|
Name |
Accession |
Description |
Interval |
E-value |
| glycerol3P_DH |
TIGR03376 |
glycerol-3-phosphate dehydrogenase (NAD(+)); Members of this protein family are the eukaryotic ... |
6-342 |
7.87e-110 |
|
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: 349.33 E-value: 7.87e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 6 KICIIGAEGWGSAIAAVVSNNVLE--GDFDSRVHLYVYDEMIRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDLLEAA 83
Cdd:TIGR03376 1 RVAVVGSGNWGTAIAKIVAENARAlpELFEESVRMWVFEEEIEGRNLTEIINTTHENVKYLPGIKLPANLVAVPDLVEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 84 QNADILVFSTPLEFVQSYCNILSGNVKESAFAVSMTKGLlSENGEGIELVSHAISESLGIPCYSMMSAHSAMEMAQGKLC 163
Cdd:TIGR03376 81 KGADILVFVIPHQFLEGICKQLKGHVKPNARAISCIKGL-EVSKDGVKLLSDIIEEELGIPCGVLSGANLANEVAKEKFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 164 EVTIGCSDNS----HSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEIMRF 239
Cdd:TIGR03376 160 ETTVGYRDPAdfdvDARVLKALFHRPYFRVNVVDDVAGVEIAGALKNVVAIAAGFVDGLGWGDNAKAAVMRRGLLEMIKF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 240 IKTFFPSSKMSTFYESCGVTNAVASSFVDKNVTFAKSLVTSGQTIEEIEANLHSGRKLLGPMVASNVNAFLENGLMQHEF 319
Cdd:TIGR03376 240 ARMFFPTGEVTFTFESCGVADLITTCLGGRNFKVGRAFAKTGKSLEELEKELLNGQSLQGVATAKEVHELLKNKNKDDEF 319
|
330 340
....*....|....*....|...
gi 386766242 320 PLFTAIHLICQSEAPPELMIEAL 342
Cdd:TIGR03376 320 PLFEAVYQILYEGLPPKKLPECL 342
|
|
| PTZ00345 |
PTZ00345 |
glycerol-3-phosphate dehydrogenase; Provisional |
1-344 |
1.13e-97 |
|
glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 240373 [Multi-domain] Cd Length: 365 Bit Score: 316.96 E-value: 1.13e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 1 MAGKLKICIIGAEGWGSAIAAVVSNNVLEGD-FDSRVHLYVYDEMIRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDL 79
Cdd:PTZ00345 8 RCGPLKVSVIGSGNWGSAISKVVGENTQRNYiFHNEVRMWVLEEIVEGEKLSDIINTKHENVKYLPGIKLPDNIVAVSDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 80 LEAAQNADILVFSTPLEFVQSYCNIL--SGNVKESAFAVSMTKGLLSENGEgIELVSHAISESLGIPCYSMMSAHSAMEM 157
Cdd:PTZ00345 88 KEAVEDADLLIFVIPHQFLESVLSQIkeNNNLKKHARAISLTKGIIVENGK-PVLCSDVIEEELGIPCCALSGANVANDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 158 AQGKLCEVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEIM 237
Cdd:PTZ00345 167 AREEFSEATIGCEDKDDALIWQRLFDRPYFKINCVPDVIGVEVCGALKNIIALAAGFCDGLGLGTNTKSAIIRIGLEEMK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 238 RFIKTFFPSSKMSTFYESCGVTNAVASSFVDKNVTFAKSLVTSG--QTIEEIEANLHSGRKLLGPMVASNVNAFLENGLM 315
Cdd:PTZ00345 247 LFGKIFFPNVMDETFFESCGLADLITTCLGGRNVRCAAEFAKRNgkKSWEEIEAELLNGQKLQGTVTLKEVYEVLESHDL 326
|
330 340
....*....|....*....|....*....
gi 386766242 316 QHEFPLFTAIHLICQSEAPPELMIEALRN 344
Cdd:PTZ00345 327 KKEFPLFTVTYKIAFEGADPSSLIDVLST 355
|
|
| GpsA |
COG0240 |
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ... |
6-342 |
1.10e-52 |
|
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: 188.32 E-value: 1.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 6 KICIIGAEGWGSAIAAVVSNNvlegdfDSRVHLYVydemiRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDLLEAAQN 85
Cdd:COG0240 2 KIAVLGAGSWGTALAKVLARN------GHEVTLWG-----RDPEVAEEINETRENPRYLPGVKLPENLRATSDLEEALAG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 86 ADILVFSTPLEFVQSYCNILSGNVKESAFAVSMTKGLlsENGEGiELVSHAISESLGI---------PCYsmmsahsAME 156
Cdd:COG0240 71 ADLVLLAVPSQALREVLEQLAPLLPPGAPVVSATKGI--EPGTG-LLMSEVIAEELPGalriavlsgPSF-------AEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 157 MAQGKLCEVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEI 236
Cdd:COG0240 141 VARGLPTAVVVASEDEEVAERLQELLSTPYFRVYTSDDVIGVELGGALKNVIAIAAGIADGLGLGDNARAALITRGLAEM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 237 MRFIKTFfpSSKMSTFYESCG-----VTnavASSFVDKNVTFAKSLVtSGQTIEEIEANLHsgrkllgpMVA---SNVNA 308
Cdd:COG0240 221 TRLGVAL--GARPETFMGLAGlgdlvLT---CTSDLSRNRRFGLALG-KGKSLEEALAEMG--------MVAegvYTAKA 286
|
330 340 350
....*....|....*....|....*....|....*..
gi 386766242 309 FLEngLMQH---EFPLFTAIHLICQSEAPPELMIEAL 342
Cdd:COG0240 287 VYE--LAEKlgvEMPITEAVYAVLYEGKSPREAVEAL 321
|
|
| NAD_Gly3P_dh_C |
pfam07479 |
NAD-dependent glycerol-3-phosphate dehydrogenase C-terminus; NAD-dependent ... |
194-340 |
5.58e-39 |
|
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: 141.76 E-value: 5.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 194 DVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEIMRFIKTFFpsSKMSTFYESCGVTNAVASSFVDK--NV 271
Cdd:pfam07479 1 DVIGVELGGALKNVIAIAAGIADGLGLGDNAKAALITRGLAEMIRLGKALG--AKPETFFGLAGLGDLIVTCTSGLsrNR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386766242 272 TFAKSLVTsGQTIEEIEANLhsGRKLLGPMVASNVNAFLENglMQHEFPLFTAIHLICQSEAPPELMIE 340
Cdd:pfam07479 79 RFGEALGK-GKSLEEAEKEL--GQVAEGVYTAKAVYELAKK--LGVEMPIFEAVYRILYEGKSPEEALE 142
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
887-1104 |
1.37e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 46.62 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 887 MNNEKIDSDEQKFYANERMETLSESD---QDKL-----QNLNYQLKEALQHDLDVMSASRGNDSNEVLSEEDSNPEAAKK 958
Cdd:PRK10263 632 AAEEKAREAQRNQYDSGDQYNDDEIDamqQDELarqfaQTQQQRYGEQYQHDVPVNAEDADAAAEAELARQFAQTQQQRY 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 959 ITEQPLNPTP---------------NQIPAVPL--PVTMPSKQ-SHIREGSPQFQNQPRSVPPPSPQTKPQSPKEQQPRR 1020
Cdd:PRK10263 712 SGEQPAGANPfslddfefspmkallDDGPHEPLftPIVEPVQQpQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQY 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 1021 TNAPVEFGNKDEAMDLNESASDQEVPKRKKiskteaviEPVAKDVSMAEPNESLHSKKETS---PASLSKQESKRKQKRS 1097
Cdd:PRK10263 792 QQPQQPVAPQPQYQQPQQPVAPQPQYQQPQ--------QPVAPQPQYQQPQQPVAPQPQDTllhPLLMRNGDSRPLHKPT 863
|
....*..
gi 386766242 1098 LRRPSSD 1104
Cdd:PRK10263 864 TPLPSLD 870
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
959-1018 |
2.36e-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: 2.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 959 ITEQPLNPTPNQIPAVPLPVTMPSKQSHIRegsPQFQNQPRSVPPPSPQTKPQSPKEQQP 1018
Cdd:smart00818 68 VPQQPLMPVPGQHSMTPTQHHQPNLPQPAQ---QPFQPQPLQPPQPQQPMQPQPPVHPIP 124
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
539-729 |
2.01e-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: 42.70 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 539 SKQNSQLMEDAETNFTERLKVNQLKEQIDKQEAaNFKAQENLIKSIRQTI----QALGDKEKMENLIA--KSKMEEDPFQ 612
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKNLDNTRESLET-QLKVLSRSINKIKQNLeqkqKELKSKEKELKKLNeeKKELEEKVKD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 613 LKSQVesSQLKSQVEGESSElKNQIQEEayepISQADEEPSQIRSQLDEEsaQLKSLMDEENRQLESEMQDESSLLKSSA 692
Cdd:TIGR04523 515 LTKKI--SSLKEKIEKLESE-KKEKESK----ISDLEDELNKDDFELKKE--NLEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
170 180 190
....*....|....*....|....*....|....*..
gi 386766242 693 DKSEFVAYNAEEEQPIEEPTDNHQYKLRSDTNKLKEL 729
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 ... |
432-781 |
2.67e-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: 42.27 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 432 QAAQLYNDIRDGNVGVAFKMDIDEGNRQVRLLLEKEDE---MASDAALTVISSRLTAGQEDDNARIGHGHITNTSAESDH 508
Cdd:pfam02463 610 KATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGlrkGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 509 MSSKSIPSGLTTKDSPDVLDLSCESEPLHSSKQNSQLMEDAETNFTERLKVNQLKEQIDKQEAANFK------------A 576
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRlkkeekeeekseL 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 577 QENLIKSIRQTIQALGDKEKMENLIAKSKMEEDPFQLKSQVESSQLKSQVEGESSELKNQIQEEAYEPISQADEEpSQIR 656
Cdd:pfam02463 770 SLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKE-EQKL 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 657 SQLDEESAQLKSLMDEENRQLESEMQDESSLLKSsaDKSEFVAYNAEEEQPIEEPTDNHQYKLRSDTNKLKELMFTDSRE 736
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQ--KLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEE 926
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 386766242 737 HLESEKHIEVKLqDEHDFDLDEEPAIGKKDPTYTKENLELQERLE 781
Cdd:pfam02463 927 AEILLKYEEEPE-ELLLEEADEKEKEENNKEEEEERNKRLLLAKE 970
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
556-788 |
5.49e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 556 RLKVNQLKEQIDKQEAANFKAQENLIKSIRQTIQALGDKEKMENLIAKSKMEEDpfQLKSQVESSQLKSQVEGESSELKN 635
Cdd:COG4372 58 REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE--ELQEELEELQKERQDLEQQRKQLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 636 QIQEEAYEPISQADEEPSQIRSQLDEESAQLKSLMDEENRQLESEMQDESSLLKSSADKSEFVAYNAEEEQPIEEPTDNH 715
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386766242 716 QYKLRSDTNKLKELmfTDSREHLESEKHIEVKLQDEHDFDLDEEPAIGKKDPTYTKENLELQERLEWQKLKQT 788
Cdd:COG4372 216 LAEELLEAKDSLEA--KLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
578-719 |
9.79e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 578 ENLIKSIRQTIQalGDKEKMENLIAKS-----KMEEDPF---QLKSQVEssQLKSQVEGESSELKNQIQEEayepISQAD 649
Cdd:PRK00409 501 ENIIEEAKKLIG--EDKEKLNELIASLeelerELEQKAEeaeALLKEAE--KLKEELEEKKEKLQEEEDKL----LEEAE 572
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386766242 650 EEPSQIRSQLDEESAQ----LKSLMDEENRQL-ESEMQDESSLLKSsadksefvAYNAEEEQPIEEPTDNHQYKL 719
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 ... |
6-342 |
7.87e-110 |
|
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: 349.33 E-value: 7.87e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 6 KICIIGAEGWGSAIAAVVSNNVLE--GDFDSRVHLYVYDEMIRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDLLEAA 83
Cdd:TIGR03376 1 RVAVVGSGNWGTAIAKIVAENARAlpELFEESVRMWVFEEEIEGRNLTEIINTTHENVKYLPGIKLPANLVAVPDLVEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 84 QNADILVFSTPLEFVQSYCNILSGNVKESAFAVSMTKGLlSENGEGIELVSHAISESLGIPCYSMMSAHSAMEMAQGKLC 163
Cdd:TIGR03376 81 KGADILVFVIPHQFLEGICKQLKGHVKPNARAISCIKGL-EVSKDGVKLLSDIIEEELGIPCGVLSGANLANEVAKEKFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 164 EVTIGCSDNS----HSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEIMRF 239
Cdd:TIGR03376 160 ETTVGYRDPAdfdvDARVLKALFHRPYFRVNVVDDVAGVEIAGALKNVVAIAAGFVDGLGWGDNAKAAVMRRGLLEMIKF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 240 IKTFFPSSKMSTFYESCGVTNAVASSFVDKNVTFAKSLVTSGQTIEEIEANLHSGRKLLGPMVASNVNAFLENGLMQHEF 319
Cdd:TIGR03376 240 ARMFFPTGEVTFTFESCGVADLITTCLGGRNFKVGRAFAKTGKSLEELEKELLNGQSLQGVATAKEVHELLKNKNKDDEF 319
|
330 340
....*....|....*....|...
gi 386766242 320 PLFTAIHLICQSEAPPELMIEAL 342
Cdd:TIGR03376 320 PLFEAVYQILYEGLPPKKLPECL 342
|
|
| PTZ00345 |
PTZ00345 |
glycerol-3-phosphate dehydrogenase; Provisional |
1-344 |
1.13e-97 |
|
glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 240373 [Multi-domain] Cd Length: 365 Bit Score: 316.96 E-value: 1.13e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 1 MAGKLKICIIGAEGWGSAIAAVVSNNVLEGD-FDSRVHLYVYDEMIRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDL 79
Cdd:PTZ00345 8 RCGPLKVSVIGSGNWGSAISKVVGENTQRNYiFHNEVRMWVLEEIVEGEKLSDIINTKHENVKYLPGIKLPDNIVAVSDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 80 LEAAQNADILVFSTPLEFVQSYCNIL--SGNVKESAFAVSMTKGLLSENGEgIELVSHAISESLGIPCYSMMSAHSAMEM 157
Cdd:PTZ00345 88 KEAVEDADLLIFVIPHQFLESVLSQIkeNNNLKKHARAISLTKGIIVENGK-PVLCSDVIEEELGIPCCALSGANVANDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 158 AQGKLCEVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEIM 237
Cdd:PTZ00345 167 AREEFSEATIGCEDKDDALIWQRLFDRPYFKINCVPDVIGVEVCGALKNIIALAAGFCDGLGLGTNTKSAIIRIGLEEMK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 238 RFIKTFFPSSKMSTFYESCGVTNAVASSFVDKNVTFAKSLVTSG--QTIEEIEANLHSGRKLLGPMVASNVNAFLENGLM 315
Cdd:PTZ00345 247 LFGKIFFPNVMDETFFESCGLADLITTCLGGRNVRCAAEFAKRNgkKSWEEIEAELLNGQKLQGTVTLKEVYEVLESHDL 326
|
330 340
....*....|....*....|....*....
gi 386766242 316 QHEFPLFTAIHLICQSEAPPELMIEALRN 344
Cdd:PTZ00345 327 KKEFPLFTVTYKIAFEGADPSSLIDVLST 355
|
|
| GpsA |
COG0240 |
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ... |
6-342 |
1.10e-52 |
|
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: 188.32 E-value: 1.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 6 KICIIGAEGWGSAIAAVVSNNvlegdfDSRVHLYVydemiRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDLLEAAQN 85
Cdd:COG0240 2 KIAVLGAGSWGTALAKVLARN------GHEVTLWG-----RDPEVAEEINETRENPRYLPGVKLPENLRATSDLEEALAG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 86 ADILVFSTPLEFVQSYCNILSGNVKESAFAVSMTKGLlsENGEGiELVSHAISESLGI---------PCYsmmsahsAME 156
Cdd:COG0240 71 ADLVLLAVPSQALREVLEQLAPLLPPGAPVVSATKGI--EPGTG-LLMSEVIAEELPGalriavlsgPSF-------AEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 157 MAQGKLCEVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEI 236
Cdd:COG0240 141 VARGLPTAVVVASEDEEVAERLQELLSTPYFRVYTSDDVIGVELGGALKNVIAIAAGIADGLGLGDNARAALITRGLAEM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 237 MRFIKTFfpSSKMSTFYESCG-----VTnavASSFVDKNVTFAKSLVtSGQTIEEIEANLHsgrkllgpMVA---SNVNA 308
Cdd:COG0240 221 TRLGVAL--GARPETFMGLAGlgdlvLT---CTSDLSRNRRFGLALG-KGKSLEEALAEMG--------MVAegvYTAKA 286
|
330 340 350
....*....|....*....|....*....|....*..
gi 386766242 309 FLEngLMQH---EFPLFTAIHLICQSEAPPELMIEAL 342
Cdd:COG0240 287 VYE--LAEKlgvEMPITEAVYAVLYEGKSPREAVEAL 321
|
|
| gpsA |
PRK00094 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; |
6-342 |
4.03e-43 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
Pssm-ID: 234629 [Multi-domain] Cd Length: 325 Bit Score: 160.23 E-value: 4.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 6 KICIIGAEGWGSAIAAVVSNNvlegdfDSRVHLYVydemiRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDLLEAAQN 85
Cdd:PRK00094 3 KIAVLGAGSWGTALAIVLARN------GHDVTLWA-----RDPEQAAEINADRENPRYLPGIKLPDNLRATTDLAEALAD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 86 ADILVFSTPLEFVQSYCNILSGNVKESAFAVSMTKGLlsENGEGiELVSHAISESLGIPC-YSMMSAHS-AMEMAQGKLC 163
Cdd:PRK00094 72 ADLILVAVPSQALREVLKQLKPLLPPDAPIVWATKGI--EPGTG-KLLSEVLEEELPDLApIAVLSGPSfAKEVARGLPT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 164 EVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEIMRFIKTF 243
Cdd:PRK00094 149 AVVIASTDEELAERVQELFHSPYFRVYTNTDVIGVELGGALKNVIAIAAGIADGLGLGDNARAALITRGLAEITRLGVAL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 244 fpSSKMSTFYESCG-----VTnavASSFVDKNVTFAKSLVtSGQTIEEIEANLhsGrkllgpMVA---SNVNAFLEngLM 315
Cdd:PRK00094 229 --GANPETFLGLAGlgdlvLT---CTSPLSRNRRFGLALG-QGKSLEEALAEI--G------MVAegvRTAKAVYE--LA 292
|
330 340 350
....*....|....*....|....*....|
gi 386766242 316 QH---EFPLFTAIHLICQSEAPPELMIEAL 342
Cdd:PRK00094 293 KKlgvEMPITEAVYAVLYEGKDPREAVEDL 322
|
|
| NAD_Gly3P_dh_C |
pfam07479 |
NAD-dependent glycerol-3-phosphate dehydrogenase C-terminus; NAD-dependent ... |
194-340 |
5.58e-39 |
|
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: 141.76 E-value: 5.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 194 DVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEIMRFIKTFFpsSKMSTFYESCGVTNAVASSFVDK--NV 271
Cdd:pfam07479 1 DVIGVELGGALKNVIAIAAGIADGLGLGDNAKAALITRGLAEMIRLGKALG--AKPETFFGLAGLGDLIVTCTSGLsrNR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386766242 272 TFAKSLVTsGQTIEEIEANLhsGRKLLGPMVASNVNAFLENglMQHEFPLFTAIHLICQSEAPPELMIE 340
Cdd:pfam07479 79 RFGEALGK-GKSLEEAEKEL--GQVAEGVYTAKAVYELAKK--LGVEMPIFEAVYRILYEGKSPEEALE 142
|
|
| NAD_Gly3P_dh_N |
pfam01210 |
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ... |
6-174 |
1.19e-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: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 6 KICIIGAEGWGSAIAAVVSNNvlegdfDSRVHLYVYDEmirdtALSEIINTRHENVKYLPGIKLPNNLIAVNDLLEAAQN 85
Cdd:pfam01210 1 KIAVLGAGSWGTALAKVLADN------GHEVRLWGRDE-----ELIEEINTTHENVRYLPGIKLPENLKATTDLAEALKG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 86 ADILVFSTPLEFVQSYCNILSGNVKESAFAVSMTKGLlsENGeGIELVSHAISESLGI--PCYSMMSAHSAMEMAQGKLC 163
Cdd:pfam01210 70 ADIIVIVVPSQALREVLKQLKGLLKPDAILVSLSKGI--EPG-TLKLLSEVIEEELGIqpPIAVLSGPSHAEEVAQGLPT 146
|
170
....*....|.
gi 386766242 164 EVTIGCSDNSH 174
Cdd:pfam01210 147 ATVIASKDEEA 157
|
|
| PRK14618 |
PRK14618 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
1-342 |
4.86e-27 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 237770 [Multi-domain] Cd Length: 328 Bit Score: 113.43 E-value: 4.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 1 MAGKLKICIIGAEGWGSAIAAVVSNNvlegdfDSRVHLYVydemiRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDLL 80
Cdd:PRK14618 1 MHHGMRVAVLGAGAWGTALAVLAASK------GVPVRLWA-----RRPEFAAALAAERENREYLPGVALPAELYPTADPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 81 EAAQNADILVFSTPLEFVQsycNILSGNVKESAFaVSMTKGLlSENGEGIELVSHAISESLGIPCYSMMSAHSAMEMAQG 160
Cdd:PRK14618 70 EALAGADFAVVAVPSKALR---ETLAGLPRALGY-VSCAKGL-APDGGRLSELARVLEFLTQARVAVLSGPNHAEEIARF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 161 KLCEVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEIMRFI 240
Cdd:PRK14618 145 LPAATVVASPEPGLARRVQAAFSGPSFRVYTSRDRVGVELGGALKNVIALAAGMVDGLKLGDNAKAALITRGLREMVRFG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 241 KTFfpSSKMSTFYESCGVTN--AVASSFVDKNVTFAKSLVtSGQTIEEIEANlhsGRKLLGPMVASNVNAF-LENGlmqH 317
Cdd:PRK14618 225 VAL--GAEEATFYGLSGLGDliATATSPHSRNRAAGEAIV-RGVDREHLEAG---GKVVEGLYTVKALDAWaKAHG---H 295
|
330 340
....*....|....*....|....*
gi 386766242 318 EFPLFTAIHLICQSEAPPELMIEAL 342
Cdd:PRK14618 296 DLPIVEAVARVARGGWDPLAGLRSL 320
|
|
| PRK12439 |
PRK12439 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
1-238 |
2.13e-24 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 171500 [Multi-domain] Cd Length: 341 Bit Score: 106.02 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 1 MAGKLKICIIGAEGWGSAIAAVVSNNvlegdfdSRVHLYVydemiRDTALSEIINTRHENVKYLP-GIKLPNNLIAVNDL 79
Cdd:PRK12439 4 AKREPKVVVLGGGSWGTTVASICARR-------GPTLQWV-----RSAETADDINDNHRNSRYLGnDVVLSDTLRATTDF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 80 LEAAQNADILVFSTPLEFVQSYCNILSGNVKESAFAVSMTKGLlsENGEGIELvSHAISESL-GIPCYSMMSAHSAMEMA 158
Cdd:PRK12439 72 AEAANCADVVVMGVPSHGFRGVLTELAKELRPWVPVVSLVKGL--EQGTNMRM-SQIIEEVLpGHPAGILAGPNIAREVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 159 QGKLCEVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEIMR 238
Cdd:PRK12439 149 EGYAAAAVLAMPDQHLATRLSPLFRTRRFRVYTTDDVVGVEMAGALKNVFAIAVGMGYSLGIGENTRAMVIARALREMTK 228
|
|
| PRK14620 |
PRK14620 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
5-236 |
3.94e-21 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173083 [Multi-domain] Cd Length: 326 Bit Score: 96.06 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 5 LKICIIGAEGWGSAIAAVVSNNvlegdfDSRVHLYVydemiRDTALSEIINTRHENVKYLPGIKLPNNLIAVNDLLEA-A 83
Cdd:PRK14620 1 MKISILGAGSFGTAIAIALSSK------KISVNLWG-----RNHTTFESINTKRKNLKYLPTCHLPDNISVKSAIDEVlS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 84 QNADILVFSTPLEFVQSYC-NILSGNVKESAFAVSMTKGLlsENGEgIELVSHAISESL-GIPCYSMMSAHSAMEMAQGK 161
Cdd:PRK14620 70 DNATCIILAVPTQQLRTICqQLQDCHLKKNTPILICSKGI--EKSS-LKFPSEIVNEILpNNPIAILSGPSFAKEIAEKL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386766242 162 LCEVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEI 236
Cdd:PRK14620 147 PCSIVLAGQNETLGSSLISKLSNENLKIIYSQDIIGVQIGAALKNIIAIACGIVLGKNLGNNAHAAVITKGMNEI 221
|
|
| PRK14619 |
PRK14619 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional |
1-342 |
1.17e-10 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
Pssm-ID: 237771 [Multi-domain] Cd Length: 308 Bit Score: 64.24 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 1 MAGKLKICIIGAEGWGSAIAAVVSNNvlegdfDSRVHLYvydemirdtalseiinTRHENvkylpgiklpnnliavNDLL 80
Cdd:PRK14619 1 TTQPKTIAILGAGAWGSTLAGLASAN------GHRVRVW----------------SRRSG----------------LSLA 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 81 EAAQNADILVFSTPLEFVQSYCNILSG-NVKESAFAVSMTKGLLSENGegieLVSHAISESLgIPCYSM--MSAHS-AME 156
Cdd:PRK14619 43 AVLADADVIVSAVSMKGVRPVAEQVQAlNLPPETIIVTATKGLDPETT----RTPSQIWQAA-FPNHPVvvLSGPNlSKE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 157 MAQGKLCEVTIGCSDNSHSKLLISAMQTNNCRVISVNDVDGVELCGTLTDVVALGAGFIDGLRLGENARLAAIHLGVKEI 236
Cdd:PRK14619 118 IQQGLPAATVVASRDLAAAETVQQIFSSERFRVYTNSDPLGTELGGTLKNVIAIAAGVCDGLQLGTNAKAALVTRALPEM 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 237 MRfIKTFFpSSKMSTFYESCGVTN--AVASSFVDKNVTFAKSLvTSGQTIEEIEANLHSgrkllgpmVASNVNAflENGL 314
Cdd:PRK14619 198 IR-VGTHL-GAQTETFYGLSGLGDllATCTSPLSRNYQVGYGL-AQGKSLEQILAELEG--------TAEGVNT--ANVL 264
|
330 340 350
....*....|....*....|....*....|....
gi 386766242 315 MQH------EFPLFTAIHLICQSEAPPELMIEAL 342
Cdd:PRK14619 265 VQLaqqqniAVPITEQVYRLLQGEITPQQALEEL 298
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
887-1104 |
1.37e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 46.62 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 887 MNNEKIDSDEQKFYANERMETLSESD---QDKL-----QNLNYQLKEALQHDLDVMSASRGNDSNEVLSEEDSNPEAAKK 958
Cdd:PRK10263 632 AAEEKAREAQRNQYDSGDQYNDDEIDamqQDELarqfaQTQQQRYGEQYQHDVPVNAEDADAAAEAELARQFAQTQQQRY 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 959 ITEQPLNPTP---------------NQIPAVPL--PVTMPSKQ-SHIREGSPQFQNQPRSVPPPSPQTKPQSPKEQQPRR 1020
Cdd:PRK10263 712 SGEQPAGANPfslddfefspmkallDDGPHEPLftPIVEPVQQpQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQY 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 1021 TNAPVEFGNKDEAMDLNESASDQEVPKRKKiskteaviEPVAKDVSMAEPNESLHSKKETS---PASLSKQESKRKQKRS 1097
Cdd:PRK10263 792 QQPQQPVAPQPQYQQPQQPVAPQPQYQQPQ--------QPVAPQPQYQQPQQPVAPQPQDTllhPLLMRNGDSRPLHKPT 863
|
....*..
gi 386766242 1098 LRRPSSD 1104
Cdd:PRK10263 864 TPLPSLD 870
|
|
| PRK13729 |
PRK13729 |
conjugal transfer pilus assembly protein TraB; Provisional |
913-1152 |
1.38e-04 |
|
conjugal transfer pilus assembly protein TraB; Provisional
Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 45.97 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 913 QDKLQNLNYQLKEaLQHDLDVMSASRGNDSN--EVLSEEDSN-PEAAKKITEQPLNPTPNQIPAVPLPVTMPskqshirE 989
Cdd:PRK13729 75 QVTAAQMQKQYEE-IRRELDVLNKQRGDDQRriEKLGQDNAAlAEQVKALGANPVTATGEPVPQMPASPPGP-------E 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 990 GSPQFQNQPRSVPPPSPQTKPqspkeqqprrtnAPVEF--GNkdeAMDLNESASDQEVPKRKKISKTEAVIEPVAKDVSM 1067
Cdd:PRK13729 147 GEPQPGNTPVSFPPQGSVAVP------------PPTAFypGN---GVTPPPQVTYQSVPVPNRIQRKTFTYNEGKKGPSL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 1068 ----------------AEPNESLHSKKETSPASLskqeskRKQKRsLRRPSS---DSDSTKTTNE----FEKQRQIIENQ 1124
Cdd:PRK13729 212 pyipsgsfakamliegADANASVTGNESTVPMQL------RITGL-VEMPNSktyDATGCFVGLEawgdVSSERAIVRTR 284
|
250 260
....*....|....*....|....*...
gi 386766242 1125 KAQLEKMGKKISVMRQGQdrrVSYKGHN 1152
Cdd:PRK13729 285 NISCLKNGKTIDMPIKGH---VSFRGKN 309
|
|
| PTZ00441 |
PTZ00441 |
sporozoite surface protein 2 (SSP2); Provisional |
912-1136 |
2.19e-04 |
|
sporozoite surface protein 2 (SSP2); Provisional
Pssm-ID: 240420 [Multi-domain] Cd Length: 576 Bit Score: 45.34 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 912 DQDKLQNLNYQLKEALQHDLDVMSASRGNDSNEVlsEEDSNPEAAKKITEQPLNPtpnqipavPLPVTMPSKQSHIREGS 991
Cdd:PTZ00441 309 DEFAVPNFNEGLDVPDNPQDPVPPPNEGKDGNPN--EENLFPPGDDEVPDESNVP--------PNPPNVPGGSNSEFSSD 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 992 PQFQNQprsvpPPSPQTKPQSPKEQQPRRTNAPVEFgNKDEAMDLNESASDQEVPKRKKISKTEAVI-EPVAKDVSMAEP 1070
Cdd:PTZ00441 379 VENPPN-----PPNPDIPEQEPNIPEDSNKEVPEDV-PMEPEDDRDNNFNEPKKPENKGDGQNEPVIpKPLDNERDQSNK 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386766242 1071 NESLH-SKKETSPASLSKQESKRKQKRSLRRPSSDSDSTKTTNEFEKQrqiiENQKAQLEKMGKKIS 1136
Cdd:PTZ00441 453 NKQVNpGNRHNSEDRYTRPHGRNNENRNYNNKNSDIPKHPERSEHEQP----EDKKKKSSNNGYKIA 515
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
959-1018 |
2.36e-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: 2.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 959 ITEQPLNPTPNQIPAVPLPVTMPSKQSHIRegsPQFQNQPRSVPPPSPQTKPQSPKEQQP 1018
Cdd:smart00818 68 VPQQPLMPVPGQHSMTPTQHHQPNLPQPAQ---QPFQPQPLQPPQPQQPMQPQPPVHPIP 124
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
539-729 |
2.01e-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: 42.70 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 539 SKQNSQLMEDAETNFTERLKVNQLKEQIDKQEAaNFKAQENLIKSIRQTI----QALGDKEKMENLIA--KSKMEEDPFQ 612
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKNLDNTRESLET-QLKVLSRSINKIKQNLeqkqKELKSKEKELKKLNeeKKELEEKVKD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 613 LKSQVesSQLKSQVEGESSElKNQIQEEayepISQADEEPSQIRSQLDEEsaQLKSLMDEENRQLESEMQDESSLLKSSA 692
Cdd:TIGR04523 515 LTKKI--SSLKEKIEKLESE-KKEKESK----ISDLEDELNKDDFELKKE--NLEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
170 180 190
....*....|....*....|....*....|....*..
gi 386766242 693 DKSEFVAYNAEEEQPIEEPTDNHQYKLRSDTNKLKEL 729
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 ... |
432-781 |
2.67e-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: 42.27 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 432 QAAQLYNDIRDGNVGVAFKMDIDEGNRQVRLLLEKEDE---MASDAALTVISSRLTAGQEDDNARIGHGHITNTSAESDH 508
Cdd:pfam02463 610 KATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGlrkGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 509 MSSKSIPSGLTTKDSPDVLDLSCESEPLHSSKQNSQLMEDAETNFTERLKVNQLKEQIDKQEAANFK------------A 576
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRlkkeekeeekseL 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 577 QENLIKSIRQTIQALGDKEKMENLIAKSKMEEDPFQLKSQVESSQLKSQVEGESSELKNQIQEEAYEPISQADEEpSQIR 656
Cdd:pfam02463 770 SLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKE-EQKL 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 657 SQLDEESAQLKSLMDEENRQLESEMQDESSLLKSsaDKSEFVAYNAEEEQPIEEPTDNHQYKLRSDTNKLKELMFTDSRE 736
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQ--KLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEE 926
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 386766242 737 HLESEKHIEVKLqDEHDFDLDEEPAIGKKDPTYTKENLELQERLE 781
Cdd:pfam02463 927 AEILLKYEEEPE-ELLLEEADEKEKEENNKEEEEERNKRLLLAKE 970
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
962-1013 |
3.51e-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: 3.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 386766242 962 QPLNPTPNQIPAVPLPVTMPSKQSHIREGSPQFQNQPRSVPPPSPQTKPQSP 1013
Cdd:smart00818 80 HSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMQPQPPVHPIPPLPPQPP 131
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
555-1094 |
3.59e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 555 ERLKVNQLK--EQIDKQEAANFKAQEnLIKSIRQTIQALGDKEKMENLiaKSKMEEdpfqlKSQVESSQLKSQVEGESSE 632
Cdd:PTZ00121 1364 EKAEAAEKKkeEAKKKADAAKKKAEE-KKKADEAKKKAEEDKKKADEL--KKAAAA-----KKKADEAKKKAEEKKKADE 1435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 633 LKNQIQE--EAYEPISQADE----EPSQIRSQLDEESAQLKSLMDEENRQLESEMQDESSLLKS-SADKSEFVAYNAEEE 705
Cdd:PTZ00121 1436 AKKKAEEakKADEAKKKAEEakkaEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdEAKKAAEAKKKADEA 1515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 706 QPIEEPTDNHQYKLRSDTNKLKELMFTDSREHLESEKHIEvKLQDEHDFDLDEEPAIGKKDPTYTKENLELQERLEWQKL 785
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 786 KQTDKPHHPYSSADLEDSTTNEgNARLPIEHDNRFQNVDRYQDRELVQVRAELKETSGAESEKEINLISEQRPDQNQDEv 865
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAE-EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE- 1672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 866 nlrphSHIKTEETGHHEWDWLMNNEKIDSDEQKFYANERMETLSESDQDKLQNLNyqlKEALQHDLDVMSASRGNDSNEV 945
Cdd:PTZ00121 1673 -----DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELK---KAEEENKIKAEEAKKEAEEDKK 1744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 946 LSEEDSNPEAAKKITEQPLNPTPNQIPAVPlpvtmPSKQSHIREGSPQFQNQPRSvpppspqtkPQSPKEQQPRRTNAPV 1025
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAHLKKEEEKKAEEIR-----KEKEAVIEEELDEEDEKRRM---------EVDKKIKDIFDNFANI 1810
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386766242 1026 EFGNKDEAMDLNESaSDQEVPKRKKISKTEAVIEPVAKDVSMAEPNESLHSKKETSPASLSKQESKRKQ 1094
Cdd:PTZ00121 1811 IEGGKEGNLVINDS-KEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKE 1878
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
556-781 |
4.07e-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: 41.59 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 556 RLKVNQLKEQIDKQEAanfkaqenLIKSIRQTIQAL-GDKEKMENL--IAKSKMEEDPFQLKSQVESSQL-KSQVEGESS 631
Cdd:TIGR02169 176 LEELEEVEENIERLDL--------IIDEKRQQLERLrREREKAERYqaLLKEKREYEGYELLKEKEALERqKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 632 ELKNQIqEEAYEPISQADEEPSQIRSQLDEESAQLKSLMDEENRQLESEMQDESSLLKSSADKSEFvaynAEEEQpieEP 711
Cdd:TIGR02169 248 SLEEEL-EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAE----KEREL---ED 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386766242 712 TDNHQYKLRSDTNKLKELMfTDSREHLESEKHIEVKLQDEHDFDLDEE-------PAIGKKDPTYTKENLELQERLE 781
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEI-EELEREIEEERKRRDKLTEEYAELKEELedlraelEEVDKEFAETRDELKDYREKLE 395
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
556-925 |
4.29e-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: 41.63 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 556 RLKVNQLKEQIDKQEaanfkaqENLIKSIRQTIQALGDKEKMenliaKSKMEEDPFQLKSQVESSQLKSQVEGESSELKn 635
Cdd:pfam05483 267 RDKANQLEEKTKLQD-------ENLKELIEKKDHLTKELEDI-----KMSLQRSMSTQKALEEDLQIATKTICQLTEEK- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 636 qiqEEAYEPISQADEEPSQIRSQLDEESAQLKSLMDEENRQLESEmQDESSLL-----KSSADKSEFVAYNAEEEQPIEE 710
Cdd:pfam05483 334 ---EAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN-EDQLKIItmelqKKSSELEEMTKFKNNKEVELEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 711 PTD--NHQYKLRSDTNKLKELMFTDSREHLESEKHIEVKLQDEHDFDLdEEPAIGKKDPTYTKENLELQERLEWQKLKQT 788
Cdd:pfam05483 410 LKKilAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEI-QLTAIKTSEEHYLKEVEDLKTELEKEKLKNI 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 789 DKPHHPySSADLEDSTTNEGNARLPIEHDNRFQNVDRYQDRElvqvRAELKETSGAEsEKEINLISE-----QRPDQNQD 863
Cdd:pfam05483 489 ELTAHC-DKLLLENKELTQEASDMTLELKKHQEDIINCKKQE----ERMLKQIENLE-EKEMNLRDElesvrEEFIQKGD 562
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386766242 864 EVNLRPHshiKTEETGHHEWDWLMNNEKIDSDEQKFYANERMETLSESDQ-DKLQNLNYQLKE 925
Cdd:pfam05483 563 EVKCKLD---KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNiEELHQENKALKK 622
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
556-788 |
5.49e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 556 RLKVNQLKEQIDKQEAANFKAQENLIKSIRQTIQALGDKEKMENLIAKSKMEEDpfQLKSQVESSQLKSQVEGESSELKN 635
Cdd:COG4372 58 REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE--ELQEELEELQKERQDLEQQRKQLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 636 QIQEEAYEPISQADEEPSQIRSQLDEESAQLKSLMDEENRQLESEMQDESSLLKSSADKSEFVAYNAEEEQPIEEPTDNH 715
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386766242 716 QYKLRSDTNKLKELmfTDSREHLESEKHIEVKLQDEHDFDLDEEPAIGKKDPTYTKENLELQERLEWQKLKQT 788
Cdd:COG4372 216 LAEELLEAKDSLEA--KLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
462-951 |
6.41e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.22 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 462 LLLEKEDEMASDAALTVISSRLTAGQEDDNARIGHGHITNTSAESDHMSSKSIPSGLTTKDSPDVLDLSCEsepLHSSKQ 541
Cdd:COG5022 862 SLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIAR---LKKLLN 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 542 NSQLMEDAETNFTERLKVNQLKEQIDKQEAANFKaQENLIKSIRQTI-QALGDKEKMENLiaKSKMEEDPFQLKSQVESS 620
Cdd:COG5022 939 NIDLEEGPSIEYVKLPELNKLHEVESKLKETSEE-YEDLLKKSTILVrEGNKANSELKNF--KKELAELSKQYGALQEST 1015
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 621 QLKSQVEGESSELKNqiqeeAYEPISQADEEpSQIRSQLDEesaqLKSLMDEENRQLESEMQDeSSLLKSSADKSEFVAY 700
Cdd:COG5022 1016 KQLKELPVEVAELQS-----ASKIISSESTE-LSILKPLQK----LKGLLLLENNQLQARYKA-LKLRRENSLLDDKQLY 1084
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 701 NAeEEQPIEEPTDNHQYKLRSDTNKLKELMFTD--------SREHLESEKHIEVKLQDEHDFDLDEEPAigKKDPTYTKE 772
Cdd:COG5022 1085 QL-ESTENLLKTINVKDLEVTNRNLVKPANVLQfivaqmikLNLLQEISKFLSQLVNTLEPVFQKLSVL--QLELDGLFW 1161
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 773 NLELQERLEWQKLKQTDKphhpysSADLEDSTTNEGNARLPIEHDNRFQNVDR--YQDRELVQVRAELKetsgaESEKEI 850
Cdd:COG5022 1162 EANLEALPSPPPFAALSE------KRLYQSALYDEKSKLSSSEVNDLKNELIAlfSKIFSGWPRGDKLK-----KLISEG 1230
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 851 NLISEQRPDQNqDEVNLrphSHIKTEETGHHEWDWLMNNEKIDSDEQKFYANERMETLseSDQDKLQNLNYQLKEALQHD 930
Cdd:COG5022 1231 WVPTEYSTSLK-GFNNL---NKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPA--TINSLLQYINVGLFNALRTK 1304
|
490 500
....*....|....*....|.
gi 386766242 931 LDVMSASRGNDSNEVLSEEDS 951
Cdd:COG5022 1305 ASSLRWKSATEVNYNSEELDD 1325
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
578-719 |
9.79e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 578 ENLIKSIRQTIQalGDKEKMENLIAKS-----KMEEDPF---QLKSQVEssQLKSQVEGESSELKNQIQEEayepISQAD 649
Cdd:PRK00409 501 ENIIEEAKKLIG--EDKEKLNELIASLeelerELEQKAEeaeALLKEAE--KLKEELEEKKEKLQEEEDKL----LEEAE 572
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386766242 650 EEPSQIRSQLDEESAQ----LKSLMDEENRQL-ESEMQDESSLLKSsadksefvAYNAEEEQPIEEPTDNHQYKL 719
Cdd:PRK00409 573 KEAQQAIKEAKKEADEiikeLRQLQKGGYASVkAHELIEARKRLNK--------ANEKKEKKKKKQKEKQEELKV 639
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
546-872 |
9.94e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 546 MEDAETNFTERLK---VNQLKEQIDKQEAANFKAQENL---IKSIRQTIQAL-GDKEKMENLIAK-----SKMEEDPFQL 613
Cdd:pfam12128 195 FRDVKSMIVAILEddgVVPPKSRLNRQQVEHWIRDIQAiagIMKIRPEFTKLqQEFNTLESAELRlshlhFGYKSDETLI 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 614 KSQVESSQ-LKSQVEGESSELKNQIQE---EAYEPISQADEEPSQIRSQLDEESAQLKSLMDEENRQLESEMQDESSLLK 689
Cdd:pfam12128 275 ASRQEERQeTSAELNQLLRTLDDQWKEkrdELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQS 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 690 SSADKSEFVAYNAEEEQPIEEPTDNHQYKLRSDTN--------KLKELMFTDSREHLESEKH---IEVKLQDEHDFDLDE 758
Cdd:pfam12128 355 ELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNrdiagikdKLAKIREARDRQLAVAEDDlqaLESELREQLEAGKLE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766242 759 epaigkkdptYTKENLELQERLEWQKLKQTDKPHHPYSSADLEDSTTNEGNARLPIEhdNRFQNVDRYQDrELVQVRAEL 838
Cdd:pfam12128 435 ----------FNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQE--AANAEVERLQS-ELRQARKRR 501
|
330 340 350
....*....|....*....|....*....|....
gi 386766242 839 KETSGAESEKEINLiSEQRPDQNQDEVNLRPHSH 872
Cdd:pfam12128 502 DQASEALRQASRRL-EERQSALDELELQLFPQAG 534
|
|
| |
