|
Name |
Accession |
Description |
Interval |
E-value |
| DCX1_RP1L1 |
cd17146 |
Doublecortin-like domain 1 found in retinitis pigmentosa 1-like 1 (RP1L1) protein; RP1L1 is a ... |
34-112 |
6.23e-49 |
|
Doublecortin-like domain 1 found in retinitis pigmentosa 1-like 1 (RP1L1) protein; RP1L1 is a member of the doublecortin (DCX) family. Its DCX domains occur in double tandem repeats. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX-domain of RP1L1 localizes to the photoreceptor and is genetically associated with retinitis pigmentosa.
Pssm-ID: 340666 Cd Length: 79 Bit Score: 168.85 E-value: 6.23e-49
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1375418697 34 KKITFLKRGDPRFAGVRLAVHQRAFKTFSALMDELSQRVPLSFGVRSVTTPRGLHSLSALEQLEDGGCYLCSDKKPPKT 112
Cdd:cd17146 1 KKITFYKSGDPQFGGVKMAVNKRTFKSFSALLDDLSQRVPLPFGVRTITTPRGTHSISRLEQLEDGGCYLCSDKKYVKP 79
|
|
| DCX2_RP1L1 |
cd17148 |
Dublecortin-like domain 2 found in retinitis pigmentosa 1-like 1 (RP1L1) protein; RP1L1 is a ... |
152-227 |
2.20e-39 |
|
Dublecortin-like domain 2 found in retinitis pigmentosa 1-like 1 (RP1L1) protein; RP1L1 is a member of doublecortin (DCX) family. Its protein domains occur in tandem repeats. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX-domain of RP1L1 localizes to the photoreceptor and is genetically associated with retinitis pigmentosa.
Pssm-ID: 340668 Cd Length: 76 Bit Score: 141.45 E-value: 2.20e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1375418697 152 RRILLIKNMDPRLQQTVVLSHRNTRNLAAFLGKASDLLRFPVKQLYTTSGKKVDSLQALLHSPSVLVCAGHEAFRT 227
Cdd:cd17148 1 KKITLVKNGDPDVRRSIILNRRNARNLRTFLDEISDLLQFPVKKLYTLEGRKIDSIQALLHCPSVLVCVGREPFKP 76
|
|
| DCX |
smart00537 |
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ... |
33-113 |
9.27e-16 |
|
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the Doublecortin gene product. Proposed to bind tubulin. Doublecortin (DCX) is mutated in human X-linked neuronal migration defects.
Pssm-ID: 214711 Cd Length: 89 Bit Score: 74.60 E-value: 9.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 33 AKKITFLKRGDPRFAGVRLAVHQRAFKTFSALMDELSQ--RVPLSFGVRSVTTPRGLHSLSaLEQLEDGGCYLCSDKKPP 110
Cdd:smart00537 5 PKRIRFYRNGDRFFKGVRLVVNRKRFKSFEALLQDLTEvvKLDLPHGVRKLYTLDGKKVTS-LDELEDGGSYVASGTEAF 83
|
...
gi 1375418697 111 KTP 113
Cdd:smart00537 84 KKV 86
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
2020-2260 |
1.46e-13 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 76.96 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2020 SDGVEAQPKSEGEEAQEVEGETQKTEGDAQPESDGveapeaEEEAQEAEGEVQEAEGEAHPESEDVDAQEAEGEAQPESE 2099
Cdd:TIGR00927 631 SKGDVAEAEHTGERTGEEGERPTEAEGENGEESGG------EAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEA 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2100 GVEAPEAEGEAQKAEG--IEAPETEGEAQPESEG-IEAPEAEGEAQPESEG-VEAQDAEGEAQPESEGieaqeaeEEAQP 2175
Cdd:TIGR00927 705 DHKGETEAEEVEHEGEteAEGTEDEGEIETGEEGeEVEDEGEGEAEGKHEVeTEGDRKETEHEGETEA-------EGKED 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2176 ELEGVEAPEAEGEAQPESEGIEAPEAEGEAqpELEGVEAPEAEEEAQPEPEGVETPEAEGEAQPESEGETQGEKKGSPQV 2255
Cdd:TIGR00927 778 EDEGEIQAGEDGEMKGDEGAEGKVEHEGET--EAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGG 855
|
....*
gi 1375418697 2256 SLGDG 2260
Cdd:TIGR00927 856 GGSDG 860
|
|
| DCX |
pfam03607 |
Doublecortin; |
52-109 |
3.23e-13 |
|
Doublecortin;
Pssm-ID: 460986 Cd Length: 60 Bit Score: 66.32 E-value: 3.23e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 52 AVHQRAFKTFSALMDELSQRVP-LSFG-VRSVTTPRGlHSLSALEQLEDGGCYLCSDKKP 109
Cdd:pfam03607 1 VVNKRRFRSFDALLDELTEKVVkLPFGaVRKLYTLDG-KRVTSLDELEDGGVYVAAGREK 59
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1824-2121 |
8.39e-11 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 67.71 E-value: 8.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1824 QDPGQSDGAEGIEAPEAEGEAQPESEGVEAPEAEGDAQ-EAEGEAQPESEDVEAPEAEGEAQPESEDVETPEAEWEVQPE 1902
Cdd:TIGR00927 639 EHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKgENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHE 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1903 segaeapeaekeaqpETESVEALETEGEDEPESEGAEAQEAEEAAQEAEGQTQPESEVIESQEAEEEaqpesedvealEV 1982
Cdd:TIGR00927 719 ---------------GETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGET-----------EA 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1983 EVETQEAEGEAQPEsEDVEAPEAEGEMQEAEEEAQPESDGVEAQPKSEGEEAQEVEGETQKTEGDAQPESDGveapeaee 2062
Cdd:TIGR00927 773 EGKEDEDEGEIQAG-EDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQG-------- 843
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1375418697 2063 EAQEAEGEVQEAEGEAHPESEDVDAQEAEGEAQPESEGvEAPEAEGEAQKAEGIEAPET 2121
Cdd:TIGR00927 844 EAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEE-EEEEEEEENEEPLSLEWPET 901
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1697-1935 |
1.79e-10 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 66.94 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1697 RGEHTDGEAAEVAPGKTHTDPTSTRTVQGAEGGLGPGLSQGPGVDEGEdGEGSQRLNRDKDPKLGEAEGDAMAQER---- 1772
Cdd:TIGR00927 641 TGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAE-RKGEQEGEGEIEAKEADHKGETEAEEVeheg 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1773 ----EGKTHNSETSAGSELGEAEQEGEGISERGETGG-QGSGHEDNLQGEAAAGG--DQDPGQSDGAEGIEAPEAEGEAQ 1845
Cdd:TIGR00927 720 eteaEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVEtEGDRKETEHEGETEAEGkeDEDEGEIQAGEDGEMKGDEGAEG 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1846 PESEGVEAPEAEGDAQEAEGEAQPESEDVEAPEAEGEAQPESEDvETPEAEWEVQPESEGAEAPEAEKEAQPETESVEAL 1925
Cdd:TIGR00927 800 KVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQG-EAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEE 878
|
250
....*....|
gi 1375418697 1926 ETEGEDEPES 1935
Cdd:TIGR00927 879 EEEEEEEEEE 888
|
|
| DCX |
pfam03607 |
Doublecortin; |
169-225 |
1.24e-08 |
|
Doublecortin;
Pssm-ID: 460986 Cd Length: 60 Bit Score: 53.22 E-value: 1.24e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1375418697 169 VLSHRNTRNLAAFLGKASDL---LRFP-VKQLYTTSGKKVDSLQaLLHSPSVLVCAGHEAF 225
Cdd:pfam03607 1 VVNKRRFRSFDALLDELTEKvvkLPFGaVRKLYTLDGKRVTSLD-ELEDGGVYVAAGREKF 60
|
|
| DCX |
smart00537 |
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ... |
147-228 |
1.07e-07 |
|
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the Doublecortin gene product. Proposed to bind tubulin. Doublecortin (DCX) is mutated in human X-linked neuronal migration defects.
Pssm-ID: 214711 Cd Length: 89 Bit Score: 51.49 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 147 SLKTPRRILLIKNMDP-RLQQTVVLSHRNTRNLAAFLGKASDLLR----FPVKQLYTTSGKKVDSLQALLHSpSVLVCAG 221
Cdd:smart00537 1 SLVKPKRIRFYRNGDRfFKGVRLVVNRKRFKSFEALLQDLTEVVKldlpHGVRKLYTLDGKKVTSLDELEDG-GSYVASG 79
|
....*..
gi 1375418697 222 HEAFRTP 228
Cdd:smart00537 80 TEAFKKV 86
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
1741-1934 |
5.16e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 51.51 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1741 DEGEDGEGSQRLNRDKDPKLGEAEGDAmaqEREGKTHNSETSAGSELGEAEQEGEGiserGETGGQGSGHEDNLQGEAAA 1820
Cdd:PHA03169 50 APTTSGPQVRAVAEQGHRQTESDTETA---EESRHGEKEERGQGGPSGSGSESVGS----PTPSPSGSAEELASGLSPEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1821 GGDQDPGQSDGAEGIEAPEAEGEAQPESEGVEAPEAEGDAQEAEGEAQPESEDVEAPEAEGEAQPESEDVETPEAEWEVQ 1900
Cdd:PHA03169 123 TSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSP 202
|
170 180 190
....*....|....*....|....*....|....*.
gi 1375418697 1901 PESEGAEAPEAEKEAQPE--TESVEALETEGEDEPE 1934
Cdd:PHA03169 203 PPQSPPDEPGEPQSPTPQqaPSPNTQQAVEHEDEPT 238
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
2027-2208 |
1.06e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 50.35 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2027 PKSEGEEAQEVEGETQKTEGDAQPESDGVEAPEAEEEAQEAEGEVQEAEGEAHPESEDVDAQEAEGEAQPESEGVEAPEA 2106
Cdd:PHA03169 51 PTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPES 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2107 EGEAQKAEGIEAPETEGEAQPESE----GIEAPEAEGEAQPESEGVEAQDAEGEAQPESEGIEAQEAEEEAQPELEGVE- 2181
Cdd:PHA03169 131 PASHSPPPSPPSHPGPHEPAPPEShnpsPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDe 210
|
170 180
....*....|....*....|....*...
gi 1375418697 2182 -APEAEGEAQPESEGIEAPEAEGEAQPE 2208
Cdd:PHA03169 211 pGEPQSPTPQQAPSPNTQQAVEHEDEPT 238
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
1694-1896 |
1.26e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 50.35 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1694 QRKRGEHTDGEAAEVAPGKTHTDPTSTRTVQGAEGGLGPGLSQGPGVDEGEDGEGSQRLNRDKDPKLGEAEGDAMAQERE 1773
Cdd:PHA03169 56 PQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1774 GKTHNSETSAGSELGEAEQEGEGISERGETGGQGSGHEDNLQGEAAAGGDQDpgqsdgaegiEAPEAEGEAQPESEGVEA 1853
Cdd:PHA03169 136 PPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEP----------DSPGPPQSETPTSSPPPQ 205
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1375418697 1854 PEAEGDAQEAEGEAQPESEDVEAPEAEGEAQPESEDVETPEAE 1896
Cdd:PHA03169 206 SPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFP 248
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
1713-2355 |
1.64e-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: 47.32 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1713 THTDPTSTRTVQGAEGGLGPGLSQGPGVDEGEDGEGSQRLNRDKDPKLGEAEGDAMAQEREGKTHNSETSAGSELGEAEQ 1792
Cdd:COG5271 370 GEAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1793 EGEGISERGETGgQGSGHEDNLQGEAAAGGDQDPGQSDGAEGIEAPEAEGEAQPESEGVEAPEAEGDA---QEAEGEAQP 1869
Cdd:COG5271 450 DSLADEEEEAEA-ELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSAddgADTDAAADP 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1870 ESEDVEAPEAEGEAQPESEDVETPEAEWEVQPESEGAEAP---EAEKEAQPETESVEAlETEGEDEPESEGAEAQEAEEA 1946
Cdd:COG5271 529 EDSDEDALEDETEGEENAPGSDQDADETDEPEATAEEDEPdeaEAETEDATENADADE-TEESADESEEAEASEDEAAEE 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1947 AQEAEGQTQPESEVIESQEAEEEAQPESEDVEALEVEVETQEAEGEAQPE---SEDVEAPEAEGEMQEAEEEAQPESDGV 2023
Cdd:COG5271 608 EEADDDEADADADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEaeaSADESEEEAEDESETSSEDAEEDADAA 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2024 EAQPKSEGEEAQEVEGETQKTEGDAQPESDGVEAPEAEEEAQEAEGEVQEAEGEAHPESEDVDAQEAEGEAQPESEGvEA 2103
Cdd:COG5271 688 AAEASDDEEETEEADEDAETASEEADAEEADTEADGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEED-DA 766
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2104 PEAEgeaqkaEGIEAPETEGEAQPESEGIEAPEAEGEAQPESEGVEAQDAEGEAQPESEGIEAQEAEEEAQPELEGVEAP 2183
Cdd:COG5271 767 DGLE------EALEEEKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEA 840
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2184 E--AEGEAQPESEGIEAPEAEGEAQPELEGVEAPEAEEEAQPEPEGVETPEAEGEAQPESEGETQGEKKGSPQVSLGDGQ 2261
Cdd:COG5271 841 GiaEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEADSSGESSAAAEDDDAAEDADSDDGAN 920
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2262 SEEASESSSPVPEDRPTPPPSPGGDTPHQRPGSQTGPSSSRASSWGNCWQKDSENDHVLGDTRSPDAKSTGTPHAERKAT 2341
Cdd:COG5271 921 DEDDDDDAEEERKDAEEDELGAAEDDLDALALDEAGDEESDDAAADDAGDDSLADDDEALADAADDAEADDSELDASEST 1000
|
650
....*....|....
gi 1375418697 2342 RMYPESSTSEQEEA 2355
Cdd:COG5271 1001 GEAEGDEDDDELED 1014
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
1688-2202 |
2.41e-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: 46.55 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1688 DLQQILQRKRGEHTDGEAAEVAPGKTHTDPTSTRTVQGAEGGLGPGLSQ--GPGVDEGEDGEGSQRLNRDKDPKLGEAEG 1765
Cdd:COG5271 249 LADDDDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQaaDPESDDDADDSTLAALEGAAEDTEIATAD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1766 DAMAQEREGKTHNSETSAGSELGEAEQEGEGISERGETGGQGSGHEDNLQGEAAAGGDQDPGQSDGAEGIEAPEAEGEAQ 1845
Cdd:COG5271 329 ELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1846 PESEGVEAPEaEGDAQEAEGEAQPESEDVEAPEAEGEAQPESEDVETPEAEWEVQPESEGAEAPEAEKEAQPETESVEAL 1925
Cdd:COG5271 409 PTSDTDEEEE-EADEDASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDA 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1926 ETEGEDEPESEGAEAQEAEEAAQEAEGQTQPESEViesqeaeeeaqPESEDVEALEVEVETQEAEGEAQPESEDVEAPEa 2005
Cdd:COG5271 488 SDDGDEEEAEEDAEAEADSDELTAEETSADDGADT-----------DAAADPEDSDEDALEDETEGEENAPGSDQDADE- 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2006 egemqeaeeeaqpesdgvEAQPKSEGEEAQEVEGETQKTEGDAQPESDGVEAPEAEEEAQEAEGEVQEAEGEAHPESEDV 2085
Cdd:COG5271 556 ------------------TDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2086 DAQEAEGEAQPESEGVEAPEAEGEAQKAEGIEA---PETEGEAQPESEGIEAPEaEGEAQPESEGVEAQDAEGEAQPESE 2162
Cdd:COG5271 618 DADGAADEEETEEEAAEDEAAEPETDASEAADEdadAETEAEASADESEEEAED-ESETSSEDAEEDADAAAAEASDDEE 696
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1375418697 2163 GIEAQEAEEEAQPELEGVEAPEAEGEAQPESEGIEAPEAE 2202
Cdd:COG5271 697 ETEEADEDAETASEEADAEEADTEADGTAEEAEEAAEEAE 736
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
561-904 |
9.08e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.78 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 561 AETSQQEASEGGDPASPALSLS----SLRSDDLQAETQGQGTEQATGAAVTREPLVLGLSCSWDSEGASSTPSTCTSSQQ 636
Cdd:PHA03307 18 GEFFPRPPATPGDAADDLLSGSqgqlVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 637 GQRRHRSRASAMSSPSSPGLGRVAPRGHPRHSHyrKDTHSPLDSSVTKQVPRPPERRRAcqDGSVPRYSGSSSSTRTQAS 716
Cdd:PHA03307 98 ASPAREGSPTPPGPSSPDPPPPTPPPASPPPSP--APDLSEMLRPVGSPGPPPAASPPA--AGASPAAVASDAASSRQAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 717 GNLRPPSSGSLPSQDLLGTSSATVTPAVHSDFVSGVSPHNAPSAGWAGDAGSRtcSPAPIPPHTSDSCSKSGAASLGEEA 796
Cdd:PHA03307 174 LPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGR--SAADDAGASSSDSSSSESSGCGWGP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 797 RD-TPQPSSPLVLQVGRPEQGAVGPHRShCCSQPGTQPAQEAQRGPSPEASWLCGRYCPTPPRGRPCPQRRSSSCGSTGS 875
Cdd:PHA03307 252 ENeCPLPRPAPITLPTRIWEASGWNGPS-SRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTS 330
|
330 340 350
....*....|....*....|....*....|
gi 1375418697 876 SHQSTARGPGGSP-QEGTRQPGPTPSPGPN 904
Cdd:PHA03307 331 SSSESSRGAAVSPgPSPSRSPSPSRPPPPA 360
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
2073-2160 |
1.85e-03 |
|
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 443611 [Multi-domain] Cd Length: 608 Bit Score: 43.63 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2073 EAEGEAHPESEDVDAQEAEGEAQPESEGVEAPEAEGEAQkaegieapETEGEAQPESEGIEAPEAEGEAQPESEGVEAQD 2152
Cdd:COG4547 208 AEELGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEG--------AEAEDAEASGDDAEEGESEAAEAESDEMAEEAE 279
|
....*...
gi 1375418697 2153 AEGEAQPE 2160
Cdd:COG4547 280 GEDSEEPG 287
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DCX1_RP1L1 |
cd17146 |
Doublecortin-like domain 1 found in retinitis pigmentosa 1-like 1 (RP1L1) protein; RP1L1 is a ... |
34-112 |
6.23e-49 |
|
Doublecortin-like domain 1 found in retinitis pigmentosa 1-like 1 (RP1L1) protein; RP1L1 is a member of the doublecortin (DCX) family. Its DCX domains occur in double tandem repeats. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX-domain of RP1L1 localizes to the photoreceptor and is genetically associated with retinitis pigmentosa.
Pssm-ID: 340666 Cd Length: 79 Bit Score: 168.85 E-value: 6.23e-49
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1375418697 34 KKITFLKRGDPRFAGVRLAVHQRAFKTFSALMDELSQRVPLSFGVRSVTTPRGLHSLSALEQLEDGGCYLCSDKKPPKT 112
Cdd:cd17146 1 KKITFYKSGDPQFGGVKMAVNKRTFKSFSALLDDLSQRVPLPFGVRTITTPRGTHSISRLEQLEDGGCYLCSDKKYVKP 79
|
|
| DCX2_RP1L1 |
cd17148 |
Dublecortin-like domain 2 found in retinitis pigmentosa 1-like 1 (RP1L1) protein; RP1L1 is a ... |
152-227 |
2.20e-39 |
|
Dublecortin-like domain 2 found in retinitis pigmentosa 1-like 1 (RP1L1) protein; RP1L1 is a member of doublecortin (DCX) family. Its protein domains occur in tandem repeats. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX-domain of RP1L1 localizes to the photoreceptor and is genetically associated with retinitis pigmentosa.
Pssm-ID: 340668 Cd Length: 76 Bit Score: 141.45 E-value: 2.20e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1375418697 152 RRILLIKNMDPRLQQTVVLSHRNTRNLAAFLGKASDLLRFPVKQLYTTSGKKVDSLQALLHSPSVLVCAGHEAFRT 227
Cdd:cd17148 1 KKITLVKNGDPDVRRSIILNRRNARNLRTFLDEISDLLQFPVKKLYTLEGRKIDSIQALLHCPSVLVCVGREPFKP 76
|
|
| DCX1_RP_like |
cd16110 |
Doublecortin-like domain 1 found in retinitis pigmentosa (RP)-like protein; RP-like protein ... |
34-108 |
4.00e-39 |
|
Doublecortin-like domain 1 found in retinitis pigmentosa (RP)-like protein; RP-like protein family is part of doublecortin (DCX) family. It has double tandem DCX repeats that are associated with retinitis pigmentosa. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. RP-like proteins are colocalized to the photoreceptor and share a function in outer segment disc morphogenesis.
Pssm-ID: 340527 Cd Length: 75 Bit Score: 140.51 E-value: 4.00e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1375418697 34 KKITFLKRGDPRFAGVRLAVHQRAFKTFSALMDELSQRVPLSFGVRSVTTPRGLHSLSALEQLEDGGCYLCSDKK 108
Cdd:cd16110 1 KNVTFYKDGDVHFSGVRVAINPRRYRTFDALLDELSRKVPLPFGVRSITTPRGRHSITSLEQLEDGGKYVCSSKR 75
|
|
| DCX1_RP1 |
cd17145 |
Doublecortin-like domain 1 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also ... |
34-111 |
1.68e-30 |
|
Doublecortin-like domain 1 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also termed oxygen-regulated protein 1, is a member of the doublecortin (DCX) family. Its DCX domains occur in double tandem repeats. RP1 is associated with retinitis pigmentosa, which is a type of inherited blindness. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The RP1 protein is expressed in photoreceptors and is required for correct stacking of outer segment discs. It interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.
Pssm-ID: 340665 Cd Length: 79 Bit Score: 116.07 E-value: 1.68e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375418697 34 KKITFLKRGDPRFAGVRLAVHQRAFKTFSALMDELSQRVPLSFGVRSVTTPRGLHSLSALEQLEDGGCYLCSDKKPPK 111
Cdd:cd17145 1 KRVCFYKSGDPQFGGLRMVVNSRSFKTFDALLDNLSKKVPLPFGVRNITTPRGVHHITSLEDLEDGKSYICSHQKKVK 78
|
|
| DCX2_RP_like |
cd17070 |
Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein ... |
152-220 |
2.65e-25 |
|
Dublecortin-like domain 2 found in retinitis pigmentosa (RP)-like protein; RP-like protein family is part of doublecortin (DCX) superfamily with double tandem DCX repeats that are associated with retinitis pigmentosa. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. RP-like proteins are colocalized to the photoreceptor and share a function in outer segment disc morphogenesis.
Pssm-ID: 340590 Cd Length: 69 Bit Score: 100.78 E-value: 2.65e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1375418697 152 RRILLIKNMDPRLQQTVVLSHRNTRNLAAFLGKASDLLRFPVKQLYTTSGKKVDSLQALLHSPSVLVCA 220
Cdd:cd17070 1 KVITVISNGDPHSRHTILLNRRTTQSFEQVLQDLSELLKGPVRKLYTTDGKKVESLSALFHGPDEYVAA 69
|
|
| DCX |
cd01617 |
Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin ... |
34-105 |
2.13e-19 |
|
Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin (DCX) is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX gene family consists of eleven paralogs in human and mouse, and its DCX protein domains can occur in double tandem or as single DCX repeats. Proteins with DCX tandem domains in general have roles in microtubule (MT) regulation and signal transduction such as X-linked doublecortin (DCX), retinitis pigmentosa-1 (RP1) and doublecortin-like kinase (DCLK). Single DCX repeat proteins are normally localized to actin-rich subcellular structures, or the nucleus such as DCDC2. DCX is not only a unique MAP in terms of structure, it also interacts with multiple additional proteins. Mutations in human DCX genes are associated with abnormal neuronal migration, epilepsy, and mental retardation.
Pssm-ID: 340456 Cd Length: 73 Bit Score: 84.20 E-value: 2.13e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1375418697 34 KKITFLKRGDPRFAGVRLAVHQRAFKTFSALMDELSQRVPL-SFGVRSVTTPRGLHSLSaLEQLEDGGCYLCS 105
Cdd:cd01617 1 KRITVFRNGDKNFKGVKVLVKPRRFRTFDQLLDELTEKLGLpTGGVRKLYTPSGKLVKS-LSDLEDGESYVVC 72
|
|
| DCX2_RP1 |
cd17147 |
Dublecortin-like domain 2 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also termed ... |
152-226 |
3.48e-19 |
|
Dublecortin-like domain 2 found in retinitis pigmentosa 1 (RP1)-like protein; RP1, also termed oxygen-regulated protein 1, is a member of doublecortin (DCX) superfamily that contains double tandem repeats of the DCX domains. RP1 is associated with retinitis pigmentosa, which is a type of inherited blindness. DCX is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The RP1 protein is expressed in photoreceptors that is required for correct stacking of outer segment discs. RP1 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.
Pssm-ID: 340667 Cd Length: 76 Bit Score: 83.65 E-value: 3.48e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1375418697 152 RRILLIKNMDPRLQQTVVLSHRNTRNLAAFLGKASDLLRFPVKQLYTTSGKKVDSLQALLHSPSVLVCAGHEAFR 226
Cdd:cd17147 1 RKLIVFKNGDPGFKHTLILNKKTTQSFEALLDHVSELMQFPVVKLYTTDGRRVDSLQALILSSGAVVAAGREPFK 75
|
|
| DCX |
smart00537 |
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ... |
33-113 |
9.27e-16 |
|
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the Doublecortin gene product. Proposed to bind tubulin. Doublecortin (DCX) is mutated in human X-linked neuronal migration defects.
Pssm-ID: 214711 Cd Length: 89 Bit Score: 74.60 E-value: 9.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 33 AKKITFLKRGDPRFAGVRLAVHQRAFKTFSALMDELSQ--RVPLSFGVRSVTTPRGLHSLSaLEQLEDGGCYLCSDKKPP 110
Cdd:smart00537 5 PKRIRFYRNGDRFFKGVRLVVNRKRFKSFEALLQDLTEvvKLDLPHGVRKLYTLDGKKVTS-LDELEDGGSYVASGTEAF 83
|
...
gi 1375418697 111 KTP 113
Cdd:smart00537 84 KKV 86
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
2020-2260 |
1.46e-13 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 76.96 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2020 SDGVEAQPKSEGEEAQEVEGETQKTEGDAQPESDGveapeaEEEAQEAEGEVQEAEGEAHPESEDVDAQEAEGEAQPESE 2099
Cdd:TIGR00927 631 SKGDVAEAEHTGERTGEEGERPTEAEGENGEESGG------EAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEA 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2100 GVEAPEAEGEAQKAEG--IEAPETEGEAQPESEG-IEAPEAEGEAQPESEG-VEAQDAEGEAQPESEGieaqeaeEEAQP 2175
Cdd:TIGR00927 705 DHKGETEAEEVEHEGEteAEGTEDEGEIETGEEGeEVEDEGEGEAEGKHEVeTEGDRKETEHEGETEA-------EGKED 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2176 ELEGVEAPEAEGEAQPESEGIEAPEAEGEAqpELEGVEAPEAEEEAQPEPEGVETPEAEGEAQPESEGETQGEKKGSPQV 2255
Cdd:TIGR00927 778 EDEGEIQAGEDGEMKGDEGAEGKVEHEGET--EAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGG 855
|
....*
gi 1375418697 2256 SLGDG 2260
Cdd:TIGR00927 856 GGSDG 860
|
|
| DCX1_DCDC2_like |
cd17071 |
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2) and ... |
34-102 |
2.25e-13 |
|
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2) and similar proteins; DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.
Pssm-ID: 340591 Cd Length: 80 Bit Score: 67.25 E-value: 2.25e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 34 KKITFLKRGDPRFAGVRLAVHQRAFKTFSALMDELSQRVPLSFG-VRSVTTPRGLHSLSALEQLEDGGCY 102
Cdd:cd17071 1 KIIVVYKNGDPFFPGKKFVVNERQVRTFDAFLNEVTSGIKAPFGaVRSIYTPTGGHRVKDLDSLQNGGVY 70
|
|
| DCX1 |
cd16109 |
Dublecortin-like domain 1; Members of the doublecortin (DCX) gene family are ... |
33-105 |
2.27e-13 |
|
Dublecortin-like domain 1; Members of the doublecortin (DCX) gene family are microtubule-associated proteins (MAPs). Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX gene family consists of eleven paralogs in human and mouse, and its protein domains can occur in double tandem or single repeats. The family represents the first repeat of the DCX domain which has a stable ubiquitin-like tertiary fold. Proteins with DCX double tandem domains in general have roles in microtubule (MT) regulation and signal transduction such as X-linked doublecortin (DCX), retinitis pigmentosa-1 (RP1) and doublecortin-like kinase (DCLK).
Pssm-ID: 340526 Cd Length: 85 Bit Score: 67.32 E-value: 2.27e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1375418697 33 AKKITFLKRGDPRFAGVRLAVHQRAFKTFSALMDEL----SQRVPLSFGVRSVTTPRGLHSLSALEQLEDGGCYLCS 105
Cdd:cd16109 2 AKKVRFYRNGDRFFKGIVYAVSSERFRSFEALLADLtrslSDNVNLPQGVRTIFTIDGSRKITSLDELEDGESYVCA 78
|
|
| DCX |
pfam03607 |
Doublecortin; |
52-109 |
3.23e-13 |
|
Doublecortin;
Pssm-ID: 460986 Cd Length: 60 Bit Score: 66.32 E-value: 3.23e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 52 AVHQRAFKTFSALMDELSQRVP-LSFG-VRSVTTPRGlHSLSALEQLEDGGCYLCSDKKP 109
Cdd:pfam03607 1 VVNKRRFRSFDALLDELTEKVVkLPFGaVRKLYTLDG-KRVTSLDELEDGGVYVAAGREK 59
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1988-2253 |
6.20e-13 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 74.65 E-value: 6.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1988 EAEGEAQPESEDVEAPEAEGEMQEAEEeaqpesdGVEAQPKSEGEEA--QEVEGETQkTEGDAQPESDGVEAPEAEEEAQ 2065
Cdd:TIGR00927 637 EAEHTGERTGEEGERPTEAEGENGEES-------GGEAEQEGETETKgeNESEGEIP-AERKGEQEGEGEIEAKEADHKG 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2066 EAEGEVQEAEGEAHPESedvDAQEAEGEAQPESEgVEAPEAEGEAQKAEGIE--APETEGEAQPESEG-IEAPEAEGEAQ 2142
Cdd:TIGR00927 709 ETEAEEVEHEGETEAEG---TEDEGEIETGEEGE-EVEDEGEGEAEGKHEVEteGDRKETEHEGETEAeGKEDEDEGEIQ 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2143 PEsEGVEAQDAEGEAQPESEGIEAQEAEEEAQPELEGVEAPEAEGEAQPESEGIEApEAEGEAQPELEGVEAPEAEEEAQ 2222
Cdd:TIGR00927 785 AG-EDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNA-ENQGEAKQDEKGVDGGGGSDGGD 862
|
250 260 270
....*....|....*....|....*....|.
gi 1375418697 2223 PEPEGVETPEAEGEAQPESEGETQGEKKGSP 2253
Cdd:TIGR00927 863 SEEEEEEEEEEEEEEEEEEEEEEEEEENEEP 893
|
|
| DCX |
cd01617 |
Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin ... |
152-220 |
6.71e-13 |
|
Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin (DCX) is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX gene family consists of eleven paralogs in human and mouse, and its DCX protein domains can occur in double tandem or as single DCX repeats. Proteins with DCX tandem domains in general have roles in microtubule (MT) regulation and signal transduction such as X-linked doublecortin (DCX), retinitis pigmentosa-1 (RP1) and doublecortin-like kinase (DCLK). Single DCX repeat proteins are normally localized to actin-rich subcellular structures, or the nucleus such as DCDC2. DCX is not only a unique MAP in terms of structure, it also interacts with multiple additional proteins. Mutations in human DCX genes are associated with abnormal neuronal migration, epilepsy, and mental retardation.
Pssm-ID: 340456 Cd Length: 73 Bit Score: 65.71 E-value: 6.71e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1375418697 152 RRILLIKNMDPRLQQTVVLSHRN-TRNLAAFLGKASDLLR---FPVKQLYTTSGKKVDSLQALLHSPSVLVCA 220
Cdd:cd01617 1 KRITVFRNGDKNFKGVKVLVKPRrFRTFDQLLDELTEKLGlptGGVRKLYTPSGKLVKSLSDLEDGESYVVCG 73
|
|
| DCX1_DCDC2C |
cd17151 |
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2C (DCDC2C); DCDC2 ... |
34-103 |
1.72e-11 |
|
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2C (DCDC2C); DCDC2 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.
Pssm-ID: 340671 Cd Length: 79 Bit Score: 62.11 E-value: 1.72e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 34 KKITFLKRGDPRFAGVRLAVHQRAFKTFSALMDELSQRVPLSFGVRSVTTPRGLHSLSALEQLEDGGCYL 103
Cdd:cd17151 1 KTILVYRNGDPFYQAHKVVIHRRRVKTFDALLRQLTETVKVPFGVRCLYTPRNGHRVKGLDDLQGGGKYV 70
|
|
| DCX1_DCLK1 |
cd17140 |
Dublecortin-like domain 1 found in doublecortin-like kinase 1 (DCLK1); DCLK1 is a member of ... |
33-111 |
6.90e-11 |
|
Dublecortin-like domain 1 found in doublecortin-like kinase 1 (DCLK1); DCLK1 is a member of doublecortin (DCX) protein superfamily that functions as a microtubule-associated protein (MAP), and contains two conserved tubulin binding domains. The DCX domain has a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. In addition to microtubule-binding domains, DCLK encodes a serine/threonine kinase domain that is similar to Ca/calmodulin-dependent (Cam) protein kinases. DCLK1 appears to regulate cyclic AMP signaling and is involved in neuronal migration, retrograde transport, neuronal apoptosis and neurogenesis. Unlike DCX, this DCLK has varying levels of expression throughout embryonic and adult life.
Pssm-ID: 340660 Cd Length: 89 Bit Score: 60.79 E-value: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 33 AKKITFLKRGDPRFAGVRLAVHQRAFKTFSALMDE----LSQRVPLSFGVRSVTTPRGLHSLSALEQLEDGGCYLCSDKK 108
Cdd:cd17140 2 AKKVRFYRNGDRYFKGIVYAISPDRFRSFEALLADltrtLSDNVNLPQGVRTIYTIDGLKKISSLDQLVEGESYVCGSIE 81
|
...
gi 1375418697 109 PPK 111
Cdd:cd17140 82 PFK 84
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1824-2121 |
8.39e-11 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 67.71 E-value: 8.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1824 QDPGQSDGAEGIEAPEAEGEAQPESEGVEAPEAEGDAQ-EAEGEAQPESEDVEAPEAEGEAQPESEDVETPEAEWEVQPE 1902
Cdd:TIGR00927 639 EHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKgENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHE 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1903 segaeapeaekeaqpETESVEALETEGEDEPESEGAEAQEAEEAAQEAEGQTQPESEVIESQEAEEEaqpesedvealEV 1982
Cdd:TIGR00927 719 ---------------GETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGET-----------EA 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1983 EVETQEAEGEAQPEsEDVEAPEAEGEMQEAEEEAQPESDGVEAQPKSEGEEAQEVEGETQKTEGDAQPESDGveapeaee 2062
Cdd:TIGR00927 773 EGKEDEDEGEIQAG-EDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQG-------- 843
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1375418697 2063 EAQEAEGEVQEAEGEAHPESEDVDAQEAEGEAQPESEGvEAPEAEGEAQKAEGIEAPET 2121
Cdd:TIGR00927 844 EAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEE-EEEEEEEENEEPLSLEWPET 901
|
|
| DCX1_DCLK2 |
cd17141 |
Dublecortin-like domain 1 found in doublecortin-like kinase 2 (DCLK2); DCLK2 is a member of ... |
33-109 |
1.43e-10 |
|
Dublecortin-like domain 1 found in doublecortin-like kinase 2 (DCLK2); DCLK2 is a member of doublecortin (DCX) protein superfamily that functions as a microtubule-associated protein (MAP), and contains two conserved tubulin binding domains, which typically occur in tandem. The DCX domain has a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier (Ubiquitination) in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. In addition to microtubule binding domains, DCLK encodes a serine/threonine kinase-domain that is similar to Ca/calmodulin-dependent (Cam) protein kinases. Molecular actions of DCX members are less well characterized and it shows that DCLK2 members regulate cyclic AMP signaling. Unlike DCX, this DCLK has varying levels of expression throughout embryonic and adult life.
Pssm-ID: 340661 Cd Length: 85 Bit Score: 59.53 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 33 AKKITFLKRGDPRFAGVRLAVHQRAFKTFSALMDEL----SQRVPLSFGVRSVTTPRGLHSLSALEQLEDGGCYLCSDKK 108
Cdd:cd17141 2 AKKVRFYRNGDRYFKGLVYAVSSDRFRSFDALLMELtrslSDNVNLPQGVRTIYTIDGSKKITSLDELLEGESYVCASNE 81
|
.
gi 1375418697 109 P 109
Cdd:cd17141 82 P 82
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1697-1935 |
1.79e-10 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 66.94 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1697 RGEHTDGEAAEVAPGKTHTDPTSTRTVQGAEGGLGPGLSQGPGVDEGEdGEGSQRLNRDKDPKLGEAEGDAMAQER---- 1772
Cdd:TIGR00927 641 TGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAE-RKGEQEGEGEIEAKEADHKGETEAEEVeheg 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1773 ----EGKTHNSETSAGSELGEAEQEGEGISERGETGG-QGSGHEDNLQGEAAAGG--DQDPGQSDGAEGIEAPEAEGEAQ 1845
Cdd:TIGR00927 720 eteaEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVEtEGDRKETEHEGETEAEGkeDEDEGEIQAGEDGEMKGDEGAEG 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1846 PESEGVEAPEAEGDAQEAEGEAQPESEDVEAPEAEGEAQPESEDvETPEAEWEVQPESEGAEAPEAEKEAQPETESVEAL 1925
Cdd:TIGR00927 800 KVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQG-EAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEE 878
|
250
....*....|
gi 1375418697 1926 ETEGEDEPES 1935
Cdd:TIGR00927 879 EEEEEEEEEE 888
|
|
| DCX1_DCDC2B |
cd17150 |
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2B (DCDC2B); DCDC2 ... |
34-103 |
1.92e-10 |
|
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2B (DCDC2B); DCDC2 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.
Pssm-ID: 340670 Cd Length: 79 Bit Score: 59.05 E-value: 1.92e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 34 KKITFLKRGDPRFAGVRLAVHQRAFKTFSALMDELSQRVPLSFGVRSVTTPRGLHSLSALEQLEDGGCYL 103
Cdd:cd17150 1 KNVVVYRNGDPFFTGRKFVVNQRQFLTFEAFLNEVTSNIQAPVAVRNLYTPREGHRVTELGDLQNGGHYV 70
|
|
| DCX1_DCDC2 |
cd17149 |
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is ... |
34-108 |
3.24e-10 |
|
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.
Pssm-ID: 340669 Cd Length: 80 Bit Score: 58.25 E-value: 3.24e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1375418697 34 KKITFLKRGDPRFAGVRLAVHQRAFKTFSALMDELSQRVPLSFG-VRSVTTPRGLHSLSALEQLEDGGCYLCSDKK 108
Cdd:cd17149 1 KNVLVYRNGDPFYAGRRLVINEKRVSSFEVFLKEVTGGVQAPFGaVRNIYTPRGGHRVRSLEQLQSGEQYVAAGRE 76
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1789-2053 |
3.71e-10 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 65.79 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1789 EAEQEGEGISERGETGGQGSGHEDNLQGEAAAGGDqdpgqsdgaegieapEAEGEAQPESEGVEAPEAEGDaQEAEGEAQ 1868
Cdd:TIGR00927 637 EAEHTGERTGEEGERPTEAEGENGEESGGEAEQEG---------------ETETKGENESEGEIPAERKGE-QEGEGEIE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1869 PESEDVEAPEAEGEAQPESE-DVETPEAEWEVQpesEGAEAPEAEKEAQPETESVEALETEGeDEPESEGAEAQEAEEAA 1947
Cdd:TIGR00927 701 AKEADHKGETEAEEVEHEGEtEAEGTEDEGEIE---TGEEGEEVEDEGEGEAEGKHEVETEG-DRKETEHEGETEAEGKE 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1948 QEAEGQTQPESEVIESQEAEEEAQPESEDVEALEVEVETQEAEGEAQPESEDVEAPEAEGEMQEAEEEAQPESDGVEAQP 2027
Cdd:TIGR00927 777 DEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGG 856
|
250 260
....*....|....*....|....*.
gi 1375418697 2028 KSEGEEAQEVEGETQKTEGDAQPESD 2053
Cdd:TIGR00927 857 GSDGGDSEEEEEEEEEEEEEEEEEEE 882
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1750-2053 |
3.90e-10 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 65.79 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1750 QRLNRDKDPKLgEAEGDAMAQEREGKTHNSETSAGSELGEAEQEGEGISERGETGGQGSGHEDnlQGEAAAGGD---QDP 1826
Cdd:TIGR00927 614 EQLSRRPVAKV-MALGDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETET--KGENESEGEipaERK 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1827 GQSDGAEGIEAPEAEGEAQPESEGVEAP---EAEGDAQEAEGEAQPESEDVEaPEAEGEAQ-PESEDVETPEAEWEVQpe 1902
Cdd:TIGR00927 691 GEQEGEGEIEAKEADHKGETEAEEVEHEgetEAEGTEDEGEIETGEEGEEVE-DEGEGEAEgKHEVETEGDRKETEHE-- 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1903 sEGAEAPEAEKEAQPETESVEALETEGEDEPESEGAEAqeaeeaaqeaegqtqpESEVIESQEAEEEAQPESEDVEALEV 1982
Cdd:TIGR00927 768 -GETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHE----------------GETEAGEKDEHEGQSETQADDTEVKD 830
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1375418697 1983 EVETQEAEGEAQPESEDVEapeaegemqeAEEEAQPESDGVEAQPKSEGEEAQEVEGETQKTEGDAQPESD 2053
Cdd:TIGR00927 831 ETGEQELNAENQGEAKQDE----------KGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENE 891
|
|
| DCX1_DCX |
cd16112 |
Dublecortin-like domain 1 found in neuronal migration protein doublecortin (DCX); DCX, also ... |
33-105 |
4.37e-10 |
|
Dublecortin-like domain 1 found in neuronal migration protein doublecortin (DCX); DCX, also termed doublin or lissencephalin-X (Lis-XDCX), is a microtubule-associated protein (MAP). It belongs to the doublecortin (DCX) family, has double tandem DCX repeats, and is expressed in migrating neurons. Structure studies show that the N-terminal DCX domain has a stable ubiquitin-like fold. DCX is not only a unique MAP in terms of structure, it also interacts with multiple additional proteins. Mutations in the human DCX genes are associated with abnormal neuronal migration, epilepsy, and mental retardation.
Pssm-ID: 340529 Cd Length: 89 Bit Score: 58.39 E-value: 4.37e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1375418697 33 AKKITFLKRGDPRFAGVRLAVHQRAFKTFSALMDEL----SQRVPLSFGVRSVTTPRGLHSLSALEQLEDGGCYLCS 105
Cdd:cd16112 2 AKKVRFYRNGDRYFKGIVYAVSSDRFRSFDALLADLtrslSDNINLPQGVRYIYTIDGSRKIGSMDELEEGESYVCS 78
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1849-2145 |
5.85e-10 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 65.02 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1849 EGVEAPEAEGDAQEAEGEAQPESEDVEAPEAEGEAQPESEDVETPEAEWEvqpesegaeapeaekeaqPETESVEALETE 1928
Cdd:TIGR00927 633 GDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESE------------------GEIPAERKGEQE 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1929 GEDEPESEGAEAQEAEEaaqeaegqtqpESEVIESQEAEEEAQPESEDVEALEV-EVETQEAEGEAQ-PESEDVEAPEAE 2006
Cdd:TIGR00927 695 GEGEIEAKEADHKGETE-----------AEEVEHEGETEAEGTEDEGEIETGEEgEEVEDEGEGEAEgKHEVETEGDRKE 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2007 GEMQEAEEEAQPESDGVEAQPKSEGEEAQEVEGETQKTEGDAQPESDGVEAPEAEEEAQEAEGEVQEAEGEAHPESEDvd 2086
Cdd:TIGR00927 764 TEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAEN-- 841
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1375418697 2087 aqeaEGEAQPESEGVEApEAEGEAQKAEGIEAPETEGEAQPESEGIEAPEAEGEAQPES 2145
Cdd:TIGR00927 842 ----QGEAKQDEKGVDG-GGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLS 895
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1734-2002 |
3.50e-09 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 62.71 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1734 LSQGpGVDEGEDgEGSQRLNRDKDPKLGEAE-----GDAMAQEREGKTHNSETSAG----SELGEAEQEGEGISERGETG 1804
Cdd:TIGR00927 630 LSKG-DVAEAEH-TGERTGEEGERPTEAEGEngeesGGEAEQEGETETKGENESEGeipaERKGEQEGEGEIEAKEADHK 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1805 GQGSGHEDNLQGEAAAGGDQDPGQSDGAEGIEAPEAEGEAqpESEGVEAPEAEGDAQEAEGEAQPESEDVEApEAEGEAQ 1884
Cdd:TIGR00927 708 GETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEG--EAEGKHEVETEGDRKETEHEGETEAEGKED-EDEGEIQ 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1885 PEsEDVETPEAEWEVQPESEGAEAPEAEKEAQPETESVEALETEGEDEPESEGAEAQEAEEAAQE------AEGQTQPES 1958
Cdd:TIGR00927 785 AG-EDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDekgvdgGGGSDGGDS 863
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1375418697 1959 EViESQEAEEEAQPESEDVEALEVEVETQEAEGEAQPESEDVEA 2002
Cdd:TIGR00927 864 EE-EEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPETRQKQA 906
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
2094-2285 |
4.04e-09 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 62.32 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2094 AQPESEGVEAPEAEGEAQKAEGIEAPETEGEAQPESEGieapeaEGEAQPESEG-VEA-----QDAEGEAQPESEGIEAQ 2167
Cdd:TIGR00927 636 AEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGET------ETKGENESEGeIPAerkgeQEGEGEIEAKEADHKGE 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2168 EAEEEAQPELEG-VEAPEAEGEAQPESEG-IEAPEAEGEAQ--PELEGVEAPEAEEEAQPEPEGVETPEAEGEAQPESEG 2243
Cdd:TIGR00927 710 TEAEEVEHEGETeAEGTEDEGEIETGEEGeEVEDEGEGEAEgkHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDG 789
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1375418697 2244 ETQGEKKGSPQVSLGDGQSEEASESSSPVPEDRPTPPPSPGG 2285
Cdd:TIGR00927 790 EMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDE 831
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1856-2161 |
9.17e-09 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 61.16 E-value: 9.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1856 AEGDAQEAEGEAQPESEDVEAP-EAEGEAQPESEDVETPEAEWEvqpesegaeapeaekeAQPETESVEALETEGEDEPE 1934
Cdd:TIGR00927 631 SKGDVAEAEHTGERTGEEGERPtEAEGENGEESGGEAEQEGETE----------------TKGENESEGEIPAERKGEQE 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1935 SegaeaqeaeeaaqeaegqtqpESEVIESQEAEEEAQPESEDVEALEVEVETQEAEGEAQPESEDVEAPEAEGEMQEAEE 2014
Cdd:TIGR00927 695 G---------------------EGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKH 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2015 EAQPESDGVEaqpkSEGEEAQEVEGETQKTEGDAQPESDGVEAPEAEEEAQEAEGEVQEAEGEAhpESEDVDAQEAEGEA 2094
Cdd:TIGR00927 754 EVETEGDRKE----TEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKD--EHEGQSETQADDTE 827
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375418697 2095 QPESEGVEAPEAEGEAQKAEGIEAPETEGEAQ-PESEGIEAPEAEGEAQPESEGVEAQDAEGEAQPES 2161
Cdd:TIGR00927 828 VKDETGEQELNAENQGEAKQDEKGVDGGGGSDgGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLS 895
|
|
| DCX |
pfam03607 |
Doublecortin; |
169-225 |
1.24e-08 |
|
Doublecortin;
Pssm-ID: 460986 Cd Length: 60 Bit Score: 53.22 E-value: 1.24e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1375418697 169 VLSHRNTRNLAAFLGKASDL---LRFP-VKQLYTTSGKKVDSLQaLLHSPSVLVCAGHEAF 225
Cdd:pfam03607 1 VVNKRRFRSFDALLDELTEKvvkLPFGaVRKLYTLDGKRVTSLD-ELEDGGVYVAAGREKF 60
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1715-1901 |
1.25e-08 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 60.78 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1715 TDPTSTRTVQGAEGGLGPGLSQGPGVDEGEDGEGSQRLNRDKDPKLGEAEGDAMAQ---EREGKTHNSETSAGSELGEAE 1791
Cdd:TIGR00927 697 GEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKhevETEGDRKETEHEGETEAEGKE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1792 QEGEGISERGETG---------GQGSGHEDNLQGEAAAGGDQDPGQSDGaEGIEAPEAEGEAQPESEGvEAPEAEGDAQE 1862
Cdd:TIGR00927 777 DEDEGEIQAGEDGemkgdegaeGKVEHEGETEAGEKDEHEGQSETQADD-TEVKDETGEQELNAENQG-EAKQDEKGVDG 854
|
170 180 190
....*....|....*....|....*....|....*....
gi 1375418697 1863 AEGEAQPESEDVEAPEAEGEAQPESEDVETPEAEWEVQP 1901
Cdd:TIGR00927 855 GGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEP 893
|
|
| DCX |
smart00537 |
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ... |
147-228 |
1.07e-07 |
|
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the Doublecortin gene product. Proposed to bind tubulin. Doublecortin (DCX) is mutated in human X-linked neuronal migration defects.
Pssm-ID: 214711 Cd Length: 89 Bit Score: 51.49 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 147 SLKTPRRILLIKNMDP-RLQQTVVLSHRNTRNLAAFLGKASDLLR----FPVKQLYTTSGKKVDSLQALLHSpSVLVCAG 221
Cdd:smart00537 1 SLVKPKRIRFYRNGDRfFKGVRLVVNRKRFKSFEALLQDLTEVVKldlpHGVRKLYTLDGKKVTSLDELEDG-GSYVASG 79
|
....*..
gi 1375418697 222 HEAFRTP 228
Cdd:smart00537 80 TEAFKKV 86
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
1741-1934 |
5.16e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 51.51 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1741 DEGEDGEGSQRLNRDKDPKLGEAEGDAmaqEREGKTHNSETSAGSELGEAEQEGEGiserGETGGQGSGHEDNLQGEAAA 1820
Cdd:PHA03169 50 APTTSGPQVRAVAEQGHRQTESDTETA---EESRHGEKEERGQGGPSGSGSESVGS----PTPSPSGSAEELASGLSPEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1821 GGDQDPGQSDGAEGIEAPEAEGEAQPESEGVEAPEAEGDAQEAEGEAQPESEDVEAPEAEGEAQPESEDVETPEAEWEVQ 1900
Cdd:PHA03169 123 TSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSP 202
|
170 180 190
....*....|....*....|....*....|....*.
gi 1375418697 1901 PESEGAEAPEAEKEAQPE--TESVEALETEGEDEPE 1934
Cdd:PHA03169 203 PPQSPPDEPGEPQSPTPQqaPSPNTQQAVEHEDEPT 238
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
2027-2208 |
1.06e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 50.35 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2027 PKSEGEEAQEVEGETQKTEGDAQPESDGVEAPEAEEEAQEAEGEVQEAEGEAHPESEDVDAQEAEGEAQPESEGVEAPEA 2106
Cdd:PHA03169 51 PTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPES 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2107 EGEAQKAEGIEAPETEGEAQPESE----GIEAPEAEGEAQPESEGVEAQDAEGEAQPESEGIEAQEAEEEAQPELEGVE- 2181
Cdd:PHA03169 131 PASHSPPPSPPSHPGPHEPAPPEShnpsPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDe 210
|
170 180
....*....|....*....|....*...
gi 1375418697 2182 -APEAEGEAQPESEGIEAPEAEGEAQPE 2208
Cdd:PHA03169 211 pGEPQSPTPQQAPSPNTQQAVEHEDEPT 238
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
1773-1959 |
1.13e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 50.35 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1773 EGKTHNSETSAGSELGEAEQEGEGISERGETGGQGSGHEDNLQGEAAAGGDQDPGQSDGAEGIEA-PEAEGEAQPESEGV 1851
Cdd:PHA03169 54 SGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLsPENTSGSSPESPAS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1852 EAPEAEGDAQEAEGEAQPESEDVEAPE--AEGEAQPESEDVETPEAEWEVQPESEGAEAPEAEKEAQPETESVEALETEG 1929
Cdd:PHA03169 134 HSPPPSPPSHPGPHEPAPPESHNPSPNqqPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGE 213
|
170 180 190
....*....|....*....|....*....|
gi 1375418697 1930 EDEPESEGAEAQEAEEAAQEAEGQTQPESE 1959
Cdd:PHA03169 214 PQSPTPQQAPSPNTQQAVEHEDEPTEPERE 243
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
1694-1896 |
1.26e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 50.35 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1694 QRKRGEHTDGEAAEVAPGKTHTDPTSTRTVQGAEGGLGPGLSQGPGVDEGEDGEGSQRLNRDKDPKLGEAEGDAMAQERE 1773
Cdd:PHA03169 56 PQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1774 GKTHNSETSAGSELGEAEQEGEGISERGETGGQGSGHEDNLQGEAAAGGDQDpgqsdgaegiEAPEAEGEAQPESEGVEA 1853
Cdd:PHA03169 136 PPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEP----------DSPGPPQSETPTSSPPPQ 205
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1375418697 1854 PEAEGDAQEAEGEAQPESEDVEAPEAEGEAQPESEDVETPEAE 1896
Cdd:PHA03169 206 SPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFP 248
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1787-2208 |
1.29e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 50.75 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1787 LGEAEQEGEGIS---ERGETGGQGSGHEDNLQGEAAAGGDQDPG-QSDGAEGIEAPEAEGEAQPESEGVEAPEAEGDAQE 1862
Cdd:PRK07764 364 LPSASDDERGLLarlERLERRLGVAGGAGAPAAAAPSAAAAAPAaAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPS 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1863 AEGEAQPESEDVEAPEAEGEAQPE--SEDVETPEAEWEVQPESEGAEAPEAEKEAQPETES----VEALETEGEDEPESE 1936
Cdd:PRK07764 444 PAGNAPAGGAPSPPPAAAPSAQPApaPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAgaddAATLRERWPEILAAV 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1937 GAEAQEAEEAAQEAEGQTQPESE--VIESQEAEEEAQPESEDVEALEVEVETQEAEGEAQPESEdVEAPEAEGEMQEAEE 2014
Cdd:PRK07764 524 PKRSRKTWAILLPEATVLGVRGDtlVLGFSTGGLARRFASPGNAEVLVTALAEELGGDWQVEAV-VGPAPGAAGGEGPPA 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2015 EAQPESDGVEAQPKSEGEEAQEVEGETQKTEGDAQPESDGVEAPEAEEEAQEAEGEVQEAEGEAHPESEDVDAQEAEGEA 2094
Cdd:PRK07764 603 PASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPP 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2095 QPESEGVEAPEAEGeaqkAEGIEAPETEGEAQPESEGIEAPEAEGEAQPESEGVEAQDAEGEAQPESEGIEAQEAEEEAQ 2174
Cdd:PRK07764 683 PAPAPAAPAAPAGA----APAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQP 758
|
410 420 430
....*....|....*....|....*....|....
gi 1375418697 2175 PELEGVEAPEAEGEAQPESEGIEAPEAEGEAQPE 2208
Cdd:PRK07764 759 PPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPS 792
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
2106-2250 |
3.61e-05 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 49.22 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2106 AEGEAQKAEGIEAPET------EGEAQPESEGIEAPEAEGEAQPESEGveaqdaEGEAQPESEGieaqeaeeeaQPELEG 2179
Cdd:TIGR00927 626 ALGDLSKGDVAEAEHTgertgeEGERPTEAEGENGEESGGEAEQEGET------ETKGENESEG----------EIPAER 689
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1375418697 2180 VEAPEAEGEAQPESEGIEAPEAEGEAQPELEGVEAPEAEEEAQPEPEG--VETPEAEGEAQPESEGETQGEKK 2250
Cdd:TIGR00927 690 KGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEgeEVEDEGEGEAEGKHEVETEGDRK 762
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
2041-2245 |
1.19e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 46.89 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2041 TQKTEGDAQPESDGVEAPEAEEEAQEAEGEVQEAEGEAHPESEDVDAQEAEGEAQPESEGVEAPEAEGEAQKAEGIEAPE 2120
Cdd:PHA03169 43 AAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2121 TEGEAQPESEGIEAPEAEGEAQPESEGVEAQDAEGEAQPESEGIEAQEAEEEAQPELEGVEAPEAEGEAQPESE--GIEA 2198
Cdd:PHA03169 123 TSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSEtpTSSP 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1375418697 2199 PEAEGEAQPELEGVEAPEAEEEAQPEPEGVETPEAEGEAQPESEGET 2245
Cdd:PHA03169 203 PPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPG 249
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
1713-2355 |
1.64e-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: 47.32 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1713 THTDPTSTRTVQGAEGGLGPGLSQGPGVDEGEDGEGSQRLNRDKDPKLGEAEGDAMAQEREGKTHNSETSAGSELGEAEQ 1792
Cdd:COG5271 370 GEAADESEGADTDAAADEADAAADDSADDEEASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1793 EGEGISERGETGgQGSGHEDNLQGEAAAGGDQDPGQSDGAEGIEAPEAEGEAQPESEGVEAPEAEGDA---QEAEGEAQP 1869
Cdd:COG5271 450 DSLADEEEEAEA-ELDTEEDTESAEEDADGDEATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSAddgADTDAAADP 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1870 ESEDVEAPEAEGEAQPESEDVETPEAEWEVQPESEGAEAP---EAEKEAQPETESVEAlETEGEDEPESEGAEAQEAEEA 1946
Cdd:COG5271 529 EDSDEDALEDETEGEENAPGSDQDADETDEPEATAEEDEPdeaEAETEDATENADADE-TEESADESEEAEASEDEAAEE 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1947 AQEAEGQTQPESEVIESQEAEEEAQPESEDVEALEVEVETQEAEGEAQPE---SEDVEAPEAEGEMQEAEEEAQPESDGV 2023
Cdd:COG5271 608 EEADDDEADADADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEaeaSADESEEEAEDESETSSEDAEEDADAA 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2024 EAQPKSEGEEAQEVEGETQKTEGDAQPESDGVEAPEAEEEAQEAEGEVQEAEGEAHPESEDVDAQEAEGEAQPESEGvEA 2103
Cdd:COG5271 688 AAEASDDEEETEEADEDAETASEEADAEEADTEADGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEED-DA 766
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2104 PEAEgeaqkaEGIEAPETEGEAQPESEGIEAPEAEGEAQPESEGVEAQDAEGEAQPESEGIEAQEAEEEAQPELEGVEAP 2183
Cdd:COG5271 767 DGLE------EALEEEKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEA 840
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2184 E--AEGEAQPESEGIEAPEAEGEAQPELEGVEAPEAEEEAQPEPEGVETPEAEGEAQPESEGETQGEKKGSPQVSLGDGQ 2261
Cdd:COG5271 841 GiaEDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADADAGEADSSGESSAAAEDDDAAEDADSDDGAN 920
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2262 SEEASESSSPVPEDRPTPPPSPGGDTPHQRPGSQTGPSSSRASSWGNCWQKDSENDHVLGDTRSPDAKSTGTPHAERKAT 2341
Cdd:COG5271 921 DEDDDDDAEEERKDAEEDELGAAEDDLDALALDEAGDEESDDAAADDAGDDSLADDDEALADAADDAEADDSELDASEST 1000
|
650
....*....|....
gi 1375418697 2342 RMYPESSTSEQEEA 2355
Cdd:COG5271 1001 GEAEGDEDDDELED 1014
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
1978-2160 |
2.04e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 46.12 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1978 EALEVEVETQEAEGEAQPESEDVEAPEAEGEMQEAEEEAQPESD--GVEAQPKSEGEEAQEVEGETQKTEGDAQPESDGV 2055
Cdd:PHA03169 69 TESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEelASGLSPENTSGSSPESPASHSPPPSPPSHPGPHE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2056 EAPEAEEEAQEAEGEVQEAEGEAHPESEDVDaqeaEGEAQPESEGVEAPEAEGEAQKAEGIEAPETEGEAQpESEGIEAP 2135
Cdd:PHA03169 149 PAPPESHNPSPNQQPSSFLQPSHEDSPEEPE----PPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQ-SPTPQQAP 223
|
170 180
....*....|....*....|....*
gi 1375418697 2136 EAEGEAQPESEGVEAQDAEGEAQPE 2160
Cdd:PHA03169 224 SPNTQQAVEHEDEPTEPEREGPPFP 248
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
1688-2202 |
2.41e-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: 46.55 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1688 DLQQILQRKRGEHTDGEAAEVAPGKTHTDPTSTRTVQGAEGGLGPGLSQ--GPGVDEGEDGEGSQRLNRDKDPKLGEAEG 1765
Cdd:COG5271 249 LADDDDTESAGATAEVGGTPDTDDEATDDADGLEAAEDDALDAELTAAQaaDPESDDDADDSTLAALEGAAEDTEIATAD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1766 DAMAQEREGKTHNSETSAGSELGEAEQEGEGISERGETGGQGSGHEDNLQGEAAAGGDQDPGQSDGAEGIEAPEAEGEAQ 1845
Cdd:COG5271 329 ELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEEASADGGTS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1846 PESEGVEAPEaEGDAQEAEGEAQPESEDVEAPEAEGEAQPESEDVETPEAEWEVQPESEGAEAPEAEKEAQPETESVEAL 1925
Cdd:COG5271 409 PTSDTDEEEE-EADEDASAGETEDESTDVTSAEDDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDA 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1926 ETEGEDEPESEGAEAQEAEEAAQEAEGQTQPESEViesqeaeeeaqPESEDVEALEVEVETQEAEGEAQPESEDVEAPEa 2005
Cdd:COG5271 488 SDDGDEEEAEEDAEAEADSDELTAEETSADDGADT-----------DAAADPEDSDEDALEDETEGEENAPGSDQDADE- 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2006 egemqeaeeeaqpesdgvEAQPKSEGEEAQEVEGETQKTEGDAQPESDGVEAPEAEEEAQEAEGEVQEAEGEAHPESEDV 2085
Cdd:COG5271 556 ------------------TDEPEATAEEDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2086 DAQEAEGEAQPESEGVEAPEAEGEAQKAEGIEA---PETEGEAQPESEGIEAPEaEGEAQPESEGVEAQDAEGEAQPESE 2162
Cdd:COG5271 618 DADGAADEEETEEEAAEDEAAEPETDASEAADEdadAETEAEASADESEEEAED-ESETSSEDAEEDADAAAAEASDDEE 696
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1375418697 2163 GIEAQEAEEEAQPELEGVEAPEAEGEAQPESEGIEAPEAE 2202
Cdd:COG5271 697 ETEEADEDAETASEEADAEEADTEADGTAEEAEEAAEEAE 736
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1977-2157 |
3.71e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 46.19 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1977 VEALEVEVETQEAEGEAQPESEDVEAPEAEGEMQEAEEEAQPESDGVEAQPKSEGEEAQEVEGETQKTEGDAQPesdgve 2056
Cdd:PRK10811 850 PQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAP------ 923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2057 apeaeeeaqeaegeVQEAEGEAHPESEDVDAQEAEgEAQPESEGVEAPEAEGEAQKAEGIEAPETEGEAQPESEGIEAPE 2136
Cdd:PRK10811 924 --------------VTEQPQVITESDVAVAQEVAE-HAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVA 988
|
170 180
....*....|....*....|.
gi 1375418697 2137 AEGEAQPESEGVEAQDAEGEA 2157
Cdd:PRK10811 989 AEVETVTAVEPEVAPAQVPEA 1009
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
1757-1929 |
4.63e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 45.35 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1757 DPKLGEAEGDAMAQEREGKTHNSETSAGSELGEAEQEGEGISERGETGGQGSGHEDNlqgEAAAGGDQDPGQSDGAEGIE 1836
Cdd:PHA03169 78 ESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASH---SPPPSPPSHPGPHEPAPPES 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1837 APEAEGEAQPESEGVEAPEAEGDAQEAEGEAQPESEDVEAPEAEGEAQPESE--DVETPEAEWEVQPESEGAEAPEAEKE 1914
Cdd:PHA03169 155 HNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSppDEPGEPQSPTPQQAPSPNTQQAVEHE 234
|
170
....*....|....*
gi 1375418697 1915 AQPETESVEALETEG 1929
Cdd:PHA03169 235 DEPTEPEREGPPFPG 249
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1726-1945 |
6.84e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.98 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1726 AEGGLGPGLSQGPGVDEGEDGEGSQRLNRDKDPklGEAEGDAMAQEREGKTHNSETSAGSELGEAEQEGEGISERGETGG 1805
Cdd:PRK07764 586 AVVGPAPGAAGGEGPPAPASSGPPEEAARPAAP--AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1806 QGSGHEDNLQGEAAAGGDQdPGQSDGAEGIEAPEAEGEAQPESEGVEAPE-AEGDAQEAEGEAQPESEDVEAPEAEGEAQ 1884
Cdd:PRK07764 664 DGGDGWPAKAGGAAPAAPP-PAPAPAAPAAPAGAAPAQPAPAPAATPPAGqADDPAAQPPQAAQGASAPSPAADDPVPLP 742
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1375418697 1885 PESEDVETPEAEWEVQPESEGAEAPEAEKEAQPETESVEALETEGEDEPESEGAEAQEAEE 1945
Cdd:PRK07764 743 PEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEE 803
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1744-2249 |
7.65e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1744 EDGEGSQRLNRDKDPKLGEAEGDAMAQEREGKTHNSETSAGSELGEAEQEGEGISE-RGETGGQGSGHEDNLQGEAAAGG 1822
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEaKKADEAKKKAEEAKKKADAAKKK 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1823 DQDPGQSDGAEGIEAPEAEGEAQPESEGVEA-----PEAEGDAQEAEGEAQPESEDVEAPEAEGEAQPESEDVETPEAEW 1897
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaekkkEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1898 ----EVQPESEGAEAPEAEKEAQPETESVEALETEGEDEPESEGAEAQEAEEAAQEAEGQTQPESEVIESQEAEEEAQPE 1973
Cdd:PTZ00121 1418 kkadEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKK 1497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1974 SEDvEALEVEVETQEAEgEAQPESEDVEAPEAEGEMQEAEEEAQPESDGV-EAQPKSEGEEAQEVEgETQKTEGDAQPES 2052
Cdd:PTZ00121 1498 KAD-EAKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKkKADELKKAEELKKAE-EKKKAEEAKKAEE 1574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2053 DGVEAPEAEEEAQEAEGEVQEAEGEAHPESEDVDAQEAEGEAQPESEGVEAPEAEGEAQKAEGIEAPETE-----GEAQP 2127
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekkkaEELKK 1654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2128 ESEGIEAPEAEGEAQPESEGVEAQDAEGEAQPESEGIEAQEAEEEAQPELEGVEAPEAEGEAQPEsegiEAPEAEGEAQP 2207
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE----ELKKAEEENKI 1730
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1375418697 2208 ELEGVEAPEAEEEAQPEPEGVETPEAEGEAQPESEGETQGEK 2249
Cdd:PTZ00121 1731 KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
1815-1898 |
8.37e-04 |
|
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 443611 [Multi-domain] Cd Length: 608 Bit Score: 44.78 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1815 QGEAAAGGDQDPGQSDGAEGIEAPEAEGEAQPESEGVEAPEAEGDAQEAEgeaQPESEDVEAPEAEGEAQPESEDVETPE 1894
Cdd:COG4547 211 LGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEGAEAEDAEASGDDAE---EGESEAAEAESDEMAEEAEGEDSEEPG 287
|
....
gi 1375418697 1895 AEWE 1898
Cdd:COG4547 288 EPWR 291
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
561-904 |
9.08e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.78 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 561 AETSQQEASEGGDPASPALSLS----SLRSDDLQAETQGQGTEQATGAAVTREPLVLGLSCSWDSEGASSTPSTCTSSQQ 636
Cdd:PHA03307 18 GEFFPRPPATPGDAADDLLSGSqgqlVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 637 GQRRHRSRASAMSSPSSPGLGRVAPRGHPRHSHyrKDTHSPLDSSVTKQVPRPPERRRAcqDGSVPRYSGSSSSTRTQAS 716
Cdd:PHA03307 98 ASPAREGSPTPPGPSSPDPPPPTPPPASPPPSP--APDLSEMLRPVGSPGPPPAASPPA--AGASPAAVASDAASSRQAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 717 GNLRPPSSGSLPSQDLLGTSSATVTPAVHSDFVSGVSPHNAPSAGWAGDAGSRtcSPAPIPPHTSDSCSKSGAASLGEEA 796
Cdd:PHA03307 174 LPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGR--SAADDAGASSSDSSSSESSGCGWGP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 797 RD-TPQPSSPLVLQVGRPEQGAVGPHRShCCSQPGTQPAQEAQRGPSPEASWLCGRYCPTPPRGRPCPQRRSSSCGSTGS 875
Cdd:PHA03307 252 ENeCPLPRPAPITLPTRIWEASGWNGPS-SRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTS 330
|
330 340 350
....*....|....*....|....*....|
gi 1375418697 876 SHQSTARGPGGSP-QEGTRQPGPTPSPGPN 904
Cdd:PHA03307 331 SSSESSRGAAVSPgPSPSRSPSPSRPPPPA 360
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
1806-1885 |
1.30e-03 |
|
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 443611 [Multi-domain] Cd Length: 608 Bit Score: 44.01 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1806 QGSGHEDNLQGEAAAGGDQDPGQSDGAEGIEAPEAEGEAQPESEGVEAPEAEGDAQEAEGEAQPESEDVEAPEAEGEAQP 1885
Cdd:COG4547 210 ELGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEGAEAEDAEASGDDAEEGESEAAEAESDEMAEEAEGEDSEEPGEP 289
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2024-2158 |
1.77e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2024 EAQPKSEGEEAQEVEGETQKTEGDAQPESDGVEAPEAEEEAQEAEGEVQEAEGEAHPESEDVDAQEAEGEAQPESEGVEA 2103
Cdd:PRK09510 113 AQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAA 192
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1375418697 2104 PEAEGEAQK---AEGIEAPETEGEAQPESEGIEAPE-AEGEAQPESEGVEAQDAEGEAQ 2158
Cdd:PRK09510 193 AKAAAEAKKkaeAEAKKKAAAEAKKKAAAEAKAAAAkAAAEAKAAAEKAAAAKAAEKAA 251
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
2073-2160 |
1.85e-03 |
|
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 443611 [Multi-domain] Cd Length: 608 Bit Score: 43.63 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2073 EAEGEAHPESEDVDAQEAEGEAQPESEGVEAPEAEGEAQkaegieapETEGEAQPESEGIEAPEAEGEAQPESEGVEAQD 2152
Cdd:COG4547 208 AEELGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEG--------AEAEDAEASGDDAEEGESEAAEAESDEMAEEAE 279
|
....*...
gi 1375418697 2153 AEGEAQPE 2160
Cdd:COG4547 280 GEDSEEPG 287
|
|
| PRK13108 |
PRK13108 |
prolipoprotein diacylglyceryl transferase; Reviewed |
1989-2152 |
2.59e-03 |
|
prolipoprotein diacylglyceryl transferase; Reviewed
Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 42.66 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1989 AEGEAQPESEDVEAPEAEGEMQEAEEEAQPESDGVEAQPKSEGEEAQEVEGETQKTEGDAQPESDGVEAPEAEEEAQEAE 2068
Cdd:PRK13108 292 VDEALEREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADI 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2069 GEVQEAEGEAHPESEDVDAQEAEGEAQPESEGVEAPEAEGEAQKAEGIEAPETeGEAQPESEGIEAPEAegeAQPESEGV 2148
Cdd:PRK13108 372 EREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIP-DPAKPDELAVAGPGD---DPAEPDGI 447
|
....
gi 1375418697 2149 EAQD 2152
Cdd:PRK13108 448 RRQD 451
|
|
| DCX2 |
cd17069 |
Dublecortin-like domain 2; Members in doublecortin (DCX) gene family are ... |
150-227 |
3.36e-03 |
|
Dublecortin-like domain 2; Members in doublecortin (DCX) gene family are microtubule-associated proteins (MAPs). Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX gene family consists of eleven paralogs in human and mouse, and its protein domains can occur in double tandem or as a single repeat. The first repeat of DCX domain has a stable ubiquitin-like tertiary fold. Proteins with DCX double tandem domains in general have roles in microtubule (MT) regulation and signal transduction such as X-linked doublecortin (DCX), retinitis pigmentosa-1 (RP1) and doublecortin-like kinase (DCLK).
Pssm-ID: 340589 Cd Length: 84 Bit Score: 38.52 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 150 TPRRILLIKN-MDPRLQQTVVLSHRNTRNLAAFLGKASDLLRF---PVKQLYTTSGKKVDSLQALLHSPSVLVCAGHEAF 225
Cdd:cd17069 3 KPKLVTVIRNgTKPRKAVRILLNKKTAHSFEQVLTDITEAIKLdsgAVRKLFTLDGRQVTCLQDFFGDDDVFIAYGPEKF 82
|
..
gi 1375418697 226 RT 227
Cdd:cd17069 83 SH 84
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
2024-2188 |
7.73e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 41.11 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2024 EAQPKSEGEEAQEVEGETQKTEGDAQPESDGV-----EAPEAEEEAQEAEGEVQEAEGEAHPESEDVDAQEAEGEAQPES 2098
Cdd:PHA03169 87 RGQGGPSGSGSESVGSPTPSPSGSAEELASGLspentSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSF 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 2099 EGveaPEAEGEAQKAEGieapeTEGEAQPESEGIEAPEAEGEAQPESEGVEAQDAEGEAQPESEGIEAQEAEEEAQPELE 2178
Cdd:PHA03169 167 LQ---PSHEDSPEEPEP-----PTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPT 238
|
170
....*....|
gi 1375418697 2179 GVEAPEAEGE 2188
Cdd:PHA03169 239 EPEREGPPFP 248
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
1718-1921 |
8.21e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 41.11 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1718 TSTRTVQGAEGGLGPGLSQGPGVDEGEDGEGSqrlnrdkDPKLGEAEGDAMAQEREGKTHNSETSAGSELGEAEQEGEGI 1797
Cdd:PHA03169 75 TAEESRHGEKEERGQGGPSGSGSESVGSPTPS-------PSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPH 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1798 SERGETGGQGSGHEdnlQGEAAAGGDQDPGQSDGAEGIEAPEAEGEAQPESEGVEAPEAEGDAQEAEGEAQPESEDvEAP 1877
Cdd:PHA03169 148 EPAPPESHNPSPNQ---QPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQ-QAP 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1375418697 1878 EAEGEAQPESEDVETPEAEwevqpesegaeapeaEKEAQPETES 1921
Cdd:PHA03169 224 SPNTQQAVEHEDEPTEPER---------------EGPPFPGHRS 252
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1695-1873 |
8.74e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 41.43 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1695 RKRGEHTDGEAAEVAPGKTHTDPTSTRTVQGAEGGLGPGLSQGPGVDEGEDGEGSQRLNRDKDPKLGEAEGDAMAQEREG 1774
Cdd:PRK12678 77 ARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375418697 1775 KTHNSETSAGSELGEAEQEGEgiseRGETGGQGSGHEDNLQGEAAAGGDQDPGQSDGAEGIEAPEAEGEAQPESEG--VE 1852
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGD----REDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGrrRR 232
|
170 180
....*....|....*....|.
gi 1375418697 1853 APEAEGDAQEAEGEAQPESED 1873
Cdd:PRK12678 233 RDRRDARGDDNREDRGDRDGD 253
|
|
| |
