|
Name |
Accession |
Description |
Interval |
E-value |
| DD_EFCAB5 |
cd22968 |
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 ... |
159-215 |
7.82e-28 |
|
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 (EFCAB5) and similar proteins; EF-hand calcium-binding domain-containing protein 5 (EFCAB5) is an uncharacterized protein that contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.
Pssm-ID: 438537 Cd Length: 60 Bit Score: 107.28 E-value: 7.82e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 159 DARAYLLDKLLPTLILGIEKLLMEAEKRGLAESNEAD---PNFNPINFLGQYLMRNNPRY 215
Cdd:cd22968 1 ETRAYLVEKVLPTLVPGLEKLLKEVERRGLLEEEGRPepaPRFNPINWLAQYLMRNNPRY 60
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
509-818 |
7.20e-10 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 63.91 E-value: 7.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 509 SEDVTEALEKVLEEDKAAEEQKIEE---------QLPEETKADEKEPTVPAETAEsvkdtAEEAKPEGQAEKPADVEE-V 578
Cdd:PRK10811 655 ESQQAEVTEKARTQDEQQQAPRRERqrrrndekrQAQQEAKALNVEEQSVQETEQ-----EERVQQVQPRRKQRQLNQkV 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 579 KAIDQTAEPSADQEKEQ-------AAETTEESAEQVVEAVGQVVEPSTELAEEPSAKPVDE------------------- 632
Cdd:PRK10811 730 RIEQSVAEEAVAPVVEEtvaaepvVQEVPAPRTELVKVPLPVVAQTAPEQDEENNAENRDNngmprrsrrsprhlrvsgq 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 633 ----------PSAKPIDETSAKPVDE-PSEK-----PVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKPVEE 696
Cdd:PRK10811 810 rrrryrderyPTQSPMPLTVACASPEmASGKvwiryPVVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVE 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 697 PSSKPVEEPATDSASQEGEPM-VEPSAKPVEGASAEQATAQEPNEPAPAAAEAVSESVGAEPTGAVPEPAATEATKAEEQ 775
Cdd:PRK10811 890 AVAEVVEEPVVVAEPQPEEVVvVETTHPEVIAAPVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVV 969
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1944883863 776 KVEETPEIVKPAAGEKEAVAETVAETSPGSEKQGVTFHRDTVE 818
Cdd:PRK10811 970 VAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVE 1012
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
441-724 |
9.17e-08 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 56.95 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 441 ELDSISEDSFVRSLPGTPAaGSIAKGLDRKPATAEKKPE-PKPSDEVPtevsSEDVISATGEKlniggASEDVTEALEKV 519
Cdd:NF033838 244 KLKEAVEKNVATSEQDKPK-RRAKRGVLGEPATPDKKENdAKSSDSSV----GEETLPSPSLK-----PEKKVAEAEKKV 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 520 LEEDKAAEEQKieeqlpEETKADEkePTVPAETAEsvkdtAEEAKPEGQAeKPADVEEVKaidQTAEPSADQEKEQAAET 599
Cdd:NF033838 314 EEAKKKAKDQK------EEDRRNY--PTNTYKTLE-----LEIAESDVKV-KEAELELVK---EEAKEPRNEEKIKQAKA 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 600 TEESAEQVVEAVGQVVEPSTELAEEPSAKPVDEPSAKpidetsakpvdepsEKPVDEPSAKPDDEPsakpdEEPSTKPvE 679
Cdd:NF033838 377 KVESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVK--------------EKPAEQPQPAPAPQP-----EKPAPKP-E 436
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1944883863 680 EPSAMP-VEEPSSKPVEEPSSKPVEEpATDSASQEGEPMVEPSAKP 724
Cdd:NF033838 437 KPAEQPkAEKPADQQAEEDYARRSEE-EYNRLTQQQPPKTEKPAQP 481
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
434-833 |
1.45e-07 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 56.56 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 434 ELDEVTDELDSISEDSFVRSLPGTPAAGSIAKGLDRKPATAEKKPEPKPSDEVPTEVSSEDVISATGEKLNIGGASEDVT 513
Cdd:COG5271 555 ETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAE 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 514 EALEKVLEEDKAAEEQKIEEQLPEETKADEKEPTVpAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEK 593
Cdd:COG5271 635 DEAAEPETDASEAADEDADAETEAEASADESEEEA-EDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASEEAD 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 594 EQAAETTEESAEQVVEAVGQVVEPS-------------------TELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPV 654
Cdd:COG5271 714 AEEADTEADGTAEEAEEAAEEAESAdeeaaslpdeadaeeeaeeAEEAEEDDADGLEEALEEEKADAEEAATDEEAEAAA 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 655 DEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPS-----SKPVEEPSSKPVEEPATDSASQEGEPMVEPSAKPVEGAS 729
Cdd:COG5271 794 EEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEEtadeaLEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEH 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 730 AEQATAQEPNEPAPAAAEAVSESVGAEPTGAVPEPAATEATKAEEQKVEETPEIVKPAAGEKEAVAETVAETSPGSEKQG 809
Cdd:COG5271 874 EAEEAQEAETDADADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALD 953
|
410 420
....*....|....*....|....
gi 1944883863 810 VTFHRDTVETTGKSDHSSIKSPTK 833
Cdd:COG5271 954 EAGDEESDDAAADDAGDDSLADDD 977
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
476-733 |
1.03e-06 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 53.23 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 476 KKPEPKPSDEVPTEVSSEDVISatgeklNIGGASEDVTEALEKVLEEDKAAEEQKIEEQLPE-----ETKADEKEPTVPA 550
Cdd:NF033839 241 KKQALSEIDNVNTKVEIENTVH------KIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKpgmqpSPQPEKKEVKPEP 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 551 ETA-ESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQ-AAETTEESAEQVVEAVGQVVEPSTELAEEPSAK 628
Cdd:NF033839 315 ETPkPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKpKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 629 pvdEPSAKPIDETSAKPVDEPSEKPvdEPSAKPDDEPsAKPDEEPSTkpvEEPSAMPVEEPSSKPVEEPSSKPVEEPATD 708
Cdd:NF033839 395 ---KPEVKPQPEKPKPEVKPQPEKP--KPEVKPQPEK-PKPEVKPQP---EKPKPEVKPQPEKPKPEVKPQPETPKPEVK 465
|
250 260
....*....|....*....|....*.
gi 1944883863 709 SASQEGEPMVEPS-AKPVEGASAEQA 733
Cdd:NF033839 466 PQPEKPKPEVKPQpEKPKPDNSKPQA 491
|
|
| Cornifin |
pfam02389 |
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ... |
613-734 |
1.73e-06 |
|
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.
Pssm-ID: 280537 [Multi-domain] Cd Length: 135 Bit Score: 48.90 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 613 QVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSK 692
Cdd:pfam02389 4 QVKQPCQPPPQEPCVPTTKEPCHSKVPEPCNPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCYPKVPEPCSP 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1944883863 693 PV--------EEPSSKPVEEPATDSASQEGEPMV-EPSAKPVEGASAEQAT 734
Cdd:pfam02389 84 KVpepchpkaPEPCHPKVPEPCYPKAPEPCQPKVpEPCPSTVTPGPAQQKT 134
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
510-627 |
2.93e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 51.94 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 510 EDVTEALEKVleEDKAAEEQKIEEQLPEETKADEKEPTVPAETAESVKDTAEEAKPEG--QAEKPADVEEVKAIDQTAEP 587
Cdd:NF033838 369 EKIKQAKAKV--ESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPapQPEKPAPKPEKPAEQPKAEK 446
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1944883863 588 SADQekeQAAETTEESAEQVVEAVGQVVEPSTELAEEPSA 627
Cdd:NF033838 447 PADQ---QAEEDYARRSEEEYNRLTQQQPPKTEKPAQPST 483
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
912-974 |
3.90e-06 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 45.62 E-value: 3.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1944883863 912 MLEQLFEKWDNDGSGYLDLEELHSVMSKFKENMEAKIMQKaktiMMKE---EYDNRLSKREFKAYI 974
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDE----MIREvdkDGDGKIDFEEFLELM 62
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
468-711 |
3.23e-05 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 48.61 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 468 DRKPATAEKKPEPKPSDEVPtevssedvisatgeklniggaSEDVTEALEKVLEEDKAAEEQKIEEQLPEETKADEKEPT 547
Cdd:NF033839 320 EVKPQLEKPKPEVKPQPEKP---------------------KPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 548 VPAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEQvveavgqvvePSTELAEEPSA 627
Cdd:NF033839 379 QPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEK----------PKPEVKPQPEK 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 628 KpvdEPSAKPIDETSAKPVDEPSEKPVDE-----PSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKpvEEPSSKPV 702
Cdd:NF033839 449 P---KPEVKPQPETPKPEVKPQPEKPKPEvkpqpEKPKPDNSKPQADDKKPSTPNNLSKDKQPSNQASTN--EKATNKPK 523
|
250
....*....|
gi 1944883863 703 EE-PATDSAS 711
Cdd:NF033839 524 KSlPSTGSIS 533
|
|
| ftsN |
TIGR02223 |
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ... |
471-635 |
6.13e-05 |
|
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis. [Cellular processes, Cell division]
Pssm-ID: 274041 [Multi-domain] Cd Length: 298 Bit Score: 46.61 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 471 PATAEKKPEPKPSDEVPTEVSSEDVISATGEKLNIGGASEDVTE--ALEKVLEEDKAAEEQKIEEQLPEETKADEKEPTV 548
Cdd:TIGR02223 70 ETAADLPPKPEERWSYIEELEAREVLINDPEEPSNGGGVEESAQltAEQRQLLEQMQADMRAAEKVLATAPSEQTVAVEA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 549 PAETAESVKD---TAEEAKPEGQAEKPADVEEVKAIDQTAEPsadqekeqaaettEESAEQVVEAVGQVVEPSTELAEEP 625
Cdd:TIGR02223 150 RKQTAEKKPQkarTAEAQKTPVETEKIASKVKEAKQKQKALP-------------KQTAETQSNSKPIETAPKADKADKT 216
|
170
....*....|
gi 1944883863 626 SAKPVDEPSA 635
Cdd:TIGR02223 217 KPKPKEKAER 226
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
1094-1186 |
1.43e-04 |
|
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.
Pssm-ID: 214500 [Multi-domain] Cd Length: 149 Bit Score: 43.52 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 1094 FRDMKGISFTSVDTGKPIHVPRVQNHGNimFWNPDRSEEDRQGSFIVIPLKDHRkRVFGVLGVDTLNDPQEksiFITHEI 1173
Cdd:smart00065 52 FPLDEGLAGRVAETGRPLNIPDVEADPL--FAEDLLGRYQGVRSFLAVPLVADG-ELVGVLALHNKKSPRP---FTEEDE 125
|
90
....*....|...
gi 1944883863 1174 SFFQGVAKAFSSA 1186
Cdd:smart00065 126 ELLQALANQLAIA 138
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
584-800 |
4.17e-04 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 45.09 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 584 TAEPsaDQEKEQAAETTEESA--EQVVEAVGQVVEPSTELAEEPSAKPVDEPSAKPIDETSAkpvdepsEKPVDEPSAKP 661
Cdd:NF033875 54 TVQP--DNPDPQSGSETPKTAvsEEATVQKDTTSQPTKVEEVASEKNGAEQSSATPNDTTNA-------QQPTVGAEKSA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 662 DDEPSAKPdeEPSTKPVEEPSAM-PVEEPSSKPVEEPssKPVEEPATDSASQEG--EPMVEPSAKPVE---GASAEQATA 735
Cdd:NF033875 125 QEQPVVSP--ETTNEPLGQPTEVaPAENEANKSTSIP--KEFETPDVDKAVDEAkkDPNITVVEKPAEdlgNVSSKDLAA 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1944883863 736 QEPNEpapaaaeavsESVGAEPTGAVPEPAATeaTKAEEQKV-EETPEIVKPAAGEKEAVAETVAE 800
Cdd:NF033875 201 KEKEV----------DQLQKEQAKKIAQQAAE--LKAKNEKIaKENAEIAAKNKAEKERYEKEVAE 254
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
539-677 |
1.01e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 43.22 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 539 TKADEKEPTVPAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEQVVEAVGQVVEPS 618
Cdd:NF040712 188 IDPDFGRPLRPLATVPRLAREPADARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPA 267
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1944883863 619 TELAEEPSAKPVDEPSAKPiDETSAKPVDEPSEKPvDEPSAKPDDEPSAKPDEEPSTKP 677
Cdd:NF040712 268 AEPDEATRDAGEPPAPGAA-ETPEAAEPPAPAPAA-PAAPAAPEAEEPARPEPPPAPKP 324
|
|
| EF-hand_6 |
pfam13405 |
EF-hand domain; |
913-940 |
1.62e-03 |
|
EF-hand domain;
Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 37.16 E-value: 1.62e-03
10 20
....*....|....*....|....*...
gi 1944883863 913 LEQLFEKWDNDGSGYLDLEELHSVMSKF 940
Cdd:pfam13405 2 LREAFKLFDKDGDGKISLEELRKALRSL 29
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
477-722 |
2.02e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 42.45 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 477 KPEPKPSDEVP-TEVSSEDVISATGEKLNIGGASEDVTEALEKVLEEDKAAEEQKIEEQLPE-ETKADEKEPTvPAETAE 554
Cdd:NF033839 285 KEPGNKKPSAPkPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQlETPKPEVKPQ-PEKPKP 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 555 SVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQaaetteesaeqvveavgqvvePSTELAEEPSAKpvdEPS 634
Cdd:NF033839 364 EVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEK---------------------PKPEVKPQPEKP---KPE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 635 AKPIDETSAKPVDEPSEKPVDEPSAKPDD-EPSAKPD-EEPSTKPVEEPSA-MPVEEPSSKPVEEPSSKPVEE----PAT 707
Cdd:NF033839 420 VKPQPEKPKPEVKPQPEKPKPEVKPQPEKpKPEVKPQpETPKPEVKPQPEKpKPEVKPQPEKPKPDNSKPQADdkkpSTP 499
|
250
....*....|....*
gi 1944883863 708 DSASQEGEPMVEPSA 722
Cdd:NF033839 500 NNLSKDKQPSNQAST 514
|
|
| Dpy-30 |
pfam05186 |
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ... |
160-213 |
3.75e-03 |
|
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the Dpy-30 proteins hence the motifs name. It is about 40 residues long and is probably formed of two alpha-helices. It may be a dimerization motif analogous to pfam02197 (Bateman A pers obs).
Pssm-ID: 428357 Cd Length: 42 Bit Score: 36.43 E-value: 3.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1944883863 160 ARAYLLDKLLPTLILGIEKLlmeAEKRglaesneadPNfNPINFLGQYLMRNNP 213
Cdd:pfam05186 2 ARQYLNKTVAPILLQGLTEL---AKER---------PE-DPIEYLADYLLKNNP 42
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
883-938 |
8.07e-03 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 36.37 E-value: 8.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1944883863 883 GEGYIETEEekYLRLQKSRREAQSAKRklmLEQLFEKWDNDGSGYLDLEELHSVMS 938
Cdd:cd00051 13 GDGTISADE--LKAALKSLGEGLSEEE---IDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
543-701 |
8.20e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 40.14 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 543 EKEPTVPAETAESVKDTAeeakPEGQAEKPADVEEVKAIDqtaEPSADQEKEQAAETTEESAEQVVEAVGqvvepsTELA 622
Cdd:NF040712 189 DPDFGRPLRPLATVPRLA----REPADARPEEVEPAPAAE---GAPATDSDPAEAGTPDDLASARRRRAG------VEQP 255
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1944883863 623 EEPSAKPVDEPSAKPIDETSAKPVDEPSEKPvdepsakpdDEPSAKPDEEPSTKPVEEPsAMPVEEPSSKPVEEPSSKP 701
Cdd:NF040712 256 EDEPVGPGAAPAAEPDEATRDAGEPPAPGAA---------ETPEAAEPPAPAPAAPAAP-AAPEAEEPARPEPPPAPKP 324
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
912-976 |
8.40e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 38.23 E-value: 8.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1944883863 912 MLEQLFEKWDNDGSGYLDLEELHSVMSKfkeNMEAKIMQKAKTIMMK--EEYDNRLSKREFKAYIEA 976
Cdd:COG5126 34 LWATLFSEADTDGDGRISREEFVAGMES---LFEATVEPFARAAFDLldTDGDGKISADEFRRLLTA 97
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
468-736 |
8.84e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 40.77 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 468 DRKPATAEKKPEPKPSDEVPTEVSSEDVISATGEKLNIGGASE-DVTEALEKVLEEDKAAEEQKI----EEQLPEETKAD 542
Cdd:NF033838 203 EEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLkEAVEKNVATSEQDKPKRRAKRgvlgEPATPDKKEND 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 543 EK-------EPTVPAETAESVKDTAEEAKPEGQAEKpadveevKAIDQTAEpsadQEKEQAAETTEESAEQVVEAVGQVV 615
Cdd:NF033838 283 AKssdssvgEETLPSPSLKPEKKVAEAEKKVEEAKK-------KAKDQKEE----DRRNYPTNTYKTLELEIAESDVKVK 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 616 EPSTELAEEPSAKPVDEpsaKPIDETSAKPVDEPSEKPVDEpSAKPDDEpsaKPDEEPSTKPVEEpsampvEEPSSKPVE 695
Cdd:NF033838 352 EAELELVKEEAKEPRNE---EKIKQAKAKVESKKAEATRLE-KIKTDRK---KAEEEAKRKAAEE------DKVKEKPAE 418
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1944883863 696 EPSSKPVEEPATDSASQEgEPMVEPSAKPVEGASAEQATAQ 736
Cdd:NF033838 419 QPQPAPAPQPEKPAPKPE-KPAEQPKAEKPADQQAEEDYAR 458
|
|
| EFh |
smart00054 |
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ... |
913-940 |
9.42e-03 |
|
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.
Pssm-ID: 197492 [Multi-domain] Cd Length: 29 Bit Score: 35.05 E-value: 9.42e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DD_EFCAB5 |
cd22968 |
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 ... |
159-215 |
7.82e-28 |
|
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 (EFCAB5) and similar proteins; EF-hand calcium-binding domain-containing protein 5 (EFCAB5) is an uncharacterized protein that contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.
Pssm-ID: 438537 Cd Length: 60 Bit Score: 107.28 E-value: 7.82e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 159 DARAYLLDKLLPTLILGIEKLLMEAEKRGLAESNEAD---PNFNPINFLGQYLMRNNPRY 215
Cdd:cd22968 1 ETRAYLVEKVLPTLVPGLEKLLKEVERRGLLEEEGRPepaPRFNPINWLAQYLMRNNPRY 60
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
509-818 |
7.20e-10 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 63.91 E-value: 7.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 509 SEDVTEALEKVLEEDKAAEEQKIEE---------QLPEETKADEKEPTVPAETAEsvkdtAEEAKPEGQAEKPADVEE-V 578
Cdd:PRK10811 655 ESQQAEVTEKARTQDEQQQAPRRERqrrrndekrQAQQEAKALNVEEQSVQETEQ-----EERVQQVQPRRKQRQLNQkV 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 579 KAIDQTAEPSADQEKEQ-------AAETTEESAEQVVEAVGQVVEPSTELAEEPSAKPVDE------------------- 632
Cdd:PRK10811 730 RIEQSVAEEAVAPVVEEtvaaepvVQEVPAPRTELVKVPLPVVAQTAPEQDEENNAENRDNngmprrsrrsprhlrvsgq 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 633 ----------PSAKPIDETSAKPVDE-PSEK-----PVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKPVEE 696
Cdd:PRK10811 810 rrrryrderyPTQSPMPLTVACASPEmASGKvwiryPVVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVE 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 697 PSSKPVEEPATDSASQEGEPM-VEPSAKPVEGASAEQATAQEPNEPAPAAAEAVSESVGAEPTGAVPEPAATEATKAEEQ 775
Cdd:PRK10811 890 AVAEVVEEPVVVAEPQPEEVVvVETTHPEVIAAPVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVV 969
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1944883863 776 KVEETPEIVKPAAGEKEAVAETVAETSPGSEKQGVTFHRDTVE 818
Cdd:PRK10811 970 VAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVE 1012
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
507-676 |
8.71e-10 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 63.07 E-value: 8.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 507 GASEDVTEALEKVLEEDKAAEEQKIEEQLPeetKADEKEPTVPAETAESVKDTAEEAKPEGQAEKPADV-----EEVKAI 581
Cdd:PRK13108 287 GSEYVVDEALEREPAELAAAAVASAASAVG---PVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVadrdgESTPAV 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 582 DQTAEPsaDQEKEQAAETT-EESAEQVVEAVGQVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPvDEPSEKPVDEPSAK 660
Cdd:PRK13108 364 EETSEA--DIEREQPGDLAgQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDP-AKPDELAVAGPGDD 440
|
170
....*....|....*..
gi 1944883863 661 P-DDEPSAKPDEEPSTK 676
Cdd:PRK13108 441 PaEPDGIRRQDDFSSRR 457
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
469-807 |
4.25e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 469 RKPATAEKKPEPKPSDEVPTEvsSEDVISATGEKLNIGGASEDVTEALEKVLEEDKAAEEQKIEEQLP--------EETK 540
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAadeaeaaeEKAE 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 541 ADEKEPTVPAETAESVKDTAEEAKPEGQAEKPADvEEVKAIDQTAEPSADQEKeqaAETTEESAEQVVEAvgqvvEPSTE 620
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE-EDKKKADELKKAAAAKKK---ADEAKKKAEEKKKA-----DEAKK 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 621 LAEEpsAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDE-----EPSTKPVEEpsAMPVEEPSSKPve 695
Cdd:PTZ00121 1439 KAEE--AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEakkkaEEAKKKADE--AKKAAEAKKKA-- 1512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 696 EPSSKPVEEPATDSASQEGEPMVEPSAKPVEGASAEQATAQEPNEPAPAAAEAVSESVGAEPTGAVPEPAATEATKAEEQ 775
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA 1592
|
330 340 350
....*....|....*....|....*....|..
gi 1944883863 776 KVEETPEIVKPAAGEKEAVAETVAETSPGSEK 807
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
549-735 |
7.72e-09 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 60.63 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 549 PAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEQVVEAVGqvVEPSTELAEEPSAK 628
Cdd:PRK07003 360 PAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRA--EAPPAAPAPPATAD 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 629 PVDEPSAKPidetSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKPVEEPSSKPVEEPATD 708
Cdd:PRK07003 438 RGDDAADGD----APVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAP 513
|
170 180
....*....|....*....|....*..
gi 1944883863 709 SASQEGEPMVEPSAKPVEGASAEQATA 735
Cdd:PRK07003 514 AAASREDAPAAAAPPAPEARPPTPAAA 540
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
509-971 |
9.53e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 9.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 509 SEDVTEALE-KVLEEDKAAEEQKIEEQLpeETKADEKEPTVPA-ETAESVKDTAEEAKPEG-QAEKPADVEEVKAIDQTA 585
Cdd:PTZ00121 1280 ADELKKAEEkKKADEAKKAEEKKKADEA--KKKAEEAKKADEAkKKAEEAKKKADAAKKKAeEAKKAAEAAKAEAEAAAD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 586 EPSADQEKEQAAETTEESAEQVVEAVGQVVEPSTELAE-----EPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAK 660
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEakkkaEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK 1437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 661 PDDEPSAKPDE---EPSTKPVEEPSAMPVEEpsSKPVEEPSSKPVEEPATDSASQEGEpmvEPSAKPVEGASAEQATAQE 737
Cdd:PTZ00121 1438 KKAEEAKKADEakkKAEEAKKAEEAKKKAEE--AKKADEAKKKAEEAKKADEAKKKAE---EAKKKADEAKKAAEAKKKA 1512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 738 PNEPAPAAAEAVSESVGAEptgavPEPAATEATKAEEQKVEEtpEIVKPAAGEKEAVAETVAETSPGSEKQGVTFHRdtV 817
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAE-----EAKKADEAKKAEEKKKAD--ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK--A 1583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 818 ETTGKSDHSSIKSPTKTPTSHRCGSVATSIFDENLLNSSQFVQIVEAFLGESPPEEVVQQLLKYLGEGYIETEEEKYLRL 897
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1944883863 898 QKSRREAQSAKRKLMLEQLFEKWDNDGSGYLDLEELHSVMSKFKENMEAKIMQKAKTImMKEEYDNRLSKREFK 971
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL-KKAEEENKIKAEEAK 1736
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
543-714 |
1.12e-08 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 59.22 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 543 EKEPTVPAETAESVKDTAEEAKPEGqaekPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEQVVEAVGQVVEPSTELA 622
Cdd:PRK13108 292 VDEALEREPAELAAAAVASAASAVG----PVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETS 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 623 EEPSAKPVDEpsakpidETSAKPVDEPSEkpvdepsakpDDEPSAKPDEEPSTKPVEEPSAmpvEEPSSKPVEEPSSKP- 701
Cdd:PRK13108 368 EADIEREQPG-------DLAGQAPAAHQV----------DAEAASAAPEEPAALASEAHDE---TEPEVPEKAAPIPDPa 427
|
170
....*....|....*....
gi 1944883863 702 ------VEEPATDSASQEG 714
Cdd:PRK13108 428 kpdelaVAGPGDDPAEPDG 446
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
546-735 |
1.68e-08 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 59.67 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 546 PTVPAETAESVkdtaEEAKPEGQAEKPAdVEEVKAIDQTAEPSADQEKEQAAETTEesaEQVVEAVGQVVEPSTELAEEP 625
Cdd:PRK10811 846 PVVRPQDVQVE----EQREAEEVQVQPV-VAEVPVAAAVEPVVSAPVVEAVAEVVE---EPVVVAEPQPEEVVVVETTHP 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 626 sakpvdEPSAKPIDEtsAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPS--SKPVEEPSSKPVE 703
Cdd:PRK10811 918 ------EVIAAPVTE--QPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEvvAQPAAPVVAEVAA 989
|
170 180 190
....*....|....*....|....*....|..
gi 1944883863 704 EPATDSASqegEPMVEPSAKPVEGASAEQATA 735
Cdd:PRK10811 990 EVETVTAV---EPEVAPAQVPEATVEHNHATA 1018
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
494-715 |
2.82e-08 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 58.64 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 494 DVISATGEKLN-IGGASEDVTEALEKVLEEDKAAEEQKIEEQLPEETKADEKEpTVPAETAESVKDTAEEAKPEGQAEK- 571
Cdd:PTZ00341 909 DAKDLSGNIAHeINLINKELKNQNENVPEHLKEHAEANIEEDAEENVEEDAEE-NVEENVEENVEENVEENVEENVEENv 987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 572 PADVEEvkAIDQTAEPSADQE-KEQAAETTEESAEQVVEAVGQVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPS 650
Cdd:PTZ00341 988 EENVEE--NVEENVEENIEENvEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYD 1065
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1944883863 651 EKPVD--EPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKPVEEPSSKPVEEPATDSASQEGE 715
Cdd:PTZ00341 1066 EENVEeiEENIEENIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENAEEYDDENPEEHNE 1132
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
452-721 |
5.62e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.03 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 452 RSLPgtPAAGSIAKGLDrkPATAEKKPEPKPSDEVPTEVSSEDVISATGEK--LNIGGASEDVTEALEKVLEEDKAAEEQ 529
Cdd:PHA03247 2686 RAAR--PTVGSLTSLAD--PPPPPPTPEPAPHALVSATPLPPGPAAARQASpaLPAAPAPPAVPAGPATPGGPARPARPP 2761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 530 KIEEQLPEETKADEKEPTVPAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQ---------EKEQAAETT 600
Cdd:PHA03247 2762 TTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASpagplppptSAQPTAPPP 2841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 601 EESAEQVVEAVGQVVEPSTELAEEPSAKPvdePSAKPidETSAKP----VDEPSEKPVDEPSAKPDDEPSAKPDEEPSTK 676
Cdd:PHA03247 2842 PPGPPPPSLPLGGSVAPGGDVRRRPPSRS---PAAKP--AAPARPpvrrLARPAVSRSTESFALPPDQPERPPQPQAPPP 2916
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1944883863 677 PVEEPSAMPVEEPSSKPVEEPSSKPVEEPATDSASQEGEPMVEPS 721
Cdd:PHA03247 2917 PQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQ 2961
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
441-724 |
9.17e-08 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 56.95 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 441 ELDSISEDSFVRSLPGTPAaGSIAKGLDRKPATAEKKPE-PKPSDEVPtevsSEDVISATGEKlniggASEDVTEALEKV 519
Cdd:NF033838 244 KLKEAVEKNVATSEQDKPK-RRAKRGVLGEPATPDKKENdAKSSDSSV----GEETLPSPSLK-----PEKKVAEAEKKV 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 520 LEEDKAAEEQKieeqlpEETKADEkePTVPAETAEsvkdtAEEAKPEGQAeKPADVEEVKaidQTAEPSADQEKEQAAET 599
Cdd:NF033838 314 EEAKKKAKDQK------EEDRRNY--PTNTYKTLE-----LEIAESDVKV-KEAELELVK---EEAKEPRNEEKIKQAKA 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 600 TEESAEQVVEAVGQVVEPSTELAEEPSAKPVDEPSAKpidetsakpvdepsEKPVDEPSAKPDDEPsakpdEEPSTKPvE 679
Cdd:NF033838 377 KVESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVK--------------EKPAEQPQPAPAPQP-----EKPAPKP-E 436
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1944883863 680 EPSAMP-VEEPSSKPVEEPSSKPVEEpATDSASQEGEPMVEPSAKP 724
Cdd:NF033838 437 KPAEQPkAEKPADQQAEEDYARRSEE-EYNRLTQQQPPKTEKPAQP 481
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
510-672 |
1.02e-07 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 57.10 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 510 EDVTEALEKVLEEDKaaeEQKIEEQLpEETKADEKEPTVPAETAESVKDTAEEAKPEGQAEKPADVEE-----VKAIDQT 584
Cdd:PTZ00341 973 ENVEENVEENVEENV---EENVEENV-EENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEydeenVEEIEEN 1048
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 585 AEPSADQEKEqaaETTEESAEQVVEAVGQVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDE 664
Cdd:PTZ00341 1049 AEENVEENIE---ENIEEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENAEEYDDE 1125
|
....*...
gi 1944883863 665 PSAKPDEE 672
Cdd:PTZ00341 1126 NPEEHNEE 1133
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
455-807 |
1.05e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 56.92 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 455 PGTPAAGSIAKGLDRK-PA------------TAEKKPEPKPSDEVPTEVSSEDVISATGEKLNIGGASEDVTEALEKVLE 521
Cdd:PRK07764 500 PAAPAGADDAATLRERwPEilaavpkrsrktWAILLPEATVLGVRGDTLVLGFSTGGLARRFASPGNAEVLVTALAEELG 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 522 EDKAaeeqkieeqlpeetkadekePTVPAETAESVKDtAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTE 601
Cdd:PRK07764 580 GDWQ--------------------VEAVVGPAPGAAG-GEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAE 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 602 ESAEQvveavgqvvePSTELAEEPSAKPVDEPSakPIDETSAKPVDEPSEKPVDEPSAkPDDEPSAKPDEEPSTKPVEEP 681
Cdd:PRK07764 639 ASAAP----------APGVAAPEHHPKHVAVPD--ASDGGDGWPAKAGGAAPAAPPPA-PAPAAPAAPAGAAPAQPAPAP 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 682 SAMPVEEPSSKPVEEPSSKPVEEPATDSASQEGEPMV-EPSAKPVEGASAEQAtaqepnepApaaaeavSESVGAEPTGA 760
Cdd:PRK07764 706 AATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPpEPDDPPDPAGAPAQP--------P-------PPPAPAPAAAP 770
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1944883863 761 VPEPAATEATKAEEQKVEETPEIVKPAAGEKEAVAETVAETSPGSEK 807
Cdd:PRK07764 771 AAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVAMELLEEELGAKK 817
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
434-833 |
1.45e-07 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 56.56 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 434 ELDEVTDELDSISEDSFVRSLPGTPAAGSIAKGLDRKPATAEKKPEPKPSDEVPTEVSSEDVISATGEKLNIGGASEDVT 513
Cdd:COG5271 555 ETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAE 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 514 EALEKVLEEDKAAEEQKIEEQLPEETKADEKEPTVpAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEK 593
Cdd:COG5271 635 DEAAEPETDASEAADEDADAETEAEASADESEEEA-EDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASEEAD 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 594 EQAAETTEESAEQVVEAVGQVVEPS-------------------TELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPV 654
Cdd:COG5271 714 AEEADTEADGTAEEAEEAAEEAESAdeeaaslpdeadaeeeaeeAEEAEEDDADGLEEALEEEKADAEEAATDEEAEAAA 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 655 DEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPS-----SKPVEEPSSKPVEEPATDSASQEGEPMVEPSAKPVEGAS 729
Cdd:COG5271 794 EEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEEtadeaLEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEH 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 730 AEQATAQEPNEPAPAAAEAVSESVGAEPTGAVPEPAATEATKAEEQKVEETPEIVKPAAGEKEAVAETVAETSPGSEKQG 809
Cdd:COG5271 874 EAEEAQEAETDADADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDELGAAEDDLDALALD 953
|
410 420
....*....|....*....|....
gi 1944883863 810 VTFHRDTVETTGKSDHSSIKSPTK 833
Cdd:COG5271 954 EAGDEESDDAAADDAGDDSLADDD 977
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
453-808 |
1.56e-07 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 56.18 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 453 SLPGTPAAGSIAKGLDRKPATAEKKPEPKPSDEVPTEVSSEDVISATGEKLNIGGASEDVTEALEKVLEEDKAAEEQKIE 532
Cdd:COG5271 276 DDADGLEAAEDDALDAELTAAQAADPESDDDADDSTLAALEGAAEDTEIATADELAAADDEDDDDSAAEDAAEEAATAED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 533 EQLPEETKADEKEPTVPAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEQVVEavg 612
Cdd:COG5271 356 SAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDE--- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 613 qvvepSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSK 692
Cdd:COG5271 433 -----STDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSD 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 693 PVEEPSSKPVEEPATDSASQEGEPMVEPSAKPVEGASAEQ---ATAQEPNEPAPAAAEAVSESVGAEPTGAVPEPAATEA 769
Cdd:COG5271 508 ELTAEETSADDGADTDAAADPEDSDEDALEDETEGEENAPgsdQDADETDEPEATAEEDEPDEAEAETEDATENADADET 587
|
330 340 350
....*....|....*....|....*....|....*....
gi 1944883863 770 TKAEEQKVEETPEIVKPAAGEKEAVAETVAETSPGSEKQ 808
Cdd:COG5271 588 EESADESEEAEASEDEAAEEEEADDDEADADADGAADEE 626
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
585-765 |
3.03e-07 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 55.43 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 585 AEPSADQEKEQAAETTEESAEQVVE----AVGQVVEPSTELAEEPSAKPVDEPSAKPIdETSAKPVDEPSEKPVDEPSak 660
Cdd:PRK10811 848 VRPQDVQVEEQREAEEVQVQPVVAEvpvaAAVEPVVSAPVVEAVAEVVEEPVVVAEPQ-PEEVVVVETTHPEVIAAPV-- 924
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 661 pDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKPVEEPSSKPVEEPATDSASQEGEPMVEPSAkPVEGASAEQATAQEPNE 740
Cdd:PRK10811 925 -TEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVA-EVAAEVETVTAVEPEVA 1002
|
170 180
....*....|....*....|....*
gi 1944883863 741 PAPAAAEAVSESVGAEPTGAVPEPA 765
Cdd:PRK10811 1003 PAQVPEATVEHNHATAPMTRAPAPE 1027
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
476-733 |
1.03e-06 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 53.23 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 476 KKPEPKPSDEVPTEVSSEDVISatgeklNIGGASEDVTEALEKVLEEDKAAEEQKIEEQLPE-----ETKADEKEPTVPA 550
Cdd:NF033839 241 KKQALSEIDNVNTKVEIENTVH------KIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKpgmqpSPQPEKKEVKPEP 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 551 ETA-ESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQ-AAETTEESAEQVVEAVGQVVEPSTELAEEPSAK 628
Cdd:NF033839 315 ETPkPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPKPEVKPQPEKpKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 629 pvdEPSAKPIDETSAKPVDEPSEKPvdEPSAKPDDEPsAKPDEEPSTkpvEEPSAMPVEEPSSKPVEEPSSKPVEEPATD 708
Cdd:NF033839 395 ---KPEVKPQPEKPKPEVKPQPEKP--KPEVKPQPEK-PKPEVKPQP---EKPKPEVKPQPEKPKPEVKPQPETPKPEVK 465
|
250 260
....*....|....*....|....*.
gi 1944883863 709 SASQEGEPMVEPS-AKPVEGASAEQA 733
Cdd:NF033839 466 PQPEKPKPEVKPQpEKPKPDNSKPQA 491
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
563-730 |
1.37e-06 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 52.67 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 563 AKPEGQaEKPadvEEVKAIDQTAEPSADQEKEQAAETTEESAEQVVEAVGQvVEPS-----TELAEEPSAKPVDEPSAKP 637
Cdd:PRK13108 274 LAPKGR-EAP---GALRGSEYVVDEALEREPAELAAAAVASAASAVGPVGP-GEPNqpddvAEAVKAEVAEVTDEVAAES 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 638 IDET------SAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKPVEEPSSKPVEEPATDSAS 711
Cdd:PRK13108 349 VVQVadrdgeSTPAVEETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAK 428
|
170
....*....|....*....
gi 1944883863 712 QEGEPMVEPSAKPVEGASA 730
Cdd:PRK13108 429 PDELAVAGPGDDPAEPDGI 447
|
|
| Cornifin |
pfam02389 |
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ... |
613-734 |
1.73e-06 |
|
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.
Pssm-ID: 280537 [Multi-domain] Cd Length: 135 Bit Score: 48.90 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 613 QVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSK 692
Cdd:pfam02389 4 QVKQPCQPPPQEPCVPTTKEPCHSKVPEPCNPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCYPKVPEPCSP 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1944883863 693 PV--------EEPSSKPVEEPATDSASQEGEPMV-EPSAKPVEGASAEQAT 734
Cdd:pfam02389 84 KVpepchpkaPEPCHPKVPEPCYPKAPEPCQPKVpEPCPSTVTPGPAQQKT 134
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
483-830 |
1.75e-06 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 52.71 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 483 SDEVPTEVSSEDVI----SATGEKLNIGGASEDVTEALEKVLEEDKAAEEQKIEEQLPEETKADEKEPTVPAETAESVKD 558
Cdd:COG5271 506 SDELTAEETSADDGadtdAAADPEDSDEDALEDETEGEENAPGSDQDADETDEPEATAEEDEPDEAEAETEDATENADAD 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 559 -TAEEAKPEGQAEKPAD--VEEVKAIDQTAEPSADQEKEQAAETTEESAEQVVEAVGQVVEPSTELAEEPSAKPVDEPSA 635
Cdd:COG5271 586 eTEESADESEEAEASEDeaAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEASADES 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 636 KPIDETSAKPVDEPSEKPVDEP--SAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKPvEEPSSKPVEEPATDSASQE 713
Cdd:COG5271 666 EEEAEDESETSSEDAEEDADAAaaEASDDEEETEEADEDAETASEEADAEEADTEADGTA-EEAEEAAEEAESADEEAAS 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 714 GEPMVEPSAKPVEGASAEQATAQEPNEPAPAAAEAVSESvgaePTGAVPEPAATEATKAEEQKVEETPEIVKPAAGEKEA 793
Cdd:COG5271 745 LPDEADAEEEAEEAEEAEEDDADGLEEALEEEKADAEEA----ATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEE 820
|
330 340 350
....*....|....*....|....*....|....*..
gi 1944883863 794 VAETVAETSPGSEKQGVTFHRDTVETTGKSDHSSIKS 830
Cdd:COG5271 821 EDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKD 857
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
471-643 |
1.80e-06 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 52.73 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 471 PATAEKKPEPKPSDEVPTEVSSEDVISATGEKLniggASEDVTEALEKVLEEDKAAEEqkieeqlPEETKADEKEPTVPA 550
Cdd:PRK10811 850 PQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPV----VSAPVVEAVAEVVEEPVVVAE-------PQPEEVVVVETTHPE 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 551 ETAESVkdtAEEAKPEGQAEKPADVEEVkaidQTAEPSA-DQEKEQAAETTEESAEQVVEAVGQVVEPSTELAEEPSAKP 629
Cdd:PRK10811 919 VIAAPV---TEQPQVITESDVAVAQEVA----EHAEPVVePQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEV 991
|
170
....*....|....
gi 1944883863 630 VDEPSAKPIDETSA 643
Cdd:PRK10811 992 ETVTAVEPEVAPAQ 1005
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
514-834 |
1.92e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 514 EALEKVLEEDKAAEEQKIEEQlpEETKADEKEPTVPAETAESVKdTAEEAKpegQAEKPADVEEVKAIDQT--------A 585
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAE--AKKKADEAKKAEEAKKADEAK-KAEEAK---KADEAKKAEEKKKADELkkaeelkkA 1560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 586 EPSADQEKEQAAETTEESAEQVVEAVGQV----VEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKP 661
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAeearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 662 DDEPSAKPDEEpsTKPVEEPSAMPVEEPSSKPVEEpssKPVEEPATDSASQEGEPMVEPSAKPVEGASAEQATAQEPNEP 741
Cdd:PTZ00121 1641 KEAEEKKKAEE--LKKAEEENKIKAAEEAKKAEED---KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 742 APAAAEAVSESVGAEPTGAVPEPAATEATKAEEQKVEEtpeivkpaaGEKEAVAETVAETSPGSEKQGVTFHRDTVETTG 821
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE---------EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
330
....*....|...
gi 1944883863 822 KSDHSSIKSPTKT 834
Cdd:PTZ00121 1787 EEDEKRRMEVDKK 1799
|
|
| DD_DPY30_SDC1-like |
cd22958 |
dimerization/docking (D/D) domain found in the DPY30/SDC1-like family; The DPY30/SDC1-like ... |
160-212 |
2.33e-06 |
|
dimerization/docking (D/D) domain found in the DPY30/SDC1-like family; The DPY30/SDC1-like family includes DPY30 from animals and its homolog SDC1 from yeast, DPY30 domain-containing protein (DYDC), adenylate kinase 7 (AK7), IQ domain-containing protein K (IQCK), nucleoside diphosphate kinase homolog 5 (NDKH5), EF-hand calcium-binding domain-containing protein 5 (EFCAB5), and Chlamydomonas reinhardtii flagellar radial spoke proteins, RSP2 and RSP23. DPY30, also called dumpy-30, was initially discovered in Caenorhabditis elegans as a key player in X chromosome dosage compensation. Human DPY30 plays a dual function in moderately allosterically regulating the methyltransferase activity of SET1/COMPASS (COMplex of Proteins ASsociated with Set1) enzymes and contributing to the recruitment of the complex to chromatin. Yeast SDC1, also called complex proteins associated with SET1 protein SDC1, Set1C component SDC1, or suppressor of CDC25 protein 1, is the smallest subunit of COMPASS (COMplex of Proteins ASsociated with Set1) and interacts exclusively with Bre2 at the distal end of the catalytic module. It positively regulates the COMPASS catalytic module by stabilizing the non-canonical Bre2 SPRY domain. DYDC1 plays a crucial role during acrosome biogenesis. AK7 (EC2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 7, is a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It is involved in maintaining ciliary structure and function. IQ motif-containing proteins may play an active role in cell polarization and migration, and even in ciliary function. The function of IQCK remains unclear. NDKH5, also called NME5, NDP kinase homolog 5, inhibitor of p53-induced apoptosis-beta (IPIA-beta), testis-specific nm23 homolog, or nm23-H5, is specifically expressed in testis germinal cells. It may not have NDK kinase activity. It confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes including Gpx5. It may play a role in spermiogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species. RSP2 is a calmodulin binding spoke stalk protein required for motility in Chlamydomonas reinhardtii. It binds calmodulin in a calcium-dependent manner. RSP23, also called p61, is a functional Ca2+/calmodulin-regulated nucleoside diphosphate kinase (NDK) from the flagella of Chlamydomonas that is present in the radial spoke stalk. It binds calmodulin in a calcium-dependent manner. Members of this family contain a DPY30/SDC1 helical bundle domain that is formed by two alpha-helices. The DPY30/SDC1 helical bundle domain is also called D/D domain and might be analogous to the D/D domain found in the regulatory subunit of cAMP-dependent protein kinase (PKA).
Pssm-ID: 438527 Cd Length: 40 Bit Score: 45.51 E-value: 2.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1944883863 160 ARAYLLDKLLPTLILGIEKLLMEAEKrglaesneadpnfNPINFLGQYLMRNN 212
Cdd:cd22958 1 AREYLSETVLPTLIPALAELLKARPE-------------DPLEWLAEYLLRNN 40
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
464-968 |
2.47e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 464 AKGLDRKPATAEKKPEPKPSDEvptevssedviSATGEKLNiggASEDVTEALE-KVLEEDKAAEEQKieEQLPEETKAD 542
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEA-----------EAAADEAE---AAEEKAEAAEkKKEEAKKKADAAK--KKAEEKKKAD 1394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 543 EKEptvpaETAESVKDTAEEAKPEGQAEKPAD-----VEEVKAIDQTAEPSADQEKEQAAETTEESAEQVVEAVGQV--- 614
Cdd:PTZ00121 1395 EAK-----KKAEEDKKKADELKKAAAAKKKADeakkkAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAeea 1469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 615 --VEPSTELAEEpsAKPVDEpsAKPIDETSAKPVDEPSEKpvDEPSAKPDD----EPSAKPDE----EPSTKPVEEPSAM 684
Cdd:PTZ00121 1470 kkADEAKKKAEE--AKKADE--AKKKAEEAKKKADEAKKA--AEAKKKADEakkaEEAKKADEakkaEEAKKADEAKKAE 1543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 685 PVEEPSSKPVEEPSSKPVEEPATDSASQEGEPMVEPSAKPVEGASAEQATAQEPNEPAPAAAEAVSESVGAEPTGAVpep 764
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI--- 1620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 765 AATEATKAEEQKveETPEIVKPAAGEKEAVAETVAETSPGSEKQGVTFHRDTVETTGKSDHSSIKSPTKTPTShrcgsva 844
Cdd:PTZ00121 1621 KAEELKKAEEEK--KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA------- 1691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 845 tsifdENLLNSSQFVQIVEAfLGESPPEEVVQqllkylGEGYIETEEEKYLRLQKSRREAQSAKRKlmLEQLfekwdndg 924
Cdd:PTZ00121 1692 -----EALKKEAEEAKKAEE-LKKKEAEEKKK------AEELKKAEEENKIKAEEAKKEAEEDKKK--AEEA-------- 1749
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1944883863 925 sgYLDLEELHSVMS-KFKENMEAKIMQKAKTIMMKEEYDNRLSKR 968
Cdd:PTZ00121 1750 --KKDEEEKKKIAHlKKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
510-627 |
2.93e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 51.94 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 510 EDVTEALEKVleEDKAAEEQKIEEQLPEETKADEKEPTVPAETAESVKDTAEEAKPEG--QAEKPADVEEVKAIDQTAEP 587
Cdd:NF033838 369 EKIKQAKAKV--ESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPapQPEKPAPKPEKPAEQPKAEK 446
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1944883863 588 SADQekeQAAETTEESAEQVVEAVGQVVEPSTELAEEPSA 627
Cdd:NF033838 447 PADQ---QAEEDYARRSEEEYNRLTQQQPPKTEKPAQPST 483
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
912-974 |
3.90e-06 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 45.62 E-value: 3.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1944883863 912 MLEQLFEKWDNDGSGYLDLEELHSVMSKFKENMEAKIMQKaktiMMKE---EYDNRLSKREFKAYI 974
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDE----MIREvdkDGDGKIDFEEFLELM 62
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
506-731 |
4.19e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 51.12 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 506 GGASEDVTEALEKVLEEDKAAEEQKIEEQlpEETKADEKEPTvpaetaesvkdtaEEAKPEGQAEKPADVEEvkaidqtA 585
Cdd:PHA03169 48 PPAPTTSGPQVRAVAEQGHRQTESDTETA--EESRHGEKEER-------------GQGGPSGSGSESVGSPT-------P 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 586 EPSADQEkEQAAETTEESAEQVVEAvgqvvepSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEP 665
Cdd:PHA03169 106 SPSGSAE-ELASGLSPENTSGSSPE-------SPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1944883863 666 SAKPDEEPstkpveEPSAmpvEEPSSKPVEEPSSKPVEEPATDSASQEGEPMVEPSAKPVEGASAE 731
Cdd:PHA03169 178 PEPPTSEP------EPDS---PGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHE 234
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
545-767 |
5.11e-06 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 51.03 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 545 EPTVPAETAESVKDTAEEAKPEGQAEkPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEQVVEAVGQVVEPSTELAEE 624
Cdd:PRK12323 371 GAGPATAAAAPVAQPAPAAAAPAAAA-PAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 625 PSAKPVDEPSAkpideTSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPsaMPVEEPSSKPVE-EPSSKPVE 703
Cdd:PRK12323 450 PAPAPAAAPAA-----AARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEE--LPPEFASPAPAQpDAAPAGWV 522
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1944883863 704 -EPATDSASQEGEPMVEPSAKPVEGASAEQATAQEPNEPAPAAAEAVSESVGAEPTGAVPEPAAT 767
Cdd:PRK12323 523 aESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPALAAR 587
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
526-808 |
6.05e-06 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 50.83 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 526 AEEQKIEEQlPEETKADEKEPTVPAETAESVK-DTAEEAKPEGQAEKPADVEE---VKAIDQTAEPSADQEKEQAAETTE 601
Cdd:pfam04747 124 AEQERIQKE-QEKKEADLKKLQAEKKKEKAVKaEKAEKAEKTKKASTPAPVEEeivVKKVANDRSAAPAPEPKTPTNTPA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 602 ESAEQVVEAVGQVVEPSTELAE-EPSAKPVdepSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEP--STKPV 678
Cdd:pfam04747 203 EPAEQVQEITGKKNKKNKKKSEsEATAAPA---SVEQVVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPaaSETPV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 679 EE------PSAMPVEEPSSKPVEEPSSKPVEEPATDSASQEGEPMVEPSAKPVEGASAEQATAQEPNEPAPAAAEAVSES 752
Cdd:pfam04747 280 EPvvettpPASENQKKNKKDKKKSESEKVVEEPVQAEAPKSKKPTADDNMDFLDFVTAKEEPKDEPAETPAAPVEEVVEN 359
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1944883863 753 VGAEPTGAVPEPAATE--------ATKAEEQKVEETPEIVKPAAGEKEAVAETVAETSPGSEKQ 808
Cdd:pfam04747 360 VVENVVEKSTTPPATEnkkknkkdKKKSESEKVTEQPVESAPAPPQVEQVVETTPPASENKKKN 423
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
534-768 |
1.09e-05 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 50.47 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 534 QLPEETKADEKEPTVPAETAESVKDTAEE-----AKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEqvv 608
Cdd:PRK10263 367 QTGEPVIAPAPEGYPQQSQYAQPAVQYNEplqqpVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVA--- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 609 EAVGQVVEPSTELAEEPSAKP---VDEPSAKPIDETSAKPVDEPsekPVDEPSAKPDDEPSAKPD-------EEPSTKPV 678
Cdd:PRK10263 444 GNAWQAEEQQSTFAPQSTYQTeqtYQQPAAQEPLYQQPQPVEQQ---PVVEPEPVVEETKPARPPlyyfeevEEKRARER 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 679 EEPSA--MPVEEPSSKPVEEPSSKPVEEPATDSASqEGEPMVEPSAKPVEGASAEQATAqepnepapaaaEAVSESVGAE 756
Cdd:PRK10263 521 EQLAAwyQPIPEPVKEPEPIKSSLKAPSVAAVPPV-EAAAAVSPLASGVKKATLATGAA-----------ATVAAPVFSL 588
|
250
....*....|..
gi 1944883863 757 PTGAVPEPAATE 768
Cdd:PRK10263 589 ANSGGPRPQVKE 600
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
514-796 |
1.31e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 514 EALEKVLEEDKAAEEQKIEEQlpeeTKADEKEPTVPAETAESVKDTAEEAKpegQAEKPADVEEVKAIDQTaePSADQEK 593
Cdd:PTZ00121 1197 EDARKAEAARKAEEERKAEEA----RKAEDAKKAEAVKKAEEAKKDAEEAK---KAEEERNNEEIRKFEEA--RMAHFAR 1267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 594 EQAAETTEES--AEQVVEAvgQVVEPSTELAEEPSAKPVDEPSAKPIDETSA---KPVDEPSEKPVDEPSAKPDD----- 663
Cdd:PTZ00121 1268 RQAAIKAEEArkADELKKA--EEKKKADEAKKAEEKKKADEAKKKAEEAKKAdeaKKKAEEAKKKADAAKKKAEEakkaa 1345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 664 -----EPSAKPDEEPSTKPVEEPSAMPVEEpSSKPVEEPSSKPVEEPATDSASQEGEPMvEPSAKPVEGASAEQATAQEP 738
Cdd:PTZ00121 1346 eaakaEAEAAADEAEAAEEKAEAAEKKKEE-AKKKADAAKKKAEEKKKADEAKKKAEED-KKKADELKKAAAAKKKADEA 1423
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1944883863 739 NEPAPAAAEAVSESVGAEPTGAVPE--PAATEATKAEE--QKVEET--PEIVKPAAGEKEAVAE 796
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEakKKAEEAKKAEEakKKAEEAkkADEAKKKAEEAKKADE 1487
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
434-811 |
1.41e-05 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 50.01 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 434 ELDEVTDELDSISEDSFVRSLPGTPAAGSIAKGLDRKPATAEKKPEPKPSDEVPtevSSEDVISATGEKLNIGGASEDVT 513
Cdd:COG5271 384 AADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVT---SAEDDIATDEEADSLADEEEEAE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 514 EALEKVLEEDKAAEEQKIEEQLPEETKADEKEPTVPAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEK 593
Cdd:COG5271 461 AELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGADTDAAADPEDSDEDALEDET 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 594 EQAAET----TEESAEQVVEAVGQVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPS--- 666
Cdd:COG5271 541 EGEENApgsdQDADETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADAdad 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 667 -AKPDEEPSTKPVEEPSAMPVEEPSSKPVEEPSSKPVEEPATDS----ASQEGEPMVEPSAKPVEGASAEQATAQEPNEP 741
Cdd:COG5271 621 gAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEASADEseeeAEDESETSSEDAEEDADAAAAEASDDEEETEE 700
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 742 APAAAEAVSESVGAEPTGAVPEPAATEATKAEEQKVEETPEIVKPAAGEKEAVAETVAETSPGSEKQGVT 811
Cdd:COG5271 701 ADEDAETASEEADAEEADTEADGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLE 770
|
|
| FimV |
COG3170 |
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures]; |
462-721 |
1.47e-05 |
|
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];
Pssm-ID: 442403 [Multi-domain] Cd Length: 508 Bit Score: 49.41 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 462 SIAKGLDRKPATAEKKP-EPKPSDEVPTEVSSEDVISATGEKLNIGGASEDVTEALEKVLEEDKAAEE--QKIEEQLPEE 538
Cdd:COG3170 229 DWAAYRARLAAAVEPAPaAAAPAAPPAAAAAAGPVPAAAEDTLSPEVTAAAAAEEADALPEAAAELAErlAALEAQLAEL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 539 TKADEKEPTVPAE-----TAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAE-QVVEAVG 612
Cdd:COG3170 309 QRLLALKNPAPAAavsapAAAAAAATVEAAAPAAAAQPAAAAPAPALDNPLLLAGLLRRRKAEADEVDPVAEaDVYLAYG 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 613 QVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPS-EKPVDEPSAKPDDEPSAKPDEEPSTKPVEE--PSAMPVEEP 689
Cdd:COG3170 389 RDDQAEEILKEALASEPERLDLRLKLLEIYAARGDRAAfEALAAELYALTGGGRALDPDNPLYAPGAAAaaEDAPAAEAE 468
|
250 260 270
....*....|....*....|....*....|....*
gi 1944883863 690 SSKPVEEPSSKPVEEPA---TDSASQEGEPMVEPS 721
Cdd:COG3170 469 DDSPAEEPAASAAAAAElgdEEGARELLEEVLAEG 503
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
643-808 |
2.05e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 49.09 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 643 AKPVDEPSEKPVDEPSAkpddePSAKPDEEPSTKPVEEPSAMPVEEPSSKPVEEPSSKPVEEPATDSASQEGEPMVEPSA 722
Cdd:PRK07994 362 AAPLPEPEVPPQSAAPA-----ASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGAT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 723 KPVEGASAEQATAQEPNEPAPAAAEAVSESVGAEPTGAVPEPAATEATKAEEQKVEE--TPEIVKPAAgEKEAVAETVAE 800
Cdd:PRK07994 437 KAKKSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPvaTPKALKKAL-EHEKTPELAAK 515
|
....*...
gi 1944883863 801 TSPGSEKQ 808
Cdd:PRK07994 516 LAAEAIER 523
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
514-672 |
2.73e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.26 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 514 EALEKVLEEDKAAEEQKIEEQLPEETKADEKEptvpAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEK 593
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQKQAAEQERLKQLEKE----RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEA 153
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1944883863 594 EQAAETTEESAEqvveavgqvvEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEE 672
Cdd:PRK09510 154 KRAAAAAKKAAA----------EAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAE 222
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
625-707 |
3.03e-05 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 46.92 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 625 PSAKPVDEpSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKPveEPSSKPVEE 704
Cdd:PRK11633 64 PTQPPEGA-AEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAPPAP--KPEPKPVVE 140
|
...
gi 1944883863 705 PAT 707
Cdd:PRK11633 141 EKA 143
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
468-711 |
3.23e-05 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 48.61 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 468 DRKPATAEKKPEPKPSDEVPtevssedvisatgeklniggaSEDVTEALEKVLEEDKAAEEQKIEEQLPEETKADEKEPT 547
Cdd:NF033839 320 EVKPQLEKPKPEVKPQPEKP---------------------KPEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 548 VPAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEQvveavgqvvePSTELAEEPSA 627
Cdd:NF033839 379 QPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEK----------PKPEVKPQPEK 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 628 KpvdEPSAKPIDETSAKPVDEPSEKPVDE-----PSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKpvEEPSSKPV 702
Cdd:NF033839 449 P---KPEVKPQPETPKPEVKPQPEKPKPEvkpqpEKPKPDNSKPQADDKKPSTPNNLSKDKQPSNQASTN--EKATNKPK 523
|
250
....*....|
gi 1944883863 703 EE-PATDSAS 711
Cdd:NF033839 524 KSlPSTGSIS 533
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
471-609 |
3.45e-05 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 48.50 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 471 PATAEKKPEPKPSDEVPTEVSSEDVISATgeklniggasedVTEALEKVLEEDKAAEEQKIEEQLPEETKADEKEPTVPA 550
Cdd:PRK10811 895 VEEPVVVAEPQPEEVVVVETTHPEVIAAP------------VTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEA 962
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1944883863 551 ETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPsadqekeqaAETTEESAEQVVE 609
Cdd:PRK10811 963 AETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEP---------EVAPAQVPEATVE 1012
|
|
| PRK14960 |
PRK14960 |
DNA polymerase III subunit gamma/tau; |
473-618 |
4.04e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237868 [Multi-domain] Cd Length: 702 Bit Score: 48.12 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 473 TAEKKPEPKPSDEvPTEVSSEDVISATGEKLNIGGASEDVTEALEKVLEEDKAAEEQKIEEQLPEETKADEKEPTvPAET 552
Cdd:PRK14960 427 EPEPEPEPEPEPE-PEPQPNQDLMVFDPNHHELIGLESAVVQETVSVLEEDFIPVPEQKLVQVQAETQVKQIEPE-PAST 504
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1944883863 553 AESVkdtaeeAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAEtteesaeqVVEAVGQVVEPS 618
Cdd:PRK14960 505 AEPI------GLFEASSAEFSLAQDTSAYDLVSEPVIEQQSLVQAE--------IVETVAVVKEPN 556
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
622-702 |
4.37e-05 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 46.53 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 622 AEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPsampveEPSSKPVEEPSSKP 701
Cdd:PRK11633 72 AEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAPPAP------KPEPKPVVEEKAAP 145
|
.
gi 1944883863 702 V 702
Cdd:PRK11633 146 T 146
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
614-803 |
4.75e-05 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 48.16 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 614 VVEPSTELAEEPSAKPVDEPSAKPIDETSAKP-VDEPSEKPVDEPSAKP---DDEPSAKPDEEPST-KPVEEPSAMPVEE 688
Cdd:PRK10263 316 ITEPVAVAAAATTATQSWAAPVEPVTQTPPVAsVDVPPAQPTVAWQPVPgpqTGEPVIAPAPEGYPqQSQYAQPAVQYNE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 689 PSSKPVEEPSSKPVEEPATDSASQEGEPMVEPSAKPVEGASAEQATAQEPNEPAPAAAEAVSESVGAEPTGAVPEPAATE 768
Cdd:PRK10263 396 PLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQE 475
|
170 180 190
....*....|....*....|....*....|....*
gi 1944883863 769 ATKAEEQKVEEtpeivkPAAGEKEAVAETVAETSP 803
Cdd:PRK10263 476 PLYQQPQPVEQ------QPVVEPEPVVEETKPARP 504
|
|
| PRK12495 |
PRK12495 |
hypothetical protein; Provisional |
584-688 |
6.07e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 183558 [Multi-domain] Cd Length: 226 Bit Score: 46.02 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 584 TAEPSADQEKEQAAETTEESAEQVVEAVGQVVEPStelAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPV-DEPSAKPD 662
Cdd:PRK12495 69 TEDGAAGDDAGDGAEATAPSDAGSQASPDDDAQPA---AEAEAADQSAPPEASSTSATDEAATDPPATAAArDGPTPDPT 145
|
90 100
....*....|....*....|....*.
gi 1944883863 663 DEPsAKPDEEPSTKPVEEPSAMPVEE 688
Cdd:PRK12495 146 AQP-ATPDERRSPRQRPPVSGEPPTP 170
|
|
| ftsN |
TIGR02223 |
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ... |
471-635 |
6.13e-05 |
|
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis. [Cellular processes, Cell division]
Pssm-ID: 274041 [Multi-domain] Cd Length: 298 Bit Score: 46.61 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 471 PATAEKKPEPKPSDEVPTEVSSEDVISATGEKLNIGGASEDVTE--ALEKVLEEDKAAEEQKIEEQLPEETKADEKEPTV 548
Cdd:TIGR02223 70 ETAADLPPKPEERWSYIEELEAREVLINDPEEPSNGGGVEESAQltAEQRQLLEQMQADMRAAEKVLATAPSEQTVAVEA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 549 PAETAESVKD---TAEEAKPEGQAEKPADVEEVKAIDQTAEPsadqekeqaaettEESAEQVVEAVGQVVEPSTELAEEP 625
Cdd:TIGR02223 150 RKQTAEKKPQkarTAEAQKTPVETEKIASKVKEAKQKQKALP-------------KQTAETQSNSKPIETAPKADKADKT 216
|
170
....*....|
gi 1944883863 626 SAKPVDEPSA 635
Cdd:TIGR02223 217 KPKPKEKAER 226
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
674-836 |
6.26e-05 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 47.28 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 674 STKPVEEPSAMPVEEPSSKPVEEPssKPVEEPATDSASQEGE-PMVEP--SAKPVEGASAEQATAQEPNEPAPAAAEAVS 750
Cdd:PRK13108 275 APKGREAPGALRGSEYVVDEALER--EPAELAAAAVASAASAvGPVGPgePNQPDDVAEAVKAEVAEVTDEVAAESVVQV 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 751 ESVGAEPTGAV----------PEPAATEATKAEEQKVEETPEIVKPAAGEKEAVAETVAETSPGSEKQgvtfhrDTVETT 820
Cdd:PRK13108 353 ADRDGESTPAVeetseadierEQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKA------APIPDP 426
|
170
....*....|....*.
gi 1944883863 821 GKSDHSSIKSPTKTPT 836
Cdd:PRK13108 427 AKPDELAVAGPGDDPA 442
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
606-805 |
7.36e-05 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 47.23 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 606 QVVEAVGQVVEPSTE----LAEEPSAKPvdePSAKPIDETSAKPVdePSEKPVDEPSAKPDDEPSAKPdEEPSTKPVEEP 681
Cdd:PLN03209 301 KVVEVIAETTAPLTPmeelLAKIPSQRV---PPKESDAADGPKPV--PTKPVTPEAPSPPIEEEPPQP-KAVVPRPLSPY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 682 SAMPVEEPSSKPVE-EPSSKPVEEPATDSASQEGEPMVEPSAKPVEGASAEQATAQEPNEPAPAAAEAVSESVgAEPTGA 760
Cdd:PLN03209 375 TAYEDLKPPTSPIPtPPSSSPASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYARYEDL-KPPTSP 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1944883863 761 VPEP-AATEATKAEEQKVEETPEiVKPAAGEKEAVAETVAETSPGS 805
Cdd:PLN03209 454 SPTApTGVSPSVSSTSSVPAVPD-TAPATAATDAAAPPPANMRPLS 498
|
|
| EFh_PRIP |
cd16206 |
EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); ... |
913-980 |
8.90e-05 |
|
EF-hand motif found in phospholipase C-related but catalytically inactive proteins (PRIP); This family represents a class of metazoan phospholipase C related, but catalytically inactive proteins (PRIP), which belong to a group of novel inositol 1,4,5-trisphosphate (InsP3) binding protein. PRIP has a primary structure and domain architecture, incorporating a pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain with highly conserved X- and Y-regions split by a linker sequence, and a C-terminal C2 domain, similar to phosphoinositide-specific phospholipases C (PI-PLC, EC 3.1.4.11)-delta isoforms. Due to replacement of critical catalytic residues, PRIP do not have PLC enzymatic activity. PRIP consists of two subfamilies, PRIP-1(also known as p130 or PLC-L1), which is predominantly expressed in the brain, and PRIP-2 (also known as PLC-L2), which exhibits a relatively ubiquitous expression. Experiments show both, PRIP-1 and PRIP-2, are involved in InsP3-mediated calcium signaling pathway and GABA(A)receptor-mediated signaling pathway. In addition, PRIP-2 acts as a negative regulator of B-cell receptor signaling and immune responses.
Pssm-ID: 320036 [Multi-domain] Cd Length: 143 Bit Score: 44.12 E-value: 8.90e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 913 LEQLFEKWDNDGSGYLDLEELHSVMSKFKENM-EAKIMQKAKTIMMKEE-YDNRLSKREFkayIEAVCSM 980
Cdd:cd16206 2 LESVFEEADTNKSGFLDEEEAVQLIKQLNPGLsTSRIKQKLKELQKKKDgARGRVSSDEF---VELFKEL 68
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
510-651 |
9.05e-05 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 47.47 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 510 EDVTEALEKVLEEDKaaeEQKIEEQLPE--ETKADEKEPTVPAETAESVKDTAEEAKPEGQAEKPADVEE------VKAI 581
Cdd:PTZ00341 985 ENVEENVEENVEENV---EENIEENVEEnvEENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEEnveeniEENI 1061
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1944883863 582 DQTAEPSADQEKEQAAETTEESAEQVVEAVGQVVEPSTEL-----AEEPSAKPVDEPSAKPIDETSAKPVDEPSE 651
Cdd:PTZ00341 1062 EEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEEnveenAEENAEENAEENAEEYDDENPEEHNEEYDE 1136
|
|
| Neisseria_TspB |
pfam05616 |
Neisseria meningitidis TspB protein; This family consists of several Neisseria meningitidis ... |
557-727 |
9.59e-05 |
|
Neisseria meningitidis TspB protein; This family consists of several Neisseria meningitidis TspB virulence factor proteins.
Pssm-ID: 283306 [Multi-domain] Cd Length: 517 Bit Score: 47.01 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 557 KDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAET-------TEESAE--QVVEAVGQVVEPST----ELAE 623
Cdd:pfam05616 247 KEEMDAKKLEEILSLKVDADPDKYIEATGYPGYSEKVEVAPGTkvnmgpvTDRNGNpvQVAATFGRDAQGNTtadvQVIP 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 624 EPSAKP--VDEPSAKPIDETSakpvdePSEKPVDEPSakpddepsakPDEEPSTKPVEEPsampveepsskpveEPSSKP 701
Cdd:pfam05616 327 RPDLTPasAEAPHAQPLPEVS------PAENPANNPD----------PDENPGTRPNPEP--------------DPDLNP 376
|
170 180
....*....|....*....|....*.
gi 1944883863 702 VEEPATDsasqeGEPMVEPSAKPVEG 727
Cdd:pfam05616 377 DANPDTD-----GQPGTRPDSPAVPD 397
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
472-616 |
9.92e-05 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 47.34 E-value: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 472 ATAEKKPEPKPSDEVPTEVSSEDVISATGEKlnigGASEDVTEALEKVLEEDKAAEEQKIEEQLP--EETKADEKEPTVP 549
Cdd:PRK10811 876 AAAVEPVVSAPVVEAVAEVVEEPVVVAEPQP----EEVVVVETTHPEVIAAPVTEQPQVITESDVavAQEVAEHAEPVVE 951
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1944883863 550 AETAESVKDTAEEAKPEGQAEKPADVEEVkaidqtAEPSADQEKEQAAETTEESAEQVVEAVGQVVE 616
Cdd:PRK10811 952 PQDETADIEEAAETAEVVVAEPEVVAQPA------APVVAEVAAEVETVTAVEPEVAPAQVPEATVE 1012
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
585-730 |
1.07e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 46.78 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 585 AEPSADQekeQAAETTEESAEQVVEAVGQVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDE 664
Cdd:PRK07994 366 PEPEVPP---QSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKSE 442
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1944883863 665 PSAKPDEEPSTKPVEepsamPVEEPSSKPVEEPSSKPVEEPATDSASQEGEPMVEPSAKPVEGASA 730
Cdd:PRK07994 443 PAAASRARPVNSALE-----RLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKA 503
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
461-707 |
1.09e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 46.91 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 461 GSIAKGLDRKPATAEKKPEPKPSDEVPTEVSSEDV--ISATGEKLNIGGASEDVTEALEKVLEEDKAAEEQKIEEQlpEE 538
Cdd:TIGR00927 660 GEESGGEAEQEGETETKGENESEGEIPAERKGEQEgeGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETG--EE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 539 TKADEKEPTVPAETAESVKDTAEEAKPEGQAEKPADVEEVkaiDQTAEPSADQEKEQAAETTEESAEQVVEAVGQVVEPS 618
Cdd:TIGR00927 738 GEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKED---EDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDE 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 619 TELAEEPSAKPVDEPSAKPIDETSAKPVDEPS--EKPVD--EPSAKPDDEPSAKPDEEPSTKPVEEPSampvEEPSSKPV 694
Cdd:TIGR00927 815 HEGQSETQADDTEVKDETGEQELNAENQGEAKqdEKGVDggGGSDGGDSEEEEEEEEEEEEEEEEEEE----EEEEEEEN 890
|
250
....*....|...
gi 1944883863 695 EEPSSkpVEEPAT 707
Cdd:TIGR00927 891 EEPLS--LEWPET 901
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
617-832 |
1.33e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 46.41 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 617 PSTELAEEPSAKPVDEPSAKPIDETSA-KPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKPVE 695
Cdd:PRK12323 365 PGQSGGGAGPATAAAAPVAQPAPAAAApAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGP 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 696 EPSSKPVEEPATDSASQEGEPMVEPSAKPVEGASAEQATAQEPNEPAPAAAEAVSESVGAEPtgAVPEPAATEATKAEeq 775
Cdd:PRK12323 445 GGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEF--ASPAPAQPDAAPAG-- 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1944883863 776 kvEETPEIVKPAAGEKEAVAETVAETSPGSEKQGVTFHRDTVETTGKSDHSSIKSPT 832
Cdd:PRK12323 521 --WVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPD 575
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
1094-1186 |
1.43e-04 |
|
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.
Pssm-ID: 214500 [Multi-domain] Cd Length: 149 Bit Score: 43.52 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 1094 FRDMKGISFTSVDTGKPIHVPRVQNHGNimFWNPDRSEEDRQGSFIVIPLKDHRkRVFGVLGVDTLNDPQEksiFITHEI 1173
Cdd:smart00065 52 FPLDEGLAGRVAETGRPLNIPDVEADPL--FAEDLLGRYQGVRSFLAVPLVADG-ELVGVLALHNKKSPRP---FTEEDE 125
|
90
....*....|...
gi 1944883863 1174 SFFQGVAKAFSSA 1186
Cdd:smart00065 126 ELLQALANQLAIA 138
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
540-713 |
1.47e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 46.40 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 540 KADEKEPTVPAETAESVKDTAEEAKPEGQAEKPADVEEVKAidQTAEPSAdqekeQAAETTEESAEQVVEAVGQVVEPSt 619
Cdd:PRK07994 362 AAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPP--PASAPQQ-----APAVPLPETTSQLLAARQQLQRAQ- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 620 ELAEEPSAKPVDEPSAKPidetsAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKPV--EEP 697
Cdd:PRK07994 434 GATKAKKSEPAAASRARP-----VNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKAleHEK 508
|
170
....*....|....*.
gi 1944883863 698 SSKPVEEPATDSASQE 713
Cdd:PRK07994 509 TPELAAKLAAEAIERD 524
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
615-839 |
1.50e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 46.70 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 615 VEPSTELAEEPSAKPVDEPSAKPIDETSAKPvdEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKPV 694
Cdd:PHA03307 70 GPPPGPGTEAPANESRSTPTWSLSTLAPASP--AREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 695 EEPSSKPVEEPATDSASQEGEPmvePSAKPVegASAEQATAQEPNepapaaaeavseSVGAEPTGAVPePAATEATKAEE 774
Cdd:PHA03307 148 PAASPPAAGASPAAVASDAASS---RQAALP--LSSPEETARAPS------------SPPAEPPPSTP-PAAASPRPPRR 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1944883863 775 QKVEETPEIVKPAAGEKEAVAETVAETSPGSEKQGVTFHRDTVETTGKSDHSSIKSPTKTPTSHR 839
Cdd:PHA03307 210 SSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASG 274
|
|
| PRK08691 |
PRK08691 |
DNA polymerase III subunits gamma and tau; Validated |
473-807 |
1.53e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 46.24 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 473 TAEKKPEPKPSDE---VPTEVSSEDVISATGeklniggasedvtealeKVLEEDKAAEEQKIEEQLPEETKADEKEPTVP 549
Cdd:PRK08691 389 TAAKKPQPRPEAEtaqTPVQTASAAAMPSEG-----------------KTAGPVSNQENNDVPPWEDAPDEAQTAAGTAQ 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 550 AeTAESVKDTAEEAKPegqaeKPADVEEVKAID-QTAEPSADQEKEQAAETTEESaeQVVEAVGQVVEPSTELAEEPSAK 628
Cdd:PRK08691 452 T-SAKSIQTASEAETP-----PENQVSKNKAADnETDAPLSEVPSENPIQATPND--EAVETETFAHEAPAEPFYGYGFP 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 629 PVDEPsakPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKpvEEPSAMPVEEPSSKPVEEPSSK--PVEEPA 706
Cdd:PRK08691 524 DNDCP---PEDGAEIPPPDWEHAAPADTAGGGADEEAEAGGIGGNNTP--SAPPPEFSTENWAAIVRHFARKlgAAQMPA 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 707 TDSASQEgepmVEPSAKPVEGASAEQATAQEPNEPAPAAAEAVSESVGAEPTGAVpepaateaTKAEEQKVEETPEIV-K 785
Cdd:PRK08691 599 QHSAWTE----YHPDTGLMVLAMTAEARATADKKRLDKIRDTLAQAYGLQLTLQT--------QDWRDEAGRETPAMQdK 666
|
330 340
....*....|....*....|..
gi 1944883863 786 PAAGEKEAVAETVAETSPGSEK 807
Cdd:PRK08691 667 RVQAEDRQKAQALLEADPAAQK 688
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
571-694 |
1.56e-04 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 44.99 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 571 KPADVEEVKAIDQTAEPSADQEKEQAAEtteesAEQVVEAVGQVVEPSTELAEEPSAKPvdEPsakpidetsaKPVDEPS 650
Cdd:PRK11633 46 KPGDRDEPDMMPAATQALPTQPPEGAAE-----AVRAGDAAAPSLDPATVAPPNTPVEP--EP----------APVEPPK 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1944883863 651 EKPVDEPSAKPDDEPSAKPDEEPstKPVEEpsamPVEEPSSKPV 694
Cdd:PRK11633 109 PKPVEKPKPKPKPQQKVEAPPAP--KPEPK----PVVEEKAAPT 146
|
|
| PT |
pfam04886 |
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a ... |
640-675 |
1.65e-04 |
|
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat.
Pssm-ID: 282710 [Multi-domain] Cd Length: 36 Bit Score: 40.15 E-value: 1.65e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1944883863 640 ETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPST 675
Cdd:pfam04886 1 QPTAQPTAQPTVQPTGQPTAQPTDQPTAQPTDAPTA 36
|
|
| PRK14949 |
PRK14949 |
DNA polymerase III subunits gamma and tau; Provisional |
483-781 |
1.76e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237863 [Multi-domain] Cd Length: 944 Bit Score: 46.26 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 483 SDEVPTEVSSEDVISATgeklniggASEDVTEALEKVLEEDKAAEEQKIEEQLPEETKADEKEPTVPAETAESVKDTA-- 560
Cdd:PRK14949 478 LDADNSAVPEQIDSTAE--------QSVVNPSVTDTQVDDTSASNNSAADNTVDDNYSAEDTLESNGLDEGDYAQDSApl 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 561 ------------EEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEQ---VVEAV--------GQVVEP 617
Cdd:PRK14949 550 dayqddyvafssESYNALSDDEQHSANVQSAQSAAEAQPSSQSLSPISAVTTAAASLAdddILDAVlaardsllSDLDAL 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 618 STElaEEPSAKPVDE--PSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAM-----PVEEPS 690
Cdd:PRK14949 630 SPK--EGDGKKSSADrkPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAALASGSapappPVPDPY 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 691 SKP--VEEPSSKPVEEPATDSASQEGEPMVEPSAKPvEGASAEQATAQEpnepapaaaeavsESVGAEPTGAVPEPAATE 768
Cdd:PRK14949 708 DRPpwEEAPEVASANDGPNNAAEGNLSESVEDASNS-ELQAVEQQATHQ-------------PQVQAEAQSPASTTALTQ 773
|
330
....*....|...
gi 1944883863 769 ATKAEEQKVEETP 781
Cdd:PRK14949 774 TSSEVQDTELNLV 786
|
|
| DamX |
COG3266 |
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ... |
510-735 |
1.78e-04 |
|
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442497 [Multi-domain] Cd Length: 455 Bit Score: 46.00 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 510 EDVTEALEKVLEEDKAAEEQKIEEQLPEETKADEKEPTVPAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSA 589
Cdd:COG3266 139 LLALLLDLPLLTLLIVLPLLEEQLLLLALQDIQGTLQALGAVAALLGLRKAEEALALRAGSAAADALALLLLLLASALGE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 590 DQEKEQAAETTEESAEQVVEAVGQVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVdepsakPDDEPSAKP 669
Cdd:COG3266 219 AVAAAAELAALALLAAGAAEVLTARLVLLLLIIGSALKAPSQASSASAPATTSLGEQQEVSLPPA------VAAQPAAAA 292
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1944883863 670 DEEP--STKPVEEPSAMPVEEP--SSKPVEEPSsKPVEEPATDSAS---QEGEPMVEPSAKPVEGASAEQATA 735
Cdd:COG3266 293 AAQPsaVALPAAPAAAAAAAAPaeAAAPQPTAA-KPVVTETAAPAApapEAAAAAAAPAAPAVAKKLAADEQW 364
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
642-806 |
2.18e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 46.00 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 642 SAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKPVeePSSKPVEEPATDSASQEGEPMVEPS 721
Cdd:PRK07003 366 GAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAA--AATRAEAPPAAPAPPATADRGDDAA 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 722 AKPVEGASAEQATAQEPNEPAPAAAEAVSESV-GAEPTGAVPEPAATEATKAEEQKVEETPEIVKPAAgeKEAVAETVAE 800
Cdd:PRK07003 444 DGDAPVPAKANARASADSRCDERDAQPPADSGsASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDAR--APAAASREDA 521
|
....*.
gi 1944883863 801 TSPGSE 806
Cdd:PRK07003 522 PAAAAP 527
|
|
| DUF4045 |
pfam13254 |
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ... |
539-716 |
2.29e-04 |
|
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.
Pssm-ID: 433066 [Multi-domain] Cd Length: 415 Bit Score: 45.54 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 539 TKADEKEPTVPAETAESVKDTAEEAKPE-GQAEKPADVEEVKaIDQTAEPSADQEKEQAAETTEESAEQVVEAVGQVVEP 617
Cdd:pfam13254 166 PKAQPSQPAQPAWMKELNKIRQSRASVDlGRPNSFKEVTPVG-LMRSPAPGGHSKSPSVSGISADSSPTKEEPSEEADTL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 618 STELAEEPSAKPVDEPsakPIDETSAKPVDEPSEKPVDEPSAKPDDEpsaKPDEEPSTKPVEEPSAMPVEEPSSKPVeep 697
Cdd:pfam13254 245 STDKEQSPAPTSASEP---PPKTKELPKDSEEPAAPSKSAEASTEKK---EPDTESSPETSSEKSAPSLLSPVSKAS--- 315
|
170
....*....|....*....
gi 1944883863 698 SSKPVEEPATDSASQEGEP 716
Cdd:pfam13254 316 IDKPLSSPDRDPLSPKPKP 334
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
469-701 |
2.59e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 45.35 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 469 RKPATAEKKPEPKPSDevPTEvssedvisaTGEKLNIGGASEDVTEALEKVLEEDKAAEEQKIEEQLPEETKADEKEPTV 548
Cdd:PHA03169 35 RRRGTAARAAKPAPPA--PTT---------SGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 549 PAETAESVKDTAEEAKPE----GQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEQVVEAVGQ----VVEPSTE 620
Cdd:PHA03169 104 TPSPSGSAEELASGLSPEntsgSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEdspeEPEPPTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 621 LAEEPSAKPVDEPSAKPiDETSAKPVDEPSEKPVDEP--SAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKPV-EEP 697
Cdd:PHA03169 184 EPEPDSPGPPQSETPTS-SPPPQSPPDEPGEPQSPTPqqAPSPNTQQAVEHEDEPTEPEREGPPFPGHRSHSYTVVgWKP 262
|
....
gi 1944883863 698 SSKP 701
Cdd:PHA03169 263 STRP 266
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
633-725 |
2.60e-04 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 44.22 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 633 PSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPsakpdEEPSTKPVEEPSAMPVEEPSSKPVEEPSSKPVEEPATDSAsq 712
Cdd:PRK11633 64 PTQPPEGAAEAVRAGDAAAPSLDPATVAPPNTP-----VEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAPPAPKPEPK-- 136
|
90
....*....|...
gi 1944883863 713 egePMVEPSAKPV 725
Cdd:PRK11633 137 ---PVVEEKAAPT 146
|
|
| motB |
PRK05996 |
MotB family protein; |
537-754 |
2.73e-04 |
|
MotB family protein;
Pssm-ID: 235665 [Multi-domain] Cd Length: 423 Bit Score: 45.07 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 537 EETKA------------DEKeptvPAEtaESVKDTAEEAKPEGQAEKpADVEEVKAIDQTAEPSADQEKEQAAETTEESA 604
Cdd:PRK05996 58 EETKAavasyfnpikltDRK----PSE--KGLKDPVDGAEGEQKPGK-SKFEEDQRVEGSSAVTGDDTTRTSGDQTNYSE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 605 EQVVEavgqvvEPSTELAEEPSAKPVDE-PSAK-------------------------PIDETSAKPVDE-----PSEKP 653
Cdd:PRK05996 131 ADLFR------NPYAVLAEIAQEVGQQAnVSAKgdggaaqsgpatgadggeayrdpfdPDFWSKQVEVTTagdllPPGQA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 654 VDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKpvEEPSSKPVEEPATDSASQEGEPMVEPSAKPVEGASAEQA 733
Cdd:PRK05996 205 REQAQGAKSATAAPATVPQAAPLPQAQPKKAATEEELIA--DAKKAATGEPAANAAKAAKPEPMPDDQQKEAEQLQAAIA 282
|
250 260
....*....|....*....|.
gi 1944883863 734 TAQEPNEPAPAAAEAVSESVG 754
Cdd:PRK05996 283 QAIGGVAGKLAEGVTVTPVEG 303
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
517-829 |
2.90e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.42 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 517 EKVLEEDKAAEEQKIEEQLPEEtKADEKEPTVPAETAESVKDT-AEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQ 595
Cdd:COG3064 30 EAEQKAKEEAEEERLAELEAKR-QAEEEAREAKAEAEQRAAELaAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 596 AAETTEESAEQVV----------EAVGQVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEP 665
Cdd:COG3064 109 AAEKAAAAAEKEKaeeakrkaeeEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 666 SAKPDEEPSTKPVEEPSAMPVEEPSSKPVEEPSSKPVEEPATDSASQEGEPMVEPSAKPVEGASAEQATAQEPNEPAPAA 745
Cdd:COG3064 189 AVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 746 AEAVSESVGAEPTGAVPEPAATEATKAEEQKVEETPEIVKPAAGEKEAVAETVAETSPGSEKQGVTFHRDTVETTGKSDH 825
Cdd:COG3064 269 AGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGA 348
|
....
gi 1944883863 826 SSIK 829
Cdd:COG3064 349 AAAA 352
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
439-710 |
3.36e-04 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 45.45 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 439 TDELDSISEDSFVRSLPGTPAAG-SIAKGLDRKPATAEKKPEPKPSDevPTEVSSEDVisatgeklniggasedvtEALE 517
Cdd:PTZ00449 692 TVVLDESFESILKETLPETPGTPfTTPRPLPPKLPRDEEFPFEPIGD--PDAEQPDDI------------------EFFT 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 518 KVLEEDKAAEEQKIEEQLPEETKADEKEPTVPAETAEsvkdtAEEakPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAA 597
Cdd:PTZ00449 752 PPEEERTFFHETPADTPLPDILAEEFKEEDIHAETGE-----PDE--AMKRPDSPSEHEDKPPGDHPSLPKKRHRLDGLA 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 598 ETTEEsaeqvVEAvgqvvEPStELAEEPSAKPVDEPSAKPIDETSAkpVDEPSEKPVDEPSAKPDDEPSAKPDEEpsTKP 677
Cdd:PTZ00449 825 LSTTD-----LES-----DAG-RIAKDASGKIVKLKRSKSFDDLTT--VEEAEEMGAEARKIVVDDDGTEADDED--THP 889
|
250 260 270
....*....|....*....|....*....|....*.
gi 1944883863 678 VEEPSAMPV--EEPSSKPVEEP-SSKPVEEPATDSA 710
Cdd:PTZ00449 890 PEEKHKSEVrrRRPPKKPSKPKkPSKPKKPKKPDSA 925
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
546-711 |
3.44e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 45.23 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 546 PTVPAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEQVVEAVGQVVEPSTELAEEP 625
Cdd:PRK07003 383 PGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSR 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 626 SAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTkpveePSAMPVEEPSSKPVEEPSSKPVEEP 705
Cdd:PRK07003 463 CDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARA-----PAAASREDAPAAAAPPAPEARPPTP 537
|
....*.
gi 1944883863 706 ATDSAS 711
Cdd:PRK07003 538 AAAAPA 543
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
523-876 |
3.56e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.03 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 523 DKAAEEQKIEEQLPEETKADEKEPTVPAEtaesvkdTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEE 602
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAE-------AEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 603 SAEQVVEAVGQVVEPSTELAEEpSAKPVDEPSAKPIDEtsaKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPS 682
Cdd:COG3064 75 AAKKLAEAEKAAAEAEKKAAAE-KAKAAKEAEAAAAAE---KAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 683 AMPVEEP--SSKPVEEPSSKPVEEPATDSASQEGEPMVEPSAKPVEGASAEQATAQEPNEPAPAAAEAVSESVGAEPTGA 760
Cdd:COG3064 151 KAEAEAAraAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 761 VPEPAATEATKAEEQKVEETPEIVKPAAGEKEAVAETVAETSPGSEKQGVTFHRDTVETTGKSDHSSIKSPTKTPTSHRC 840
Cdd:COG3064 231 EAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGA 310
|
330 340 350
....*....|....*....|....*....|....*.
gi 1944883863 841 GSVATSIFDENLLNSSQFVQIVEAFLGESPPEEVVQ 876
Cdd:COG3064 311 VAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAA 346
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
628-735 |
3.77e-04 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 43.84 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 628 KPVDEpsakpiDETSAKPvdePSEKPVdePSAKPDD---EPSAKPDEEPSTKPVEEPSAMPVEEPSSKPVEEPSSKPVEE 704
Cdd:PRK11633 46 KPGDR------DEPDMMP---AATQAL--PTQPPEGaaeAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEK 114
|
90 100 110
....*....|....*....|....*....|.
gi 1944883863 705 PATDSASQEgEPMVEPSAKPVEGASAEQATA 735
Cdd:PRK11633 115 PKPKPKPQQ-KVEAPPAPKPEPKPVVEEKAA 144
|
|
| PRK14960 |
PRK14960 |
DNA polymerase III subunit gamma/tau; |
580-782 |
3.98e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237868 [Multi-domain] Cd Length: 702 Bit Score: 45.04 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 580 AIDQTAEPSADQEKEQAAETTEESAEQVveavgQVVEPSTELaeepsaKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSA 659
Cdd:PRK14960 362 APNEILVSEPVQQNGQAEVGLNSQAQTA-----QEITPVSAV------QPVEVISQPAMVEPEPEPEPEPEPEPEPEPEP 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 660 KPDDEPSAKPDEEPS-----------------------TKPVEEPSAMPVEEPSSKPVE-EPSSKPVE-EPAtdsasQEG 714
Cdd:PRK14960 431 EPEPEPEPEPEPQPNqdlmvfdpnhheliglesavvqeTVSVLEEDFIPVPEQKLVQVQaETQVKQIEpEPA-----STA 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1944883863 715 EPMVEPSAKPVEGASAEQATAQEPNEPAPAAAEAVSESVGAEPTGAVPEPAATEATKAEEQKVEETPE 782
Cdd:PRK14960 506 EPIGLFEASSAEFSLAQDTSAYDLVSEPVIEQQSLVQAEIVETVAVVKEPNATDNSQLMPQDILKLPS 573
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
584-800 |
4.17e-04 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 45.09 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 584 TAEPsaDQEKEQAAETTEESA--EQVVEAVGQVVEPSTELAEEPSAKPVDEPSAKPIDETSAkpvdepsEKPVDEPSAKP 661
Cdd:NF033875 54 TVQP--DNPDPQSGSETPKTAvsEEATVQKDTTSQPTKVEEVASEKNGAEQSSATPNDTTNA-------QQPTVGAEKSA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 662 DDEPSAKPdeEPSTKPVEEPSAM-PVEEPSSKPVEEPssKPVEEPATDSASQEG--EPMVEPSAKPVE---GASAEQATA 735
Cdd:NF033875 125 QEQPVVSP--ETTNEPLGQPTEVaPAENEANKSTSIP--KEFETPDVDKAVDEAkkDPNITVVEKPAEdlgNVSSKDLAA 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1944883863 736 QEPNEpapaaaeavsESVGAEPTGAVPEPAATeaTKAEEQKV-EETPEIVKPAAGEKEAVAETVAE 800
Cdd:NF033875 201 KEKEV----------DQLQKEQAKKIAQQAAE--LKAKNEKIaKENAEIAAKNKAEKERYEKEVAE 254
|
|
| PRK08691 |
PRK08691 |
DNA polymerase III subunits gamma and tau; Validated |
621-808 |
4.39e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 45.08 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 621 LAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVdepSAKpddEPSAKPDEEPSTKPVEEPS--AMPVEEPSSKPV--EE 696
Cdd:PRK08691 356 LAFAPLAAASCDANAVIENTELQSPSAQTAEKET---AAK---KPQPRPEAETAQTPVQTASaaAMPSEGKTAGPVsnQE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 697 PSSKPVEEPATDSAsQEGEPMVEPSAKPVEGASAEQATAQ----EPNEPAPAAAEAVSESVGAEPTGAVP--EPAATEAT 770
Cdd:PRK08691 430 NNDVPPWEDAPDEA-QTAAGTAQTSAKSIQTASEAETPPEnqvsKNKAADNETDAPLSEVPSENPIQATPndEAVETETF 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1944883863 771 KAE--------------EQKVEETPEIVKP----AAGEKEAVAETVAETSPGSEKQ 808
Cdd:PRK08691 509 AHEapaepfygygfpdnDCPPEDGAEIPPPdwehAAPADTAGGGADEEAEAGGIGG 564
|
|
| PRK05901 |
PRK05901 |
RNA polymerase sigma factor; Provisional |
476-677 |
5.61e-04 |
|
RNA polymerase sigma factor; Provisional
Pssm-ID: 235640 [Multi-domain] Cd Length: 509 Bit Score: 44.22 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 476 KKPEPKPSDEVPTEVSSEDVISATGEKLNIggASEDVTEALEKVLEEDKAAEEQKIEEQLPEETKADEKEPTVPAETAE- 554
Cdd:PRK05901 4 ASTKAELAAEEEAKKKLKKLAAKSKSKGFI--TKEEIKEALESKKKTPEQIDQVLIFLSGMVKDTDDATESDIPKKKTKt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 555 SVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEQVVEAVGQVVEPstELAEEPSAKPVDEPS 634
Cdd:PRK05901 82 AAKAAAAKAPAKKKLKDELDSSKKAEKKNALDKDDDLNYVKDIDVLNQADDDDDDDDDDDLDD--DDIDDDDDDEDDDED 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1944883863 635 AKPIDETSAkpvDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKP 677
Cdd:PRK05901 160 DDDDDVDDE---DEEKKEAKELEKLSDDDDFVWDEDDSEALRQ 199
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
541-814 |
5.65e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 541 ADEKEPTVPAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTA---EPSADQEKE-QAAETTEESAEQVVEAVGQVVE 616
Cdd:PHA03247 2584 SRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPpspSPAANEPDPhPPPTVPPPERPRDDPAPGRVSR 2663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 617 P----STELAEEPSAKPVD--EPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPdeePSTKPVEEPSAMPVEEPS 690
Cdd:PHA03247 2664 PrrarRLGRAAQASSPPQRprRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLP---PGPAAARQASPALPAAPA 2740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 691 SKPVEEPSSKPV-EEPATDSASQEGEPMVEPSAKPVEGASAeQATAQEPNEPAPAAAEAVSESVGAEPTGAVPEPAATEA 769
Cdd:PHA03247 2741 PPAVPAGPATPGgPARPARPPTTAGPPAPAPPAAPAAGPPR-RLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALP 2819
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1944883863 770 TKAEEQKVEETPEIVKPAAGEKEAVAETVAETSPGSEKQGVTFHR 814
Cdd:PHA03247 2820 PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRR 2864
|
|
| PRK14960 |
PRK14960 |
DNA polymerase III subunit gamma/tau; |
614-801 |
6.14e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237868 [Multi-domain] Cd Length: 702 Bit Score: 44.27 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 614 VVEPSTELAEEPSAKPVDEPSAKPIDETSA-KPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSK 692
Cdd:PRK14960 368 VSEPVQQNGQAEVGLNSQAQTAQEITPVSAvQPVEVISQPAMVEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPQPNQD 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 693 -PVEEPSSKpvEEPATDSA-SQEGEPMVEPSAKPVEGASAEQATAQEPNEPAPAAAEAVSESVGAEPTGAVPEPAA--TE 768
Cdd:PRK14960 448 lMVFDPNHH--ELIGLESAvVQETVSVLEEDFIPVPEQKLVQVQAETQVKQIEPEPASTAEPIGLFEASSAEFSLAqdTS 525
|
170 180 190
....*....|....*....|....*....|...
gi 1944883863 769 ATKAEEQKVEETPEIVKPAAGEKEAVAETVAET 801
Cdd:PRK14960 526 AYDLVSEPVIEQQSLVQAEIVETVAVVKEPNAT 558
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
596-769 |
6.24e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.59 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 596 AAETTEESAEQVVEAVGQVVEPStelAEEPSAKPVDEPSAkpidetsakpvdePSEKPVDEPSAKPDDEPSAKPDEEPST 675
Cdd:PRK07764 366 SASDDERGLLARLERLERRLGVA---GGAGAPAAAAPSAA-------------AAAPAAAPAPAAAAPAAAAAPAPAAAP 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 676 KPVEEPSamPVEEPSSKPVEEPSSKPVEEPATDSASQEGEPMVEPSAKPVEGASAEQATAQepnepapaaaeavsesvga 755
Cdd:PRK07764 430 QPAPAPA--PAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAP------------------- 488
|
170
....*....|....
gi 1944883863 756 EPTGAVPEPAATEA 769
Cdd:PRK07764 489 APAAAPAAPAAPAA 502
|
|
| PRK14949 |
PRK14949 |
DNA polymerase III subunits gamma and tau; Provisional |
555-837 |
6.55e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237863 [Multi-domain] Cd Length: 944 Bit Score: 44.33 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 555 SVKDTAEEAKPEGQAEKP--ADVEEVKAIDQTAEPSADQEKEQA--AETTEESAEQVVEAVGQVVE-PSTELAE------ 623
Cdd:PRK14949 367 QVDDPAEISLPEGQTPSAlaAAVQAPHANEPQFVNAAPAEKKTAltEQTTAQQQVQAANAEAVAEAdASAEPADtveqal 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 624 --------------------------EPSAKPVDEPSAKP--IDETSAKPVDEPS--EKPVDEPSAKPDDEPSAKPDEEP 673
Cdd:PRK14949 447 ddesellaalnaeqavilsqaqsqgfEASSSLDADNSAVPeqIDSTAEQSVVNPSvtDTQVDDTSASNNSAADNTVDDNY 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 674 STKPVEEPSAMPVEEPS--SKPVEEPSSKPVEEPATDSASQEGEPMVEPSAKPVEGASAEQATAQEPNEPAPAAAEAVSE 751
Cdd:PRK14949 527 SAEDTLESNGLDEGDYAqdSAPLDAYQDDYVAFSSESYNALSDDEQHSANVQSAQSAAEAQPSSQSLSPISAVTTAAASL 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 752 S------------------VGAEptgavpEPAATEATKAEEQKVEETPEIVKPAAGEKEAVAETVAETSPGSEKQGVTFH 813
Cdd:PRK14949 607 AdddildavlaardsllsdLDAL------SPKEGDGKKSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFE 680
|
330 340
....*....|....*....|....
gi 1944883863 814 RDTVETTGKSDHSSIKSPTKTPTS 837
Cdd:PRK14949 681 LATHQSVPEAALASGSAPAPPPVP 704
|
|
| FimV |
COG3170 |
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures]; |
527-802 |
6.94e-04 |
|
Type IV pilus assembly protein FimV [Cell motility, Extracellular structures];
Pssm-ID: 442403 [Multi-domain] Cd Length: 508 Bit Score: 44.01 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 527 EEQKIEEQLPEETKADEKEPTVPAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEQ 606
Cdd:COG3170 207 AAEEVAALSPAEARQEVQAQSADWAAYRARLAAAVEPAPAAAAPAAPPAAAAAAGPVPAAAEDTLSPEVTAAAAAEEADA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 607 VVEAVGQVVEPSTELAEEPSA--KPVDEPSAKPiDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAM 684
Cdd:COG3170 287 LPEAAAELAERLAALEAQLAElqRLLALKNPAP-AAAVSAPAAAAAAATVEAAAPAAAAQPAAAAPAPALDNPLLLAGLL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 685 PVEEPSSKPVEEPSSKPVEEPATDSASQEGEPMVEPSAKPVEGASA-EQATAQEPNEPAPAAAEAVSESVGAEPTGAVPE 763
Cdd:COG3170 366 RRRKAEADEVDPVAEADVYLAYGRDDQAEEILKEALASEPERLDLRlKLLEIYAARGDRAAFEALAAELYALTGGGRALD 445
|
250 260 270
....*....|....*....|....*....|....*....
gi 1944883863 764 PAATEATKAEEQKVEETPEIVKPAAGEKEAVAETVAETS 802
Cdd:COG3170 446 PDNPLYAPGAAAAAEDAPAAEAEDDSPAEEPAASAAAAA 484
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
534-724 |
7.39e-04 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 44.30 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 534 QLPEETKADEkEPTVPAETAESVKDTAEEaKPEG----QAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEQVVE 609
Cdd:PTZ00449 619 DIPKSPKRPE-SPKSPKRPPPPQRPSSPE-RPEGpkiiKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLD 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 610 AVGQVVEPST--ELAEEPSAKPVDEPSAKPIDETSakpvdePSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVE 687
Cdd:PTZ00449 697 ESFESILKETlpETPGTPFTTPRPLPPKLPRDEEF------PFEPIGDPDAEQPDDIEFFTPPEEERTFFHETPADTPLP 770
|
170 180 190
....*....|....*....|....*....|....*..
gi 1944883863 688 EPSSKPVEEPsskpveepatDSASQEGEPMvEPSAKP 724
Cdd:PTZ00449 771 DILAEEFKEE----------DIHAETGEPD-EAMKRP 796
|
|
| NESP55 |
pfam06390 |
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ... |
545-705 |
7.98e-04 |
|
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian neuroendocrine-specific golgi protein P55 (NESP55) sequences. NESP55 is a novel member of the chromogranin family and is a soluble, acidic, heat-stable secretory protein that is expressed exclusively in endocrine and nervous tissues, although less widely than chromogranins.
Pssm-ID: 115071 [Multi-domain] Cd Length: 261 Bit Score: 42.93 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 545 EPTVPAETAESVKDTAEEAKPEGQAEKPADVEevKAIDQTAEPSADQEKEQAAETTEESaeqvveavgqvvEPSTELAEE 624
Cdd:pfam06390 82 EPSEPESDHEDEDFEPELARPECLEYDEDDFD--TETDSETEPESDIESETEFETEPET------------EPDTAPTTE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 625 PSAKPVDEPSakPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPdeePSTKPVEEPSAMpvEEPSSKPVEEPSSKPVEE 704
Cdd:pfam06390 148 PETEPEDEPG--PVVPKGATFHQSLTERLHALKLQSADASPRRAP---PSTQEPESAREG--EEPERGPLDKDPRDPEEE 220
|
.
gi 1944883863 705 P 705
Cdd:pfam06390 221 E 221
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
432-808 |
8.14e-04 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 44.24 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 432 VVELDEVTDELDSISEDSFVRSLPGTPAAGSIAKGLDRKPATAEKKPEPKPSDEVPTEVSSEDVISATGEKLNIGGASED 511
Cdd:COG5271 231 VEEEDASEDAVAAADETLLADDDDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQAADPESDDDADDS 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 512 VTEALEKVLEEDKAAEEQKIEEQLPEETKaDEKEPTVPAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQ 591
Cdd:COG5271 311 TLAALEGAAEDTEIATADELAAADDEDDD-DSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEAD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 592 EKEQAAETTEESAEQVVEAVGQVVEPSTELAEEPSAKPVDEPSAKPIDETSAK-PVDEPSEKPVDEPSAKPDDEPSAKPD 670
Cdd:COG5271 390 AAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDiATDEEADSLADEEEEAEAELDTEEDT 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 671 EEPSTKPVEEPSAMPVEEPSSKPVEEPSSKPVEEPATDSASQEGEP--------MVEPSAKPVEGASAEQATAQEPNEPA 742
Cdd:COG5271 470 ESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSaddgadtdAAADPEDSDEDALEDETEGEENAPGS 549
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1944883863 743 PAAAEAVSESVGAEPTGAVPEPAATEATKAEEQKVEETPEIVKPAAGEKEAVAETVAETSPGSEKQ 808
Cdd:COG5271 550 DQDADETDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEA 615
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
514-807 |
8.24e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 514 EALEKVLEEDKAAEE-QKIEEQLPEETKADEKEPTVPAETAESVKDTAEEAKPEGQ---AEKPADVEEVKAIDQTAEpsA 589
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEaKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElkkAEEKKKADEAKKAEEKKK--A 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 590 DQEKEQAAETTE-ESAEQVVEAVGQVVEPSTELAEEpsAKPVDEpSAKPIDETSAKPVDEPSEKpvdEPSAKPDDEPSAK 668
Cdd:PTZ00121 1305 DEAKKKAEEAKKaDEAKKKAEEAKKKADAAKKKAEE--AKKAAE-AAKAEAEAAADEAEAAEEK---AEAAEKKKEEAKK 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 669 PDEEPSTKPVEEPSAMPVE---EPSSKPVEEPSSKPVEEPATDSASQEGEPMV---EPSAKPVEGASAEQATAQEPNEPA 742
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEAKkkaEEDKKKADELKKAAAAKKKADEAKKKAEEKKkadEAKKKAEEAKKADEAKKKAEEAKK 1458
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1944883863 743 PAA-AEAVSESVGAEPTGAVPEPA--ATEATKAEEQKVEETPEIVKPAAGEKEAVAETVAETSPGSEK 807
Cdd:PTZ00121 1459 AEEaKKKAEEAKKADEAKKKAEEAkkADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
617-716 |
8.44e-04 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 43.95 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 617 PSTELAEEPSAKPVDePSAKPIDETSAKPvdEPSEKPVDEPSAKPD------------DEPSAKPDEEPSTKPveEPSAM 684
Cdd:PHA03269 27 PIPELHTSAATQKPD-PAPAPHQAASRAP--DPAVAPTSAASRKPDlaqaptpaasekFDPAPAPHQAASRAP--DPAVA 101
|
90 100 110
....*....|....*....|....*....|....*....
gi 1944883863 685 PV--EEPSSKPVEEPSSKPVEEPA-----TDSASQEGEP 716
Cdd:PHA03269 102 PQlaAAPKPDAAEAFTSAAQAHEApadagTSAASKKPDP 140
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
608-790 |
9.15e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 43.70 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 608 VEAVGQVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVE 687
Cdd:PRK07994 362 AAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKS 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 688 EPSSKPVEEPSSKPVEEPATdsasqegepmVEPSAKPVEGASAEQATAQEpnepapaaaeavsESVGAEPTGAVPEPAAT 767
Cdd:PRK07994 442 EPAAASRARPVNSALERLAS----------VRPAPSALEKAPAKKEAYRW-------------KATNPVEVKKEPVATPK 498
|
170 180
....*....|....*....|...
gi 1944883863 768 EATKAEEQkvEETPEIVKPAAGE 790
Cdd:PRK07994 499 ALKKALEH--EKTPELAAKLAAE 519
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
520-671 |
1.01e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.30 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 520 LEEDKAAEEQKI---EEQLPEETKADEKEPTvpAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQA 596
Cdd:TIGR02794 80 AEKQRAAEQARQkelEQRAAAEKAAKQAEQA--AKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAK 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1944883863 597 AETTEESAEQVVEAVGQvVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDE 671
Cdd:TIGR02794 158 AKAAAEAKKKAEEAKKK-AEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADE 231
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
539-677 |
1.01e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 43.22 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 539 TKADEKEPTVPAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEQVVEAVGQVVEPS 618
Cdd:NF040712 188 IDPDFGRPLRPLATVPRLAREPADARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPA 267
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1944883863 619 TELAEEPSAKPVDEPSAKPiDETSAKPVDEPSEKPvDEPSAKPDDEPSAKPDEEPSTKP 677
Cdd:NF040712 268 AEPDEATRDAGEPPAPGAA-ETPEAAEPPAPAPAA-PAAPAAPEAEEPARPEPPPAPKP 324
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
458-620 |
1.04e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 43.43 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 458 PAAGSIAKGLDRkpATAEKKPEPKpsdEVPTEVSSEDVISATGEKLNIGGASEDVTEA-LEKVLEEDKAAEEQKIEEqlp 536
Cdd:PRK13108 317 PVGPGEPNQPDD--VAEAVKAEVA---EVTDEVAAESVVQVADRDGESTPAVEETSEAdIEREQPGDLAGQAPAAHQ--- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 537 EETKADEKEPTVPAETAESVKDTAEEAKPEGQAekpadveevkaidqtAEPSADQEKEQAAETTEESAEQVVEAVGQVVE 616
Cdd:PRK13108 389 VDAEAASAAPEEPAALASEAHDETEPEVPEKAA---------------PIPDPAKPDELAVAGPGDDPAEPDGIRRQDDF 453
|
....
gi 1944883863 617 PSTE 620
Cdd:PRK13108 454 SSRR 457
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
523-735 |
1.13e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.91 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 523 DKAAEEQKIEEQLPEETKADEKEPTVPAETAEsvkdTAEEAKPEGQAEKPAdveevkaIDQTAEPSADQEKEQAAEtteE 602
Cdd:TIGR02794 44 DPGAVAQQANRIQQQKKPAAKKEQERQKKLEQ----QAEEAEKQRAAEQAR-------QKELEQRAAAEKAAKQAE---Q 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 603 SAEQVVEAVGQvvepstelAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEepstkpveeps 682
Cdd:TIGR02794 110 AAKQAEEKQKQ--------AEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEE----------- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1944883863 683 AMPVEEPSSKPVEEPSSKPVEEPATDSASQEGEPMVEPSAKPVEGASAEQATA 735
Cdd:TIGR02794 171 AKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAA 223
|
|
| Cornifin |
pfam02389 |
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ... |
651-720 |
1.26e-03 |
|
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.
Pssm-ID: 280537 [Multi-domain] Cd Length: 135 Bit Score: 40.81 E-value: 1.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1944883863 651 EKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKPVEEPSSKPVEEPATDSASQEGEPMV-EP 720
Cdd:pfam02389 2 QQQVKQPCQPPPQEPCVPTTKEPCHSKVPEPCNPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCCPKVpEP 72
|
|
| PRK05901 |
PRK05901 |
RNA polymerase sigma factor; Provisional |
508-708 |
1.35e-03 |
|
RNA polymerase sigma factor; Provisional
Pssm-ID: 235640 [Multi-domain] Cd Length: 509 Bit Score: 43.06 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 508 ASEDVTEALEKVLEEDKAAEEQKIEE---QLPEETKADEKEPTVPAETAESVKDTAEeaKPEGQAEKPADVEEVKAIDQT 584
Cdd:PRK05901 12 AEEEAKKKLKKLAAKSKSKGFITKEEikeALESKKKTPEQIDQVLIFLSGMVKDTDD--ATESDIPKKKTKTAAKAAAAK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 585 AEPSADQEKEQAAETTEESAEQVVEAVGQVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDE 664
Cdd:PRK05901 90 APAKKKLKDELDSSKKAEKKNALDKDDDLNYVKDIDVLNQADDDDDDDDDDDLDDDDIDDDDDDEDDDEDDDDDDVDDED 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1944883863 665 PSakpDEEPSTKPVEEPSAMPVEEPSSKPVEEPSSKPVEEPATD 708
Cdd:PRK05901 170 EE---KKEAKELEKLSDDDDFVWDEDDSEALRQARKDAKLTATA 210
|
|
| PT |
pfam04886 |
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a ... |
629-667 |
1.41e-03 |
|
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat.
Pssm-ID: 282710 [Multi-domain] Cd Length: 36 Bit Score: 37.84 E-value: 1.41e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1944883863 629 PVDEPSAKPIDETSAKPVDEPSekpvDEPSAKPDDEPSA 667
Cdd:pfam04886 2 PTAQPTAQPTVQPTGQPTAQPT----DQPTAQPTDAPTA 36
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
479-643 |
1.49e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 43.04 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 479 EPKPSDEVPTEVSSEDVISATGEKLNIGGA--------SEDVTEALEKVLEEDKAAEEQKIEEQLPEETKADEKEPTVPA 550
Cdd:PRK13108 292 VDEALEREPAELAAAAVASAASAVGPVGPGepnqpddvAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADI 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 551 ETAESvKDTAEEAKPEGQAEKPADVEEvkaidqtAEPSADQEKEQAAETTEESAEQvVEAVGQVVEPSTELAEEPSAKPV 630
Cdd:PRK13108 372 EREQP-GDLAGQAPAAHQVDAEAASAA-------PEEPAALASEAHDETEPEVPEK-AAPIPDPAKPDELAVAGPGDDPA 442
|
170
....*....|...
gi 1944883863 631 DEPSAKPIDETSA 643
Cdd:PRK13108 443 EPDGIRRQDDFSS 455
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
551-810 |
1.60e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 42.65 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 551 ETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEES-AEQVVEAVGQVVEPSTELAEEPSAK- 628
Cdd:PHA03169 28 GTREQAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRhGEKEERGQGGPSGSGSESVGSPTPSp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 629 ----PVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAkPDEEPSTKPVEEPSAMpvEEPSSKPVEEPSSKPVEE 704
Cdd:PHA03169 108 sgsaEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPA-PPESHNPSPNQQPSSF--LQPSHEDSPEEPEPPTSE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 705 PATDSASQEGEPMVEPSAKPVEGASAEqataqepnepapaaaeavSESVGAEPTGAvpePAATEATKAEEQKVEETPEIV 784
Cdd:PHA03169 185 PEPDSPGPPQSETPTSSPPPQSPPDEP------------------GEPQSPTPQQA---PSPNTQQAVEHEDEPTEPERE 243
|
250 260
....*....|....*....|....*.
gi 1944883863 785 KPAAGEKEAVAETVAETSPGSEKQGV 810
Cdd:PHA03169 244 GPPFPGHRSHSYTVVGWKPSTRPGGV 269
|
|
| EF-hand_6 |
pfam13405 |
EF-hand domain; |
913-940 |
1.62e-03 |
|
EF-hand domain;
Pssm-ID: 463869 [Multi-domain] Cd Length: 30 Bit Score: 37.16 E-value: 1.62e-03
10 20
....*....|....*....|....*...
gi 1944883863 913 LEQLFEKWDNDGSGYLDLEELHSVMSKF 940
Cdd:pfam13405 2 LREAFKLFDKDGDGKISLEELRKALRSL 29
|
|
| PT |
pfam04886 |
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a ... |
624-659 |
1.75e-03 |
|
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat.
Pssm-ID: 282710 [Multi-domain] Cd Length: 36 Bit Score: 37.46 E-value: 1.75e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1944883863 624 EPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSA 659
Cdd:pfam04886 1 QPTAQPTAQPTVQPTGQPTAQPTDQPTAQPTDAPTA 36
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
584-711 |
1.88e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.05 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 584 TAEPSADQEKEQAAETTEESAEQVVEAVGQVVEpstelAEEPSAKPVDEPSAKPiDETSAKPVDEPSEKPVDEPSAKPDD 663
Cdd:PRK07764 391 AGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAP-----APAAAPQPAPAPAPAP-APPSPAGNAPAGGAPSPPPAAAPSA 464
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1944883863 664 EPSAKPDEEPSTKPVEEPSAMPVEEPSSKPvEEPSSKPVEEPATDSAS 711
Cdd:PRK07764 465 QPAPAPAAAPEPTAAPAPAPPAAPAPAAAP-AAPAAPAAPAGADDAAT 511
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
477-722 |
2.02e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 42.45 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 477 KPEPKPSDEVP-TEVSSEDVISATGEKLNIGGASEDVTEALEKVLEEDKAAEEQKIEEQLPE-ETKADEKEPTvPAETAE 554
Cdd:NF033839 285 KEPGNKKPSAPkPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQlETPKPEVKPQ-PEKPKP 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 555 SVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQaaetteesaeqvveavgqvvePSTELAEEPSAKpvdEPS 634
Cdd:NF033839 364 EVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEK---------------------PKPEVKPQPEKP---KPE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 635 AKPIDETSAKPVDEPSEKPVDEPSAKPDD-EPSAKPD-EEPSTKPVEEPSA-MPVEEPSSKPVEEPSSKPVEE----PAT 707
Cdd:NF033839 420 VKPQPEKPKPEVKPQPEKPKPEVKPQPEKpKPEVKPQpETPKPEVKPQPEKpKPEVKPQPEKPKPDNSKPQADdkkpSTP 499
|
250
....*....|....*
gi 1944883863 708 DSASQEGEPMVEPSA 722
Cdd:NF033839 500 NNLSKDKQPSNQAST 514
|
|
| DD_IQCK |
cd22969 |
dimerization/docking (D/D) domain found in IQ domain-containing protein K (IQCK) and similar ... |
160-213 |
2.03e-03 |
|
dimerization/docking (D/D) domain found in IQ domain-containing protein K (IQCK) and similar proteins; IQ motif-containing proteins may play an active role in cell polarization and migration, and even in ciliary function. Although its function remains unclear, IQCK contains a conserved region that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.
Pssm-ID: 438538 Cd Length: 58 Bit Score: 37.87 E-value: 2.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1944883863 160 ARAYLLDKLLPTLILGIEKLLMEAEKRGLAEsnEADPNFNPINFLGQYLMRNNP 213
Cdd:cd22969 7 PVEYLEEYIFPVLLPALEEMLEEAKKEDCFE--RKRTKFNGLDFLTEYLYNNNP 58
|
|
| ZipA |
COG3115 |
Cell division protein ZipA, interacts with FtsZ [Cell cycle control, cell division, chromosome ... |
518-637 |
2.04e-03 |
|
Cell division protein ZipA, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442349 [Multi-domain] Cd Length: 298 Bit Score: 41.99 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 518 KVLEEDKAAEEQKIEEQLPEETKADEKEPTVPAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAA 597
Cdd:COG3115 32 SSFRDKPSKRDVLLDDDGIGEVRVVAAEAPERVEPEASFDAEDEVREPDQEEVDPLLDDEADIEAAPAEPVRWAGTAAAV 111
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1944883863 598 E-TTEESAEQVVEAVGQVVEPSTELAEEPSAKPVDEPSAKP 637
Cdd:COG3115 112 EpAPEQEAYEEAGPAGESAEQEDAPAEEPEAEAPAEEALAA 152
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
568-728 |
2.22e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 42.55 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 568 QAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEQVVEAVGQVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVD 647
Cdd:PRK07994 362 AAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKS 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 648 EPSEKPVDEPsAKPDDEPSAKPDEEPSTKPVEEPSAMPVEEPSSKPVEEPSSKPVEEPATDSASqEGEPMVEPSAKPVEG 727
Cdd:PRK07994 442 EPAAASRARP-VNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKAL-EHEKTPELAAKLAAE 519
|
.
gi 1944883863 728 A 728
Cdd:PRK07994 520 A 520
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
453-716 |
2.32e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 453 SLPGTPAAGSIAKGlDRKPATAEKKPEPKPSDEVPTEVSSEDVISATGEKLNIGGASEDVTEALEKVLEEDKAAEEQKIE 532
Cdd:PHA03247 2734 ALPAAPAPPAVPAG-PATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVL 2812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 533 EQLPEETKADEKEPTVPAETAesvkdtaeeAKPEGQAEKPADVEEVKAIDQTAEPSAD-QEKEQAAETTEESAEQVVEAV 611
Cdd:PHA03247 2813 APAAALPPAASPAGPLPPPTS---------AQPTAPPPPPGPPPPSLPLGGSVAPGGDvRRRPPSRSPAAKPAAPARPPV 2883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 612 GQVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMPVEE--- 688
Cdd:PHA03247 2884 RRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPqpw 2963
|
250 260 270
....*....|....*....|....*....|....*..
gi 1944883863 689 -----PSSKPVEE---PSSKP-VEEPATDSASQEGEP 716
Cdd:PHA03247 2964 lgalvPGRVAVPRfrvPQPAPsREAPASSTPPLTGHS 3000
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
514-736 |
2.41e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.73 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 514 EALEKVLEEDkaaeEQKIEEQLPEETKADEKEPTVPAETAESVKDTAEEAKPEGQAEK--PADVEEVKAIDQTAEPSADQ 591
Cdd:PTZ00108 1135 DKFEEALEEQ----EEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKskKASVVGNSKRVDSDEKRKLD 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 592 EKEQAAETTEESAEQVVEAVGQVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVdEPSEKPVDEPS-------AKPDDE 664
Cdd:PTZ00108 1211 DKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDL-SKEGKPKNAPKrvsavqySPPPPS 1289
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1944883863 665 PSAKPDEEPSTKPVEEPSAMPVEEPSSKPVEEPSSKPVEEPATDSASqegepmvepSAKPVEGASAEQATAQ 736
Cdd:PTZ00108 1290 KRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKK---------SKTRVKQASASQSSRL 1352
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
515-683 |
2.45e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 515 ALEKvlEEDKAAEEQKIEEQlpEETKADEKEptvpaetaesvKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKE 594
Cdd:PRK09510 105 QLEK--ERLAAQEQKKQAEE--AAKQAALKQ-----------KQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 595 QAAETTEESAEQvveavgqvvEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDE---PSAKPDDEPSAKPDE 671
Cdd:PRK09510 170 KAEAEAAKKAAA---------EAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEakaAAAKAAAEAKAAAEK 240
|
170
....*....|..
gi 1944883863 672 EPSTKPVEEPSA 683
Cdd:PRK09510 241 AAAAKAAEKAAA 252
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
548-814 |
2.59e-03 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 42.36 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 548 VPAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETT----EESAEQVVEAVGQVVEPSTELAE 623
Cdd:COG5180 148 VALAAALLQRSDPILAKDPDGDSASTLPPPAEKLDKVLTEPRDALKDSPEKLDrpkvEVKDEAQEEPPDLTGGADHPRPE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 624 EPSAKPVDEPSAKpidETSAKPVDEPSEKPVDEPSAKPDDEPsaKPDEEPstkPVEEPSAMPVEEPSSKPVEEPSSKPVE 703
Cdd:COG5180 228 AASSPKVDPPSTS---EARSRPATVDAQPEMRPPADAKERRR--AAIGDT---PAAEPPGLPVLEAGSEPQSDAPEAETA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 704 EPATDSASQegepMVEPSAKPVEGA-SAEQATAQEPnepapaaaeavsESVGAEPTGaVPEPAATEATKAEEQKVEETPE 782
Cdd:COG5180 300 RPIDVKGVA----SAPPATRPVRPPgGARDPGTPRP------------GQPTERPAG-VPEAASDAGQPPSAYPPAEEAV 362
|
250 260 270
....*....|....*....|....*....|..
gi 1944883863 783 IVKPAAGEKEAVAETVAETSPGSEKQGVTFHR 814
Cdd:COG5180 363 PGKPLEQGAPRPGSSGGDGAPFQPPNGAPQPG 394
|
|
| ActA |
pfam05058 |
ActA Protein; The ActA family is found in Listeria and is associated with motility. ActA ... |
475-708 |
2.73e-03 |
|
ActA Protein; The ActA family is found in Listeria and is associated with motility. ActA protein acts as a scaffold to assemble and activate host cell actin cytoskeletal factors at the bacterial surface, resulting in directional actin polymerization and propulsion of the bacterium through the cytoplasm of the host cell.
Pssm-ID: 282861 [Multi-domain] Cd Length: 633 Bit Score: 42.26 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 475 EKKPEPKPSD-------EVPTEVSSEDV--ISATGEKLNIGGAS--EDVTEALEKVLEEDKAAEEQKIEEQLPEET---- 539
Cdd:pfam05058 39 EEKTEEQPSEvntgpryETAREVSSRDIkeLEKSNKVRNTNKADliAMLKEKAEKGPNINNNNSEQTENAAINEEAsgad 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 540 ----KADEKEPTVPAETAESVK-------DTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEQVV 608
Cdd:pfam05058 119 rpaiQVERRHPGLPSDSAAEIKkrrkaiaSSDSELESLTYPDKPTKVNKKKVAKESVADASESDLDSSMQSADESSPQPL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 609 EAVGQVVEPSTELAEEPSAK----PVDE-PSA-KPIDETSAKPVDEPSEKPVDEpSAKPDDEPSAKPDEEPSTKPVEEPS 682
Cdd:pfam05058 199 KANQQPFFPKVFKKIKDAGKwvrdKIDEnPEVkKAIVDKSAGLIDQLLTKKKSE-EVNASDFPPPPTDEELRLALPETPM 277
|
250 260
....*....|....*....|....*.
gi 1944883863 683 AMPVEEPSSkpvEEPSSKPVEEPATD 708
Cdd:pfam05058 278 LLGFNAPAT---SEPSSFEFPPPPTD 300
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
625-811 |
2.94e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 625 PSAKPVDEPSAKPIDETSAKPvDEPSEK-----PVDEPSAKPDDEPSAK--PDEEPSTKPVEEPSAMPVEEPSSKPVEEP 697
Cdd:PHA03247 2569 PPPRPAPRPSEPAVTSRARRP-DAPPQSarpraPVDDRGDPRGPAPPSPlpPDTHAPDPPPPSPSPAANEPDPHPPPTVP 2647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 698 sskPVEEPATDSASqegePMVEPSAKPVEGASAEQATAQEPNEPAPAAAEAV---SESVGAEPTGAVPEPAATEATKAee 774
Cdd:PHA03247 2648 ---PPERPRDDPAP----GRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVgslTSLADPPPPPPTPEPAPHALVSA-- 2718
|
170 180 190
....*....|....*....|....*....|....*..
gi 1944883863 775 qkveeTPEIVKPAAGEKEAVAETVAETSPGSEKQGVT 811
Cdd:PHA03247 2719 -----TPLPPGPAAARQASPALPAAPAPPAVPAGPAT 2750
|
|
| PRK10819 |
PRK10819 |
transport protein TonB; Provisional |
568-693 |
3.29e-03 |
|
transport protein TonB; Provisional
Pssm-ID: 236768 [Multi-domain] Cd Length: 246 Bit Score: 40.82 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 568 QAEKPADVEEVKAIDQTAEPSADQEKEQAAETtEESAEQVVEAVgqVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPvd 647
Cdd:PRK10819 43 APAQPISVTMVAPADLEPPQAVQPPPEPVVEP-EPEPEPIPEPP--KEAPVVIPKPEPKPKPKPKPKPKPVKKVEEQP-- 117
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1944883863 648 EPSEKPVDEPSAKPDDEPsakPDEEPSTKPVEEPSAMPVEEPSSKP 693
Cdd:PRK10819 118 KREVKPVEPRPASPFENT---APARPTSSTATAAASKPVTSVSSGP 160
|
|
| Treacle |
pfam03546 |
Treacher Collins syndrome protein Treacle; |
521-736 |
3.40e-03 |
|
Treacher Collins syndrome protein Treacle;
Pssm-ID: 460967 [Multi-domain] Cd Length: 531 Bit Score: 41.98 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 521 EEDKAAEEQKIEEQLPEETKADEKEPTVPAETA---ESVKDTAEEAKP--EGQAEKPADVEEVKAIDQTAEPSADQEKEQ 595
Cdd:pfam03546 29 EEESDSEEETPAAKTPLQAKPSGKTPQVRAASApakESPRKGAPPVPPgkTGPAAAQAQAGKPEEDSESSSEESDSDGET 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 596 AAETTEESAEQVVEAVGQV--VEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEP 673
Cdd:pfam03546 109 PAAATLTTSPAQVKPLGKNsqVRPASTVGKGPSGKGANPAPPGKAGSAAPLVQVGKKEEDSESSSEESDSEGEAPPAATQ 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1944883863 674 STKPVEEPSAMPVEEPSSKPVEEPSSK--PVEEPATDSASQEGEPMVEPSAKPVEGASAEQATAQ 736
Cdd:pfam03546 189 AKPSGKILQVRPASGPAKGAAPAPPQKagPVATQVKAERSKEDSESSEESSDSEEEAPAAATPAQ 253
|
|
| PHA03369 |
PHA03369 |
capsid maturational protease; Provisional |
455-679 |
3.41e-03 |
|
capsid maturational protease; Provisional
Pssm-ID: 223061 [Multi-domain] Cd Length: 663 Bit Score: 41.91 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 455 PGTPAAGSIAKGLDRKPATAEKKPEP---KPSDEVPTEVSSEDVISATGEklniggASEDVTEALE---KVLEEDKAAEE 528
Cdd:PHA03369 424 PGTSYGPEPVGPVPPQPTNPYVMPISmanMVYPGHPQEHGHERKRKRGGE------LKEELIETLKlvkKLKEEQESLAK 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 529 QKIEEQLPEETK--ADEKEPTVPAETAESVKDTAEEAKPEGQAEKPA------DVEEVK----AIDQTAEPSADQEKEQA 596
Cdd:PHA03369 498 ELEATAHKSEIKkiAESEFKNAGAKTAAANIEPNCSADAAAPATKRArpetktELEAVVrfpyQIRNMESPAFVHSFTST 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 597 AETTEESA-EQVVEAVGQVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSekpVDEPSAKPDDEPSAKPDEEPST 675
Cdd:PHA03369 578 TLAAAAGQgSDTAEALAGAIETLLTQASAQPAGLSLPAPAVPVNASTPASTPPPL---APQEPPQPGTSAPSLETSLPQQ 654
|
....
gi 1944883863 676 KPVE 679
Cdd:PHA03369 655 KPVL 658
|
|
| DD_DPY30_SDC1 |
cd22965 |
dimerization/docking (D/D) domain found in the DPY30/SDC1 family; This family includes DPY30 ... |
160-213 |
3.42e-03 |
|
dimerization/docking (D/D) domain found in the DPY30/SDC1 family; This family includes DPY30 from animals and its homologs, including SDC1 from yeast. DPY30, also called dumpy-30, was initially discovered in Caenorhabditis elegans as a key player in X chromosome dosage compensation. Human DPY30 plays a dual function in moderately allosterically regulating the methyltransferase activity of SET1/COMPASS (COMplex of Proteins ASsociated with Set1) enzymes and contributing to the recruitment of the complex to chromatin. DPY30 is the core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7. As part of the MLL1/MLL complex, DPY30 is involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. In a teratocarcinoma cell, DPY30 plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. It may also play an indirect or direct role in endosomal transport. Yeast SDC1, also called complex proteins associated with SET1 (COMPASS) protein SDC1, Set1C component SDC1, or suppressor of CDC25 protein 1, is the smallest subunit of COMPASS and interacts exclusively with Bre2 at the distal end of the catalytic module. It positively regulates the COMPASS catalytic module by stabilizing the non-canonical Bre2 SPRY domain. The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently activates gene expression by regulating transcription elongation and plays a role in telomere length maintenance. This model corresponds to the C-terminal helical bundle domain of DPY30/SDC1, which is called dimerization/docking (D/D) domain. It forms a homodimer, which directly interacts with the Ash2L (Bre2 in yeast) subunit of COMPASS through its DPY30-binding motif (DBM).
Pssm-ID: 438534 Cd Length: 41 Bit Score: 36.63 E-value: 3.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1944883863 160 ARAYLLDKLLPTLILGIEKLlmeAEKRglaesneadPNfNPINFLGQYLMRNNP 213
Cdd:cd22965 1 TRQYLDKTVVPVLLEGLKEL---AKER---------PE-DPLEFLAEYLLKNSP 41
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
621-835 |
3.51e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 42.14 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 621 LAEEP-----SAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPddePSAKPDEEPSTKPVEEPSAMPVEEPSSKPVE 695
Cdd:PRK07003 356 LAFEPavtggGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTA---VTGAAGAALAPKAAAAAAATRAEAPPAAPAP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 696 EPSSKPVEEPATDSASQEGEPMVEPSAKPVEGASAEQATAQEPNEPAPAAAEAVSESVGAEPTgAVPEPAAT--EATKAE 773
Cdd:PRK07003 433 PATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPR-AAAPSAATpaAVPDAR 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1944883863 774 EQKVEETPEIVKPAAG-EKEAVAETVAETSPGSEKQGVTFHRDTVETTG---KSDHSSIKSPTKTP 835
Cdd:PRK07003 512 APAAASREDAPAAAAPpAPEARPPTPAAAAPAARAGGAAAALDVLRNAGmrvSSDRGARAAAAAKP 577
|
|
| Dpy-30 |
pfam05186 |
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ... |
160-213 |
3.75e-03 |
|
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the Dpy-30 proteins hence the motifs name. It is about 40 residues long and is probably formed of two alpha-helices. It may be a dimerization motif analogous to pfam02197 (Bateman A pers obs).
Pssm-ID: 428357 Cd Length: 42 Bit Score: 36.43 E-value: 3.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1944883863 160 ARAYLLDKLLPTLILGIEKLlmeAEKRglaesneadPNfNPINFLGQYLMRNNP 213
Cdd:pfam05186 2 ARQYLNKTVAPILLQGLTEL---AKER---------PE-DPIEYLADYLLKNNP 42
|
|
| EF-hand_1 |
pfam00036 |
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
913-940 |
3.83e-03 |
|
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.
Pssm-ID: 425435 [Multi-domain] Cd Length: 29 Bit Score: 36.22 E-value: 3.83e-03
10 20
....*....|....*....|....*...
gi 1944883863 913 LEQLFEKWDNDGSGYLDLEELHSVMSKF 940
Cdd:pfam00036 2 LKEIFRLFDKDGDGKIDFEEFKELLKKL 29
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
516-733 |
4.45e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 41.56 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 516 LEKVLEEDKA--AEEQKIEEQLPEE------TKADEKEPTVPAETAESVKDTAEEAKPEGQAEKP--------------A 573
Cdd:PRK10811 502 LPKLHEEAMAlpSEEEFAERKRPEQpalatfAMPDVPPAPTPAEPAAPVVAAAPKAAAATPPAQPgllsrffgalkalfS 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 574 DVEEVKAIDQTAEPS----------------------------ADQEKEQAAETTEESAEQVVEAVGQVVEPSTELAEEP 625
Cdd:PRK10811 582 GGEETKPQEQPAPKAeakperqqdrrkprqnnrrdrnerrdtrDNRTRREGRENREENRRNRRQAQQQTAETRESQQAEV 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 626 SAKPV--DEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVeepsaMP------------VEEPSS 691
Cdd:PRK10811 662 TEKARtqDEQQQAPRRERQRRRNDEKRQAQQEAKALNVEEQSVQETEQEERVQQV-----QPrrkqrqlnqkvrIEQSVA 736
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1944883863 692 KPVEEPSS--KPVEEPATDSASQEGEPMVEPSAKPVEGASAEQA 733
Cdd:PRK10811 737 EEAVAPVVeeTVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQD 780
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
520-676 |
4.52e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.33 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 520 LEEDKAAEEQKIEEQLPEETKADEKEptvpaetaesvKDTAEEAKPEGQAEKpadveevkaidqtaepsadQEKEQAAET 599
Cdd:PRK09510 92 LQQKQAAEQERLKQLEKERLAAQEQK-----------KQAEEAAKQAALKQK-------------------QAEEAAAKA 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1944883863 600 TEESAEQVVEAVGQVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTK 676
Cdd:PRK09510 142 AAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKK 218
|
|
| PRK05901 |
PRK05901 |
RNA polymerase sigma factor; Provisional |
526-735 |
4.89e-03 |
|
RNA polymerase sigma factor; Provisional
Pssm-ID: 235640 [Multi-domain] Cd Length: 509 Bit Score: 41.13 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 526 AEEQKIEEQLPEETKADEKEPTVPAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAE 605
Cdd:PRK05901 8 AELAAEEEAKKKLKKLAAKSKSKGFITKEEIKEALESKKKTPEQIDQVLIFLSGMVKDTDDATESDIPKKKTKTAAKAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 606 qvveavgqVVEPSTELAEEPSAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDEPSAKPDEEPSTKPVEEPSAMP 685
Cdd:PRK05901 88 --------AKAPAKKKLKDELDSSKKAEKKNALDKDDDLNYVKDIDVLNQADDDDDDDDDDDLDDDDIDDDDDDEDDDED 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1944883863 686 VEEPSSKPVEEPSSKPVEEP-ATDSASQEGEPMVEPSAKPVEGASAEQATA 735
Cdd:PRK05901 160 DDDDDVDDEDEEKKEAKELEkLSDDDDFVWDEDDSEALRQARKDAKLTATA 210
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
468-593 |
5.14e-03 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 41.52 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 468 DRKPATAEKKPEPKPSDEVPTEVSSEDVISATGEKLNigGASEDVTEALEKVLEE--------------DKAAEEQKIEE 533
Cdd:PRK14900 921 EQKPTQDGPAAEAQPAQENTVVESAEKAVAAVSEAAQ--QAATAVASGIEKVAEAvrktvrrsvkkaaaTRAAMKKKVAK 998
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 534 QLPEETKADEKeptVPAETAESVKDTAEEAKPEGQAEKPAdveEVKAIDQTAEPSADQEK 593
Cdd:PRK14900 999 KAPAKKAAAKK---AAAKKAAAKKKVAKKAPAKKVARKPA---AKKAAKKPARKAAGRKA 1052
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
470-712 |
5.34e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 470 KPATAEKKPEPKPSDEVPTEVSSEDVISATGEKLNIGGASEDvtealEKVLEEDKAAEEQKIEEQlpEETKADE--KEPT 547
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA-----KKAEEDKKKAEEAKKAEE--DEKKAAEalKKEA 1698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 548 VPAETAESVKDTAEEAKPegQAEKPADVEEVKAID-QTAEPSADQEKEQAAETTEESAEQvvEAVGQVVEPSTELAEEPS 626
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKK--KAEELKKAEEENKIKaEEAKKEAEEDKKKAEEAKKDEEEK--KKIAHLKKEEEKKAEEIR 1774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 627 AKP-------VDEPSAKPIDETSAKPVDEPSEKPVDEPSAKPDDE--PSAKPDEEPSTKPVEEPSAMPVEEpsSKPVEEP 697
Cdd:PTZ00121 1775 KEKeavieeeLDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLviNDSKEMEDSAIKEVADSKNMQLEE--ADAFEKH 1852
|
250
....*....|....*
gi 1944883863 698 SSKPVEEPATDSASQ 712
Cdd:PTZ00121 1853 KFNKNNENGEDGNKE 1867
|
|
| DUF3664 |
pfam12406 |
Surface protein; This family of proteins is found in eukaryotes. Proteins in this family are ... |
637-706 |
6.35e-03 |
|
Surface protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 131 and 312 amino acids in length.
Pssm-ID: 289191 [Multi-domain] Cd Length: 99 Bit Score: 37.93 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 637 PIDETSAKPVDEPSEKPVDEPSAKPDD--EPSAKPDE-EPSTKPVEEPSAMPVEEPSS----------KPVEEPSSKPVE 703
Cdd:pfam12406 17 PLDPDQLIDQIEPSEQPAQQEPIEPQQptQPSTEPEElQPETVTVEVPEPVTSEEPKEsdqteeqkheEPEASPAPEPVD 96
|
...
gi 1944883863 704 EPA 706
Cdd:pfam12406 97 EPA 99
|
|
| DD_AK7 |
cd22967 |
dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate ... |
161-212 |
7.42e-03 |
|
dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate kinase (AK7, EC2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 7, is a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. It also displays broad nucleoside diphosphate kinase activity. AK7 is involved in maintaining ciliary structure and function. This model corresponds to the C-terminal domain of AK7, which shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.
Pssm-ID: 438536 [Multi-domain] Cd Length: 41 Bit Score: 35.54 E-value: 7.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1944883863 161 RAYLLDKLLPTLIlgiekllmeaekRGLAESNEADPNfNPINFLGQYLMRNN 212
Cdd:cd22967 3 RNYLMKYVMPTLT------------EGLVEVCKVRPE-DPVDFLAEYLFKHN 41
|
|
| DD_NDKH5-like |
cd22970 |
dimerization/docking (D/D) domain found in nucleoside diphosphate kinase homolog 5 (NDKH5) ... |
159-213 |
7.81e-03 |
|
dimerization/docking (D/D) domain found in nucleoside diphosphate kinase homolog 5 (NDKH5)-like family; The NDKH5 family includes NDKH5, Chlamydomonas reinhardtii flagellar radial spoke protein 23 (RSP23) and similar proteins. NDKH5, also called NME5, NDP kinase homolog 5, inhibitor of p53-induced apoptosis-beta (IPIA-beta), testis-specific nm23 homolog, or nm23-H5, is specifically expressed in testis germinal cells. It may not have NDK kinase activity. It confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes including Gpx5. It may play a role in spermiogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species. RSP23, also called p61, is a functional Ca2+/calmodulin-regulated nucleoside diphosphate kinase (NDK) from the flagella of Chlamydomonas that is present in the radial spoke stalk. It binds calmodulin in a calcium-dependent manner. Members of this family contain a C-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.
Pssm-ID: 438539 Cd Length: 45 Bit Score: 35.59 E-value: 7.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1944883863 159 DARAYLLDKLLPTLIlgiekllmeaekRGLAESNEADPNfNPINFLGQYLMRNNP 213
Cdd:cd22970 4 AAKDYLSKHVNPTLL------------KGLTELCKEKPA-DPVTWLADWLLENNP 45
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
883-938 |
8.07e-03 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 36.37 E-value: 8.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1944883863 883 GEGYIETEEekYLRLQKSRREAQSAKRklmLEQLFEKWDNDGSGYLDLEELHSVMS 938
Cdd:cd00051 13 GDGTISADE--LKAALKSLGEGLSEEE---IDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
543-701 |
8.20e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 40.14 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 543 EKEPTVPAETAESVKDTAeeakPEGQAEKPADVEEVKAIDqtaEPSADQEKEQAAETTEESAEQVVEAVGqvvepsTELA 622
Cdd:NF040712 189 DPDFGRPLRPLATVPRLA----REPADARPEEVEPAPAAE---GAPATDSDPAEAGTPDDLASARRRRAG------VEQP 255
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1944883863 623 EEPSAKPVDEPSAKPIDETSAKPVDEPSEKPvdepsakpdDEPSAKPDEEPSTKPVEEPsAMPVEEPSSKPVEEPSSKP 701
Cdd:NF040712 256 EDEPVGPGAAPAAEPDEATRDAGEPPAPGAA---------ETPEAAEPPAPAPAAPAAP-AAPEAEEPARPEPPPAPKP 324
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
913-974 |
8.31e-03 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 36.46 E-value: 8.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1944883863 913 LEQLFEKWDNDGSGYLDLEELHSVMSKFKENMEakiMQKAKTIMMKEEYD----NRLSKREFKAYI 974
Cdd:pfam13499 4 LKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEP---LSDEEVEELFKEFDldkdGRISFEEFLELY 66
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
912-976 |
8.40e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 38.23 E-value: 8.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1944883863 912 MLEQLFEKWDNDGSGYLDLEELHSVMSKfkeNMEAKIMQKAKTIMMK--EEYDNRLSKREFKAYIEA 976
Cdd:COG5126 34 LWATLFSEADTDGDGRISREEFVAGMES---LFEATVEPFARAAFDLldTDGDGKISADEFRRLLTA 97
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
529-788 |
8.44e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 40.68 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 529 QKIEEQLPEETKADEKEPTVPAE-TAESVKDTAEEAKPEGQAEKP----ADVEEVKAidqTAEPSADQEKEQAAETTEes 603
Cdd:PLN03209 326 QRVPPKESDAADGPKPVPTKPVTpEAPSPPIEEEPPQPKAVVPRPlspyTAYEDLKP---PTSPIPTPPSSSPASSKS-- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 604 aeqvVEAVGQVVEPSTElaeePSAKPvdepsAKPIDETSAKPVDEPSEKPVdEPSAkpddepsAKPDEEPSTKP---VEE 680
Cdd:PLN03209 401 ----VDAVAKPAEPDVV----PSPGS-----ASNVPEVEPAQVEAKKTRPL-SPYA-------RYEDLKPPTSPsptAPT 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 681 PSAMPVEEPSSKPvEEPSSKPVEEpATDSASQEGEPMVEPSAKPVEgASAEQATAQEPNEPAPAAAEAVSESVGAEPTGA 760
Cdd:PLN03209 460 GVSPSVSSTSSVP-AVPDTAPATA-ATDAAAPPPANMRPLSPYAVY-DDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSA 536
|
250 260 270
....*....|....*....|....*....|..
gi 1944883863 761 VPEPAATEATKAEEQKVEETP----EIVKPAA 788
Cdd:PLN03209 537 PPTALADEQHHAQPKPRPLSPytmyEDLKPPT 568
|
|
| PHA03381 |
PHA03381 |
tegument protein VP22; Provisional |
649-808 |
8.62e-03 |
|
tegument protein VP22; Provisional
Pssm-ID: 177618 [Multi-domain] Cd Length: 290 Bit Score: 39.99 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 649 PSEKP--VDEPSAKPDDEPSAkPDEEPSTKPVEEPSA---MPVEEPSSKPVEEPSSKPVEEP------ATDSASQEGEPM 717
Cdd:PHA03381 7 PRPKPhgTDEVEADVYYDFIS-PDASPARVSFEEPADrarRGAGQARGRSQAERRFHHYDEAradypyYTGSSSEDERPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 718 -VEPSAKPVEGASAEQATAQEPNEPApaaaeavsesvgAEPTGAVPEPAATEATKAEEQKVEETPEIVKPAAGEKEAVAE 796
Cdd:PHA03381 86 dPRPSRRPHAQPEASGPGPARGARGP------------AGSRGRGRRAESPSPRDPPNPKGASAPRGRKSACADSAALLD 153
|
170
....*....|..
gi 1944883863 797 TVAETSPGSEKQ 808
Cdd:PHA03381 154 APAPAAPKRQKT 165
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
468-736 |
8.84e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 40.77 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 468 DRKPATAEKKPEPKPSDEVPTEVSSEDVISATGEKLNIGGASE-DVTEALEKVLEEDKAAEEQKI----EEQLPEETKAD 542
Cdd:NF033838 203 EEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLkEAVEKNVATSEQDKPKRRAKRgvlgEPATPDKKEND 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 543 EK-------EPTVPAETAESVKDTAEEAKPEGQAEKpadveevKAIDQTAEpsadQEKEQAAETTEESAEQVVEAVGQVV 615
Cdd:NF033838 283 AKssdssvgEETLPSPSLKPEKKVAEAEKKVEEAKK-------KAKDQKEE----DRRNYPTNTYKTLELEIAESDVKVK 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 616 EPSTELAEEPSAKPVDEpsaKPIDETSAKPVDEPSEKPVDEpSAKPDDEpsaKPDEEPSTKPVEEpsampvEEPSSKPVE 695
Cdd:NF033838 352 EAELELVKEEAKEPRNE---EKIKQAKAKVESKKAEATRLE-KIKTDRK---KAEEEAKRKAAEE------DKVKEKPAE 418
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1944883863 696 EPSSKPVEEPATDSASQEgEPMVEPSAKPVEGASAEQATAQ 736
Cdd:NF033838 419 QPQPAPAPQPEKPAPKPE-KPAEQPKAEKPADQQAEEDYAR 458
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
646-818 |
9.34e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 40.35 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 646 VDEPSEKPVDEPSAKpdDEPSAKPDEEPStKPVEEPSAMPVEEPSSKPVEEPSSKPVEEPATDSASQEGE--PMVEPSAK 723
Cdd:PRK13108 292 VDEALEREPAELAAA--AVASAASAVGPV-GPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGEstPAVEETSE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 724 P-VEGASAEQATAQEPNEPAPAaaeavSESVGAEPTGAVPEPAatEATKAEEQKVEETPEIVKPAAGEKEAVAETVAETS 802
Cdd:PRK13108 369 AdIEREQPGDLAGQAPAAHQVD-----AEAASAAPEEPAALAS--EAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDP 441
|
170
....*....|....*.
gi 1944883863 803 PGSEKQGVTFHRDTVE 818
Cdd:PRK13108 442 AEPDGIRRQDDFSSRR 457
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
466-677 |
9.35e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 40.34 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 466 GLDRKPATAEKKPEPKPSDEVPTEVSSEDviSATGEKLNIGGASEDVTEALEKVLEEDKAAEEQKIEEQLPEETKADEKE 545
Cdd:PHA03169 70 ESDTETAEESRHGEKEERGQGGPSGSGSE--SVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPH 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 546 PTVPAETAESVKDTAEEAKPEGQAEKPADVEEvkaiDQTAEPSADQEKEQAAETTEESAEQvveavgqvVEPSTELAEEP 625
Cdd:PHA03169 148 EPAPPESHNPSPNQQPSSFLQPSHEDSPEEPE----PPTSEPEPDSPGPPQSETPTSSPPP--------QSPPDEPGEPQ 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1944883863 626 SAKPVDEPSAKPIDETSAKPVDEPSEKPVDEPSaKPDDEPSAKPDEEPSTKP 677
Cdd:PHA03169 216 SPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFP-GHRSHSYTVVGWKPSTRP 266
|
|
| EFh |
smart00054 |
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ... |
913-940 |
9.42e-03 |
|
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.
Pssm-ID: 197492 [Multi-domain] Cd Length: 29 Bit Score: 35.05 E-value: 9.42e-03
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
536-736 |
9.63e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 40.60 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 536 PEETKADEKEPTVPAETAESVKDTAEEAKPEGQAEKPADVEEVKAIDQTAEPSADQEKEQAAETTEESAEQVVEAVGQ-- 613
Cdd:PRK07003 391 VGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAqp 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1944883863 614 VVEPSTELAEEPSAKPV----DEPSAKPIDETSAKPVDEP----SEKPVDEPSAKPDDEPSAKPDEEPSTKP-------- 677
Cdd:PRK07003 471 PADSGSASAPASDAPPDaafePAPRAAAPSAATPAAVPDArapaAASREDAPAAAAPPAPEARPPTPAAAAPaaraggaa 550
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1944883863 678 ----VEEPSAMPVEEPSSKPVEEPSSKPVEEPATDSAS---------QEGEPMVEPSAKPVEGASAEQATAQ 736
Cdd:PRK07003 551 aaldVLRNAGMRVSSDRGARAAAAAKPAAAPAAAPKPAaprvavqvpTPRARAATGDAPPNGAARAEQAAES 622
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