|
Name |
Accession |
Description |
Interval |
E-value |
| glycerol3P_DH |
TIGR03376 |
glycerol-3-phosphate dehydrogenase (NAD(+)); Members of this protein family are the eukaryotic ... |
6-312 |
2.53e-100 |
|
glycerol-3-phosphate dehydrogenase (NAD(+)); Members of this protein family are the eukaryotic enzyme, glycerol-3-phosphate dehydrogenase (NAD(+)) (EC 1.1.1.8). Enzymatic activity for 1.1.1.8 is defined as sn-glycerol 3-phosphate + NAD(+) = glycerone phosphate + NADH. Note the very similar reactions of enzymes defined as EC 1.1.1.94 and 1.1.99.5, assigned to families of proteins in the bacteria.
Pssm-ID: 274551 [Multi-domain] Cd Length: 342 Bit Score: 323.14 E-value: 2.53e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 6 KICIIGAEGWGSAIAAVVSNNVLE--GDFDSRVHLYVYDEMIRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDLLEAA 83
Cdd:TIGR03376 1 RVAVVGSGNWGTAIAKIVAENARAlpELFEESVRMWVFEEEIEGRNLTEIINTTHENVKYLPGIKLPANLVAVPDLVEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 84 QNADILVFSTPLEFVQSYCNILSGNVKESAFAVSMTKGLlSENGEGIELVSHAISESLGIPCYSMMSAHSAMEMAQGKLC 163
Cdd:TIGR03376 81 KGADILVFVIPHQFLEGICKQLKGHVKPNARAISCIKGL-EVSKDGVKLLSDIIEEELGIPCGVLSGANLANEVAKEKFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 164 EVTIGCSDNS----HSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEIMRF 239
Cdd:TIGR03376 160 ETTVGYRDPAdfdvDARVLKALFHRPYFRVNVVDDVAGVEIAGALKNVVAIAAGFVDGLGWGDNAKAAVMRRGLLEMIKF 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281362270 240 IKTFFPSSKMSTFYESCGVTNAVASSFVDKNVTFAKSLVTSGQTIEEIEANLHSGRKLLGPMVASNVNAFLEN 312
Cdd:TIGR03376 240 ARMFFPTGEVTFTFESCGVADLITTCLGGRNFKVGRAFAKTGKSLEELEKELLNGQSLQGVATAKEVHELLKN 312
|
|
| PTZ00345 |
PTZ00345 |
glycerol-3-phosphate dehydrogenase; Provisional |
1-318 |
3.08e-89 |
|
glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 240373 [Multi-domain] Cd Length: 365 Bit Score: 293.46 E-value: 3.08e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 1 MAGKLKICIIGAEGWGSAIAAVVSNNVLEGD-FDSRVHLYVYDEMIRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDL 79
Cdd:PTZ00345 8 RCGPLKVSVIGSGNWGSAISKVVGENTQRNYiFHNEVRMWVLEEIVEGEKLSDIINTKHENVKYLPGIKLPDNIVAVSDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 80 LEAAQNADILVFSTPLEFVQSYCNIL--SGNVKESAFAVSMTKGLLSENGEgIELVSHAISESLGIPCYSMMSAHSAMEM 157
Cdd:PTZ00345 88 KEAVEDADLLIFVIPHQFLESVLSQIkeNNNLKKHARAISLTKGIIVENGK-PVLCSDVIEEELGIPCCALSGANVANDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 158 AQGKLCEVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEIM 237
Cdd:PTZ00345 167 AREEFSEATIGCEDKDDALIWQRLFDRPYFKINCVPDVIGVEVCGALKNIIALAAGFCDGLGLGTNTKSAIIRIGLEEMK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 238 RFIKTFFPSSKMSTFYESCGVTNAVASSFVDKNVTFAKSLVTSG--QTIEEIEANLHSGRKLLGPMVASNVNAFLENGLM 315
Cdd:PTZ00345 247 LFGKIFFPNVMDETFFESCGLADLITTCLGGRNVRCAAEFAKRNgkKSWEEIEAELLNGQKLQGTVTLKEVYEVLESHDL 326
|
...
gi 281362270 316 QHD 318
Cdd:PTZ00345 327 KKE 329
|
|
| GpsA |
COG0240 |
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ... |
6-303 |
7.98e-50 |
|
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440010 [Multi-domain] Cd Length: 327 Bit Score: 179.85 E-value: 7.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 6 KICIIGAEGWGSAIAAVVSNNvlegdfDSRVHLYVydemiRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDLLEAAQN 85
Cdd:COG0240 2 KIAVLGAGSWGTALAKVLARN------GHEVTLWG-----RDPEVAEEINETRENPRYLPGVKLPENLRATSDLEEALAG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 86 ADILVFSTPLEFVQSYCNILSGNVKESAFAVSMTKGLlsENGEGiELVSHAISESLGI---------PCYsmmsahsAME 156
Cdd:COG0240 71 ADLVLLAVPSQALREVLEQLAPLLPPGAPVVSATKGI--EPGTG-LLMSEVIAEELPGalriavlsgPSF-------AEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 157 MAQGKLCEVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEI 236
Cdd:COG0240 141 VARGLPTAVVVASEDEEVAERLQELLSTPYFRVYTSDDVIGVELGGALKNVIAIAAGIADGLGLGDNARAALITRGLAEM 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281362270 237 MRFIKTFfpSSKMSTFYESCG-----VTnavASSFVDKNVTFAKSLVtSGQTIEEIEANLHsgrkllgpMVA 303
Cdd:COG0240 221 TRLGVAL--GARPETFMGLAGlgdlvLT---CTSDLSRNRRFGLALG-KGKSLEEALAEMG--------MVA 278
|
|
| NAD_Gly3P_dh_N |
pfam01210 |
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ... |
6-174 |
1.18e-37 |
|
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. This family represents the N-terminal NAD-binding domain.
Pssm-ID: 395967 [Multi-domain] Cd Length: 158 Bit Score: 138.86 E-value: 1.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 6 KICIIGAEGWGSAIAAVVSNNvlegdfDSRVHLYVYDEmirdtALSEIINTRHENVKYLPGIKLPNNLIAVNDLLEAAQN 85
Cdd:pfam01210 1 KIAVLGAGSWGTALAKVLADN------GHEVRLWGRDE-----ELIEEINTTHENVRYLPGIKLPENLKATTDLAEALKG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 86 ADILVFSTPLEFVQSYCNILSGNVKESAFAVSMTKGLlsENGeGIELVSHAISESLGI--PCYSMMSAHSAMEMAQGKLC 163
Cdd:pfam01210 70 ADIIVIVVPSQALREVLKQLKGLLKPDAILVSLSKGI--EPG-TLKLLSEVIEEELGIqpPIAVLSGPSHAEEVAQGLPT 146
|
170
....*....|.
gi 281362270 164 EVTIGCSDNSH 174
Cdd:pfam01210 147 ATVIASKDEEA 157
|
|
| PRK13729 |
PRK13729 |
conjugal transfer pilus assembly protein TraB; Provisional |
901-1140 |
1.37e-04 |
|
conjugal transfer pilus assembly protein TraB; Provisional
Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 45.97 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 901 QDKLQNLNYQLKEaLQHDLDVMSASRGNDSN--EVLSEEDSN-PEAAKKITEQPLNPTPNQIPAVPLPVTMPskqshirE 977
Cdd:PRK13729 75 QVTAAQMQKQYEE-IRRELDVLNKQRGDDQRriEKLGQDNAAlAEQVKALGANPVTATGEPVPQMPASPPGP-------E 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 978 GSPQFQNQPRSVPPPSPQTKPqspkeqqprrtnAPVEF--GNkdeAMDLNESASDQEVPKRKKISKTEAVIEPVAKDVSM 1055
Cdd:PRK13729 147 GEPQPGNTPVSFPPQGSVAVP------------PPTAFypGN---GVTPPPQVTYQSVPVPNRIQRKTFTYNEGKKGPSL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 1056 ----------------AEPNESLHSKKETSPASLskqeskRKQKRsLRRPSS---DSDSTKTTNE----FEKQRQIIENQ 1112
Cdd:PRK13729 212 pyipsgsfakamliegADANASVTGNESTVPMQL------RITGL-VEMPNSktyDATGCFVGLEawgdVSSERAIVRTR 284
|
250 260
....*....|....*....|....*...
gi 281362270 1113 KAQLEKMGKKISVMRQGQdrrVSYKGHN 1140
Cdd:PRK13729 285 NISCLKNGKTIDMPIKGH---VSFRGKN 309
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
947-1006 |
2.27e-04 |
|
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: 43.24 E-value: 2.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 947 ITEQPLNPTPNQIPAVPLPVTMPSKQSHIRegsPQFQNQPRSVPPPSPQTKPQSPKEQQP 1006
Cdd:smart00818 68 VPQQPLMPVPGQHSMTPTQHHQPNLPQPAQ---QPFQPQPLQPPQPQQPMQPQPPVHPIP 124
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
527-717 |
2.64e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 527 SKQNSQLMEDAETNFTERLKVNQLKEQIDKQEAaNFKAQENLIKSIRQTI----QALGDKEKMENLIA--KSKMEEDPFQ 600
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKNLDNTRESLET-QLKVLSRSINKIKQNLeqkqKELKSKEKELKKLNeeKKELEEKVKD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 601 LKSQVesSQLKSQVEGESSElKNQIQEEayepISQADEEPSQIRSQLDEEsaQLKSLMDEENRQLESEMQDESSLLKSSA 680
Cdd:TIGR04523 515 LTKKI--SSLKEKIEKLESE-KKEKESK----ISDLEDELNKDDFELKKE--NLEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
170 180 190
....*....|....*....|....*....|....*..
gi 281362270 681 DKSEFVAYNAEEEQPIEEPTDNHQYKLRSDTNKLKEL 717
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
420-769 |
3.08e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 420 QAAQLYNDIRDGNVGVAFKMDIDEGNRQVRLLLEKEDE---MASDAALTVISSRLTAGQEDDNARIGHGHITNTSAESDH 496
Cdd:pfam02463 610 KATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGlrkGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 497 MSSKSIPSGLTTKDSPDVLDLSCESEPLHSSKQNSQLMEDAETNFTERLKVNQLKEQIDKQEAANFK------------A 564
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRlkkeekeeekseL 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 565 QENLIKSIRQTIQALGDKEKMENLIAKSKMEEDPFQLKSQVESSQLKSQVEGESSELKNQIQEEAYEPISQADEEpSQIR 644
Cdd:pfam02463 770 SLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKE-EQKL 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 645 SQLDEESAQLKSLMDEENRQLESEMQDESSLLKSsaDKSEFVAYNAEEEQPIEEPTDNHQYKLRSDTNKLKELMFTDSRE 724
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQ--KLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEE 926
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 281362270 725 HLESEKHIEVKLqDEHDFDLDEEPAIGKKDPTYTKENLELQERLE 769
Cdd:pfam02463 927 AEILLKYEEEPE-ELLLEEADEKEKEENNKEEEEERNKRLLLAKE 970
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
450-939 |
6.56e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 450 LLLEKEDEMASDAALTVISSRLTAGQEDDNARIGHGHITNTSAESDHMSSKSIPSGLTTKDSPDVLDLSCEsepLHSSKQ 529
Cdd:COG5022 862 SLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIAR---LKKLLN 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 530 NSQLMEDAETNFTERLKVNQLKEQIDKQEAANFKaQENLIKSIRQTI-QALGDKEKMENLiaKSKMEEDPFQLKSQVESS 608
Cdd:COG5022 939 NIDLEEGPSIEYVKLPELNKLHEVESKLKETSEE-YEDLLKKSTILVrEGNKANSELKNF--KKELAELSKQYGALQEST 1015
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 609 QLKSQVEGESSELKNqiqeeAYEPISQADEEpSQIRSQLDEesaqLKSLMDEENRQLESEMQDeSSLLKSSADKSEFVAY 688
Cdd:COG5022 1016 KQLKELPVEVAELQS-----ASKIISSESTE-LSILKPLQK----LKGLLLLENNQLQARYKA-LKLRRENSLLDDKQLY 1084
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 689 NAeEEQPIEEPTDNHQYKLRSDTNKLKELMFTD--------SREHLESEKHIEVKLQDEHDFDLDEEPAigKKDPTYTKE 760
Cdd:COG5022 1085 QL-ESTENLLKTINVKDLEVTNRNLVKPANVLQfivaqmikLNLLQEISKFLSQLVNTLEPVFQKLSVL--QLELDGLFW 1161
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 761 NLELQERLEWQKLKQTDKphhpysSADLEDSTTNEGNARLPIEHDNRFQNVDR--YQDRELVQVRAELKetsgaESEKEI 838
Cdd:COG5022 1162 EANLEALPSPPPFAALSE------KRLYQSALYDEKSKLSSSEVNDLKNELIAlfSKIFSGWPRGDKLK-----KLISEG 1230
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 839 NLISEQRPDQNqDEVNLrphSHIKTEETGHHEWDWLMNNEKIDSDEQKFYANERMETLseSDQDKLQNLNYQLKEALQHD 918
Cdd:COG5022 1231 WVPTEYSTSLK-GFNNL---NKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPA--TINSLLQYINVGLFNALRTK 1304
|
490 500
....*....|....*....|.
gi 281362270 919 LDVMSASRGNDSNEVLSEEDS 939
Cdd:COG5022 1305 ASSLRWKSATEVNYNSEELDD 1325
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
544-913 |
7.43e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 544 RLKVNQLKEQIDKQEaanfkaqENLIKSIRQTIQALGDKEKMenliaKSKMEEDPFQLKSQVESSQLKSQVEGESSELKn 623
Cdd:pfam05483 267 RDKANQLEEKTKLQD-------ENLKELIEKKDHLTKELEDI-----KMSLQRSMSTQKALEEDLQIATKTICQLTEEK- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 624 qiqEEAYEPISQADEEPSQIRSQLDEESAQLKSLMDEENRQLESEmQDESSLL-----KSSADKSEFVAYNAEEEQPIEE 698
Cdd:pfam05483 334 ---EAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN-EDQLKIItmelqKKSSELEEMTKFKNNKEVELEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 699 PTD--NHQYKLRSDTNKLKELMFTDSREHLESEKHIEVKLQDEHDFDLdEEPAIGKKDPTYTKENLELQERLEWQKLKQT 776
Cdd:pfam05483 410 LKKilAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEI-QLTAIKTSEEHYLKEVEDLKTELEKEKLKNI 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 777 DKPHHPySSADLEDSTTNEGNARLPIEHDNRFQNVDRYQDRElvqvRAELKETSGAEsEKEINLISE-----QRPDQNQD 851
Cdd:pfam05483 489 ELTAHC-DKLLLENKELTQEASDMTLELKKHQEDIINCKKQE----ERMLKQIENLE-EKEMNLRDElesvrEEFIQKGD 562
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281362270 852 EVNLRPHshiKTEETGHHEWDWLMNNEKIDSDEQKFYANERMETLSESDQ-DKLQNLNYQLKE 913
Cdd:pfam05483 563 EVKCKLD---KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNiEELHQENKALKK 622
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
544-776 |
7.56e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 544 RLKVNQLKEQIDKQEAANFKAQENLIKSIRQTIQALGDKEKMENLIAKSKMEEDpfQLKSQVESSQLKSQVEGESSELKN 623
Cdd:COG4372 58 REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE--ELQEELEELQKERQDLEQQRKQLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 624 QIQEEAYEPISQADEEPSQIRSQLDEESAQLKSLMDEENRQLESEMQDESSLLKSSADKSEFVAYNAEEEQPIEEPTDNH 703
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281362270 704 QYKLRSDTNKLKELmfTDSREHLESEKHIEVKLQDEHDFDLDEEPAIGKKDPTYTKENLELQERLEWQKLKQT 776
Cdd:COG4372 216 LAEELLEAKDSLEA--KLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
566-707 |
9.93e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 566 ENLIKSIRQTIQalGDKEKMENLIAKS-----KMEEDPF---QLKSQVEssQLKSQVEGESSELKNQIQEEayepISQAD 637
Cdd:PRK00409 501 ENIIEEAKKLIG--EDKEKLNELIASLeelerELEQKAEeaeALLKEAE--KLKEELEEKKEKLQEEEDKL----LEEAE 572
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281362270 638 EEPSQIRSQLDEESAQ----LKSLMDEENRQL-ESEMQDESSLLKSsadksefvAYNAEEEQPIEEPTDNHQYKL 707
Cdd:PRK00409 573 KEAQQAIKEAKKEADEiikeLRQLQKGGYASVkAHELIEARKRLNK--------ANEKKEKKKKKQKEKQEELKV 639
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| glycerol3P_DH |
TIGR03376 |
glycerol-3-phosphate dehydrogenase (NAD(+)); Members of this protein family are the eukaryotic ... |
6-312 |
2.53e-100 |
|
glycerol-3-phosphate dehydrogenase (NAD(+)); Members of this protein family are the eukaryotic enzyme, glycerol-3-phosphate dehydrogenase (NAD(+)) (EC 1.1.1.8). Enzymatic activity for 1.1.1.8 is defined as sn-glycerol 3-phosphate + NAD(+) = glycerone phosphate + NADH. Note the very similar reactions of enzymes defined as EC 1.1.1.94 and 1.1.99.5, assigned to families of proteins in the bacteria.
Pssm-ID: 274551 [Multi-domain] Cd Length: 342 Bit Score: 323.14 E-value: 2.53e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 6 KICIIGAEGWGSAIAAVVSNNVLE--GDFDSRVHLYVYDEMIRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDLLEAA 83
Cdd:TIGR03376 1 RVAVVGSGNWGTAIAKIVAENARAlpELFEESVRMWVFEEEIEGRNLTEIINTTHENVKYLPGIKLPANLVAVPDLVEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 84 QNADILVFSTPLEFVQSYCNILSGNVKESAFAVSMTKGLlSENGEGIELVSHAISESLGIPCYSMMSAHSAMEMAQGKLC 163
Cdd:TIGR03376 81 KGADILVFVIPHQFLEGICKQLKGHVKPNARAISCIKGL-EVSKDGVKLLSDIIEEELGIPCGVLSGANLANEVAKEKFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 164 EVTIGCSDNS----HSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEIMRF 239
Cdd:TIGR03376 160 ETTVGYRDPAdfdvDARVLKALFHRPYFRVNVVDDVAGVEIAGALKNVVAIAAGFVDGLGWGDNAKAAVMRRGLLEMIKF 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281362270 240 IKTFFPSSKMSTFYESCGVTNAVASSFVDKNVTFAKSLVTSGQTIEEIEANLHSGRKLLGPMVASNVNAFLEN 312
Cdd:TIGR03376 240 ARMFFPTGEVTFTFESCGVADLITTCLGGRNFKVGRAFAKTGKSLEELEKELLNGQSLQGVATAKEVHELLKN 312
|
|
| PTZ00345 |
PTZ00345 |
glycerol-3-phosphate dehydrogenase; Provisional |
1-318 |
3.08e-89 |
|
glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 240373 [Multi-domain] Cd Length: 365 Bit Score: 293.46 E-value: 3.08e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 1 MAGKLKICIIGAEGWGSAIAAVVSNNVLEGD-FDSRVHLYVYDEMIRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDL 79
Cdd:PTZ00345 8 RCGPLKVSVIGSGNWGSAISKVVGENTQRNYiFHNEVRMWVLEEIVEGEKLSDIINTKHENVKYLPGIKLPDNIVAVSDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 80 LEAAQNADILVFSTPLEFVQSYCNIL--SGNVKESAFAVSMTKGLLSENGEgIELVSHAISESLGIPCYSMMSAHSAMEM 157
Cdd:PTZ00345 88 KEAVEDADLLIFVIPHQFLESVLSQIkeNNNLKKHARAISLTKGIIVENGK-PVLCSDVIEEELGIPCCALSGANVANDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 158 AQGKLCEVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEIM 237
Cdd:PTZ00345 167 AREEFSEATIGCEDKDDALIWQRLFDRPYFKINCVPDVIGVEVCGALKNIIALAAGFCDGLGLGTNTKSAIIRIGLEEMK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 238 RFIKTFFPSSKMSTFYESCGVTNAVASSFVDKNVTFAKSLVTSG--QTIEEIEANLHSGRKLLGPMVASNVNAFLENGLM 315
Cdd:PTZ00345 247 LFGKIFFPNVMDETFFESCGLADLITTCLGGRNVRCAAEFAKRNgkKSWEEIEAELLNGQKLQGTVTLKEVYEVLESHDL 326
|
...
gi 281362270 316 QHD 318
Cdd:PTZ00345 327 KKE 329
|
|
| GpsA |
COG0240 |
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ... |
6-303 |
7.98e-50 |
|
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440010 [Multi-domain] Cd Length: 327 Bit Score: 179.85 E-value: 7.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 6 KICIIGAEGWGSAIAAVVSNNvlegdfDSRVHLYVydemiRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDLLEAAQN 85
Cdd:COG0240 2 KIAVLGAGSWGTALAKVLARN------GHEVTLWG-----RDPEVAEEINETRENPRYLPGVKLPENLRATSDLEEALAG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 86 ADILVFSTPLEFVQSYCNILSGNVKESAFAVSMTKGLlsENGEGiELVSHAISESLGI---------PCYsmmsahsAME 156
Cdd:COG0240 71 ADLVLLAVPSQALREVLEQLAPLLPPGAPVVSATKGI--EPGTG-LLMSEVIAEELPGalriavlsgPSF-------AEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 157 MAQGKLCEVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEI 236
Cdd:COG0240 141 VARGLPTAVVVASEDEEVAERLQELLSTPYFRVYTSDDVIGVELGGALKNVIAIAAGIADGLGLGDNARAALITRGLAEM 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281362270 237 MRFIKTFfpSSKMSTFYESCG-----VTnavASSFVDKNVTFAKSLVtSGQTIEEIEANLHsgrkllgpMVA 303
Cdd:COG0240 221 TRLGVAL--GARPETFMGLAGlgdlvLT---CTSDLSRNRRFGLALG-KGKSLEEALAEMG--------MVA 278
|
|
| gpsA |
PRK00094 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; |
6-291 |
2.95e-41 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
Pssm-ID: 234629 [Multi-domain] Cd Length: 325 Bit Score: 154.84 E-value: 2.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 6 KICIIGAEGWGSAIAAVVSNNvlegdfDSRVHLYVydemiRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDLLEAAQN 85
Cdd:PRK00094 3 KIAVLGAGSWGTALAIVLARN------GHDVTLWA-----RDPEQAAEINADRENPRYLPGIKLPDNLRATTDLAEALAD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 86 ADILVFSTPLEFVQSYCNILSGNVKESAFAVSMTKGLlsENGEGiELVSHAISESLGIPC-YSMMSAHS-AMEMAQGKLC 163
Cdd:PRK00094 72 ADLILVAVPSQALREVLKQLKPLLPPDAPIVWATKGI--EPGTG-KLLSEVLEEELPDLApIAVLSGPSfAKEVARGLPT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 164 EVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEIMRFIKTF 243
Cdd:PRK00094 149 AVVIASTDEELAERVQELFHSPYFRVYTNTDVIGVELGGALKNVIAIAAGIADGLGLGDNARAALITRGLAEITRLGVAL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 281362270 244 fpSSKMSTFYESCG-----VTnavASSFVDKNVTFAKSLVtSGQTIEEIEANL 291
Cdd:PRK00094 229 --GANPETFLGLAGlgdlvLT---CTSPLSRNRRFGLALG-QGKSLEEALAEI 275
|
|
| NAD_Gly3P_dh_N |
pfam01210 |
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ... |
6-174 |
1.18e-37 |
|
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. This family represents the N-terminal NAD-binding domain.
Pssm-ID: 395967 [Multi-domain] Cd Length: 158 Bit Score: 138.86 E-value: 1.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 6 KICIIGAEGWGSAIAAVVSNNvlegdfDSRVHLYVYDEmirdtALSEIINTRHENVKYLPGIKLPNNLIAVNDLLEAAQN 85
Cdd:pfam01210 1 KIAVLGAGSWGTALAKVLADN------GHEVRLWGRDE-----ELIEEINTTHENVRYLPGIKLPENLKATTDLAEALKG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 86 ADILVFSTPLEFVQSYCNILSGNVKESAFAVSMTKGLlsENGeGIELVSHAISESLGI--PCYSMMSAHSAMEMAQGKLC 163
Cdd:pfam01210 70 ADIIVIVVPSQALREVLKQLKGLLKPDAILVSLSKGI--EPG-TLKLLSEVIEEELGIqpPIAVLSGPSHAEEVAQGLPT 146
|
170
....*....|.
gi 281362270 164 EVTIGCSDNSH 174
Cdd:pfam01210 147 ATVIASKDEEA 157
|
|
| NAD_Gly3P_dh_C |
pfam07479 |
NAD-dependent glycerol-3-phosphate dehydrogenase C-terminus; NAD-dependent ... |
194-327 |
8.76e-32 |
|
NAD-dependent glycerol-3-phosphate dehydrogenase C-terminus; NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. This family represents the C-terminal substrate-binding domain.
Pssm-ID: 462178 [Multi-domain] Cd Length: 142 Bit Score: 121.34 E-value: 8.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 194 DVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEIMRFIKTFFpsSKMSTFYESCGVTNAVASSFVDK--NV 271
Cdd:pfam07479 1 DVIGVELGGALKNVIAIAAGIADGLGLGDNAKAALITRGLAEMIRLGKALG--AKPETFFGLAGLGDLIVTCTSGLsrNR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281362270 272 TFAKSLVTsGQTIEEIEANLhsGRKLLGPMVASNVNAFLENGLMQ-----------HDEAPPELMIE 327
Cdd:pfam07479 79 RFGEALGK-GKSLEEAEKEL--GQVAEGVYTAKAVYELAKKLGVEmpifeavyrilYEGKSPEEALE 142
|
|
| PRK14618 |
PRK14618 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
1-289 |
3.07e-25 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 237770 [Multi-domain] Cd Length: 328 Bit Score: 108.42 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 1 MAGKLKICIIGAEGWGSAIAAVVSNNvlegdfDSRVHLYVydemiRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDLL 80
Cdd:PRK14618 1 MHHGMRVAVLGAGAWGTALAVLAASK------GVPVRLWA-----RRPEFAAALAAERENREYLPGVALPAELYPTADPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 81 EAAQNADILVFSTPLEFVQsycNILSGNVKESAFaVSMTKGLlSENGEGIELVSHAISESLGIPCYSMMSAHSAMEMAQG 160
Cdd:PRK14618 70 EALAGADFAVVAVPSKALR---ETLAGLPRALGY-VSCAKGL-APDGGRLSELARVLEFLTQARVAVLSGPNHAEEIARF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 161 KLCEVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEIMRFI 240
Cdd:PRK14618 145 LPAATVVASPEPGLARRVQAAFSGPSFRVYTSRDRVGVELGGALKNVIALAAGMVDGLKLGDNAKAALITRGLREMVRFG 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 281362270 241 KTFfpSSKMSTFYESCGVTN--AVASSFVDKNVTFAKSLVtSGQTIEEIEA 289
Cdd:PRK14618 225 VAL--GAEEATFYGLSGLGDliATATSPHSRNRAAGEAIV-RGVDREHLEA 272
|
|
| PRK12439 |
PRK12439 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
1-238 |
2.11e-24 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 171500 [Multi-domain] Cd Length: 341 Bit Score: 106.02 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 1 MAGKLKICIIGAEGWGSAIAAVVSNNvlegdfdSRVHLYVydemiRDTALSEIINTRHENVKYLP-GIKLPNNLIAVNDL 79
Cdd:PRK12439 4 AKREPKVVVLGGGSWGTTVASICARR-------GPTLQWV-----RSAETADDINDNHRNSRYLGnDVVLSDTLRATTDF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 80 LEAAQNADILVFSTPLEFVQSYCNILSGNVKESAFAVSMTKGLlsENGEGIELvSHAISESL-GIPCYSMMSAHSAMEMA 158
Cdd:PRK12439 72 AEAANCADVVVMGVPSHGFRGVLTELAKELRPWVPVVSLVKGL--EQGTNMRM-SQIIEEVLpGHPAGILAGPNIAREVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 159 QGKLCEVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEIMR 238
Cdd:PRK12439 149 EGYAAAAVLAMPDQHLATRLSPLFRTRRFRVYTTDDVVGVEMAGALKNVFAIAVGMGYSLGIGENTRAMVIARALREMTK 228
|
|
| PRK14620 |
PRK14620 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
5-236 |
3.15e-21 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173083 [Multi-domain] Cd Length: 326 Bit Score: 96.44 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 5 LKICIIGAEGWGSAIAAVVSNNvlegdfDSRVHLYVydemiRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDLLEA-A 83
Cdd:PRK14620 1 MKISILGAGSFGTAIAIALSSK------KISVNLWG-----RNHTTFESINTKRKNLKYLPTCHLPDNISVKSAIDEVlS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 84 QNADILVFSTPLEFVQSYC-NILSGNVKESAFAVSMTKGLlsENGEgIELVSHAISESL-GIPCYSMMSAHSAMEMAQGK 161
Cdd:PRK14620 70 DNATCIILAVPTQQLRTICqQLQDCHLKKNTPILICSKGI--EKSS-LKFPSEIVNEILpNNPIAILSGPSFAKEIAEKL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281362270 162 LCEVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEI 236
Cdd:PRK14620 147 PCSIVLAGQNETLGSSLISKLSNENLKIIYSQDIIGVQIGAALKNIIAIACGIVLGKNLGNNAHAAVITKGMNEI 221
|
|
| PRK14619 |
PRK14619 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
1-293 |
2.50e-10 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 237771 [Multi-domain] Cd Length: 308 Bit Score: 63.08 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 1 MAGKLKICIIGAEGWGSAIAAVVSNNvlegdfDSRVHLYvydemirdtalseiinTRHENvkylpgiklpnnliavNDLL 80
Cdd:PRK14619 1 TTQPKTIAILGAGAWGSTLAGLASAN------GHRVRVW----------------SRRSG----------------LSLA 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 81 EAAQNADILVFSTPLEFVQSYCNILSG-NVKESAFAVSMTKGLLSENGegieLVSHAISESLgIPCYSM--MSAHS-AME 156
Cdd:PRK14619 43 AVLADADVIVSAVSMKGVRPVAEQVQAlNLPPETIIVTATKGLDPETT----RTPSQIWQAA-FPNHPVvvLSGPNlSKE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 157 MAQGKLCEVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEI 236
Cdd:PRK14619 118 IQQGLPAATVVASRDLAAAETVQQIFSSERFRVYTNSDPLGTELGGTLKNVIAIAAGVCDGLQLGTNAKAALVTRALPEM 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 281362270 237 MRfIKTFFpSSKMSTFYESCGVTN--AVASSFVDKNVTFAKSLvTSGQTIEEIEANLHS 293
Cdd:PRK14619 198 IR-VGTHL-GAQTETFYGLSGLGDllATCTSPLSRNYQVGYGL-AQGKSLEQILAELEG 253
|
|
| PRK13729 |
PRK13729 |
conjugal transfer pilus assembly protein TraB; Provisional |
901-1140 |
1.37e-04 |
|
conjugal transfer pilus assembly protein TraB; Provisional
Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 45.97 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 901 QDKLQNLNYQLKEaLQHDLDVMSASRGNDSN--EVLSEEDSN-PEAAKKITEQPLNPTPNQIPAVPLPVTMPskqshirE 977
Cdd:PRK13729 75 QVTAAQMQKQYEE-IRRELDVLNKQRGDDQRriEKLGQDNAAlAEQVKALGANPVTATGEPVPQMPASPPGP-------E 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 978 GSPQFQNQPRSVPPPSPQTKPqspkeqqprrtnAPVEF--GNkdeAMDLNESASDQEVPKRKKISKTEAVIEPVAKDVSM 1055
Cdd:PRK13729 147 GEPQPGNTPVSFPPQGSVAVP------------PPTAFypGN---GVTPPPQVTYQSVPVPNRIQRKTFTYNEGKKGPSL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 1056 ----------------AEPNESLHSKKETSPASLskqeskRKQKRsLRRPSS---DSDSTKTTNE----FEKQRQIIENQ 1112
Cdd:PRK13729 212 pyipsgsfakamliegADANASVTGNESTVPMQL------RITGL-VEMPNSktyDATGCFVGLEawgdVSSERAIVRTR 284
|
250 260
....*....|....*....|....*...
gi 281362270 1113 KAQLEKMGKKISVMRQGQdrrVSYKGHN 1140
Cdd:PRK13729 285 NISCLKNGKTIDMPIKGH---VSFRGKN 309
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
875-1092 |
1.55e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 46.23 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 875 MNNEKIDSDEQKFYANERMETLSESD---QDKL-----QNLNYQLKEALQHDLDVMSASRGNDSNEVLSEEDSNPEAAKK 946
Cdd:PRK10263 632 AAEEKAREAQRNQYDSGDQYNDDEIDamqQDELarqfaQTQQQRYGEQYQHDVPVNAEDADAAAEAELARQFAQTQQQRY 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 947 ITEQPLNPTP---------------NQIPAVPL--PVTMPSKQ-SHIREGSPQFQNQPRSVPPPSPQTKPQSPKEQQPRR 1008
Cdd:PRK10263 712 SGEQPAGANPfslddfefspmkallDDGPHEPLftPIVEPVQQpQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQY 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 1009 TNAPVEFGNKDEAMDLNESASDQEVPKRKKiskteaviEPVAKDVSMAEPNESLHSKKETS---PASLSKQESKRKQKRS 1085
Cdd:PRK10263 792 QQPQQPVAPQPQYQQPQQPVAPQPQYQQPQ--------QPVAPQPQYQQPQQPVAPQPQDTllhPLLMRNGDSRPLHKPT 863
|
....*..
gi 281362270 1086 LRRPSSD 1092
Cdd:PRK10263 864 TPLPSLD 870
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
947-1006 |
2.27e-04 |
|
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: 43.24 E-value: 2.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 947 ITEQPLNPTPNQIPAVPLPVTMPSKQSHIRegsPQFQNQPRSVPPPSPQTKPQSPKEQQP 1006
Cdd:smart00818 68 VPQQPLMPVPGQHSMTPTQHHQPNLPQPAQ---QPFQPQPLQPPQPQQPMQPQPPVHPIP 124
|
|
| PTZ00441 |
PTZ00441 |
sporozoite surface protein 2 (SSP2); Provisional |
900-1124 |
2.76e-04 |
|
sporozoite surface protein 2 (SSP2); Provisional
Pssm-ID: 240420 [Multi-domain] Cd Length: 576 Bit Score: 45.34 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 900 DQDKLQNLNYQLKEALQHDLDVMSASRGNDSNEVlsEEDSNPEAAKKITEQPLNPtpnqipavPLPVTMPSKQSHIREGS 979
Cdd:PTZ00441 309 DEFAVPNFNEGLDVPDNPQDPVPPPNEGKDGNPN--EENLFPPGDDEVPDESNVP--------PNPPNVPGGSNSEFSSD 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 980 PQFQNQprsvpPPSPQTKPQSPKEQQPRRTNAPVEFgNKDEAMDLNESASDQEVPKRKKISKTEAVI-EPVAKDVSMAEP 1058
Cdd:PTZ00441 379 VENPPN-----PPNPDIPEQEPNIPEDSNKEVPEDV-PMEPEDDRDNNFNEPKKPENKGDGQNEPVIpKPLDNERDQSNK 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281362270 1059 NESLH-SKKETSPASLSKQESKRKQKRSLRRPSSDSDSTKTTNEFEKQrqiiENQKAQLEKMGKKIS 1124
Cdd:PTZ00441 453 NKQVNpGNRHNSEDRYTRPHGRNNENRNYNNKNSDIPKHPERSEHEQP----EDKKKKSSNNGYKIA 515
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
527-717 |
2.64e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 527 SKQNSQLMEDAETNFTERLKVNQLKEQIDKQEAaNFKAQENLIKSIRQTI----QALGDKEKMENLIA--KSKMEEDPFQ 600
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKNLDNTRESLET-QLKVLSRSINKIKQNLeqkqKELKSKEKELKKLNeeKKELEEKVKD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 601 LKSQVesSQLKSQVEGESSElKNQIQEEayepISQADEEPSQIRSQLDEEsaQLKSLMDEENRQLESEMQDESSLLKSSA 680
Cdd:TIGR04523 515 LTKKI--SSLKEKIEKLESE-KKEKESK----ISDLEDELNKDDFELKKE--NLEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
170 180 190
....*....|....*....|....*....|....*..
gi 281362270 681 DKSEFVAYNAEEEQPIEEPTDNHQYKLRSDTNKLKEL 717
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
420-769 |
3.08e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 420 QAAQLYNDIRDGNVGVAFKMDIDEGNRQVRLLLEKEDE---MASDAALTVISSRLTAGQEDDNARIGHGHITNTSAESDH 496
Cdd:pfam02463 610 KATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGlrkGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 497 MSSKSIPSGLTTKDSPDVLDLSCESEPLHSSKQNSQLMEDAETNFTERLKVNQLKEQIDKQEAANFK------------A 564
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRlkkeekeeekseL 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 565 QENLIKSIRQTIQALGDKEKMENLIAKSKMEEDPFQLKSQVESSQLKSQVEGESSELKNQIQEEAYEPISQADEEpSQIR 644
Cdd:pfam02463 770 SLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKE-EQKL 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 645 SQLDEESAQLKSLMDEENRQLESEMQDESSLLKSsaDKSEFVAYNAEEEQPIEEPTDNHQYKLRSDTNKLKELMFTDSRE 724
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQ--KLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEE 926
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 281362270 725 HLESEKHIEVKLqDEHDFDLDEEPAIGKKDPTYTKENLELQERLE 769
Cdd:pfam02463 927 AEILLKYEEEPE-ELLLEEADEKEKEENNKEEEEERNKRLLLAKE 970
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
950-1001 |
3.41e-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: 39.77 E-value: 3.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 281362270 950 QPLNPTPNQIPAVPLPVTMPSKQSHIREGSPQFQNQPRSVPPPSPQTKPQSP 1001
Cdd:smart00818 80 HSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMQPQPPVHPIPPLPPQPP 131
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
544-769 |
4.93e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 544 RLKVNQLKEQIDKQEAanfkaqenLIKSIRQTIQAL-GDKEKMENL--IAKSKMEEDPFQLKSQVESSQL-KSQVEGESS 619
Cdd:TIGR02169 176 LEELEEVEENIERLDL--------IIDEKRQQLERLrREREKAERYqaLLKEKREYEGYELLKEKEALERqKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 620 ELKNQIqEEAYEPISQADEEPSQIRSQLDEESAQLKSLMDEENRQLESEMQDESSLLKSSADKSEFvaynAEEEQpieEP 699
Cdd:TIGR02169 248 SLEEEL-EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAE----KEREL---ED 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281362270 700 TDNHQYKLRSDTNKLKELMfTDSREHLESEKHIEVKLQDEHDFDLDEE-------PAIGKKDPTYTKENLELQERLE 769
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEI-EELEREIEEERKRRDKLTEEYAELKEELedlraelEEVDKEFAETRDELKDYREKLE 395
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
543-950 |
5.70e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 543 ERLKVNQLK--EQIDKQEAANFKAQEnLIKSIRQTIQALGDKEKMENLiaKSKMEEdpfqlKSQVESSQLKSQVEGESSE 620
Cdd:PTZ00121 1364 EKAEAAEKKkeEAKKKADAAKKKAEE-KKKADEAKKKAEEDKKKADEL--KKAAAA-----KKKADEAKKKAEEKKKADE 1435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 621 LKNQIQE--EAYEPISQADE----EPSQIRSQLDEESAQLKSLMDEENRQLESEMQDESSLLKS-SADKSEFVAYNAEEE 693
Cdd:PTZ00121 1436 AKKKAEEakKADEAKKKAEEakkaEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdEAKKAAEAKKKADEA 1515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 694 QPIEEPTDNHQYKLRSDTNKLKELMFTDSREHLESEKHIEvKLQDEHDFDLDEEPAIGKKDPTYTKENLELQERLEWQKL 773
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 774 KQTDKPHHPYSSADLEDSTTNEgNARLPIEHDNRFQNVDRYQDRELVQVRAELKETSGAESEKEINLISEQRPDQNQDEv 853
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAE-EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE- 1672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 854 nlrphSHIKTEETGHHEWDWLMNNEKIDSDEQKFYANERMETLSESDQDKLQNLNyqlKEALQHDLDVMSASRGNDSNEV 933
Cdd:PTZ00121 1673 -----DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELK---KAEEENKIKAEEAKKEAEEDKK 1744
|
410
....*....|....*..
gi 281362270 934 LSEEDSNPEAAKKITEQ 950
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAH 1761
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
450-939 |
6.56e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 450 LLLEKEDEMASDAALTVISSRLTAGQEDDNARIGHGHITNTSAESDHMSSKSIPSGLTTKDSPDVLDLSCEsepLHSSKQ 529
Cdd:COG5022 862 SLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIAR---LKKLLN 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 530 NSQLMEDAETNFTERLKVNQLKEQIDKQEAANFKaQENLIKSIRQTI-QALGDKEKMENLiaKSKMEEDPFQLKSQVESS 608
Cdd:COG5022 939 NIDLEEGPSIEYVKLPELNKLHEVESKLKETSEE-YEDLLKKSTILVrEGNKANSELKNF--KKELAELSKQYGALQEST 1015
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 609 QLKSQVEGESSELKNqiqeeAYEPISQADEEpSQIRSQLDEesaqLKSLMDEENRQLESEMQDeSSLLKSSADKSEFVAY 688
Cdd:COG5022 1016 KQLKELPVEVAELQS-----ASKIISSESTE-LSILKPLQK----LKGLLLLENNQLQARYKA-LKLRRENSLLDDKQLY 1084
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 689 NAeEEQPIEEPTDNHQYKLRSDTNKLKELMFTD--------SREHLESEKHIEVKLQDEHDFDLDEEPAigKKDPTYTKE 760
Cdd:COG5022 1085 QL-ESTENLLKTINVKDLEVTNRNLVKPANVLQfivaqmikLNLLQEISKFLSQLVNTLEPVFQKLSVL--QLELDGLFW 1161
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 761 NLELQERLEWQKLKQTDKphhpysSADLEDSTTNEGNARLPIEHDNRFQNVDR--YQDRELVQVRAELKetsgaESEKEI 838
Cdd:COG5022 1162 EANLEALPSPPPFAALSE------KRLYQSALYDEKSKLSSSEVNDLKNELIAlfSKIFSGWPRGDKLK-----KLISEG 1230
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 839 NLISEQRPDQNqDEVNLrphSHIKTEETGHHEWDWLMNNEKIDSDEQKFYANERMETLseSDQDKLQNLNYQLKEALQHD 918
Cdd:COG5022 1231 WVPTEYSTSLK-GFNNL---NKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPA--TINSLLQYINVGLFNALRTK 1304
|
490 500
....*....|....*....|.
gi 281362270 919 LDVMSASRGNDSNEVLSEEDS 939
Cdd:COG5022 1305 ASSLRWKSATEVNYNSEELDD 1325
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
544-913 |
7.43e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 544 RLKVNQLKEQIDKQEaanfkaqENLIKSIRQTIQALGDKEKMenliaKSKMEEDPFQLKSQVESSQLKSQVEGESSELKn 623
Cdd:pfam05483 267 RDKANQLEEKTKLQD-------ENLKELIEKKDHLTKELEDI-----KMSLQRSMSTQKALEEDLQIATKTICQLTEEK- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 624 qiqEEAYEPISQADEEPSQIRSQLDEESAQLKSLMDEENRQLESEmQDESSLL-----KSSADKSEFVAYNAEEEQPIEE 698
Cdd:pfam05483 334 ---EAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN-EDQLKIItmelqKKSSELEEMTKFKNNKEVELEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 699 PTD--NHQYKLRSDTNKLKELMFTDSREHLESEKHIEVKLQDEHDFDLdEEPAIGKKDPTYTKENLELQERLEWQKLKQT 776
Cdd:pfam05483 410 LKKilAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEI-QLTAIKTSEEHYLKEVEDLKTELEKEKLKNI 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 777 DKPHHPySSADLEDSTTNEGNARLPIEHDNRFQNVDRYQDRElvqvRAELKETSGAEsEKEINLISE-----QRPDQNQD 851
Cdd:pfam05483 489 ELTAHC-DKLLLENKELTQEASDMTLELKKHQEDIINCKKQE----ERMLKQIENLE-EKEMNLRDElesvrEEFIQKGD 562
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281362270 852 EVNLRPHshiKTEETGHHEWDWLMNNEKIDSDEQKFYANERMETLSESDQ-DKLQNLNYQLKE 913
Cdd:pfam05483 563 EVKCKLD---KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNiEELHQENKALKK 622
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
544-776 |
7.56e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 544 RLKVNQLKEQIDKQEAANFKAQENLIKSIRQTIQALGDKEKMENLIAKSKMEEDpfQLKSQVESSQLKSQVEGESSELKN 623
Cdd:COG4372 58 REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE--ELQEELEELQKERQDLEQQRKQLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 624 QIQEEAYEPISQADEEPSQIRSQLDEESAQLKSLMDEENRQLESEMQDESSLLKSSADKSEFVAYNAEEEQPIEEPTDNH 703
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281362270 704 QYKLRSDTNKLKELmfTDSREHLESEKHIEVKLQDEHDFDLDEEPAIGKKDPTYTKENLELQERLEWQKLKQT 776
Cdd:COG4372 216 LAEELLEAKDSLEA--KLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
566-707 |
9.93e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362270 566 ENLIKSIRQTIQalGDKEKMENLIAKS-----KMEEDPF---QLKSQVEssQLKSQVEGESSELKNQIQEEayepISQAD 637
Cdd:PRK00409 501 ENIIEEAKKLIG--EDKEKLNELIASLeelerELEQKAEeaeALLKEAE--KLKEELEEKKEKLQEEEDKL----LEEAE 572
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281362270 638 EEPSQIRSQLDEESAQ----LKSLMDEENRQL-ESEMQDESSLLKSsadksefvAYNAEEEQPIEEPTDNHQYKL 707
Cdd:PRK00409 573 KEAQQAIKEAKKEADEiikeLRQLQKGGYASVkAHELIEARKRLNK--------ANEKKEKKKKKQKEKQEELKV 639
|
|
| |
