KSISSQQPEKikSQPPGTGKPIQGPTQTP 265
Cdd:pfam03157  177 QQPGQGQQLRQGQQGQQSGQGQPGYYPTSSQQPGQLQQTGQG--QQGQQPeRGQQGQQPGQ--GQQPGQGQQGQQPGQPQ 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   266 QTDHAKLPLQRDASRPQTKQADIVRGEsvkpslPSPSKPPIQQPTPGkppaqQPGHEKSQPGPAKPPAQPSGLTKPLAQQ 345
Cdd:pfam03157  253 QLGQGQQGYYPISPQQPRQWQQSGQGQ------QGYYPTSLQQPGQG-----QSGYYPTSQQQAGQLQQEQQLGQEQQDQ 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   346 PGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQP 425
Cdd:pfam03157  322 QPGQGRQGQQPGQGQQGQQPAQGQQPGQGQPGYYPTSPQQPGQGQPGYYPTSQQQPQQGQQPEQGQQGQQQGQGQQGQQP 401
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   426 GL-QSPAKA-PGPTKTPVQQPGPGkipaqQAGPGKTSAQQTGPTKPPSQLPGPAKPPP---QQPGPAKP--PPQQPGSAK 498
Cdd:pfam03157  402 GQgQQPGQGqPGYYPTSPQQSGQG-----QPGYYPTSPQQSGQGQQPGQGQQPGQEQPgqgQQPGQGQQgqQPGQPEQGQ 476
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   499 PPSQ-QPGSTKPPPQQPGPAKPSPQ-------QPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPP 570
Cdd:pfam03157  477 QPGQgQPGYYPTSPQQSGQGQQLGQwqqqgqgQPGYYPTSPLQPGQGQPGYYPTSPQQPGQGQQLGQLQQPTQGQQGQQS 556
                          410
                   ....*....|....*.
gi 150170670   571 TVSPSAKQPPSQGLPK 586
Cdd:pfam03157  557 GQGQQGQQPGQGQQGQ 572
PHA03378 PHA03378
EBNA-3B; Provisional
307-590 9.38e-17

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 88.59  E-value: 9.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  307 QQPTPGKPPAQQPGHEKSQPGPA---------KPPAQ----PSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPA 373
Cdd:PHA03378  461 PLEGPTGPLSVQAPLEPWQPLPHpqvtpvilhQPPAQgvqaHGSMLDLLEKDDEDMEQRVMATLLPPSPPQPRAGRRAPC 540
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  374 QQTG-----SEKPSSEQPGPKALAQPPGVGKTP-------------------AQQPGPAKPPTQQVGTPKPLAQQPGLQS 429
Cdd:PHA03378  541 VYTEdldieSDEPASTEPVHDQLLPAPGLGPLQiqpltspttsqlassapsyAQTPWPVPHPSQTPEPPTTQSHIPETSA 620
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  430 PAKAPGPTKtpvqqPGPGKIPAQQAGPGKTSAQQTgPTKPPSQLPGPAKPPPQQPG--PAKPPPQQPGSAKPPSQQPGST 507
Cdd:PHA03378  621 PRQWPMPLR-----PIPMRPLRMQPITFNVLVFPT-PHQPPQVEITPYKPTWTQIGhiPYQPSPTGANTMLPIQWAPGTM 694
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  508 KPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPsQGLPKT 587
Cdd:PHA03378  695 QPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPP-AAAPGA 773

                  ...
gi 150170670  588 ICP 590
Cdd:PHA03378  774 PTP 776
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
226-585 1.01e-16

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: 88.08  E-value: 1.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   226 GRDPLQQDGTPKSISSQQPEKikSQPPGTGKPIQGPTQTPQTDHAKLPLQRDASRPQTKQADIVRGESVKPSLPSPSKPP 305
Cdd:pfam03157  230 GQQPGQGQQPGQGQQGQQPGQ--PQQLGQGQQGYYPISPQQPRQWQQSGQGQQGYYPTSLQQPGQGQSGYYPTSQQQAGQ 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   306 IQQPTPGKPPAQQP----GHEKSQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKP 381
Cdd:pfam03157  308 LQQEQQLGQEQQDQqpgqGRQGQQPGQGQQGQQPAQGQQPGQGQPGYYPTSPQQPGQGQPGYYPTSQQQPQQGQQPEQGQ 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   382 SSEQPGPKALAQPPGVGKTPAQ-QPG--PAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQ-QPGPGKIPAQ----Q 453
Cdd:pfam03157  388 QGQQQGQGQQGQQPGQGQQPGQgQPGyyPTSPQQSGQGQPGYYPTSPQQSGQGQQPGQGQQPGQeQPGQGQQPGQgqqgQ 467
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   454 AGPGKTSAQQTG-------PTKPPSQLPGPAKPPPQQPGPAKP-----PPQQPGSAKP-----PSQQPGSTKPPPQQPGP 516
Cdd:pfam03157  468 QPGQPEQGQQPGqgqpgyyPTSPQQSGQGQQLGQWQQQGQGQPgyyptSPLQPGQGQPgyyptSPQQPGQGQQLGQLQQP 547
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670   517 AKPSPQQPGSTKPPSQQPGSAKPSAQqpsPAKPSAQQSTKPVSQTGSGKPLQPPT--------VSPSAKQPPSQGLP 585
Cdd:pfam03157  548 TQGQQGQQSGQGQQGQQPGQGQQGQQ---PGQGQQGQQPGQGQQPGQGQPGYYPTspqqsgqgQQPGQWQQPGQGQP 621
C2E_Ferlin cd04037
C2 domain fifth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
4711-4810 1.47e-16

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: 78.75  E-value: 1.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4711 IHILQARNLVPRDNNGYSDPFVKVyllpgrgqvmvvQNASAEYKRRTKHVQKSLNPEWNQTVIYK-SISMEqlkkKTLEV 4789
Cdd:cd04037     4 VYVVRARNLQPKDPNGKSDPYLKI------------KLGKKKINDRDNYIPNTLNPVFGKMFELEaTLPGN----SILKI 67
                          90       100
                  ....*....|....*....|.
gi 150170670 4790 TVWDYDRFSSNDFLGEVLIDL 4810
Cdd:cd04037    68 SVMDYDLLGSDDLIGETVIDL 88
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
307-595 2.89e-16

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: 86.74  E-value: 2.89e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   307 QQPTPGKPPAQQPGHEKSQPGPAKPPAQPSGLTKPLA--QQPGTVKPPVQPpgTTKPPAQPLGPAKPPAQQTGSEKPSSE 384
Cdd:pfam03154  193 QAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTliQQTPTLHPQRLP--SPHPPLQPMTQPPPPSQVSPQPLPQPS 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   385 QPGP-KALAQPPGVGKTPAQQPGPAKPptqqVGTPKPLAQQPGLQSPA-KAPGPTKTPVQQPgPGKIPAQQAGPGKTSAQ 462
Cdd:pfam03154  271 LHGQmPPMPHSLQTGPSHMQHPVPPQP----FPLTPQSSQSQVPPGPSpAAPGQSQQRIHTP-PSQSQLQSQQPPREQPL 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   463 QTGPTKPPSQLPGPAKPPPQQPGP---------AKPPPQQPGSAKPP-----------SQQPGSTKPPPQQPGPAK---- 518
Cdd:pfam03154  346 PPAPLSMPHIKPPPTTPIPQLPNPqshkhpphlSGPSPFQMNSNLPPppalkplsslsTHHPPSAHPPPLQLMPQSqqlp 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   519 -PSPQQPGSTKPPSQQPGSAK---PSAQQPSPAK-PSAQQSTKPVSQTGSGKPLQPPTVSPSAK---QPPSQGLPKTICP 590
Cdd:pfam03154  426 pPPAQPPVLTQSQSLPPPAAShppTSGLHQVPSQsPFPQHPFVPGGPPPITPPSGPPTSTSSAMpgiQPPSSASVSSSGP 505

                   ....*
gi 150170670   591 LCNTT 595
Cdd:pfam03154  506 VPAAV 510
PHA03378 PHA03378
EBNA-3B; Provisional
236-577 3.48e-16

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 86.66  E-value: 3.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  236 PKSISSQQPE--KIKSQPPGTGKPIQGPTQTPQTDHAKLPLQRDASRP-------QTKQADIVRGESVKPSLPSPSKppi 306
Cdd:PHA03378  598 PVPHPSQTPEppTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITFNVlvfptphQPPQVEITPYKPTWTQIGHIPY--- 674
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  307 qQPTPG-----KPPAQQPGHEK---SQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPaqqtgs 378
Cdd:PHA03378  675 -QPSPTgantmLPIQWAPGTMQpppRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPP------ 747
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  379 ekpsseqpgpkalAQPPGVGKTPAQQPGPAKPPTQQVGTPKPlaqqpglQSPAKAPgptKTPVQQPgpgkipaqQAGPGK 458
Cdd:PHA03378  748 -------------AAAPGRARPPAAAPGRARPPAAAPGAPTP-------QPPPQAP---PAPQQRP--------RGAPTP 796
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  459 TSAQQTGPTkpPSQLPGPAkpPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPP---QQPGPAKPSPQQPGSTK------- 528
Cdd:PHA03378  797 QPPPQAGPT--SMQLMPRA--APGQQGPTKQILRQLLTGGVKRGRPSLKKPAAlerQAAAGPTPSPGSGTSDKivqapvf 872
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 150170670  529 -PPSQQPGSAKPSAQQPSPAKPSA--QQSTKPVSQTGSGKPLQPPTVSPSAK 577
Cdd:PHA03378  873 yPPVLQPIQVMRQLGSVRAAAASTvtQAPTEYTGERRGVGPMHPTDIPPSKR 924
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
229-583 4.36e-16

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: 86.15  E-value: 4.36e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   229 PLQQDGTPKSISSQQPEKikSQPPGTGKPIQGPTQTPQTDHAKLPLQrdasrpqtkqadivrGESVKPSLPSPSKPPIQQ 308
Cdd:pfam03157  116 PQQVSYYPGQASPQRPGQ--GQQPGQGQQWYYPTSPQQPGQWQQPGQ---------------GQQGYYPTSPQQSGQRQQ 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   309 PTPGKPPAQqpGHEKSQPGPAKPPAQPSGLTKP-LAQQPGTVKPPVQPpGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPG 387
Cdd:pfam03157  179 PGQGQQLRQ--GQQGQQSGQGQPGYYPTSSQQPgQLQQTGQGQQGQQP-ERGQQGQQPGQGQQPGQGQQGQQPGQPQQLG 255
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   388 PKALAQPPGVGKTPAQ-------QPGPAKPPTQQVGTPK----PLAQQPGLQSPAKAPGPTKTPVQQPGPGKiPAQQAGP 456
Cdd:pfam03157  256 QGQQGYYPISPQQPRQwqqsgqgQQGYYPTSLQQPGQGQsgyyPTSQQQAGQLQQEQQLGQEQQDQQPGQGR-QGQQPGQ 334
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   457 GKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKP-----PPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKpPS 531
Cdd:pfam03157  335 GQQGQQPAQGQQPGQGQPGYYPTSPQQPGQGQPgyyptSQQQPQQGQQPEQGQQGQQQGQGQQGQQPGQGQQPGQGQ-PG 413
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 150170670   532 QQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKplQPPTVSPSAKQPPSQG 583
Cdd:pfam03157  414 YYPTSPQQSGQGQPGYYPTSPQQSGQGQQPGQGQ--QPGQEQPGQGQQPGQG 463
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
4496-4587 5.93e-16

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: 75.66  E-value: 5.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4496 RIKITRDSkdhtvsGNGLGIRIVGGKEIPGhsgeiGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSII 4575
Cdd:cd00136     1 TVTLEKDP------GGGLGFSIRGGKDGGG-----GIFVSRVEPGGPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELL 69
                          90
                  ....*....|..
gi 150170670 4576 SQQSGEAEICVR 4587
Cdd:cd00136    70 KSAGGEVTLTVR 81
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
307-559 6.62e-16

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: 85.47  E-value: 6.62e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   307 QQPTPGKPPAQQPGHEKSQPGPAKPPAQPSGLTKPLA------QQPGTVkPPVQPP----GTT-KPPAQPlgpakPPAQQ 375
Cdd:pfam09770  105 QQPAARAAQSSAQPPASSLPQYQYASQQSQQPSKPVRtgyekyKEPEPI-PDLQVDaslwGVApKKAAAP-----APAPQ 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   376 TGSEKPSSEQPGPKALAqppgVGKTPAQQPGPAKPPTQQVgtPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAG 455
Cdd:pfam09770  179 PAAQPASLPAPSRKMMS----LEEVEAAMRAQAKKPAQQP--APAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQ 252
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   456 PGktsaQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKP---PPQQPGPAKPSPQQPgstkPPSQ 532
Cdd:pfam09770  253 PQ----QHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQIlqnPNRLSAARVGYPQNP----QPGV 324
                          250       260
                   ....*....|....*....|....*..
gi 150170670   533 QPGSAKPSAQQPSPAKPSAQQSTKPVS 559
Cdd:pfam09770  325 QPAPAHQAHRQQGSFGRQAPIITHPQQ 351
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
312-583 7.88e-16

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 85.04  E-value: 7.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  312 GKPPAQQPGHEKSQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKAL 391
Cdd:PRK07764  392 GAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPA 471
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  392 AQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQ----------------------SPAKAPGPTKTPVQ------- 442
Cdd:PRK07764  472 AAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDaatlrerwpeilaavpkrsrktWAILLPEATVLGVRgdtlvlg 551
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  443 -----------QPGPGKIPAQ--------------QAGPGKTSAQQTGPTKPPSQLPGP--AKPPPQQPGPAKPPPQQPG 495
Cdd:PRK07764  552 fstgglarrfaSPGNAEVLVTalaeelggdwqveaVVGPAPGAAGGEGPPAPASSGPPEeaARPAAPAAPAAPAAPAPAG 631
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  496 SAKPPSQQPGSTKPPPQQPGPAKPSPQQPGST------------KPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGS 563
Cdd:PRK07764  632 AAAAPAEASAAPAPGVAAPEHHPKHVAVPDASdggdgwpakaggAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPA 711
                         330       340
                  ....*....|....*....|
gi 150170670  564 GKPLQPPTVSPSAKQPPSQG 583
Cdd:PRK07764  712 GQADDPAAQPPQAAQGASAP 731
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
184-583 8.47e-16

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: 85.00  E-value: 8.47e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   184 ASQEETTKKQKVVQKEQGKPEGiikpplqqqpPKPIPKQQGPGRDPLQQDGTPKSISSQQPekiksqppGTGKPIQGPTQ 263
Cdd:pfam03157  372 TSQQQPQQGQQPEQGQQGQQQG----------QGQQGQQPGQGQQPGQGQPGYYPTSPQQS--------GQGQPGYYPTS 433
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   264 TPQTDHAKLPLQRDASRPQTKQADIVRGESVKPSLPSPSKPPiQQPTPGKP-----PAQQPGH-----EKSQPGPAKPPA 333
Cdd:pfam03157  434 PQQSGQGQQPGQGQQPGQEQPGQGQQPGQGQQGQQPGQPEQG-QQPGQGQPgyyptSPQQSGQgqqlgQWQQQGQGQPGY 512
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   334 QPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGvgktpaqQPGPAKPPTQ 413
Cdd:pfam03157  513 YPTSPLQPGQGQPGYYPTSPQQPGQGQQLGQLQQPTQGQQGQQSGQGQQGQQPGQGQQGQQPG-------QGQQGQQPGQ 585
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   414 qvgtpkplAQQPGLQSPAKAPgptkTPVQQPGPGKIPA--QQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAkppp 491
Cdd:pfam03157  586 --------GQQPGQGQPGYYP----TSPQQSGQGQQPGqwQQPGQGQPGYYPTSSLQLGQGQQGYYPTSPQQPGQG---- 649
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   492 QQPGSAKPPSQ-QPGSTKPPPQQPGpakpSPQQPGSTKPPSQ--QPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQ 568
Cdd:pfam03157  650 QQPGQWQQSGQgQQGYYPTSPQQSG----QAQQPGQGQQPGQwlQPGQGQQGYYPTSPQQPGQGQQLGQGQQSGQGQQGY 725
                          410
                   ....*....|....*
gi 150170670   569 PPTvSPSAKQPPSQG 583
Cdd:pfam03157  726 YPT-SPGQGQQSGQG 739
C2D_Ferlin cd04017
C2 domain fourth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
4711-4826 8.65e-16

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: 77.20  E-value: 8.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4711 IHILQARNLVPRDNNGYSDPFVKVYLLpgrgqvmvvqNASAEykrrTKHVQKSLNPEWNQTVIYKSISMEQLKKKTLE-- 4788
Cdd:cd04017     5 AYIYQARDLLAADKSGLSDPFARVSFL----------NQSQE----TEVIKETLSPTWDQTLIFDEVELYGSPEEIAQnp 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 150170670 4789 ----VTVWDYDRFSSNDFLGEVLID----LSSTSHLDNTPRWYPLK 4826
Cdd:cd04017    71 plvvVELFDQDSVGKDEFLGRSVAKplvkLDLEEDFPPKLQWFPIY 116
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
316-541 1.35e-15

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 84.16  E-value: 1.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  316 AQQPGHEKSQPGPAKPPAQPSGLTKPLAQQPGTVKP-PVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQP 394
Cdd:PRK12323  362 AFRPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPaPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASA 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  395 PGVGKTPAQQPGPAKPPtqqVGTPKPLAQQPGlqsPAKAPGPTKTPVQQPGPGKIPAQQAGPgktsAQQTGPTKPPSqlP 474
Cdd:PRK12323  442 RGPGGAPAPAPAPAAAP---AAAARPAAAGPR---PVAAAAAAAPARAAPAAAPAPADDDPP----PWEELPPEFAS--P 509
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670  475 GPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSA 541
Cdd:PRK12323  510 APAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDM 576
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
307-585 1.44e-15

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 84.27  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  307 QQPTPGKPPAQQPGHEKSQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKP-PAQQTGSEKPSSEQ 385
Cdd:PRK07764  396 AAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAaPSAQPAPAPAAAPE 475
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  386 PGPKALAQPPGVGKTPAQQPGPAKPPTQQ--------------------------------------------------- 414
Cdd:PRK07764  476 PTAAPAPAPPAAPAPAAAPAAPAAPAAPAgaddaatlrerwpeilaavpkrsrktwaillpeatvlgvrgdtlvlgfstg 555
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  415 --------------------------------VGTPKPLAQQPGlqSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQ 462
Cdd:PRK07764  556 glarrfaspgnaevlvtalaeelggdwqveavVGPAPGAAGGEG--PPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAA 633
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  463 QTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQ 542
Cdd:PRK07764  634 AAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQ 713
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 150170670  543 QPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPSQGLP 585
Cdd:PRK07764  714 ADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPA 756
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
307-587 1.97e-15

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 84.45  E-value: 1.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  307 QQPTPGKPPAQQPGHEKSQPGPAKPPAQPSGltkplaqqpgtvkPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQP 386
Cdd:PHA03307  111 PSSPDPPPPTPPPASPPPSPAPDLSEMLRPV-------------GSPGPPPAASPPAAGASPAAVASDAASSRQAALPLS 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  387 GPKALAQPPGvgkTPAQQPGPAKPPTQqvGTPKPLAQQPGLQSPAKAPGPT--KTPVQQPGPGKIPAQQAGPGKTSAQQT 464
Cdd:PHA03307  178 SPEETARAPS---SPPAEPPPSTPPAA--ASPRPPRRSSPISASASSPAPApgRSAADDAGASSSDSSSSESSGCGWGPE 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  465 GPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPS--QQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQ 542
Cdd:PHA03307  253 NECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSspRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSS 332
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 150170670  543 QPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPSQGLPKT 587
Cdd:PHA03307  333 SESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSS 377
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
255-585 3.76e-15

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 83.11  E-value: 3.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  255 GKPIQGPTQTPQTDHaklPLQRDASRPQTKQADIVRGESVKPSLPSPSKPPIQQPTPGKPPAQQPG-HEKSQPGPAKPPA 333
Cdd:PRK07764  384 RLGVAGGAGAPAAAA---PSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGnAPAGGAPSPPPAA 460
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  334 QPSGLTKPLAQQPG--TVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQppgVGK------------ 399
Cdd:PRK07764  461 APSAQPAPAPAAAPepTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWPEILAA---VPKrsrktwaillpe 537
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  400 -TPAQQPGPA------KPPTQQ----------------------------VGTPKPLAQQPGlqSPAKAPGPTKTPVQQP 444
Cdd:PRK07764  538 aTVLGVRGDTlvlgfsTGGLARrfaspgnaevlvtalaeelggdwqveavVGPAPGAAGGEG--PPAPASSGPPEEAARP 615
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  445 GPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQ---QPGSAKPPSQQPGSTKPPPQQPGPAKPSP 521
Cdd:PRK07764  616 AAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASdggDGWPAKAGGAAPAAPPPAPAPAAPAAPAG 695
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150170670  522 QQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQP-PTVSPSAKQPPSQGLP 585
Cdd:PRK07764  696 AAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPePDDPPDPAGAPAQPPP 760
C2B_RIM1alpha cd04028
C2 domain second repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ...
4686-4833 3.81e-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: 75.50  E-value: 3.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4686 GTKVVSHPITGEIQLQINYDLGNLIIHILQARNLVPRDNNGY-SDPFVKVYLLPGRGQVMvvqnasaeyKRRTKHVQKSL 4764
Cdd:cd04028     8 GRQVLASPSMGDIQLGLYDKKGQLEVEVIRARGLVQKPGSKVlPAPYVKVYLLEGKKCIA---------KKKTKIARKTL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4765 NPEWNQTVIYKsismEQLKKKTLEVTVW-DYDRFSSNDFLGEVLIDLSSTSHLDNTPRWYPLKEQTESID 4833
Cdd:cd04028    79 DPLYQQQLVFD----VSPTGKTLQVIVWgDYGRMDKKVFMGVAQILLDDLDLSNLVIGWYKLFPTSSLVD 144
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
318-525 4.53e-15

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 82.73  E-value: 4.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  318 QPGHEKSQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQPPGTtKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQP--- 394
Cdd:PRK07764  587 VVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAP-APAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAsdg 665
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  395 PGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQA-----GPGKTSAQQTGPTKP 469
Cdd:PRK07764  666 GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAqgasaPSPAADDPVPLPPEP 745
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670  470 PSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPgstkPPPQQPGPAKPSPQQPG 525
Cdd:PRK07764  746 DDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPS----EEEEMAEDDAPSMDDED 797
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
343-585 4.61e-15

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: 82.78  E-value: 4.61e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   343 AQQPgtvkPPVQPPGTTKPPAQPLGPAKPPAQQ---------TGSEKPSSEQPGPK--ALAQPPGVG-KTPAQQPGPAKP 410
Cdd:pfam09770  104 RQQP----AARAAQSSAQPPASSLPQYQYASQQsqqpskpvrTGYEKYKEPEPIPDlqVDASLWGVApKKAAAPAPAPQP 179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   411 PTQQVGTPKP---------LAQQPGLQSPAKAPGPTKTPVQQPGPgkIPAQQAgpgktsaqqtgptKPPSQLPGPAKPPP 481
Cdd:pfam09770  180 AAQPASLPAPsrkmmsleeVEAAMRAQAKKPAQQPAPAPAQPPAA--PPAQQA-------------QQQQQFPPQIQQQQ 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   482 QQPGPAKPPPQQPGSAKPPS--QQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVS 559
Cdd:pfam09770  245 QPQQQPQQPQQHPGQGHPVTilQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQILQNPNRLSAARVGYPQNPQPGV 324
                          250       260
                   ....*....|....*....|....*.
gi 150170670   560 QTGSGKPlQPPTVSPSAKQPPSQGLP 585
Cdd:pfam09770  325 QPAPAHQ-AHRQQGSFGRQAPIITHP 349
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
356-553 5.55e-15

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 82.34  E-value: 5.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  356 PGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPG 435
Cdd:PRK07764  588 VGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  436 PTKTPVQQPGPGKiPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPG 515
Cdd:PRK07764  668 GWPAKAGGAAPAA-PPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 150170670  516 PAkPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQ 553
Cdd:PRK07764  747 DP-PDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
C2A_MCTP_PRT_plant cd04022
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
4709-4825 7.62e-15

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: 73.91  E-value: 7.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4709 LIIHILQARNLVPRDNNGYSDPFVKVYLLpgrGQvmvvqnasaeyKRRTKHVQKSLNPEWNQTVIYKSISMEQLKKKTLE 4788
Cdd:cd04022     2 LVVEVVDAQDLMPKDGQGSSSAYVELDFD---GQ-----------KKRTRTKPKDLNPVWNEKLVFNVSDPSRLSNLVLE 67
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 150170670 4789 VTVWDYDRFS-SNDFLGEVLIDLSS-TSHLDNTPRWYPL 4825
Cdd:cd04022    68 VYVYNDRRSGrRRSFLGRVRISGTSfVPPSEAVVQRYPL 106
C2A_Synaptotagmin-4-11 cd08388
C2A domain first repeat present in Synaptotagmins 4 and 11; Synaptotagmin is a ...
4696-4813 1.09e-14

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: 73.54  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4696 GEIQLQINYDLGN--LIIHILQARNLVPRD-NNGYSDPFVKVYLLPGRgqvmvvqnasaEYKRRTKHVQKSLNPEWNQTV 4772
Cdd:cd08388     3 GTLFFSLRYNSEKkaLLVNIIECRDLPAMDeQSGTSDPYVKLQLLPEK-----------EHKVKTRVLRKTRNPVYDETF 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 150170670 4773 IYKSISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSST 4813
Cdd:cd08388    72 TFYGIPYNQLQDLSLHFAVLSFDRYSRDDVIGEVVCPLAGA 112
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
224-570 1.65e-14

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: 80.82  E-value: 1.65e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   224 GPGRDPLQQDGTPKSISSQQPEKIKSQPPgtgkpiQGPTQTPQTDHAKLPLQRDASRPQTKQADIVRGESVKPSLPSPSK 303
Cdd:pfam09606  105 GPGGPMGQQMGGPGTASNLLASLGRPQMP------MGGAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNG 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   304 PPIQQPTPGKPPAQQPGHEKSQPGPAKPPAQPsGLTKPLAQQPGTVKPPVQPPgttkPPAQPLGPAKPPAQQtgsekpss 383
Cdd:pfam09606  179 GPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMP-GPADAGAQMGQQAQANGGMN----PQQMGGAPNQVAMQQ-------- 245
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   384 EQPGPKALAQPPGVGKTPAQQPGPAKPPTQQVGTP----KPLAQQPGLQSPAKAPGPTKTPVQQPG-PGKIPAQQAGPGK 458
Cdd:pfam09606  246 QQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPgqpmGPPGQQPGAMPNVMSIGDQNNYQQQQTrQQQQQQGGNHPAA 325
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   459 TSAQQTGPTKPPSQ---LPGPAKPPPQQPG---PAKPPPQQPG------------SAKPPSQQPGSTKPPPQQPgpAKPS 520
Cdd:pfam09606  326 HQQQMNQSVGQGGQvvaLGGLNHLETWNPGnfgGLGANPMQRGqpgmmsspspvpGQQVRQVTPNQFMRQSPQP--SVPS 403
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 150170670   521 PQQPGSTKPPSQQPGSAKPSA--QQPSPAKPSAQQSTKPVSQTGSGKPLQPP 570
Cdd:pfam09606  404 PQGPGSQPPQSHPGGMIPSPAliPSPSPQMSQQPAQQRTIGQDSPGGSLNTP 455
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
4707-4835 2.26e-14

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: 72.32  E-value: 2.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4707 GNLIIHILQARNLVPRDNN------GYSDPFVKVyllpgrgQVmvvqnasAEYKRRTKHVQKSLNPEWNQTviYKSIsME 4780
Cdd:cd08391     1 GVLRIHVIEAQDLVAKDKFvgglvkGKSDPYVIV-------RV-------GAQTFKSKVIKENLNPKWNEV--YEAV-VD 63
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 150170670 4781 QLKKKTLEVTVWDYDRfSSNDFLGEVLIDLSSTSHLDNTPRWYPLkeqtESIDHG 4835
Cdd:cd08391    64 EVPGQELEIELFDEDP-DKDDFLGRLSIDLGSVEKKGFIDEWLPL----EDVKSG 113
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
186-585 2.29e-14

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: 80.44  E-value: 2.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   186 QEETTKKQKVVQKEQGKPEGIIKPPLQQQPPKPIPKQQGPGRDPLQQDGTPKSISSQQPEKIKSQPPGTGKPIQGPTQTP 265
Cdd:pfam09606   51 RDMSKKAAQQQQPQGGQGNGGMGGGQQGMPDPINALQNLAGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASNLLASLGRP 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   266 QTDHAKlplqrdASRPQTKQAdivrgesVKPSLPSPSKPPIQQPTPGKPPAQQPghekSQPGPAKPPAQPSGLTKPLAQQ 345
Cdd:pfam09606  131 QMPMGG------AGFPSQMSR-------VGRMQPGGQAGGMMQPSSGQPGSGTP----NQMGPNGGPGQGQAGGMNGGQQ 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   346 PGtvkPPVQPPGTTKPPAqPLGPAKPPAQqTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQ---QVGTPKPLA 422
Cdd:pfam09606  194 GP---MGGQMPPQMGVPG-MPGPADAGAQ-MGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQlgmGINQMQQMP 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   423 QQPGLQSPAKAPGPTKTPVQQpGPGKIPAQQAGPGKTSAQQTGpTKPPSQLPGPAKPP--PQQP----GPAKPPPQQPGS 496
Cdd:pfam09606  269 QGVGGGAGQGGPGQPMGPPGQ-QPGAMPNVMSIGDQNNYQQQQ-TRQQQQQQGGNHPAahQQQMnqsvGQGGQVVALGGL 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   497 AKPPSQQPGSTKP---PPQQPGPA--KPSPQQPGSTKPPSQQPGSAKPSAQQPSpaKPSAQQSTKPVSQTGSGKPLQPPT 571
Cdd:pfam09606  347 NHLETWNPGNFGGlgaNPMQRGQPgmMSSPSPVPGQQVRQVTPNQFMRQSPQPS--VPSPQGPGSQPPQSHPGGMIPSPA 424
                          410
                   ....*....|....
gi 150170670   572 VSPSAKQPPSQGLP 585
Cdd:pfam09606  425 LIPSPSPQMSQQPA 438
C2A_MCTP_PRT cd04042
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
4709-4812 2.52e-14

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: 72.31  E-value: 2.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4709 LIIHILQARNLVPRDNNGYSDPFVKVYLlpgrGQVMVvqnasaeYKRRTKHvqKSLNPEWNQTViykSISMEQLKKKtLE 4788
Cdd:cd04042     2 LDIHLKEGRNLAARDRGGTSDPYVKFKY----GGKTV-------YKSKTIY--KNLNPVWDEKF---TLPIEDVTQP-LY 64
                          90       100
                  ....*....|....*....|....
gi 150170670 4789 VTVWDYDRFSSNDFLGEVLIDLSS 4812
Cdd:cd04042    65 IKVFDYDRGLTDDFMGSAFVDLST 88
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
338-583 2.88e-14

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 79.92  E-value: 2.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  338 LTKPLAQQPGTVKPPVQPPGTTKPP-AQPLGPAKPPAQQTgsEKPSSEQPGPKALAQPPGVGKTPAQQPGPAKPPtqqvg 416
Cdd:PRK12323  357 LLRMLAFRPGQSGGGAGPATAAAAPvAQPAPAAAAPAAAA--PAPAAPPAAPAAAPAAAAAARAVAAAPARRSPA----- 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  417 tpkPLAQQPGLQSPAKAPGPTKTPVqqPGPGKIPAQQAGPgktsaqqtgPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGS 496
Cdd:PRK12323  430 ---PEALAAARQASARGPGGAPAPA--PAPAAAPAAAARP---------AAAGPRPVAAAAAAAPARAAPAAAPAPADDD 495
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  497 AKPPSQQPgstkPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPA-KPSAQQSTKPVSQTGSGKPLQPPTVSPS 575
Cdd:PRK12323  496 PPPWEELP----PEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLApAPAAAPAPRAAAATEPVVAPRPPRASAS 571

                  ....*...
gi 150170670  576 AKQPPSQG 583
Cdd:PRK12323  572 GLPDMFDG 579
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
372-587 4.53e-14

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 79.15  E-value: 4.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  372 PAQQTGSEKPSSEQPGP-----KALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGP 446
Cdd:PRK12323  365 PGQSGGGAGPATAAAAPvaqpaPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGP 444
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  447 GKIPAQQAGPGKTSAQQTGPtkppsqlpgPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPG-PAKPSPQQPG 525
Cdd:PRK12323  445 GGAPAPAPAPAAAPAAAARP---------AAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPeFASPAPAQPD 515
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150170670  526 STKPPSQQPGSAKPSAQQPSPAKPSaqQSTKPVSQTGSGKPLQPPTVSPSakQPPSQGLPKT 587
Cdd:PRK12323  516 AAPAGWVAESIPDPATADPDDAFET--LAPAPAAAPAPRAAAATEPVVAP--RPPRASASGL 573
C2C_MCTP_PRT cd08377
C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
4707-4826 4.76e-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: 71.56  E-value: 4.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4707 GNLIIHILQARNLVPRDNNGYSDPFVkvyllpgrgqVMVVQNAsaeyKRRTKHVQKSLNPEWNQTVIYKSISMEQLkkkt 4786
Cdd:cd08377     1 GFLQVKVIRASGLAAADIGGKSDPFC----------VLELVNA----RLQTHTIYKTLNPEWNKIFTFPIKDIHDV---- 62
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 150170670 4787 LEVTVWDYDRFSSNDFLGEVLIDLSSTShlDNTPRWYPLK 4826
Cdd:cd08377    63 LEVTVYDEDKDKKPEFLGKVAIPLLSIK--NGERKWYALK 100
C2B_MCTP_PRT_plant cd08378
C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
4732-4825 7.42e-14

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: 71.19  E-value: 7.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4732 VKVYLLPGRGQVMVVQNASAEYKRRTKHVQKSLNPEWNQTViykSISMEQLKKKTLEVTVWDYDrFSSNDFLGEVLIDLS 4811
Cdd:cd08378     7 VKARGLPANSNDPVVEVKLGNYKGSTKAIERTSNPEWNQVF---AFSKDRLQGSTLEVSVWDKD-KAKDDFLGGVCFDLS 82
                          90       100
                  ....*....|....*....|.
gi 150170670 4812 ST-------SHLdnTPRWYPL 4825
Cdd:cd08378    83 EVptrvppdSPL--APQWYRL 101
C2B_RasA1_RasA4 cd04025
C2 domain second repeat present in RasA1 and RasA4; RasA1 and RasA4 are GAP1s (GTPase ...
4712-4834 8.45e-14

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: 70.98  E-value: 8.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4712 HILQARNLVPRDNNGYSDPFVKVYLlpgRGQVmvvqnasaeykRRTKHVQKSLNPEWNQTVIYKsisMEQLKKKTLEVTV 4791
Cdd:cd04025     5 HVLEARDLAPKDRNGTSDPFVRVFY---NGQT-----------LETSVVKKSCYPRWNEVFEFE---LMEGADSPLSVEV 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 150170670 4792 WDYDRFSSNDFLGEVLIDLSSTSHLDNTPRWYPLKEQTESIDH 4834
Cdd:cd04025    68 WDWDLVSKNDFLGKVVFSIQTLQQAKQEEGWFRLLPDPRAEEE 110
C2B_Synaptotagmin-4 cd08404
C2 domain second repeat present in Synaptotagmin 4; Synaptotagmin is a membrane-trafficking ...
4696-4815 1.44e-13

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: 70.92  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4696 GEIQLQINYD--LGNLIIHILQARNLVPRDNNGYSDPFVKVYLLPGRGQVMvvqnasaeyKRRTkHVQK-SLNPEWNQTV 4772
Cdd:cd08404     2 GELLLSLCYQptTNRLTVVVLKARHLPKMDVSGLADPYVKVNLYYGKKRIS---------KKKT-HVKKcTLNPVFNESF 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 150170670 4773 IYKsISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSTSH 4815
Cdd:cd08404    72 VFD-IPSEELEDISVEFLVLDSDRVTKNEVIGRLVLGPKASGS 113
PRK10263 PRK10263
DNA translocase FtsK; Provisional
320-923 1.82e-13

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 77.82  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  320 GHEKSQPGPAKPPAQPSGLTKPLAQQPGTVKPPVqpPGTTKPPAQPLGPAKP-PAQQTG----SEKPSSEQPGPKaLAQP 394
Cdd:PRK10263  313 GAPITEPVAVAAAATTATQSWAAPVEPVTQTPPV--ASVDVPPAQPTVAWQPvPGPQTGepviAPAPEGYPQQSQ-YAQP 389
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  395 PGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAkapgptkTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLP 474
Cdd:PRK10263  390 AVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPE-------QPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTY 462
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  475 GPAKPPPqQPGPAKPPPQQPgsakPPSQQPGSTKPPP--QQPGPAKP--------------SPQQPGSTKPPSQQPgsak 538
Cdd:PRK10263  463 QTEQTYQ-QPAAQEPLYQQP----QPVEQQPVVEPEPvvEETKPARPplyyfeeveekrarEREQLAAWYQPIPEP---- 533
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  539 psAQQPSPAKPSAQQSTKPVSqtgsgkplqPPTVSPSAKQPPSQGLPKTIcpLCNTTELLLHVPEkanFNTCTecqttvc 618
Cdd:PRK10263  534 --VKEPEPIKSSLKAPSVAAV---------PPVEAAAAVSPLASGVKKAT--LATGAAATVAAPV---FSLAN------- 590
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  619 slcGFNPNPhltevkewlclncQMKRALGgdlapvPSSPQPKLKTAPvTTTSAVSKSSPQPQQTSPKKDAAPKQdlSKAP 698
Cdd:PRK10263  591 ---SGGPRP-------------QVKEGIG------PQLPRPKRIRVP-TRRELASYGIKLPSQRAAEEKAREAQ--RNQY 645
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  699 EPKKPPPLVKQPTLHGSPSAKAKQPPEADSLSKPAPPKEPSVPSEQDKAPVAD--DKPKQPKMVKPTTDLVSSSSATTKP 776
Cdd:PRK10263  646 DSGDQYNDDEIDAMQQDELARQFAQTQQQRYGEQYQHDVPVNAEDADAAAEAElaRQFAQTQQQRYSGEQPAGANPFSLD 725
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  777 DIPSSKVQSQAEEKTTPPLKTDSAKPSQSfpPTGEKVSPFDSKAIPRPASDSKIISHPGPSSESKGQKQVDPVQKKEEPK 856
Cdd:PRK10263  726 DFEFSPMKALLDDGPHEPLFTPIVEPVQQ--PQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQ 803
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670  857 KAQTKMSPKPdaKPMPKGSPTPPGPRPTAGQtvptPQQSPKPQEQSRRFSLNLGSITDA-PKSQPTTP 923
Cdd:PRK10263  804 YQQPQQPVAP--QPQYQQPQQPVAPQPQYQQ----PQQPVAPQPQDTLLHPLLMRNGDSrPLHKPTTP 865
C2B_MCTP_PRT cd08376
C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
4711-4833 4.01e-13

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: 68.82  E-value: 4.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4711 IHILQARNLVPRDNNGYSDPFVKVYLlpgRGQvmvvqnasaeyKRRTKHVQKSLNPEWnqtviyksisMEQL-------K 4783
Cdd:cd08376     4 IVLVEGKNLPPMDDNGLSDPYVKFRL---GNE-----------KYKSKVCSKTLNPQW----------LEQFdlhlfddQ 59
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 150170670 4784 KKTLEVTVWDYDRFSSNDFLGEVLIDLSSTSHLDNTPRWYPLKEQTESID 4833
Cdd:cd08376    60 SQILEIEVWDKDTGKKDEFIGRCEIDLSALPREQTHSLELELEDGEGSLL 109
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
324-582 6.25e-13

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 75.66  E-value: 6.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  324 SQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQPPGttkpPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKtpAQ 403
Cdd:PRK07003  366 GAPGGGVPARVAGAVPAPGARAAAAVGASAVPAV----TAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATAD--RG 439
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  404 QPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQ 483
Cdd:PRK07003  440 DDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASRE 519
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  484 PGPAKPPPQQPGSAKPpsqQPGSTKPPPQQPGPAKP-----SPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPV 558
Cdd:PRK07003  520 DAPAAAAPPAPEARPP---TPAAAAPAARAGGAAAAldvlrNAGMRVSSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQV 596
                         250       260
                  ....*....|....*....|....
gi 150170670  559 SQTGSGKPLQPPTVSPSAKQPPSQ 582
Cdd:PRK07003  597 PTPRARAATGDAPPNGAARAEQAA 620
C2A_Munc13-like cd08676
C2 domain first repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are ...
4709-4825 8.89e-13

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: 68.94  E-value: 8.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4709 LIIHILQARNLVPRDNNGYSDPFVKVYLLPG---------------RGQVMVVQNASAEYKRRTKHVQKSLNPEWNQTVI 4773
Cdd:cd08676    30 LKVTVIEAKGLLAKDVNGFSDPYCMLGIVPAsrernsekskkrkshRKKAVLKDTVPAKSIKVTEVKPQTLNPVWNETFR 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 150170670 4774 YKsisMEQLKKKTLEVTVWDYDrfssNDFLGEVLIDLSStSHLDNTPRWYPL 4825
Cdd:cd08676   110 FE---VEDVSNDQLHLDIWDHD----DDFLGCVNIPLKD-LPSCGLDSWFKL 153
PDZ1_GgSTXBP4-like cd06692
PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, ...
4511-4588 1.05e-12

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


Pssm-ID: 467179 [Multi-domain]  Cd Length: 88  Bit Score: 66.48  E-value: 1.05e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670 4511 NGLGIRIVGGkeIPGHSGE-IGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSgeAEICVRL 4588
Cdd:cd06692     8 KGLGIKIIGG--YRENTGEeFGIFIKRILPGGLAATDGRLKEGDLILEVNGESLQGVTNERAVSILRSAS--ASNHMSL 82
PHA03247 PHA03247
large tegument protein UL36; Provisional
654-1073 1.56e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 74.97  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  654 PSSPQPKlKTAPVTTTSAVSKSSPqPQQTSPKKDAAPKQDLSkapepkkppplvkqptlhgSPSAKAKQPPeADSLSKPA 733
Cdd:PHA03247 2570 PPRPAPR-PSEPAVTSRARRPDAP-PQSARPRAPVDDRGDPR-------------------GPAPPSPLPP-DTHAPDPP 2627
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  734 PPKEPSVPSEQDKAPVADDKPKQPKMVKPTTDLVSSS---SATTKPDIPSSKVQSQAEEKTTPPLK--TDSAKPSQSfPP 808
Cdd:PHA03247 2628 PPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrraRRLGRAAQASSPPQRPRRRAARPTVGslTSLADPPPP-PP 2706
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  809 TGEKVSPFDSKAIPRP-ASDSKIISHPG----PSSESKGQKQVDPVQKKEEPKKAQTKMSPKPDAKPMPKGSPTPPGPRP 883
Cdd:PHA03247 2707 TPEPAPHALVSATPLPpGPAAARQASPAlpaaPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRP 2786
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  884 TAGQTVPTPQQSPKPQEQS--------RRFSLNLGSITDAPKSQPTTPQETVTGKLFGFGASIFSQASNLI--------- 946
Cdd:PHA03247 2787 AVASLSESRESLPSPWDPAdppaavlaPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVApggdvrrrp 2866
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  947 -STAGQPGPHSQSGPGAPMKQAPAPSQPPTSQGPPKSTGQAPPAPAKSIPVKKETKAPAAEKLEPKAE-----QAPTVKR 1020
Cdd:PHA03247 2867 pSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPppprpQPPLAPT 2946
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670 1021 TETEKKPPP---IKDSKSLTAEPQKAVLPTKLEKSPKPESTCPLCKTELNIGSKDP 1073
Cdd:PHA03247 2947 TDPAGAGEPsgaVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLS 3002
C2B_RasGAP cd08675
C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
4709-4834 1.85e-12

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: 67.40  E-value: 1.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4709 LIIHILQARNLVPRdNNGYSDPFVKVYLLPGRGQVMvvqnasaeykRRTKHVQKSLNPEWNQTVIY----------KSIS 4778
Cdd:cd08675     1 LSVRVLECRDLALK-SNGTCDPFARVTLNYSSKTDT----------KRTKVKKKTNNPRFDEAFYFeltigfsyekKSFK 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670 4779 M--EQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSTSHLDNTPRWYPLKEQTESIDH 4834
Cdd:cd08675    70 VeeEDLEKSELRVELWHASMVSGDDFLGEVRIPLQGLQQAGSHQAWYFLQPREAPGTR 127
C2A_SLP-3 cd08392
C2 domain first repeat present in Synaptotagmin-like protein 3; All Slp members basically ...
4695-4826 2.16e-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: 67.16  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4695 TGEIQLQINY--DLGNLIIHILQARNLVPRDNNGYS-DPFVKVYLLPGRgqvmvvqnaSAEYKRRTKHVQKSLNPEWNQT 4771
Cdd:cd08392     1 TGEIEFALHYnfRTSCLEITIKACRNLAYGDEKKKKcHPYVKVCLLPDK---------SHNSKRKTAVKKGTVNPVFNET 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670 4772 VIYKsISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSTSHLDNTP---RWYPLK 4826
Cdd:cd08392    72 LKYV-VEADLLSSRQLQVSVWHSRTLKRRVFLGEVLIPLADWDFEDTDSqrfLWYPLN 128
PHA03379 PHA03379
EBNA-3A; Provisional
369-591 2.73e-12

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 73.94  E-value: 2.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  369 AKPPAQQTGSEKPSSEQPGPKA---LAQPPGVGktPAQQPgpaKPPTQQVGTPKPLAQQPGLqspakAPGPtktpVQQPG 445
Cdd:PHA03379  406 EKASEPTYGTPRPPVEKPRPEVpqsLETATSHG--SAQVP---EPPPVHDLEPGPLHDQHSM-----APCP----VAQLP 471
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  446 PGkiPAQQAGPGKtsaQQTGPTKPPSQLPGPAKPP------PQQPGPAKPPPQQPGSAKP------PSQQPGSTKPPPQQ 513
Cdd:PHA03379  472 PG--PLQDLEPGD---QLPGVVQDGRPACAPVPAPagpivrPWEASLSQVPGVAFAPVMPqpmpvePVPVPTVALERPVC 546
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670  514 PGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKpvSQTGSGKPLQPPTVSPSAKQPPSQGLPKTICPL 591
Cdd:PHA03379  547 PAPPLIAMQGPGETSGIVRVRERWRPAPWTPNPPRSPSQMSVR--DRLARLRAEAQPYQASVEVQPPQLTQVSPQQPM 622
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
270-585 3.41e-12

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 72.79  E-value: 3.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  270 AKLPLQRDASRPQTKQADIVRGESVKPSLPSPSKPPIQQPTPgKPPAQQPGHEKSQPGPAKPPAQPSGLTKPLAQQPGTV 349
Cdd:COG5180   146 AGVALAAALLQRSDPILAKDPDGDSASTLPPPAEKLDKVLTE-PRDALKDSPEKLDRPKVEVKDEAQEEPPDLTGGADHP 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  350 KPPVQPPGTTKPPAQPLGPAKPPaqqTGSEKPSSEQPGPKALAQPPGVGKTPAQQPgpakpptqqvgtpkplaqqPGLQS 429
Cdd:COG5180   225 RPEAASSPKVDPPSTSEARSRPA---TVDAQPEMRPPADAKERRRAAIGDTPAAEP-------------------PGLPV 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  430 PAKAPGPTKTPVQQPGPGKIpaqQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPG--PAKPPPQQPGSAKPPSQQPGST 507
Cdd:COG5180   283 LEAGSEPQSDAPEAETARPI---DVKGVASAPPATRPVRPPGGARDPGTPRPGQPTerPAGVPEAASDAGQPPSAYPPAE 359
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670  508 KPPPQQPGPA-KPSPQQPGSTKPPSQqPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPSQGLP 585
Cdd:COG5180   360 EAVPGKPLEQgAPRPGSSGGDGAPFQ-PPNGAPQPGLGRRGAPGPPMGAGDLVQAALDGGGRETASLGGAAGGAGQGPK 437
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
410-886 3.87e-12

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 73.28  E-value: 3.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  410 PPTQQVGTPKPLAQQPGLQspAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKP--PPQQPGPA 487
Cdd:PHA03307   39 SQGQLVSDSAELAAVTVVA--GAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPtpPGPSSPDP 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  488 KPPPQQPGSAkPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSqtgSGKPL 567
Cdd:PHA03307  117 PPPTPPPASP-PPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPS---SPPAE 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  568 QPPTVSPSAKQPPSQGLPKTICPlcnttelllhvpekanfntctecqttvcslcgfnpnphltevkewlclncqmkRALG 647
Cdd:PHA03307  193 PPPSTPPAAASPRPPRRSSPISA-----------------------------------------------------SASS 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  648 GDLAPVPSSPQPKLKTAPVTTTSAVSKSSPQPQQTSPKKDAAPKQDLSKAPEPKKPPPLVKQPTL---HGSPSAKAKQPP 724
Cdd:PHA03307  220 PAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPassSSSPRERSPSPS 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  725 EADSLSKPAPPKEPSVPSEQDKAPVADDKPKqpkmvkpttdlvSSSSATTKPDIPSSKVQSQAEEKTTPPLKTDSAKPSQ 804
Cdd:PHA03307  300 PSSPGSGPAPSSPRASSSSSSSRESSSSSTS------------SSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRK 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  805 SFPPTGEKVSPFDSKAIPRPASDSKIISHPGPSSESKGQ---KQVDPVQKKEEPKKAQTKMSPKPDakpMPKGSPTPPGP 881
Cdd:PHA03307  368 RPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRfpaGRPRPSPLDAGAASGAFYARYPLL---TPSGEPWPGSP 444

                  ....*
gi 150170670  882 RPTAG 886
Cdd:PHA03307  445 PPPPG 449
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
285-581 4.04e-12

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 73.28  E-value: 4.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  285 QADIVRGESVKPSLPSPSKPPIQQPTPGKPPAQQPGHEKSQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQPPgttkPPAQ 364
Cdd:PHA03307   47 SAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPP----PTPP 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  365 PLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQ-QVGTPKPLAQQPGLQSPAKAPGPTKTPVQQ 443
Cdd:PHA03307  123 PASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQaALPLSSPEETARAPSSPPAEPPPSTPPAAA 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  444 PGPG---KIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKP------PPQQPGSAKPPSQQPGSTKPPPQQP 514
Cdd:PHA03307  203 SPRPprrSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPenecplPRPAPITLPTRIWEASGWNGPSSRP 282
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670  515 GPAK---------PSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPS 581
Cdd:PHA03307  283 GPASssssprersPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPP 358
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
4509-4587 4.99e-12

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: 64.71  E-value: 4.99e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670   4509 SGNGLGIRIVGGKEIPGhsgeiGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGEAEICVR 4587
Cdd:smart00228   10 GGGGLGFSLVGGKDEGG-----GVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
C2A_fungal cd04041
C2 domain first repeat; fungal group; C2 domains were first identified in Protein Kinase C ...
4707-4829 7.22e-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: 64.98  E-value: 7.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4707 GNLIIHILQARNLVPRDNN-GYSDPFVKVYLlpgrgqvmvvqNASAEYKRRTKHVQKSLNPEWNQT-VIykSISMEQLK- 4783
Cdd:cd04041     1 GVLVVTIHRATDLPKADFGtGSSDPYVTASF-----------AKFGKPLYSTRIIRKDLNPVWEETwFV--LVTPDEVKa 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 150170670 4784 KKTLEVTVWDYDRFSSNDFLGEVLIDLSStshLDNTPRWYPLKEQT 4829
Cdd:cd04041    68 GERLSCRLWDSDRFTADDRLGRVEIDLKE---LIEDRNWMGRREDG 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 ...
4696-4825 1.41e-11

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: 64.84  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4696 GEIQLQINY--DLGNLIIHILQARNLVPRDNNGYSDPFVKVYLL-PGRgqvmvvqnasaEYKRRTKHVQKS-LNPEWNQT 4771
Cdd:cd08403     1 GELMFSLCYlpTAGRLTLTIIKARNLKAMDITGFSDPYVKVSLMcEGR-----------RLKKKKTSVKKNtLNPTYNEA 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670 4772 VIYkSISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSTSH--------LDN----TPRWYPL 4825
Cdd:cd08403    70 LVF-DVPPENVDNVSLIIAVVDYDRVGHNELIGVCRVGPNADGQgrehwnemLANprkpIAQWHQL 134
C2_Intersectin cd08375
C2 domain present in Intersectin; A single instance of the C2 domain is located C terminally ...
4707-4812 1.46e-11

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: 65.10  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4707 GNLIIHILQARNLVPRDNNGYSDPFVKVYLlpgrgqvmvvqnASAEYKrrTKHVQKSLNPEWNQTVIYKSISMEQlkkKT 4786
Cdd:cd08375    15 GRLMVVIVEGRDLKPCNSNGKSDPYCEVSM------------GSQEHK--TKVVSDTLNPKWNSSMQFFVKDLEQ---DV 77
                          90       100
                  ....*....|....*....|....*.
gi 150170670 4787 LEVTVWDYDRFSSNDFLGEVLIDLSS 4812
Cdd:cd08375    78 LCITVFDRDFFSPDDFLGRTEIRVAD 103
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
263-578 1.46e-11

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 70.86  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  263 QTPQTDHAKLPLQRDASRPQTKQADIVRGESVKPSLPSPSKPPIQQPTPGKPPAQQPGHEKSQPGP--AKPPAQPSGLTK 340
Cdd:COG5180   156 QRSDPILAKDPDGDSASTLPPPAEKLDKVLTEPRDALKDSPEKLDRPKVEVKDEAQEEPPDLTGGAdhPRPEAASSPKVD 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  341 PLAQQPGTVKPPVQPpgtTKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPAK---------PP 411
Cdd:COG5180   236 PPSTSEARSRPATVD---AQPEMRPPADAKERRRAAIGDTPAAEPPGLPVLEAGSEPQSDAPEAETARPidvkgvasaPP 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  412 TQQVGTPKPLAQQPGLQ-------SPAKAPgPTKTPVQQPGPGKIPAQQAGPGK------TSAQQTGPTKPPSQLPGPAK 478
Cdd:COG5180   313 ATRPVRPPGGARDPGTPrpgqpteRPAGVP-EAASDAGQPPSAYPPAEEAVPGKpleqgaPRPGSSGGDGAPFQPPNGAP 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  479 PPPQQPGPAKPPPQQPG-SAKPPSQQPGSTKPPPQQPGpakpspQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQ----Q 553
Cdd:COG5180   392 QPGLGRRGAPGPPMGAGdLVQAALDGGGRETASLGGAA------GGAGQGPKADFVPGDAESVSGPAGLADQAGAaastA 465
                         330       340
                  ....*....|....*....|....*
gi 150170670  554 STKPVSQTGSGKPLQPPTVSPSAKQ 578
Cdd:COG5180   466 MADFVAPVTDATPVDVADVLGVRPD 490
C2B_Synaptotagmin-17 cd08410
C2 domain second repeat present in Synaptotagmin 17; Synaptotagmin is a membrane-trafficking ...
4696-4819 1.93e-11

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: 64.53  E-value: 1.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4696 GEIQLQINY--DLGNLIIHILQARNLVPRDNNGYSDPFVKVYLLPGrgqVMVVQNASAEYKRRTkhvqksLNPEWNQTVI 4773
Cdd:cd08410     1 GELLLSLNYlpSAGRLNVDIIRAKQLLQTDMSQGSDPFVKIQLVHG---LKLIKTKKTSCMRGT------IDPFYNESFS 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 150170670 4774 YKsISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSTSHLDNT 4819
Cdd:cd08410    72 FK-VPQEELENVSLVFTVYGHNVKSSNDFIGRIVIGQYSSGPSETN 116
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
225-589 2.01e-11

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 70.97  E-value: 2.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  225 PGRDPLQQDGTPKSISSQQPEKIKS-QPPGTGKPIQGPTQTPQTDHAklPLQRDASRPQTKQAdivRGESVKPSLPSPSK 303
Cdd:PHA03307   73 PGPGTEAPANESRSTPTWSLSTLAPaSPAREGSPTPPGPSSPDPPPP--TPPPASPPPSPAPD---LSEMLRPVGSPGPP 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  304 PPIQQPTPGKPPAQQPGHEKSQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGS----- 378
Cdd:PHA03307  148 PAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPapgrs 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  379 ------EKPSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQ--QVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIP 450
Cdd:PHA03307  228 aaddagASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRiwEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGP 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  451 AqqAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPgSAKPPSQQPGSTKPPPQQPGPAKPSPQqpgstkPP 530
Cdd:PHA03307  308 A--PSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSR-SPSPSRPPPPADPSSPRKRPRPSRAPS------SP 378
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670  531 SQQPGSAKPSAQQPSPAkPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPSQGLPKTIC 589
Cdd:PHA03307  379 AASAGRPTRRRARAAVA-GRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPLLTPS 436
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
401-590 2.53e-11

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 70.29  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  401 PAQQPGPAKPPTQQ---VGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTS---AQQTGPTKPPSQLP 474
Cdd:PRK12323  365 PGQSGGGAGPATAAaapVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSpapEALAAARQASARGP 444
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  475 GPAKPPPQQPGPAkPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPG---SAKPSAQQPSPAKPSA 551
Cdd:PRK12323  445 GGAPAPAPAPAAA-PAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPefaSPAPAQPDAAPAGWVA 523
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 150170670  552 QQSTKP-VSQTGSGKPLQPPTVSPSAKQPPSQGLPKTICP 590
Cdd:PRK12323  524 ESIPDPaTADPDDAFETLAPAPAAAPAPRAAAATEPVVAP 563
PHA03247 PHA03247
large tegument protein UL36; Provisional
351-575 2.83e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 70.74  E-value: 2.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  351 PPVQPPGTTKPPAQPLGPAKPPAqqtgseKPSSEQPGPKAlAQPPGV------GKTPAQQPGPAKPPTQQVGTPKPLAQQ 424
Cdd:PHA03247  258 PPVVGEGADRAPETARGATGPPP------PPEAAAPNGAA-APPDGVwgaalaGAPLALPAPPDPPPPAPAGDAEEEDDE 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  425 PG---LQSPAKAPG------------PTKTP---VQQPGPGKIPAQQAGPGKTSAQQTGPTKPP--SQLPGPAKPPPQQP 484
Cdd:PHA03247  331 DGameVVSPLPRPRqhyplgfpkrrrPTWTPpssLEDLSAGRHHPKRASLPTRKRRSARHAATPfaRGPGGDDQTRPAAP 410
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  485 GPAKPPpqQPGSAKPPSQQPgstkPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPakpsAQQSTKPVSQTGSG 564
Cdd:PHA03247  411 VPASVP--TPAPTPVPASAP----PPPATPLPSAEPGSDDGPAPPPERQPPAPATEPAPDDP----DDATRKALDALRER 480
                         250
                  ....*....|.
gi 150170670  565 KPLQPPTVSPS 575
Cdd:PHA03247  481 RPPEPPGADLA 491
C2_ArfGAP cd04038
C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating ...
4706-4810 4.00e-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: 63.88  E-value: 4.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4706 LGNLIIHILQARNLVPRDNNGySDPFVKVYLlpgrgqvmvvqnasAEYKRRTKHVQKSLNPEWNQTVIYKSISMEQLkkk 4785
Cdd:cd04038     1 LGLLKVRVVRGTNLAVRDFTS-SDPYVVLTL--------------GNQKVKTRVIKKNLNPVWNEELTLSVPNPMAP--- 62
                          90       100
                  ....*....|....*....|....*
gi 150170670 4786 tLEVTVWDYDRFSSNDFLGEVLIDL 4810
Cdd:cd04038    63 -LKLEVFDKDTFSKDDSMGEAEIDL 86
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
309-549 5.03e-11

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 69.49  E-value: 5.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  309 PTPGKPPAQQPGhekSQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQPpgtTKPPAQPLGPAKPPAQQTGSEKPSSEQPGP 388
Cdd:PRK07003  367 APGGGVPARVAG---AVPAPGARAAAAVGASAVPAVTAVTGAAGAAL---APKAAAAAAATRAEAPPAAPAPPATADRGD 440
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  389 KALAQPPGVgKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTK---TPVQQPGPGKIPAQQAGPGKTSAQQTG 465
Cdd:PRK07003  441 DAADGDAPV-PAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAfepAPRAAAPSAATPAAVPDARAPAAASRE 519
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  466 PTKPPSQLPGPAKPPPQqPGPAKPPPQQ-------------------------PGSAKPPSQQPGSTKPPPQQPGPAKPS 520
Cdd:PRK07003  520 DAPAAAAPPAPEARPPT-PAAAAPAARAggaaaaldvlrnagmrvssdrgaraAAAAKPAAAPAAAPKPAAPRVAVQVPT 598
                         250       260
                  ....*....|....*....|....*....
gi 150170670  521 PQQPGSTKPPSQQPGSAKPSAQQPSPAKP 549
Cdd:PRK07003  599 PRARAATGDAPPNGAARAEQAAESRGAPP 627
PRK10263 PRK10263
DNA translocase FtsK; Provisional
429-585 5.50e-11

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 69.73  E-value: 5.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  429 SPAKA---PGPTKtPVQQPG--PGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPgpAKPPPQQPGSAKPPSQQ 503
Cdd:PRK10263  730 SPMKAlldDGPHE-PLFTPIvePVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQP--QYQQPQQPVAPQPQYQQ 806
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  504 PGStkppPQQPGPAKPSPQQPGSTKPPSQQPgsakpsaQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVS-PS---AKQP 579
Cdd:PRK10263  807 PQQ----PVAPQPQYQQPQQPVAPQPQYQQP-------QQPVAPQPQDTLLHPLLMRNGDSRPLHKPTTPlPSldlLTPP 875

                  ....*.
gi 150170670  580 PSQGLP 585
Cdd:PRK10263  876 PSEVEP 881
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
308-570 7.18e-11

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 69.11  E-value: 7.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  308 QPTPGKPPAQQPGHEKSQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQPPGTTKP-PAQPLGPAKPPAQQTGSEKPSSEQP 386
Cdd:PRK07003  359 EPAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPkAAAAAAATRAEAPPAAPAPPATADR 438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  387 GPKALAQPPGVgktPAQQPGPAKPPTQqvgtPKPLAQQPGLQSPAKAPGPTKTPvqqPGPGKIPAQQAGPGKTS-AQQTG 465
Cdd:PRK07003  439 GDDAADGDAPV---PAKANARASADSR----CDERDAQPPADSGSASAPASDAP---PDAAFEPAPRAAAPSAAtPAAVP 508
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  466 PTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPG---------------STKPPPQQPGPAKPSPQQPGSTKPP 530
Cdd:PRK07003  509 DARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAGGaaaaldvlrnagmrvSSDRGARAAAAAKPAAAPAAAPKPA 588
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 150170670  531 SQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPP 570
Cdd:PRK07003  589 APRVAVQVPTPRARAATGDAPPNGAARAEQAAESRGAPPP 628
C2_KIAA0528-like cd08688
C2 domain found in the Human KIAA0528 cDNA clone; The members of this CD are named after the ...
4711-4825 7.36e-11

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: 61.94  E-value: 7.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4711 IHILQARNL-VPRDNNGYSDPFVKVYLlpgrgqvmvvqnASAEYKrrTKHVQKSLNPEWNQTVIYKSISMEQLKKKTLEV 4789
Cdd:cd08688     3 VRVVAARDLpVMDRSSDLTDAFVEVKF------------GSTTYK--TDVVKKSLNPVWNSEWFRFEVDDEELQDEPLQI 68
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 150170670 4790 TVWDYDRFSSNDFLGEVLIDLSSTSHLDNTPR---WYPL 4825
Cdd:cd08688    69 RVMDHDTYSANDAIGKVYIDLNPLLLKDSVSQisgWFPI 107
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
307-587 7.69e-11

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: 69.03  E-value: 7.69e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   307 QQPTPGKPPAQQpghekSQPGPAKPPAQPSGLTKPLAQqpgtvkpPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPsseqp 386
Cdd:pfam03154  164 QQILQTQPPVLQ-----AQSGAASPPSPPPPGTTQAAT-------AGPTPSAPSVPPQGSPATSQPPNQTQSTAA----- 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   387 gPKALAQPpGVGKTPAQQPGPaKPPTQQVGTPKPlaqqPGLQSPAKAPGPTKTPVQQPGPGKIpaqqagpgktsaqQTGP 466
Cdd:pfam03154  227 -PHTLIQQ-TPTLHPQRLPSP-HPPLQPMTQPPP----PSQVSPQPLPQPSLHGQMPPMPHSL-------------QTGP 286
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   467 TKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTkpPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSP 546
Cdd:pfam03154  287 SHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHT--PPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIP 364
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670   547 AKPSAQQSTKPVSQTGSgKPLQ-------PPTVS----------PSAKQPPSQGLPKT 587
Cdd:pfam03154  365 QLPNPQSHKHPPHLSGP-SPFQmnsnlppPPALKplsslsthhpPSAHPPPLQLMPQS 421
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
337-582 1.01e-10

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: 68.26  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  337 GLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSE-KPSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQqv 415
Cdd:NF033839  278 GLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEvKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVK-- 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  416 gtPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPgKTSAQQTGPTKPPSQLPGPAKPPPQqpgpAKPPPQQPG 495
Cdd:NF033839  356 --PQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKP-KPEVKPQPEKPKPEVKPQPEKPKPE----VKPQPEKPK 428
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  496 SAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQStKPvsQTGSGKPLQPPTVSPS 575
Cdd:NF033839  429 PEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNS-KP--QADDKKPSTPNNLSKD 505

                  ....*..
gi 150170670  576 aKQPPSQ 582
Cdd:NF033839  506 -KQPSNQ 511
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
225-538 1.09e-10

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: 68.64  E-value: 1.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   225 PGRDPLQQDGTPKSISSQ--QPEKIKSQPPGTGKPIQ-GPTQTPQtdhaKLPLQRDASRPQTKQADIVRGESVKPSLPSP 301
Cdd:pfam03154  247 PPLQPMTQPPPPSQVSPQplPQPSLHGQMPPMPHSLQtGPSHMQH----PVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQ 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   302 SKPPiQQPTPGKPPAQQPGHEksQPGPAKPPAQPSglTKPlaqQPGTVKPPVQPPGTTKPPAQPLGPAK---------PP 372
Cdd:pfam03154  323 QRIH-TPPSQSQLQSQQPPRE--QPLPPAPLSMPH--IKP---PPTTPIPQLPNPQSHKHPPHLSGPSPfqmnsnlppPP 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   373 AQQTGSEKPSSEQPGpkalAQPPGVGKTPAQQ---PGPAKPP--TQQVGTPKPLAQQPGL----QSPAKAPGPTKtPVQQ 443
Cdd:pfam03154  395 ALKPLSSLSTHHPPS----AHPPPLQLMPQSQqlpPPPAQPPvlTQSQSLPPPAASHPPTsglhQVPSQSPFPQH-PFVP 469
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   444 PGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPakpspqQ 523
Cdd:pfam03154  470 GGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSP------E 543
                          330
                   ....*....|....*
gi 150170670   524 PGSTKPPSQQPGSAK 538
Cdd:pfam03154  544 PTVVNTPSHASQSAR 558
PHA03247 PHA03247
large tegument protein UL36; Provisional
311-522 1.63e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 68.43  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  311 PGKPPAQQPGHEKSqPGPAKPPAQPSGLTKPLAQQPGTVKPP----VQPPGTtkPPAQPLGPAKPPAQQTGSEKPSSEQP 386
Cdd:PHA03247  255 PAPPPVVGEGADRA-PETARGATGPPPPPEAAAPNGAAAPPDgvwgAALAGA--PLALPAPPDPPPPAPAGDAEEEDDED 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  387 GPKALAQPpgVGKTPAQQPGPAKPPTQQVGTPKPLAQQ--PGLQSPAKAPGPT---------KTPVQQPGPGKIPAQQAG 455
Cdd:PHA03247  332 GAMEVVSP--LPRPRQHYPLGFPKRRRPTWTPPSSLEDlsAGRHHPKRASLPTrkrrsarhaATPFARGPGGDDQTRPAA 409
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670  456 PGKTSAqqtgPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQ 522
Cdd:PHA03247  410 PVPASV----PTPAPTPVPASAPPPPATPLPSAEPGSDDGPAPPPERQPPAPATEPAPDDPDDATRK 472
PTZ00121 PTZ00121
MAEBL; Provisional
1157-1700 1.93e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.86  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1157 VKKQEQEVKTEAEkvilEKVKETLSMEKIPPMVTTDQKQEESKLEKDKASALQEKKPLPEEKKLiPEEEKIRSEEKKPLL 1236
Cdd:PTZ00121 1320 AKKKAEEAKKKAD----AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK-ADAAKKKAEEKKKAD 1394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1237 EEKKPTPEDKKLLPEAKTSAPEEQKHDLLKSQvqiAEEKLEGRVAPKTVQEGKQP-QTKMEGLPSGTPQSLPKEDDKTTK 1315
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKK---AEEKKKADEAKKKAEEAKKAdEAKKKAEEAKKAEEAKKKAEEAKK 1471
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1316 TIKEQPQPPCTAKPDQVEPGKEKTEKEDDKSDTSSSQQPKSPQGL-SDTGYSSDGI--------------------SSSL 1374
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKkAEEAKKADEAkkaeeakkadeakkaeekkkADEL 1551
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1375 GEIPSLIPTDEKDILKGLKKDSFSQESSPSSPSDLAKLESTVLSILEAQASTLADEKSE--KKTQPHEVSPEQPKDQEKT 1452
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEeaKKAEEAKIKAEELKKAEEE 1631
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1453 QSLSETLEITISEEEIKESQEERKDTFKK-DSQQDIPSSKDHKEKSEfvddiTTRREPYDSVEESSESENSPvPQRKRRT 1531
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKiKAAEEAKKAEEDKKKAE-----EAKKAEEDEKKAAEALKKEA-EEAKKAE 1705
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1532 SVGSSSSDEYKQEDSQGSGEEEDFIRKQIIEMSADEDASGSED---DEFIRNQLKEISSSTESQKKEETKGKGKITAGKH 1608
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEakkDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1609 RRltrksstsidEDAGRRHSWHDEDDEAFDESPELK------------YRETKSQESEELVVTGGGGLRRFKTIELNSTI 1676
Cdd:PTZ00121 1786 DE----------EDEKRRMEVDKKIKDIFDNFANIIeggkegnlvindSKEMEDSAIKEVADSKNMQLEEADAFEKHKFN 1855
                         570       580       590
                  ....*....|....*....|....*....|
gi 150170670 1677 ADKYSAESSQ------KKTSLYFDEEPELE 1700
Cdd:PTZ00121 1856 KNNENGEDGNkeadfnKEKDLKEDDEEEIE 1885
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 ...
4510-4587 2.07e-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: 2.07e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670 4510 GNGLGIRIVGGKEIPghSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEE-VQSIISQQSGEAEICVR 4587
Cdd:cd06759    11 GKGLGFSIVGGRDSP--RGPMGIYVKTIFPGGAAAEDGRLKEGDEILEVNGESLQGLTHQEaIQKFKQIKKGLVVLTVR 87
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
306-531 2.64e-10

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 63.85  E-value: 2.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   306 IQQPTPGKPPAQQPGhEKSQPGPAKPPAQPSGL-------TKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGS 378
Cdd:pfam15822   18 VSNPKPGQPPQGWPG-SNPWNNPSAPPAVPSGLppstapsTVPFGPAPTGMYPSIPLTGPSPGPPAPFPPSGPSCPPPGG 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   379 EKPSSEQPGPKAlaqppgvgktpaqqPGPAKPPTQQVgtpkplaqqPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGk 458
Cdd:pfam15822   97 PYPAPTVPGPGP--------------IGPYPTPNMPF---------PELPRPYGAPTDPAAAAPSGPWGSMSSGPWAPG- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   459 TSAQQTGPTKP-PSQLPGPAKPPPQQPGPAKPPPQ---QPGSAKPPSQQP---GSTKPPPQQPGPAKPSPQQPGSTKPPS 531
Cdd:pfam15822  153 MGGQYPAPNMPyPSPGPYPAVPPPQSPGAAPPVPWgtvPPGPWGPPAPYPdptGSYPMPGLYPTPNNPFQVPSGPSGAPP 232
PHA03377 PHA03377
EBNA-3C; Provisional
316-582 3.50e-10

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 67.00  E-value: 3.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  316 AQQPGHEKSQPGPAKPPAQPS--------GLTKPLAQQPgtvkPPVQPPGTTKPPAQPLGPAKPPA------------QQ 375
Cdd:PHA03377  443 AEQAQSTPERPGPSDQPSVPVepahltpvEHTTVILHQP----PQSPPTVAIKPAPPPSRRRRGACvvydddiievidVE 518
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  376 TGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAqqag 455
Cdd:PHA03377  519 TTEEEESVTQPAKPHRKVQDGFQRSGRRQKRATPPKVSPSDRGPPKASPPVMAPPSTGPRVMATPSTGPRDMAPPS---- 594
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  456 pgktsaqqtgpTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPP--------SQQPGSTKPPPQQPGPAKPSPQQPGST 527
Cdd:PHA03377  595 -----------TGPRQQAKCKDGPPASGPHEKQPPSSAPRDMAPSvvrmflreRLLEQSTGPKPKSFWEMRAGRDGSGIQ 663
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670  528 KPPSQQPGsakpSAQQPSPAKPSAQQS--TKPVSQTGSGKPLQPPTVSP-SAKQPPSQ 582
Cdd:PHA03377  664 QEPSSRRQ----PATQSTPPRPSWLPSvfVLPSVDAGRAQPSEESHLSSmSPTQPISH 717
PHA03377 PHA03377
EBNA-3C; Provisional
251-549 5.30e-10

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 66.23  E-value: 5.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  251 PPGTGKPIQGPTQTPQTDHAKLPLQRDASRPQTKQADIVRGESVKPSLPSP--SKPPIQQPTPGKPPA------------ 316
Cdd:PHA03377  582 TPSTGPRDMAPPSTGPRQQAKCKDGPPASGPHEKQPPSSAPRDMAPSVVRMflRERLLEQSTGPKPKSfwemragrdgsg 661
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  317 -QQPGHEKSQPGPAKPPAQPSGLtkplaqqPGTVKPPVQPPGTTKPPAQ----PLGPAKPPAQqtgSEKPSSEQP-GPKA 390
Cdd:PHA03377  662 iQQEPSSRRQPATQSTPPRPSWL-------PSVFVLPSVDAGRAQPSEEshlsSMSPTQPISH---EEQPRYEDPdDPLD 731
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  391 LAQPPGVGKTPAQQ---PGPAKPPTQQvgtpkplAQQPGLQSPAKAPGPTKTpVQQPGPGKIPAQQ----AGPGKTSAQQ 463
Cdd:PHA03377  732 LSLHPDQAPPPSHQapySGHEEPQAQQ-------APYPGYWEPRPPQAPYLG-YQEPQAQGVQVSSypgyAGPWGLRAQH 803
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  464 T---GPTKPPSQLPGPAKP-PPQQPGPAKPPPQQPGSAKPPSQQpgSTKPPPQQPGPAKPSPQQPGSTKPPSQQP--GSA 537
Cdd:PHA03377  804 PryrHSWAYWSQYPGHGHPqGPWAPRPPHLPPQWDGSAGHGQDQ--VSQFPHLQSETGPPRLQLSQVPQLPYSQTlvSSS 881
                         330
                  ....*....|..
gi 150170670  538 KPSAQQPSPAKP 549
Cdd:PHA03377  882 APSWSSPQPRAP 893
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
430-872 5.45e-10

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 66.25  E-value: 5.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  430 PAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQL-------PGPAK--PPPQQPGPAKPP--PQQPGSAK 498
Cdd:PTZ00449  510 PPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKegevgkkPGPAKehKPSKIPTLSKKPefPKDPKHPK 589
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  499 PPsQQPGSTKPP--PQQPgPAKPSPQQPGSTKPP--SQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTV-- 572
Cdd:PTZ00449  590 DP-EEPKKPKRPrsAQRP-TRPKSPKLPELLDIPksPKRPESPKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPpf 667
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  573 SPSAKQppsqglpkticplcnttELLLHVPEKAnfNTCTECQTTVCSLCGFNPNPHLTEVKEwlclncqmkralGGDLAP 652
Cdd:PTZ00449  668 DPKFKE-----------------KFYDDYLDAA--AKSKETKTTVVLDESFESILKETLPET------------PGTPFT 716
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  653 VPSSPQPKLKTAPVTTTSAVSKssPQPQQTSPKKDAAPKQDLSKAPEPKKPPPLvkqptLHGSPSAKAKQPP-EADSLSK 731
Cdd:PTZ00449  717 TPRPLPPKLPRDEEFPFEPIGD--PDAEQPDDIEFFTPPEEERTFFHETPADTP-----LPDILAEEFKEEDiHAETGEP 789
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  732 PAPPKEPSVPSEQDKAPVAdDKPKQPK-------MVKPTTDLVSSSSATTKPdiPSSKVQSQAEEKTTPPLKTDSAKPSQ 804
Cdd:PTZ00449  790 DEAMKRPDSPSEHEDKPPG-DHPSLPKkrhrldgLALSTTDLESDAGRIAKD--ASGKIVKLKRSKSFDDLTTVEEAEEM 866
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670  805 SfpPTGEKVSPFDSKAiprPASDSKiiSHPGPSSESKGQKQVDPVQKKEEPKKAQTKMSP-KPDAKPMP 872
Cdd:PTZ00449  867 G--AEARKIVVDDDGT---EADDED--THPPEEKHKSEVRRRRPPKKPSKPKKPSKPKKPkKPDSAFIP 928
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
453-901 6.21e-10

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 65.78  E-value: 6.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  453 QAGPGKTSAQQTGPtkPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQP-----GPAKPSPQQPGST 527
Cdd:PRK07764  386 GVAGGAGAPAAAAP--SAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAgnapaGGAPSPPPAAAPS 463
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  528 KPPSQQPGSAKPSAQQPSPAKPSAQQSTKPvsqtgsgkplQPPTVSPSAKQPPS-------------QGLPK-------- 586
Cdd:PRK07764  464 AQPAPAPAAAPEPTAAPAPAPPAAPAPAAA----------PAAPAAPAAPAGADdaatlrerwpeilAAVPKrsrktwai 533
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  587 -----TICPLCNTTELLLHV--PEKANFNtctecqttvcslcgfnpNPHLTEVkewlcLNCQMKRALGGDLAP-VPSSPQ 658
Cdd:PRK07764  534 llpeaTVLGVRGDTLVLGFStgGLARRFA-----------------SPGNAEV-----LVTALAEELGGDWQVeAVVGPA 591
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  659 PKLktAPVTTTSAVSKSSPQPQQTSPKKDAAPKQDlskapepkkppplvkqptlhgSPSAKAKQPPEADSLSKPAPPKEP 738
Cdd:PRK07764  592 PGA--AGGEGPPAPASSGPPEEAARPAAPAAPAAP---------------------AAPAPAGAAAAPAEASAAPAPGVA 648
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  739 SVPSEQDKAPVADdkpkqpkmvkpTTDLVSSSSATTKPDIPSSKVQSQAEekTTPPLKTDSAKPSQSFPPTGEKVSPFDS 818
Cdd:PRK07764  649 APEHHPKHVAVPD-----------ASDGGDGWPAKAGGAAPAAPPPAPAP--AAPAAPAGAAPAQPAPAPAATPPAGQAD 715
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  819 KAIPRPASDSKIISHPGPSSEskgqkqvDPVQKKEEPkkaqtkmsPKPDAKPMPKGSPTPPGPRPTAGQTVPTPQQSPKP 898
Cdd:PRK07764  716 DPAAQPPQAAQGASAPSPAAD-------DPVPLPPEP--------DDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPS 780

                  ...
gi 150170670  899 QEQ 901
Cdd:PRK07764  781 EEE 783
C2_fungal_Inn1p-like cd08681
C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 ...
4707-4826 8.94e-10

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: 59.18  E-value: 8.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4707 GNLIIHILQARNLVPRDNNGYSDPFVKVYLlpgrgqvmvvqnasAEYKRRTKHVQKS-LNPEWNQTV---IYKSismeql 4782
Cdd:cd08681     1 GTLVVVVLKARNLPNKRKLDKQDPYCVLRI--------------GGVTKKTKTDFRGgQHPEWDEELrfeITED------ 60
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 150170670 4783 KKKTLEVTVWDyDRFSSNDFLGEVLIDLSSTSHLDNTPRWYPLK 4826
Cdd:cd08681    61 KKPILKVAVFD-DDKRKPDLIGDTEVDLSPALKEGEFDDWYELT 103
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
4705-4815 1.18e-09

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 65.17  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4705 DLGNLIIHILQARNLVPRDNNGYSDPFVKVYLlpgrgqvmvvqnaSAEYKRRTKHVQKSLNPEWNQtviykSISMEQLKK 4784
Cdd:COG5038  1038 NSGYLTIMLRSGENLPSSDENGYSDPFVKLFL-------------NEKSVYKTKVVKKTLNPVWNE-----EFTIEVLNR 1099
                          90       100       110
                  ....*....|....*....|....*....|...
gi 150170670 4785 KT--LEVTVWDYDRFSSNDFLGEVLIDLSSTSH 4815
Cdd:COG5038  1100 VKdvLTINVNDWDSGEKNDLLGTAEIDLSKLEP 1132
C2B_Munc13 cd04027
C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins; C2-like domains are ...
4709-4830 1.28e-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: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4709 LIIHILQARNLVPRDNNGYSDPFVKVyllpgrgQVmvvqnasAEYKRRTKHVQKSLNPEWNQTVIYK-SISMEQLKkktl 4787
Cdd:cd04027     3 ISITVVCAQGLIAKDKTGTSDPYVTV-------QV-------GKTKKRTKTIPQNLNPVWNEKFHFEcHNSSDRIK---- 64
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 150170670 4788 eVTVWDYD---------RFS--SNDFLGEVLIDLSSTS-HLDntpRWYPLKEQTE 4830
Cdd:cd04027    65 -VRVWDEDddiksrlkqKFTreSDDFLGQTIIEVRTLSgEMD---VWYNLEKRTD 115
PRK10263 PRK10263
DNA translocase FtsK; Provisional
241-586 1.59e-09

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 64.72  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  241 SQQPEkIKSQP---PGTGKPIQGP---TQTPQTDHAKL------PLQRDASRPQTKQADIVRGESVKPSLPSPSKPPIQQ 308
Cdd:PRK10263  353 PAQPT-VAWQPvpgPQTGEPVIAPapeGYPQQSQYAQPavqynePLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQ 431
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  309 PTPGKPPAQQPGHEKSQPGPAKPPAQP-------SGLTKPLAQQPGTVKPPVQPPGTT---KPPAQPLGPAKPPAQ--QT 376
Cdd:PRK10263  432 PYYAPAPEQPVAGNAWQAEEQQSTFAPqstyqteQTYQQPAAQEPLYQQPQPVEQQPVvepEPVVEETKPARPPLYyfEE 511
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  377 GSEKPSSE--------QPGPKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQ-----------QPGLQSPAKAPGPT 437
Cdd:PRK10263  512 VEEKRAREreqlaawyQPIPEPVKEPEPIKSSLKAPSVAAVPPVEAAAAVSPLASgvkkatlatgaAATVAAPVFSLANS 591
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  438 KTPVQQ---------PGPG---------------KIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQ- 492
Cdd:PRK10263  592 GGPRPQvkegigpqlPRPKrirvptrrelasygiKLPSQRAAEEKAREAQRNQYDSGDQYNDDEIDAMQQDELARQFAQt 671
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  493 -------------------------------------------QPGSAKP-------------------------PSQQP 504
Cdd:PRK10263  672 qqqrygeqyqhdvpvnaedadaaaeaelarqfaqtqqqrysgeQPAGANPfslddfefspmkallddgpheplftPIVEP 751
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  505 GSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQ------PSPAKPSAQQSTKPVS-QTGSGKPLQPPTVSPSAK 577
Cdd:PRK10263  752 VQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQyqqpqqPVAPQPQYQQPQQPVApQPQYQQPQQPVAPQPQYQ 831

                  ....*....
gi 150170670  578 QPPSQGLPK 586
Cdd:PRK10263  832 QPQQPVAPQ 840
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
308-579 3.48e-09

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 63.02  E-value: 3.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  308 QPTPGKPPAQQPGHEKSQPGPAKPPAQpsgLTKPLAqqPGTVKPPVQPPgTTKPPAQPLGPAKPPAQQTGSEKPSSEQPG 387
Cdd:PLN03209  340 KPVPTKPVTPEAPSPPIEEEPPQPKAV---VPRPLS--PYTAYEDLKPP-TSPIPTPPSSSPASSKSVDAVAKPAEPDVV 413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  388 PKAlAQPPGVgktPAQQPGPAkpPTQQVGTPKPLAQQPGLQSPAkAPGPTKtpvqqPGPGKIPAQQAgpgkTSAQQTGPT 467
Cdd:PLN03209  414 PSP-GSASNV---PEVEPAQV--EAKKTRPLSPYARYEDLKPPT-SPSPTA-----PTGVSPSVSST----SSVPAVPDT 477
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  468 KPPSQLPGPAKPPPQQPGPAKPPPQQpGSAKPPsqqpgsTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPA 547
Cdd:PLN03209  478 APATAATDAAAPPPANMRPLSPYAVY-DDLKPP------TSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQP 550
                         250       260       270
                  ....*....|....*....|....*....|..
gi 150170670  548 KPsaqqstKPVSQTGSGKPLQPPTvSPSAKQP 579
Cdd:PLN03209  551 KP------RPLSPYTMYEDLKPPT-SPTPSPV 575
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
314-467 4.36e-09

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 62.97  E-value: 4.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  314 PPAQQPGHEKSQPGPAKPPAQPSGltkPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQ 393
Cdd:PRK12323  434 AAARQASARGPGGAPAPAPAPAAA---PAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPA 510
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670  394 PpgvgktpaQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPT 467
Cdd:PRK12323  511 P--------AQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDM 576
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
445-595 4.45e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 62.74  E-value: 4.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  445 GPGKIPAQQAGPGKTSAQQTGPTKPPSqlPGPAKPPPQQPGpAKPPPQQPGSAKPPSQQPGSTKP-------PPQQPGPA 517
Cdd:COG5164     5 GPGKTGPSDPGGVTTPAGSQGSTKPAQ--NQGSTRPAGNTG-GTRPAQNQGSTTPAGNTGGTRPAgnqgatgPAQNQGGT 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670  518 KPsPQQPGSTKPPSQQPGSaKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPSQGLPKTICPLCNTT 595
Cdd:COG5164    82 TP-AQNQGGTRPAGNTGGT-TPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDGGSTPPGPGSTGPGGSTT 157
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
649-1010 4.81e-09

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 63.27  E-value: 4.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  649 DLAPVPSSPQPklktAPVTTTSAVSKSSPQPQQTSPKKDAAPKQDLSKAPEPKKPPPLVKQPTLHGSPSakakqPPEADS 728
Cdd:PHA03307   63 DRFEPPTGPPP----GPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPP-----PSPAPD 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  729 LSKPAPPKEPSVPSEQDKAPVADDKPKQPkmvkpTTDLVSSSSATTKPDIPSSKVQSQAEEKTTPPLKTDSAKPSQSFPP 808
Cdd:PHA03307  134 LSEMLRPVGSPGPPPAASPPAAGASPAAV-----ASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPR 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  809 TGEKVSPFDSKAIPRPASDSKIISHPGPSSESKGQKQVdpvqKKEEPKKAQTKMSPKPDAKPMPKGSPTPPGPRPTAGQT 888
Cdd:PHA03307  209 RSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSG----CGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGP 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  889 V----PTPQQSPKPQEqsrrfslnlgsitDAPKSQPTTPQETVTGKLFGfgasifSQASNLISTAgqPGPHSQSGPGAPm 964
Cdd:PHA03307  285 AssssSPRERSPSPSP-------------SSPGSGPAPSSPRASSSSSS------SRESSSSSTS--SSSESSRGAAVS- 342
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 150170670  965 kQAPAPSQPPTSQGPPKSTgqAPPAPAKSIPVKKETKAPAAEKLEP 1010
Cdd:PHA03307  343 -PGPSPSRSPSPSRPPPPA--DPSSPRKRPRPSRAPSSPAASAGRP 385
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
421-550 5.32e-09

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 62.81  E-value: 5.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  421 LAQQPGLQSPAKAPGPTKTPVQ--QPGPGKIPAQQAGPGKTSAQ-QTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSA 497
Cdd:PRK14951  362 LAFKPAAAAEAAAPAEKKTPARpeAAAPAAAPVAQAAAAPAPAAaPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAA 441
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 150170670  498 KPPSQQPGSTKPPPQQPGPAKPSPQQPGstkPPSQQPGSAKPSAQQPSPAKPS 550
Cdd:PRK14951  442 PAAVALAPAPPAQAAPETVAIPVRVAPE---PAVASAAPAPAAAPAAARLTPT 491
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
4511-4577 5.87e-09

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


Pssm-ID: 467254 [Multi-domain]  Cd Length: 87  Bit Score: 56.07  E-value: 5.87e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670 4511 NGLGIRIVGGKEIPGHSGeiGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQ 4577
Cdd:cd06792    12 GSLGISVTGGINTSVRHG--GIYVKSLVPGGAAEQDGRIQKGDRLLEVNGVSLEGVTHKQAVECLKN 76
PDZ2_PDZD2-like cd06758
PDZ domain 2 of PDZ domain containing 2 (PDZD2), and related domains; PDZ (PSD-95 ...
4504-4580 6.21e-09

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


Pssm-ID: 467239 [Multi-domain]  Cd Length: 88  Bit Score: 55.82  E-value: 6.21e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670 4504 KDHTVSGN-GLGIRIVGGKEipGHSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSG 4580
Cdd:cd06758     4 KMHLLKEKgGLGIQITGGKG--SKRGDIGIFVAGVEEGGSADRDGRLKKGDELLMINGQSLIGLSHQEAVAILRSSAS 79
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
251-530 6.76e-09

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 62.56  E-value: 6.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  251 PPGTGKPIQGPTQTPqtdhaklplqrdASRPQtkqADIVRGESVKPSLPSPSKPPIQQPTPgKPPAQQPGHEKSQPGPAK 330
Cdd:PRK07003  367 APGGGVPARVAGAVP------------APGAR---AAAAVGASAVPAVTAVTGAAGAALAP-KAAAAAAATRAEAPPAAP 430
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  331 PPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPAKP 410
Cdd:PRK07003  431 APPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDA 510
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  411 PTQQVgtpkplAQQPGLQSPAKAPGPTKTPvQQPGPGKIPAQQAGPG-----------KTSAQQTGPTkppsqlPGPAKP 479
Cdd:PRK07003  511 RAPAA------ASREDAPAAAAPPAPEARP-PTPAAAAPAARAGGAAaaldvlrnagmRVSSDRGARA------AAAAKP 577
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 150170670  480 PPQQPGPAKPPPQQPGSAKPPSQQPGSTkpPPQQPGPAKPSPQQPGSTKPP 530
Cdd:PRK07003  578 AAAPAAAPKPAAPRVAVQVPTPRARAAT--GDAPPNGAARAEQAAESRGAP 626
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
322-583 8.23e-09

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 61.46  E-value: 8.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  322 EKSQPGPAKP--------PAQPSGLTKPlaQQPGTVKPPVQPPGTTKP-----PAQPLGPAKPPAQQtGSEKPSSE--QP 386
Cdd:NF038329  118 EKGEPGPAGPagpageqgPRGDRGETGP--AGPAGPPGPQGERGEKGPagpqgEAGPQGPAGKDGEA-GAKGPAGEkgPQ 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  387 GPKALAQPPGvGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPT-----KTPVQQPGPGKIPAQQAGPGKT-- 459
Cdd:NF038329  195 GPRGETGPAG-EQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTgedgpQGPDGPAGKDGPRGDRGEAGPDgp 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  460 --SAQQTGPTKPPSQ--------LPGPAKPPPQQPGPAKP-------PPQQPGSAKPPSQ--QPGstKPPPQQPG-PAKP 519
Cdd:NF038329  274 dgKDGERGPVGPAGKdgqngkdgLPGKDGKDGQNGKDGLPgkdgkdgQPGKDGLPGKDGKdgQPG--KPAPKTPEvPQKP 351
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150170670  520 SpQQPGSTKPPsQQPGSAKPSAqqPSPAKPSAQQSTKPvsQTGSGKPL-QPPTVSPSAKQPPSQG 583
Cdd:NF038329  352 D-TAPHTPKTP-QIPGQSKDVT--PAPQNPSNRGLNKP--QTQGGNQLaKTPAAHDTHRQLPATG 410
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
4493-4575 1.04e-08

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


Pssm-ID: 467159 [Multi-domain]  Cd Length: 96  Bit Score: 55.40  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4493 PHARIKITRDSkdhtvsGNGLGIRIVGGKEIPGH--SGEI--GAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTY 4568
Cdd:cd06671     1 PPRRVELWREP------GKSLGISIVGGRVMGSRlsNGEEirGIFIKHVLEDSPAGRNGTLKTGDRILEVNGVDLRNATH 74

                  ....*..
gi 150170670 4569 EEVQSII 4575
Cdd:cd06671    75 EEAVEAI 81
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
663-992 1.04e-08

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 62.01  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  663 TAPVTTTSAVSKSSPQPQQTSPKKDAAPKQDLSKAPEPKKPPPLVKQPTLHGSPSAKAKQPPEADSLSKPAPPKEPSVPS 742
Cdd:PTZ00449  522 KAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKKPKRPR 601
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  743 EQDKaPVADDKPKQPKMvkptTDLVSSSSATTKPDIPSSKVQSQaeeKTTPPLKTDSAK-PSQSFPPTGEKVsPFDSK-- 819
Cdd:PTZ00449  602 SAQR-PTRPKSPKLPEL----LDIPKSPKRPESPKSPKRPPPPQ---RPSSPERPEGPKiIKSPKPPKSPKP-PFDPKfk 672
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  820 -----AIPRPASDSKIISHPGPSSESkgQKQVDPVQKKEEPKKAQTKMSPKPDAKPMPKGSPTPPGPRPTAGQTVPTPQQ 894
Cdd:PTZ00449  673 ekfydDYLDAAAKSKETKTTVVLDES--FESILKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFF 750
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  895 SPkPQEQSRRFSlnlgsitdapKSQPTTPQETVTGKLFgfgasifsqasnlistaGQPGPHSQSG-PGAPMKQAPAPsqp 973
Cdd:PTZ00449  751 TP-PEEERTFFH----------ETPADTPLPDILAEEF-----------------KEEDIHAETGePDEAMKRPDSP--- 799
                         330
                  ....*....|....*....
gi 150170670  974 ptSQGPPKSTGQAPPAPAK 992
Cdd:PTZ00449  800 --SEHEDKPPGDHPSLPKK 816
C2_Kibra cd08680
C2 domain found in Human protein Kibra; Kibra is thought to be a regulator of the Salvador ...
4698-4825 1.29e-08

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: 56.09  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4698 IQLQINYDLGN--LIIHILQARN---LVPRDNngySDPFVKVYLLPGrgqvmvVQNASAEYkrRTKHVQKSLNPEWNqTV 4772
Cdd:cd08680     3 VQIGLRYDSGDssLVISVEQLRNlsaLSIPEN---SKVYVRVALLPC------SSSTSCLF--RTKALEDQDKPVFN-EV 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 150170670 4773 IYKSISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSTSHLDN-TPRWYPL 4825
Cdd:cd08680    71 FRVPISSTKLYQKTLQVDVCSVGPDQQEECLGGAQISLADFESSEEmSTKWYNL 124
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
4708-4812 1.40e-08

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: 55.73  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4708 NLIIHILQARNLVPRDNNGYSDPFVKVYLlPgrgqvmvvqNASAEyKRRTKHVQKSLNPEWNQTVIYKsISMEQlkKKTL 4787
Cdd:cd04036     1 LLTVRVLRATNITKGDLLSTPDCYVELWL-P---------TASDE-KKRTKTIKNSINPVWNETFEFR-IQSQV--KNVL 66
                          90       100
                  ....*....|....*....|....*
gi 150170670 4788 EVTVWDYDRFSSnDFLGEVLIDLSS 4812
Cdd:cd04036    67 ELTVMDEDYVMD-DHLGTVLFDVSK 90
dnaA PRK14086
chromosomal replication initiator protein DnaA;
351-566 1.49e-08

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 60.99  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  351 PPVQPPGTTKPPAQPLGPAKPPAQQTgsEKPSSEQPGPKALaqpPGVGKTPAQQPGPAKPPTQQVGTPKPLAqqPGLQSP 430
Cdd:PRK14086   80 RPIRIAITVDPSAGEPAPPPPHARRT--SEPELPRPGRRPY---EGYGGPRADDRPPGLPRQDQLPTARPAY--PAYQQR 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  431 AKaPGPTKTPvqqpgPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGS-AKPPSQQPGSTKP 509
Cdd:PRK14086  153 PE-PGAWPRA-----ADDYGWQQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDhPRPDWDRPRRDRT 226
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670  510 PpqQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPvsqtGSGKP 566
Cdd:PRK14086  227 D--RPEPPPGAGHVHRGGPGPPERDDAPVVPIRPSAPGPLAAQPAPAP----GPGEP 277
PDZ_SYNJ2BP-like cd06709
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ...
4497-4571 1.52e-08

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: 54.61  E-value: 1.52e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150170670 4497 IKITRDskdhtvsGNGLGIRIVGGKEIPGHSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEV 4571
Cdd:cd06709     3 ITLKRG-------PSGLGFNIVGGTDQPYIPNDSGIYVAKIKEDGAAAIDGRLQEGDKILEINGQSLENLTHQDA 70
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
307-550 1.54e-08

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 60.94  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  307 QQPTPGKPPAQQPGHEKSQPGPAKPPAQPSgltkplaQQPGTVKPPVQP-PGTTKPPAQPlGPAKPPAQQtgseKPSSEQ 385
Cdd:NF033839  304 QPEKKEVKPEPETPKPEVKPQLEKPKPEVK-------PQPEKPKPEVKPqLETPKPEVKP-QPEKPKPEV----KPQPEK 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  386 PGPKALAQPPGVGKTPAQQPGPAKPPTQqvgtPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPgKTSAQQTG 465
Cdd:NF033839  372 PKPEVKPQPETPKPEVKPQPEKPKPEVK----PQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKP-KPEVKPQP 446
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  466 PTKPPSQLPGPAKPPPQ-QPGPAKPPPQqpgsAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQP 544
Cdd:NF033839  447 EKPKPEVKPQPETPKPEvKPQPEKPKPE----VKPQPEKPKPDNSKPQADDKKPSTPNNLSKDKQPSNQASTNEKATNKP 522

                  ....*.
gi 150170670  545 SPAKPS 550
Cdd:NF033839  523 KKSLPS 528
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
4512-4586 1.79e-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: 54.30  E-value: 1.79e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150170670 4512 GLGIRIVGGKEipgHSGEIgaYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGEAEICV 4586
Cdd:cd06800    12 GLGISITGGKE---HGVPI--LISEIHEGQPADRCGGLYVGDAILSVNGIDLRDAKHKEAVTILSQQRGEITLEV 81
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
383-527 2.19e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 60.77  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  383 SEQPGPKALAQ---------PPGVGKTPAQQPGPakPPTQQVGTPKPLAQQPGLQSPAK-APGPTKTPVQQPGPGKIPAQ 452
Cdd:PRK07764  366 SASDDERGLLArlerlerrlGVAGGAGAPAAAAP--SAAAAAPAAAPAPAAAAPAAAAApAPAAAPQPAPAPAPAPAPPS 443
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150170670  453 QAGPGKTSAqqtgptkPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGST 527
Cdd:PRK07764  444 PAGNAPAGG-------APSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAAT 511
PRK10263 PRK10263
DNA translocase FtsK; Provisional
244-776 2.41e-08

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 60.87  E-value: 2.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  244 PEKIKSQPPGTGKPIQGPtQTPQTDHAKLPlqrDASRPQTKQADIVRGESVKPSLPSPSKPPIQQPTPGKPPaQQPGHEK 323
Cdd:PRK10263  349 VDVPPAQPTVAWQPVPGP-QTGEPVIAPAP---EGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPA-QQPYYAP 423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  324 SQPGPAKPPAQPSGLTKPLAQQPGTVKPPvQPPGTTKPPAQPLGPAKPPAQQTGSEKPsseqpgPKALAQPPGVGKTP-A 402
Cdd:PRK10263  424 APEQPAQQPYYAPAPEQPVAGNAWQAEEQ-QSTFAPQSTYQTEQTYQQPAAQEPLYQQ------PQPVEQQPVVEPEPvV 496
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  403 QQPGPAKPP--------TQQVGTPKPLAQ--QPgLQSPAKAPGPTKTPVQQPGPGKIP----AQQAGPGKTSAQQ----- 463
Cdd:PRK10263  497 EETKPARPPlyyfeeveEKRAREREQLAAwyQP-IPEPVKEPEPIKSSLKAPSVAAVPpveaAAAVSPLASGVKKatlat 575
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  464 ---TGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGST---KPPPQQPGPAKPSPQQPGSTKPPSQQPGSA 537
Cdd:PRK10263  576 gaaATVAAPVFSLANSGGPRPQVKEGIGPQLPRPKRIRVPTRRELASygiKLPSQRAAEEKAREAQRNQYDSGDQYNDDE 655
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  538 KPSAQQPSPAKP-SAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPSQGLPKTicplcNTTELLLHVPEKANFNTCTECQtt 616
Cdd:PRK10263  656 IDAMQQDELARQfAQTQQQRYGEQYQHDVPVNAEDADAAAEAELARQFAQT-----QQQRYSGEQPAGANPFSLDDFE-- 728
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  617 vcslcgFNPNPHLTEVKEWLCLNCQMKRALGGDLAPVPSSPQPKLKTAPVtttsavsksSPQPQQTSPKKDAAPKQDLSK 696
Cdd:PRK10263  729 ------FSPMKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPV---------APQPQYQQPQQPVAPQPQYQQ 793
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  697 APEPKKPPPLVKQPTLHGSPSAKAKQPPEADSLSKP-APPKEPSVPSEQDKA--PV----ADDKPKQ-PKMVKPTTDLVS 768
Cdd:PRK10263  794 PQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQyQQPQQPVAPQPQDTLlhPLlmrnGDSRPLHkPTTPLPSLDLLT 873

                  ....*...
gi 150170670  769 SSSATTKP 776
Cdd:PRK10263  874 PPPSEVEP 881
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
465-591 2.42e-08

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 60.50  E-value: 2.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  465 GPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAkPPSQQPGSTKPPPQQPGPAKPSP-QQPGSTKPPSQQPGSAKPSAQQ 543
Cdd:PRK14951  370 AEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPA-PAAAPAAAASAPAAPPAAAPPAPvAAPAAAAPAAAPAAAPAAVALA 448
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 150170670  544 PSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPSQGLPKTICPL 591
Cdd:PRK14951  449 PAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEGDV 496
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
4510-4586 2.61e-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: 2.61e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670 4510 GNGLGIRIVGGKEipghsGEiGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGEAEICV 4586
Cdd:cd06795    11 STGLGFNIVGGED-----GE-GIFISFILAGGPADLSGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTIIA 81
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
312-583 2.67e-08

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 60.47  E-value: 2.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  312 GKPPAQQPGHEKSQPGPAKPpAQPSGLtkplaqqPGTVKPPvQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKAL 391
Cdd:PTZ00449  547 GKPGETKEGEVGKKPGPAKE-HKPSKI-------PTLSKKP-EFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPEL 617
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  392 AQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKI------PAQQAGPGKTSAQQTG 465
Cdd:PTZ00449  618 LDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPKFKEKFyddyldAAAKSKETKTTVVLDE 697
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  466 PTKPPSQLPGPAKPPPQQPGPAKPPPQQPgsakppsQQPGSTKPPPQQPGPAKPSPQQPgSTKPPSQQPGSAKPSAQQPS 545
Cdd:PTZ00449  698 SFESILKETLPETPGTPFTTPRPLPPKLP-------RDEEFPFEPIGDPDAEQPDDIEF-FTPPEEERTFFHETPADTPL 769
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 150170670  546 PAKPSAQQSTKPV-SQTGS-GKPLQPPTvSPSAKQPPSQG 583
Cdd:PTZ00449  770 PDILAEEFKEEDIhAETGEpDEAMKRPD-SPSEHEDKPPG 808
C2_Rab11-FIP_classI cd08682
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ...
4713-4826 3.17e-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: 55.15  E-value: 3.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4713 ILQARNLVPRDNNGYSDPFVkvyllpgrgqvmVVQNASAEYkrRTKHVQKSLNPEWNQTVIYK--SISMEQLKKKTLEVT 4790
Cdd:cd08682     5 VLQARGLLCKGKSGTNDAYV------------IIQLGKEKY--STSVKEKTTSPVWKEECSFElpGLLSGNGNRATLQLT 70
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150170670 4791 VWDYDRFSSNDFLGEVLIDLSSTSHLDNTPR--WYPLK 4826
Cdd:cd08682    71 VMHRNLLGLDKFLGQVSIPLNDLDEDKGRRRtrWFKLE 108
PDZ1_MUPP1-like cd06689
PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
4478-4586 3.46e-08

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: 54.17  E-value: 3.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4478 EQIIQM--NGKTMHYIfphariKITRDSkdhtvsGNGLGIRIVGGKEipGHSGEIGAYIAKILPGGSAEQTGKLMEGMQV 4555
Cdd:cd06689     3 EQAIQSmaQGRQVEYI------ELEKPE------SGGLGFSVVGLKS--ENRGELGIFVQEIQPGSVAARDGRLKENDQI 68
                          90       100       110
                  ....*....|....*....|....*....|..
gi 150170670 4556 LEWNGIPL-TSKTYEEVQSIISQQSGEAEICV 4586
Cdd:cd06689    69 LAINGQPLdQSISHQQAIAILQQAKGSVELVV 100
C2B_Synaptotagmin-12 cd08406
C2 domain second repeat present in Synaptotagmin 12; Synaptotagmin is a membrane-trafficking ...
4696-4808 4.18e-08

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: 55.18  E-value: 4.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4696 GEIQLQINY--DLGNLIIHILQARNLVPRDNNGYSDPFVKVYLLpgrgqvmvvQNASAEYKRRTKHVQKSLNPEWNQTVI 4773
Cdd:cd08406     2 GEILLSLSYlpTAERLTVVVVKARNLVWDNGKTTADPFVKVYLL---------QDGRKISKKKTSVKRDDTNPIFNEAMI 72
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 150170670 4774 YkSISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLI 4808
Cdd:cd08406    73 F-SVPAIVLQDLSLRVTVAESTEDGKTPNVGHVII 106
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
4534-4580 4.72e-08

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: 53.04  E-value: 4.72e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 150170670 4534 IAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSG 4580
Cdd:cd06726    26 VARILHGGMAHRSGLLHVGDEILEINGIPVSGKTVDELQKLLSSLSG 72
PHA03377 PHA03377
EBNA-3C; Provisional
312-580 6.49e-08

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 59.30  E-value: 6.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  312 GKPPAQQPGHEKSQPGP-------AKPPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPP-AQPLGPAKPPAQQTGSEKPSS 383
Cdd:PHA03377  561 GPPKASPPVMAPPSTGPrvmatpsTGPRDMAPPSTGPRQQAKCKDGPPASGPHEKQPPsSAPRDMAPSVVRMFLRERLLE 640
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  384 EQPGPK--------------ALAQPPGVGKTPAQQPGPAKP---------PTQQVGTPKPL----------------AQQ 424
Cdd:PHA03377  641 QSTGPKpksfwemragrdgsGIQQEPSSRRQPATQSTPPRPswlpsvfvlPSVDAGRAQPSeeshlssmsptqpishEEQ 720
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  425 PGLQSPAKAPGPTKTPVQQPGPgkiPAQQAGPGKTSAQQTGPTKPPSQLPgpakPPPQQP--GPAKPPPQQ------PGS 496
Cdd:PHA03377  721 PRYEDPDDPLDLSLHPDQAPPP---SHQAPYSGHEEPQAQQAPYPGYWEP----RPPQAPylGYQEPQAQGvqvssyPGY 793
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  497 AKP---PSQQP---GSTKPPPQQPGPAKP-SPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQP 569
Cdd:PHA03377  794 AGPwglRAQHPryrHSWAYWSQYPGHGHPqGPWAPRPPHLPPQWDGSAGHGQDQVSQFPHLQSETGPPRLQLSQVPQLPY 873
                         330
                  ....*....|.
gi 150170670  570 PTVSPSAKQPP 580
Cdd:PHA03377  874 SQTLVSSSAPS 884
PHA03377 PHA03377
EBNA-3C; Provisional
352-550 6.60e-08

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 59.30  E-value: 6.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  352 PVQPPGTTKPPAQPLGPAKPPAQQTgsEKPSSEQPGPKALAQPPGVGKTPaqqPGPAKPP-TQQVGTPKPLAQQPGLQSP 430
Cdd:PHA03377  412 PWRKPRTLPWPTPKTHPVKRTLVKT--SGRSDEAEQAQSTPERPGPSDQP---SVPVEPAhLTPVEHTTVILHQPPQSPP 486
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  431 AKAPGPTKTPVQQPGPGKI-----------------------PAQQAGPGKTSAQQTGPTKPPSQLPgPAKPPPQQPGPA 487
Cdd:PHA03377  487 TVAIKPAPPPSRRRRGACVvydddiievidvetteeeesvtqPAKPHRKVQDGFQRSGRRQKRATPP-KVSPSDRGPPKA 565
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150170670  488 KPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPS 550
Cdd:PHA03377  566 SPPVMAPPSTGPRVMATPSTGPRDMAPPSTGPRQQAKCKDGPPASGPHEKQPPSSAPRDMAPS 628
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
4510-4586 6.63e-08

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: 53.04  E-value: 6.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4510 GNGLGIRIVGGK---EIPGHSGeigAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGEAEICV 4586
Cdd:cd06724     8 PKGLGFSIAGGVgnqHIPGDNG---IYVTKIIEGGAAQKDGRLQVGDKLLAVNDVSLEEVTHEEAVAALKNTSDVVYLKV 84
PDZ1_LNX1_2-like cd06677
PDZ domain 1 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
4497-4577 6.87e-08

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: 53.02  E-value: 6.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4497 IKITRDSKDhtvsgNGLGIRIVGGKEIPghsgEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIIS 4576
Cdd:cd06677     6 IEIHRSDPY-----EELGISIVGGNDTP----LINIVIQEVYRDGVIARDGRLLPGDQILEVNGVDISNVTHSQARSVLR 76

                  .
gi 150170670 4577 Q 4577
Cdd:cd06677    77 Q 77
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
4510-4586 7.82e-08

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: 53.03  E-value: 7.82e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670 4510 GNGLGIRIVGGKE-IPGHSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGEAEICV 4586
Cdd:cd06703    11 GKGLGFSIAGGKGsTPFRDGDEGIFISRITEGGAADRDGKLQVGDRVLSINGVDVTEARHDQAVALLTSSSPTITLVV 88
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
329-810 8.33e-08

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 59.03  E-value: 8.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  329 AKPPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPA---KPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQP 405
Cdd:PHA03307   22 PRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACdrfEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  406 GPAKP--PTQQVGTPKPLAQQPGlqSPAKAPGPTKTPVQQPGPGKIPAQQ---AGPGKTSAQQTGPTKPPSQLPGPAKPP 480
Cdd:PHA03307  102 REGSPtpPGPSSPDPPPPTPPPA--SPPPSPAPDLSEMLRPVGSPGPPPAaspPAAGASPAAVASDAASSRQAALPLSSP 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  481 PQQPGPAKPPPQQPGsakpPSQQPGSTKPPPQQPGpakPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQ 560
Cdd:PHA03307  180 EETARAPSSPPAEPP----PSTPPAAASPRPPRRS---SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPE 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  561 TGSGKPLQPPTVSPSAKQPPSQGLPKTICPLcnttelllhvpekanfntctecqttvcslcgfnpnphltevkewlclnC 640
Cdd:PHA03307  253 NECPLPRPAPITLPTRIWEASGWNGPSSRPG------------------------------------------------P 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  641 QMKRALGGDLAPVPSSPQPKlKTAPVTTTSAVSKSSPQPQQTSPKKDAAPkqdlskapepkkppplvkqptlHGSPSAKA 720
Cdd:PHA03307  285 ASSSSSPRERSPSPSPSSPG-SGPAPSSPRASSSSSSSRESSSSSTSSSS----------------------ESSRGAAV 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  721 KQPPEADSLSKPAPPKEPSVPSEQDKAPVADDKPKQPKMVKPttdlvSSSSATTKPDIPSSKVQSQAEEKTT----PPLK 796
Cdd:PHA03307  342 SPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAG-----RPTRRRARAAVAGRARRRDATGRFPagrpRPSP 416
                         490
                  ....*....|....
gi 150170670  797 TDSAKPSQSFPPTG 810
Cdd:PHA03307  417 LDAGAASGAFYARY 430
PDZ3_MAGI-1_3-like cd06733
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
4511-4587 8.97e-08

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: 52.61  E-value: 8.97e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670 4511 NGLGIRIVGGKEiPGHSGEIGAyiakILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQ--QSGEAEICVR 4587
Cdd:cd06733    11 TGFGFRILGGTE-EGSQVSIGA----IVPGGAADLDGRLRTGDELLSVDGVNVVGASHHKVVDLMGNaaRNGQVNLTVR 84
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
391-535 1.01e-07

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 58.57  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  391 LAQPPGVGkTPAQQPGPAKPPTQqvgtpkplaqqPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPP 470
Cdd:PRK14951  362 LAFKPAAA-AEAAAPAEKKTPAR-----------PEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAP 429
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150170670  471 SQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPG 535
Cdd:PRK14951  430 AAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEG 494
PDZ2_Par3-like cd23058
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
4483-4574 1.13e-07

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


Pssm-ID: 467271 [Multi-domain]  Cd Length: 93  Bit Score: 52.64  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4483 MNGKTMHyifpharIKITRDSkdhtvsgNGLGIRIVGGKEIPGHSGEIgaYIAKILPGGSAEQTGKLMEGMQVLEWNGIP 4562
Cdd:cd23058     1 KIGKKLH-------IQLKKGP-------EGLGFSITSRDNPTGGSGPI--YIKNILPKGAAIQDGRLKAGDRLLEVNGVD 64
                          90
                  ....*....|..
gi 150170670 4563 LTSKTYEEVQSI 4574
Cdd:cd23058    65 VTGKTQEEVVSL 76
C2A_Synaptotagmin-14_16 cd08389
C2A domain first repeat present in Synaptotagmins 14 and 16; Synaptotagmin 14 and 16 are ...
4696-4826 1.16e-07

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: 53.40  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4696 GEIQLQINYDLGN--LIIHILQARNLVPRDNNGYSDPFVKVYLLPGRGQvmvvqnasaeyKRRTKhVQKSLNPEWNQTVI 4773
Cdd:cd08389     3 GDLDVAFEYDPSArkLTVTVIRAQDIPTKDRGGASSWQVHLVLLPSKKQ-----------RAKTK-VQRGPNPVFNETFT 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 150170670 4774 YKSISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSSTSHLDNTPRWYPLK 4826
Cdd:cd08389    71 FSRVEPEELNNMALRFRLYGVERMRKERLIGEKVVPLSQLNLEGETTVWLTLE 123
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
4711-4828 1.19e-07

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: 53.42  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4711 IHILQARNLVPRDNNGYSDPFVkvyllpgrgqVMVVQNASAEYKrRTKHVQKSLNPEWNQTViykSISMEQLKKKTLEVT 4790
Cdd:cd04043     5 IRIVRAENLKADSSNGLSDPYV----------TLVDTNGKRRIA-KTRTIYDTLNPRWDEEF---ELEVPAGEPLWISAT 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 150170670 4791 VWDYDRFSSNDFLGEVLIDLSSTSHLDN-TPR--WYPLKEQ 4828
Cdd:cd04043    71 VWDRSFVGKHDLCGRASLKLDPKRFGDDgLPReiWLDLDTQ 111
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
4512-4587 1.26e-07

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: 52.05  E-value: 1.26e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670 4512 GLGIRIVGGKEipgHSGEIgaYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGEAEICVR 4587
Cdd:cd06796    13 GLGFNVMGGKE---QNSPI--YISRIIPGGVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKLVVR 83
PDZ_MPP3-MPP4-MPP7-like cd06799
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ...
4515-4580 1.37e-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: 51.86  E-value: 1.37e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150170670 4515 IRIVGGKEIPG-------HSGEIgaYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSG 4580
Cdd:cd06799     3 VRLVKNNEPLGatikrdeKTGAI--VVARIMRGGAADRSGLIHVGDELREVNGISVEGKDPEEVIQILANSQG 73
PHA03379 PHA03379
EBNA-3A; Provisional
234-578 1.41e-07

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 58.15  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  234 GTPKS-ISSQQPEKIKS--QPPGTGkPIQGPTQTPQTDHAKLPLQRDASRPQTKQADIVRGESVKPSLPSPSKPPIQQPT 310
Cdd:PHA03379  414 GTPRPpVEKPRPEVPQSleTATSHG-SAQVPEPPPVHDLEPGPLHDQHSMAPCPVAQLPPGPLQDLEPGDQLPGVVQDGR 492
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  311 PGKPPAQQPGHEKSQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPL-------GPAKPPAQQTGSEK--P 381
Cdd:PHA03379  493 PACAPVPAPAGPIVRPWEASLSQVPGVAFAPVMPQPMPVEPVPVPTVALERPVCPAppliamqGPGETSGIVRVRERwrP 572
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  382 SSEQPGP-------------------------KALAQPPGVGKTPAQQP--GPAKPPTQQVgtpkPLAQQPGLQSPAKAP 434
Cdd:PHA03379  573 APWTPNPprspsqmsvrdrlarlraeaqpyqaSVEVQPPQLTQVSPQQPmeYPLEPEQQMF----PGSPFSQVADVMRAG 648
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  435 GptkTPVQQPG----PGKIPAQQAGPGKTSAQQTGPTKP-----PSQLPGPAKPP-----------PQQP--GPAKPP-P 491
Cdd:PHA03379  649 G---VPAMQPQyfdlPLQQPISQGAPLAPLRASMGPVPPvpatqPQYFDIPLTEPinqgasaahflPQQPmeGPLVPErW 725
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  492 QQPGSAKPPSQQPGSTKP-----PPQQP----GPAKPSPQQPGSTKP--PSQQPGSAKPsaqqPSPAKPSAQQSTKPVSQ 560
Cdd:PHA03379  726 MFQGATLSQSVRPGVAQSqyfdlPLTQPinhgAPAAHFLHQPPMEGPwvPEQWMFQGAP----PSQGTDVVQHQLDALGY 801
                         410
                  ....*....|....*...
gi 150170670  561 TGSGKPLQPPTVSPSAKQ 578
Cdd:PHA03379  802 VLHVLNHPGVPVSPAVNQ 819
PDZ4_Scribble-like cd06701
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
4510-4586 1.43e-07

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: 52.23  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4510 GNGLGIRIVGGkeIPGHSG------EIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGEAE 4583
Cdd:cd06701    14 GEKLGISIRGG--AKGHAGnpldptDEGIFISKINPDGAAARDGRLKVGQRILEVNGQSLLGATHQEAVRILRSVGDTLT 91

                  ...
gi 150170670 4584 ICV 4586
Cdd:cd06701    92 LLV 94
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
386-517 1.49e-07

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 57.80  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  386 PGPKALAQPPGVGKTPAQQPGP---AKPPTQQVGTPKPLAQQPGLQSPAKAPgptkTPVQQPGPGKIPAQQAGPGKTSAQ 462
Cdd:PRK14951  366 PAAAAEAAAPAEKKTPARPEAAapaAAPVAQAAAAPAPAAAPAAAASAPAAP----PAAAPPAPVAAPAAAAPAAAPAAA 441
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 150170670  463 QTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPA 517
Cdd:PRK14951  442 PAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEGDV 496
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
476-905 1.53e-07

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 58.24  E-value: 1.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   476 PAKPPPQ--QPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGP------AKPSPQQPGSTKPPSQQPGSAKPSAQQPSPA 547
Cdd:pfam03154  146 PSIPSPQdnESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPpgttqaATAGPTPSAPSVPPQGSPATSQPPNQTQSTA 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   548 KP-SAQQST---KPVSQTGSGKPLQPPTVSPSAKQPPSQGLPKTIC---------PLCNTTELLLH-VPEKANFNTCTEC 613
Cdd:pfam03154  226 APhTLIQQTptlHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLhgqmppmphSLQTGPSHMQHpVPPQPFPLTPQSS 305
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   614 QTTVCSLCGFNPNPHLTEVKEWLCLNCQMKRALGGDLAPVPSSPQPKLKTAPVTTTSAVSKSSPQPQQTSPKKDAAPKQD 693
Cdd:pfam03154  306 QSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQ 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   694 LSKAPEPKKPPPLVKQPTLHGSPSAkakQPPEADSLSK----PAPPKEPsvpseqdkaPVADDKPKQPKMVKPTTDLVSS 769
Cdd:pfam03154  386 MNSNLPPPPALKPLSSLSTHHPPSA---HPPPLQLMPQsqqlPPPPAQP---------PVLTQSQSLPPPAASHPPTSGL 453
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   770 SSATTKPDIPSSKVQSQAEEKTTPPLktdsaKPSQSFPPTGEKVSPfdskaiprPASDSKIISHPGPSSESkgqKQVDPV 849
Cdd:pfam03154  454 HQVPSQSPFPQHPFVPGGPPPITPPS-----GPPTSTSSAMPGIQP--------PSSASVSSSGPVPAAVS---CPLPPV 517
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670   850 QKKEEPKKAqtkmSPKPDAKPMPKGSPTPPgprptagqtvPTPQQSPKPQEQSRRF 905
Cdd:pfam03154  518 QIKEEALDE----AEEPESPPPPPRSPSPE----------PTVVNTPSHASQSARF 559
PHA03247 PHA03247
large tegument protein UL36; Provisional
823-1389 1.65e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.41  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  823 RPAsDSKIISHPGPSSESKGQKQVDPVQKKEEPKKAQTKMSPKPDAKPMP-----------------KGSPTPP----GP 881
Cdd:PHA03247 2482 RPA-EARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVHprmltwirgleelasddAGDPPPPlppaAP 2560
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  882 RPTAGQTVPTPQQSPKPQEQSRRfslnlgsitdAPKSQPTTPQETVTGKlfgfgasifsqasnliSTAGQPGPHSQSGPG 961
Cdd:PHA03247 2561 PAAPDRSVPPPRPAPRPSEPAVT----------SRARRPDAPPQSARPR----------------APVDDRGDPRGPAPP 2614
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  962 APMKQAPAPSQPPTSQGPPKSTGQAPPAPAKSIPVKKETKAPAAEKLEPKaeqaptvKRTETEKKPP----PIKDSKSLT 1037
Cdd:PHA03247 2615 SPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRP-------RRARRLGRAAqassPPQRPRRRA 2687
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1038 AEPQKAVLpTKLEKSPKPESTCPLCKTELNIGSKDPPNFNTCTecknqvcnlcGFNPTPHLTEIQEwlclncQTQRAISG 1117
Cdd:PHA03247 2688 ARPTVGSL-TSLADPPPPPPTPEPAPHALVSATPLPPGPAAAR----------QASPALPAAPAPP------AVPAGPAT 2750
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1118 QLGDIRKM-PPAPSGPKASPMPVPTESSSQKTAVPPQVklvkkqeQEVKTEAEKVILEKVKETLSMEKIPPMVTTDQKQE 1196
Cdd:PHA03247 2751 PGGPARPArPPTTAGPPAPAPPAAPAAGPPRRLTRPAV-------ASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS 2823
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1197 ESKLEKDKASALQEKKPLPEEkkliPEEEKIRSE---------EKKPLLEEKKPTPEDKKLLPEAKTSAPEEQKHDLLKS 1267
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPPG----PPPPSLPLGgsvapggdvRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFA 2899
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1268 QVQIAEEKLEGRVAPKTVQEGKQPQTKMEGLPSGTPQSLPKEDDKTTKTIKEQPQPPCTAK--------PDQVEPGKEKT 1339
Cdd:PHA03247 2900 LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPqpwlgalvPGRVAVPRFRV 2979
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|
gi 150170670 1340 EKEDDKSDTSSSQQPkSPQGLSDTGYSSDGISSSLGEIPSLIPTDEKDIL 1389
Cdd:PHA03247 2980 PQPAPSREAPASSTP-PLTGHSLSRVSSWASSLALHEETDPPPVSLKQTL 3028
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
499-1049 1.86e-07

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 57.78  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  499 PPSQQPGSTK--PPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSA 576
Cdd:PTZ00449  497 APIEEEDSDKhdEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLS 576
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  577 KQPPSQGLPKTicplcnttelllhvpekanfntctecqttvcslcgfnpnphltevkewlclncqmkralggdlapvPSS 656
Cdd:PTZ00449  577 KKPEFPKDPKH------------------------------------------------------------------PKD 590
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  657 PQ-PKLKTAPVTTTSAVSKSSPQPQQTS--PKKDAAPKQDLSKAPEPKKPPPLvkqptlhgSPsakaKQPPEADSLSKPA 733
Cdd:PTZ00449  591 PEePKKPKRPRSAQRPTRPKSPKLPELLdiPKSPKRPESPKSPKRPPPPQRPS--------SP----ERPEGPKIIKSPK 658
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  734 PPKEPSVPSEQD-KAPVADD---KPKQPKMVKPTTDLVSSSSATTKPDIPSSKVQSQAEEKTTPPLKTDSakPSQSFPPT 809
Cdd:PTZ00449  659 PPKSPKPPFDPKfKEKFYDDyldAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKLPRD--EEFPFEPI 736
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  810 GEKVSPF--DSKAIPRPASDSKIISHPGPSSESKGqkqVDPVQKKEEPKKAQTKMSPKPDAKPMP--KGSPTPPGPRPTA 885
Cdd:PTZ00449  737 GDPDAEQpdDIEFFTPPEEERTFFHETPADTPLPD---ILAEEFKEEDIHAETGEPDEAMKRPDSpsEHEDKPPGDHPSL 813
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  886 gqtvptpqqsPKPQEQSRRFSLNlgsitdapksqpTTPQETVTGKLFgfgasifsqasnlistagqpgpHSQSGPGAPMK 965
Cdd:PTZ00449  814 ----------PKKRHRLDGLALS------------TTDLESDAGRIA----------------------KDASGKIVKLK 849
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  966 QAPAPSQPPTSQGPPKStgqapPAPAKSIPVKKE-TKAPAAEKLEPKAEQAPTVKRTETEKKP--PPIKDSKSLTAEPQK 1042
Cdd:PTZ00449  850 RSKSFDDLTTVEEAEEM-----GAEARKIVVDDDgTEADDEDTHPPEEKHKSEVRRRRPPKKPskPKKPSKPKKPKKPDS 924

                  ....*..
gi 150170670 1043 AVLPTKL 1049
Cdd:PTZ00449  925 AFIPSII 931
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
453-557 1.89e-07

trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia intracellular motility A), WP_004266405.1-like proteins in Burkholderia mallei or B. pseudomallei. The term BimA has also been used for WP_011205626.1-like homologs that have a very different N-terminal half.


Pssm-ID: 468913 [Multi-domain]  Cd Length: 382  Bit Score: 56.83  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  453 QAGPGKTSAQQTGPTKPPSQLPGPakPPPQQPGPAKPPPQQPGSAKPPSqqPGSTKPPPQQPGPAKPSPQQPgSTKPPSQ 532
Cdd:NF040983   69 QIKKGDFKLKPVGDRTLPNKVPPP--PPPPPPPPPPPPTPPPPPPPPPP--PPPPSPPPPPPPSPPPSPPPP-TTTPPTR 143
                          90       100
                  ....*....|....*....|....*
gi 150170670  533 QPgsakPSAQQPSPAKPSAQQSTKP 557
Cdd:NF040983  144 TT----PSTTTPTPSMHPIQPTQLP 164
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
4502-4581 1.92e-07

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 51.51  E-value: 1.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  4502 DSKDHTVSGNGLGIRIVGGKEipghSGEIGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGE 4581
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSD----QGDPGIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGK 75
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
4506-4587 2.02e-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: 51.49  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4506 HTVSGNG-LGIRIVGGKEIPGH---SGEIGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGE 4581
Cdd:cd06702     4 HLVKAGGpLGLSIVGGSDHSSHpfgVDEPGIFISKVIPDGAAAKSG-LRIGDRILSVNGKDLRHATHQEAVSALLSPGQE 82

                  ....*.
gi 150170670 4582 AEICVR 4587
Cdd:cd06702    83 IKLLVR 88
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
4510-4587 2.29e-07

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: 51.42  E-value: 2.29e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670 4510 GNGLGIRIVGGKEipgHSGEIgaYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGEAEICVR 4587
Cdd:cd06801    10 VGGLGISIKGGAE---HKMPI--LISKIFKGQAADQTGQLFVGDAILSVNGENLEDATHDEAVQALKNAGDEVTLTVK 82
SSDP pfam04503
Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA ...
355-555 2.76e-07

Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA binding proteins with specificity to a pyrimidine-rich element found in the promoter region of the alpha2(I) collagen gene.


Pssm-ID: 461334 [Multi-domain]  Cd Length: 293  Bit Score: 55.73  E-value: 2.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   355 PPGTTKPpAQPLGPA--KPPAQQTGSEKPSSEQPGPKALAQPPGVGKTP---AQQPGPAKP----PTQQVGTPKPLAQQP 425
Cdd:pfam04503   29 PPGDGMP-GGPMPPGffQSPPSHPSSQPSPHAQPPPHNPATMMGPHSQPfmgPRYPGGPRPsvrmPQQGNDFNGPPGQQP 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   426 GLqspakaPGPTKTPVQQPGPGKIPAQQAGPGkTSAQQTGPTKPPSQLPGPAKPPPQQP-GPAKPPPQQPG-SAKPPSQQ 503
Cdd:pfam04503  108 MM------PNSMDPTRPGGHPNMGGPMQRMNP-PRGPGMGPMGPQSYGPGMRGPPPNSTdGPGGMPPMNMGpGGRRPWPQ 180
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 150170670   504 PGSTKPPPQqpgpakpSPQQPGSTKPPsqqPGSAKPSAqqPSPAKPSAQQST 555
Cdd:pfam04503  181 PNASNPLPY-------SSSSPGSYGGP---PGGGGPPG--PTPIMPSPQDST 220
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
416-586 3.21e-07

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: 56.70  E-value: 3.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  416 GTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKP----------PSQLPGPAKPPPQ-QP 484
Cdd:NF033839  288 GNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPevkpqletpkPEVKPQPEKPKPEvKP 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  485 GPAKPPPQ---QPGSAKPPSQQPGSTKPPPQQPGPAKPSPQ-QPGSTKP-PSQQPGSAKPSAQ-QPSPAKPSAQQSTKPV 558
Cdd:NF033839  368 QPEKPKPEvkpQPETPKPEVKPQPEKPKPEVKPQPEKPKPEvKPQPEKPkPEVKPQPEKPKPEvKPQPEKPKPEVKPQPE 447
                         170       180
                  ....*....|....*....|....*...
gi 150170670  559 SQTGSGKPlQPPTVSPSAKQPPSQGLPK 586
Cdd:NF033839  448 KPKPEVKP-QPETPKPEVKPQPEKPKPE 474
C2B_Copine cd04047
C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
4714-4806 3.30e-07

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: 51.80  E-value: 3.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4714 LQARNLVPRDNNGYSDPFVKVYLLPGRGQ-VMVvqnasaeykRRTKHVQKSLNPEWNQTviykSISMEQL----KKKTLE 4788
Cdd:cd04047     7 FSGKKLDKKDFFGKSDPFLEISRQSEDGTwVLV---------YRTEVIKNTLNPVWKPF----TIPLQKLcngdYDRPIK 73
                          90
                  ....*....|....*...
gi 150170670 4789 VTVWDYDRFSSNDFLGEV 4806
Cdd:cd04047    74 IEVYDYDSSGKHDLIGEF 91
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
463-584 4.15e-07

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 56.32  E-value: 4.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  463 QTGPTKPPSQLPG-PAKPPPQQPGPAKPPPQQPGsakpPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAK--P 539
Cdd:PRK14971  364 QKGDDASGGRGPKqHIKPVFTQPAAAPQPSAAAA----ASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPvnP 439
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 150170670  540 SAQQPSPAKPSAQQSTK--PVSQTGSgkpLQPPTVSPsaKQPPSQGL 584
Cdd:PRK14971  440 PSTAPQAVRPAQFKEEKkiPVSKVSS---LGPSTLRP--IQEKAEQA 481
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
647-1029 4.88e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 56.53  E-value: 4.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  647 GGDLAPVPSSPQPKLKTAPVTTTSAVSKSSPQPQQTSPKKDAAPKQDLSKAPEPKKPPPLVKQPTLHGSPSAKAKQPPEA 726
Cdd:PRK07764  403 AAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAP 482
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  727 DSLSKPAPPKEPSVPSE----QDKAPVADDKPKQPKMVkpttDLVSSSSATTKPDIpSSKVQSQAEEKTTPPLKTDSakp 802
Cdd:PRK07764  483 APPAAPAPAAAPAAPAApaapAGADDAATLRERWPEIL----AAVPKRSRKTWAIL-LPEATVLGVRGDTLVLGFST--- 554
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  803 sqsfPPTGEKVSPFDSKAIPRPA------SDSKIISHPGPSSESKG-QKQVDPVQKKEEPKKAQTKMSPKPDAKPMPKGS 875
Cdd:PRK07764  555 ----GGLARRFASPGNAEVLVTAlaeelgGDWQVEAVVGPAPGAAGgEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPA 630
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  876 PTPPGPRPTAGQTVPTPQQSPKPQEQSRRFSLNLGSITDAPKSQPTTPQETVTGklfgfGASIFSQASnlistAGQPGPH 955
Cdd:PRK07764  631 GAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPA-----PAPAAPAAP-----AGAAPAQ 700
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670  956 SQSGPGAPMKQAPAPSQPPTSQGPPKSTGQAPPAPAKSIPVKKETKAPAAEKLEPKAEQAPTVKRTETEKKPPP 1029
Cdd:PRK07764  701 PAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAP 774
PDZ1_PTPN13_FRMPD2-like cd06694
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ...
4496-4580 5.32e-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: 50.47  E-value: 5.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4496 RIKITRDSKdhtvsgNGLGIRIVGGkEIPGhSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTY------- 4568
Cdd:cd06694     4 IVTLKKDPQ------KGLGFTIVGG-ENSG-SLDLGIFVKSIIPGGPADKDGRIKPGDRIIAINGQSLEGKTHhaaveii 75
                          90
                  ....*....|....*.
gi 150170670 4569 ----EEVQSIISQQSG 4580
Cdd:cd06694    76 qnapDKVELIISQPKS 91
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
425-585 5.49e-07

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 56.40  E-value: 5.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  425 PGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPqQPGPAKPPPQQPGSAKPPSQQP 504
Cdd:PRK07003  368 PGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAE-APPAAPAPPATADRGDDAADGD 446
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  505 GSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSG-KPLQPPTVSPSAKQPPSQG 583
Cdd:PRK07003  447 APVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAvPDARAPAAASREDAPAAAA 526

                  ..
gi 150170670  584 LP 585
Cdd:PRK07003  527 PP 528
GGN pfam15685
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ...
349-554 5.53e-07

Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.


Pssm-ID: 434857 [Multi-domain]  Cd Length: 668  Bit Score: 56.31  E-value: 5.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   349 VKPPVQPPGTTKPPAQPLG-----PAKPPAQQTGSEKPSSEQPGPKALAQPPGVgktpaqQPGPAKPPTQQVGTPKPLAQ 423
Cdd:pfam15685   31 VEPEVTPSSPAMRLAQGLGvwfpgSSAPPGLLVPPEPQASPSPLPLTLELPLPV------TPPPEEAAAAAVSTAPPPAV 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   424 QPGLQSPAKAPGPTKTPVQQPgPGKIPAQQAGPGKTSAQQTGPTKPPSQL------PG-PAKPPPQQPGPAKPPPQQPGS 496
Cdd:pfam15685  105 GSLLPAPSKWRKPTGTAVARI-RGLLEASHRGQGDPLSLRPLLPLLPRQLiekdpaPGaPAPPPPTPLEPRKPPPLPPSD 183
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670   497 AKPPSQQPgSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQS 554
Cdd:pfam15685  184 RQPPNRGI-TPALATSATSPTDSQAKHIAEGKTAGGACGGAPPQAGEGEMARFAASES 240
dnaA PRK14086
chromosomal replication initiator protein DnaA;
309-524 6.05e-07

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 55.99  E-value: 6.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  309 PTPGKPPAQQPgHEKSQPGPAKPPAQPSGlTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPGP 388
Cdd:PRK14086   90 PSAGEPAPPPP-HARRTSEPELPRPGRRP-YEGYGGPRADDRPPGLPRQDQLPTARPAYPAYQQRPEPGAWPRAADDYGW 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  389 kalaQPPGVGKTPAQQPGPakpPTQQVGTPKPLAQQPGLQSPAKAPGptKTPVQQPGPgkipaqqagpgktsaQQTGPTK 468
Cdd:PRK14086  168 ----QQQRLGFPPRAPYAS---PASYAPEQERDREPYDAGRPEYDQR--RRDYDHPRP---------------DWDRPRR 223
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670  469 PPSQLPGPAkPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAkPSPQQP 524
Cdd:PRK14086  224 DRTDRPEPP-PGAGHVHRGGPGPPERDDAPVVPIRPSAPGPLAAQPAPA-PGPGEP 277
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
458-563 6.10e-07

trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia intracellular motility A), WP_004266405.1-like proteins in Burkholderia mallei or B. pseudomallei. The term BimA has also been used for WP_011205626.1-like homologs that have a very different N-terminal half.


Pssm-ID: 468913 [Multi-domain]  Cd Length: 382  Bit Score: 55.29  E-value: 6.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  458 KTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQpgSTKPPSQQP--G 535
Cdd:NF040983   83 RTLPNKVPPPPPPPPPPPPPPPTPPPPPPPPPPPPPPSPPPPPPPSPPPSPPPPTTTPPTRTTPST--TTPTPSMHPiqP 160
                          90       100
                  ....*....|....*....|....*...
gi 150170670  536 SAKPSAQQPSPAKPSAQQSTKPVSQTGS 563
Cdd:NF040983  161 TQLPSIPNATPTSGSATNVTINFNSTGA 188
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
446-565 6.74e-07

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 55.94  E-value: 6.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  446 PGKIPAQQAGP---GKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQ 522
Cdd:PRK14971  371 GGRGPKQHIKPvftQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPVNPPSTAPQAVRPA 450
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 150170670  523 QPGSTKPPS-QQPGSAKPSAQQpsPAKPSAQQSTK--PVSQTGSGK 565
Cdd:PRK14971  451 QFKEEKKIPvSKVSSLGPSTLR--PIQEKAEQATGniKEAPTGTQK 494
dnaA PRK14086
chromosomal replication initiator protein DnaA;
400-580 8.50e-07

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 55.60  E-value: 8.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  400 TPAQQPGPAKPPTQQVgTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPgkipaqqAGPGKTSAQQTGPTKPPSQLPGPakp 479
Cdd:PRK14086   89 DPSAGEPAPPPPHARR-TSEPELPRPGRRPYEGYGGPRADDRPPGLP-------RQDQLPTARPAYPAYQQRPEPGA--- 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  480 ppqQPGPAKP-PPQQPGSAKPPSQQPGS-TKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQpspakPSAQQSTKP 557
Cdd:PRK14086  158 ---WPRAADDyGWQQQRLGFPPRAPYASpASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWDR-----PRRDRTDRP 229
                         170       180
                  ....*....|....*....|....*.
gi 150170670  558 VSQTGSGKPL---QPPTVSPSAKQPP 580
Cdd:PRK14086  230 EPPPGAGHVHrggPGPPERDDAPVVP 255
C2A_Copine cd04048
C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
4713-4812 8.80e-07

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: 50.65  E-value: 8.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4713 ILQARNLVPRDNNGYSDPFVKVYllpgrgqvmVVQNASAEYKR--RTKHVQKSLNPEWNQTVI--YKsISMEQlkkkTLE 4788
Cdd:cd04048     6 SISCRNLLDKDVLSKSDPFVVVY---------VKTGGSGQWVEigRTEVIKNNLNPDFVTTFTvdYY-FEEVQ----KLR 71
                          90       100
                  ....*....|....*....|....*...
gi 150170670 4789 VTVWDYD----RFSSNDFLGEVLIDLSS 4812
Cdd:cd04048    72 FEVYDVDskskDLSDHDFLGEAECTLGE 99
PDZ2_LNX1_2-like cd06678
PDZ domain 2 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
4506-4581 9.39e-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: 49.55  E-value: 9.39e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670 4506 HTVSGNGLGIRIVGGKEIPGhsgeigAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIIsQQSGE 4581
Cdd:cd06678     6 NKRDGEQLGIKLVRKKDEPG------VFILDLLEGGLAARDGRLKSDDRVLAINGQDLRHGTPEQAAQII-QASGE 74
PRK10263 PRK10263
DNA translocase FtsK; Provisional
424-991 1.12e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 55.48  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  424 QPGLQSPAkAPGPtKTPVQQPgpgkIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAkpPPQQPGSAKPPSQQ 503
Cdd:PRK10263  338 EPVTQTPP-VASV-DVPPAQP----TVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNE--PLQQPVQPQQPYYA 409
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  504 PGSTKPPPQQPGPAKPSPqqpgSTKPPSQQPGSAKPSAQQPSPAKPSAQQ-STKPVSQTGSGKPlQPPTVSPSAKQPPSQ 582
Cdd:PRK10263  410 PAAEQPAQQPYYAPAPEQ----PAQQPYYAPAPEQPVAGNAWQAEEQQSTfAPQSTYQTEQTYQ-QPAAQEPLYQQPQPV 484
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  583 GLPKTICPLCNTTELLLHVPekanfntctecqttvcslcgfnPNPHLTEVKEwlclncqmKRALGGDLAPVPSSPQPKLK 662
Cdd:PRK10263  485 EQQPVVEPEPVVEETKPARP----------------------PLYYFEEVEE--------KRAREREQLAAWYQPIPEPV 534
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  663 TAPVTTTSAVskSSPQPQQTSPKKDAAPKQDLSkapepkkppPLVKQPTLHGSPSAKAKQPpeADSLSKPAPPKepsvps 742
Cdd:PRK10263  535 KEPEPIKSSL--KAPSVAAVPPVEAAAAVSPLA---------SGVKKATLATGAAATVAAP--VFSLANSGGPR------ 595
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  743 EQDKAPVADDKPKQPKMVKPTTDLVSSSSATtkpdIPSskvQSQAEEKTTpplKTDSAKPSQSFPPTGEKVSPFDSKAIP 822
Cdd:PRK10263  596 PQVKEGIGPQLPRPKRIRVPTRRELASYGIK----LPS---QRAAEEKAR---EAQRNQYDSGDQYNDDEIDAMQQDELA 665
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  823 RPASDSK------IISHPGP--------SSESKGQKQVDPVQKK----EEPKKAQTKMSPKPDAKPMPK-GSPTPPGPRP 883
Cdd:PRK10263  666 RQFAQTQqqrygeQYQHDVPvnaedadaAAEAELARQFAQTQQQrysgEQPAGANPFSLDDFEFSPMKAlLDDGPHEPLF 745
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  884 TAG-QTVPTPQQSPKPQEQSRRFSLNLgsitdAPKSQPTTPQETVtgklfgfgASIFSQASNLISTAGQPGPHSQSGPGA 962
Cdd:PRK10263  746 TPIvEPVQQPQQPVAPQQQYQQPQQPV-----APQPQYQQPQQPV--------APQPQYQQPQQPVAPQPQYQQPQQPVA 812
                         570       580
                  ....*....|....*....|....*....
gi 150170670  963 PMKQAPAPSQPPTSQgPPKSTGQAPPAPA 991
Cdd:PRK10263  813 PQPQYQQPQQPVAPQ-PQYQQPQQPVAPQ 840
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
332-495 1.14e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 55.11  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  332 PAQPSGLT----KPLAQQPGTvKPPVQPPGTTKPPAQPlgPAKPPAQqtgseKPSSEQPGPKALAQPPgvgktPAQQPGP 407
Cdd:PRK14951  348 PDEYAALTmvllRLLAFKPAA-AAEAAAPAEKKTPARP--EAAAPAA-----APVAQAAAAPAPAAAP-----AAAASAP 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  408 AKPPTQQVGTPkplAQQPGLQSPAKAPGPTKTPVQQPgpgkiPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPA 487
Cdd:PRK14951  415 AAPPAAAPPAP---VAAPAAAAPAAAPAAAPAAVALA-----PAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAA 486

                  ....*...
gi 150170670  488 KPPPQQPG 495
Cdd:PRK14951  487 RLTPTEEG 494
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
390-568 1.25e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 54.87  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  390 ALA-QPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPgpgkiPAQQAGPGKTSAQQTGPTK 468
Cdd:PRK07994  356 MLAfHPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAP-----AVPLPETTSQLLAARQQLQ 430
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  469 PPSQLPGPAKPPPQQPGPAKP--PPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPgSTKPPSQQPGSAKPSAQQ--- 543
Cdd:PRK07994  431 RAQGATKAKKSEPAAASRARPvnSALERLASVRPAPSALEKAPAKKEAYRWKATNPVE-VKKEPVATPKALKKALEHekt 509
                         170       180       190
                  ....*....|....*....|....*....|.
gi 150170670  544 PSPAKPSAQQSTKP------VSQTGSGKPLQ 568
Cdd:PRK07994  510 PELAAKLAAEAIERdpwaalVSQLGLPGLVE 540
PDZ4_MUPP1-like cd06668
PDZ domain 4 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
4497-4588 1.26e-06

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: 49.22  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4497 IKITRDSKDHTVSGNGLGIRIVGGKEIPGHSgeigaYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIIS 4576
Cdd:cd06668     2 IVVAQLSKFSESSGLGISLEGTVDVEVRGHH-----YIRSILPEGPVGRNGKLFSGDELLEVNGIQLLGLSHKEVVSILK 76
                          90
                  ....*....|..
gi 150170670 4577 qqsgEAEICVRL 4588
Cdd:cd06668    77 ----ELPPPVRL 84
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
438-580 1.50e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 54.87  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  438 KTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSA-----KPPSQQPGSTKPP-- 510
Cdd:PRK07994  362 AAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQllaarQQLQRAQGATKAKks 441
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150170670  511 -PQQPGPAKP--SPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTgsgKPLQPPTVSPSAKQPP 580
Cdd:PRK07994  442 ePAAASRARPvnSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVA---TPKALKKALEHEKTPE 511
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
411-534 1.60e-06

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 51.19  E-value: 1.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   411 PTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQqagPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPP 490
Cdd:pfam15240   38 QSQQGGQGPQGPPPGGFPPQPPASDDPPGPPPPGGPQQPPPQ---GGKQKPQGPPPQGGPRPPPGKPQGPPPQGGNQQQG 114
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 150170670   491 PQQPGSAKPPSQQPGStkPPPQQPGPAKPSPQQPGSTKPPSQQP 534
Cdd:pfam15240  115 PPPPGKPQGPPPQGGG--PPPQGGNQQGPPPPPPGNPQGPPQRP 156
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
673-1061 1.69e-06

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 54.77  E-value: 1.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   673 SKSSPQPQQTSPKKDAAPKQDLskapepkKPPPLVKQPTLHGSPSAKAKQPPEADSLSKPAP-PKEPSVPSEqdKAPVAD 751
Cdd:pfam03154  145 SPSIPSPQDNESDSDSSAQQQI-------LQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPtPSAPSVPPQ--GSPATS 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   752 DKPKQPKMVKPTTDLVSSSSATTKPDIPSSKVQSQAEEKTTPPLKTdSAKPSQS------FPPTGEKVS--------PFD 817
Cdd:pfam03154  216 QPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQV-SPQPLPQpslhgqMPPMPHSLQtgpshmqhPVP 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   818 SKAIPRPASDSKIISHPGPSSESKGQKQvdpvQKKEEPKKAQTKMSPKPdakpmPKGSPTPPGPRPTAG----QTVPTPQ 893
Cdd:pfam03154  295 PQPFPLTPQSSQSQVPPGPSPAAPGQSQ----QRIHTPPSQSQLQSQQP-----PREQPLPPAPLSMPHikppPTTPIPQ 365
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   894 QsPKPQEQSRRFSLNLGSITDAPKSQPTTPqetvtgklfgfgasifsqASNLISTAGQPGPHSQSGPGAPMKQAPAPSQP 973
Cdd:pfam03154  366 L-PNPQSHKHPPHLSGPSPFQMNSNLPPPP------------------ALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPP 426
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   974 PTSQGPPKSTGQAPPAPAKSIPVKKETKAPAAEKLEPKAEQAPTVKRTETEKKPPPIKDSKSLTAEPQKAVLPTKLEKSP 1053
Cdd:pfam03154  427 PPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPV 506

                   ....*...
gi 150170670  1054 KPESTCPL 1061
Cdd:pfam03154  507 PAAVSCPL 514
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
442-570 1.72e-06

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 51.19  E-value: 1.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   442 QQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGpaKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSP 521
Cdd:pfam15240   38 QSQQGGQGPQGPPPGGFPPQPPASDDPPGPPPPGGPQQPPPQGG--KQKPQGPPPQGGPRPPPGKPQGPPPQGGNQQQGP 115
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 150170670   522 QQPGSTKPPSQQPGSAKP---SAQQPSPAKPSAQQSTkPVSQTGSGKPLQPP 570
Cdd:pfam15240  116 PPPGKPQGPPPQGGGPPPqggNQQGPPPPPPGNPQGP-PQRPPQPGNPQGPP 166
PDZ12_MUPP1-like cd06675
PDZ domain 12 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 10 of protein-associated tight ...
4496-4586 1.73e-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: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4496 RIKITRDSKDhtvsgnGLGIRIVGGKEIPghSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSII 4575
Cdd:cd06675     2 TVEIKRGPQD------SLGISIAGGVGSP--LGDVPVFIAMIQPNGVAAQTGKLKVGDRIVSINGQSTDGLTHSEAVNLL 73
                          90
                  ....*....|.
gi 150170670 4576 SQQSGEAEICV 4586
Cdd:cd06675    74 KNASGTIILQV 84
PDZ2_MUPP1-like cd06667
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
4510-4578 1.90e-06

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


Pssm-ID: 467155 [Multi-domain]  Cd Length: 80  Bit Score: 48.43  E-value: 1.90e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670 4510 GNGLGIRIVGGKEIpghsgeiGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQ 4578
Cdd:cd06667     9 GSGLGFGIVGGKST-------GVVVKTILPGGVADRDGRLRSGDHILQIGDTNLRGMGSEQVAQVLRQC 70
PDZ13_MUPP1-like cd06676
PDZ domain 13 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
4512-4586 1.92e-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: 48.49  E-value: 1.92e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150170670 4512 GLGIRIVGGKEIPghSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGEAEICV 4586
Cdd:cd06676    10 GLGFSIVGGFGSP--HGDLPIYVKTVFEKGAAAEDGRLKRGDQILAVNGESLEGVTHEEAVNILKKTKGTVTLTV 82
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
425-557 1.94e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 54.40  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  425 PGLQSPAKapgPTKTPVQQPGPGKIPAQQAGPgktsAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAK-PPSQQ 503
Cdd:PRK14971  370 SGGRGPKQ---HIKPVFTQPAAAPQPSAAAAA----SPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPvNPPST 442
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 150170670  504 PGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPgsAKPSAQQPSPAKPSAQQSTKP 557
Cdd:PRK14971  443 APQAVRPAQFKEEKKIPVSKVSSLGPSTLRP--IQEKAEQATGNIKEAPTGTQK 494
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
250-474 1.95e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 54.47  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  250 QPPGTGKPIQGPTQTPQTDHAKLPLQRDASRPQTKQAdivrGESVKPSLPSPSKPPIQQPTPGKPPAQQPGHEKSQPGPA 329
Cdd:PRK07003  399 VTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPAT----ADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADS 474
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  330 KPPAQPSGLTKPLAQ-QPGTvkPPVQPPGTTKPPAQPlgPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQ---- 404
Cdd:PRK07003  475 GSASAPASDAPPDAAfEPAP--RAAAPSAATPAAVPD--ARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAggaa 550
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  405 ---------------------PGPAKPPTQQVGTPKPLAQQPGLQSPakAPGPTKTPVQQPGPGKIPAQQAgpgktsAQQ 463
Cdd:PRK07003  551 aaldvlrnagmrvssdrgaraAAAAKPAAAPAAAPKPAAPRVAVQVP--TPRARAATGDAPPNGAARAEQA------AES 622
                         250
                  ....*....|.
gi 150170670  464 TGPTKPPSQLP 474
Cdd:PRK07003  623 RGAPPPWEDIP 633
PDZ11_MUPP1-PDZ9_PATJ-like cd06674
PDZ domain 11 of MUPP1 of multi-PDZ-domain protein 1 (MUPP1), domain 9 of PATJ ...
4509-4581 2.40e-06

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: 48.43  E-value: 2.40e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150170670 4509 SGNGLGIRIVGGKEipghsgEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGE 4581
Cdd:cd06674    12 PGRGLGLSIVGKRN------DTGVFVSDIVKGGAADADGRLMQGDQILSVNGEDVRNASQEAAAALLKCAQGK 78
PDZ1_FRMPD2-like cd23071
PDZ domain 1 of FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ ...
4496-4580 2.66e-06

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: 48.64  E-value: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4496 RIKITRDSKdhtvsgNGLGIRIVGGKEIpgHSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTY------- 4568
Cdd:cd23071     4 CVTLKRDPK------RGFGFVIVGGENT--GKLDLGIFIASIIPGGPAEKDGRIKPGGRLISLNNISLEGVTFntavkil 75
                          90
                  ....*....|....*.
gi 150170670 4569 ----EEVQSIISQQSG 4580
Cdd:cd23071    76 qnspDEVELIISQPKD 91
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 ...
4506-4587 2.81e-06

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: 48.42  E-value: 2.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4506 HTVSGNGLGIRIVGgkeIPGHSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQ-QSGEAEI 4584
Cdd:cd06760    10 NKEPGVGLGIGLCC---LPLENDIPGIFIHHLSPGSVAHMDGRLRRGDQILEINGTSLRNVTLNEAYAILSQcKPGPVTL 86

                  ...
gi 150170670 4585 CVR 4587
Cdd:cd06760    87 IIS 89
PHA01929 PHA01929
putative scaffolding protein
439-575 3.17e-06

putative scaffolding protein


Pssm-ID: 177328  Cd Length: 306  Bit Score: 52.75  E-value: 3.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  439 TPVQQPGPGKIPAQQAgpgktsaqqtgpTKPPSQLPGPAKPPPQQPGPAKPP--PQQPGSAKPPSQQPGSTKPPPQQPGP 516
Cdd:PHA01929    2 TQNEQQLPPGLAGLVA------------NVPPAAAPTPQPNPVIQPQAPVQPgqPGAPQQLAIPTQQPQPVPTSAMTPHV 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670  517 AKPSPQQPGSTKPPSqqPGSAKPSAQQPSPakPSAQQSTKPVSQTGSGKPLQPPTVSPS 575
Cdd:PHA01929   70 VQQAPAQPAPAAPPA--AGAALPEALEVPP--PPAFTPNGEIVGTLAGNLEGDPQLAPS 124
PHA01929 PHA01929
putative scaffolding protein
411-513 3.37e-06

putative scaffolding protein


Pssm-ID: 177328  Cd Length: 306  Bit Score: 52.36  E-value: 3.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  411 PTQQVGTPKpLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPG--KTSAQQTGPTKPPSQLPGPAKPPPQQPGPAK 488
Cdd:PHA01929    3 QNEQQLPPG-LAGLVANVPPAAAPTPQPNPVIQPQAPVQPGQPGAPQqlAIPTQQPQPVPTSAMTPHVVQQAPAQPAPAA 81
                          90       100
                  ....*....|....*....|....*..
gi 150170670  489 PPPqqPGSAKPPSQQPG--STKPPPQQ 513
Cdd:PHA01929   82 PPA--AGAALPEALEVPppPAFTPNGE 106
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
374-524 3.90e-06

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 50.04  E-value: 3.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   374 QQTGSEKPSSEQPGPKALAQPPGvGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPaKAPGPTKTPVQQPGPGKIPAQQ 453
Cdd:pfam15240   30 SLISEEEGQSQQGGQGPQGPPPG-GFPPQPPASDDPPGPPPPGGPQQPPPQGGKQKP-QGPPPQGGPRPPPGKPQGPPPQ 107
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150170670   454 AGPgktsaQQTGPTKPPsqlpGPAKPPPQQPGpakPPPQQPGSAKPPSQQPGSTKPPPQQPgPAKPSPQQP 524
Cdd:pfam15240  108 GGN-----QQQGPPPPG----KPQGPPPQGGG---PPPQGGNQQGPPPPPPGNPQGPPQRP-PQPGNPQGP 165
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
373-494 4.02e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 53.24  E-value: 4.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  373 AQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQS-PAKAPGPTKTPVQQPGPGKIPA 451
Cdd:PRK14971  360 AQLTQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSaTQPAGTPPTVSVDPPAAVPVNP 439
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 150170670  452 QQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQpGPAKPPPQQP 494
Cdd:PRK14971  440 PSTAPQAVRPAQFKEEKKIPVSKVSSLGPSTL-RPIQEKAEQA 481
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
712-1043 4.60e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 53.25  E-value: 4.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  712 LHGSPSAKAKQPPEADSLSKPAPPKEPSVPSEQDKAPVADDKPKQPKMVKPTTDLVSSSSATTKPDIPSSkvqsqaEEKT 791
Cdd:PHA03307   42 QLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGP------SSPD 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  792 TPPLKTDSAKP--------SQSFPPTGEKVSPFDSKAIPRPASDSKIISHPGPSSESkgqkqVDPVQKKEEPkkAQTKMS 863
Cdd:PHA03307  116 PPPPTPPPASPppspapdlSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQA-----ALPLSSPEET--ARAPSS 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  864 PKPDA---KPMPKGSPTPPGPRPTAGQTVPTPQQSPKPQEQSRRFSLNLGSITDAPKSQPTTPQETVTGKLFGFGASIFS 940
Cdd:PHA03307  189 PPAEPppsTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTR 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  941 QASNLISTAGQPGPHSQSGPGAPMKQAPAPSqPPTSQGPPKSTGqaPPAPAKSIPVKKETKAPAAEKLEPKAEQAPTVKR 1020
Cdd:PHA03307  269 IWEASGWNGPSSRPGPASSSSSPRERSPSPS-PSSPGSGPAPSS--PRASSSSSSSRESSSSSTSSSSESSRGAAVSPGP 345
                         330       340
                  ....*....|....*....|...
gi 150170670 1021 TETEkKPPPIKDSKSLTAEPQKA 1043
Cdd:PHA03307  346 SPSR-SPSPSRPPPPADPSSPRK 367
PDZ10_MUPP1-PDZ8_PATJ-like cd06673
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ...
4512-4577 4.84e-06

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: 47.67  E-value: 4.84e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670 4512 GLGIRIVGGKEIPghsgeIGA-YIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQ 4577
Cdd:cd06673    14 GLGLSIVGGSDTL-----LGAiIIHEVYEDGAAAKDGRLWAGDQILEVNGEDLRKATHDEAINVLRQ 75
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
4510-4581 5.12e-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: 47.56  E-value: 5.12e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150170670 4510 GNGLGIRIVGGKEIpghsgeiGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTSKTYEE-VQSIISQQSGE 4581
Cdd:cd06729    10 GGSVGLRLAGGNDV-------GIFVAGVQEGSPAEKQG-LQEGDQILKVNGVDFRNLTREEaVLFLLDLPKGE 74
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
331-591 5.39e-06

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


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 52.62  E-value: 5.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  331 PPAQPSGLTKPLAQQPGTVKPPVQppgttKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQ--PGPA 408
Cdd:cd22540    39 PPAVEAAVTPPAPPQPTPRKLVPI-----KPAPLPLGPGKNSIGFLSAKGNIIQLQGSQLSSSAPGGQQVFAIQnpTMII 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  409 KPPTQQVGTPKPLAQQPGLQspakapgptkTPVQQPGPGKIpaqQAGPGKTSAQ----QTGPTKPPSQLPGPAKPPPQQP 484
Cdd:cd22540   114 KGSQTRSSTNQQYQISPQIQ----------AAGQINNSGQI---QIIPGTNQAIitpvQVLQQPQQAHKPVPIKPAPLQT 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  485 GPA-KPPPQQPGSA--KPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQT 561
Cdd:cd22540   181 SNTnSASLQVPGNVikLQSGGNVALTLPVNNLVGTQDGATQLQLAAAPSKPSKKIRKKSAQAAQPAVTVAEQVETVLIET 260
                         250       260       270
                  ....*....|....*....|....*....|
gi 150170670  562 GSGKPLQPPTvSPSAKQPPSQGLPKTICPL 591
Cdd:cd22540   261 TADNIIQAGN-NLLIVQSPGTGQPAVLQQV 289
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
313-446 5.43e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 52.79  E-value: 5.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  313 KPPAqqpGHEKSQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQ---PPGTTKPPAQPLGPAKP-PAQQTGSEKPSSEQPGP 388
Cdd:PRK14951  365 KPAA---AAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPaaaPAAAASAPAAPPAAAPPaPVAAPAAAAPAAAPAAA 441
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670  389 KALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPglqsPAKAPGPTKTPVQQPGP 446
Cdd:PRK14951  442 PAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPA----PAAAPAAARLTPTEEGD 495
PDZ3_PTPN13_FRMPD2-like cd06695
PDZ domain 3 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), FERM and PDZ ...
4509-4581 5.60e-06

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


Pssm-ID: 467181 [Multi-domain]  Cd Length: 90  Bit Score: 47.64  E-value: 5.60e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670 4509 SGNGLGIRIVGGK-EIPGHSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGE 4581
Cdd:cd06695     9 GSSGLGFSFLGGEnNSPEDPFSGLVRIKKLFPGQPAAESGLIQEGDVILAVNGEPLKGLSYQEVLSLLRGAPPE 82
PDZ_AFDN-like cd06789
PDZ domain of afadin (AFDN), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
4510-4577 5.62e-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: 47.67  E-value: 5.62e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670 4510 GNGLGIRIVGGKEIpgHSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQ 4577
Cdd:cd06789    12 GNGMGLSIVAAKGA--GQDKLGIYIKSVVKGGAADLDGRLQAGDQLLSVDGHSLVGLSQERAAELMTK 77
C2_NEDD4_NEDD4L cd04033
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ...
4709-4812 5.72e-06

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: 48.89  E-value: 5.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4709 LIIHILQARNLVPRDNNGYSDPFVKVYLLPGR--GQVMVVQnasaeykrrTKHVQKSLNPEWNQTVIYKSISMEQlkkkT 4786
Cdd:cd04033     2 LRVKVLAGIDLAKKDIFGASDPYVKISLYDPDgnGEIDSVQ---------TKTIKKTLNPKWNEEFFFRVNPREH----R 68
                          90       100
                  ....*....|....*....|....*.
gi 150170670 4787 LEVTVWDYDRFSSNDFLGEVLIDLSS 4812
Cdd:cd04033    69 LLFEVFDENRLTRDDFLGQVEVPLNN 94
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
652-1016 5.74e-06

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 52.85  E-value: 5.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   652 PVPSSPQPKLKTAPVTTTSAVSKSSPQPQQTSPKKDAAPKQDLSKAPEPKKPPPLVkqpTLHgSPSAKAKQPPEADSLSK 731
Cdd:pfam03154  180 AASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTP---TLH-PQRLPSPHPPLQPMTQP 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   732 PAPPKEPSVPSEQDKA---------PVADDKPKQPKMVKPTT-DLVSSSSATTKPDIPSSKVQSQAEEKTTPPLKTDSAK 801
Cdd:pfam03154  256 PPPSQVSPQPLPQPSLhgqmppmphSLQTGPSHMQHPVPPQPfPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQ 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   802 PSQsfpPTGEKVSPFDSKAIP--RPASDSKIISHPGPSSESKGQKQVDPvqkkeEPKKAQTKMSPKPDAKPMPKGSP-TP 878
Cdd:pfam03154  336 SQQ---PPREQPLPPAPLSMPhiKPPPTTPIPQLPNPQSHKHPPHLSGP-----SPFQMNSNLPPPPALKPLSSLSThHP 407
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   879 PGPRPTAGQTVPTPQQSPKPQEQSRrfslnlgSITDAPKSQPTTPQETVTGKLFGfGASIFSQASNLISTAGQPGPHSQS 958
Cdd:pfam03154  408 PSAHPPPLQLMPQSQQLPPPPAQPP-------VLTQSQSLPPPAASHPPTSGLHQ-VPSQSPFPQHPFVPGGPPPITPPS 479
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670   959 GPGAPMKQAPAPSQPPTSqGPPKSTGQAPPAPAKSIPVKKETKAPAAEKLEPKAEQAP 1016
Cdd:pfam03154  480 GPPTSTSSAMPGIQPPSS-ASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPP 536
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
326-587 5.78e-06

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 52.62  E-value: 5.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  326 PGPAKPPAQPSGltkplAQQPGTVKPPVQPPGTTKPPAQPlGPAKPPAQQTGSEKPSSEQPGPKalaqppgvgktPAQQP 405
Cdd:PLN03209  324 PSQRVPPKESDA-----ADGPKPVPTKPVTPEAPSPPIEE-EPPQPKAVVPRPLSPYTAYEDLK-----------PPTSP 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  406 GPAkPPTQQVGTPKPL--AQQPGLQSPAKAPGPTKTpVQQPGPGKIPAQQAGPGKTSAQQTGpTKPPSqLPGPAKPPPQQ 483
Cdd:PLN03209  387 IPT-PPSSSPASSKSVdaVAKPAEPDVVPSPGSASN-VPEVEPAQVEAKKTRPLSPYARYED-LKPPT-SPSPTAPTGVS 462
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  484 PGPAKPP--PQQPGSAKPPS----QQPGSTKPPPQQP--------GPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKP 549
Cdd:PLN03209  463 PSVSSTSsvPAVPDTAPATAatdaAAPPPANMRPLSPyavyddlkPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALA 542
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 150170670  550 SAQQSTKPvsqtgSGKPLQPPTVSPSAKqPPSQGLPKT 587
Cdd:PLN03209  543 DEQHHAQP-----KPRPLSPYTMYEDLK-PPTSPTPSP 574
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
448-684 5.87e-06

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 52.62  E-value: 5.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  448 KIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPP-----PQQPGSA----KPPsqqpgsTKPPPQQPGPAK 518
Cdd:PLN03209  322 KIPSQRVPPKESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKavvprPLSPYTAyedlKPP------TSPIPTPPSSSP 395
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  519 PSPQQPGSTKPPSQ---QPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTvSPSAKQPPSQGLPKTicplcnTT 595
Cdd:PLN03209  396 ASSKSVDAVAKPAEpdvVPSPGSASNVPEVEPAQVEAKKTRPLSPYARYEDLKPPT-SPSPTAPTGVSPSVS------ST 468
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  596 ELLLHVPEKANFNTCTECQTTVCSlcgfNPNPH-LTEVKEWLCLNCQMKRALGGDLAPVPSSPQPKLKTAPVTTTSAVSK 674
Cdd:PLN03209  469 SSVPAVPDTAPATAATDAAAPPPA----NMRPLsPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADE 544
                         250
                  ....*....|...
gi 150170670  675 ---SSPQPQQTSP 684
Cdd:PLN03209  545 qhhAQPKPRPLSP 557
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
718-1053 6.18e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.77  E-value: 6.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  718 AKAKQPP--EADSLSKPAPPKEPSVPSEQDKAPvaDDKPKQPKMVKPttdlvssSSATTKPDIPSSKVQSQAEEKTTPPL 795
Cdd:PTZ00449  492 SKKKLAPieEEDSDKHDEPPEGPEASGLPPKAP--GDKEGEEGEHED-------SKESDEPKEGGKPGETKEGEVGKKPG 562
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  796 KTDSAKPSQSFPPTGEKVSPFDSKAIPRPASDSKIISHPGPSSESKGQKQVDPvQKKEEPKKAQTKMSPKPDAKPMPKGS 875
Cdd:PTZ00449  563 PAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLP-ELLDIPKSPKRPESPKSPKRPPPPQR 641
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  876 PTPPG-PRPTAGQTVPTPQQSPK-PQEQSRRFSLNLGSITDAPKSQPTTPQETVTGKLFGFGASIFSQASNLISTAGQP- 952
Cdd:PTZ00449  642 PSSPErPEGPKIIKSPKPPKSPKpPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPRPl 721
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  953 ---GPHSQSGPGAPMKQAPAPSQPPTSQGPP--------KSTGQAPPAPA------KSIPVKKETKAPaaeklepkaEQA 1015
Cdd:PTZ00449  722 ppkLPRDEEFPFEPIGDPDAEQPDDIEFFTPpeeertffHETPADTPLPDilaeefKEEDIHAETGEP---------DEA 792
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 150170670 1016 PTVKRTETEKKPPPIKDSKSLTAEPQK----AVLPTKLEKSP 1053
Cdd:PTZ00449  793 MKRPDSPSEHEDKPPGDHPSLPKKRHRldglALSTTDLESDA 834
PTZ00121 PTZ00121
MAEBL; Provisional
1153-1712 6.73e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 6.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1153 QVKLVKKQEQEVKTEAEKVILEKVKETLSMEKIPP--MVTTDQKQEESKL-EKDKASAL---QEKKPLPE----EKKLIP 1222
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEarMAHFARRQAAIKAeEARKADELkkaEEKKKADEakkaEEKKKA 1304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1223 EEEKIRSEEKKPLLEEKKPTPEDKKLLPEAKTSAPEEQKHD-LLKSQVQIAEEKLEGRVAPKTVQEGKQPQTKMEGLPSG 1301
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAeAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK 1384
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1302 TPQSLPKEDDKTTKTIKEQPQppctaKPDQVEPGKEKTEKEDD-KSDTSSSQQPKSPQGLSDTGYSSDGISSSlgeipsl 1380
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKK-----KADELKKAAAAKKKADEaKKKAEEKKKADEAKKKAEEAKKADEAKKK------- 1452
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1381 ipTDEKDILKGLKKdsfsqESSPSSPSDLAKLESTvlsilEAQASTLADEKSEKKTQPHEVSPEQPKDQEKTQSLSETLE 1460
Cdd:PTZ00121 1453 --AEEAKKAEEAKK-----KAEEAKKADEAKKKAE-----EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1461 ITISEEEIKESQEERKDTFKKDSQ----QDIPSSKDHKEKSEFVDDITTRREPYDSVEESSESENSPVPQRKRRTSVGSS 1536
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEkkkaDELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1537 SSDEYKQEDSQGSGEEEDFIRKqiiemsadEDASGSEDDEFIRNQLKEiSSSTESQKKEETKGKGKITAGKHRRLTRKSs 1616
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKA--------EELKKAEEEKKKVEQLKK-KEAEEKKKAEELKKAEEENKIKAAEEAKKA- 1670
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1617 tsiDEDAGRRHSWHDEDDEAFDESPELKYRETKSQESEELVVTGGGGLRRFKTI----ELNSTIAD--KYSAESSQKKT- 1689
Cdd:PTZ00121 1671 ---EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELkkaeEENKIKAEeaKKEAEEDKKKAe 1747
                         570       580
                  ....*....|....*....|...
gi 150170670 1690 SLYFDEEPELEMESLTDSPEDRS 1712
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKA 1770
C2C_Ferlin cd04018
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
4722-4815 6.99e-06

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: 49.17  E-value: 6.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4722 RDNNGYSDPFVKVYLLpgrGQvmvvqnasaeyKRRTKHVQKSLNPEWNQTVIYKSI--SMEQlkkkTLEVTVWDYDRFSS 4799
Cdd:cd04018    29 GEKKELVDPYVEVSFA---GQ-----------KVKTSVKKNSYNPEWNEQIVFPEMfpPLCE----RIKIQIRDWDRVGN 90
                          90
                  ....*....|....*.
gi 150170670 4800 NDFLGEVLIDLSSTSH 4815
Cdd:cd04018    91 DDVIGTHFIDLSKISN 106
PRK14948 PRK14948
DNA polymerase III subunit gamma/tau;
335-550 7.40e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237862 [Multi-domain]  Cd Length: 620  Bit Score: 52.27  E-value: 7.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  335 PSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPlgPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQQ 414
Cdd:PRK14948  361 PSAFISEIANASAPANPTPAPNPSPPPAPIQ--PSAPKTKQAATTPSPPPAKASPPIPVPAEPTEPSPTPPANAANAPPS 438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  415 VGTpKPLAQQ--PGLQSPAkapgpTKTPVQQPG------PGKIPAQQAG----------PGKTSA--------------Q 462
Cdd:PRK14948  439 LNL-EELWQQilAKLELPS-----TRMLLSQQAelvsldSNRAVIAVSPnwlgmvqsrkPLLEQAfakvlgrsiklnleS 512
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  463 QTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPgstkPPPQQPGPAKPSPQQPGSTKPPSQQPgsakPSAQ 542
Cdd:PRK14948  513 QSGSASNTAKTPPPPQKSPPPPAPTPPLPQPTATAPPPTPPP----PPPTATQASSNAPAQIPADSSPPPPI----PEEP 584

                  ....*...
gi 150170670  543 QPSPAKPS 550
Cdd:PRK14948  585 TPSPTKDS 592
PRK11633 PRK11633
cell division protein DedD; Provisional
479-560 7.78e-06

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 50.39  E-value: 7.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  479 PPPQQPGPAKPPP-----QQPGSAKPPSQQPGSTKPPP----QQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPA-K 548
Cdd:PRK11633   57 PAATQALPTQPPEgaaeaVRAGDAAAPSLDPATVAPPNtpvePEPAPVEPPKPKPVEKPKPKPKPQQKVEAPPAPKPEpK 136
                          90
                  ....*....|..
gi 150170670  549 PSAQQSTKPVSQ 560
Cdd:PRK11633  137 PVVEEKAAPTGK 148
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
391-579 9.09e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 52.16  E-value: 9.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  391 LAQPPGVGKTPAqqPGPAKPPTQQVGTPKPLAQqpglqsPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPP 470
Cdd:PRK07003  356 LAFEPAVTGGGA--PGGGVPARVAGAVPAPGAR------AAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPP 427
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  471 SQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGStKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPS 550
Cdd:PRK07003  428 AAPAPPATADRGDDAADGDAPVPAKANARASADSRC-DERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAA 506
                         170       180
                  ....*....|....*....|....*....
gi 150170670  551 AQQSTKPVSQTGSGKPLQPPTVSPSAKQP 579
Cdd:PRK07003  507 VPDARAPAAASREDAPAAAAPPAPEARPP 535
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
491-588 9.18e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 52.09  E-value: 9.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  491 PQQPGSAKPPSQQPGSTKPPPQQPGpakpSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPV--SQTGSGKPLQ 568
Cdd:PRK14971  363 TQKGDDASGGRGPKQHIKPVFTQPA----AAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTvsVDPPAAVPVN 438
                          90       100
                  ....*....|....*....|
gi 150170670  569 PPTVSPSAKQPPSQGLPKTI 588
Cdd:PRK14971  439 PPSTAPQAVRPAQFKEEKKI 458
C2B_Synaptotagmin-15 cd08409
C2 domain second repeat present in Synaptotagmin 15; Synaptotagmin is a membrane-trafficking ...
4695-4808 9.29e-06

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: 48.49  E-value: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4695 TGEIQLQINYD--LGNLIIHILQARNLVPRDNNGySDPFVKVYLLPGRGQVMvvqnasaeyKRRTKHVQKSLNPEWNQTV 4772
Cdd:cd08409     1 LGDIQISLTYNptLNRLTVVVLRARGLRQLDHAH-TSVYVKVSLMIHNKVVK---------TKKTEVVDGAASPSFNESF 70
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 150170670 4773 IYKsISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLI 4808
Cdd:cd08409    71 SFK-VTSRQLDTASLSLSVMQSGGVRKSKLLGRVVL 105
PRK12727 PRK12727
flagellar biosynthesis protein FlhF;
343-546 1.09e-05

flagellar biosynthesis protein FlhF;


Pssm-ID: 237182 [Multi-domain]  Cd Length: 559  Bit Score: 51.91  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  343 AQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQP---------GPKALAQPPGVgktPAQQPGPAkpPTQ 413
Cdd:PRK12727   57 TARSDTPATAAAPAPAPQAPTKPAAPVHAPLKLSANANMSQRQRvasaaedmiAAMALRQPVSV---PRQAPAAA--PVR 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  414 QVGTPKPLAQqpglqspAKAPGPTKTPVQQPGPG--KIPAQqagpGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPP 491
Cdd:PRK12727  132 AASIPSPAAQ-------ALAHAAAVRTAPRQEHAlsAVPEQ----LFADFLTTAPVPRAPVQAPVVAAPAPVPAIAAALA 200
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670  492 QQPGSAKPPSQQPGSTKPPPQQ-PGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSP 546
Cdd:PRK12727  201 AHAAYAQDDDEQLDDDGFDLDDaLPQILPPAALPPIVVAPAAPAALAAVAAAAPAP 256
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
328-522 1.24e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.10  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  328 PAKPPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGP-AKPPAQQTGSEKPSSEQPGPKALAQPPGvgktPAQQPG 406
Cdd:PHA03307  765 PAKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSgPAADAASRTASKRKSRSHTPDGGSESSG----PARPPG 840
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  407 PAkpptqqvGTPKPLAQQPGLQSPAKAPGPtktpvqqPGPGKIPAQQAGPGKTSAQQTGPTKPPSQ-LPGPAKPPPQQPG 485
Cdd:PHA03307  841 AA-------ARPPPARSSESSKSKPAAAGG-------RARGKNGRRRPRPPEPRARPGAAAPPKAAaAAPPAGAPAPRPR 906
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 150170670  486 PAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQ 522
Cdd:PHA03307  907 PAPRVKLGPMPPGGPDPRGGFRRVPPGDLHTPAPSAA 943
SAP130_C pfam16014
Histone deacetylase complex subunit SAP130 C-terminus;
446-585 1.24e-05

Histone deacetylase complex subunit SAP130 C-terminus;


Pssm-ID: 464973 [Multi-domain]  Cd Length: 371  Bit Score: 51.09  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   446 PGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQqpgPAKPPPQQPGSAkpPSQQPGS---TKPPPQQPGPAKPSPQ 522
Cdd:pfam16014   32 PPVTVAVEALPGQNSEQQTASASPPSQHPAQAIPTIL---APAAPPSQPSVV--LSTLPAAmavTPPIPASMANVVAPPT 106
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670   523 QPGSTKPPSQQPGSAKPSAQQPSPAKP-SAQQSTKPVSQTGSGKPLqpPTVSPSAKQPPSQGLP 585
Cdd:pfam16014  107 QPAASSTAACAVSSVLPEIKIKQEAEPmDTSQSVPPLTPTSISPAL--TSLANNLSVPAGDLLP 168
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
327-487 1.32e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 51.64  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  327 GPAKPPAQPSGLTKPLAQQPGTVKPPvqppgttkPPAQPLGPAKPPAQQTgsekpsSEQPGPKALAQPPGVGKTPAQQPG 406
Cdd:PRK14951  370 AEAAAPAEKKTPARPEAAAPAAAPVA--------QAAAAPAPAAAPAAAA------SAPAAPPAAAPPAPVAAPAAAAPA 435
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  407 PAKPPtqqvgTPKPLAQQPGLQSPAkAPGPTKTPVQ-QPGPgkiPAQQAGPgktsaqqtgptkPPSQLPGPAKPPPQQPG 485
Cdd:PRK14951  436 AAPAA-----APAAVALAPAPPAQA-APETVAIPVRvAPEP---AVASAAP------------APAAAPAAARLTPTEEG 494

                  ..
gi 150170670  486 PA 487
Cdd:PRK14951  495 DV 496
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
269-422 1.40e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 51.40  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  269 HAKLPLQRDASRPQTKQADIVRGESVKPSLPSPSKPPIQQPTPGKP-PAQQPgheksQPGPAKPPAQPSGLTKPLAQQPG 347
Cdd:PRK07994  360 HPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASaPQQAP-----AVPLPETTSQLLAARQQLQRAQG 434
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  348 TVKPPVQPPGTTKPP-----AQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLA 422
Cdd:PRK07994  435 ATKAKKSEPAAASRArpvnsALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKALEHEKTPELAA 514
PHA03378 PHA03378
EBNA-3B; Provisional
654-1043 1.44e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 51.61  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  654 PSSPQPKL-KTAPVTTTSAVSKSSPQPQQTSPKKDAAPKQDLSKAPEPKKPPPLVKQPTLHGSPSAKAKQPPeadslsKP 732
Cdd:PHA03378  527 PSPPQPRAgRRAPCVYTEDLDIESDEPASTEPVHDQLLPAPGLGPLQIQPLTSPTTSQLASSAPSYAQTPWP------VP 600
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  733 APPKEPSVPSEQDKAPVADDKPKQPKMVKP-----------TTDLVSSSSATTKPDIPSSKVQSQAEEKTTPPLKTDSAK 801
Cdd:PHA03378  601 HPSQTPEPPTTQSHIPETSAPRQWPMPLRPipmrplrmqpiTFNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTG 680
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  802 PSQSFPPTGEKVSPFDSKAIPRPASDSKIisHPGPSSESKGQKQVDPV-----QKKEEPKKAQTKMSP---KPDAKPMPK 873
Cdd:PHA03378  681 ANTMLPIQWAPGTMQPPPRAPTPMRPPAA--PPGRAQRPAAATGRARPpaaapGRARPPAAAPGRARPpaaAPGRARPPA 758
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  874 GSPT---PPGPRPTAGQTVPTPQQSPKPQEQSRrfslnlGSITDAPKSQ-PTTPQETVTGKLFGFGASIFSQASNLISTA 949
Cdd:PHA03378  759 AAPGrarPPAAAPGAPTPQPPPQAPPAPQQRPR------GAPTPQPPPQaGPTSMQLMPRAAPGQQGPTKQILRQLLTGG 832
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  950 GQPGPHSQSGPGAPMKQAPAPSQPPTSQGPPKSTGQAP---PAPAKSIPVKKETKAPAAEKLEpKAEQAPTVKRTET--- 1023
Cdd:PHA03378  833 VKRGRPSLKKPAALERQAAAGPTPSPGSGTSDKIVQAPvfyPPVLQPIQVMRQLGSVRAAAAS-TVTQAPTEYTGERrgv 911
                         410       420
                  ....*....|....*....|....*
gi 150170670 1024 -----EKKPPPIKDSKSLTAEPQKA 1043
Cdd:PHA03378  912 gpmhpTDIPPSKRAKTDAYVESQPP 936
C2_putative_Elicitor-responsive_gene cd04049
C2 domain present in the putative elicitor-responsive gene; In plants elicitor-responsive ...
4707-4810 1.65e-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: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4707 GNLIIHILQARNLvpRDNN--GYSDPFVkvyLLPGRGQVmvvqnasaeykRRTKhVQKSL--NPEWNQTVIYKsISMEQL 4782
Cdd:cd04049     1 GTLEVLLISAKGL--QDTDflGKIDPYV---IIQCRTQE-----------RKSK-VAKGDgrNPEWNEKFKFT-VEYPGW 62
                          90       100
                  ....*....|....*....|....*....
gi 150170670 4783 KKKT-LEVTVWDYDRFSSNDFLGEVLIDL 4810
Cdd:cd04049    63 GGDTkLILRIMDKDNFSDDDFIGEATIHL 91
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
329-434 1.75e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 51.31  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  329 AKPPAQPSGLTKPL------AQQPGTVKPPVQPPGTTKPPAQPlgPAKPPA-QQTGSEKPSSEQPGPKALAQPPGVGK-- 399
Cdd:PRK14971  369 ASGGRGPKQHIKPVftqpaaAPQPSAAAAASPSPSQSSAAAQP--SAPQSAtQPAGTPPTVSVDPPAAVPVNPPSTAPqa 446
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 150170670  400 -TPAQQPGPAKPPTQQVGTPKPLAQQPgLQSPAKAP 434
Cdd:PRK14971  447 vRPAQFKEEKKIPVSKVSSLGPSTLRP-IQEKAEQA 481
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
947-1027 1.90e-05

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 51.43  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  947 STAGQPGPHSQSGPGAPMKQAPAPSQPPTSQGPPKSTGQAPPAPAKsipvKKETKAPAAEKLEPKAEQAPTVKRTETEKK 1026
Cdd:PRK12270   43 APTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAA----AAAAAAAPAAPPAAAAAAAPAAAAVEDEVT 118

                  .
gi 150170670 1027 P 1027
Cdd:PRK12270  119 P 119
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
4506-4587 1.92e-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: 46.11  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4506 HTV-----SGNGLGIRIVGGKEIPG-HSGEIGAYIAKILPGGSAEqtGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQS 4579
Cdd:cd06727     1 HTVtlhraPGFGFGIAVSGGRDNPHfQSGDTSIVISDVLKGGPAE--GKLQENDRVVSVNGVSMENVEHSFAVQILRKCG 78

                  ....*...
gi 150170670 4580 GEAEICVR 4587
Cdd:cd06727    79 KTANITVK 86
PDZ3_LNX1_2-like cd06679
PDZ domain 3 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
4513-4587 2.16e-05

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: 45.71  E-value: 2.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150170670 4513 LGIRIVGGKEipGHSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGEAEICVR 4587
Cdd:cd06679    13 LGISVAGGRG--SRRGDLPIYVTNVQPDGCLGRDGRIKKGDVLLSINGISLTNLSHSEAVAVLKASAASSSIVLK 85
PHA03160 PHA03160
hypothetical protein; Provisional
446-560 2.27e-05

hypothetical protein; Provisional


Pssm-ID: 165431  Cd Length: 499  Bit Score: 50.47  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  446 PGKIPAQQAG------PGKTSAQQTGPTKppsqLPGPAKPPPQQPGPAKPPPQQPGSAK-PPSQQPgSTKPPPQQPgPAK 518
Cdd:PHA03160  376 PNRIIPHHFSnpysfdPGHAPFFRYAPYG----APKNDHHLLPPLACSQQLPMQPLHVQqAPMQAP-HVAPPPMQP-PHV 449
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 150170670  519 PSPQQPGSTKPPSQQpgSAKPSAQQPSPAKPSAQQStkPVSQ 560
Cdd:PHA03160  450 QQPRVLPSTDGASNE--APKPSAQEPVHIDASFAQD--PVSK 487
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
485-590 2.29e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 50.87  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  485 GPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSqtgsg 564
Cdd:PRK14951  369 AAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPA----- 443
                          90       100
                  ....*....|....*....|....*.
gi 150170670  565 kPLQPPTVSPSAKQPPSQGLPKTICP 590
Cdd:PRK14951  444 -AVALAPAPPAQAAPETVAIPVRVAP 468
PRK14954 PRK14954
DNA polymerase III subunits gamma and tau; Provisional
443-566 2.36e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184918 [Multi-domain]  Cd Length: 620  Bit Score: 50.71  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  443 QPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPpqQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQ 522
Cdd:PRK14954  375 RNDGGVAPSPAGSPDVKKKAPEPDLPQPDRHPGPAKPEAPGARPAELP--SPASAPTPEQQPPVARSAPLPPSPQASAPR 452
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 150170670  523 QPGSTKpPSQQPGS---------AKPSAQQPspakpsAQQSTKPVSQTGSGKP 566
Cdd:PRK14954  453 NVASGK-PGVDLGSwqgkfmnftRNGSRKQP------VQASSSDAAQTGVFEG 498
PDZ_MPP5-like cd06798
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related ...
4534-4580 2.41e-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: 45.41  E-value: 2.41e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 150170670 4534 IAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSG 4580
Cdd:cd06798    25 ISRIVKGGAAEKSGLLHEGDEILEINGIEIRGKDVNEVCDLLADMHG 71
PRK11901 PRK11901
hypothetical protein; Reviewed
367-540 2.47e-05

hypothetical protein; Reviewed


Pssm-ID: 237015 [Multi-domain]  Cd Length: 327  Bit Score: 50.07  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  367 GPAKPPAQQT----GSEK-----PSSEQPGPkalAQPPGVGKTPAQqPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPgpt 437
Cdd:PRK11901   60 SPTEHESQQSsnnaGAEKnidlsGSSSLSSG---NQSSPSAANNTS-DGHDASGVKNTAPPQDISAPPISPTPTQAA--- 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  438 ktPVQQPG-------PGKIP---AQQAG------PGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPs 501
Cdd:PRK11901  133 --PPQTPNgqqrielPGNISdalSQQQGqvnaasQNAQGNTSTLPTAPATVAPSKGAKVPATAETHPTPPQKPATKKPA- 209
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 150170670  502 qqpgsTKPPPQQPGPAKPSPQ-QPGSTKPPSQQPGSAKPS 540
Cdd:PRK11901  210 -----VNHHKTATVAVPPATSgKPKSGAASARALSSAPAS 244
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
235-565 2.60e-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: 50.69  E-value: 2.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   235 TPKSISSQQPEKIKSQPPGTGKPIQGPTQT---PQTDHAKLPLQRDASR-PQTKQADIVRGESVKPSLPSPskppiqqPT 310
Cdd:pfam05109  416 THKVIFSKAPESTTTSPTLNTTGFAAPNTTtglPSSTHVPTNLTAPASTgPTVSTADVTSPTPAGTTSGAS-------PV 488
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   311 PGKPPAQQPGHEKSQPGPAKPPaqpSGLTKPL----AQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQP 386
Cdd:pfam05109  489 TPSPSPRDNGTESKAPDMTSPT---SAVTTPTpnatSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTP 565
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   387 GPKALAqpPGVGKTPaqqpgpakpPTQQVGTPKPLAQQP--GLQSPAKAP------GPTKTPV-QQPGPGKIPAQQAGPG 457
Cdd:pfam05109  566 TPNATI--PTLGKTS---------PTSAVTTPTPNATSPtvGETSPQANTtnhtlgGTSSTPVvTSPPKNATSAVTTGQH 634
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   458 K-TSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPP-----------------PQQPG----SAKPPSQQPGSTKpppQQPG 515
Cdd:pfam05109  635 NiTSSSTSSMSLRPSSISETLSPSTSDNSTSHMPlltsahptggenitqvtPASTSthhvSTSSPAPRPGTTS---QASG 711
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 150170670   516 PAKPSPqqpgSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGK 565
Cdd:pfam05109  712 PGNSST----STKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGK 757
PDZ3_Par3-like cd23059
PDZ domain 3 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ...
4512-4575 2.67e-05

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


Pssm-ID: 467272 [Multi-domain]  Cd Length: 103  Bit Score: 46.12  E-value: 2.67e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670 4512 GLGIRIVG--GKEIPGHSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSII 4575
Cdd:cd23059    17 GLGVSVKGktSKEDNGGKADLGIFIKSIIHGGAASKDGRLRVNDQLIAVNGESLLGLTNSEAMETL 82
PDZ2_DLG5-like cd06765
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
4515-4576 2.92e-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: 45.03  E-value: 2.92e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150170670 4515 IRIVGGKEiPGHSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIIS 4576
Cdd:cd06765     2 INLSGQKD-SGISLENGVFISRIVPGSPAAKEGSLTVGDRIIAINGIALDNKSLSECEALLR 62
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
468-582 3.02e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 50.25  E-value: 3.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  468 KPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQ--QPGSAKPSAQQPS 545
Cdd:PRK07994  360 HPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAarQQLQRAQGATKAK 439
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150170670  546 PAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPSQ 582
Cdd:PRK07994  440 KSEPAAASRARPVNSALERLASVRPAPSALEKAPAKK 476
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
346-511 3.28e-05

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 47.17  E-value: 3.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   346 PGTVKPPVQPPGTTKPPAQPLGPAKPPAqqtgsekPSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQP 425
Cdd:pfam06346    7 PGDSSTIPLPPGACIPTPPPLPGGGGPP-------PPPPLPGSAAIPPPPPLPGGTSIPPPPPLPGAASIPPPPPLPGST 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   426 GLQSPAKAPGPTKTPvqqPGPGKIPAqqaGPGKtsaqqtgPTKPPSQLPGPAKPPPqqpgpaKPPPQQPGSAKPPsqqPG 505
Cdd:pfam06346   80 GIPPPPPLPGGAGIP---PPPPPLPG---GAGV-------PPPPPPLPGGPGIPPP------PPFPGGPGIPPPP---PG 137

                   ....*.
gi 150170670   506 STKPPP 511
Cdd:pfam06346  138 MGMPPP 143
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
455-538 3.37e-05

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 50.66  E-value: 3.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  455 GPGKTSAQQTGPTKP----PSQLPGPAKPPPQQPGPAKPPPQQPgSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPP 530
Cdd:PRK12270   37 GPGSTAAPTAAAAAAaaaaSAPAAAPAAKAPAAPAPAPPAAAAP-AAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVED 115
                          90
                  ....*....|
gi 150170670  531 SQQP--GSAK 538
Cdd:PRK12270  116 EVTPlrGAAA 125
PRK14965 PRK14965
DNA polymerase III subunits gamma and tau; Provisional
461-527 3.64e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237871 [Multi-domain]  Cd Length: 576  Bit Score: 50.13  E-value: 3.64e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150170670  461 AQQTGPTKPPSQLPGPAKPPPQQPGP--AKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPS--PQQPGST 527
Cdd:PRK14965  376 ALERGAPAPPSAAWGAPTPAAPAAPPpaAAPPVPPAAPARPAAARPAPAPAPPAAAAPPARSadPAAAASA 446
PHA03418 PHA03418
hypothetical E4 protein; Provisional
338-516 3.73e-05

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 48.58  E-value: 3.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  338 LTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPS-SEQPGPKALAQPPGVGKTPAQQPGPakpptqqvg 416
Cdd:PHA03418   31 LCLPLLPAPHHPNPQEDPDKNPSPPPDPPLTPRPPAQPNGHNKPPvTKQPGGEGTEEDHQAPLAADADDDP--------- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  417 tpkplaqQPGLQSPAKAPGPTKTPvQQPGPGKIPAQQAGPgktsaqQTGPTKPPSQLPGPAKPPPQQPGPAKPPP----- 491
Cdd:PHA03418  102 -------RPGKRSKADEHGPAPGR-AALAPFKLDLDQDPL------HGDPDPPPGATGGQGEEPPEGGEESQPPLgegeg 167
                         170       180
                  ....*....|....*....|....*
gi 150170670  492 QQPGSAKPPsqqpgstkPPPQQPGP 516
Cdd:PHA03418  168 AVEGHPPPL--------PPAPEPKP 184
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
461-552 3.98e-05

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 49.62  E-value: 3.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  461 AQQTGPTKPPSQlpgpakPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPA-KPSPQQPGSTKPPSQQPGSAKP 539
Cdd:NF041121   12 AAQMGRAAAPPS------PEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLpAPYPGSLAPPPPPPPGPAGAAP 85
                          90
                  ....*....|....*
gi 150170670  540 SAQQP--SPAKPSAQ 552
Cdd:NF041121   86 GAALPvrVPAPPALP 100
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
464-544 4.02e-05

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 50.27  E-value: 4.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  464 TGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQ 543
Cdd:PRK12270   39 GSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVT 118

                  .
gi 150170670  544 P 544
Cdd:PRK12270  119 P 119
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
497-758 4.03e-05

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 49.92  E-value: 4.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  497 AKPPSQqpgstKPPPQQPGPA---KPSPQQPGSTKPPSqqpgsakpSAQQPSPAKPSAQqSTKPVSQTGSGKPLQPPTvS 573
Cdd:PLN03209  321 AKIPSQ-----RVPPKESDAAdgpKPVPTKPVTPEAPS--------PPIEEEPPQPKAV-VPRPLSPYTAYEDLKPPT-S 385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  574 PSAKQPPSQglPKTICPLCNTTelllhVPEKANFNTCTECQTTVcslcgfnpnphltEVKEWLCLNCQMKRALG-----G 648
Cdd:PLN03209  386 PIPTPPSSS--PASSKSVDAVA-----KPAEPDVVPSPGSASNV-------------PEVEPAQVEAKKTRPLSpyaryE 445
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  649 DLAPvPSSPQPKLKTA---PVTTTSAVSKSSPQPQQTSPKKDAAPKQDLSKAPEPKKPPPLVKQPTlhgSPSAKAKQPPE 725
Cdd:PLN03209  446 DLKP-PTSPSPTAPTGvspSVSSTSSVPAVPDTAPATAATDAAAPPPANMRPLSPYAVYDDLKPPT---SPSPAAPVGKV 521
                         250       260       270
                  ....*....|....*....|....*....|...
gi 150170670  726 ADSLSKPAPPKEPSVPseqDKAPVADDKPKQPK 758
Cdd:PLN03209  522 APSSTNEVVKVGNSAP---PTALADEQHHAQPK 551
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
469-586 4.17e-05

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 47.34  E-value: 4.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   469 PPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKP-SPQQPGSTKPPSQQPGSAKPSA--QQPS 545
Cdd:pfam15240   35 EEGQSQQGGQGPQGPPPGGFPPQPPASDDPPGPPPPGGPQQPPPQGGKQKPqGPPPQGGPRPPPGKPQGPPPQGgnQQQG 114
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 150170670   546 PAKPSAQQSTKPVSQTGS---GKPLQPPTVSPSAKQPPSQGLPK 586
Cdd:pfam15240  115 PPPPGKPQGPPPQGGGPPpqgGNQQGPPPPPPGNPQGPPQRPPQ 158
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
362-593 4.18e-05

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 49.48  E-value: 4.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  362 PAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPAKP-PTQQVGTPKPLAqqpgLQSPAKAPGPTKTP 440
Cdd:cd23959    53 QEEPLYGAVSPEGENPFDGPGLVTASTVSDCYVGNANFYEVDMSDAFAMaPDESLGPFRAAR----VPNPFSASSSTQRE 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  441 VQQPGPGKIPaqqagpgkTSAQQTGPTKPPSQLPGPAkpppQQPGPAKPPPqqPGSAKPPSQQPGSTKPPPQQPGPAKPS 520
Cdd:cd23959   129 THKTAQVAPP--------KAEPQTAPVTPFGQLPMFG----QHPPPAKPLP--AAAAAQQSSASPGEVASPFASGTVSAS 194
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670  521 P-QQPGSTKPPSQQPGSAKPSAQQPSPAKPSAqqstkpvsqtgSGKPLQPPTVSPSAKQPPSQGlpktiCPLCN 593
Cdd:cd23959   195 PfATATDTAPSSGAPDGFPAEASAPSPFAAPA-----------SAASFPAAPVANGEAATPTHA-----CTICG 252
PRK10905 PRK10905
cell division protein DamX; Validated
367-587 4.43e-05

cell division protein DamX; Validated


Pssm-ID: 236792 [Multi-domain]  Cd Length: 328  Bit Score: 49.17  E-value: 4.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  367 GPAKPPAQQTGSEKPS---SEQPGPKALAQPPGVGKTPAQQPGPAKPptQQVGTPkPLAQQPGL-QSPAKAPGPTKTPVQ 442
Cdd:PRK10905   22 APSTSSSDQTASGEKSidlAGNATDQANGVQPAPGTTSAEQTAGNTQ--QDVSLP-PISSTPTQgQTPVATDGQQRVEVQ 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  443 QPGPGKI--PAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPgPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPs 520
Cdd:PRK10905   99 GDLNNALtqPQNQQQLNNVAVNSTLPTEPATVAPVRNGNASRQT-AKTQTAERPATTRPARKQAVIEPKKPQATAKTEP- 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670  521 pqqpgstKPPSQQPGSAKPSAqQPSPAKPSAQQSTKPVSQTGSGKPLQppTVSPSAKQPPSQGLPKT 587
Cdd:PRK10905  177 -------KPVAQTPKRTEPAA-PVASTKAPAATSTPAPKETATTAPVQ--TASPAQTTATPAAGGKT 233
PRK11633 PRK11633
cell division protein DedD; Provisional
420-530 4.43e-05

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 48.08  E-value: 4.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  420 PLAQQPGLQSPAKA-PGPTKTPVQQPGPGKIPAQQAGPGKTSAQQtgptkpPSQLPGPAKPPPQQPGPAKPPPQQPGSAK 498
Cdd:PRK11633   42 PLVPKPGDRDEPDMmPAATQALPTQPPEGAAEAVRAGDAAAPSLD------PATVAPPNTPVEPEPAPVEPPKPKPVEKP 115
                          90       100       110
                  ....*....|....*....|....*....|..
gi 150170670  499 PPSQQPGSTKPPPQQPgpaKPSPQQPGSTKPP 530
Cdd:PRK11633  116 KPKPKPQQKVEAPPAP---KPEPKPVVEEKAA 144
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
4496-4575 4.92e-05

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: 44.66  E-value: 4.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4496 RIKITRDSKDHTvsgnGLGIRIVGGKEipgHSgeIGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTSKTYEEVQSII 4575
Cdd:cd06740     2 RQVTLKRSKSHE----GLGFSIRGGAE---HG--VGIYVSLVEPGSLAEKEG-LRVGDQILRVNDVSFEKVTHAEAVKIL 71
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
459-599 5.01e-05

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 48.77  E-value: 5.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   459 TSAQQTGPTKPPsqlPGPAKPPPqQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQ------QPGPAKPSPQQPGSTKPPSQ 532
Cdd:pfam07174   36 VAHADPEPAPPP---PSTATAPP-APPPPPPAPAAPAPPPPPAAPNAPNAPPPPadpnapPPPPADPNAPPPPAVDPNAP 111
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670   533 QPGSAKPSAQQPSPAKPSAQQSTKpVSQTGSGKPLqpptVSPSAKQPPSQGLPKticPLCNTTELLL 599
Cdd:pfam07174  112 EPGRIDNAVGGFSYVVPAGWVESD-ATHLDYGSAL----LSKTTGQPPEGGQPP---PVANDTRVVL 170
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
481-587 5.07e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 49.77  E-value: 5.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  481 PQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQpgpAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQ 560
Cdd:PRK14971  363 TQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAA---AAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPVNP 439
                          90       100
                  ....*....|....*....|....*..
gi 150170670  561 TGSGKPLQPPTVSPSAKQPPSQGLPKT 587
Cdd:PRK14971  440 PSTAPQAVRPAQFKEEKKIPVSKVSSL 466
PRK11633 PRK11633
cell division protein DedD; Provisional
440-534 5.32e-05

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 48.08  E-value: 5.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  440 PVQQPGPGKIPaqqagPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPaKPPPQQPGSAKPPSQqpgsTKPPPQQPGPAKP 519
Cdd:PRK11633   58 AATQALPTQPP-----EGAAEAVRAGDAAAPSLDPATVAPPNTPVEP-EPAPVEPPKPKPVEK----PKPKPKPQQKVEA 127
                          90
                  ....*....|....*
gi 150170670  520 SPQQPGSTKPPSQQP 534
Cdd:PRK11633  128 PPAPKPEPKPVVEEK 142
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
450-580 5.65e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 49.48  E-value: 5.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  450 PAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGStkPPPQQPGPAKPSPQQPGSTKP 529
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPE--TTSQLLAARQQLQRAQGATKA 438
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 150170670  530 PSQQPGSAKPSAQQPSPAKPSAQQStkPVSQTGSGKPLQPPTVSPSAKQPP 580
Cdd:PRK07994  439 KKSEPAAASRARPVNSALERLASVR--PAPSALEKAPAKKEAYRWKATNPV 487
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
375-533 5.76e-05

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 49.42  E-value: 5.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   375 QTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPaKPPTQQVGTPKPLAQQPGLQSPAKAPGPtktPVQQPGPGKiPAQQA 454
Cdd:TIGR01628  379 QPRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNG-QPLGWPRMSMMPTPMGPGGPLRPNGLAP---MNAVRAPSR-NAQNA 453
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670   455 gpgktsaqqtgptkppsqlpgpAKPPPQQPGPAkPPPQQPGSAKPPSQQPGSTkppPQQPGPAKPSPQQPGSTkPPSQQ 533
Cdd:TIGR01628  454 ----------------------AQKPPMQPVMY-PPNYQSLPLSQDLPQPQST---ASQGGQNKKLAQVLASA-TPQMQ 505
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
422-542 5.96e-05

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 49.42  E-value: 5.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   422 AQQPGLQSPAKAPGPT---KTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQlPGPAKPPPQQPGPAKPPPQQPGSAK 498
Cdd:TIGR01628  378 LQPRMRQLPMGSPMGGamgQPPYYGQGPQQQFNGQPLGWPRMSMMPTPMGPGGP-LRPNGLAPMNAVRAPSRNAQNAAQK 456
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 150170670   499 PPSQ----QPGSTKPPPQQPGPAKPS-PQQPGSTKPPSQQPGSAKPSAQ 542
Cdd:TIGR01628  457 PPMQpvmyPPNYQSLPLSQDLPQPQStASQGGQNKKLAQVLASATPQMQ 505
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
391-514 6.06e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 49.39  E-value: 6.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  391 LAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPP 470
Cdd:PRK14971  359 LAQLTQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPVN 438
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 150170670  471 SQLPGPAKPPPQQPGPAKP-PPQQPGSAKPPSQQPgsTKPPPQQP 514
Cdd:PRK14971  439 PPSTAPQAVRPAQFKEEKKiPVSKVSSLGPSTLRP--IQEKAEQA 481
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
402-929 6.34e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.78  E-value: 6.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  402 AQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQqpgpGKIPAQQAGPgktsaqqtgPTKPPsqlPGPAKPPP 481
Cdd:PHA03307   17 GGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVA----GAAACDRFEP---------PTGPP---PGPGTEAP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  482 QQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPsqqPGSAKPSAQQPSPAKPSAQQSTKPvsqt 561
Cdd:PHA03307   81 ANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPS---PAPDLSEMLRPVGSPGPPPAASPP---- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  562 gsgkplqPPTVSPSAKQppsqglpkticplcnttelllhvpekanfntctecqttvcslcgfnpnphltevkewlclncq 641
Cdd:PHA03307  154 -------AAGASPAAVA--------------------------------------------------------------- 163
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  642 mkralggdlAPVPSSPQPKLktaPVTTTSAVSKSSPQPQQTSPKKDAAPkqdlskapepkkppplvkqptlHGSPSAKAK 721
Cdd:PHA03307  164 ---------SDAASSRQAAL---PLSSPEETARAPSSPPAEPPPSTPPA----------------------AASPRPPRR 209
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  722 QPPEADSLSKPAP--PKEPSVPSEQD-------KAPVADDKP--KQPKMVKPTTDLVSSSSATTKPDIPSSKVQSQAEEK 790
Cdd:PHA03307  210 SSPISASASSPAPapGRSAADDAGASssdssssESSGCGWGPenECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSS 289
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  791 TTPPlktDSAKPSQSFPPTGEKVSPF-------------DSKAIPRPASDSKIISHPGPSSESKGQKQVDPVQKKEEPKK 857
Cdd:PHA03307  290 SPRE---RSPSPSPSSPGSGPAPSSPrasssssssressSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPR 366
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150170670  858 AQTKMSPKPDAKPMPKGSPTPPGPRPTAGQTvPTPQQSPKPQEQSRRFSLNLGSITDAPKSQPTTPQETVTG 929
Cdd:PHA03307  367 KRPRPSRAPSSPAASAGRPTRRRARAAVAGR-ARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPLLTPSG 437
PDZ1_hSTXBP4-PDZ2_GgSTXBP4-like cd06698
PDZ1 domain of human syntaxin-binding protein 4 (STXBP4), PDZ2 domain of Gallus gallus ...
4512-4575 6.71e-05

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


Pssm-ID: 467184 [Multi-domain]  Cd Length: 89  Bit Score: 44.60  E-value: 6.71e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670 4512 GLGIRIVGGKEipgHSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSII 4575
Cdd:cd06698    12 GLGLSIVGGIN---RPEGPMVFIQEVIPGGDCYKDGRLRPGDQLVSINKESLIGVTLEEAKSIL 72
Treacle pfam03546
Treacher Collins syndrome protein Treacle;
328-581 6.88e-05

Treacher Collins syndrome protein Treacle;


Pssm-ID: 460967 [Multi-domain]  Cd Length: 531  Bit Score: 49.30  E-value: 6.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   328 PAKPPAQPSGLTKPLAQQPGTVKPPV-QPPGTTKPPAQPLGPAKPPAQQTGSEKPS-SEQPGPKAL--AQPPGVGKTPAQ 403
Cdd:pfam03546  184 PAATQAKPSGKILQVRPASGPAKGAApAPPQKAGPVATQVKAERSKEDSESSEESSdSEEEAPAAAtpAQAKPALKTPQT 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   404 Q----------PGPAKPPTQQVGTPKP-----LAQQPGLQSPAKAPGPTKTPVQQ-------------PGPGKIPAQQAG 455
Cdd:pfam03546  264 KasprkgtpitPTSAKVPPVRVGTPAPwkagtVTSPACASSPAVARGAQRPEEDSssseeseseeetaPAAAVGQAKSVG 343
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   456 PGKTSAQQTGPTKPPSQlPGPAKPPPQQPGPAKPPPQ-QPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPgstkppsqqP 534
Cdd:pfam03546  344 KGLQGKAASAPTKGPSG-QGTAPVPPGKTGPAVAQVKaEAQEDSESSEEESDSEEAAATPAQVKASGKTP---------Q 413
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 150170670   535 GSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPS 581
Cdd:pfam03546  414 AKANPAPTKASSAKGAASAPGKVVAAAAQAKQGSPAKVKPPARTPQN 460
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
381-530 6.89e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 49.40  E-value: 6.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  381 PSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPT---KTPVQQPGPGKIPAQQAGPG 457
Cdd:PHA03307  760 NPSLVPAKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTAskrKSRSHTPDGGSESSGPARPP 839
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  458 KTSAQQTGPTKPPSQLPGPAKPPPQQPG-------PAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAkPSPQQPGSTKPP 530
Cdd:PHA03307  840 GAAARPPPARSSESSKSKPAAAGGRARGkngrrrpRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPR-PAPRVKLGPMPP 918
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
443-566 7.07e-05

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 49.03  E-value: 7.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   443 QPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGpaKPPPQQPGPAKPPPQQPGSAKPPS--QQPGSTKPPPQQPGPAKPS 520
Cdd:TIGR01628  379 QPRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNG--QPLGWPRMSMMPTPMGPGGPLRPNglAPMNAVRAPSRNAQNAAQK 456
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 150170670   521 PQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKP 566
Cdd:TIGR01628  457 PPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASATP 502
C2_Perforin cd04032
C2 domain of Perforin; Perforin contains a single copy of a C2 domain in its C-terminus and ...
4706-4815 7.16e-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: 7.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4706 LGNLIIHILQARNLvprdnNG----YSDPFVKVYLlpgRGQVmvvqnasaeykRRTKHVQKSLNPEWNQTVIYKSISMEQ 4781
Cdd:cd04032    27 LATLTVTVLRATGL-----WGdyftSTDGYVKVFF---GGQE-----------KRTEVIWNNNNPRWNATFDFGSVELSP 87
                          90       100       110
                  ....*....|....*....|....*....|....
gi 150170670 4782 LKKKTLEVtvWDYDRFSSNDFLGEVLIDLSSTSH 4815
Cdd:cd04032    88 GGKLRFEV--WDRDNGWDDDLLGTCSVVPEAGVH 119
PRK12373 PRK12373
NADH-quinone oxidoreductase subunit E;
398-566 7.28e-05

NADH-quinone oxidoreductase subunit E;


Pssm-ID: 237082 [Multi-domain]  Cd Length: 400  Bit Score: 48.64  E-value: 7.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  398 GKTPAQQPGPakpptqQVG--TPKPLAqqpGLQSPAKAPGPTKTpvqqpGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPG 475
Cdd:PRK12373  172 GKGPVVKPGP------QIGryASEPAG---GLTSLTEEAGKARY-----NASKALAEDIGDTVKRIDGTEVPLLAPWQGD 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  476 PAKPPPQqpGPAKPPPQqpgsakPPSQQPGSTKPPPQQPGPAKP--SPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQ 553
Cdd:PRK12373  238 AAPVPPS--EAARPKSA------DAETNAALKTPATAPKAAAKNakAPEAQPVSGTAAAEPAPKEAAKAAAAAAKPALED 309
                         170
                  ....*....|...
gi 150170670  554 STKPVSQTGSGKP 566
Cdd:PRK12373  310 KPRPLGIARPGGA 322
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
32-411 7.34e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.21  E-value: 7.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   32 PSHTAIPAGMEADLSQLSEEERRQIAAVMSRAQGLPKGSVPPAAAESPSMHRKQELDSSHPPKQSGRPPDPGRPAQPGLS 111
Cdd:PRK07764  427 AAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGA 506
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  112 ksRTTDTFRSE-----QKLPGRSPSTISLKESKSR------TDLKEEHKSSMMPGFLSEVNALSAVSSVVnkfnpfdlis 180
Cdd:PRK07764  507 --DDAATLRERwpeilAAVPKRSRKTWAILLPEATvlgvrgDTLVLGFSTGGLARRFASPGNAEVLVTAL---------- 574
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  181 dseasQEETTKKQKVVQKEQGKPEGiikPPLQQQPPKPIPKQQGPGRDPLQQDGTPKSISSQQPEKikSQPPGTGKPIQG 260
Cdd:PRK07764  575 -----AEELGGDWQVEAVVGPAPGA---AGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGA--AAAPAEASAAPA 644
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  261 PTQTPQTDHAKLPLQRDASRPQTKQADIVRGESVKPSLPSPSKPPIQQPTPGKPPAQQPgheKSQPGPAKPPAQPSGLTK 340
Cdd:PRK07764  645 PGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAP---APAATPPAGQADDPAAQP 721
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150170670  341 PLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQqtgsekPSSEQPGPKALAQPPGVGKTPAQQPGPAKPP 411
Cdd:PRK07764  722 PQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAP------AQPPPPPAPAPAAAPAAAPPPSPPSEEEEMA 786
PTZ00395 PTZ00395
Sec24-related protein; Provisional
451-587 7.74e-05

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 49.30  E-value: 7.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  451 AQQAGPGKTSAQ--QTGPTKPPSQLPGPAKPPPQQPGPAKPP-PQQPGSAKPPSQQPGSTKPPPQQP---GPAKPSPQQP 524
Cdd:PTZ00395  397 AAQSNAAQSNAGfsNAGYSNPGNSNPGYNNAPNSNTPYNNPPnSNTPYSNPPNSNPPYSNLPYSNTPysnAPLSNAPPSS 476
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150170670  525 GSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPSQGLPKT 587
Cdd:PTZ00395  477 AKDHHSAYHAAYQHRAANQPAANLPTANQPAANNFHGAAGNSVGNPFASRPFGSAPYGGNAAT 539
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
456-548 7.91e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 49.04  E-value: 7.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  456 PGKTSAQQTGPTKPPSQ-LPGPAKPPPqqPGPAKPPPQQPGSAKPPSQQPgstkPPPQQPGPAKPSPQQPGSTKPPSQQP 534
Cdd:PRK14950  364 PAPQPAKPTAAAPSPVRpTPAPSTRPK--AAAAANIPPKEPVRETATPPP----VPPRPVAPPVPHTPESAPKLTRAAIP 437
                          90
                  ....*....|....
gi 150170670  535 GSAKPSAQQPSPAK 548
Cdd:PRK14950  438 VDEKPKYTPPAPPK 451
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
339-810 7.98e-05

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: 49.00  E-value: 7.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  339 TKPLAQQPGTVKP--PVQPPGTTKPPAQPLGPaKPPAQQTGSEKpssEQPGPKALAQPPGVGKTPAQQPGPAKPPTQQVG 416
Cdd:NF033839  157 TKPETPQPENPEHqkPTTPAPDTKPSPQPEGK-KPSVPDINQEK---EKAKLAVATYMSKILDDIQKHHLQKEKHRQIVA 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  417 TPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQ-QPGPAKPPPQQPG 495
Cdd:NF033839  233 LIKELDELKKQALSEIDNVNTKVEIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGmQPSPQPEKKEVKP 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  496 SAKPPSQQpgsTKPPPQQPGP-AKPSPQQPGSTKPPsqQPGSAKPSAQqPSPAKPSAQQSTKPVSQTGSGKPlQPPTVSP 574
Cdd:NF033839  313 EPETPKPE---VKPQLEKPKPeVKPQPEKPKPEVKP--QLETPKPEVK-PQPEKPKPEVKPQPEKPKPEVKP-QPETPKP 385
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  575 SAKQPPSQGLPkticplcnttelllhvpekanfntctecqttvcslcgfnpnphltevkewlclncqmkralggDLAPVP 654
Cdd:NF033839  386 EVKPQPEKPKP---------------------------------------------------------------EVKPQP 402
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  655 SSPQPKLKTAPVTttsavSKSSPQPQQTSPKKDAAPKQDlskapepkkppplvkqptlhgSPSAKAKQPPEAdslSKPAP 734
Cdd:NF033839  403 EKPKPEVKPQPEK-----PKPEVKPQPEKPKPEVKPQPE---------------------KPKPEVKPQPEK---PKPEV 453
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670  735 PKEPSVPSEQDKAPVADDKPK-QPKMVKPTTDLVSSSSATTKPDIPSSKVQSQAEEKTTPPLKTDSAKPSQSFPPTG 810
Cdd:NF033839  454 KPQPETPKPEVKPQPEKPKPEvKPQPEKPKPDNSKPQADDKKPSTPNNLSKDKQPSNQASTNEKATNKPKKSLPSTG 530
PDZ4_GRIP1-2-like cd06686
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
4511-4589 8.14e-05

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: 44.64  E-value: 8.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4511 NGLGIRIVGGkeipGHSGEIGAY---IAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGEAEICVR 4587
Cdd:cd06686    18 KGFGIQLQGG----VFATETLSSpplISFIEPDSPAERCGVLQVGDRVLSINGIPTEDRTLEEANQLLRDSASKVTLEIE 93

                  ..
gi 150170670 4588 LD 4589
Cdd:cd06686    94 FD 95
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
225-490 8.21e-05

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 48.91  E-value: 8.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  225 PGRDPLQQDGTPKSISSQQPEKIKSQPPGTGKPIQGPTQT---PQTDHAKLPLQRDASRPQTKQADIVrGESVKPSLPSP 301
Cdd:COG5180   246 PATVDAQPEMRPPADAKERRRAAIGDTPAAEPPGLPVLEAgsePQSDAPEAETARPIDVKGVASAPPA-TRPVRPPGGAR 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  302 SKPPIQQPTPGKPPAQQP--GHEKSQPGPAKPPAQPSGLTKPLAQ------QPGTVKPPVQPPGTTKPPAQPLGPAKPPA 373
Cdd:COG5180   325 DPGTPRPGQPTERPAGVPeaASDAGQPPSAYPPAEEAVPGKPLEQgaprpgSSGGDGAPFQPPNGAPQPGLGRRGAPGPP 404
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  374 Q------QTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPAKPptqqVGTPKPLAQQPGlQSPAKAPGPTKTPVQQPGPG 447
Cdd:COG5180   405 MgagdlvQAALDGGGRETASLGGAAGGAGQGPKADFVPGDAES----VSGPAGLADQAG-AAASTAMADFVAPVTDATPV 479
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 150170670  448 KIPAQQAGPGKtsAQQTGPTKPPSQLPGPAKPPPQQPGPAKPP 490
Cdd:COG5180   480 DVADVLGVRPD--AILGGNVAPASGLDAETRIIEAEGAPATED 520
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
4512-4578 8.23e-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: 8.23e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670 4512 GLGIRIVGGKeipghSGeiGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTSKTYEEVQSIISQQ 4578
Cdd:cd06767    14 PLGISIVSGE-----NG--GIFVSSVTEGSLAHQAG-LEYGDQLLEVNGINLRNATEQQAALILRQC 72
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
308-456 8.40e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 49.21  E-value: 8.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  308 QPTPGKPPAQQPGHEKSQPGPAKPPAQPSGLTKPL-AQQPGTVKPPVQPPGTTKPPAQPL---GPAKPPAQqtgSEKPSS 383
Cdd:PRK07764  643 PAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAApAAPPPAPAPAAPAAPAGAAPAQPApapAATPPAGQ---ADDPAA 719
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150170670  384 EQPGPKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGP 456
Cdd:PRK07764  720 QPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPS 792
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
465-549 8.58e-05

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 49.12  E-value: 8.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  465 GPTKPPSQLPGPAKPPPQQPGPAKPPPQQPgsAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQP 544
Cdd:PRK12270   37 GPGSTAAPTAAAAAAAAAASAPAAAPAAKA--PAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVE 114

                  ....*
gi 150170670  545 SPAKP 549
Cdd:PRK12270  115 DEVTP 119
BimA_second NF040983
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ...
436-527 8.65e-05

trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia intracellular motility A), WP_004266405.1-like proteins in Burkholderia mallei or B. pseudomallei. The term BimA has also been used for WP_011205626.1-like homologs that have a very different N-terminal half.


Pssm-ID: 468913 [Multi-domain]  Cd Length: 382  Bit Score: 48.36  E-value: 8.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  436 PTKTPVQQPGPGKIPaqqagPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPqqpgSAKPPSQQPGSTKPPPQQPG 515
Cdd:NF040983   86 PNKVPPPPPPPPPPP-----PPPPTPPPPPPPPPPPPPPSPPPPPPPSPPPSPPPP----TTTPPTRTTPSTTTPTPSMH 156
                          90
                  ....*....|....
gi 150170670  516 PAKPS--PQQPGST 527
Cdd:NF040983  157 PIQPTqlPSIPNAT 170
PHA03269 PHA03269
envelope glycoprotein C; Provisional
412-544 9.01e-05

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 48.96  E-value: 9.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  412 TQQVGTPKPLAQ---QPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQqtGPTKPPSQLPGPAKPPPQQPGPAK 488
Cdd:PHA03269   19 IANLNTNIPIPElhtSAATQKPDPAPAPHQAASRAPDPAVAPTSAASRKPDLAQ--APTPAASEKFDPAPAPHQAASRAP 96
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670  489 PPPQQPGSAKPPSQQPGStkpPPQQPGPAKPSP-QQPGSTKPPSQQPGSAKPSAQQP 544
Cdd:PHA03269   97 DPAVAPQLAAAPKPDAAE---AFTSAAQAHEAPaDAGTSAASKKPDPAAHTQHSPPP 150
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
478-569 9.10e-05

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 49.12  E-value: 9.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  478 KPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPspqqpgstkPPSQQPGSAKPSAQQPSPAKPSAQQSTKP 557
Cdd:PRK12270   37 GPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAA---------APAAPPKPAAAAAAAAAPAAPPAAAAAAA 107
                          90
                  ....*....|..
gi 150170670  558 VSQTGSGKPLQP 569
Cdd:PRK12270  108 PAAAAVEDEVTP 119
PRK10263 PRK10263
DNA translocase FtsK; Provisional
3460-3965 9.36e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 49.31  E-value: 9.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3460 RRRRTKKSVDTSVQTDDEDQDEW---------DMPTRSRRKARVGKY--------GDSMTEADKTKPLSKVSSIAVQTVA 3522
Cdd:PRK10263  258 MGRQTDAALFSGKRMDDDEEITYtargvaadpDDVLFSGNRATQPEYdeydpllnGAPITEPVAVAAAATTATQSWAAPV 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3523 EISVQTEPVGTIRTPSIRARVDAKVEIIKHISAPEktykggslgCQTEADSDTQSPQYLSATSPPKDK-KRPTPLEIGYS 3601
Cdd:PRK10263  338 EPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPV---------IAPAPEGYPQQSQYAQPAVQYNEPlQQPVQPQQPYY 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3602 SHLRADSTVQLAPSPPKSPKVLYSPISPLSPGKALESAFVPYEKPLPDDisPQKVLHPDMAKVPPASPKTAKMMQRSMSD 3681
Cdd:PRK10263  409 APAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFA--PQSTYQTEQTYQQPAAQEPLYQQPQPVEQ 486
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3682 PKPLSPT--ADES--SRAPFQYTEGYTTKGSQTMTSSGA-----QKKVKRTLPN------------PPPEEIST------ 3734
Cdd:PRK10263  487 QPVVEPEpvVEETkpARPPLYYFEEVEEKRAREREQLAAwyqpiPEPVKEPEPIksslkapsvaavPPVEAAAAvsplas 566
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3735 ----GTQSTFSTMGTVSRRRICRTNTMARAKILQDIDRELDLVERESAKLRKKQAELD--------EEEKEIDAKLRYLE 3802
Cdd:PRK10263  567 gvkkATLATGAAATVAAPVFSLANSGGPRPQVKEGIGPQLPRPKRIRVPTRRELASYGiklpsqraAEEKAREAQRNQYD 646
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3803 MGINRRK---EALLKEREKRERAYLQ-------------GVAEDRDYMSDSEVSSTRPTRIESQHGIERPRTAPQTEFSQ 3866
Cdd:PRK10263  647 SGDQYNDdeiDAMQQDELARQFAQTQqqrygeqyqhdvpVNAEDADAAAEAELARQFAQTQQQRYSGEQPAGANPFSLDD 726
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3867 F-----------------IPPQTQTESQlvPPTSPYTQYQYSSPALPTQAPTSYTQ-QSHFEQQTLYHQQVSPYQTQPTF 3928
Cdd:PRK10263  727 FefspmkallddgpheplFTPIVEPVQQ--PQQPVAPQQQYQQPQQPVAPQPQYQQpQQPVAPQPQYQQPQQPVAPQPQY 804
                         570       580       590
                  ....*....|....*....|....*....|....*..
gi 150170670 3929 QavatmsftpQVQPTPTPQPSYQLPSQMMVIQQKPRQ 3965
Cdd:PRK10263  805 Q---------QPQQPVAPQPQYQQPQQPVAPQPQYQQ 832
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
487-576 9.62e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 48.65  E-value: 9.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  487 AKPPPQQPGSAKPPSQQPGSTKPPPQQP---GPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGS 563
Cdd:PRK14950  361 VPVPAPQPAKPTAAAPSPVRPTPAPSTRpkaAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVDE 440
                          90
                  ....*....|...
gi 150170670  564 GKPLQPPTVSPSA 576
Cdd:PRK14950  441 KPKYTPPAPPKEE 453
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
369-484 1.04e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 48.62  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  369 AKPPAQQTGSEKPSSEQPgpkALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQS-PAKAPGPTKTPVQQPGPG 447
Cdd:PRK14971  369 ASGGRGPKQHIKPVFTQP---AAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTvSVDPPAAVPVNPPSTAPQ 445
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150170670  448 KIPAQQAGPGKTSAQQTGPTKPPSQLpGPAKPPPQQP 484
Cdd:PRK14971  446 AVRPAQFKEEKKIPVSKVSSLGPSTL-RPIQEKAEQA 481
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
4509-4575 1.10e-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: 43.79  E-value: 1.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670 4509 SGNGLGIRIVGGKEIpghsgEIGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTSKTYEEVQSII 4575
Cdd:cd06741    10 DGQSLGLMIRGGAEY-----GLGIYVTGVDPGSVAENAG-LKVGDQILEVNGRSFLDITHDEAVKIL 70
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
428-518 1.13e-04

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 48.73  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  428 QSPAKAPGPTK--TPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPqqpgsAKPPSQQPG 505
Cdd:PRK12270   36 YGPGSTAAPTAaaAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPA-----AAAAAAPAA 110
                          90
                  ....*....|....*
gi 150170670  506 STKPPPQQP--GPAK 518
Cdd:PRK12270  111 AAVEDEVTPlrGAAA 125
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
464-585 1.27e-04

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 45.63  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   464 TGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSA--KPPSQQPGSTKPPPQQPGPAKPS----PQQPGSTKPPSQQPGSA 537
Cdd:pfam06346   10 SSTIPLPPGACIPTPPPLPGGGGPPPPPPLPGSAaiPPPPPLPGGTSIPPPPPLPGAASipppPPLPGSTGIPPPPPLPG 89
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 150170670   538 KPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAK----QPPSQGLP 585
Cdd:pfam06346   90 GAGIPPPPPPLPGGAGVPPPPPPLPGGPGIPPPPPFPGGPgippPPPGMGMP 141
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
290-471 1.28e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.44  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  290 RGESVKPSLPSPSKPPIQQPTPGKPPAQQPGHekSQPGPAKPPAQPSGLTKPLAQQPGTVKPPV------------QPPG 357
Cdd:PRK07764  596 GGEGPPAPASSGPPEEAARPAAPAAPAAPAAP--APAGAAAAPAEASAAPAPGVAAPEHHPKHVavpdasdggdgwPAKA 673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  358 TTKPPAQPLGPAKPPAQQTGSEKPSSeQPGPKALAQPPGVgktPAQQPGPAKPPTQQVGTPK-----------------P 420
Cdd:PRK07764  674 GGAAPAAPPPAPAPAAPAAPAGAAPA-QPAPAPAATPPAG---QADDPAAQPPQAAQGASAPspaaddpvplppepddpP 749
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 150170670  421 LAQQPGLQSPAKAPGPtktPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPS 471
Cdd:PRK07764  750 DPAGAPAQPPPPPAPA---PAAAPAAAPPPSPPSEEEEMAEDDAPSMDDED 797
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
724-1058 1.30e-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: 48.37  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   724 PEADSLSKPAPPKEPSVPSEQdKAPVADDKPKQPKMVKPTTDLVSSSSATT----KPDIPSSKVQSQAEEKTTPPLKTds 799
Cdd:pfam05109  432 PTLNTTGFAAPNTTTGLPSST-HVPTNLTAPASTGPTVSTADVTSPTPAGTtsgaSPVTPSPSPRDNGTESKAPDMTS-- 508
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   800 akpsqsfpPTGEKVSPFDSKAIPRPAsdskiISHPGPSSESkgqkqvdPVQKKEEPKKAQTKMSPKPDAKPMPKGSPTPP 879
Cdd:pfam05109  509 --------PTSAVTTPTPNATSPTPA-----VTTPTPNATS-------PTLGKTSPTSAVTTPTPNATSPTPAVTTPTPN 568
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   880 GPRPTAGQTVPTPQ-QSPKPQE----------QSRRFSLNLGSITDAPKSqpTTPQETVTGKLFGFGASIFSQASNLIST 948
Cdd:pfam05109  569 ATIPTLGKTSPTSAvTTPTPNAtsptvgetspQANTTNHTLGGTSSTPVV--TSPPKNATSAVTTGQHNITSSSTSSMSL 646
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   949 AgqpgPHSQSGPGAPMKQAPAPSQPP--TSQGPPKSTGQAPPAPAKSIPVKKETKAPAAEKLEPKAEQAPTVKRTETE-- 1024
Cdd:pfam05109  647 R----PSSISETLSPSTSDNSTSHMPllTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKpg 722
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 150170670  1025 -----KKPPPIKDSKSLTAEPQKAVLPTKLEKSPKPEST 1058
Cdd:pfam05109  723 evnvtKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANST 761
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
747-1032 1.32e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 48.31  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  747 APVADDKPKQPKMVkPTTDLVSSSSATTKPDIPSSKVQSQAEEKTTPPLKTdSAKPSQSFPPTGEKVSPFDSKAIPRPAS 826
Cdd:PRK07003  367 APGGGVPARVAGAV-PAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAA-AAAATRAEAPPAAPAPPATADRGDDAAD 444
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  827 DSKIISHPGPSSESKGQKQVDPVQkkEEPKKAQTKMSPKPDAKPMPKGSPTPPGPRPTAGQTVPTPQqsPKPQEQSRRFS 906
Cdd:PRK07003  445 GDAPVPAKANARASADSRCDERDA--QPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPD--ARAPAAASRED 520
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  907 LNLGSITDAPKSQPTTPQETVTGKLFGfGASifsQASNLISTAGQpgpHSQSGPGAPMKQAPAPSQPPTSQGPPkstgqA 986
Cdd:PRK07003  521 APAAAAPPAPEARPPTPAAAAPAARAG-GAA---AALDVLRNAGM---RVSSDRGARAAAAAKPAAAPAAAPKP-----A 588
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 150170670  987 PPAPAKSIPVkkeTKAPAAEKLEPKAEQAPTVKRTETEKKPPPIKD 1032
Cdd:PRK07003  589 APRVAVQVPT---PRARAATGDAPPNGAARAEQAAESRGAPPPWED 631
PHA03269 PHA03269
envelope glycoprotein C; Provisional
467-580 1.36e-04

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 48.19  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  467 TKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPgSTKPPPQ---QPGPAkPSPQQPGSTKPpsqQPGSAKPSAQQ 543
Cdd:PHA03269   33 TSAATQKPDPAPAPHQAASRAPDPAVAPTSAASRKPDL-AQAPTPAaseKFDPA-PAPHQAASRAP---DPAVAPQLAAA 107
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150170670  544 PSPakpsaqqstkpvsqtgsgKPLQPPTVSPSAKQPP 580
Cdd:PHA03269  108 PKP------------------DAAEAFTSAAQAHEAP 126
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
437-528 1.39e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 48.27  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  437 TKTPVQQPGPGKIPAQQAGPGKTsAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGP 516
Cdd:PRK14950  361 VPVPAPQPAKPTAAAPSPVRPTP-APSTRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVD 439
                          90
                  ....*....|..
gi 150170670  517 AKPSPQQPGSTK 528
Cdd:PRK14950  440 EKPKYTPPAPPK 451
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
470-560 1.41e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 48.27  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  470 PSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQP-GSAKPSAQQPSPAK 548
Cdd:PRK14950  362 PVPAPQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPEsAPKLTRAAIPVDEK 441
                          90
                  ....*....|..
gi 150170670  549 PSAQQSTKPVSQ 560
Cdd:PRK14950  442 PKYTPPAPPKEE 453
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
446-587 1.47e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 48.14  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  446 PGKIPAQQAGPGKtsaqqtGPTKPPSqlpGPAKPPPQQPGPAKPPPqqPGSAKPPSQQPGSTKPP----PQQPGPAK-PS 520
Cdd:PRK14959  363 PRLMPVESLRPSG------GGASAPS---GSAAEGPASGGAATIPT--PGTQGPQGTAPAAGMTPssaaPATPAPSAaPS 431
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670  521 PQQPGSTKPPSQQPGSAKPsaqQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPSQGLPKT 587
Cdd:PRK14959  432 PRVPWDDAPPAPPRSGIPP---RPAPRMPEASPVPGAPDSVASASDAPPTLGDPSDTAEHTPSGPRT 495
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
716-1072 1.50e-04

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 48.23  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  716 PSAKAKQPPEADSLSKPAPPKEPSVPSEQDKAPVADDKPKQPK--------MVKPTTDLVSSSSATTKPDIPSSKVQSQA 787
Cdd:NF033839  159 PETPQPENPEHQKPTTPAPDTKPSPQPEGKKPSVPDINQEKEKaklavatyMSKILDDIQKHHLQKEKHRQIVALIKELD 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  788 EEKTTPPLKTDSAKPSQSFPPTGEKVSPfDSKAIPRPASDSKIISHPGPsseskgqkqvdPVQKKEEPKKAQTKMSPKPD 867
Cdd:NF033839  239 ELKKQALSEIDNVNTKVEIENTVHKIFA-DMDAVVTKFKKGLTQDTPKE-----------PGNKKPSAPKPGMQPSPQPE 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  868 AKPmPKGSPTPPGPRPTAGQTVPTPQQSPKPQEQSRRFSLNLGSITDAPKSQPTTPQETVTGKLFGFGASIfsqasnlis 947
Cdd:NF033839  307 KKE-VKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEV--------- 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  948 tagQPGPHSQSGPGAPMKQAPAPSQPPTsqgPPKSTGQAPPAPAKSIPVKKETKAPAAEKLEPKAEQAPTVKRTETEKKP 1027
Cdd:NF033839  377 ---KPQPETPKPEVKPQPEKPKPEVKPQ---PEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPK 450
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 150170670 1028 PPIKdsksltAEPQKAvlptKLEKSPKPESTCPLCKTELNIGSKD 1072
Cdd:NF033839  451 PEVK------PQPETP----KPEVKPQPEKPKPEVKPQPEKPKPD 485
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
450-585 1.54e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 48.31  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  450 PAQQAGPGKTSAQqtgPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQ---------QPGSTKPPPQQPGPAKPS 520
Cdd:PRK07003  360 PAVTGGGAPGGGV---PARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAAlapkaaaaaAATRAEAPPAAPAPPATA 436
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670  521 PQ-QPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTV---SPSAKQPPSQGLP 585
Cdd:PRK07003  437 DRgDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAfepAPRAAAPSAATPA 505
dnaA PRK14086
chromosomal replication initiator protein DnaA;
281-499 1.54e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 48.28  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  281 PQTKQADIVRGESVKPSLPSPSKPPIQQP-TPGKPPAQQPGH---------EKSQPGPAKPPAQPsglTKPLAQQPGTVK 350
Cdd:PRK14086   80 RPIRIAITVDPSAGEPAPPPPHARRTSEPeLPRPGRRPYEGYggpraddrpPGLPRQDQLPTARP---AYPAYQQRPEPG 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  351 PPVQPPGTTKPPAQPLGPakPPAQQTGSekPSSEQPGPKALAQPPGvgktpaQQPGPAKPPTQQVGTPKPLAQQPGLQSp 430
Cdd:PRK14086  157 AWPRAADDYGWQQQRLGF--PPRAPYAS--PASYAPEQERDREPYD------AGRPEYDQRRRDYDHPRPDWDRPRRDR- 225
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670  431 akapgpTKTPVQQPGPGKIPaqQAGPGKTSAQQTGPTKPPSQLPGpakPPPQQPGPAKPPPQQPGSAKP 499
Cdd:PRK14086  226 ------TDRPEPPPGAGHVH--RGGPGPPERDDAPVVPIRPSAPG---PLAAQPAPAPGPGEPTARLNP 283
Androgen_recep pfam02166
Androgen receptor;
482-589 1.61e-04

Androgen receptor;


Pssm-ID: 426632 [Multi-domain]  Cd Length: 501  Bit Score: 48.00  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   482 QQPGPAKPppQQPGSAKPP----SQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKp 557
Cdd:pfam02166   30 QNPGPRHP--EAAGGAAPPgarlQHQQQQQQQVPQQPQQQESSPRQPQASVQPQQAGDDGSPPAHNRGPAGYLALEDDE- 106
                           90       100       110
                   ....*....|....*....|....*....|..
gi 150170670   558 vsqtgsgkplQPptvSPSAKQPPSQGLPKTIC 589
Cdd:pfam02166  107 ----------QP---QPSQAQPAAECCPENGC 125
PDZ_Radil-like cd06690
PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; ...
4510-4581 1.72e-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: 43.43  E-value: 1.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150170670 4510 GNGLGIRIVGGKEIPGHSGeiGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIIsQQSGE 4581
Cdd:cd06690    12 PKGLGLGLIDGLHTPLRSP--GIYIRTLVPDSPAARDGRLRLGDRILAVNGTSLVGADYQSAMDLI-RTSGD 80
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
442-522 2.01e-04

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 47.96  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  442 QQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSP 521
Cdd:PRK12270   36 YGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVED 115

                  .
gi 150170670  522 Q 522
Cdd:PRK12270  116 E 116
PHA03160 PHA03160
hypothetical protein; Provisional
326-405 2.08e-04

hypothetical protein; Provisional


Pssm-ID: 165431  Cd Length: 499  Bit Score: 47.39  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  326 PGPAKPPAQPSGLTKPLAQQPGTVK-PPVQPPGTTKPPAQPLGPAKPPAQQTgSEKPSSEQPGPKAlAQPPGVGKTPAQQ 404
Cdd:PHA03160  406 PKNDHHLLPPLACSQQLPMQPLHVQqAPMQAPHVAPPPMQPPHVQQPRVLPS-TDGASNEAPKPSA-QEPVHIDASFAQD 483

                  .
gi 150170670  405 P 405
Cdd:PHA03160  484 P 484
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
445-529 2.18e-04

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 47.96  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  445 GPGKIPAQQAGPGKTSAQQTGPTKPPsqlPGPAKPPPQQPGPAKPPPQQ-PGSAKPPSQQPGSTKPPPQQPGPAKPSPQQ 523
Cdd:PRK12270   37 GPGSTAAPTAAAAAAAAAASAPAAAP---AAKAPAAPAPAPPAAAAPAApPKPAAAAAAAAAPAAPPAAAAAAAPAAAAV 113

                  ....*.
gi 150170670  524 PGSTKP 529
Cdd:PRK12270  114 EDEVTP 119
C2_PSD cd04039
C2 domain present in Phosphatidylserine decarboxylase (PSD); PSD is involved in the ...
4707-4812 2.19e-04

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: 43.40  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4707 GNLIIHILQARNLVPRDN---NGYS-DPFV------KVYllpgrgqvmvvqnasaeykrRTKHVQKSLNPEWNQTVIYKS 4776
Cdd:cd04039     1 GVVFMEIKSITDLPPLKNmtrTGFDmDPFViisfgrRVF--------------------RTSWRRHTLNPVFNERLAFEV 60
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 150170670 4777 ISMEqlKKKTLEVTVWDYDRFSSNDFLGEVLIDLSS 4812
Cdd:cd04039    61 YPHE--KNFDIQFKVLDKDKFSFNDYVATGSLSVQE 94
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
4496-4579 2.27e-04

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: 42.76  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4496 RIKITRDSKDHTVsgngLGIRIVGGKEIPghsgeIGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTSKTYEEVQSII 4575
Cdd:cd10834     2 RIVHLYTTSDDYC----LGFNIRGGSEYG-----LGIYVSKVDPGGLAEQNG-IKVGDQILAVNGVSFEDITHSKAVEVL 71

                  ....
gi 150170670 4576 SQQS 4579
Cdd:cd10834    72 KSQT 75
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
915-1061 2.33e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 47.55  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  915 APKSQPTTPQETVTgklfgfgASIFSQASNLISTAGQPGPHSQSGP---GAPMKQAPAPSQPPTSQ----GPPKSTGQAP 987
Cdd:PRK07994  363 APLPEPEVPPQSAA-------PAASAQATAAPTAAVAPPQAPAVPPppaSAPQQAPAVPLPETTSQllaaRQQLQRAQGA 435
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670  988 PAPAKSIPVKKETKAPAAEKLEPKAEQAPTVKRTETEKK---PPPIKDSKSLTAEPQKAVLPTKLEKSPKPESTCPL 1061
Cdd:PRK07994  436 TKAKKSEPAAASRARPVNSALERLASVRPAPSALEKAPAkkeAYRWKATNPVEVKKEPVATPKALKKALEHEKTPEL 512
FimV COG3170
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];
309-550 2.44e-04

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


Pssm-ID: 442403 [Multi-domain]  Cd Length: 508  Bit Score: 47.48  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  309 PTPGKPPAQQPGHEkSQPGPAKPPAQPSGLTKPLAQQPGTVKP---PVQPPGT-TKPPAQPLGPAKPPAQQTGSEK---- 380
Cdd:COG3170   106 PPAYAAAAAAPAAA-PAPAPAAPAAAAAAADQPAAEAAPAASGeyyPVRPGDTlWSIAARPVRPSSGVSLDQMMVAlyra 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  381 -PSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKT 459
Cdd:COG3170   185 nPDAFIDGNINRLKAGAVLRVPAAEEVAALSPAEARQEVQAQSADWAAYRARLAAAVEPAPAAAAPAAPPAAAAAAGPVP 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  460 SAQQTG--PTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSA 537
Cdd:COG3170   265 AAAEDTlsPEVTAAAAAEEADALPEAAAELAERLAALEAQLAELQRLLALKNPAPAAAVSAPAAAAAAATVEAAAPAAAA 344
                         250
                  ....*....|...
gi 150170670  538 KPSAQQPSPAKPS 550
Cdd:COG3170   345 QPAAAAPAPALDN 357
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 ...
4512-4587 2.45e-04

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


Pssm-ID: 467244 [Multi-domain]  Cd Length: 86  Bit Score: 42.60  E-value: 2.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670 4512 GLGIRIVGGKEIPghSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSII-SQQSGEAEICVR 4587
Cdd:cd06763    12 GLGFSLEGGKGSP--LGDRPLTIKRIFKGGAAEQSGVLQVGDEILQINGTSLQGLTRFEAWNIIkSLPEGPVTLLIR 86
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
1211-1554 2.51e-04

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 47.73  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1211 KKPLPEE-KKL----IPEEEKIRSEEKKPLLEEKKPTPEDKKLLPEAKTSAPEEQKHDLL-KSQVQIAEEKLEgrvapKT 1284
Cdd:PTZ00108 1033 KKDLVKElKKLgyvrFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSYDYLLsMPIWSLTKEKVE-----KL 1107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1285 VQEGKQPQTKMEGLPSGTPQSLPKED-DKTTKTIKEQPQPpctakpDQVEPGKEKTEKEDDKSDTSSSQQPKSPQGLSDT 1363
Cdd:PTZ00108 1108 NAELEKKEKELEKLKNTTPKDMWLEDlDKFEEALEEQEEV------EEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKK 1181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1364 G--------YSSDGISSSLGEIPSLIPTDEKDILKGLKKDSFSQESSPSSPSDLAKLESTVLSILEAQASTLADEKSEKK 1435
Cdd:PTZ00108 1182 KkssadkskKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFS 1261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1436 TQPHEVSPEQPKDQEKTQSLSE-------TLEITISEEEIKESQEERKDTFKKDSQQDIPSSKDHKEKSEFVDDITTRRE 1508
Cdd:PTZ00108 1262 SDDLSKEGKPKNAPKRVSAVQYsppppskRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRV 1341
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 150170670 1509 PYdsveesseSENSPVPQRKRRTSVGSSSSDE--------YKQEDSQGSGEEED 1554
Cdd:PTZ00108 1342 KQ--------ASASQSSRLLRRPRKKKSDSSSeddddsevDDSEDEDDEDDEDD 1387
PDZ1_Dlg1-2-4-like cd06723
PDZ domain 1 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
4510-4549 2.52e-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: 42.69  E-value: 2.52e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 150170670 4510 GNGLGIRIVGGKEIPGHSGEIGAYIAKILPGGSAEQTGKL 4549
Cdd:cd06723    10 NSGLGFSIAGGTDNPHIGDDPSIYITKIIPGGAAAADGRL 49
motB PRK05996
MotB family protein;
380-560 2.56e-04

MotB family protein;


Pssm-ID: 235665 [Multi-domain]  Cd Length: 423  Bit Score: 47.00  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  380 KPSSEQPGPKALaQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQqpGLQSPAKAPGPTK--------TP-------VQQP 444
Cdd:PRK05996   72 KLTDRKPSEKGL-KDPVDGAEGEQKPGKSKFEEDQRVEGSSAVT--GDDTTRTSGDQTNyseadlfrNPyavlaeiAQEV 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  445 GPgkiPAQQAGPGKTSAQQTGPT---------KPP-------SQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTK 508
Cdd:PRK05996  149 GQ---QANVSAKGDGGAAQSGPAtgadggeayRDPfdpdfwsKQVEVTTAGDLLPPGQAREQAQGAKSATAAPATVPQAA 225
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 150170670  509 PPPqQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQ 560
Cdd:PRK05996  226 PLP-QAQPKKAATEEELIADAKKAATGEPAANAAKAAKPEPMPDDQQKEAEQ 276
Androgen_recep pfam02166
Androgen receptor;
379-520 2.62e-04

Androgen receptor;


Pssm-ID: 426632 [Multi-domain]  Cd Length: 501  Bit Score: 47.23  E-value: 2.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   379 EKPSSEQPGPKALAQPPGVGKTPAQQpgpakpptQQVGTPKPLAQQpglQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGK 458
Cdd:pfam02166   30 QNPGPRHPEAAGGAAPPGARLQHQQQ--------QQQQVPQQPQQQ---ESSPRQPQASVQPQQAGDDGSPPAHNRGPAG 98
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150170670   459 TSAQQTGPTKPPSQLPGPAKPPPQQpgPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPS 520
Cdd:pfam02166   99 YLALEDDEQPQPSQAQPAAECCPEN--GCVPEPGAAAAAGKGLPQQAVAPAAPDDDDSAAPS 158
PRK14948 PRK14948
DNA polymerase III subunit gamma/tau;
421-588 2.65e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237862 [Multi-domain]  Cd Length: 620  Bit Score: 47.26  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  421 LAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPG---KTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQP--- 494
Cdd:PRK14948  360 LPSAFISEIANASAPANPTPAPNPSPPPAPIQPSAPKtkqAATTPSPPPAKASPPIPVPAEPTEPSPTPPANAANAPpsl 439
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  495 ----------GSAKPPS--------------------------------------------------------QQPGSTK 508
Cdd:PRK14948  440 nleelwqqilAKLELPStrmllsqqaelvsldsnraviavspnwlgmvqsrkplleqafakvlgrsiklnlesQSGSASN 519
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  509 PPPQQPGPAKPSPQQPgsTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPSQGLPKTI 588
Cdd:PRK14948  520 TAKTPPPPQKSPPPPA--PTPPLPQPTATAPPPTPPPPPPTATQASSNAPAQIPADSSPPPPIPEEPTPSPTKDSSPEEI 597
motB PRK12799
flagellar motor protein MotB; Reviewed
447-561 2.72e-04

flagellar motor protein MotB; Reviewed


Pssm-ID: 183756 [Multi-domain]  Cd Length: 421  Bit Score: 47.02  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  447 GKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQ---PGPAKPSPQQ 523
Cdd:PRK12799  297 GTVPVAAVTPSSAVTQSSAITPSSAAIPSPAVIPSSVTTQSATTTQASAVALSSAGVLPSDVTLPGTvalPAAEPVNMQP 376
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 150170670  524 PGSTKPPSQQP--GSAKPSAQQPSPAKPSAQQSTKPVSQT 561
Cdd:PRK12799  377 QPMSTTETQQSstGNITSTANGPTTSLPAAPASNIPVSPT 416
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
4494-4582 2.91e-04

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: 42.61  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4494 HARIKITRDskdhtvsGNGLGIRIVGGKeipgHSGEIGAY---IAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEE 4570
Cdd:cd06681     2 TVEVTLEKE-------GNSFGFVIRGGA----HEDRNKSRpltVTHVRPGGPADREGTIKPGDRLLSVDGISLHGATHAE 70
                          90
                  ....*....|..
gi 150170670 4571 VQSIISQQSGEA 4582
Cdd:cd06681    71 AMSILKQCGQEA 82
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
4509-4579 2.93e-04

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: 42.63  E-value: 2.93e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150170670 4509 SGNGLGIRIVGGKEipgHSgeIGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTSKTYEEVQSIISQQS 4579
Cdd:cd06737    11 GPESLGFSVRGGLE---HG--CGLFVSHVSPGSQADNKG-LRVGDEIVRINGYSISQCTHEEVINLIKTKK 75
PRK12727 PRK12727
flagellar biosynthesis protein FlhF;
314-512 3.03e-04

flagellar biosynthesis protein FlhF;


Pssm-ID: 237182 [Multi-domain]  Cd Length: 559  Bit Score: 46.91  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  314 PPAQQPgheksqpgPAKPPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPL-GPAKPPAQQTGSEK-PSSEQPGPKAL 391
Cdd:PRK12727   70 APAPQA--------PTKPAAPVHAPLKLSANANMSQRQRVASAAEDMIAAMALrQPVSVPRQAPAAAPvRAASIPSPAAQ 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  392 AQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPgLQSPAKAPGPTKTPVQQPG-PGKIPAQQAGPGKTSAQQTGPTKPP 470
Cdd:PRK12727  142 ALAHAAAVRTAPRQEHALSAVPEQLFADFLTTAP-VPRAPVQAPVVAAPAPVPAiAAALAAHAAYAQDDDEQLDDDGFDL 220
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 150170670  471 SQLPGPAKPPPQQPGPAKPPPQQPGSAkppsqQPGSTKPPPQ 512
Cdd:PRK12727  221 DDALPQILPPAALPPIVVAPAAPAALA-----AVAAAAPAPQ 257
PDZ3_FL-whirlin-like cd06742
PDZ domain 3 of the full-length isoform of whirlin, PDZ domain 1 of the short isoform of ...
4513-4577 3.25e-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: 42.73  E-value: 3.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150170670 4513 LGIRIVGGkeipGHSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQ 4577
Cdd:cd06742    13 LGIAIEGG----ANTKQPLPRVINIQRGGSAHNCGGLKVGHVILEVNGTSLRGLEHREAARLIAE 73
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
650-898 4.01e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 46.84  E-value: 4.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  650 LAPVPSSPQPKLKTAPVTTTSAVSKSSPQPQQTSPKKDAAPKQDLSKAPEPKKPPPL-----VKQPTLHGSPSAKAKQPP 724
Cdd:PLN03209  320 LAKIPSQRVPPKESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAyedlkPPTSPIPTPPSSSPASSK 399
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  725 EADSLSKPAPPKEPSVPSEQDKAPVADDKPKQPKMVKPTtdlvssSSATTKPDI-PSSKVQSQAEEKTTPPLKTDSAKPS 803
Cdd:PLN03209  400 SVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPL------SPYARYEDLkPPTSPSPTAPTGVSPSVSSTSSVPA 473
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  804 --QSFPPTGEKVSPFDSKAIPRPASDSKIISHPGPSSESKGQKQVDPVQKKEEPkKAQTKMSPKPDAKPMPKGSPTPPGP 881
Cdd:PLN03209  474 vpDTAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTN-EVVKVGNSAPPTALADEQHHAQPKP 552
                         250       260
                  ....*....|....*....|
gi 150170670  882 RPTAGQTV---PTPQQSPKP 898
Cdd:PLN03209  553 RPLSPYTMyedLKPPTSPTP 572
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
362-521 4.05e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 46.78  E-value: 4.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  362 PAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTqqvgTPKPLAQQPGLQSpakAPGPTKTPV 441
Cdd:PRK07994  368 PEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPET----TSQLLAARQQLQR---AQGATKAKK 440
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  442 QQPgpgkiPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPgSAKPPSQQPGSTKPPPQQPGPAKPSP 521
Cdd:PRK07994  441 SEP-----AAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVE-VKKEPVATPKALKKALEHEKTPELAA 514
PRK12373 PRK12373
NADH-quinone oxidoreductase subunit E;
447-578 4.13e-04

NADH-quinone oxidoreductase subunit E;


Pssm-ID: 237082 [Multi-domain]  Cd Length: 400  Bit Score: 46.33  E-value: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  447 GKIPAQQAGP--GKTSAQqtgPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQP 524
Cdd:PRK12373  172 GKGPVVKPGPqiGRYASE---PAGGLTSLTEEAGKARYNASKALAEDIGDTVKRIDGTEVPLLAPWQGDAAPVPPSEAAR 248
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 150170670  525 GSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQ 578
Cdd:PRK12373  249 PKSADAETNAALKTPATAPKAAAKNAKAPEAQPVSGTAAAEPAPKEAAKAAAAA 302
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
426-528 4.21e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 46.60  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  426 GLQSPAKAPGP-TKTPVQQPGPGKIPAQQAGP--GKTSAQQTGPTKPPSQLPGPAKP-------PPQQPGPAKPPPQQPG 495
Cdd:PRK14959  379 SAPSGSAAEGPaSGGAATIPTPGTQGPQGTAPaaGMTPSSAAPATPAPSAAPSPRVPwddappaPPRSGIPPRPAPRMPE 458
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 150170670  496 SAK---PPSQQPGSTKPPPQQPGPAKPSPQQPGSTK 528
Cdd:PRK14959  459 ASPvpgAPDSVASASDAPPTLGDPSDTAEHTPSGPR 494
PHA03269 PHA03269
envelope glycoprotein C; Provisional
437-568 4.32e-04

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 46.65  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  437 TKTPVQQPGPGKIPAQQAGPGKTSAqqTGPTKPPSQLPGPAKPPP----QQPGPAKPPPQQPGSAKPPSQQPGSTKPPpq 512
Cdd:PHA03269   33 TSAATQKPDPAPAPHQAASRAPDPA--VAPTSAASRKPDLAQAPTpaasEKFDPAPAPHQAASRAPDPAVAPQLAAAP-- 108
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670  513 QPGPAKPSPQQPGSTKPPSQQPGSAkpSAQQPSPAKpSAQQSTKPVSQTGSGKPLQ 568
Cdd:PHA03269  109 KPDAAEAFTSAAQAHEAPADAGTSA--ASKKPDPAA-HTQHSPPPFAYTRSMEHIA 161
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
366-570 4.46e-04

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


Pssm-ID: 464609 [Multi-domain]  Cd Length: 325  Bit Score: 45.96  E-value: 4.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   366 LGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQP-GPAKPPTQQVGTPKPLAQQPGLQSPAKAPgptktpVQQP 444
Cdd:pfam15279   91 ESVSPGPSSSASPSSSPTSSNSSKPLISVASSSKLLAPKPhEPPSLPPPPLPPKKGRRHRPGLHPPLGRP------PGSP 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   445 GPGKIPAQQAGPGKTsaQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPP-------------P 511
Cdd:pfam15279  165 PMSMTPRGLLGKPQQ--HPPPSPLPAFMEPSSMPPPFLRPPPSIPQPNSPLSNPMLPGIGPPPKPPrnlgppsnpmhrpP 242
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670   512 QQPGPAKPSPQQPGSTkPPSQQPGsakPSAQQPSPAKPSAQQSTKPVSQ-----TGSGKPLQPP 570
Cdd:pfam15279  243 FSPHHPPPPPTPPGPP-PGLPPPP---PRGFTPPFGPPFPPVNMMPNPPemnfgLPSLAPLVPP 302
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
316-500 4.47e-04

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 44.26  E-value: 4.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   316 AQQPGHEKSQPGpakppaQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPP 395
Cdd:pfam15240   16 AQSSSEDVSQED------SPSLISEEEGQSQQGGQGPQGPPPGGFPPQPPASDDPPGPPPPGGPQQPPPQGGKQKPQGPP 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   396 gvgktpaQQPGPAKPPTQQVGTPKPLAQQPglQSPAKAPGPTKTPVQQPGPGKIPAQQAGPgktsaqqtgptkPPsqlpg 475
Cdd:pfam15240   90 -------PQGGPRPPPGKPQGPPPQGGNQQ--QGPPPPGKPQGPPPQGGGPPPQGGNQQGP------------PP----- 143
                          170       180
                   ....*....|....*....|....*.
gi 150170670   476 pakPPPQQP-GPAKPPPQQPGSAKPP 500
Cdd:pfam15240  144 ---PPPGNPqGPPQRPPQPGNPQGPP 166
PHA03369 PHA03369
capsid maturational protease; Provisional
460-776 4.55e-04

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 46.53  E-value: 4.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  460 SAQQTGPTKPPSQLPGPAKPPPQQPgPAKPPPQQPGSAKPPSQqpgSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKP 539
Cdd:PHA03369  350 TASLTAPSRVLAAAAKVAVIAAPQT-HTGPADRQRPQRPDGIP---YSVPARSPMTAYPPVPQFCGDPGLVSPYNPQSPG 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  540 SAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTV-SPSAKQppsQGLPKTICPLCNTTELLLHVPEKANFNTCTECQTTVC 618
Cdd:PHA03369  426 TSYGPEPVGPVPPQPTNPYVMPISMANMVYPGHpQEHGHE---RKRKRGGELKEELIETLKLVKKLKEEQESLAKELEAT 502
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  619 SLCGFNPNPHLTEVKewlclNCQMKRAlGGDLAPVPSSPQ--PKLKTAPVTTTSAVSKSSPQPQQTSPKKDAAPKQDL-S 695
Cdd:PHA03369  503 AHKSEIKKIAESEFK-----NAGAKTA-AANIEPNCSADAaaPATKRARPETKTELEAVVRFPYQIRNMESPAFVHSFtS 576
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  696 KAPEPKKPPPLVKQPTLHG---SPSAKAKQPPEADSLSKPAPPKEPSVPSEQDKaPVADDKPKQPKMVKPTTDlvsSSSA 772
Cdd:PHA03369  577 TTLAAAAGQGSDTAEALAGaieTLLTQASAQPAGLSLPAPAVPVNASTPASTPP-PLAPQEPPQPGTSAPSLE---TSLP 652

                  ....
gi 150170670  773 TTKP 776
Cdd:PHA03369  653 QQKP 656
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
309-390 4.56e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 46.34  E-value: 4.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  309 PTPGKPPAQQPGHEKSQPGPAKPPAQPSGLTKPLAQ-QPGTVKPPVQPP---GTTKPPAQPLGPAKPPAQQTGSEKPSSE 384
Cdd:PRK14950  366 PQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEpVRETATPPPVPPrpvAPPVPHTPESAPKLTRAAIPVDEKPKYT 445

                  ....*.
gi 150170670  385 QPGPKA 390
Cdd:PRK14950  446 PPAPPK 451
PRK11633 PRK11633
cell division protein DedD; Provisional
461-547 4.74e-04

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 44.99  E-value: 4.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  461 AQQTGPTKPP-----SQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPgstKPPPQQPGPAKPSPQQPgSTKPPSQQPG 535
Cdd:PRK11633   59 ATQALPTQPPegaaeAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPP---KPKPVEKPKPKPKPQQK-VEAPPAPKPE 134
                          90
                  ....*....|..
gi 150170670  536 SAKPSAQQPSPA 547
Cdd:PRK11633  135 PKPVVEEKAAPT 146
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
508-591 4.82e-04

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 46.81  E-value: 4.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  508 KPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPSQGLPKT 587
Cdd:PRK12270   37 GPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDE 116

                  ....
gi 150170670  588 ICPL 591
Cdd:PRK12270  117 VTPL 120
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
240-500 4.97e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.70  E-value: 4.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  240 SSQQPEKIKSQPPGTGKPIQGPTQTPQTDHAK-----LPLQRDASRPQTKQADIVRGESVKPSLPSPSKPPIQQPTPGKP 314
Cdd:PHA03307  178 SPEETARAPSSPPAEPPPSTPPAAASPRPPRRsspisASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPL 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  315 PAQQPGHEKSQPGPAKPPAQPSGLtkplaqqPGTVKPPVQPPGTTkPPAQPLGPAKPPA-------------QQTGSEKP 381
Cdd:PHA03307  258 PRPAPITLPTRIWEASGWNGPSSR-------PGPASSSSSPRERS-PSPSPSSPGSGPApssprasssssssRESSSSST 329
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  382 SSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSA 461
Cdd:PHA03307  330 SSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPA 409
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 150170670  462 QQTGPTKPPSQLPGPAKPPPQQPGPAKPPPqQPGSAKPP 500
Cdd:PHA03307  410 GRPRPSPLDAGAASGAFYARYPLLTPSGEP-WPGSPPPP 447
Totivirus_coat pfam05518
Totivirus coat protein;
365-523 4.97e-04

Totivirus coat protein;


Pssm-ID: 428505  Cd Length: 727  Bit Score: 46.68  E-value: 4.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   365 PLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGK-TPAQQPGPAKPPTQQVGTPKPlaqqpGLQSPAKAPGPTktpvqQ 443
Cdd:pfam05518  589 PTGLASGASNAEDPEVRRARTRGARALAQARTFGRaTVGEMIISGFPPVFKTALPRP-----DYNRGGEAGGPG-----V 658
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   444 PGPGkipaQQAGPGKTsaqqtgpTKPPSQLPG-PAKPPPQ-QPGPAKPPPQQPGSAKPPSqqPGSTKPPPQQPGPAKPSP 521
Cdd:pfam05518  659 PGPV----PVGMEAHT-------VRPSRVARGdPVRPTAHhAALRAPQAPRGPSSLIPSP--TAPPEPEPPGAEQADRAE 725

                   ..
gi 150170670   522 QQ 523
Cdd:pfam05518  726 NQ 727
PRK11901 PRK11901
hypothetical protein; Reviewed
455-582 5.14e-04

hypothetical protein; Reviewed


Pssm-ID: 237015 [Multi-domain]  Cd Length: 327  Bit Score: 45.83  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  455 GPGKTSAQQTGPTKPP---------SQLPGPAKPPPQQPGPAKPPPQQPGSAkpPSQQPGSTKPPPQQPGPAKPSPQQPg 525
Cdd:PRK11901   60 SPTEHESQQSSNNAGAeknidlsgsSSLSSGNQSSPSAANNTSDGHDASGVK--NTAPPQDISAPPISPTPTQAAPPQT- 136
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150170670  526 stkPPSQQ----PGSAkPSA--QQPSPAKPSAQQSTKPvsqtGSGKPLQPPTVSPSAKQPPSQ 582
Cdd:PRK11901  137 ---PNGQQrielPGNI-SDAlsQQQGQVNAASQNAQGN----TSTLPTAPATVAPSKGAKVPA 191
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
468-556 5.24e-04

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 46.81  E-value: 5.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  468 KPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPgstkPPPQQPGPAKPSPQQPGSTKPPsqQPGSAKPSAQQPSPA 547
Cdd:PRK12270   37 GPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPA----PPAAAAPAAPPKPAAAAAAAAA--PAAPPAAAAAAAPAA 110

                  ....*....
gi 150170670  548 KPSAQQSTK 556
Cdd:PRK12270  111 AAVEDEVTP 119
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
308-453 5.40e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 46.40  E-value: 5.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  308 QPTPGKPPAQQPGHEKSQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPG 387
Cdd:PRK07994  365 LPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKSEPA 444
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670  388 PKALAQPpgvgKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQ 453
Cdd:PRK07994  445 AASRARP----VNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKALEH 506
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
660-1055 5.42e-04

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 46.30  E-value: 5.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  660 KLKTAPVTTTSAVSKSSPQPQQTSPKKDAAPKQDLSKapepkkppplvkqptlhgSPSAKAKQPPEADSLSKPAPPKePS 739
Cdd:NF033839  145 KDSSSSSSSGSSTKPETPQPENPEHQKPTTPAPDTKP------------------SPQPEGKKPSVPDINQEKEKAK-LA 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  740 VPSEQDKapVADDKPKQPKMVKPTTDLVSsssatTKPDIPSSKVQSQAEEKTTPPLKTDSAKPSQSFPPTGEKVSPFDSK 819
Cdd:NF033839  206 VATYMSK--ILDDIQKHHLQKEKHRQIVA-----LIKELDELKKQALSEIDNVNTKVEIENTVHKIFADMDAVVTKFKKG 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  820 AIPRPAS--DSKIISHPGPSSESKGQKQVDPVQKKEEPKKAQTKMSPKpdaKPMPKGSPTPPGPRPTAGQTVPTPQQSPK 897
Cdd:NF033839  279 LTQDTPKepGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLE---KPKPEVKPQPEKPKPEVKPQLETPKPEVK 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  898 PQEQSRRFSLNLGSITDAP--KSQPTTPQETVTGKLFGFGASIfsqasnlistagQPGPHSQSGPGAPMKQAPAPSQPPT 975
Cdd:NF033839  356 PQPEKPKPEVKPQPEKPKPevKPQPETPKPEVKPQPEKPKPEV------------KPQPEKPKPEVKPQPEKPKPEVKPQ 423
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  976 SQGPPKSTGQAPPAPAKSIPVKKETKAPA--AEKLEPKAEQAPTVKRTETEKKPPPIK---DSKSLTAEPQKAVLPTKLE 1050
Cdd:NF033839  424 PEKPKPEVKPQPEKPKPEVKPQPEKPKPEvkPQPETPKPEVKPQPEKPKPEVKPQPEKpkpDNSKPQADDKKPSTPNNLS 503

                  ....*
gi 150170670 1051 KSPKP 1055
Cdd:NF033839  504 KDKQP 508
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
651-1047 5.42e-04

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 46.30  E-value: 5.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  651 APVPSSPQPKLKTAPVTTTsavsKSSPQPQQTSPKK-DAAPKQDLSKAPEPKKPPPLVKQPTLHGSPSAKAKQP----PE 725
Cdd:NF033839  161 TPQPENPEHQKPTTPAPDT----KPSPQPEGKKPSVpDINQEKEKAKLAVATYMSKILDDIQKHHLQKEKHRQIvaliKE 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  726 ADSLSKPAPPKEPSV-----PSEQDKAPVADDKPKQPKMVKPTTDLVSSSSATTKPDIPSSKVQSQAEEKTtPPLKTDSA 800
Cdd:NF033839  237 LDELKKQALSEIDNVntkveIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEK-KEVKPEPE 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  801 KPSQSFPPTGEKVSPfdsKAIPRPAsdskiishpGPSSESKGQKQVDPVQKKEEPKKAQTKMSPKPDaKPMPKGSPTPPG 880
Cdd:NF033839  316 TPKPEVKPQLEKPKP---EVKPQPE---------KPKPEVKPQLETPKPEVKPQPEKPKPEVKPQPE-KPKPEVKPQPET 382
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  881 PRPTAGQTVPTPQQSPKPQEQSRRFSLNLGSITDAP--KSQPTTPQETVtgklfgfgasifsqasnlistagQPGPHSQS 958
Cdd:NF033839  383 PKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPevKPQPEKPKPEV-----------------------KPQPEKPK 439
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  959 GPGAPMKQAPAPSQPPTSQGPPKSTGQAPPAPAKSIPVKKETKAPAAEKLEPKAEQAPTVKRTETEKKPPPIKDSKSLTA 1038
Cdd:NF033839  440 PEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPSTPNNLSKDKQPSNQASTNEKAT 519

                  ....*....
gi 150170670 1039 EPQKAVLPT 1047
Cdd:NF033839  520 NKPKKSLPS 528
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
450-519 5.50e-04

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 45.69  E-value: 5.50e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150170670   450 PAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGP-AKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKP 519
Cdd:pfam07174   43 PAPPPPSTATAPPAPPPPPPAPAAPAPPPPPAAPNAPnAPPPPADPNAPPPPPADPNAPPPPAVDPNAPEP 113
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
481-586 5.54e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 46.40  E-value: 5.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  481 PQQPGPAkpPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQqpgsakPSAQQPSPAKPSAQQSTKPVSQ 560
Cdd:PRK07994  361 PAAPLPE--PEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQA------PAVPLPETTSQLLAARQQLQRA 432
                          90       100
                  ....*....|....*....|....*.
gi 150170670  561 TGSGKPLQPPTVSPSAKQPPSQGLPK 586
Cdd:PRK07994  433 QGATKAKKSEPAAASRARPVNSALER 458
C2C_Tricalbin-like cd04045
C2 domain third repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
4707-4811 5.62e-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: 5.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4707 GNLIIHILQARNLVPRDNNGYSDPFVKVYLlpgRGQVmvvqnasaeyKRRTKHVQKSLNPEWNQtVIYKSIsMEQLKKKT 4786
Cdd:cd04045     1 GVLRLHIRKANDLKNLEGVGKIDPYVRVLV---NGIV----------KGRTVTISNTLNPVWDE-VLYVPV-TSPNQKIT 65
                          90       100
                  ....*....|....*....|....*
gi 150170670 4787 LEvtVWDYDRFSSNDFLGEVLIDLS 4811
Cdd:cd04045    66 LE--VMDYEKVGKDRSLGSVEINVS 88
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
397-488 5.74e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 46.34  E-value: 5.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  397 VGKTPAQQPGPAKPPTQQVGTPKPLAQQPgLQSPAKAPGPTKTPVQQPG-PGKIPAQQAGPGKTSAQQTGPTKPPSQLPG 475
Cdd:PRK14950  360 LVPVPAPQPAKPTAAAPSPVRPTPAPSTR-PKAAAAANIPPKEPVRETAtPPPVPPRPVAPPVPHTPESAPKLTRAAIPV 438
                          90
                  ....*....|...
gi 150170670  476 PAKPPPQQPGPAK 488
Cdd:PRK14950  439 DEKPKYTPPAPPK 451
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
863-1061 5.84e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.41  E-value: 5.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  863 SPKPDAKPMPKGSPTPPGPRPTAGQTVPTPQQSPKPQEqsrrfslnlgsitdAPKSQPTTPQETVTGKlfgfgASIFSQA 942
Cdd:PRK12323  372 AGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAA--------------PAAAAAARAVAAAPAR-----RSPAPEA 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  943 SNLISTAGQPGPHSQSGPGAPMKQAPAPSQPPTSQGPPKSTGQAPPAPAKSIPVKkeTKAPAAEKLEPKAEQAPTVKRTE 1022
Cdd:PRK12323  433 LAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAA--APAPADDDPPPWEELPPEFASPA 510
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 150170670 1023 -TEKKPPPIKDSKSLTAEPQKAVLPTKLEKSPKPESTCPL 1061
Cdd:PRK12323  511 pAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPA 550
Med25_SD1 pfam11235
Mediator complex subunit 25 synapsin 1; The overall function of the full-length Med25 is ...
418-548 5.91e-04

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


Pssm-ID: 463244 [Multi-domain]  Cd Length: 157  Bit Score: 43.62  E-value: 5.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   418 PKPL-AQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKP----PSQLPG------PAKPPPQ-QPG 485
Cdd:pfam11235    9 PGPLqSKQPVPLPPAAPSGATLSAAPQQPLPPVPPQYQVPGNLSAAQVAAQNAveaaKNQKAGlgprfsPITPLQQaAPG 88
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   486 PAKPPPQQPGSAKPPSQqPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGS-------AKPSAQQPSPAK 548
Cdd:pfam11235   89 VGPPFSQAPAPQLPPGP-PGAPKPVPPASQPSLVSTVAPGSGLAPTAQPGApsmagtvAPGGVSGPSPAQ 157
C2B_Ferlin cd04011
C2 domain second repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
4711-4812 6.10e-04

C2 domain second 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 second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 175978 [Multi-domain]  Cd Length: 111  Bit Score: 42.56  E-value: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4711 IHILQARNLVprdnNGYSDPFVKVYLLpgrGQvmvvqnasaeyKRRTKhVQKSLN-PEWNQTVIYK-SISMEQLKKKTLE 4788
Cdd:cd04011     8 VRVIEARQLV----GGNIDPVVKVEVG---GQ-----------KKYTS-VKKGTNcPFYNEYFFFNfHESPDELFDKIIK 68
                          90       100
                  ....*....|....*....|....
gi 150170670 4789 VTVWDYDRFSSNDFLGEVLIDLSS 4812
Cdd:cd04011    69 ISVYDSRSLRSDTLIGSFKLDVGT 92
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
444-524 6.20e-04

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 46.42  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  444 PGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPgPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQ 523
Cdd:PRK12270   40 STAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAP-AAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVT 118

                  .
gi 150170670  524 P 524
Cdd:PRK12270  119 P 119
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
342-468 6.32e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 45.92  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  342 LAQQPGTVKPPVQP-----PGTTKPPAQPLGPAKP-PAQQTGSEKPSSEQPGPKALAQPPGVGKT-PAQQPGPAKPPTQQ 414
Cdd:PRK14971  362 LTQKGDDASGGRGPkqhikPVFTQPAAAPQPSAAAaASPSPSQSSAAAQPSAPQSATQPAGTPPTvSVDPPAAVPVNPPS 441
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670  415 VGTPK-PLAQQPGLQSPAKAPGPTKTP-VQQPgpgKIPAQQAGPGKTSAQQTGPTK 468
Cdd:PRK14971  442 TAPQAvRPAQFKEEKKIPVSKVSSLGPsTLRP---IQEKAEQATGNIKEAPTGTQK 494
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
4514-4581 6.43e-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: 6.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4514 GIRIVGGKE--IPghsgeigAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGE 4581
Cdd:cd06753    11 GFRLQGGKDfnQP-------LTISRVTPGGKAAQAN-LRPGDVILAINGESTEGMTHLEAQNKIKAATGS 72
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
469-585 6.48e-04

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 43.32  E-value: 6.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   469 PPSQLPGPAKPPPQQPG---PAKPPPQQPGSAKPPSQQPGST--KPPPQQPGPA--KPSPQQPGSTKPPSQQPGSAKPSA 541
Cdd:pfam06346    2 PPPPLPGDSSTIPLPPGaciPTPPPLPGGGGPPPPPPLPGSAaiPPPPPLPGGTsiPPPPPLPGAASIPPPPPLPGSTGI 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 150170670   542 QQPSPAKPSAQQSTKPVSQTGS-GKPLQPPTVSPSAKQPPSQGLP 585
Cdd:pfam06346   82 PPPPPLPGGAGIPPPPPPLPGGaGVPPPPPPLPGGPGIPPPPPFP 126
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
314-461 6.48e-04

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 43.32  E-value: 6.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   314 PPAQQPGHEKSQPGPAKPPAQPsglTKPLAQQPGTVKPPVQPPGTTKPPAQPLG-----PAKPPAQQTGSEKPSSEQPGP 388
Cdd:pfam06346    2 PPPPLPGDSSTIPLPPGACIPT---PPPLPGGGGPPPPPPLPGSAAIPPPPPLPggtsiPPPPPLPGAASIPPPPPLPGS 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670   389 KALAQPP------GVGKTPAQQPGPAKPPTqqvgTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSA 461
Cdd:pfam06346   79 TGIPPPPplpggaGIPPPPPPLPGGAGVPP----PPPPLPGGPGIPPPPPFPGGPGIPPPPPGMGMPPPPPFGFGVPAA 153
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
4510-4590 6.61e-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: 41.83  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4510 GNGLGIRIVG--GKeipGHSGEI-GAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIIsQQSGEaeiCV 4586
Cdd:cd06791    11 EQGLGITIAGyvGE---KASGELsGIFVKSIIPGSAADQDGRIQVNDQIIAVDGVNLQGFTNQEAVEVL-RNTGQ---VV 83

                  ....
gi 150170670 4587 RLDL 4590
Cdd:cd06791    84 HLTL 87
PRK10263 PRK10263
DNA translocase FtsK; Provisional
651-1054 7.16e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 46.23  E-value: 7.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  651 APVPSSPQPKLKTAPVTTTSAVSKSSPQPQQTSPKKDAAPKQDLSKAPEPKKPPPLVKQPTLHGSPSA------------ 718
Cdd:PRK10263  363 VPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQqpyyapapeqpv 442
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  719 --KAKQPPEADSLSKPAPPKEPSVPSEQdkaPVADDKPKQPKMVKPTTDLVSSSSAT--TKPDIPSSKVQSQAEEKTTPP 794
Cdd:PRK10263  443 agNAWQAEEQQSTFAPQSTYQTEQTYQQ---PAAQEPLYQQPQPVEQQPVVEPEPVVeeTKPARPPLYYFEEVEEKRARE 519
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  795 lKTDSAKPSQSFP-PTGEKVSPFDSKAIPRPASDSKIISHPGPSSESKGQKQVdPVQKKEEPKKAQTKMSPKPDAKPMP- 872
Cdd:PRK10263  520 -REQLAAWYQPIPePVKEPEPIKSSLKAPSVAAVPPVEAAAAVSPLASGVKKA-TLATGAAATVAAPVFSLANSGGPRPq 597
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  873 -KGSPTPPGPRP------------TAGQTVPTPQQSPKPQEQSRRFSLNLGSIT----------DAPKSQPTTPQETVTG 929
Cdd:PRK10263  598 vKEGIGPQLPRPkrirvptrrelaSYGIKLPSQRAAEEKAREAQRNQYDSGDQYnddeidamqqDELARQFAQTQQQRYG 677
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  930 KLFGFGASIFSQASNLIS--------TAGQPGPHSQSGPG------------APMKQA--PAPSQPPTSQG-PPKSTGQA 986
Cdd:PRK10263  678 EQYQHDVPVNAEDADAAAeaelarqfAQTQQQRYSGEQPAganpfslddfefSPMKALldDGPHEPLFTPIvEPVQQPQQ 757
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670  987 PPAPAKSIPVKKETKAPAAEKLEPKAEQAPTVKRTETEKKPPPikdsKSLTAEPQKAVLPTKLEKSPK 1054
Cdd:PRK10263  758 PVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAP----QPQYQQPQQPVAPQPQYQQPQ 821
PDZ2-PDZRN4-like cd06716
PDZ domain 2 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
4529-4579 7.47e-04

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: 41.49  E-value: 7.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 150170670 4529 EIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKtyEEVQSIISQQS 4579
Cdd:cd06716    30 DTGIYVSEVDPNSIAAKDGRIREGDQILQINGVDVQNR--EEAIALLSEEE 78
Androgen_recep pfam02166
Androgen receptor;
456-591 7.55e-04

Androgen receptor;


Pssm-ID: 426632 [Multi-domain]  Cd Length: 501  Bit Score: 45.69  E-value: 7.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   456 PGKTSAQQTGPTKPP----SQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPS 531
Cdd:pfam02166   32 PGPRHPEAAGGAAPPgarlQHQQQQQQQVPQQPQQQESSPRQPQASVQPQQAGDDGSPPAHNRGPAGYLALEDDEQPQPS 111
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   532 QqpgsakpsAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPSQGLPKTICPL 591
Cdd:pfam02166  112 Q--------AQPAAECCPENGCVPEPGAAAAAGKGLPQQAVAPAAPDDDDSAAPSTLSLL 163
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
244-437 7.78e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.02  E-value: 7.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  244 PEKIKSQPPGTGKPIQGPTQTPQTDHAKLPLQRDASRPQTKQADIVRGESVKPSLPSPSKPpiqqPTPGKPPAQQPghek 323
Cdd:PRK12323  397 PAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAA----PAAAARPAAAG---- 468
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  324 SQPGPAKPPAQPSGLTKPLAQQPGTVKPPV---QPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPgvGKT 400
Cdd:PRK12323  469 PRPVAAAAAAAPARAAPAAAPAPADDDPPPweeLPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAP--APA 546
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 150170670  401 PAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPT 437
Cdd:PRK12323  547 AAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPA 583
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
449-524 8.05e-04

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 45.38  E-value: 8.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670  449 IPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQP 524
Cdd:NF041121   15 MGRAAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPGAALP 90
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
226-489 8.24e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.84  E-value: 8.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  226 GRDPLQQDGTPKSISSQQPEKiKSQPPGTGKPIQGPTQTPQTDHAKLPLQ-RDASRPQTKQADIvrgesvkpslpsPSKP 304
Cdd:PTZ00449  539 ESDEPKEGGKPGETKEGEVGK-KPGPAKEHKPSKIPTLSKKPEFPKDPKHpKDPEEPKKPKRPR------------SAQR 605
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  305 PIQQPTPGKPPAQQPGHEKSQPGPAKPPAQPSGLTKPLA----QQPGTVKPPvQPPGTTKPPAQP---------LGPAKP 371
Cdd:PTZ00449  606 PTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSperpEGPKIIKSP-KPPKSPKPPFDPkfkekfyddYLDAAA 684
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  372 PAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPAKP--PTQQVGTPKPLaQQPGLQSPAKAPGPT----------KT 439
Cdd:PTZ00449  685 KSKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPklPRDEEFPFEPI-GDPDAEQPDDIEFFTppeeertffhET 763
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 150170670  440 PVQQPGPGkIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPG--PAKP 489
Cdd:PTZ00449  764 PADTPLPD-ILAEEFKEEDIHAETGEPDEAMKRPDSPSEHEDKPPGdhPSLP 814
C2F_Ferlin cd08374
C2 domain sixth repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
4780-4811 8.38e-04

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: 42.65  E-value: 8.38e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 150170670 4780 EQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLS 4811
Cdd:cd08374    88 EYKIPPKLTLQVWDNDKFSPDDFLGSLELDLS 119
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
863-1032 8.76e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 45.63  E-value: 8.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  863 SPKPDAKPMPKGSPTPPGPRPTAGQTVPTPQQSPKPQEQsrrfslnlgsiTDAPKSQPTTPQETVTGKLfgfgasifSQA 942
Cdd:PRK07994  365 LPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPP-----------ASAPQQAPAVPLPETTSQL--------LAA 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  943 SNLISTAGQPGPHSQSGPGAPMKQAPAPSQPPTSQGPPKSTGQAPPAPAKSIPVKKETKAPAAEKLEPKAEQAPTVKRTE 1022
Cdd:PRK07994  426 RQQLQRAQGATKAKKSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKALE 505
                         170
                  ....*....|
gi 150170670 1023 TEKKPPPIKD 1032
Cdd:PRK07994  506 HEKTPELAAK 515
HC2 pfam07382
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ...
323-487 8.78e-04

Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.


Pssm-ID: 369339 [Multi-domain]  Cd Length: 187  Bit Score: 43.61  E-value: 8.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   323 KSQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKppaqQTGSEKPSSEQPGPKALAQPPGVGKTPA 402
Cdd:pfam07382    5 QKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKK----TVAAKKPAAKKAAKKAVAKKVVAKKPVA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   403 QQPGPAKPPTQQVGTPKPLAQQ-PGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPP 481
Cdd:pfam07382   81 KKAVAKKATAKKVAAKKVVAKKtVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAKKAASTCHKNHKHTAACKRVASSSA 160

                   ....*.
gi 150170670   482 QQPGPA 487
Cdd:pfam07382  161 TRAACG 166
COG3416 COG3416
Uncharacterized conserved protein, DUF2076 domain [Function unknown];
485-539 8.91e-04

Uncharacterized conserved protein, DUF2076 domain [Function unknown];


Pssm-ID: 442642 [Multi-domain]  Cd Length: 237  Bit Score: 44.24  E-value: 8.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 150170670  485 GPAKPPPQQPGSAKPPSQqpgstkPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKP 539
Cdd:COG3416    93 GQRPPPAPQPSQPGPQQQ------PAPPSGPWGQAAPQQPGYGQPQYGQPAAGPS 141
PHA03247 PHA03247
large tegument protein UL36; Provisional
386-581 9.13e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 9.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  386 PGPKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQP-GLQSPAKAPGPTKTPVQQPGPgkiPAQQAGPGKTSAQQT 464
Cdd:PHA03247  255 PAPPPVVGEGADRAPETARGATGPPPPPEAAAPNGAAAPPdGVWGAALAGAPLALPAPPDPP---PPAPAGDAEEEDDED 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  465 GPTKPPSQLPGP-AKPP---PQQPGPAKPPPQQ-----PGSAKPPSQQPGST--KPPPQQPGPAKPSPQQPGSTKPPSQQ 533
Cdd:PHA03247  332 GAMEVVSPLPRPrQHYPlgfPKRRRPTWTPPSSledlsAGRHHPKRASLPTRkrRSARHAATPFARGPGGDDQTRPAAPV 411
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 150170670  534 PGSAKPSAQQPSPA-KPSAQQSTKPVSQTGSGK-PLQPPTVSPSAKQPPS 581
Cdd:PHA03247  412 PASVPTPAPTPVPAsAPPPPATPLPSAEPGSDDgPAPPPERQPPAPATEP 461
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
470-573 9.57e-04

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 45.57  E-value: 9.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   470 PSQLPGPAKPPP-QQPGPAKPPPQQP-----GSAKPPSQQPGStkpPPQQPGPAKPSPQQpgsTKPPSQQPGSAKPSaQQ 543
Cdd:TIGR01628  388 GSPMGGAMGQPPyYGQGPQQQFNGQPlgwprMSMMPTPMGPGG---PLRPNGLAPMNAVR---APSRNAQNAAQKPP-MQ 460
                           90       100       110
                   ....*....|....*....|....*....|
gi 150170670   544 PSPAKPSAQQstKPVSQtgsGKPLQPPTVS 573
Cdd:TIGR01628  461 PVMYPPNYQS--LPLSQ---DLPQPQSTAS 485
PHA02682 PHA02682
ORF080 virion core protein; Provisional
409-549 9.63e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 44.47  E-value: 9.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  409 KPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGkipaqqagpgktsaqqtgPTKPPSQlpGPAKPPPqqpgPAK 488
Cdd:PHA02682   75 RPSGQSPLAPSPACAAPAPACPACAPAAPAPAVTCPAPA------------------PACPPAT--APTCPPP----AVC 130
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670  489 PPPQQPGSAKPPSQQPGSTKPPPQQPGP---AKPSPQQpgSTKPPSQQPGSAKPSAQQPSPAKP 549
Cdd:PHA02682  131 PAPARPAPACPPSTRQCPPAPPLPTPKPapaAKPIFLH--NQLPPPDYPAASCPTIETAPAASP 192
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
713-896 9.98e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 45.49  E-value: 9.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  713 HGSPSAKAKQPPEADSLSKPAPPKEPSVPSEQD---------------------------KAPVADDKPKQPKMVKPTtd 765
Cdd:PRK14949  577 VQSAQSAAEAQPSSQSLSPISAVTTAAASLADDdildavlaardsllsdldalspkegdgKKSSADRKPKTPPSRAPP-- 654
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  766 lVSSSSATTKPDiPSSKVQSQAEEKTTPPLKTDSAKPSQSFPPTGEKVSPfDSKAIPRPASDSKIISHPGPSSESKGQKQ 845
Cdd:PRK14949  655 -ASLSKPASSPD-ASQTSASFDLDPDFELATHQSVPEAALASGSAPAPPP-VPDPYDRPPWEEAPEVASANDGPNNAAEG 731
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 150170670  846 VDPVQKKEEPKKAQTKMSPKPDAKPMPKGSPTPPGPRPTAGQTVPTPQQSP 896
Cdd:PRK14949  732 NLSESVEDASNSELQAVEQQATHQPQVQAEAQSPASTTALTQTSSEVQDTE 782
C2A_Ferlin cd08373
C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
4713-4816 9.99e-04

C2 domain first 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 first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176019 [Multi-domain]  Cd Length: 127  Bit Score: 42.24  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4713 ILQARNLVPrdNNGYSDPFVKVYLlpgRGQvmvvqnasaeyKRRTKHVQKSLNPEWNQTV---IYKSISMEQLkkktLEV 4789
Cdd:cd08373     2 VVSLKNLPG--LKGKGDRIAKVTF---RGV-----------KKKTRVLENELNPVWNETFewpLAGSPDPDES----LEI 61
                          90       100       110
                  ....*....|....*....|....*....|
gi 150170670 4790 TVWDYDRFSSNDFLGE---VLIDLSSTSHL 4816
Cdd:cd08373    62 VVKDYEKVGRNRLIGSatvSLQDLVSEGLL 91
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
224-521 1.02e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.55  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  224 GPGRDPlQQDGTPKSISSQQPEKIKSQPPGTGKPiQGPTQTPQTDHAKLPLQRDASRPQTKQADIVRGESVKPSLPSPSK 303
Cdd:PHA03307  116 PPPPTP-PPASPPPSPAPDLSEMLRPVGSPGPPP-AASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEP 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  304 PPIQQPTPGKPPAQ------QPGHEKSQPGPAK-----PPAQPSGLTKPLAQ-----QPGTVKPPVQPPGTTKPPAQPLG 367
Cdd:PHA03307  194 PPSTPPAAASPRPPrrsspiSASASSPAPAPGRsaaddAGASSSDSSSSESSgcgwgPENECPLPRPAPITLPTRIWEAS 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  368 PAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPAKP---PTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQP 444
Cdd:PHA03307  274 GWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSsssSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSP 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  445 GPGKIPA-----QQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKP---------- 509
Cdd:PHA03307  354 SRPPPPAdpsspRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASgafyarypll 433
                         330
                  ....*....|...
gi 150170670  510 -PPQQPGPAKPSP 521
Cdd:PHA03307  434 tPSGEPWPGSPPP 446
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
417-518 1.10e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 45.19  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  417 TPKPLAQQPGLQSPAKAPgptktpvQQPGPGkipaqQAGPGKTSAQQTGPTKPPS-QLPGPAKPPPQQPGPAKPPPQQPG 495
Cdd:PRK14950  361 VPVPAPQPAKPTAAAPSP-------VRPTPA-----PSTRPKAAAAANIPPKEPVrETATPPPVPPRPVAPPVPHTPESA 428
                          90       100
                  ....*....|....*....|...
gi 150170670  496 SAKPPSQQPGSTKPPPQQPGPAK 518
Cdd:PRK14950  429 PKLTRAAIPVDEKPKYTPPAPPK 451
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
1154-1558 1.18e-03

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


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 45.39  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1154 VKLVKKQeQEVKTE---AEKVILEKVKETLSMEKippmvttdQKQEESKLEKDKASALQEKKPLPEEKKLIPEEEKiRSE 1230
Cdd:NF033838   87 VALNKKL-SDIKTEylyELNVLKEKSEAELTSKT--------KKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEK-KAK 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1231 EKKPLLEEKKPTPEDKKLLPEAKTSAPEEQKHDLLKSQVQIAEEKLEGRV--APKTVQEGKQPQTKMEGLPsgTPQSLPK 1308
Cdd:NF033838  157 DQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIkqAKAKVESKKAEATRLEKIK--TDREKAE 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1309 EDDKTTKTIKEQpqppctakpDQVEPGKEKTEKEDDKSDT--SSSQQPKSPQGLSDTGYSSDgisSSLGE----IPSLIP 1382
Cdd:NF033838  235 EEAKRRADAKLK---------EAVEKNVATSEQDKPKRRAkrGVLGEPATPDKKENDAKSSD---SSVGEetlpSPSLKP 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1383 tdEKDILKGLKK-DSFSQESSPSSPSDLAKLESTVLSILEAQastLADEKSEKKTQPHEVSPE---QPKDQEKTQSLSET 1458
Cdd:NF033838  303 --EKKVAEAEKKvEEAKKKAKDQKEEDRRNYPTNTYKTLELE---IAESDVKVKEAELELVKEeakEPRNEEKIKQAKAK 377
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1459 LEitiseeeIKESQEERKDTFKKDSQQdipSSKDHKEKSEFVDDIttrrepydSVEESSESENSPVPQRKRRTSVGSSSS 1538
Cdd:NF033838  378 VE-------SKKAEATRLEKIKTDRKK---AEEEAKRKAAEEDKV--------KEKPAEQPQPAPAPQPEKPAPKPEKPA 439
                         410       420
                  ....*....|....*....|
gi 150170670 1539 DEYKQEDSQGSGEEEDFIRK 1558
Cdd:NF033838  440 EQPKAEKPADQQAEEDYARR 459
Treacle pfam03546
Treacher Collins syndrome protein Treacle;
238-579 1.22e-03

Treacher Collins syndrome protein Treacle;


Pssm-ID: 460967 [Multi-domain]  Cd Length: 531  Bit Score: 45.06  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   238 SISSQQPEKIKSQPPGTGKPIQgPTQTPQTDHAKLPLQRdaSRPQTKQADIVRGESVKPSLPSPSKPPIQQPTPGKPPAQ 317
Cdd:pfam03546  178 SEGEAPPAATQAKPSGKILQVR-PASGPAKGAAPAPPQK--AGPVATQVKAERSKEDSESSEESSDSEEEAPAAATPAQA 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   318 QPGHEKSQP--GPAK-PPAQPSGlTKPLAQQPGTVKP----PVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQ----P 386
Cdd:pfam03546  255 KPALKTPQTkaSPRKgTPITPTS-AKVPPVRVGTPAPwkagTVTSPACASSPAVARGAQRPEEDSSSSEESESEEetapA 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   387 GPKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPlaqqPGLQSPAKAPGPTKTPvQQPGPGKIPAQQAGPGKTSAQQTGP 466
Cdd:pfam03546  334 AAVGQAKSVGKGLQGKAASAPTKGPSGQGTAPVP----PGKTGPAVAQVKAEAQ-EDSESSEEESDSEEAAATPAQVKAS 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   467 TKPPsqlPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPgPAKPSPQQPGSTKPPSQQPGSAKPSA----Q 542
Cdd:pfam03546  409 GKTP---QAKANPAPTKASSAKGAASAPGKVVAAAAQAKQGSPAKVKP-PARTPQNSAISVRGQASVPAVGKAVAtaaqA 484
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 150170670   543 QPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQP 579
Cdd:pfam03546  485 QKGPVGGPQEEDSESSEEESDSEEEAPAQAKPSGKTP 521
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
946-1028 1.28e-03

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 44.67  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  946 ISTAGQPGPHsqsgpgaPMKQAPAPSQPPTSQGPPKSTGQAPPAPAKSIPVKKETKAPAAEKLEPKAEQAPTVKRTETEK 1025
Cdd:PTZ00144  118 IDTGGAPPAA-------APAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPPEPAPAAKPPPTPVARADPRET 190

                  ...
gi 150170670 1026 KPP 1028
Cdd:PTZ00144  191 RVP 193
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
388-543 1.31e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 45.24  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  388 PKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPlaQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPT 467
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAP--PQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKA 438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  468 KPPSQLPGPAKPP-----------PQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQ-QPGPAKPSPQQPgstKPPSQQPG 535
Cdd:PRK07994  439 KKSEPAAASRARPvnsalerlasvRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVaTPKALKKALEHE---KTPELAAK 515

                  ....*...
gi 150170670  536 SAKPSAQQ 543
Cdd:PRK07994  516 LAAEAIER 523
COG3416 COG3416
Uncharacterized conserved protein, DUF2076 domain [Function unknown];
451-515 1.39e-03

Uncharacterized conserved protein, DUF2076 domain [Function unknown];


Pssm-ID: 442642 [Multi-domain]  Cd Length: 237  Bit Score: 43.86  E-value: 1.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  451 AQQAGPGKTSA-----QQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGstkPPPQQPG 515
Cdd:COG3416    78 QPQSSGGFLSGlfgggQRPPPAPQPSQPGPQQQPAPPSGPWGQAAPQQPGYGQPQYGQPA---AGPSGGG 144
PHA03291 PHA03291
envelope glycoprotein I; Provisional
394-516 1.41e-03

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 44.56  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  394 PPGVGKTPAQQPgPAKPPTQQVGTPKPLAQQPGLQSPAKAPGptktPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQL 473
Cdd:PHA03291  160 PLGLAAFPAEGT-LAAPPLGEGSADGSCDPALPLSAPRLGPA----DVFVPATPRPTPRTTASPETTPTPSTTTSPPSTT 234
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 150170670  474 PGPAKPPPQQPGPAKpPPQQPGSAKPPSQQPGSTKPPPQQPGP 516
Cdd:PHA03291  235 IPAPSTTIAAPQAGT-TPEAEGTPAPPTPGGGEAPPANATPAP 276
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
252-555 1.44e-03

Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442497 [Multi-domain]  Cd Length: 455  Bit Score: 44.84  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  252 PGTGKPIQGPTQTPQTDHAKLPLQRDASRPQTKQADIVRGESVKPSLPSPSKPPIQQPTPGKPPAQQPGHEKSQPGPAKP 331
Cdd:COG3266    53 LLAGLLLLLIRLLSEAVDLGALASAALLLALASLALLGILLLALLALLLDLLLLADLLRAAALLLLKLLLLLLTLLLLVL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  332 PAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTP-------AQQ 404
Cdd:COG3266   133 LLLLALLLALLLDLPLLTLLIVLPLLEEQLLLLALQDIQGTLQALGAVAALLGLRKAEEALALRAGSAAAdalalllLLL 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  405 PGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQP 484
Cdd:COG3266   213 ASALGEAVAAAAELAALALLAAGAAEVLTARLVLLLLIIGSALKAPSQASSASAPATTSLGEQQEVSLPPAVAAQPAAAA 292
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150170670  485 GPAKPPPQQPgsAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQqpsPAKPSAQQST 555
Cdd:COG3266   293 AAQPSAVALP--AAPAAAAAAAAPAEAAAPQPTAAKPVVTETAAPAAPAPEAAAAAAA---PAAPAVAKKL 358
PHA03247 PHA03247
large tegument protein UL36; Provisional
308-515 1.47e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  308 QPTPGKPPAQQPGHeksqpgPAKPPAQPSGL-TKPLAQQPGTVKPPVQPPgtTKPPAQ---------------------- 364
Cdd:PHA03247  273 RGATGPPPPPEAAA------PNGAAAPPDGVwGAALAGAPLALPAPPDPP--PPAPAGdaeeeddedgamevvsplprpr 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  365 ---PLGPAK-------PPAQ---QTGSEKPSSEQPGPKA-----------LAQPPGVGKTPAQQ-PGPAKPPTqqvgtpk 419
Cdd:PHA03247  345 qhyPLGFPKrrrptwtPPSSledLSAGRHHPKRASLPTRkrrsarhaatpFARGPGGDDQTRPAaPVPASVPT------- 417
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  420 plaqqpglqspakaPGPTKTPVQQPGPGKIPAQQAGPGKTSaqqtGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKp 499
Cdd:PHA03247  418 --------------PAPTPVPASAPPPPATPLPSAEPGSDD----GPAPPPERQPPAPATEPAPDDPDDATRKALDALR- 478
                         250
                  ....*....|....*.
gi 150170670  500 psqqpgsTKPPPQQPG 515
Cdd:PHA03247  479 -------ERRPPEPPG 487
COG3416 COG3416
Uncharacterized conserved protein, DUF2076 domain [Function unknown];
471-535 1.48e-03

Uncharacterized conserved protein, DUF2076 domain [Function unknown];


Pssm-ID: 442642 [Multi-domain]  Cd Length: 237  Bit Score: 43.47  E-value: 1.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670  471 SQLPGPAKPPPQQPGP---------AKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPG 535
Cdd:COG3416    69 AQLAQLQQQQPQSSGGflsglfgggQRPPPAPQPSQPGPQQQPAPPSGPWGQAAPQQPGYGQPQYGQPAAGPSG 142
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1127-1363 1.51e-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: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1127 PAPSGPKASPMPVPTESSSQKTAVPPQVKLVKKQEQEVKTEAEKVILEKVKETlsmEKIPPMVTTDQKQEESKLEKDKAS 1206
Cdd:NF033839  284 PKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQP---EKPKPEVKPQLETPKPEVKPQPEK 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1207 ALQEKKPLPEEKK-LIPEEEKIRSEEKKPLLEEKKP--TPEDKKLLPEAKtsaPEEQKHdllKSQVQIAEEKLEGRVAPK 1283
Cdd:NF033839  361 PKPEVKPQPEKPKpEVKPQPETPKPEVKPQPEKPKPevKPQPEKPKPEVK---PQPEKP---KPEVKPQPEKPKPEVKPQ 434
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1284 TVQEGKQPQTKMEG-LPSGTPQslPKEDDKTTKTIKEQPQPPCTAKPDQVEPGKEKTEKEDDK-SDTSSSQQPKSPQGLS 1361
Cdd:NF033839  435 PEKPKPEVKPQPEKpKPEVKPQ--PETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKpSTPNNLSKDKQPSNQA 512

                  ..
gi 150170670 1362 DT 1363
Cdd:NF033839  513 ST 514
PHA03247 PHA03247
large tegument protein UL36; Provisional
11-517 1.52e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   11 GLPEGLAAAAAAGGGASGAGSPSHTAIPAGMEADLSQLSEEERRQIAAVMSRAQGLPKGSVPPAAAESPSMHRKQELDSS 90
Cdd:PHA03247 2718 ATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRES 2797
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   91 HPPkqsgrPPDPGRPAQPGLSKSRTTDTfrSEQKLPGRSPSTISLKESKSRTdlkeehkssmmPGFLSEvnALSAVSSVV 170
Cdd:PHA03247 2798 LPS-----PWDPADPPAAVLAPAAALPP--AASPAGPLPPPTSAQPTAPPPP-----------PGPPPP--SLPLGGSVA 2857
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  171 nkfnpfdlisdseasqeettkkqkvvqkeqgkpegiikpplqqqppkpipkqqgPGRDplqqdgtpksissqqpekIKSQ 250
Cdd:PHA03247 2858 ------------------------------------------------------PGGD------------------VRRR 2865
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  251 PPgTGKPIQGPTQTPQtdhaklPLQRDASRPQTKQAdivrgesvkpslpspskppiQQPTPGKPPAQQPgheksqpgPAK 330
Cdd:PHA03247 2866 PP-SRSPAAKPAAPAR------PPVRRLARPAVSRS--------------------TESFALPPDQPER--------PPQ 2910
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  331 PPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQplgpakPPAQQTGSEKPSSEQPGPKALAQPPG---VGKTPAQQPGP 407
Cdd:PHA03247 2911 PQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA------PTTDPAGAGEPSGAVPQPWLGALVPGrvaVPRFRVPQPAP 2984
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  408 AKPPTQQVGTPKPLAQQPGLQSPAKAPG----PTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQ 483
Cdd:PHA03247 2985 SREAPASSTPPLTGHSLSRVSSWASSLAlheeTDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDPLPPEPHD 3064
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 150170670  484 P--GPAKPPPQQPGSAKPPSQQPGstkPPPQQPGPA 517
Cdd:PHA03247 3065 PfaHEPDPATPEAGARESPSSQFG---PPPLSANAA 3097
PDZ4_INAD-like cd23065
PDZ domain 4 of inactivation-no-after-potential D (INAD), and related domains; PDZ (PSD-95 ...
4497-4586 1.53e-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: 40.58  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4497 IKITRDSKDhtvsgngLGIRIVGGKEipghSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIIS 4576
Cdd:cd23065     2 IELKTDKSP-------LGVSVVGGKN----HVTTGCIITHIYPNSIVAADKRLKVFDQILDINGTKVHVMTTLKVHQLFH 70
                          90
                  ....*....|
gi 150170670 4577 QQSGEAEICV 4586
Cdd:cd23065    71 KTYEKAVTLV 80
Treacle pfam03546
Treacher Collins syndrome protein Treacle;
651-1067 1.55e-03

Treacher Collins syndrome protein Treacle;


Pssm-ID: 460967 [Multi-domain]  Cd Length: 531  Bit Score: 44.68  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   651 APVPSSPQPKLKTAPVTTTSAVSKSSPQ-------PQQTSPKKDAA----PKQDLSKAPEPKKPPPLVKQPTLHGSPSAK 719
Cdd:pfam03546   41 AKTPLQAKPSGKTPQVRAASAPAKESPRkgappvpPGKTGPAAAQAqagkPEEDSESSSEESDSDGETPAAATLTTSPAQ 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   720 AKqPPEADSLSKPA------PPKEPSVPSEQDKAPVADDKPKQPKMVKPTtdlvSSSSATTKPDIPSSKVQSQAE-EKTT 792
Cdd:pfam03546  121 VK-PLGKNSQVRPAstvgkgPSGKGANPAPPGKAGSAAPLVQVGKKEEDS----ESSSEESDSEGEAPPAATQAKpSGKI 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   793 PPLKTDSAKPSQSFPPTGEKVSPFDSKAIPRPASDSKIISHPGPSSESKGQKQVDPVQKKEEPKKAQTKMSPKPDAKPMP 872
Cdd:pfam03546  196 LQVRPASGPAKGAAPAPPQKAGPVATQVKAERSKEDSESSEESSDSEEEAPAAATPAQAKPALKTPQTKASPRKGTPITP 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   873 KGSPTPP------GPRPTAGQTVPTPQQSPKPQEQSRRFSLNLGSITDAPKSQPTTPQETVtgklfgfgasifsqasnli 946
Cdd:pfam03546  276 TSAKVPPvrvgtpAPWKAGTVTSPACASSPAVARGAQRPEEDSSSSEESESEEETAPAAAV------------------- 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   947 stagqpGPHSQSGPGAPMKQAPAPSQPPTSQgppkstGQAPPAPAKSIPVKKETKAPAAEKLEPKAEQA----------- 1015
Cdd:pfam03546  337 ------GQAKSVGKGLQGKAASAPTKGPSGQ------GTAPVPPGKTGPAVAQVKAEAQEDSESSEEESdseeaaatpaq 404
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670  1016 --PTVKRTETEKKPPPIKDS--KSLTAEPQKAVLPTKLEKSPKPESTCPLCKTELN 1067
Cdd:pfam03546  405 vkASGKTPQAKANPAPTKASsaKGAASAPGKVVAAAAQAKQGSPAKVKPPARTPQN 460
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
416-580 1.55e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  416 GTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPG 495
Cdd:PHA03307  731 RTVAPLVRYSPRRARARASAWDITDALFSNPSLVPAKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAAD 810
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  496 SAKPPSQQPGSTKPPPQ----QPGPAKPSPqqPGSTKPPSQQPGSAKPSAQQPSPA----------KPSAQQSTKPVSQT 561
Cdd:PHA03307  811 AASRTASKRKSRSHTPDggseSSGPARPPG--AAARPPPARSSESSKSKPAAAGGRargkngrrrpRPPEPRARPGAAAP 888
                         170
                  ....*....|....*....
gi 150170670  562 GSGKPLQPPTVSPSAKQPP 580
Cdd:PHA03307  889 PKAAAAAPPAGAPAPRPRP 907
TYA pfam01021
Ty transposon capsid protein; Ty are yeast transposons. A 5.7kb transcript codes for p3 a ...
425-577 1.55e-03

Ty transposon capsid protein; Ty are yeast transposons. A 5.7kb transcript codes for p3 a fusion protein of TYA and TYB. The TYA protein is analogous to the gag protein of retroviruses. TYA a is cleaved to form 46kd protein which can form mature virion like particles. This entry corresponds to the capsid protein from Ty1 and Ty2 transposons.


Pssm-ID: 425992  Cd Length: 384  Bit Score: 44.56  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   425 PGLQSPAKAPGpTKTPVQQPGPGKIPAQQAGPGKTSAQqtgPTKPPSQLPGPAKPPPQQPGPAK-----PPPQQPGSAKP 499
Cdd:pfam01021   11 HTNQDPLDVSA-SKLQEYDKDSTKANSQQTTTPGSSAV---PENHHHASPQPASVPPPQNGPYSqqcmmTPNQANPSGWP 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   500 PSQQPGSTKPPPQQ-------PGPAKPSPQQPGSTKPPSqqpgsakpSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTV 572
Cdd:pfam01021   87 FYGHPSMMPYTPYQmspmyfpPGPQSQFPQYPSSVGTPL--------STPSPESGNTFTDSSSAKSDMTSTNKYVRPPPI 158

                   ....*
gi 150170670   573 SPSAK 577
Cdd:pfam01021  159 LTSPN 163
COG3416 COG3416
Uncharacterized conserved protein, DUF2076 domain [Function unknown];
482-536 1.63e-03

Uncharacterized conserved protein, DUF2076 domain [Function unknown];


Pssm-ID: 442642 [Multi-domain]  Cd Length: 237  Bit Score: 43.47  E-value: 1.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 150170670  482 QQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGstkPPSQQPGS 536
Cdd:COG3416    94 QRPPPAPQPSQPGPQQQPAPPSGPWGQAAPQQPGYGQPQYGQPA---AGPSGGGG 145
Neisseria_TspB pfam05616
Neisseria meningitidis TspB protein; This family consists of several Neisseria meningitidis ...
395-515 1.71e-03

Neisseria meningitidis TspB protein; This family consists of several Neisseria meningitidis TspB virulence factor proteins.


Pssm-ID: 283306 [Multi-domain]  Cd Length: 517  Bit Score: 44.70  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   395 PGVGKTPAQQPGPA---KPPTQQVGTPKPLAQQPGlqspAKAPGPTKTPVQQ-PGPGKIPAQQAGPGKTSAQQTGPTKPP 470
Cdd:pfam05616  277 PGYSEKVEVAPGTKvnmGPVTDRNGNPVQVAATFG----RDAQGNTTADVQViPRPDLTPASAEAPHAQPLPEVSPAENP 352
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 150170670   471 SQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPG 515
Cdd:pfam05616  353 ANNPDPDENPGTRPNPEPDPDLNPDANPDTDGQPGTRPDSPAVPD 397
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
1146-1290 1.71e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.41  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1146 QKTAVPPQVKLVKKQEQEVKTEaekvILEKVKEtlsmekippmvttdQKQEESKLEKDKASALQEKKPLPEEKKLIPEEE 1225
Cdd:PRK09510   70 QQKSAKRAEEQRKKKEQQQAEE----LQQKQAA--------------EQERLKQLEKERLAAQEQKKQAEEAAKQAALKQ 131
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1226 KIRSEEKKPLLEE--KKPTPEDKKLLPEAKTSAPEEQKHDLLKSQVQIAEE---KLEGRVAPKTVQEGKQ 1290
Cdd:PRK09510  132 KQAEEAAAKAAAAakAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEakkKAEAEAAAKAAAEAKK 201
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
422-565 1.72e-03

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 44.17  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  422 AQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAG-PGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPP 500
Cdd:PTZ00436  208 AAAPSGKKSAKAAAPAKAAAAPAKAAAPPAKAAAaPAKAAAAPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAKAAAPPAK 287
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150170670  501 SQQP---GSTKPPPQQPGPAKPSPQQPGSTKPPSQqpGSAKPSAQQPSPAK---PSAQQSTKPVSQTGSGK 565
Cdd:PTZ00436  288 AAAPpakAAAAPAKAAAAPAKAAAAPAKAAAPPAK--AAAPPAKAATPPAKaaaPPAKAAAAPVGKKAGGK 356
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
476-587 1.91e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 44.47  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  476 PAKPPPQQPGPAKPPPQQPGSAKPPSQQPGStkPPPQQPGPAKPSPQQPgstkpPSQQPGSAKPSAQQPSPAKPSAQQST 555
Cdd:PRK07994  364 PLPEPEVPPQSAAPAASAQATAAPTAAVAPP--QAPAVPPPPASAPQQA-----PAVPLPETTSQLLAARQQLQRAQGAT 436
                          90       100       110
                  ....*....|....*....|....*....|..
gi 150170670  556 KPVSQTGSGKPLQPPTVSPSAKQPPSQGLPKT 587
Cdd:PRK07994  437 KAKKSEPAAASRARPVNSALERLASVRPAPSA 468
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
354-522 1.99e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  354 QPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKA 433
Cdd:PHA03307  759 SNPSLVPAKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKSRSHTPDGGSESSGPARP 838
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  434 PGPTKTPVqqpgpgkiPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPqQPGSAKPPSQQPGSTKPPPQQ 513
Cdd:PHA03307  839 PGAAARPP--------PARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAP-PKAAAAAPPAGAPAPRPRPAP 909

                  ....*....
gi 150170670  514 PGPAKPSPQ 522
Cdd:PHA03307  910 RVKLGPMPP 918
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
322-409 2.01e-03

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 44.88  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  322 EKSQPGPAKPPAQPSGLTKPLAQQPgtvKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTP 401
Cdd:PRK12270   39 GSTAAPTAAAAAAAAAASAPAAAPA---AKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVED 115
                          90
                  ....*....|
gi 150170670  402 AQQP--GPAK 409
Cdd:PRK12270  116 EVTPlrGAAA 125
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
502-559 2.02e-03

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 44.13  E-value: 2.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670  502 QQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVS 559
Cdd:PRK01297   14 AEQPAPAPPSPAAAPAPPPPAKTAAPATKAAAPAAAAPRAEKPKKDKPRRERKPKPAS 71
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
415-581 2.11e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  415 VGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPpsqlpgpaKPPPQQPGPAKPPPqqP 494
Cdd:PHA03307  772 LALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKSRSHTP--------DGGSESSGPARPPG--A 841
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  495 GSAKPPSQQPGSTKPPPQQPGPAKP--SPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQStkpvsqtgSGKPLQPPTV 572
Cdd:PHA03307  842 AARPPPARSSESSKSKPAAAGGRARgkNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAP--------RPRPAPRVKL 913

                  ....*....
gi 150170670  573 SPSAKQPPS 581
Cdd:PHA03307  914 GPMPPGGPD 922
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
4752-4813 2.12e-03

C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc 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.


Pssm-ID: 175988 [Multi-domain]  Cd Length: 125  Bit Score: 41.11  E-value: 2.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670 4752 EYKRRTKHVQKSLNPEWNQ--TVIYKSISmeqlkkkTLEVTVWDYDRFSSNDFLGEVLIDLSST 4813
Cdd:cd04021    33 QPPKKTEVSKKTSNPKWNEhfTVLVTPQS-------TLEFKVWSHHTLKADVLLGEASLDLSDI 89
PDZ3_PDZD7-like cd06751
PDZ domain 3 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
4513-4577 2.19e-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: 40.11  E-value: 2.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150170670 4513 LGIRIVGGKEipgHSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQ 4577
Cdd:cd06751    13 LGISISGGIE---SKVQPVVKIEKIFPGGAAALSGNLKAGYELVSVDGESLQQVTHQQAVDIIRR 74
C2A_RasGAP cd08383
C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
4709-4825 2.24e-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: 41.10  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4709 LIIHILQARNLVPRdnnGYSDPFVKVYLlpgrGQVMVVqnasaeykrRTKHVQKsLNPEWNQTVIYKSISMEqLKKKTLE 4788
Cdd:cd08383     2 LRLRILEAKNLPSK---GTRDPYCTVSL----DQVEVA---------RTKTVEK-LNPFWGEEFVFDDPPPD-VTFFTLS 63
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150170670 4789 VTVWDYDRFSSNDFLGEVLID-LSSTSHLDNtprWYPL 4825
Cdd:cd08383    64 FYNKDKRSKDRDIVIGKVALSkLDLGQGKDE---WFPL 98
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
471-552 2.26e-03

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 44.50  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  471 SQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPS 550
Cdd:PRK12270   35 DYGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVE 114

                  ..
gi 150170670  551 AQ 552
Cdd:PRK12270  115 DE 116
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
4509-4587 2.29e-03

PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZD11, and related domains. PDZD11 (also known as ATPase-interacting PDZ protein, plasma membrane calcium ATPase-interacting single-PDZ protein, PMCA-interacting single-PDZ protein, PISP) is involved in the dynamic assembly of apical junctions (AJs). It is recruited by PLEKHA7 to AJs to promote the efficient junctional recruitment and stabilization of nectins, and the efficient early phases of assembly of AJs in epithelial cells. The PDZD11 PDZ domain binds nectin-1 and nectin-3. PDZD11 also binds to a PDZ binding motif located in the C-terminal tail of the human sodium-dependent multivitamin transporter, to the cytoplasmic tail of the Menkes copper ATPase ATP7A, and to the cytoplasmic tail of all plasma membrane Ca2+-ATPase b-splice variants. 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 PDZD11-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: 467234 [Multi-domain]  Cd Length: 83  Bit Score: 39.99  E-value: 2.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670 4509 SGNGLGIRIVGGKEipghsGEIGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTSKTYEEVQSIIsQQSGEAEICVR 4587
Cdd:cd06752     9 PGEQLGFNIRGGKA-----SGLGIFISKVIPDSDAHRLG-LKEGDQILSVNGVDFEDIEHSEAVKVL-KTAREIQMRVR 80
PHA03291 PHA03291
envelope glycoprotein I; Provisional
418-536 2.31e-03

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 43.79  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  418 PKPLAQQPGLQSPAKAPGpTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQLPGP--AKPPPQQPGPAKPPPQQPG 495
Cdd:PHA03291  160 PLGLAAFPAEGTLAAPPL-GEGSADGSCDPALPLSAPRLGPADVFVPATPRPTPRTTASpeTTPTPSTTTSPPSTTIPAP 238
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 150170670  496 SAKPPSQQPGSTKPPPQQPGPAKPSpqqPGSTKPPSQQPGS 536
Cdd:PHA03291  239 STTIAAPQAGTTPEAEGTPAPPTPG---GGEAPPANATPAP 276
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
4706-4812 2.32e-03

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


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 44.36  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4706 LGNLIIHILQARNLVPRDN--NGYSDPFVkVYLLPGRgqvmvvqnasaeYKRRTKHVQKSLNPEWNQTvIYksISMEQLK 4783
Cdd:COG5038   435 IGVVEVKIKSAEGLKKSDStiNGTVDPYI-TVTFSDR------------VIGKTRVKKNTLNPVWNET-FY--ILLNSFT 498
                          90       100
                  ....*....|....*....|....*....
gi 150170670 4784 KKtLEVTVWDYDRFSSNDFLGEVLIDLSS 4812
Cdd:COG5038   499 DP-LNLSLYDFNSFKSDKVVGSTQLDLAL 526
DUF4106 pfam13388
Protein of unknown function (DUF4106); This family of proteins are found in large numbers in ...
436-524 2.36e-03

Protein of unknown function (DUF4106); This family of proteins are found in large numbers in the Trichomonas vaginalis proteome. The function of this protein is unknown.


Pssm-ID: 404296  Cd Length: 431  Bit Score: 44.12  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   436 PTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTkppsqlpgpAKPPPQQP---GPAKPPPQQPGSAKPPSQQPGSTKPPPQ 512
Cdd:pfam13388  173 PPNPPREAPAPGLPKTFTSSHGHRHRHAPKPT---------VQNPAQQPtvqNPAQQPTQQPTVQNPAQQQNPAQQPPPQ 243
                           90
                   ....*....|....*
gi 150170670   513 ---QPGPAKPSPQQP 524
Cdd:pfam13388  244 paqQPTVQNPAQQQP 258
PRK14954 PRK14954
DNA polymerase III subunits gamma and tau; Provisional
404-527 2.39e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184918 [Multi-domain]  Cd Length: 620  Bit Score: 44.16  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  404 QPGPAK-PPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAqqagpgktsaqqtgptkpPSQLPGPAKPPPQ 482
Cdd:PRK14954  381 APSPAGsPDVKKKAPEPDLPQPDRHPGPAKPEAPGARPAELPSPASAPT------------------PEQQPPVARSAPL 442
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 150170670  483 QPGPAKPPPQQPGSAKP----PSQQPGSTK--PPPQQPGPAKPSPQQPGST 527
Cdd:PRK14954  443 PPSPQASAPRNVASGKPgvdlGSWQGKFMNftRNGSRKQPVQASSSDAAQT 493
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
848-1055 2.40e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.10  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  848 PVQKKEEPKKAQTKMSPKP-DAKPMPKGSPTPPGPRPTAGQTVPTPQQSPKPQEQSRRFSLNLGSITDAPKSQPTTpqet 926
Cdd:PRK12323  381 PVAQPAPAAAAPAAAAPAPaAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAA---- 456
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  927 vtgklfgfgasifSQASNLISTAGQPGPHSQSGPGAPMKQAPAPSQPPTSQGPPKSTgQAPPAPAKSIPVKKETKAPAAE 1006
Cdd:PRK12323  457 -------------APAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWE-ELPPEFASPAPAQPDAAPAGWV 522
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 150170670 1007 K---LEPKAEQAPTVKRTETEKKPPPIKDSKSLTAEPQKAVLPTKLEKSPKP 1055
Cdd:PRK12323  523 AesiPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLP 574
PRK10927 PRK10927
cell division protein FtsN;
368-553 2.51e-03

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 43.52  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  368 PAKPPAQQTGSEKPSSEQPGPKALAQPPGVG--KTPAQQPGPAKPPTQQVGTPkpLAQQPglQSPAKAPGPTKTPVQQpg 445
Cdd:PRK10927   76 PPKPEERWRYIKELESRQPGVRAPTEPSAGGevKTPEQLTPEQRQLLEQMQAD--MRQQP--TQLVEVPWNEQTPEQR-- 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  446 pgkipaQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQP---GPAKPPPQQPGSAKP-PSQQPGSTKPPPQQPGPAKPSP 521
Cdd:PRK10927  150 ------QQTLQRQRQAQQLAEQQRLAQQSRTTEQSWQQQtrtSQAAPVQAQPRQSKPaSTQQPYQDLLQTPAHTTAQSKP 223
                         170       180       190
                  ....*....|....*....|....*....|..
gi 150170670  522 QQpgstkppsqqpgsAKPSAQQPSPAKPSAQQ 553
Cdd:PRK10927  224 QQ-------------AAPVTRAADAPKPTAEK 242
Androgen_recep pfam02166
Androgen receptor;
423-549 2.52e-03

Androgen receptor;


Pssm-ID: 426632 [Multi-domain]  Cd Length: 501  Bit Score: 44.15  E-value: 2.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   423 QQPGLQSPAKAPG--PTKTPVQQpgpgKIPAQQAGPGKTSAQQTGPTKP-----PSQLPGPAKPPPQQPGPA-------- 487
Cdd:pfam02166   30 QNPGPRHPEAAGGaaPPGARLQH----QQQQQQQVPQQPQQQESSPRQPqasvqPQQAGDDGSPPAHNRGPAgylaledd 105
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150170670   488 -KPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKP 549
Cdd:pfam02166  106 eQPQPSQAQPAAECCPENGCVPEPGAAAAAGKGLPQQAVAPAAPDDDDSAAPSTLSLLGPSFP 168
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
647-879 2.57e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.10  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  647 GGDLAPVPSSPQPKLKTAPVTTTSAVSKSSPQPQQTSPKKDAAPkqdlskapepKKPPPLVKQPTLHGSPSAKAKQPPEA 726
Cdd:PRK12323  369 GGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAA----------AAAARAVAAAPARRSPAPEALAAARQ 438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  727 DSLSKPAPPKEPsvPSEQDKAPVADDKPkqpkmvkPTTDLVSSSSATTKPDIPSSKVQSQAEEKTTPPlktdsakPSQSF 806
Cdd:PRK12323  439 ASARGPGGAPAP--APAPAAAPAAAARP-------AAAGPRPVAAAAAAAPARAAPAAAPAPADDDPP-------PWEEL 502
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150170670  807 PPTGEKVSPFDSKAIPRPAsDSKIISHPGPSseskgqkQVDPVQKKEEPKKAQTKMsPKPDAKPMPKGSPTPP 879
Cdd:PRK12323  503 PPEFASPAPAQPDAAPAGW-VAESIPDPATA-------DPDDAFETLAPAPAAAPA-PRAAAATEPVVAPRPP 566
PHA02682 PHA02682
ORF080 virion core protein; Provisional
458-581 2.57e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 43.31  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  458 KTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPP-QQPGSAKPPSQQPgSTKPPPQQPGPAKPSPQQPGSTKPPSqqPGS 536
Cdd:PHA02682   75 RPSGQSPLAPSPACAAPAPACPACAPAAPAPAVTcPAPAPACPPATAP-TCPPPAVCPAPARPAPACPPSTRQCP--PAP 151
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 150170670  537 AKPSAQQPSPAKPSAQQSTKPvsqtgsgKPLQPPTVSPSAKQPPS 581
Cdd:PHA02682  152 PLPTPKPAPAAKPIFLHNQLP-------PPDYPAASCPTIETAPA 189
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
1134-1261 2.62e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.68  E-value: 2.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  1134 ASPMPVPTESSSQKTAVPPQVKLVKKQEQEVKTEAEKVILEKVKETLSMEKIPPMVTTDQKQEESKLEKDKASAL-QEKK 1212
Cdd:TIGR02794   25 HSVKPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAaEKAA 104
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 150170670  1213 PLPEEKKLIPEEEKIRSEEKKP-LLEEKKPTPE---DKKLLPEAKTSAPEEQK 1261
Cdd:TIGR02794  105 KQAEQAAKQAEEKQKQAEEAKAkQAAEAKAKAEaeaERKAKEEAAKQAEEEAK 157
PDZ1_PTPN13-like cd23072
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
4512-4577 2.63e-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: 40.17  E-value: 2.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670 4512 GLGIRIVGGkEIPGHSgEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTY-----------EEVQSIISQ 4577
Cdd:cd23072    14 GLGFQIVGG-EKSGRL-DLGIFISSITPGGPADLDGRLKPGDRLISVNDVSLEGLSHdaaveilqnapEDVTLVVSQ 88
COG3416 COG3416
Uncharacterized conserved protein, DUF2076 domain [Function unknown];
490-549 2.73e-03

Uncharacterized conserved protein, DUF2076 domain [Function unknown];


Pssm-ID: 442642 [Multi-domain]  Cd Length: 237  Bit Score: 42.70  E-value: 2.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670  490 PPQQPGS------AKPPSQQPGStkPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKP 549
Cdd:COG3416    78 QPQSSGGflsglfGGGQRPPPAP--QPSQPGPQQQPAPPSGPWGQAAPQQPGYGQPQYGQPAAGPS 141
PHA02682 PHA02682
ORF080 virion core protein; Provisional
355-509 2.84e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 43.31  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  355 PPGTTKPPAQPLGP-------AKPPAQQTGSEKPSSEQPGPKALAQPpgVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGL 427
Cdd:PHA02682   30 PQATIPAPAAPCPPdadvdplDKYSVKEAGRYYQSRLKANSACMQRP--SGQSPLAPSPACAAPAPACPACAPAAPAPAV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  428 QSPAKAPG-PTKTPVQQPGPGKIPAqQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPG---PAKPPPQQPGSAKPPSQQ 503
Cdd:PHA02682  108 TCPAPAPAcPPATAPTCPPPAVCPA-PARPAPACPPSTRQCPPAPPLPTPKPAPAAKPIflhNQLPPPDYPAASCPTIET 186

                  ....*.
gi 150170670  504 PGSTKP 509
Cdd:PHA02682  187 APAASP 192
C2B_Synaptotagmin-13 cd08407
C2 domain second repeat present in Synaptotagmin 13; Synaptotagmin is a membrane-trafficking ...
4695-4825 2.92e-03

C2 domain second repeat present in Synaptotagmin 13; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Synaptotagmin 13, a member of class 6 synaptotagmins, is located in the brain. It functions are unknown. It, like synaptotagmins 8 and 12, does 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: 176052 [Multi-domain]  Cd Length: 138  Bit Score: 41.12  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4695 TGEIQLQINY--DLGNLIIHILQARNL-----VPRDNNGYSdpfVKVYLLPgrgqvmvvQNASAEyKRRTKHVQKSLNPE 4767
Cdd:cd08407     1 TGEVLLSISYlpAANRLLVVVIKAKNLhsdqlKLLLGIDVS---VKVTLKH--------QNAKLK-KKQTKRAKHKINPV 68
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150170670 4768 WNQTVIYKsISMEQLKKKTLEVTVWDYDRFSSNDFLGEVLIDLSST----SH----LDNtPR-----WYPL 4825
Cdd:cd08407    69 WNEMIMFE-LPSELLAASSVELEVLNQDSPGQSLPLGRCSLGLHTSgterQHweemLDN-PRrqiamWHQL 137
DUF2076 pfam09849
Uncharacterized protein conserved in bacteria (DUF2076); This domain, found in various ...
451-551 2.92e-03

Uncharacterized protein conserved in bacteria (DUF2076); This domain, found in various hypothetical prokaryotic proteins, has no known function. The domain, however, is found in various periplasmic ligand-binding sensor proteins.


Pssm-ID: 430876  Cd Length: 263  Bit Score: 42.81  E-value: 2.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   451 AQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPakPPPQQPGSAkppsqqpgstkPPPQQPGPAKPSPQQPGStkPP 530
Cdd:pfam09849   69 AQLQQLQQQQQQAQAQPSSGGFLGGLFGGGSQSRPP--PPPQARPAW-----------PAGQAPGQPQPYPGQPGY--AQ 133
                           90       100
                   ....*....|....*....|.
gi 150170670   531 SQQPGSAKPSAQQPSPAKPSA 551
Cdd:pfam09849  134 QGQPQYGQPAQPPRGPWGPGG 154
PRK14948 PRK14948
DNA polymerase III subunit gamma/tau;
331-521 3.16e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237862 [Multi-domain]  Cd Length: 620  Bit Score: 43.80  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  331 PPAQPSGLTKPLAQQPGTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPA-- 408
Cdd:PRK14948  361 PSAFISEIANASAPANPTPAPNPSPPPAPIQPSAPKTKQAATTPSPPPAKASPPIPVPAEPTEPSPTPPANAANAPPSln 440
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  409 -KPPTQQV-------GTPKPLAQQPGL----------------------------QSPAKAPG-PTKT--PVQQPGPGKI 449
Cdd:PRK14948  441 lEELWQQIlaklelpSTRMLLSQQAELvsldsnraviavspnwlgmvqsrkplleQAFAKVLGrSIKLnlESQSGSASNT 520
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150170670  450 PAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTK-PPPQQPGPAKPSP 521
Cdd:PRK14948  521 AKTPPPPQKSPPPPAPTPPLPQPTATAPPPTPPPPPPTATQASSNAPAQIPADSSPPPPiPEEPTPSPTKDSS 593
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
332-583 3.19e-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: 43.80  E-value: 3.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   332 PAQPSGLTKPLAQQPGTVKPpvQPPGTTKPPAQPLGPAKP----PAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGP 407
Cdd:pfam17823  131 PAAIAALPSEAFSAPRAAAC--RANASAAPRAAIAAASAPhaasPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTP 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   408 AKP-PTQQVGTPKPLAQQPGLQSP--AKAPGPTKTPVQQPGPGKIP--AQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQ 482
Cdd:pfam17823  209 ARGiSTAATATGHPAAGTALAAVGnsSPAAGTVTAAVGTVTPAALAtlAAAAGTVASAAGTINMGDPHARRLSPAKHMPS 288
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   483 QPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGpaKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQ---STKPVS 559
Cdd:pfam17823  289 DTMARNPAAPMGAQAQGPIIQVSTDQPVHNTAG--EPTPSPSNTTLEPNTPKSVASTNLAVVTTTKAQAKEpsaSPVPVL 366
                          250       260
                   ....*....|....*....|....*.
gi 150170670   560 QTGSGKPLQ--PPTVSPSAkQPPSQG 583
Cdd:pfam17823  367 HTSMIPEVEatSPTTQPSP-LLPTQG 391
PRK11901 PRK11901
hypothetical protein; Reviewed
406-568 3.45e-03

hypothetical protein; Reviewed


Pssm-ID: 237015 [Multi-domain]  Cd Length: 327  Bit Score: 43.13  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  406 GPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTgpTKPPsqlpgPAKPPPQQPG 485
Cdd:PRK11901   60 SPTEHESQQSSNNAGAEKNIDLSGSSSLSSGNQSSPSAANNTSDGHDASGVKNTAPPQD--ISAP-----PISPTPTQAA 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  486 PAKPPPQQ-----PG--------------SAKPPSQQPGS---TKPPPQQPGPAKPSPQQPGSTKPPSQQPGSAKPSAQQ 543
Cdd:PRK11901  133 PPQTPNGQqrielPGnisdalsqqqgqvnAASQNAQGNTStlpTAPATVAPSKGAKVPATAETHPTPPQKPATKKPAVNH 212
                         170       180
                  ....*....|....*....|....*..
gi 150170670  544 PS--PAKPSAQQSTKPVSQTGSGKPLQ 568
Cdd:PRK11901  213 HKtaTVAVPPATSGKPKSGAASARALS 239
PDZ6_PDZD2-PDZ3_hPro-IL-16-like cd06762
PDZ domain 6 of PDZ domain containing 2 (PDZD2), PDZ domain 3 of human pro-interleukin-16 ...
4506-4577 3.47e-03

PDZ domain 6 of PDZ domain containing 2 (PDZD2), PDZ domain 3 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 6 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 third PDZ domain (PDZ3) 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 PDZ6 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: 467243 [Multi-domain]  Cd Length: 86  Bit Score: 39.55  E-value: 3.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670 4506 HTVSGNGLGIRIVGG-----KEIPGHsgeigayiaKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQ 4577
Cdd:cd06762     7 HKEEGSGLGFSLAGGsdlenKSITVH---------RVFPSGLAAQEGTIQKGDRILSINGKSLKGVTHGDALSVLKQ 74
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
307-400 3.57e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 43.61  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  307 QQPTPGKPPAQQPGHEKSQPGPAKPPA--QPSGLTKPLAQQPGT---VKPPVQPPGTTKPPAQPlGPAKPPAQQTGSEKP 381
Cdd:PRK14971  390 PQPSAAAAASPSPSQSSAAAQPSAPQSatQPAGTPPTVSVDPPAavpVNPPSTAPQAVRPAQFK-EEKKIPVSKVSSLGP 468
                          90
                  ....*....|....*....
gi 150170670  382 SSEQPGPKALAQPPGVGKT 400
Cdd:PRK14971  469 STLRPIQEKAEQATGNIKE 487
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
793-1064 3.70e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 43.91  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  793 PPLKTDSAKPSQSFPPTGEKVSPFDSKAiPRPASDSKIISHPGPSSESKGQKQVDPVQKKEEPKKAQTKMSPKPDAKPMP 872
Cdd:PTZ00449  521 PKAPGDKEGEEGEHEDSKESDEPKEGGK-PGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKKPKR 599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  873 KGSPTPPGPRPTAGQtvptPQQSPKPQEQSRRFSlnlgsiTDAPKSqPTTPQETVTgklfgfgasifsqasnlistagqp 952
Cdd:PTZ00449  600 PRSAQRPTRPKSPKL----PELLDIPKSPKRPES------PKSPKR-PPPPQRPSS------------------------ 644
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  953 gPHSQSGPGAPmkQAPAPSQPPTSQGPPKSTGQAPPAPAKSIPVKKETKAPAA------EKLEPKAEQAPTVKRTETEKK 1026
Cdd:PTZ00449  645 -PERPEGPKII--KSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVldesfeSILKETLPETPGTPFTTPRPL 721
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 150170670 1027 PPPIKDSKSLTAEPQKAvlPTKLEKSPKPESTCPLCKT 1064
Cdd:PTZ00449  722 PPKLPRDEEFPFEPIGD--PDAEQPDDIEFFTPPEEER 757
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
475-530 3.89e-03

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 43.36  E-value: 3.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670  475 GPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGST--KPPPQQPGPAKPSPQQPGSTKPP 530
Cdd:PRK01297   10 GKGEAEQPAPAPPSPAAAPAPPPPAKTAAPATKaaAPAAAAPRAEKPKKDKPRRERKP 67
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
3758-3821 3.97e-03

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


Pssm-ID: 462322  Cd Length: 323  Bit Score: 42.94  E-value: 3.97e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670  3758 ARAKILQDIDRELDLVERESAKLRKKQAELDEEEKEIDaklrylEMGINRRKEALLKEREKRER 3821
Cdd:pfam07946  265 TREEEIEKIKKAAEEERAEEAQEKKEEAKKKEREEKLA------KLSPEEQRKYEEKERKKEQR 322
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1142-1309 4.37e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 43.10  E-value: 4.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1142 ESSSQKTAVPPQVKLVKKQEQEVKTEAEkvILEKVKETLSMEKIPPMVTT--------------DQKQEESKLEKDKASA 1207
Cdd:COG3064     3 EALEEKAAEAAAQERLEQAEAEKRAAAE--AEQKAKEEAEEERLAELEAKrqaeeeareakaeaEQRAAELAAEAAKKLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1208 LQEKKPLPEEKKLIPEEEKIRSEEKKPLLEEKKPTPEDKKLLPEAKTSAPEEQKHDLLKSQVQIAEEKLEGRVAPKTVQE 1287
Cdd:COG3064    81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAA 160
                         170       180
                  ....*....|....*....|..
gi 150170670 1288 GKQPQTKMEGLPSGTPQSLPKE 1309
Cdd:COG3064   161 AAAAAAAAAAAARAAAGAAAAL 182
PHA03418 PHA03418
hypothetical E4 protein; Provisional
307-486 4.56e-03

hypothetical E4 protein; Provisional


Pssm-ID: 177646 [Multi-domain]  Cd Length: 230  Bit Score: 42.03  E-value: 4.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  307 QQPTPGKPPAQQPGHEKSQPGPAKPPAQPSGLTKP-LAQQPGTvkppvqpPGTTKPPAQPLGPakppaqqTGSEKPsseQ 385
Cdd:PHA03418   40 HHPNPQEDPDKNPSPPPDPPLTPRPPAQPNGHNKPpVTKQPGG-------EGTEEDHQAPLAA-------DADDDP---R 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  386 PGPKALAQPPGvgktpaqqPGPAKpptqqvGTPKP----LAQQPGLQSPAKAPGPTKTPVQQPGPGKiPAQQAGPGKTSA 461
Cdd:PHA03418  103 PGKRSKADEHG--------PAPGR------AALAPfkldLDQDPLHGDPDPPPGATGGQGEEPPEGG-EESQPPLGEGEG 167
                         170       180
                  ....*....|....*....|....*
gi 150170670  462 QQTGPTKPPsqlpgpakPPPQQPGP 486
Cdd:PHA03418  168 AVEGHPPPL--------PPAPEPKP 184
PRK10263 PRK10263
DNA translocase FtsK; Provisional
855-1060 4.63e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.54  E-value: 4.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  855 PKKAQTKMSPKPDAKPMPKgSPT---PPGPRPTAGQTVPTPQ-QSPKPQEQSRRFSLNlgsiTDAPKSQPTTPQETVTGK 930
Cdd:PRK10263  336 PVEPVTQTPPVASVDVPPA-QPTvawQPVPGPQTGEPVIAPApEGYPQQSQYAQPAVQ----YNEPLQQPVQPQQPYYAP 410
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  931 LFGFGASIFSQASNLISTAGQPGPHSQsgPGAPMKQAPAPSQPPTSQGPPKSTGQAPPAPAKSIPVKKETKAPAAEKLEP 1010
Cdd:PRK10263  411 AAEQPAQQPYYAPAPEQPAQQPYYAPA--PEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQP 488
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670 1011 KAEQAPTVKrtETEKKPPPI-----------KDSKSLTA------EPQKAVLPTKLEKSPKPESTCP 1060
Cdd:PRK10263  489 VVEPEPVVE--ETKPARPPLyyfeeveekraREREQLAAwyqpipEPVKEPEPIKSSLKAPSVAAVP 553
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
501-584 4.71e-03

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 43.34  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  501 SQQPGSTKPPPQQPGPAKP--SPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQ 578
Cdd:PRK12270   35 DYGPGSTAAPTAAAAAAAAaaSAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVE 114

                  ....*.
gi 150170670  579 PPSQGL 584
Cdd:PRK12270  115 DEVTPL 120
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
429-597 4.71e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 43.16  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  429 SPAKAPGPTKTPVQQPGPGKIPAQQAGPGKTSAQQTGPtKPPSQlpgPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTK 508
Cdd:PRK08691  359 APLAAASCDANAVIENTELQSPSAQTAEKETAAKKPQP-RPEAE---TAQTPVQTASAAAMPSEGKTAGPVSNQENNDVP 434
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  509 PPPQQPGPAK-PSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPTVS-----------PSA 576
Cdd:PRK08691  435 PWEDAPDEAQtAAGTAQTSAKSIQTASEAETPPENQVSKNKAADNETDAPLSEVPSENPIQATPNDeavetetfaheAPA 514
                         170       180
                  ....*....|....*....|.
gi 150170670  577 KQPPSQGLPKTICPLCNTTEL 597
Cdd:PRK08691  515 EPFYGYGFPDNDCPPEDGAEI 535
C2A_RasA2_RasA3 cd08401
C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 are GAP1s (GTPase ...
4709-4826 4.86e-03

C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 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. RasA2 and RasA3 are both inositol 1,3,4,5-tetrakisphosphate-binding proteins and contain an N-terminal C2 domain, a Ras-GAP domain, a pleckstrin-homology (PH) domain which localizes it to the plasma membrane, and Bruton's Tyrosine Kinase (BTK) a 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 first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176046 [Multi-domain]  Cd Length: 121  Bit Score: 40.11  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 4709 LIIHILQARNLVPRDN-NGYSDPFVKVyllpgrgqvmvvqNASAEYKRRTKHVQKSLNPEWNQTVIYKSismeQLKKKTL 4787
Cdd:cd08401     2 LKIKIGEAKNLPPRSGpNKMRDCYCTV-------------NLDQEEVFRTKTVEKSLCPFFGEDFYFEI----PRTFRHL 64
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 150170670 4788 EVTVWDYDRFSSNDFLGEVLI---DLSSTSHLDNtprWYPLK 4826
Cdd:cd08401    65 SFYIYDRDVLRRDSVIGKVAIkkeDLHKYYGKDT---WFPLQ 103
PRK14965 PRK14965
DNA polymerase III subunits gamma and tau; Provisional
495-557 5.05e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237871 [Multi-domain]  Cd Length: 576  Bit Score: 43.19  E-value: 5.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150170670  495 GSAKPPSQQPGSTKPPPQQPGP--AKPSPQQPGSTKPPSQQPGSAKPSAQQPSPAKPSAQQSTKP 557
Cdd:PRK14965  380 GAPAPPSAAWGAPTPAAPAAPPpaAAPPVPPAAPARPAAARPAPAPAPPAAAAPPARSADPAAAA 444
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
67-447 5.06e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 5.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   67 PKGSVPPAAAESPSMHRKQELDSSHPPKQSGRPPDPGRPAQPglSKSRTTDTFRSEQKlPGRSPSTISLKESKSRTDLKE 146
Cdd:PHA03307   88 PTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPS--PAPDLSEMLRPVGS-PGPPPAASPPAAGASPAAVAS 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  147 EHKSSMMPGFLSEVnALSAVSSVVNKFNPFDLISDSEAsqeettkkqkvvqkeqgkPEGIIKPPLQQQPPKPIPKQQGPG 226
Cdd:PHA03307  165 DAASSRQAALPLSS-PEETARAPSSPPAEPPPSTPPAA------------------ASPRPPRRSSPISASASSPAPAPG 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  227 RDplQQDGTPKSISSQQPekikSQPPGTGKPIQGPTQTPQTDHAKLPLQ-RDASRPQTKQADIVRGESVKpslpspskpp 305
Cdd:PHA03307  226 RS--AADDAGASSSDSSS----SESSGCGWGPENECPLPRPAPITLPTRiWEASGWNGPSSRPGPASSSS---------- 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  306 iqqPTPGKPPAQQPGHEKSQPGPAKPPA-------QPSGLTKPLAQQPGTVKPPVQPPgttKPPAQPLGPAKPPAQQTGS 378
Cdd:PHA03307  290 ---SPRERSPSPSPSSPGSGPAPSSPRAsssssssRESSSSSTSSSSESSRGAAVSPG---PSPSRSPSPSRPPPPADPS 363
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670  379 EKPSSEQP--GPKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQP--------GLQSPAKAPGPTKTPVQQPGPG 447
Cdd:PHA03307  364 SPRKRPRPsrAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPrpspldagAASGAFYARYPLLTPSGEPWPG 442
PHA03291 PHA03291
envelope glycoprotein I; Provisional
329-486 5.33e-03

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 42.63  E-value: 5.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  329 AKPPAQPSgLTKPLAQQP------------GTVKPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPG-----PKAL 391
Cdd:PHA03291  113 TQSPAYAT-LTLDLARQPllrargaaravvGLYVLRVWVEGATNASLFPLGLAAFPAEGTLAAPPLGEGSAdgscdPALP 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  392 AQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPtktpvqqPGPGKIPAQQAGpgkTSAQQTGPTKPPS 471
Cdd:PHA03291  192 LSAPRLGPADVFVPATPRPTPRTTASPETTPTPSTTTSPPSTTIP-------APSTTIAAPQAG---TTPEAEGTPAPPT 261
                         170
                  ....*....|....*
gi 150170670  472 QLPGPAKPPPQQPGP 486
Cdd:PHA03291  262 PGGGEAPPANATPAP 276
PDZ4_LNX1_2-like cd06680
PDZ domain 4 of human Ligand of Numb protein X 1 (LNX1) and LNX2, and related domains; PDZ ...
4513-4586 5.50e-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: 38.87  E-value: 5.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670 4513 LGIRIVGGKEipGHSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGEAEICV 4586
Cdd:cd06680    13 LGFSIVGGYE--ESHGNQPFFVKSIVPGTPAYNDGRLKCGDIILAVNGVSTVGMSHAALVPLLKEQRGRVTLTV 84
PDZ_Par6-like cd06718
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ...
4513-4576 5.62e-03

PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F (RhoGAP100F), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Par6 (also known as PAR6 or Par-6), RhoGAP100F, and related domains. Par6 is part of a conserved machinery that directs metazoan cell polarity, a process necessary for the function of diverse cell types. Par6 forms a cell polarity-regulatory complex with atypical protein kinase C (aPKC) and Par3. Par6 can also directly associate with PALS1 (proteins associated with Lin7, also known as Stardust) providing a link between the Par3/aPKC/Par6 complex and the PALS1-PATJ (protein-associated TJ) complex. Binding partners of the Par6-PDZ domain include Par3, PALS1/Stardust; leucine-rich repeat-containing protein netrin-G ligand-2 (NGL-2), human crumbs (CRB3) involve in the morphogenesis of the tight junctions in mammalian epithelial cells, and PAR-6 co-operates with the Par6 semi-CRIB domain to bind CDC42. CDC42 regulates the Par6 PDZ domain through an allosteric CRIB-PDZ transition. Drosophila RhoGAP100F, also known as synapse defective protein 1 homolog (syd-1 homolog), is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound form. The RhoGAP100F-PDZ domain binds the neurexin C terminus to control synapse formation at the Drosophila neuromuscular junction. 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 Par6-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: 467202 [Multi-domain]  Cd Length: 84  Bit Score: 38.70  E-value: 5.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670 4513 LGIRIVGGKEIPGHSGeigAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIIS 4576
Cdd:cd06718    13 LGFYIRDGNGVERVPG---IFISRLVLGSLADSTGLLAVGDEILEVNGVEVTGKSLDDVTDMMV 73
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
307-432 5.62e-03

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 40.79  E-value: 5.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   307 QQPTPGKPPAQQPGHEKSQPGPAKPPAQPSGLTKPLAQQPGTVKPPVQPPGTTKP--PAQPLGPAKPPA------QQTGS 378
Cdd:pfam15240   31 LISEEEGQSQQGGQGPQGPPPGGFPPQPPASDDPPGPPPPGGPQQPPPQGGKQKPqgPPPQGGPRPPPGkpqgppPQGGN 110
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670   379 EKPSSEQPGPKALAQPPGVGKTPA---QQPGPAKPPTQQVGTPKPLAQQPGLQSPAK 432
Cdd:pfam15240  111 QQQGPPPPGKPQGPPPQGGGPPPQggnQQGPPPPPPGNPQGPPQRPPQPGNPQGPPQ 167
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
430-509 5.66e-03

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 42.22  E-value: 5.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   430 PAKAPGPTKTPVQQPGPGKIPAQQAGPGktsaqqtgPTKPPSQLPGP-AKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTK 508
Cdd:pfam07174   41 PEPAPPPPSTATAPPAPPPPPPAPAAPA--------PPPPPAAPNAPnAPPPPADPNAPPPPPADPNAPPPPAVDPNAPE 112

                   .
gi 150170670   509 P 509
Cdd:pfam07174  113 P 113
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
4497-4572 5.89e-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: 38.80  E-value: 5.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 150170670 4497 IKITRDskdhtvsGNGLGIRIVGGK-EIPGHSGEIGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTSKT-YEEVQ 4572
Cdd:cd06704     3 ITIERQ-------TGGLGISIAGGKgSTPYKGDDEGIFISRVTEGGPAAKAG-VRVGDKLLEVNGVDLVDADhHEAVE 72
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
808-1060 6.19e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.99  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  808 PTGEKVSPFDSKAIPRPASDSKIISHPGPsSESKGQKQVDPVQKKEEPKKAQTKMSPKP------DAKPMPKGSPTPPGP 881
Cdd:PLN03209  315 PMEELLAKIPSQRVPPKESDAADGPKPVP-TKPVTPEAPSPPIEEEPPQPKAVVPRPLSpytayeDLKPPTSPIPTPPSS 393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  882 RPTAGQTVPTPQQSPKPQEQSrrfslNLGSITDAPKSQPTTPQETVTGKLfgfgaSIFSQASNLiSTAGQPGPHSQSGPG 961
Cdd:PLN03209  394 SPASSKSVDAVAKPAEPDVVP-----SPGSASNVPEVEPAQVEAKKTRPL-----SPYARYEDL-KPPTSPSPTAPTGVS 462
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  962 APMKQAPAPSQPPTSQGPPKSTGQAPPAPAKSIPVkketkAPAAEKLEPKAEQAPTVKRTETEKKPPPIKD-SKSLTAEP 1040
Cdd:PLN03209  463 PSVSSTSSVPAVPDTAPATAATDAAAPPPANMRPL-----SPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEvVKVGNSAP 537
                         250       260
                  ....*....|....*....|
gi 150170670 1041 QKAVLPTKLEKSPKPESTCP 1060
Cdd:PLN03209  538 PTALADEQHHAQPKPRPLSP 557
PHA02682 PHA02682
ORF080 virion core protein; Provisional
468-594 6.51e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 42.16  E-value: 6.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  468 KPPSQLPGPAKPPPQQPGPAKPPPqqpgsaKPPSQQPGSTKPPPQQPGPAKPSPQQPgstkppsqqPGSAKPSAQQPSPA 547
Cdd:PHA02682   75 RPSGQSPLAPSPACAAPAPACPAC------APAAPAPAVTCPAPAPACPPATAPTCP---------PPAVCPAPARPAPA 139
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 150170670  548 KPSAQQSTKPVSQTGSGKPLQPPTVSPSAKQPPSQGLPKTICPLCNT 594
Cdd:PHA02682  140 CPPSTRQCPPAPPLPTPKPAPAAKPIFLHNQLPPPDYPAASCPTIET 186
PRK14965 PRK14965
DNA polymerase III subunits gamma and tau; Provisional
475-549 6.52e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237871 [Multi-domain]  Cd Length: 576  Bit Score: 42.81  E-value: 6.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150170670  475 GPAKPPPQQPGPAKPPPqqpgsakpPSQQPGSTKPPPQQPGPAKPSPQQPgstKPPSQQPGSAKPSAQQPSPAKP 549
Cdd:PRK14965  380 GAPAPPSAAWGAPTPAA--------PAAPPPAAAPPVPPAAPARPAAARP---APAPAPPAAAAPPARSADPAAA 443
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
4506-4571 6.52e-03

PDZ domain 2 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 2 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 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: 467220 [Multi-domain]  Cd Length: 82  Bit Score: 38.46  E-value: 6.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670 4506 HTVSGNGLGIRIVGGkeiPGHSGeiGAYIAKILPGGSAEQTGkLMEGMQVLEWNGIPLTSKTYEEV 4571
Cdd:cd06738     8 SLVGTRGLGCSISSG---PTQKP--GIFISNVKPGSLAEEVG-LEVGDQIVEVNGTSFTNVDHKEA 67
PRK14965 PRK14965
DNA polymerase III subunits gamma and tau; Provisional
452-526 6.69e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237871 [Multi-domain]  Cd Length: 576  Bit Score: 42.81  E-value: 6.69e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670  452 QQAGPGKTSAQQTGPTKPPSQLPGPA-KPPPQQPGPAKPPPQQPGSAKPPSQQPgstkPPPQQPGPAKPSPQQPGS 526
Cdd:PRK14965  378 ERGAPAPPSAAWGAPTPAAPAAPPPAaAPPVPPAAPARPAAARPAPAPAPPAAA----APPARSADPAAAASAGDR 449
PRK10263 PRK10263
DNA translocase FtsK; Provisional
3844-4002 6.70e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.15  E-value: 6.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 3844 PTRIESQHGIERPRTAPQTEFSQFIPPQTQTESQLVPPTSPYTQYQYSSPALPTQAPTSYTQQSHFEQQTlYHQQVSPYQ 3923
Cdd:PRK10263  747 PIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQ-YQQPQQPVA 825
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 150170670 3924 TQPTFQavatmsfTPQVQPTPTPQPSYQLPSQMMVIQQKPRQTTLYLEPKItsnyEVIRNQPLMIAPVstdNTFAVSHL 4002
Cdd:PRK10263  826 PQPQYQ-------QPQQPVAPQPQDTLLHPLLMRNGDSRPLHKPTTPLPSL----DLLTPPPSEVEPV---DTFALEQM 890
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
382-500 7.26e-03

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


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 40.54  E-value: 7.26e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670    382 SSEQPGPKALAQPPGVGKTPAQQPGpakPPTQqvgtpkPLAQQPGLQSpakapgptKTPVQQPGPGKIPAQQAGPGKTSA 461
Cdd:smart00818   43 SQQHPPTHTLQPHHHIPVLPAQQPV---VPQQ------PLMPVPGQHS--------MTPTQHHQPNLPQPAQQPFQPQPL 105
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 150170670    462 QQTGPTKPPSQLPGPAKPPPQQPGPAKPP--PQQPGSAKPP 500
Cdd:smart00818  106 QPPQPQQPMQPQPPVHPIPPLPPQPPLPPmfPMQPLPPLLP 146
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
942-1007 7.29e-03

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 42.96  E-value: 7.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150170670  942 ASNLISTAGQPGPHSQSGPGAPMKQAPAPSQPPTSQGPPKSTGQAPPAPAKSIPVKKETKAPAAEK 1007
Cdd:PRK12270   46 AAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAA 111
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
361-546 7.38e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 42.77  E-value: 7.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  361 PPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPgvgktpaqQPGPAKPPTQqvgTPKPLAQQPGLQSPAKAPGPTKTP 440
Cdd:PRK08691  360 PLAAASCDANAVIENTELQSPSAQTAEKETAAKKP--------QPRPEAETAQ---TPVQTASAAAMPSEGKTAGPVSNQ 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  441 VQQPGPgkipaqqagPGKTSAQQTGPTKPPSQLPgpAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPS 520
Cdd:PRK08691  429 ENNDVP---------PWEDAPDEAQTAAGTAQTS--AKSIQTASEAETPPENQVSKNKAADNETDAPLSEVPSENPIQAT 497
                         170       180
                  ....*....|....*....|....*.
gi 150170670  521 PQQPGSTKPPSQQPGSAKPSAQQPSP 546
Cdd:PRK08691  498 PNDEAVETETFAHEAPAEPFYGYGFP 523
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
4509-4580 7.48e-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: 7.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150170670 4509 SGNGLGIRIVGGKEipghSGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIIsQQSG 4580
Cdd:cd06735     9 GPKGFGFSIRGGRE----YNNMPLYVLRLAEDGPAQRDGRLRVGDQILEINGESTQGMTHAQAIELI-RSGG 75
Jun pfam03957
Jun-like transcription factor;
364-454 7.64e-03

Jun-like transcription factor;


Pssm-ID: 461108 [Multi-domain]  Cd Length: 231  Bit Score: 41.44  E-value: 7.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   364 QPLGPAKPPAQQTGSekPSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQQPGLQSPAKAPGPTKTPVQQ 443
Cdd:pfam03957  125 QNQLPGATPAPQALA--AGGGGSGPGALAAGGIATEPPVYANLSSFNPAAAPASGAAPAQPPQPVSYAAEPPPFAVPVQH 202
                           90
                   ....*....|.
gi 150170670   444 PGPGKIPAQQA 454
Cdd:pfam03957  203 PPPGRPPRLQA 213
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
447-510 7.85e-03

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 42.21  E-value: 7.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150170670  447 GKIPAQQAGPGKTSAQQTGPTKPPsqlpgpAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTKPP 510
Cdd:PRK01297   10 GKGEAEQPAPAPPSPAAAPAPPPP------AKTAAPATKAAAPAAAAPRAEKPKKDKPRRERKP 67
PRK14965 PRK14965
DNA polymerase III subunits gamma and tau; Provisional
505-583 8.13e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237871 [Multi-domain]  Cd Length: 576  Bit Score: 42.42  E-value: 8.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  505 GSTKPPPQQPGPAKPSPQQ--PGSTKPPSQQPGSAKPSAQQPSPAKPSAQqstkpvsqtgsgkPLQPPTVSPSAKQPPSQ 582
Cdd:PRK14965  380 GAPAPPSAAWGAPTPAAPAapPPAAAPPVPPAAPARPAAARPAPAPAPPA-------------AAAPPARSADPAAAASA 446

                  .
gi 150170670  583 G 583
Cdd:PRK14965  447 G 447
PRK12757 PRK12757
cell division protein FtsN; Provisional
469-565 8.14e-03

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 41.57  E-value: 8.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  469 PPSQLPGPA--KPPPQQPGPAKPPPQQPGSAKPPSQQpgsTKPPPQQPGPAKPSPQQPGSTKPPSQQPgsAKPSAQQPSP 546
Cdd:PRK12757   98 QPTQLSEVPynEQTPQVPRSTVQIQQQAQQQQPPATT---AQPQPVTPPRQTTAPVQPQTPAPVRTQP--AAPVTQAVEA 172
                          90       100
                  ....*....|....*....|.
gi 150170670  547 AKPSAQQST--KPVSQTGSGK 565
Cdd:PRK12757  173 PKVEAEKEKeqRWMVQCGSFK 193
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
789-1044 8.17e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 8.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  789 EKTTPPLKTDSAKPSQSFPPTGEKVSPFDSKAIPRPASDSKIISH---PGPSSESKGQKQVDPVQKKEEPKKAQTKM--- 862
Cdd:PHA03307   49 ELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLStlaPASPAREGSPTPPGPSSPDPPPPTPPPASppp 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  863 SPKPDAKPMPKGSPTPPGPRPTAGQTVPTPQQSPKPQEQSRRFSLNLGSITDAPKSQPTTPQETVTGKLFGFGASIFSQA 942
Cdd:PHA03307  129 SPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPR 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  943 SNLISTAGQPGPHSQSGPGAPMKQAPAPSQPPTSQGPPKSTGQ--APPAPAKSIPVKKETKAPAAEKLEPKAEQAPTVKR 1020
Cdd:PHA03307  209 RSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPenECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSS 288
                         250       260
                  ....*....|....*....|....*..
gi 150170670 1021 T---ETEKKPPPIKDSKSLTAEPQKAV 1044
Cdd:PHA03307  289 SsprERSPSPSPSSPGSGPAPSSPRAS 315
HC2 pfam07382
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ...
370-560 8.23e-03

Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.


Pssm-ID: 369339 [Multi-domain]  Cd Length: 187  Bit Score: 40.92  E-value: 8.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   370 KPPAQQTGSEKPSSEQPGPKALAqppgVGKTPAQQPGPAKPPTQQVGTPKPLA-QQPGLQSPAKAPGPTKTPVQQPGPGK 448
Cdd:pfam07382    7 KRSSKKTAAKKAAVRKPAAKKAA----AKKTVVRKVAAKKPAARKTVAKKTVAaKKPAAKKAAKKAVAKKVVAKKPVAKK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670   449 IPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQPGSAKPPSQQPGSTkppPQQPGPAKPSPQQPGStk 528
Cdd:pfam07382   83 AVAKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAKKAAST---CHKNHKHTAACKRVAS-- 157
                          170       180       190
                   ....*....|....*....|....*....|..
gi 150170670   529 PPSQQPGSAKPSAQQPSPAKPsaQQSTKPVSQ 560
Cdd:pfam07382  158 SSATRAACGSKSRVNPAHGWR--QQLMKLVSR 187
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
400-580 8.45e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 42.39  E-value: 8.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  400 TPAQQPG-PAKPPTQQVGTPKPLAQQPGLQSPAKAPGP------TKTPVQQPGPGKIPAQQAGPGKTSAQQTGPTKPPSQ 472
Cdd:PRK08691  359 APLAAAScDANAVIENTELQSPSAQTAEKETAAKKPQPrpeaetAQTPVQTASAAAMPSEGKTAGPVSNQENNDVPPWED 438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  473 LPGPAkpppqqpgpAKPPPQQPGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGS--TKPPSQQPGSAKPSAQQPSPAKPS 550
Cdd:PRK08691  439 APDEA---------QTAAGTAQTSAKSIQTASEAETPPENQVSKNKAADNETDAplSEVPSENPIQATPNDEAVETETFA 509
                         170       180       190
                  ....*....|....*....|....*....|
gi 150170670  551 AQQSTKPvsQTGSGKPLQPPTVSPSAKQPP 580
Cdd:PRK08691  510 HEAPAEP--FYGYGFPDNDCPPEDGAEIPP 537
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
835-1065 8.76e-03

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.45  E-value: 8.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  835 GPSSESKGQKQVDPVQKKEEPKKAQTKMSPKPDAKPMPKGSPTPPgPRPTAGQTVPTPQ--------------QSPKPQE 900
Cdd:NF033839  146 DSSSSSSSGSSTKPETPQPENPEHQKPTTPAPDTKPSPQPEGKKP-SVPDINQEKEKAKlavatymskilddiQKHHLQK 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  901 QSRRFSLNLGSITDAPKSQPTTPQETV---------TGKLFGFGASIFSQASNLIS--TAGQPGPHSQSGPGAPMKQAPA 969
Cdd:NF033839  225 EKHRQIVALIKELDELKKQALSEIDNVntkveientVHKIFADMDAVVTKFKKGLTqdTPKEPGNKKPSAPKPGMQPSPQ 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  970 PSQPPTSQGPPKSTGQAPPAPAKSIPVKK---ETKAPA--AEKLEPKAEQAPTVKRTETEKKPPPIKDSKSLTAEPQKAv 1044
Cdd:NF033839  305 PEKKEVKPEPETPKPEVKPQLEKPKPEVKpqpEKPKPEvkPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETP- 383
                         250       260
                  ....*....|....*....|.
gi 150170670 1045 lptKLEKSPKPESTCPLCKTE 1065
Cdd:NF033839  384 ---KPEVKPQPEKPKPEVKPQ 401
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
645-997 8.82e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.53  E-value: 8.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  645 ALGGDLAPVPSSPQPKLKTAPVTTTSAVSKSSPQPQQTSPKKDAAPKQDLSKAPEPKKppplvkqptlhgSPSAKAKQPP 724
Cdd:PRK07003  367 APGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAE------------APPAAPAPPA 434
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  725 EADSLSKPApPKEPSVPSEQDkAPVADDKPKQPKMVKPTTDLVSSSSATtkPDIPSSkVQSQAEEKTTPPLKTDSAKPSQ 804
Cdd:PRK07003  435 TADRGDDAA-DGDAPVPAKAN-ARASADSRCDERDAQPPADSGSASAPA--SDAPPD-AAFEPAPRAAAPSAATPAAVPD 509
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  805 SFPPTGEK--------VSPFDSKAIPRPASDSKIISHPGPSS-----ESKGQKqVDPVQKKEEPKKAQTKMSPKPDAKPM 871
Cdd:PRK07003  510 ARAPAAASredapaaaAPPAPEARPPTPAAAAPAARAGGAAAaldvlRNAGMR-VSSDRGARAAAAAKPAAAPAAAPKPA 588
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  872 PkgsPTPPGPRPTAGQTVPTPQQSPKPQEQSRRFSLNLGSI---TDAPKSQ--PTTPQETVTGKLFGFgASIFSQASNLI 946
Cdd:PRK07003  589 A---PRVAVQVPTPRARAATGDAPPNGAARAEQAAESRGAPppwEDIPPDDyvPLSADEGFGGPDDGF-VPVFDSGPDDV 664
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 150170670  947 STAGQPGPHsqsgPGAPMKQAPAPsqPPTSQGPPKSTGQApPAPAKSIPVK 997
Cdd:PRK07003  665 RVAPKPADA----PAPPVDTRPLP--PAIPLDAIGFDGEW-PALAARLPLK 708
PHA03247 PHA03247
large tegument protein UL36; Provisional
446-603 8.99e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 8.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  446 PGKIPAQQAGPGKTSAQQTGPTKPPsqlpgpAKPPPQQP-GPAKPPPQQPGSA--KPPSQQPGSTKPPPQQPGPAK---- 518
Cdd:PHA03247  255 PAPPPVVGEGADRAPETARGATGPP------PPPEAAAPnGAAAPPDGVWGAAlaGAPLALPAPPDPPPPAPAGDAeeed 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  519 ------------PSPQQ-----------PGSTKPPSQQPGSA----KPSAQQPSPAKPSAQQSTKPVSQtGSGKPLQPPT 571
Cdd:PHA03247  329 dedgamevvsplPRPRQhyplgfpkrrrPTWTPPSSLEDLSAgrhhPKRASLPTRKRRSARHAATPFAR-GPGGDDQTRP 407
                         170       180       190
                  ....*....|....*....|....*....|..
gi 150170670  572 VSPSAKQPPSQGLPKTICPLCNTTELLLHVPE 603
Cdd:PHA03247  408 AAPVPASVPTPAPTPVPASAPPPPATPLPSAE 439
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
668-883 9.01e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 42.73  E-value: 9.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  668 TTSAVSKSSPQPQQ----TSPKKDAAPKQDLSKAPEPKKPPPLVKQPTLHGSPSAKAKQPPEADSLSKPAPPKEPSVPSE 743
Cdd:PTZ00108 1161 KTKGKASKLRKPKLkkkeKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSV 1240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  744 QDKAPVADDKPKQPKMVKPTTDLVSSSSATTKPDIPSSkvqsQAEEKTTPPLKTDSAKPSQsfppTGEKVSPFDSKAIPR 823
Cdd:PTZ00108 1241 KRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRV----SAVQYSPPPPSKRPDGESN----GGSKPSSPTKKKVKK 1312
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  824 PasdskiishpgpssesKGQKQVDPVQKKEEPKKAQTKMSPKPDAKPMPKGSPTPPGPRP 883
Cdd:PTZ00108 1313 R----------------LEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRP 1356
PRK11633 PRK11633
cell division protein DedD; Provisional
341-454 9.10e-03

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 41.14  E-value: 9.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  341 PLAQQPGTVKPP-VQPPGTTKPPAQPLGPAKPpAQQTGSEKPSSEQPgpKALAQPPGvgkTPAQQPGP-AKPPTQQVGTP 418
Cdd:PRK11633   42 PLVPKPGDRDEPdMMPAATQALPTQPPEGAAE-AVRAGDAAAPSLDP--ATVAPPNT---PVEPEPAPvEPPKPKPVEKP 115
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 150170670  419 KPLAQQPGLQSPAKAPGPTKTPVQQPGPGkiPAQQA 454
Cdd:PRK11633  116 KPKPKPQQKVEAPPAPKPEPKPVVEEKAA--PTGKA 149
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
4512-4586 9.17e-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: 38.10  E-value: 9.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150170670 4512 GLGIRIVGGKeipghsGEIGAYIAKILPGGSAEQTGKLMEGMQVLEWNGIPLTSKTYEEVQSIISQQSGEAEICV 4586
Cdd:cd23060    11 GLGFSLVGGE------GGSGIFVKSISPGGVADRDGRLQVGDRLLQVNGESVIGLSHSKAVNILRKAKGTVQLTV 79
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1142-1322 9.18e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 42.33  E-value: 9.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1142 ESSSQKTAVPPQVKLVKKQEQEVKTEAEKVILEKVKEtlsmekippmvttdqkQEESKLEKDKASALQEKKPLPEEKKLI 1221
Cdd:COG3064    38 EAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAE----------------AAKKLAEAEKAAAEAEKKAAAEKAKAA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670 1222 PEEEKIRSEEKKPLLEEKKPTPEDKKLLPEAKTSAPEEQKHDLLKSQVQIAEEKLEGRVAPKTVQEGKQPQTKMEGLPSG 1301
Cdd:COG3064   102 KEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAA 181
                         170       180
                  ....*....|....*....|.
gi 150170670 1302 TPQSLPKEDDKTTKTIKEQPQ 1322
Cdd:COG3064   182 LVAAAAAAVEAADTAAAAAAA 202
PHA02682 PHA02682
ORF080 virion core protein; Provisional
498-600 9.35e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 41.39  E-value: 9.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  498 KPPSQQPGSTKPPPQQPGPAKPSPqqpgstKPPSQQPGSAKPSaqqPSPAKPSAQQSTKPVSQTGSGKPLQPPTVSPSAK 577
Cdd:PHA02682   75 RPSGQSPLAPSPACAAPAPACPAC------APAAPAPAVTCPA---PAPACPPATAPTCPPPAVCPAPARPAPACPPSTR 145
                          90       100
                  ....*....|....*....|....
gi 150170670  578 Q-PPSQGLPkTICPLCNTTELLLH 600
Cdd:PHA02682  146 QcPPAPPLP-TPKPAPAAKPIFLH 168
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
360-472 9.39e-03

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 42.21  E-value: 9.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  360 KPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAQPPGVGKTPAQQPGPAKPPTQQVGTPKPLAQ---------------- 423
Cdd:PRK01297   11 KGEAEQPAPAPPSPAAAPAPPPPAKTAAPATKAAAPAAAAPRAEKPKKDKPRRERKPKPASLWKledfvvepqegktrfh 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670  424 ----QPGLQSPAKAPG-PTKTPVQQ-------PGPGKIPAQQAGPGKTSA------QQTGPTKPPSQ 472
Cdd:PRK01297   91 dfnlAPELMHAIHDLGfPYCTPIQAqvlgytlAGHDAIGRAQTGTGKTAAflisiiNQLLQTPPPKE 157
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
350-440 9.62e-03

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 42.57  E-value: 9.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  350 KPPVQPPGTTKPPAQPLGPAKPPAQQTGSEKPSSEQPGPKALAqppgvgktPAQQPGPAKPPTQQVGTPKPLAQQPGLQS 429
Cdd:PRK12270   37 GPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAA--------PAAPPKPAAAAAAAAAPAAPPAAAAAAAP 108
                          90
                  ....*....|.
gi 150170670  430 PAKAPGPTKTP 440
Cdd:PRK12270  109 AAAAVEDEVTP 119
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
447-583 9.71e-03

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 41.86  E-value: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  447 GKIPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQpgSAKPPSQqpGSTKPPPQQPGPAKPSPQQPGS 526
Cdd:PTZ00436  213 GKKSAKAAAPAKAAAAPAKAAAPPAKAAAAPAKAAAAPAKAAAPPAK--AAAPPAK--AAAPPAKAAAPPAKAAAPPAKA 288
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 150170670  527 TKPPSQQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGkPLQPPTVSPSAKQPPSQG 583
Cdd:PTZ00436  289 AAPPAKAAAAPAKAAAAPAKAAAAPAKAAAPPAKAAAP-PAKAATPPAKAAAPPAKA 344
FimV COG3170
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];
353-584 9.98e-03

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


Pssm-ID: 442403 [Multi-domain]  Cd Length: 508  Bit Score: 42.09  E-value: 9.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  353 VQPPGTTKPPAQPLG-----PAKPPAQQTGSEKPSSEQPGPKALAQPP-----GVGKTPAQQPGPAKPPTQQVGTPKPLA 422
Cdd:COG3170   104 LDPPAYAAAAAAPAAapapaPAAPAAAAAAADQPAAEAAPAASGEYYPvrpgdTLWSIAARPVRPSSGVSLDQMMVALYR 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  423 QQPG---------LQSPAKAPGPTKTPVQQPGPGKiPAQQAGPGKTSAQQTGPTKPPSQLPGPAKPPPQQPGPAKPPPQQ 493
Cdd:COG3170   184 ANPDafidgninrLKAGAVLRVPAAEEVAALSPAE-ARQEVQAQSADWAAYRARLAAAVEPAPAAAAPAAPPAAAAAAGP 262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150170670  494 PGSAKPPSQQPGSTKPPPQQPGPAKPSPQQPGSTKPPS--QQPGSAKPSAQQPSPAKPSAQQSTKPVSQTGSGKPLQPPT 571
Cdd:COG3170   263 VPAAAEDTLSPEVTAAAAAEEADALPEAAAELAERLAAleAQLAELQRLLALKNPAPAAAVSAPAAAAAAATVEAAAPAA 342
                         250
                  ....*....|...
gi 150170670  572 VSPSAKQPPSQGL 584
Cdd:COG3170   343 AAQPAAAAPAPAL 355
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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