|
Name |
Accession |
Description |
Interval |
E-value |
| DD_EFCAB5 |
cd22968 |
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 ... |
111-167 |
1.49e-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: 109.21 E-value: 1.49e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 111 ETRVYLVDKVLPTMILGMEKLLLEVDKRGLAEKE---EQDPNFNPINYLAQYLMRNNPRY 167
Cdd:cd22968 1 ETRAYLVEKVLPTLVPGLEKLLKEVERRGLLEEEgrpEPAPRFNPINWLAQYLMRNNPRY 60
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
555-701 |
3.91e-09 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 61.59 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 555 VQEGDAKPSEQDQPKEPATEQPSEQAKTEEQVTEESAKPASQEVPEQPVEQAsTQEEETEESGKPAENVTAQSEAAPVSD 634
Cdd:PRK10811 848 VRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPV-VVAEPQPEEVVVVETTHPEVIAAPVTE 926
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919047147 635 IPTVVTDDTAAVASETTAGSAPEPTSAPETSP--------PQAVVSDKEKSSANVEEKEKDEAETEGQDAFEDDV 701
Cdd:PRK10811 927 QPQVITESDVAVAQEVAEHAEPVVEPQDETADieeaaetaEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEV 1001
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
387-606 |
3.92e-06 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 51.53 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 387 DEVESTYSDDEDLADPKFFNNSIEVNEEGSPKPEEKQDEGTEKKTED--VKNPEVKVTEETEKKENESSEETGAEGGKGE 464
Cdd:TIGR00927 691 GEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEgeEVEDEGEGEAEGKHEVETEGDRKETEHEGET 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 465 GEEVVTKEGEQNIEESSKGETA--EESAETKEHPAAEKEEDKKELDETVQETADVKEGEAVTEEKG-TVETTEEPPSDQP 541
Cdd:TIGR00927 771 EAEGKEDEDEGEIQAGEDGEMKgdEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQElNAENQGEAKQDEK 850
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919047147 542 VTEAKpeaaaeekvQEGDAKPSEQDQPKEPATEQPSEQAKTEEQVTEESAKPASQEVPEQPVEQA 606
Cdd:TIGR00927 851 GVDGG---------GGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPETRQKQA 906
|
|
| DamX |
COG3266 |
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ... |
572-680 |
1.27e-05 |
|
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: 49.46 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 572 ATEQPSEQAKTEEQVTeeSAKPASQEVPEQPVEQA---STQEEETEESGKPAENVTAQSEAAPVSDIPTVVTdDTAAVAS 648
Cdd:COG3266 254 ALKAPSQASSASAPAT--TSLGEQQEVSLPPAVAAqpaAAAAAQPSAVALPAAPAAAAAAAAPAEAAAPQPT-AAKPVVT 330
|
90 100 110
....*....|....*....|....*....|..
gi 919047147 649 ETTAGSAPEPTSAPETSPPQAVVSDKEKSSAN 680
Cdd:COG3266 331 ETAAPAAPAPEAAAAAAAPAAPAVAKKLAADE 362
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
470-630 |
4.02e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 44.58 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 470 TKEGEQNIEESSKGETAEES--------AETKEHPAAEKEEDKKELDETVQETADVKEGEAVTEEKGTVETTEEPPSDQP 541
Cdd:PHA03169 69 TESDTETAEESRHGEKEERGqggpsgsgSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 542 VTEAKPEAAAEEKVQEGDAKPS--EQDQPKEPATEQPSEQAKTEEQVTEESAKPASQEVPEQPVEQAStQEEETEESGKP 619
Cdd:PHA03169 149 PAPPESHNPSPNQQPSSFLQPSheDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQS-PTPQQAPSPNT 227
|
170
....*....|.
gi 919047147 620 AENVTAQSEAA 630
Cdd:PHA03169 228 QQAVEHEDEPT 238
|
|
| Dpy-30 |
pfam05186 |
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ... |
111-165 |
7.01e-04 |
|
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: 38.75 E-value: 7.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 919047147 111 ETRVYLVDKVLPTmilgmeklLLEvdkrGLAEKEEQDPNfNPINYLAQYLMRNNP 165
Cdd:pfam05186 1 PARQYLNKTVAPI--------LLQ----GLTELAKERPE-DPIEYLADYLLKNNP 42
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
397-865 |
1.99e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 397 EDLADPKFFNNSIEVNEEGSPKPEEKQDEGTEKKTEDVKNPEVKVTEETEKKENESSEETGAEGGKGEGEEVVTKEGEQN 476
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 477 IEESSKGETAEESAETKEHPAAEKEEDKKELDETVQETADvKEGEAVTEEKGTVETTEEppsdqpvteakpeaaaEEKVQ 556
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK-KKADAAKKKAEEKKKADE----------------AKKKA 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 557 EGDAKPSEQDQPKEPATEQPSEQAKTEEQV--TEESAKPASQEVPEQPVEQASTQEEETEESGKPAENVTAQSEAAPVSD 634
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKkkADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 635 iptvvtddtAAVASETTAGSAPEPTSAPETSPPQAVVSDKEKSSANVEEKEKDEAETEGQDAFEDDVRLPSPPPTADRPP 714
Cdd:PTZ00121 1481 ---------EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 715 PTRQSVTFAEGTRFDEERKALETRGTGSMSQAsafdetslnvsqfvnlietflgdEPGMEAFNSLVRYVRDGYMETEEEK 794
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKA-----------------------EEAKKAEEARIEEVMKLYEEEKKMK 1608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 795 RERLLKAHREHVTA---------KRKTRVDGLFEKWDNDGSGYLDMDEIETILSKYKDGMEKETVRRVKSKLRKDETDNR 865
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAeelkkaeeeKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
818-876 |
4.78e-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: 36.76 E-value: 4.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 919047147 818 FEKWDNDGSGYLDMDEIETILSKYKDGMEKETVRRVKSKLRKDEtDNRLSKREFREFVT 876
Cdd:cd00051 6 FRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDG-DGKIDFEEFLELMA 63
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
1005-1086 |
6.93e-03 |
|
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: 38.52 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 1005 VETGKPIHVPRVNNHgsiYFWNTDRDAEDRD-GSLIVVAVKDQRkRVFGLLAIDTLRDPHTkaiFITHEIQFFQGVGKAF 1083
Cdd:smart00065 63 AETGRPLNIPDVEAD---PLFAEDLLGRYQGvRSFLAVPLVADG-ELVGVLALHNKKSPRP---FTEEDEELLQALANQL 135
|
...
gi 919047147 1084 SIA 1086
Cdd:smart00065 136 AIA 138
|
|
| GAF |
pfam01590 |
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ... |
1005-1086 |
8.28e-03 |
|
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 460259 [Multi-domain] Cd Length: 133 Bit Score: 38.23 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 1005 VETGKPIHVPRVNNHGSiyfWNTDRDAEDRDG--SLIVVAVKDQRkRVFGLLAIDTLRDPHTKaifitHEIQFFQGVGKA 1082
Cdd:pfam01590 58 LRTGRPLVVPDAAGDPR---FLDPLLLLRNFGirSLLAVPIIDDG-ELLGVLVLHHPRPPFTE-----EELELLEVLADQ 128
|
....
gi 919047147 1083 FSIA 1086
Cdd:pfam01590 129 VAIA 132
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
817-876 |
8.53e-03 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 36.46 E-value: 8.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919047147 817 LFEKWDNDGSGYLDMDEIETILSKYKDG--MEKETVRRVKSKLRKDEtDNRLSKREFREFVT 876
Cdd:pfam13499 7 AFKLLDSDGDGYLDVEELKKLLRKLEEGepLSDEEVEELFKEFDLDK-DGRISFEEFLELYS 67
|
|
| ftsN |
TIGR02223 |
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ... |
562-734 |
9.57e-03 |
|
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: 39.67 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 562 PSEQDQPKEPATEQPSEQAKTEEQVTEESAKPASQ-----EVPEQPVEQASTQEEETEESGKPAENVTAQSEAAPVSDIP 636
Cdd:TIGR02223 48 LTESKQANEPETLQPKNQTENGETAADLPPKPEERwsyieELEAREVLINDPEEPSNGGGVEESAQLTAEQRQLLEQMQA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 637 TVVTDDTAAVASETTAGSAPEPTSAPETSPPQAvVSDKEKSSANVEEKEKDEAETEGQDAFEDDVRLPSPPPTADRPPPT 716
Cdd:TIGR02223 128 DMRAAEKVLATAPSEQTVAVEARKQTAEKKPQK-ARTAEAQKTPVETEKIASKVKEAKQKQKALPKQTAETQSNSKPIET 206
|
170
....*....|....*...
gi 919047147 717 RQSVTFAEGTRFDEERKA 734
Cdd:TIGR02223 207 APKADKADKTKPKPKEKA 224
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DD_EFCAB5 |
cd22968 |
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 5 ... |
111-167 |
1.49e-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: 109.21 E-value: 1.49e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 111 ETRVYLVDKVLPTMILGMEKLLLEVDKRGLAEKE---EQDPNFNPINYLAQYLMRNNPRY 167
Cdd:cd22968 1 ETRAYLVEKVLPTLVPGLEKLLKEVERRGLLEEEgrpEPAPRFNPINWLAQYLMRNNPRY 60
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
555-701 |
3.91e-09 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 61.59 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 555 VQEGDAKPSEQDQPKEPATEQPSEQAKTEEQVTEESAKPASQEVPEQPVEQAsTQEEETEESGKPAENVTAQSEAAPVSD 634
Cdd:PRK10811 848 VRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPV-VVAEPQPEEVVVVETTHPEVIAAPVTE 926
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919047147 635 IPTVVTDDTAAVASETTAGSAPEPTSAPETSP--------PQAVVSDKEKSSANVEEKEKDEAETEGQDAFEDDV 701
Cdd:PRK10811 927 QPQVITESDVAVAQEVAEHAEPVVEPQDETADieeaaetaEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEV 1001
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
490-684 |
6.33e-08 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 57.36 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 490 AETKEHPAAEKEEDKKELDETVQETADVKEGEAVTEEKGTVETTEEPPSDQPVTEAkpeaaaeekVQEGDAKPSEQDQPK 569
Cdd:PRK10811 848 VRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAE---------PQPEEVVVVETTHPE 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 570 ---EPATEQPSEQAKTEEQVTEESAKPASQEVPEQPVEQASTQEEETEESGKPAENVTAQSEAAPVSDIPTVVTDDTAAV 646
Cdd:PRK10811 919 viaAPVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVE 998
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 919047147 647 ASETTAGSAPEPTS------------APETSPPQAVVSDKEKSSANVEEK 684
Cdd:PRK10811 999 PEVAPAQVPEATVEhnhatapmtrapAPEYVPEAPRHSDWQRPTFAFEGK 1048
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
387-606 |
3.92e-06 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 51.53 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 387 DEVESTYSDDEDLADPKFFNNSIEVNEEGSPKPEEKQDEGTEKKTED--VKNPEVKVTEETEKKENESSEETGAEGGKGE 464
Cdd:TIGR00927 691 GEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEgeEVEDEGEGEAEGKHEVETEGDRKETEHEGET 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 465 GEEVVTKEGEQNIEESSKGETA--EESAETKEHPAAEKEEDKKELDETVQETADVKEGEAVTEEKG-TVETTEEPPSDQP 541
Cdd:TIGR00927 771 EAEGKEDEDEGEIQAGEDGEMKgdEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQElNAENQGEAKQDEK 850
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919047147 542 VTEAKpeaaaeekvQEGDAKPSEQDQPKEPATEQPSEQAKTEEQVTEESAKPASQEVPEQPVEQA 606
Cdd:TIGR00927 851 GVDGG---------GGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPETRQKQA 906
|
|
| DD_IQCK |
cd22969 |
dimerization/docking (D/D) domain found in IQ domain-containing protein K (IQCK) and similar ... |
115-165 |
1.18e-05 |
|
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: 44.03 E-value: 1.18e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 919047147 115 YLVDKVLPTMILGMEKLLLEVDKRGLaeKEEQDPNFNPINYLAQYLMRNNP 165
Cdd:cd22969 10 YLEEYIFPVLLPALEEMLEEAKKEDC--FERKRTKFNGLDFLTEYLYNNNP 58
|
|
| DamX |
COG3266 |
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ... |
572-680 |
1.27e-05 |
|
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: 49.46 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 572 ATEQPSEQAKTEEQVTeeSAKPASQEVPEQPVEQA---STQEEETEESGKPAENVTAQSEAAPVSDIPTVVTdDTAAVAS 648
Cdd:COG3266 254 ALKAPSQASSASAPAT--TSLGEQQEVSLPPAVAAqpaAAAAAQPSAVALPAAPAAAAAAAAPAEAAAPQPT-AAKPVVT 330
|
90 100 110
....*....|....*....|....*....|..
gi 919047147 649 ETTAGSAPEPTSAPETSPPQAVVSDKEKSSAN 680
Cdd:COG3266 331 ETAAPAAPAPEAAAAAAAPAAPAVAKKLAADE 362
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
568-681 |
2.91e-05 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 48.01 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 568 PKEPATEQP----SEQAKTEEQVTEESAKPASQEVPEQPVEQASTQEEETEESGKPAENVTAQSEAAPVSDIPTVVTddT 643
Cdd:PRK10905 124 PTEPATVAPvrngNASRQTAKTQTAERPATTRPARKQAVIEPKKPQATAKTEPKPVAQTPKRTEPAAPVASTKAPAA--T 201
|
90 100 110
....*....|....*....|....*....|....*...
gi 919047147 644 AAVASETTAGSAPEPTSAPETSPPQAVVSDkeKSSANV 681
Cdd:PRK10905 202 STPAPKETATTAPVQTASPAQTTATPAAGG--KTAGNV 237
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
570-733 |
6.57e-05 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 47.28 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 570 EPATEQPSEQAKTEEQVTEESAKPASQEVPEQP--VEQASTQEEETEESGKPAENVTAQSEAAPVSDIPTVVTDDTAAV- 646
Cdd:PRK13108 294 EALEREPAELAAAAVASAASAVGPVGPGEPNQPddVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEr 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 647 -ASETTAGSAPEptsAPETSPPQAVVSDKEKSSANVEEKEKDEAETEGQDAFEDDVRLPSPPPTADRPPPTRQSVTFAEG 725
Cdd:PRK13108 374 eQPGDLAGQAPA---AHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPAEPDGIRRQ 450
|
....*...
gi 919047147 726 TRFDEERK 733
Cdd:PRK13108 451 DDFSSRRR 458
|
|
| DD_DPY30_SDC1-like |
cd22958 |
dimerization/docking (D/D) domain found in the DPY30/SDC1-like family; The DPY30/SDC1-like ... |
115-164 |
6.61e-05 |
|
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: 41.28 E-value: 6.61e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 919047147 115 YLVDKVLPTMILGMEKLLlevdkrglAEKEEqdpnfNPINYLAQYLMRNN 164
Cdd:cd22958 4 YLSETVLPTLIPALAELL--------KARPE-----DPLEWLAEYLLRNN 40
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
471-646 |
1.47e-04 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 46.32 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 471 KEGEQNIEESSKGETAEESAEtkEHpAAEKEEDKKELDETVQE-TADVKEGEAVTEEKGTVETTEEPPSDQPVTEAKPEA 549
Cdd:PTZ00341 421 KQKYMDMLDGSEDESVEDNEE--EH-SGDANEEELSVDEHVEEhNADDSGEQQSDDESGEHQSVNEIVEEQSVNEHVEEP 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 550 AAEEKVQEGDAKPSEQDQPKEPATEQPSEQAKTEEQVTEESAKPASQEVPEQPVEQastqeeeteesgkPAENVTAQSEA 629
Cdd:PTZ00341 498 TVADIVEQETVDEHVEEPAVDENEEQQTADEHVEEPTIAEEHVEEEISTAEEHIEE-------------PASDVQQDSEA 564
|
170
....*....|....*..
gi 919047147 630 APVSDIPTVVTDDTAAV 646
Cdd:PTZ00341 565 APTIEIPDTLFYDILGV 581
|
|
| PRK13914 |
PRK13914 |
invasion associated endopeptidase; |
498-696 |
1.60e-04 |
|
invasion associated endopeptidase;
Pssm-ID: 237555 [Multi-domain] Cd Length: 481 Bit Score: 45.95 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 498 AEKEEDKKELDET---VQETADVkEGEAVTEEKG----TVETTEEPPSDQpVTEAKPEAAAEEKVQEGDAKPS-----EQ 565
Cdd:PRK13914 75 AAAEKTEKSVSATwlnVRSGAGV-DNSIITSIKGgtkvTVETTESNGWHK-ITYNDGKTGFVNGKYLTDKVTStpvapTQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 566 DQPKEPATEQ--PSEQAKTE-EQVTEESA-KPASQEVPEQPV--EQASTQEEeteesgKPAENVTAQS--EAAPVSDI-- 635
Cdd:PRK13914 153 EVKKETTTQQaaPAAETKTEvKQTTQATTpAPKVAETKETPVvdQNATTHAV------KSGDTIWALSvkYGVSVQDIms 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919047147 636 ------PTVVTDDTAAV--ASETTAGSAPEPTSAPeTSPPQAVVSDKEKSSANVEEKEKDEAETEGQDA 696
Cdd:PRK13914 227 wnnlssSSIYVGQKLAIkqTANTATPKAEVKTEAP-AAEKQAAPVVKENTNTNTATTEKKETTTQQQTA 294
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
469-634 |
3.76e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 45.03 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 469 VTKEGEQNIEESSKGETAEESAETKEHPAAEKEEDKKELDETVQETADVKE----GEAVTEEKGTVETTEEPPSDQPVTE 544
Cdd:PRK10811 847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEpvvvAEPQPEEVVVVETTHPEVIAAPVTE 926
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 545 AKPEAAAEEKVQEG-----------DAKPSEQDQPKEPATEQPSEQAKTEEQVTEESAKPASQEVPEQPVEQASTQEEET 613
Cdd:PRK10811 927 QPQVITESDVAVAQevaehaepvvePQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQV 1006
|
170 180
....*....|....*....|.
gi 919047147 614 EESGKPAENVTAQSEAAPVSD 634
Cdd:PRK10811 1007 PEATVEHNHATAPMTRAPAPE 1027
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
470-630 |
4.02e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 44.58 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 470 TKEGEQNIEESSKGETAEES--------AETKEHPAAEKEEDKKELDETVQETADVKEGEAVTEEKGTVETTEEPPSDQP 541
Cdd:PHA03169 69 TESDTETAEESRHGEKEERGqggpsgsgSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 542 VTEAKPEAAAEEKVQEGDAKPS--EQDQPKEPATEQPSEQAKTEEQVTEESAKPASQEVPEQPVEQAStQEEETEESGKP 619
Cdd:PHA03169 149 PAPPESHNPSPNQQPSSFLQPSheDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQS-PTPQQAPSPNT 227
|
170
....*....|.
gi 919047147 620 AENVTAQSEAA 630
Cdd:PHA03169 228 QQAVEHEDEPT 238
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
417-603 |
4.52e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 45.03 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 417 PKPEEKQDEGTEKKTEDVKNPEVKVTEETEKKENESSEETGAEGGKGEGEEVVTKEGEQ-NIEESSKGETAEESAETKEH 495
Cdd:PRK10811 848 VRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPeEVVVVETTHPEVIAAPVTEQ 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 496 PAAEKEEDKKELDETVQETADVKEGEAVTEEKGTVETTEEPPSDQPVteakpeaaaeekVQEGDAKPSEQDQPKEPATEQ 575
Cdd:PRK10811 928 PQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPE------------VVAQPAAPVVAEVAAEVETVT 995
|
170 180 190
....*....|....*....|....*....|....*....
gi 919047147 576 PSEQAKTEEQVTEESAK-----------PASQEVPEQPV 603
Cdd:PRK10811 996 AVEPEVAPAQVPEATVEhnhatapmtraPAPEYVPEAPR 1034
|
|
| DD_DPY30_SDC1 |
cd22965 |
dimerization/docking (D/D) domain found in the DPY30/SDC1 family; This family includes DPY30 ... |
112-165 |
6.40e-04 |
|
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: 38.56 E-value: 6.40e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 919047147 112 TRVYLVDKVLPTMILGMEKLLLEvdkrglaeKEEqdpnfNPINYLAQYLMRNNP 165
Cdd:cd22965 1 TRQYLDKTVVPVLLEGLKELAKE--------RPE-----DPLEFLAEYLLKNSP 41
|
|
| Dpy-30 |
pfam05186 |
Dpy-30 motif; This motif is found in a wide variety of domain contexts. It is found in the ... |
111-165 |
7.01e-04 |
|
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: 38.75 E-value: 7.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 919047147 111 ETRVYLVDKVLPTmilgmeklLLEvdkrGLAEKEEQDPNfNPINYLAQYLMRNNP 165
Cdd:pfam05186 1 PARQYLNKTVAPI--------LLQ----GLTELAKERPE-DPIEYLADYLLKNNP 42
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
470-700 |
7.45e-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: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 470 TKEGEQNIEESSKGETAEESAET-KEHPAAEKEEDKKELDETVQETADVKEGEAVTEEKGTVETTEEPPSDQPVTEAKPE 548
Cdd:COG5271 660 ASADESEEEAEDESETSSEDAEEdADAAAAEASDDEEETEEADEDAETASEEADAEEADTEADGTAEEAEEAAEEAESAD 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 549 AAAEEKVQEGDAKPSEQDQPKEPATEQPSEQAKTEEQVTEESAKPASQEVPEQPVEQASTQEEETEESGKPAENVTAQSE 628
Cdd:COG5271 740 EEAASLPDEADAEEEAEEAEEAEEDDADGLEEALEEEKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEADE 819
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919047147 629 AAPVSDIPTVVTDDTA-AVASETTAGSAPEPTSAPETSPPQAVVSDKEKSSANVEEKEKDEAETEGQDAFEDD 700
Cdd:COG5271 820 EEDLDGEDEETADEALeDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAG 892
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
200-590 |
1.52e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 200 AKIKAEAKRKREE-REFAEQQKKK-EKARREDALKNQFSEWNLSDGKVELSLLQSALRSflevvdNLPEELKKAGQfshp 277
Cdd:PTZ00121 1475 AKKKAEEAKKADEaKKKAEEAKKKaDEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA------KKADEAKKAEE---- 1544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 278 LEPTDETGKTMSLKEfsAYISKYVEGMPSEIFDQFMLhLQRCATAHRLAAEREQRRMALTHLFIACDTSGVGVVDRHRIL 357
Cdd:PTZ00121 1545 KKKADELKKAEELKK--AEEKKKAEEAKKAEEDKNMA-LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 358 SLFERyfdqAKESYKKYLRNPRKWPVVEVDEVESTYSDDEDladpkffnNSIEVNEEGSPKPEEKQDEGTEKKTEDVKNP 437
Cdd:PTZ00121 1622 AEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE--------NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 438 EVKVTEETEKKENESSEETGAEGGKGEGEEVVTKEGEQNIEESSKGETAEESAETKEHPAAEKEEDKKEL-----DETVQ 512
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIahlkkEEEKK 1769
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919047147 513 ETADVKEGEAVTEEKgtVETTEEPPSDQPVTEAKPEAAAEEKVQEGDAKPSEQ-DQPKEPATEQPSEQAKTEEQVTEES 590
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEE--LDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLViNDSKEMEDSAIKEVADSKNMQLEEA 1846
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
478-700 |
1.97e-03 |
|
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: 42.69 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 478 EESSKGETAEESAETKEHPAAEKEEDKKELDETVQETADVKEGEAVTEEKGTVETTEEPPSDQPVTeAKPEAAAEEKVQE 557
Cdd:COG5271 508 ELTAEETSADDGADTDAAADPEDSDEDALEDETEGEENAPGSDQDADETDEPEATAEEDEPDEAEA-ETEDATENADADE 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 558 GDAKPSEQDQPKEPATEQPSEQAKTEEQVTEESAKPASQEVPEQPVEQASTQEEETEESGKPAENVTAQSEAAPVSDIPT 637
Cdd:COG5271 587 TEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEASADESE 666
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919047147 638 VVTDDTAAVASETTAGSAPEPTSAPETSPPQAVVSDKEKSSANvEEKEKDEAETEGQDAFEDD 700
Cdd:COG5271 667 EEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETAS-EEADAEEADTEADGTAEEA 728
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
397-865 |
1.99e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 397 EDLADPKFFNNSIEVNEEGSPKPEEKQDEGTEKKTEDVKNPEVKVTEETEKKENESSEETGAEGGKGEGEEVVTKEGEQN 476
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 477 IEESSKGETAEESAETKEHPAAEKEEDKKELDETVQETADvKEGEAVTEEKGTVETTEEppsdqpvteakpeaaaEEKVQ 556
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK-KKADAAKKKAEEKKKADE----------------AKKKA 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 557 EGDAKPSEQDQPKEPATEQPSEQAKTEEQV--TEESAKPASQEVPEQPVEQASTQEEETEESGKPAENVTAQSEAAPVSD 634
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKkkADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 635 iptvvtddtAAVASETTAGSAPEPTSAPETSPPQAVVSDKEKSSANVEEKEKDEAETEGQDAFEDDVRLPSPPPTADRPP 714
Cdd:PTZ00121 1481 ---------EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 715 PTRQSVTFAEGTRFDEERKALETRGTGSMSQAsafdetslnvsqfvnlietflgdEPGMEAFNSLVRYVRDGYMETEEEK 794
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKA-----------------------EEAKKAEEARIEEVMKLYEEEKKMK 1608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 795 RERLLKAHREHVTA---------KRKTRVDGLFEKWDNDGSGYLDMDEIETILSKYKDGMEKETVRRVKSKLRKDETDNR 865
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAeelkkaeeeKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
|
| PRK08691 |
PRK08691 |
DNA polymerase III subunits gamma and tau; Validated |
495-705 |
4.09e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 41.62 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 495 HPAAEKEEDKKeldeTVQETADVKEGEAVTEEKgtvETTEEPPSDQPvteakpeaaAEEKVQEGDAKPSEQDQPKEPATE 574
Cdd:PRK08691 359 APLAAASCDAN----AVIENTELQSPSAQTAEK---ETAAKKPQPRP---------EAETAQTPVQTASAAAMPSEGKTA 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 575 QPSEQaKTEEQVTEESAKPASQEVPEQPVEQASTQEEETEESGKPAENVTAQSEAA------PVSDIPT----VVTDDTA 644
Cdd:PRK08691 423 GPVSN-QENNDVPPWEDAPDEAQTAAGTAQTSAKSIQTASEAETPPENQVSKNKAAdnetdaPLSEVPSenpiQATPNDE 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919047147 645 AVASETTAGSAPEPtSAPETSPPQavvsDKEKSSANVEEKEKD---EAETEGQDAFEDDVRLPS 705
Cdd:PRK08691 502 AVETETFAHEAPAE-PFYGYGFPD----NDCPPEDGAEIPPPDwehAAPADTAGGGADEEAEAG 560
|
|
| DD_AK7 |
cd22967 |
dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins; Adenylate ... |
113-164 |
4.70e-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: 36.31 E-value: 4.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 919047147 113 RVYLVDKVLPTMIlgmeKLLLEVDKRglaekeeqDPNfNPINYLAQYLMRNN 164
Cdd:cd22967 3 RNYLMKYVMPTLT----EGLVEVCKV--------RPE-DPVDFLAEYLFKHN 41
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
818-876 |
4.78e-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: 36.76 E-value: 4.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 919047147 818 FEKWDNDGSGYLDMDEIETILSKYKDGMEKETVRRVKSKLRKDEtDNRLSKREFREFVT 876
Cdd:cd00051 6 FRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDG-DGKIDFEEFLELMA 63
|
|
| PRK10927 |
PRK10927 |
cell division protein FtsN; |
504-698 |
5.28e-03 |
|
cell division protein FtsN;
Pssm-ID: 236797 [Multi-domain] Cd Length: 319 Bit Score: 40.82 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 504 KKELDETVQETADVKEGEAVTEEKgTVETTEEPPSDQPVTEAKPEAAAEEKVQEGDAKPSEQ---------DQPKEPA-- 572
Cdd:PRK10927 58 KKEESETLQSQKVTGNGLPPKPEE-RWRYIKELESRQPGVRAPTEPSAGGEVKTPEQLTPEQrqlleqmqaDMRQQPTql 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 573 TEQP-SEQAKTEEQVTEESAKPASQEVPEQPVEQASTQEEETEESgkpaENVTAQSEAAPVSDIPTVVT------DDTAA 645
Cdd:PRK10927 137 VEVPwNEQTPEQRQQTLQRQRQAQQLAEQQRLAQQSRTTEQSWQQ----QTRTSQAAPVQAQPRQSKPAstqqpyQDLLQ 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 646 VASETTAGSAPePTSAPETSPPQAVVSDKEKSSANV------EEKEKDEAET-EGQDAFE 698
Cdd:PRK10927 213 TPAHTTAQSKP-QQAAPVTRAADAPKPTAEKKDERRwmvqcgSFRGAEQAETvRAQLAFE 271
|
|
| PRK11907 |
PRK11907 |
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase; |
624-705 |
5.93e-03 |
|
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
Pssm-ID: 237019 [Multi-domain] Cd Length: 814 Bit Score: 40.99 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 624 TAQSEAAPVSDIPTVVTDDTAAVASETTAGSAPEPTSAPETSPPQAVVSDkeksSANVEEKEKDEAETEGQDAFED---D 700
Cdd:PRK11907 40 TEAEQTTPVESDATEEADNTETPVAATTAAEAPSSSETAETSDPTSEATD----TTTSEARTVTPAATETSKPVEGqtvD 115
|
....*
gi 919047147 701 VRLPS 705
Cdd:PRK11907 116 VRILS 120
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
483-690 |
6.83e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 41.18 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 483 GETAEESAETKEHPAAEKEEDKKELDETVQ----ETADVKEGEAVTEEKGTVETTEEPPSDQPVTEAKPEAAAEEKVQEG 558
Cdd:PRK10811 582 GGEETKPQEQPAPKAEAKPERQQDRRKPRQnnrrDRNERRDTRDNRTRREGRENREENRRNRRQAQQQTAETRESQQAEV 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 559 DAKPSEQDQpkepateQPSEQAKTEEQVTEESAKPASQEVPEQPVEQASTQEEETEESGKPAENVTAQSEAAPVSDIPTV 638
Cdd:PRK10811 662 TEKARTQDE-------QQQAPRRERQRRRNDEKRQAQQEAKALNVEEQSVQETEQEERVQQVQPRRKQRQLNQKVRIEQS 734
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 919047147 639 VTDDTAAVASETTAGSAPEPTSAPETSPPQAVVSDKEKSSANVEEKEKDEAE 690
Cdd:PRK10811 735 VAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEENNAE 786
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
366-736 |
6.85e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 366 QAKESYKKYLRNPRKWPVVEVDEVESTYSDDEDLADPKFFNNSIEVNEEGSPKPEEKQDEGTEKKTEDVKNPEVKVTEET 445
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 446 EKKENESSEETGAEGGKGEGEEVVTKEGEQNIEESSKGETAEESAET--KEHPAAEKEEDKK---ELDETVQETADVKEG 520
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEakKADEAKKKAEEAKkaeEAKKKAEEAKKADEA 1475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 521 EAVTEEKGTVETTEEPPSDQPVTEAKPEAAAEEKVQEGDAKPSEQ----DQPKEPATEQPSEQAKTEEQVTEESAKPASQ 596
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEakkaDEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 597 EVPE----QPVEQASTQEEETEESGKPAEnVTAQSEAAPVSDIPTVVTDDTAAVASEttAGSAPEPTSAPETSPPQAVVS 672
Cdd:PTZ00121 1556 ELKKaeekKKAEEAKKAEEDKNMALRKAE-EAKKAEEARIEEVMKLYEEEKKMKAEE--AKKAEEAKIKAEELKKAEEEK 1632
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919047147 673 DKEKSSANVEEKEKDEAETEGQDAFEDDVRLPSPPPTADRPPPTRQSVTFAEgtrfDEERKALE 736
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE----EDEKKAAE 1692
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
1005-1086 |
6.93e-03 |
|
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: 38.52 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 1005 VETGKPIHVPRVNNHgsiYFWNTDRDAEDRD-GSLIVVAVKDQRkRVFGLLAIDTLRDPHTkaiFITHEIQFFQGVGKAF 1083
Cdd:smart00065 63 AETGRPLNIPDVEAD---PLFAEDLLGRYQGvRSFLAVPLVADG-ELVGVLALHNKKSPRP---FTEEDEELLQALANQL 135
|
...
gi 919047147 1084 SIA 1086
Cdd:smart00065 136 AIA 138
|
|
| GAF |
pfam01590 |
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ... |
1005-1086 |
8.28e-03 |
|
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 460259 [Multi-domain] Cd Length: 133 Bit Score: 38.23 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 1005 VETGKPIHVPRVNNHGSiyfWNTDRDAEDRDG--SLIVVAVKDQRkRVFGLLAIDTLRDPHTKaifitHEIQFFQGVGKA 1082
Cdd:pfam01590 58 LRTGRPLVVPDAAGDPR---FLDPLLLLRNFGirSLLAVPIIDDG-ELLGVLVLHHPRPPFTE-----EELELLEVLADQ 128
|
....
gi 919047147 1083 FSIA 1086
Cdd:pfam01590 129 VAIA 132
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
817-876 |
8.53e-03 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 36.46 E-value: 8.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 919047147 817 LFEKWDNDGSGYLDMDEIETILSKYKDG--MEKETVRRVKSKLRKDEtDNRLSKREFREFVT 876
Cdd:pfam13499 7 AFKLLDSDGDGYLDVEELKKLLRKLEEGepLSDEEVEELFKEFDLDK-DGRISFEEFLELYS 67
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
474-699 |
9.50e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 39.95 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 474 EQNIEESSKGETAEESAETKEHPAAEKEEDKKELDETVQETADVKEGEAVTEEKGTVETTEEPPSDQPVTeakpeaaaee 553
Cdd:PHA03169 64 QGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPAS---------- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 554 kvQEGDAKPSEQDQPKEPAteQPSEQAKTEEQVTEESAKPASQEVPEQPVEqastqeeeteesgkpaenvtAQSEAAPvs 633
Cdd:PHA03169 134 --HSPPPSPPSHPGPHEPA--PPESHNPSPNQQPSSFLQPSHEDSPEEPEP--------------------PTSEPEP-- 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919047147 634 diptvvtdDTAAVASETTAGSAPEPTSAPETSPPQAVVSDKEKSSANVEEKEKDEAETEGQDAFED 699
Cdd:PHA03169 188 --------DSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGP 245
|
|
| ftsN |
TIGR02223 |
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ... |
562-734 |
9.57e-03 |
|
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: 39.67 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 562 PSEQDQPKEPATEQPSEQAKTEEQVTEESAKPASQ-----EVPEQPVEQASTQEEETEESGKPAENVTAQSEAAPVSDIP 636
Cdd:TIGR02223 48 LTESKQANEPETLQPKNQTENGETAADLPPKPEERwsyieELEAREVLINDPEEPSNGGGVEESAQLTAEQRQLLEQMQA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047147 637 TVVTDDTAAVASETTAGSAPEPTSAPETSPPQAvVSDKEKSSANVEEKEKDEAETEGQDAFEDDVRLPSPPPTADRPPPT 716
Cdd:TIGR02223 128 DMRAAEKVLATAPSEQTVAVEARKQTAEKKPQK-ARTAEAQKTPVETEKIASKVKEAKQKQKALPKQTAETQSNSKPIET 206
|
170
....*....|....*...
gi 919047147 717 RQSVTFAEGTRFDEERKA 734
Cdd:TIGR02223 207 APKADKADKTKPKPKEKA 224
|
|
| |
