|
Name |
Accession |
Description |
Interval |
E-value |
| Hydin_ADK |
pfam17213 |
Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to ... |
429-630 |
1.51e-116 |
|
Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to adenylate kinases.
Pssm-ID: 465383 Cd Length: 199 Bit Score: 367.54 E-value: 1.51e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 429 AIIVHGTPLSGKTANAISMAKFYNAACLNIDSIVLEALSDTNNILGIRARELCIRAAIEQSMREAEESAaHESSMTQNTV 508
Cdd:pfam17213 1 AIIVHGAPLSGKTATAVTLAKHYGAACLTIDSIVLEAISDGNSIAGLRARELCARAAIEQSEREAEEAA-QEAAVVPGQP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 509 VPARLSTENLGRFTSELTLITQEYKVPKTVRGSVMLPKGKADSHFTGSQKQHHQHQSETPQvqISSSPLLPGPTHRRLSV 588
Cdd:pfam17213 80 TTYRLSVEALTKHTSEGTLVGPESKISKGKRGSVVSGKGKADSHGTGSQKQHHQHQSETPQ--ISSSPPPAGPIQRRLSV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720427463 589 SASIGGETGLMSCVLPDDLLIQILAERIQLSNCFRGVVFDGL 630
Cdd:pfam17213 158 SASVGGEEGLMSCVLPEDLLVEILAERIQLNDCHRGVVFDGL 199
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
668-858 |
2.98e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 69.77 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDRDVRQaLRERKKRELERLAKEMQEKKLQQELERQ 747
Cdd:pfam17380 389 QKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR-LEEERAREMERVRLEEQERQQQVERLRQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 748 KEEDELKRKVKRpkagpaAKEEPPLKKAQgatnkqlaavakiELKMESIERKVSVREHATLEETTRKK---KAMTEYPll 824
Cdd:pfam17380 468 QEEERKRKKLEL------EKEKRDRKRAE-------------EQRRKILEKELEERKQAMIEEERKRKlleKEMEERQ-- 526
|
170 180 190
....*....|....*....|....*....|....
gi 1720427463 825 IPISQEQEDSEGDFLKDSDKNLAQKFKIYDMCLK 858
Cdd:pfam17380 527 KAIYEEERRREAEEERRKQQEMEERRRIQEQMRK 560
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
668-820 |
1.10e-10 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 66.41 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEENKR--KEALAKEKERLQTLDE---DEYDALTAEEKVAFDRDVRQALRERK-KRELERLAKEMQ--EKK 739
Cdd:TIGR02794 64 KKEQERQKKLEQQAEeaEKQRAAEQARQKELEQraaAEKAAKQAEQAAKQAEEKQKQAEEAKaKQAAEAKAKAEAeaERK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 740 LQQELERQKEEDELKrkvkrpKAGPAAKeepplKKAQGATnKQLAAVAKielKMESIERKVsVREHATLEETTRKKKAMT 819
Cdd:TIGR02794 144 AKEEAAKQAEEEAKA------KAAAEAK-----KKAEEAK-KKAEAEAK---AKAEAEAKA-KAEEAKAKAEAAKAKAAA 207
|
.
gi 1720427463 820 E 820
Cdd:TIGR02794 208 E 208
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
646-817 |
1.73e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.47 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 646 LKAIGSREHIYVINMSQDYVVMKAqEKAKKEQEENKRKEALAKEKERLQTLDEDEYDalTAEEKvafdrdvRQALRERKK 725
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKA-EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK--EAEEK-------KKAEELKKA 1655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 726 RELERLAKEmQEKKLQQELERQKEEDELKRKVKRPKAGPAAKEEPPLKKAQGATNKQLAAVAKIE-LKMESIERKVSVrE 804
Cdd:PTZ00121 1656 EEENKIKAA-EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEeLKKAEEENKIKA-E 1733
|
170
....*....|...
gi 1720427463 805 HATLEETTRKKKA 817
Cdd:PTZ00121 1734 EAKKEAEEDKKKA 1746
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
667-799 |
4.62e-10 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 64.48 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 667 MKAQEKAKKEQEENKRKEALAKEKErlqtldedEYDALTAEEKVAfdrDVRQALRERKKRELERLAKEMQEKKLQQELER 746
Cdd:TIGR02794 104 AKQAEQAAKQAEEKQKQAEEAKAKQ--------AAEAKAKAEAEA---ERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK 172
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427463 747 QKEEDELK------RKVKRPKAgpAAKEEPPLKKAQgATNKQLAAVAKIELKMESIERK 799
Cdd:TIGR02794 173 KKAEAEAKakaeaeAKAKAEEA--KAKAEAAKAKAA-AEAAAKAEAEAAAAAAAEAERK 228
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
668-941 |
1.51e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 63.99 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDRDVRQ---ALRERKKRELERLAKEMQEK--KLQQ 742
Cdd:pfam17380 317 KLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQeeiAMEISRMRELERLQMERQQKneRVRQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 743 ELERQKE----EDELKRKVKRPKagpaaKEEPPLKKAQGATNKQLAAVAKIE-------LKMESIERKVSVREHATLEET 811
Cdd:pfam17380 397 ELEAARKvkilEEERQRKIQQQK-----VEMEQIRAEQEEARQREVRRLEEEraremerVRLEEQERQQQVERLRQQEEE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 812 TRKKKAMTEypllipisQEQEdsegdflkdsDKNLA--QKFKIYDMCLKdvqnilmywDRKQGMMVPHTGTDEMSHEADD 889
Cdd:pfam17380 472 RKRKKLELE--------KEKR----------DRKRAeeQRRKILEKELE---------ERKQAMIEEERKRKLLEKEMEE 524
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1720427463 890 QRQAPSGGGGRKGRKDrererlekeraeKERLEREKAERERLEK--LKALEERS 941
Cdd:pfam17380 525 RQKAIYEEERRREAEE------------ERRKQQEMEERRRIQEqmRKATEERS 566
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
662-817 |
2.79e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 61.86 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 662 QDYVVMKAQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDRDVRQALRERKKRELERLAKEMQEKK-L 740
Cdd:pfam13868 158 LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQeL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 741 QQELERQKEEDELKRKVKRpkagpaAKEEpplKKAQGATNKQLAAvAKIElKMESIERKVSVREHAT-----LEETTRKK 815
Cdd:pfam13868 238 QQAREEQIELKERRLAEEA------EREE---EEFERMLRKQAED-EEIE-QEEAEKRRMKRLEHRRelekqIEEREEQR 306
|
..
gi 1720427463 816 KA 817
Cdd:pfam13868 307 AA 308
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
666-817 |
2.84e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 666 VMKAQEKAKKEQ-----EENKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDrDVRQALRERKKRElerlAKEMQEKKL 740
Cdd:PTZ00121 1229 VKKAEEAKKDAEeakkaEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD-ELKKAEEKKKADE----AKKAEEKKK 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 741 QQELERQKEE----DELKRKVKRPKagpaAKEEPPLKKAQGATNKQLAAVAKIELKMESIERKVSVREHATLEETTRKKK 816
Cdd:PTZ00121 1304 ADEAKKKAEEakkaDEAKKKAEEAK----KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
.
gi 1720427463 817 A 817
Cdd:PTZ00121 1380 A 1380
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
670-754 |
4.92e-09 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 57.74 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 670 QEKAKKEQEENKRKEALAK--EKERLQTLDEdeydALTAEEKvafdRDVRQALRERKKRElERLAKEMQEKKLQQELERQ 747
Cdd:pfam05672 32 QERLEKEEEERLRKEELRRraEEERARREEE----ARRLEEE----RRREEEERQRKAEE-EAEEREQREQEEQERLQKQ 102
|
....*..
gi 1720427463 748 KEEDELK 754
Cdd:pfam05672 103 KEEAEAK 109
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
667-940 |
6.20e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 667 MKAQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDRDVRQALRE-RKKRELERLAKEMQEKKLQQELE 745
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKaEEAKKADEAKKKAEEAKKADEAK 1489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 746 RQKEE-----DELKRKVKRPKAGPAAKEEPPLKKAQGATNKQLAAVAKIELKMESIERKVSVREHATLEETTRKKKAMTE 820
Cdd:PTZ00121 1490 KKAEEakkkaDEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA 1569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 821 ypllipiSQEQEDSEGDFLKDSDKNLAQKFKIYDMclkdvqnILMYWDRKQGMMVPHTGTDEMSHEADDQRQAPSGGGGR 900
Cdd:PTZ00121 1570 -------KKAEEDKNMALRKAEEAKKAEEARIEEV-------MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1720427463 901 KGRKDRERERLEKERAEKERLEREKAERERLEKlKALEER 940
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK-KAEEDK 1674
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
662-955 |
7.84e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 662 QDYVVMKAQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDAlTAEEKVAFDRDVRQAlrERKKRELERLAKEMQEKKLQ 741
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK-KAEEKKKADEAKKKA--EEDKKKADELKKAAAAKKKA 1420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 742 QELERQKEE----DELKRKV-KRPKAGPAAKEEPPLKKAQGATNKQLAAVAKIELKMESIERKVSVREHATLEETTRK-- 814
Cdd:PTZ00121 1421 DEAKKKAEEkkkaDEAKKKAeEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKad 1500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 815 --KKAMTEYPLLIPISQEQEDSEGDFLKDSDK-------NLAQKFKIYDMcLKDVQNILMYWDRKQGMMVPHTGTDE--M 883
Cdd:PTZ00121 1501 eaKKAAEAKKKADEAKKAEEAKKADEAKKAEEakkadeaKKAEEKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKnmA 1579
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720427463 884 SHEADDQRQAPSGGGGRKGRKDRERERLEKERAEKERLEREKAERERleklKALEERSDVEGEGEEEHEGKK 955
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKK 1647
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
649-940 |
9.67e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 9.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 649 IGSREHIYVINMSQDYVVMKAQEKAKKEQ---EENKRKEALAKEKERLQTLDEDEYdalTAEEKVAFDRDVRQAlrERKK 725
Cdd:PTZ00121 1254 IRKFEEARMAHFARRQAAIKAEEARKADElkkAEEKKKADEAKKAEEKKKADEAKK---KAEEAKKADEAKKKA--EEAK 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 726 RELERLAKEMQEKKLQQELERQKEE---DELKRKVKRPKAGPAAKEEPPlKKAQGATNKQLAAVAKIELKMESIERKVSV 802
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEaaaDEAEAAEEKAEAAEKKKEEAK-KKADAAKKKAEEKKKADEAKKKAEEDKKKA 1407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 803 REHATLEETTRKKKAMTEYpllipiSQEQEDSEGDFLKDSDKNLAQKFKIYDMCLKDVQNILMYWDRKQgmmvphtGTDE 882
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKK------AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK-------KADE 1474
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427463 883 MSHEADDQRQAPSGGGGRKGRKDRERERLEKERAEKERLEREKAERER-LEKLKALEER 940
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkADEAKKAEEA 1533
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
669-817 |
1.06e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 669 AQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDRDVRQALRERKKRELERLAKEMQEKKLQQELERQK 748
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427463 749 EEDELKRkvkrpkagpAAKEEPPLKKAQGATNKQLAAVAKIELKMESIERKVSVREHATLEETTRKKKA 817
Cdd:COG1196 339 LEELEEE---------LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
645-835 |
1.67e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 645 LLKAIGSREHIYVINMSQDYVVMKAQEKAKKEQEENKRKEALAK----EKERLQTLDEDEYDALTAEEKVAFDRDVRQAL 720
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKkaeeDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 721 RERKKRELERLAKEMQEKKlqQELERQKEEDELKRKVK--RPKAGPAAKEEPPLKKAQGATNKQLAAVAKIELKMES-IE 797
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKK--AEEENKIKAEEAKKEAEedKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAvIE 1782
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720427463 798 RKVSVREHATLEETTRKKKAM-----------TEYPLLIPISQEQEDSE 835
Cdd:PTZ00121 1783 EELDEEDEKRRMEVDKKIKDIfdnfaniieggKEGNLVINDSKEMEDSA 1831
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
670-817 |
1.91e-08 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 59.97 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 670 QEKAKK-----EQEENKRKEALAKEKERLqtldEDEydALTAEEKVAFDRDVRQALRERKKR---ELERLAKEMQEKKLQ 741
Cdd:pfam15709 368 LERAEKmreelELEQQRRFEEIRLRKQRL----EEE--RQRQEEEERKQRLQLQAAQERARQqqeEFRRKLQELQRKKQQ 441
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720427463 742 QELERQKEEdelKRKVKrpkagpaaKEEPPLKKAQgatnKQLAAVAKiELKMESIERKVSVREHATLEETTRKKKA 817
Cdd:pfam15709 442 EEAERAEAE---KQRQK--------ELEMQLAEEQ----KRLMEMAE-EERLEYQRQKQEAEEKARLEAEERRQKE 501
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
670-799 |
3.45e-08 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 55.43 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 670 QEKAKKEQEENKRKEAlaKEKERLQtldEDEYDALTAEEKVAFDRDVRQALRERKKRELERLAKEMQEKklQQELERQKE 749
Cdd:pfam05672 22 QAREQREREEQERLEK--EEEERLR---KEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEA--EEREQREQE 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1720427463 750 EDELKRKVKrpkagpaaKEEPPlkKAQGATNKQLAAVAKIELKMES--IERK 799
Cdd:pfam05672 95 EQERLQKQK--------EEAEA--KAREEAERQRQEREKIMQQEEQerLERK 136
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
667-788 |
3.77e-08 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 56.64 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 667 MKAQEKAKKEQEENKRKEALAKE--------KERLQTLDEDEYDALTAEEKVAFDRDVRqaLRERKKRELERLAKE-MQE 737
Cdd:pfam13904 73 QAQKEEREKEEQEAELRKRLAKEkyqewlqrKARQQTKKREESHKQKAAESASKSLAKP--ERKVSQEEAKEVLQEwERK 150
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1720427463 738 KKLQQELERQKEEDELKRKvkrpkagpAAKEEPPLKKAQGATNKQLAAVAK 788
Cdd:pfam13904 151 KLEQQQRKREEEQREQLKK--------EEEEQERKQLAEKAWQKWMKNVKN 193
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
669-817 |
3.85e-08 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 58.90 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 669 AQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDAL--TAEEKVAFDRDVRQAlrerkkrelERLAK----EMQEKKLQQ 742
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKeeAEEERLAELEAKRQA---------EEEAReakaEAEQRAAEL 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720427463 743 ELERQKEEDELKRKVKRPKAGPAAKEEPPLKKA-QGATNKQLAAVAKIElKMESIERKvsVREHATLEETTRKKKA 817
Cdd:COG3064 72 AAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAeAAAAAEKAAAAAEKE-KAEEAKRK--AEEEAKRKAEEERKAA 144
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
659-835 |
9.10e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 57.24 E-value: 9.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 659 NMSQDYVVMKAQEKAKKEQE--ENKRKEALAK----------EKERLQTLDEDEYDaltaEEKVAFDRDVRQALRERKKR 726
Cdd:pfam13868 42 ERRLDEMMEEERERALEEEEekEEERKEERKRyrqeleeqieEREQKRQEEYEEKL----QEREQMDEIVERIQEEDQAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 727 ELERLAKemqEKKLQQELERQKEE-DELKRKVKRpkagpAAKEEpPLKKAQGATNKQLAAVAKIELKMESIERKVSVREH 805
Cdd:pfam13868 118 AEEKLEK---QRQLREEIDEFNEEqAEWKELEKE-----EEREE-DERILEYLKEKAEREEEREAEREEIEEEKEREIAR 188
|
170 180 190
....*....|....*....|....*....|..
gi 1720427463 806 --ATLEETTRKKKAMTEypLLIPISQEQEDSE 835
Cdd:pfam13868 189 lrAQQEKAQDEKAERDE--LRAKLYQEEQERK 218
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
667-828 |
9.59e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.21 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 667 MKAQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDRDvRQALRERKKRELER------LAKEMQEKKL 740
Cdd:pfam17380 419 KVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQ-QEEERKRKKLELEKekrdrkRAEEQRRKIL 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 741 QQELERQKE---EDELKRKV------KRPKAgPAAKEEPPLKKAQGATNKQLAAVAKIELKMESIERKVS-----VREHA 806
Cdd:pfam17380 498 EKELEERKQamiEEERKRKLlekemeERQKA-IYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSrleamERERE 576
|
170 180
....*....|....*....|..
gi 1720427463 807 TLEETTRKKKAMTEYPLLIPIS 828
Cdd:pfam17380 577 MMRQIVESEKARAEYEATTPIT 598
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
668-767 |
9.94e-08 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 54.31 E-value: 9.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEENKRKealaKEKERLQTLDEDEYDAltaEEKVAFDRDVRQALRERKKRELERLAKEMQEKKLQQELERQ 747
Cdd:pfam11600 51 RAKEEARRKKEEEKEL----KEKERREKKEKDEKEK---AEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRI 123
|
90 100
....*....|....*....|.
gi 1720427463 748 K-EEDELKRKVKRPKAGPAAK 767
Cdd:pfam11600 124 KaEKAEITRFLQKPKTQQAPK 144
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
668-942 |
1.06e-07 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 57.35 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDRDVRQALRE-------------RKKRELERLAKE 734
Cdd:pfam15558 38 RRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKesrwreqaedqenQRQEKLERARQE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 735 MQEKKLQQElERQKEEDELKRKvKRPKAGPAAKEepplKKAQGATNKQLAAvakielkMESiERKVSVREHATLEETTRK 814
Cdd:pfam15558 118 AEQRKQCQE-QRLKEKEEELQA-LREQNSLQLQE----RLEEACHKRQLKE-------REE-QKKVQENNLSELLNHQAR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 815 KKAMTeypllipiSQEQEDSEGdfLKDSdknLAQKFkiydmcLKDVQNilmywdRKQGMMVPHTGTDEMSHEADDQRQap 894
Cdd:pfam15558 184 KVLVD--------CQAKAEELL--RRLS---LEQSL------QRSQEN------YEQLVEERHRELREKAQKEEEQFQ-- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720427463 895 sggggrkgrkdrererlekeraeKERLEREKAERERLEKLKALEERSD 942
Cdd:pfam15558 237 -----------------------RAKWRAEEKEEERQEHKEALAELAD 261
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
668-836 |
1.17e-07 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 57.36 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEENKRKEALAKEKERLQTLDEDEYdaltAEEKVAfdrdvrqalreRKKRELERLAKEMQEKKLQQELERQ 747
Cdd:COG3064 19 EQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQ----AEEEAR-----------EAKAEAEQRAAELAAEAAKKLAEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 748 KEEDELKRKVKRPKAGPAAKEEPPLKKAQGATNKQLAAVAKIELKMESiERKVSVREHATLEETTRKKKAMTEYPLLIPI 827
Cdd:COG3064 84 KAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEE-EAKRKAEEERKAAEAEAAAKAEAEAARAAAA 162
|
....*....
gi 1720427463 828 SQEQEDSEG 836
Cdd:COG3064 163 AAAAAAAAA 171
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
674-819 |
1.52e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 57.46 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 674 KKEQEENKRKEALAKEKERLQTLDEDEYDALtaEEKVAFDRdvrQALRERKKRELERLAKEMqEKKLQQELERQKE--ED 751
Cdd:pfam09731 306 LKKREEKHIERALEKQKEELDKLAEELSARL--EEVRAADE---AQLRLEFEREREEIRESY-EEKLRTELERQAEahEE 379
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 752 ELKRKVKRPKAGPAAKEEPPLKKAQgATNK--QLAAVAKIELKMESIERKVSvrEHATLEETTRKKKAMT 819
Cdd:pfam09731 380 HLKDVLVEQEIELQREFLQDIKEKV-EEERagRLLKLNELLANLKGLEKATS--SHSEVEDENRKAQQLW 446
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
667-821 |
1.53e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 56.47 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 667 MKAQEKAKKEQEENKRKEalaKEKERLQTLDEDEYDALTAEEKVAFDRdVRQALRERKKRELERLAKEMQEKKLQQEL-- 744
Cdd:pfam13868 129 REEIDEFNEEQAEWKELE---KEEEREEDERILEYLKEKAEREEEREA-EREEIEEEKEREIARLRAQQEKAQDEKAErd 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 745 --------------ERQKEEDELKRKVKRpkagpaaKEEppLKKAQgatNKQLAAVAK---IELKMESIERKVSVREHAT 807
Cdd:pfam13868 205 elraklyqeeqerkERQKEREEAEKKARQ-------RQE--LQQAR---EEQIELKERrlaEEAEREEEEFERMLRKQAE 272
|
170
....*....|....*....
gi 1720427463 808 LEE-----TTRKKKAMTEY 821
Cdd:pfam13868 273 DEEieqeeAEKRRMKRLEH 291
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
670-820 |
2.32e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 55.70 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 670 QEKAKKEQEENKRKEALAK--EKERLQTLD-EDEYDALTAEEKVAFDRDVRQALRERKKRELERLAKEMQEKKLQQE-LE 745
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEmmEEERERALEeEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEiVE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720427463 746 RQKEEDELKRKVKRPKAgpaakeepplKKAQGATNKQLAavAKIELKMEsiERKVSVREHATLEETTRKKKAMTE 820
Cdd:pfam13868 109 RIQEEDQAEAEEKLEKQ----------RQLREEIDEFNE--EQAEWKEL--EKEEEREEDERILEYLKEKAEREE 169
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
668-985 |
4.71e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEENKRKEALAKEKERLQTLDEDEY--DALTAEEKVAFDrDVRQALRERKKRELERlAKEMQ--EKKLQQE 743
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKadEAKKAEEAKKAD-EAKKAEEKKKADELKK-AEELKkaEEKKKAE 1567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 744 LERQKEED--------ELKRKV--KRPKAGPAAKEEPPLKKAQGATNKQLAAVAKIELKMESIERKVSVREHATLEETTR 813
Cdd:PTZ00121 1568 EAKKAEEDknmalrkaEEAKKAeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 814 KKKAMTEYPLLIPISQEQEDSEgdflKDSDKNLAQKFKiydmclKDVQNilmywDRKQgmmvphtgTDEMSHEADDQRQA 893
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKK----AEEDKKKAEEAK------KAEED-----EKKA--------AEALKKEAEEAKKA 1704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 894 PSGGGGRKGRKDRERERLEKERAEKERLEREKAERERlEKLKALEERSD------VEGEGEEEHEGKKDLGVPFINIQSP 967
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE-DKKKAEEAKKDeeekkkIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
330
....*....|....*...
gi 1720427463 968 DFEGVSWKQALESDKLPK 985
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIK 1801
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
668-756 |
5.63e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.54 E-value: 5.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEENK-----RKEALAKEKERLQ-TLDEDEYDALTAEEKVAFDRDVRQALRERKKRELERLAKE----MQE 737
Cdd:pfam13868 222 KEREEAEKKARQRQelqqaREEQIELKERRLAeEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRElekqIEE 301
|
90
....*....|....*....
gi 1720427463 738 KKLQQELERQKEEDELKRK 756
Cdd:pfam13868 302 REEQRAAEREEELEEGERL 320
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
667-750 |
1.05e-06 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 50.30 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 667 MKAQEKAKKEQE-----ENKRKEALAkEKERLQTLDEDEydaltAEEKVAFDRDVRQALRERKKRELERLAKEMQEKKLQ 741
Cdd:pfam20492 37 EELEEERRQAEEeaerlEQKRQEAEE-EKERLEESAEME-----AEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQ 110
|
....*....
gi 1720427463 742 QELERQKEE 750
Cdd:pfam20492 111 EELEEAREE 119
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
690-835 |
1.39e-06 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 50.81 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 690 KERLQTLDEDEYDALTAEEKvafdrdvRQAlRERKKRE-LERLAKEMQEKKLQQELERQKEEDELKRkvkrpkagpaakE 768
Cdd:pfam05672 1 KPSAGTTDAEEAARILAEKR-------RQA-REQREREeQERLEKEEEERLRKEELRRRAEEERARR------------E 60
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720427463 769 EPPLKKAQgatnkqlaavakielkmesiERKVSVREHATLEETTRKKKAMTEYPLLIPISQEQEDSE 835
Cdd:pfam05672 61 EEARRLEE--------------------ERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAE 107
|
|
| CCDC50_N |
pfam15295 |
Coiled-coil domain-containing protein 50 N-terminus; |
653-748 |
1.41e-06 |
|
Coiled-coil domain-containing protein 50 N-terminus;
Pssm-ID: 464621 [Multi-domain] Cd Length: 126 Bit Score: 50.11 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 653 EHIYVINMSQDYVVMKAQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDrdvRQALRERKKRElERLA 732
Cdd:pfam15295 36 EHHYATNIQRNQLVQNDIRVAKQLQEEEELQAQTLFQRRLAQLEEQDEEIAKEIQEELQRE---AEERRRREEED-EEIA 111
|
90
....*....|....*.
gi 1720427463 733 KEMQEKKLQQElERQK 748
Cdd:pfam15295 112 RQLQERERERE-RRRK 126
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
668-817 |
1.49e-06 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 50.84 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEEnkrkealaKEKERLQTLDEDEydalTAEEKVAFDRDVRQALRERKKRELERLAKEMQEKKlqqelERQ 747
Cdd:pfam11600 1 RRSQKSVQSQEE--------KEKQRLEKDKERL----RRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKK-----EEE 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 748 KEEDELKRKVKRPKAGPAAKEEPPLKKAQgATNKQLAAVAKIELKMESIERKvsvrehaTLEETTRKKKA 817
Cdd:pfam11600 64 KELKEKERREKKEKDEKEKAEKLRLKEEK-RKEKQEALEAKLEEKRKKEEEK-------RLKEEEKRIKA 125
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
655-768 |
1.51e-06 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 50.27 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 655 IYVINMSQDYVVMKAQEKAKK--EQEENKRKEALAKEKERLQTLdEDEYDA----LTAEEkvafdrdvrqalRERKKREL 728
Cdd:smart00935 1 IGVVDVQKILQESPAGKAAQKqlEKEFKKRQAELEKLEKELQKL-KEKLQKdaatLSEAA------------REKKEKEL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1720427463 729 ERLAKEMQEK--KLQQELerQKEEDELKRKVkRPKAGPAAKE 768
Cdd:smart00935 68 QKKVQEFQRKqqKLQQDL--QKRQQEELQKI-LDKINKAIKE 106
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
685-820 |
1.67e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 53.27 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 685 ALAKEKERLQtldEDEYDALTAEEKVAFDRDvRQA--LRERKKRELERLaKEMQEKKLQ-QELERQKEEDELKRKVKRPK 761
Cdd:PRK09510 59 AVVEQYNRQQ---QQQKSAKRAEEQRKKKEQ-QQAeeLQQKQAAEQERL-KQLEKERLAaQEQKKQAEEAAKQAALKQKQ 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 762 AGPAAKEEPPLKKAQG-ATNKQLAAVAKielKMESIERKVSVREHATLEETTRKKKAMTE 820
Cdd:PRK09510 134 AEEAAAKAAAAAKAKAeAEAKRAAAAAK---KAAAEAKKKAEAEAAKKAAAEAKKKAEAE 190
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
669-802 |
1.74e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 53.31 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 669 AQEKAKKEQEENKRKEALAKEKERLQTLDEDEydaltAEEKVAFDRDVRQALRERKKRELERLAKEMQEKKLQQELERQK 748
Cdd:TIGR02794 153 EEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAE-----AEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAER 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1720427463 749 EEDELKRKvkrpKAGPAAKEEPPLKKAQGATNKQLAAVAK-IELKMESIERKVSV 802
Cdd:TIGR02794 228 KADEAELG----DIFGLASGSNAEKQGGARGAAAGSEVDKyAAIIQQAIQQNLYD 278
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
652-759 |
1.93e-06 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 49.49 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 652 REhIYVINMSQDyvvMKAQEKAKKEQEENKRKEALAKEKERLQtldedeydaltaEEKVAFDRDVR-------QALRERK 724
Cdd:pfam13863 6 RE-MFLVQLALD---AKREEIERLEELLKQREEELEKKEQELK------------EDLIKFDKFLKendakrrRALKKAE 69
|
90 100 110
....*....|....*....|....*....|....*.
gi 1720427463 725 KRELERLAKEMQEKKLQQELER-QKEEDELKRKVKR 759
Cdd:pfam13863 70 EETKLKKEKEKEIKKLTAQIEElKSEISKLEEKLEE 105
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
667-820 |
2.47e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 52.61 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 667 MKAQEKAKKEQEENKRKEALA--KEKERLQTLDEDEYDaltaEEKVAFDRDVRQ------ALRERKKRELERLAKEM--- 735
Cdd:pfam13868 60 EEEKEEERKEERKRYRQELEEqiEEREQKRQEEYEEKL----QEREQMDEIVERiqeedqAEAEEKLEKQRQLREEIdef 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 736 -QEKKLQQELERQKEEDELKR-------KVKRPKAGPAAKEEPPLKKAQgATNKQLAAVAKIELKMESIERkvsVREHAT 807
Cdd:pfam13868 136 nEEQAEWKELEKEEEREEDERileylkeKAEREEEREAEREEIEEEKER-EIARLRAQQEKAQDEKAERDE---LRAKLY 211
|
170
....*....|....*
gi 1720427463 808 LEETTRK--KKAMTE 820
Cdd:pfam13868 212 QEEQERKerQKEREE 226
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
668-849 |
2.49e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.89 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAK-------KEQEENKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDRDVRQALRERKKRELERLAKEMQEKKL 740
Cdd:PRK09510 98 AEQERLKqlekerlAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 741 QQELERQKE-EDELKRKVK---RPKAGPAAKeepplKKAQGATNKQLAAVAKIELKMESIERKVSVREHAtleettrKKK 816
Cdd:PRK09510 178 KAAAEAKKKaEAEAAAKAAaeaKKKAEAEAK-----KKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAA-------AAK 245
|
170 180 190
....*....|....*....|....*....|....*
gi 1720427463 817 AMTEYPllipiSQEQEDSEGDFLKDSD--KNLAQK 849
Cdd:PRK09510 246 AAEKAA-----AAKAAAEVDDLFGGLDsgKNAPKT 275
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
669-943 |
3.40e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.95 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 669 AQEKAKKEQEENKR----KEALAKEKERLQTLDEDEYDA---LTAEEKVAFDRDvrQALRER-KKRELERlakemqEKKL 740
Cdd:pfam02029 8 ARERRRRAREERRRqkeeEEPSGQVTESVEPNEHNSYEEdseLKPSGQGGLDEE--EAFLDRtAKREERR------QKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 741 QQELERQKEEDELKRKVKrpKAGPAAKEEPPLKKAQGATNKQLAAVAKIELKMESIERKV-SVREHATLEETTRKKKAMT 819
Cdd:pfam02029 80 QEALERQKEFDPTIADEK--ESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREkEYQENKWSTEVRQAEEEGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 820 EYPLLIPISQEQEdsEGDFLKDSDKNLAQKFKiydmcLKDVQNILMYWDRKQGMMVPHTGT-DEMSHEADDQRQAPSGGG 898
Cdd:pfam02029 158 EEEDKSEEAEEVP--TENFAKEEVKDEKIKKE-----KKVKYESKVFLDQKRGHPEVKSQNgEEEVTKLKVTTKRRQGGL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720427463 899 GRKGRKDRERERLEKERAEKERLEREKAERER----------------LEKLK-ALEERSDV 943
Cdd:pfam02029 231 SQSQEREEEAEVFLEAEQKLEELRRRRQEKESeefeklrqkqqeaeleLEELKkKREERRKL 292
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
675-799 |
4.67e-06 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 48.38 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 675 KEQEENKRKEAlakeKERLQTLDEDEydaltaeekvafdRDVRQALRE--RKKRELERLAKEMQEKKlqQELE-RQKEED 751
Cdd:pfam20492 1 REEAEREKQEL----EERLKQYEEET-------------KKAQEELEEseETAEELEEERRQAEEEA--ERLEqKRQEAE 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1720427463 752 ELKRKVKRPKAgpAAKEEpplkKAQGATnKQLAAVAKIELKMESIERK 799
Cdd:pfam20492 62 EEKERLEESAE--MEAEE----KEQLEA-ELAEAQEEIARLEEEVERK 102
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
670-756 |
6.26e-06 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 48.89 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 670 QEKAKKEQEE--NKRKEALAKEKERLqtldedeydalTAEEKVAFDRDVRQALRERKKREL-ERLAKEMQEKKLQQELER 746
Cdd:pfam15346 17 EEAVAKRVEEelEKRKDEIEAEVERR-----------VEEARKIMEKQVLEELEREREAELeEERRKEEEERKKREELER 85
|
90
....*....|....*
gi 1720427463 747 -----QKEEDELKRK 756
Cdd:pfam15346 86 ileenNRKIEEAQRK 100
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
655-769 |
6.36e-06 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 49.06 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 655 IYVINMsqDYVVMKAQE--KAKK--EQEENKRKEALAKEKERLQTLdEDEYDA----LTAEEkvafdrdvrqalRERKKR 726
Cdd:COG2825 26 IGVVDV--QRILQESPEgkAAQKklEKEFKKRQAELQKLEKELQAL-QEKLQKeaatLSEEE------------RQKKER 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1720427463 727 ELERLAKEMQEK--KLQQELerQKEEDELKRKVkRPKAGPA----AKEE 769
Cdd:COG2825 91 ELQKKQQELQRKqqEAQQDL--QKRQQELLQPI-LEKIQKAikevAKEE 136
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
675-820 |
1.20e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 51.02 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 675 KEQEENKRKEA---LAKEKERLQTLDEDEYDAL-----TAE---EKVAFDRDVRQALRE-----RKKRELERLAKEMQEK 738
Cdd:pfam02029 236 REEEAEVFLEAeqkLEELRRRRQEKESEEFEKLrqkqqEAElelEELKKKREERRKLLEeeeqrRKQEEAERKLREEEEK 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 739 -KLQQELERQKEEDELKRKvKRPKAGPAAKEEP----------------------PLKKAQGATNKQLAA-VAKIELKME 794
Cdd:pfam02029 316 rRMKEEIERRRAEAAEKRQ-KLPEDSSSEGKKPfkcfspkgsslkiteraeflnkSLQKSSSVKKTHPPAvVSKIDSRLE 394
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720427463 795 ----SIER--------KVSVREHATLEETTRKKKAMTE 820
Cdd:pfam02029 395 qytsAIESstkeakptKPAASDLPVPAEGVRNIKSMWE 432
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
662-758 |
1.59e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.92 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 662 QDYVVMKAQEKAK-KEQEENKRKEALAKEKErlqtldEDEYDALTAEEK----VAFDRDVRQALRERKKRELERLAKEMQ 736
Cdd:pfam13868 242 EEQIELKERRLAEeAEREEEEFERMLRKQAE------DEEIEQEEAEKRrmkrLEHRRELEKQIEEREEQRAAEREEELE 315
|
90 100
....*....|....*....|....*
gi 1720427463 737 EKKLQQELERQKE---EDELKRKVK 758
Cdd:pfam13868 316 EGERLREEEAERReriEEERQKKLK 340
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
646-833 |
1.68e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.12 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 646 LKAIGSREHIYVINMS--QDYVVMKAQEKAKKEQEENKRkEALAKEKERLQTLDEDEYDALTaeEKVAFDRDVRQALRER 723
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFplDQYTQLALMEFAKKKSLHGKA-ELLTLRSQLLTLCTPCMPDTYH--ERKQVLEKELKHLREA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 724 KKRELERLAKEMQEKKLQQE-LERQKEEDELKRKVKRPKAgpaakEEPPLKKAQGATNKQlAAVAKIELKMESIE--RKV 800
Cdd:TIGR00618 235 LQQTQQSHAYLTQKREAQEEqLKKQQLLKQLRARIEELRA-----QEAVLEETQERINRA-RKAAPLAAHIKAVTqiEQQ 308
|
170 180 190
....*....|....*....|....*....|....
gi 1720427463 801 SVREHATLEETTRKK-KAMTEYPLLIPISQEQED 833
Cdd:TIGR00618 309 AQRIHTELQSKMRSRaKLLMKRAAHVKQQSSIEE 342
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
671-851 |
1.76e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 671 EKAKKEQEENKRKEALAKEKER-------LQTLDEDEYDALTAEEkVAFDRDVRQALRERKKRELERLAKEMQEKKLQQE 743
Cdd:PTZ00121 1203 EAARKAEEERKAEEARKAEDAKkaeavkkAEEAKKDAEEAKKAEE-ERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 744 LERQKEE----DELKRKVKRPKAGPAAKEEPPLKKAQGATNKQLAAVAKIELKMESIERKVSVREHATLEETTRKKKAmt 819
Cdd:PTZ00121 1282 ELKKAEEkkkaDEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA-- 1359
|
170 180 190
....*....|....*....|....*....|...
gi 1720427463 820 eypllipiSQEQEDSEGDFLKDSD-KNLAQKFK 851
Cdd:PTZ00121 1360 --------EAAEEKAEAAEKKKEEaKKKADAAK 1384
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
668-820 |
2.05e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKeQEENKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDRDVRQALRERKKRELERLAKEMQEKKLQQELERQ 747
Cdd:PRK09510 76 RAEEQRKK-KEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAK 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427463 748 KEEDELKR----KVKRPKAGPAAK-EEPPLKKAQGATNKQLAAVAKIELKMESIER-KVSVREHATLEETTRKKKAMTE 820
Cdd:PRK09510 155 RAAAAAKKaaaeAKKKAEAEAAKKaAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKaAAEAKKKAAAEAKAAAAKAAAE 233
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
671-803 |
2.65e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 671 EKAKKEQEENKRKEALAKEKERLQTL-DEDEYDALTAEEKVAfdrdvrqalrERKKRELERLAKEMQEK--KLQQELERQ 747
Cdd:COG1579 60 EIKRLELEIEEVEARIKKYEEQLGNVrNNKEYEALQKEIESL----------KRRISDLEDEILELMERieELEEELAEL 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720427463 748 KEE-DELKRKVKrpkagpAAKEEppLKKAQGATNKQLAAVAKielKMESIERKVSVR 803
Cdd:COG1579 130 EAElAELEAELE------EKKAE--LDEELAELEAELEELEA---EREELAAKIPPE 175
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
655-768 |
2.80e-05 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 46.42 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 655 IYVINMSQDYVVMKAQEKAKK--EQEENKRKEALAKEKERLQTLdedeYDALTAEEKVAfdrdvrQALRERKKRELERLA 732
Cdd:pfam03938 2 IGYVDMQKILEESPEGKAAQAqlEKKFKKRQAELEAKQKELQKL----YEELQKDGALL------EEEREEKEQELQKKE 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 1720427463 733 KEMQEKKLQQELERQKEEDELKRKVkRPKAGPAAKE 768
Cdd:pfam03938 72 QELQQLQQKAQQELQKKQQELLQPI-QDKINKAIKE 106
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
668-854 |
3.02e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.36 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEenkrKEALAKEKERLQTLDEDEYDALTAEEKVAFDR-DVRQALRERKKRELERLAKEMQ--EKKLQQEL 744
Cdd:pfam02463 196 KLQELKLKEQA----KKALEYYQLKEKLELEEEYLLYLDYLKLNEERiDLLQELLRDEQEEIESSKQEIEkeEEKLAQVL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 745 ERQKEEDELKRKVKRPKAGPAAKEEpplKKAQGATNKQLAAVAKIELKMESIERKVSVREHATLEETTRKKKAmTEYPLL 824
Cdd:pfam02463 272 KENKEEEKEKKLQEEELKLLAKEEE---ELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELE-KELKEL 347
|
170 180 190
....*....|....*....|....*....|
gi 1720427463 825 IPISQEQEDSEGDFLKDSDKNLAQKFKIYD 854
Cdd:pfam02463 348 EIKREAEEEEEEELEKLQEKLEQLEEELLA 377
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
671-755 |
3.81e-05 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 45.68 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 671 EKAKKEQEEN-KRKEALAKEKERLQT----LDEDEYDALTAEEKVAfdrdvRQALRERKKRE-LERLAKEMQEKKLQQEL 744
Cdd:pfam20492 23 KKAQEELEESeETAEELEEERRQAEEeaerLEQKRQEAEEEKERLE-----ESAEMEAEEKEqLEAELAEAQEEIARLEE 97
|
90
....*....|.
gi 1720427463 745 ERQKEEDELKR 755
Cdd:pfam20492 98 EVERKEEEARR 108
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
670-761 |
4.27e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 48.34 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 670 QEKAKKEQEENKRKEALAKEKERLQTlDEDEYDALTAEEKVAFDRDVRQaLRERKKRELERLAKE---MQEKKLQQELER 746
Cdd:cd16269 194 TEKEKEIEAERAKAEAAEQERKLLEE-QQRELEQKLEDQERSYEEHLRQ-LKEKMEEERENLLKEqerALESKLKEQEAL 271
|
90 100
....*....|....*....|
gi 1720427463 747 QKEE-----DELKRKVKRPK 761
Cdd:cd16269 272 LEEGfkeqaELLQEEIRSLK 291
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
666-940 |
5.32e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.05 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 666 VMKAQEKAKKEQEENKRKEA-LAKEKERLQTLDEDEYDALTA----EEKVAFDRDVRQALRERKKR-------ELERLAK 733
Cdd:pfam10174 396 INVLQKKIENLQEQLRDKDKqLAGLKERVKSLQTDSSNTDTAlttlEEALSEKERIIERLKEQRERedrerleELESLKK 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 734 EMQEKK-----LQQEL-ERQKEEDELKRK--------VKRP------------KAGPAAKEEPPLKKAQgatNKQLAAVA 787
Cdd:pfam10174 476 ENKDLKekvsaLQPELtEKESSLIDLKEHasslassgLKKDsklksleiaveqKKEECSKLENQLKKAH---NAEEAVRT 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 788 KIEL--KMESIERKVSV-REHATleettrkkKAMTEYPLLIPISQEQEDSEgdflKDSDKNLAQKFKIYDMCLKD----V 860
Cdd:pfam10174 553 NPEIndRIRLLEQEVARyKEESG--------KAQAEVERLLGILREVENEK----NDKDKKIAELESLTLRQMKEqnkkV 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 861 QNILMywdRKQGMMVPHTGTDEMSHEADDQRQAPSGGGGRKGRKDRERERLEKERAEKERL---EREKAERE------RL 931
Cdd:pfam10174 621 ANIKH---GQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLsstQQSLAEKDghltnlRA 697
|
....*....
gi 1720427463 932 EKLKALEER 940
Cdd:pfam10174 698 ERRKQLEEI 706
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
668-836 |
5.56e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.88 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKA----KkeqEENKRKEALAKEKERLQTldEDEYDALTAEEKVAfDRDVRQALRERKKRELERLAKEMQEKKLQQe 743
Cdd:COG3064 52 QAEEEAreakA---EAEQRAAELAAEAAKKLA--EAEKAAAEAEKKAA-AEKAKAAKEAEAAAAAEKAAAAAEKEKAEE- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 744 lERQKEEDELKRKV--KRPKAGPAAKEEPPLKKAQGATNKQLAAVAKIELKMESIERKVSVREHATLEETTRKKKAMTEY 821
Cdd:COG3064 125 -AKRKAEEEAKRKAeeERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAAL 203
|
170
....*....|....*
gi 1720427463 822 PLLIPISQEQEDSEG 836
Cdd:COG3064 204 AAAAAAAAADAALLA 218
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
668-810 |
8.85e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEE-NKRKEALakekERLQTLDEDEYDALTAEEKVAfdrdvrqalreRKKRELERLAKEMQE-KKLQQELE 745
Cdd:COG4913 631 ERLEALEAELDAlQERREAL----QRLAEYSWDEIDVASAEREIA-----------ELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 746 R-QKEEDELKRKVKRpkagpaakeeppLKKAQGATNKQLAA----VAKIELKMESIERKVSVREHATLEE 810
Cdd:COG4913 696 ElEAELEELEEELDE------------LKGEIGRLEKELEQaeeeLDELQDRLEAAEDLARLELRALLEE 753
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
652-817 |
9.31e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 652 REHIYVINMSQDYVVMKAQEKAKKEQEENKrkEALAKEKERLQTLdEDEYDALTAEEkvafdRDVRQALRERKKRELERL 731
Cdd:COG4913 272 AELEYLRAALRLWFAQRRLELLEAELEELR--AELARLEAELERL-EARLDALREEL-----DELEAQIRGNGGDRLEQL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 732 AKEMQEKKLQQElERQKEEDELKRKVKRpkagpaAKEEPPLKKAQGATNKQLAAVAKIELkmESIERKVSVREHATLEET 811
Cdd:COG4913 344 EREIERLERELE-ERERRRARLEALLAA------LGLPLPASAEEFAALRAEAAALLEAL--EEELEALEEALAEAEAAL 414
|
....*.
gi 1720427463 812 TRKKKA 817
Cdd:COG4913 415 RDLRRE 420
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
714-849 |
9.86e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.28 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 714 RDVRQALRE--RKKRELERLAKEMQEKKLQQELERQKEEDELKRKVKrpKAGPAAKEEpplkkaqgatnkqlAAVAKIEL 791
Cdd:PRK00409 530 RELEQKAEEaeALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ--QAIKEAKKE--------------ADEIIKEL 593
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 792 KMESIERKVSVREHATLEETTRKKKAMTEYPLLIPISQEQEDS--EGDFLKdsDKNLAQK 849
Cdd:PRK00409 594 RQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEElkVGDEVK--YLSLGQK 651
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
669-755 |
1.02e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 45.42 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 669 AQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDRDVRQalRE----RKKRELERLAKEMQEKKLQQE- 743
Cdd:pfam05672 53 EEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQ--KEeaeaKAREEAERQRQEREKIMQQEEq 130
|
90
....*....|....*
gi 1720427463 744 --LERQKEEDE-LKR 755
Cdd:pfam05672 131 erLERKKRIEEiMKR 145
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
670-844 |
1.19e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 670 QEKAKKEQEEN---KRKEALAKEKERLQTLDEDeydaltAEEKVAFDRDVRQALrERKKRELERLAKEMQEkkLQQELER 746
Cdd:COG4372 56 QAREELEQLEEeleQARSELEQLEEELEELNEQ------LQAAQAELAQAQEEL-ESLQEEAEELQEELEE--LQKERQD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 747 -QKEEDELKRKVKRPKAGPAAKEEpPLKKAQGATNKQLAAVAKIELKMESIERKVSVREHATL----EETTRKKKAMTEY 821
Cdd:COG4372 127 lEQQRKQLEAQIAELQSEIAEREE-ELKELEEQLESLQEELAALEQELQALSEAEAEQALDELlkeaNRNAEKEEELAEA 205
|
170 180
....*....|....*....|...
gi 1720427463 822 PLLIPISQEQEDSEGDFLKDSDK 844
Cdd:COG4372 206 EKLIESLPRELAEELLEAKDSLE 228
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
670-804 |
1.27e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 670 QEKAKKEQEENKRKEALAKEKERLQtldeDEYDALTAEEKVAFDRDVRQALRERKKRELERLAKEMQEKKLQQELERQKE 749
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELR----EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 750 E-----DELKRKVKRPKAGPAAKEEPPLKKAQGATNKQLAAVAKIELKMESIERKVSVRE 804
Cdd:COG4717 167 EleaelAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
671-815 |
1.32e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 671 EKAKKEQEENKRK--------EALAKEKERLQTLdEDEYDAL-----TAEEKVAfdrDVRQALRERKKRELERLAKEMQE 737
Cdd:PRK03918 521 EKKAEEYEKLKEKliklkgeiKSLKKELEKLEEL-KKKLAELekkldELEEELA---ELLKELEELGFESVEELEERLKE 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 738 -KKLQQE-LERQKEEDELKRKVKRPKagpaaKEEPPLKKAQGATNKQLAAVAKIELKMESIERKVSVREHATLEETTRKK 815
Cdd:PRK03918 597 lEPFYNEyLELKDAEKELEREEKELK-----KLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLEL 671
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
669-817 |
1.71e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 669 AQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDALTA-EEKVAFDRDVRQALRERKKRELERLAKEMQEKKLQQELERQ 747
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEElEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 748 KEEDELKRKVKRPKAGPAAKEeppLKKAQGATNKQLAAVAKIELKMESIERKVSVREHATLEETTRKKKA 817
Cdd:COG1196 395 AAELAAQLEELEEAEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
667-816 |
1.87e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 667 MKAQEK--AKKEQEENKRKEalaKEKERLQTLDEdeYDALTAEEkvafdRDVRQALR--ERKKRELERLAKEMQEKKLQ- 741
Cdd:PRK03918 178 IERLEKfiKRTENIEELIKE---KEKELEEVLRE--INEISSEL-----PELREELEklEKEVKELEELKEEIEELEKEl 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 742 --------------QELERQ-----KEEDELKRKVKR-PKAGPAAKEEPPLKKAQGATNKQLAAV----AKIELKMESIE 797
Cdd:PRK03918 248 eslegskrkleekiRELEERieelkKEIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIekrlSRLEEEINGIE 327
|
170 180
....*....|....*....|.
gi 1720427463 798 RKVSVREH--ATLEETTRKKK 816
Cdd:PRK03918 328 ERIKELEEkeERLEELKKKLK 348
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
668-835 |
2.13e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEE-NKRKEALAKEKERLQT-LDEDEYDALTAEEKVA-FDRDVRQALRERKKRELERLAKEMQEKKLQQEL 744
Cdd:TIGR02168 698 KALAELRKELEElEEELEQLRKELEELSRqISALRKDLARLEAEVEqLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 745 ERQKEE-DELKRKVKRPKAgpAAKEeppLKKAQGATNKQL----AAVAKIELKMESIERKVSVREhATLEETTRKKKAMT 819
Cdd:TIGR02168 778 AEAEAEiEELEAQIEQLKE--ELKA---LREALDELRAELtllnEEAANLRERLESLERRIAATE-RRLEDLEEQIEELS 851
|
170
....*....|....*.
gi 1720427463 820 EypLLIPISQEQEDSE 835
Cdd:TIGR02168 852 E--DIESLAAEIEELE 865
|
|
| mS26_PET12 |
cd23703 |
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ... |
667-769 |
2.28e-04 |
|
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar proteins; mS26, also known as mitochondrial 37S ribosomal protein PET12, is a component of the mitochondrial small ribosomal subunit (mt-SSU) of Saccharomyces cerevisiae mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. The family also includes a group of uncharacterized proteins from pezizomycotina, which show high sequence similarity with mS26.
Pssm-ID: 467916 [Multi-domain] Cd Length: 179 Bit Score: 44.85 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 667 MKAQEKAKKEQEENKRK---EALAKEKERLQTLDEdeydalTAEEKVAFDRDVRQALRERKKRELERL-----AKEMQEK 738
Cdd:cd23703 45 LSEYQEWKRKMAELRRQnlrEGLRELEERKLKTEE------LRAKRSERKQAERERALNAPEREDERLtlptiESALLGP 118
|
90 100 110
....*....|....*....|....*....|.
gi 1720427463 739 KLQQELERQKEEDELKRKVKRpKAGPAAKEE 769
Cdd:cd23703 119 LMRVRTDPEREERAAKRRANR-EAKELAKKE 148
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
690-820 |
4.31e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 690 KERLQTLDE----DEYD-----ALTAEEKVAFDRDVRQALRERKKRELERLAKEMQEKKLQQELERQKEEDELKRKVKRP 760
Cdd:TIGR02169 153 VERRKIIDEiagvAEFDrkkekALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEK 232
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720427463 761 KAGPAAKEepplkkaqgATNKQLAA----VAKIELKMESIERKVSVREhATLEETTRKKKAMTE 820
Cdd:TIGR02169 233 EALERQKE---------AIERQLASleeeLEKLTEEISELEKRLEEIE-QLLEELNKKIKDLGE 286
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
670-759 |
4.57e-04 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 42.60 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 670 QEKAKKEQEEN-KRKEALAKEKERLQTLDE------DEYDALTAEEKVAfdRDVRQALRERK---KRELERLAKEMQEK- 738
Cdd:pfam20492 12 EERLKQYEEETkKAQEELEESEETAEELEEerrqaeEEAERLEQKRQEA--EEEKERLEESAemeAEEKEQLEAELAEAq 89
|
90 100
....*....|....*....|....*.
gi 1720427463 739 ----KLQQELERQKEE-DELKRKVKR 759
Cdd:pfam20492 90 eeiaRLEEEVERKEEEaRRLQEELEE 115
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
668-862 |
5.11e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDALtaeekvafdrdvrqalreRKKRELERLAKEMQEKKLQQELERQ 747
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL------------------EKLQEKLEQLEEELLAKKKLESERL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 748 KEEDELKRKVKRPKAGP--AAKEEPPLKKAQGATNKQLAAVAKIELKMESiERKVSVREHATLEETTRKKKAMTEyplli 825
Cdd:pfam02463 387 SSAAKLKEEELELKSEEekEAQLLLELARQLEDLLKEEKKEELEILEEEE-ESIELKQGKLTEEKEELEKQELKL----- 460
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720427463 826 pISQEQEDSEGDFLKDSDKNLAQKFKIYDMCLKDVQN 862
Cdd:pfam02463 461 -LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
668-806 |
5.88e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDRDVRQALRERKKRELERLAKEMQEKKLQQELERQ 747
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427463 748 KEEDELKRKVKRpkagpAAKEEPPLKKAQGATNKQLAAVAKIELKMESIERKVSVREHA 806
Cdd:COG1196 446 EAAEEEAELEEE-----EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
664-819 |
6.66e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 664 YVVMK---------AQEKAKKE-QEENKRKEALAKEKErLQTldEDEYDALTAEekvaFDRDVRQALRERKKRELERLAK 733
Cdd:PRK12704 22 YFVRKkiaeakikeAEEEAKRIlEEAKKEAEAIKKEAL-LEA--KEEIHKLRNE----FEKELRERRNELQKLEKRLLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 734 EMQEKKLQQELErqKEEDELKRKVKRPKagpaAKEEPPLKKAQGATNKQlaavAKIELKMESI------ERKVSVREhaT 807
Cdd:PRK12704 95 EENLDRKLELLE--KREEELEKKEKELE----QKQQELEKKEEELEELI----EEQLQELERIsgltaeEAKEILLE--K 162
|
170
....*....|..
gi 1720427463 808 LEETTRKKKAMT 819
Cdd:PRK12704 163 VEEEARHEAAVL 174
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
720-786 |
6.90e-04 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 45.63 E-value: 6.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720427463 720 LRERKKRELERLAKEMQEKKLQQELERQKEEDELKRKVKRPKAgpAAKEEPPLKKAQGATNKQLAAV 786
Cdd:PLN02316 250 LLEEKRRELEKLAKEEAERERQAEEQRRREEEKAAMEADRAQA--KAEVEKRREKLQNLLKKASRSA 314
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
607-849 |
7.04e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.73 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 607 LLIQILAERIQLSNCFRGVVFDGLDTLFARNAPSALHCLLKAIGSREHIYV-INMSQDYVVMKA-----QEKAKKEQEEN 680
Cdd:pfam02463 703 KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEkSRLKKEEKEEEKselslKEKELAEEREK 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 681 KRKEALAKEKERLQTLDEDEYDALTAEEKVAFDRDVRQALRERKKRELERLAKEMQEKKLQQELERQK---------EED 751
Cdd:pfam02463 783 TEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKlaeeelerlEEE 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 752 ELKRKVKRPKagpAAKEEPPLKKAQGATNKQLAAVAKIELKMESIERKVSV----REHATLEETTRKKKAMTEYPLLIPI 827
Cdd:pfam02463 863 ITKEELLQEL---LLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNlleeKENEIEERIKEEAEILLKYEEEPEE 939
|
250 260
....*....|....*....|..
gi 1720427463 828 SQEQEDSEGDFLKDSDKNLAQK 849
Cdd:pfam02463 940 LLLEEADEKEKEENNKEEEEER 961
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
668-855 |
8.20e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEE-NKRKEALAKEKERLQTLDEdEYDALTAE-EKVAFDRDVRQALRERKKRELERLAKEMQEKKLQ-QEL 744
Cdd:COG4372 91 AAQAELAQAQEElESLQEEAEELQEELEELQK-ERQDLEQQrKQLEAQIAELQSEIAEREEELKELEEQLESLQEElAAL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 745 ERQKEEDELKRKVKRPKAGPAAKEEPPLKKAQGATNKQLAAVAKIELKMESIERKVSVREHATLEETTRKKKAMTEYPLL 824
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
170 180 190
....*....|....*....|....*....|.
gi 1720427463 825 IPISQEQEDSEGDFLKDSDKNLAQKFKIYDM 855
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
666-939 |
9.22e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 666 VMKAQEKAKKEQEENKRKEALAKEKERLQTLDEDEyDALTAEEKVAFDrDVRQALRERKKRElerlAKEMQEKKLQQELE 745
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ-AAIKAEEARKAD-ELKKAEEKKKADE----AKKAEEKKKADEAK 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 746 RQKEE----DELKRKVKRPKAgpaaKEEPPLKKAQGATNKQLAAVAKIELKMESIERKVSVREHATLEETTRKKKAmtey 821
Cdd:PTZ00121 1309 KKAEEakkaDEAKKKAEEAKK----KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA---- 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 822 pllipisqeqedsegdflkDSDKNLAQKFKIYDMCLKDVQnilmywdrkqgmmvphtgtdEMSHEADDQRQAPSGgggrk 901
Cdd:PTZ00121 1381 -------------------DAAKKKAEEKKKADEAKKKAE--------------------EDKKKADELKKAAAA----- 1416
|
250 260 270
....*....|....*....|....*....|....*...
gi 1720427463 902 grkdrererleKERAekERLEREKAERERLEKLKALEE 939
Cdd:PTZ00121 1417 -----------KKKA--DEAKKKAEEKKKADEAKKKAE 1441
|
|
| Saf4_Yju2 |
pfam04502 |
Saf4/Yju2 protein; This is a family of eukaryotic proteins that includes CCDC130 and CCDC94 ... |
667-835 |
9.75e-04 |
|
Saf4/Yju2 protein; This is a family of eukaryotic proteins that includes CCDC130 and CCDC94 from humans, Saf4 from fission yeasts and Yju2 from budding yeasts. Saf4 (also known as cwc16) is involved in mRNA splicing where it associates with cdc5 and the other cwf proteins as part of the spliceosome. Yju2 is a splicing factor that is associated with the Prp 19-associated complex and acts after Prp2 in promoting the first catalytic reaction of pre-mRNA splicing.
Pssm-ID: 461333 [Multi-domain] Cd Length: 328 Bit Score: 44.27 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 667 MKAQEK----AKKEQEENKRKEALAKEKERLQTLDedeYDALtaeekvafdRDVRQALR-ERKKRELERLAKE-MQEKKL 740
Cdd:pfam04502 131 MKKLEKrtkdSKREMEALERLEELQELNQRQWKDD---YDAN---------LKLRREFReEKKEREEEEEDEEaLKEKMS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 741 QQELERQKEEDELKRKVKRPKAGPA-AKEEPPLKKAQGATNKQLAAVAKIELKMESIERKVSVREHATLEETTR--KKKA 817
Cdd:pfam04502 199 LEIIKLLPEDEEDDRRAALVEFGSRpLFGDSSPPAKTESPTDSLTSEISASSKRESLKKSLGKLTRKAADPLLLgvKRKK 278
|
170
....*....|....*...
gi 1720427463 818 MTEYPLLIPISQEQEDSE 835
Cdd:pfam04502 279 AATEEPSTPSSETSTESS 296
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
671-758 |
1.01e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 44.20 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 671 EKAKKEQEENKRKEALAKEKERLQTLDEDEYDALTAEEKvAFDRDVRQ------ALRERKKRELER-LAKEMQEKKLQQE 743
Cdd:pfam02841 201 AKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQER-SYQEHVKQliekmeAEREQLLAEQERmLEHKLQEQEELLK 279
|
90
....*....|....*
gi 1720427463 744 LERQKEEDELKRKVK 758
Cdd:pfam02841 280 EGFKTEAESLQKEIQ 294
|
|
| Cgr1 |
pfam03879 |
Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA ... |
673-762 |
1.15e-03 |
|
Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA processing.
Pssm-ID: 427562 [Multi-domain] Cd Length: 107 Bit Score: 41.07 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 673 AKKEQEENKRKEALAKEKErLQtlDEDEydaltaEEKVAfdrdVRQALRERKKRE-----LERLAKEMQEKKLQQelerq 747
Cdd:pfam03879 33 EKRQEKRLELKAIKAKEKE-LK--DEKE------AERQR----RIQAIKERREAKeekerYEELAAKMHAKKVER----- 94
|
90
....*....|....*
gi 1720427463 748 keedeLKRKVKRPKA 762
Cdd:pfam03879 95 -----LKRKEKRNKL 104
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
665-776 |
1.22e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 665 VVMKAQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDALTAEEKVA---FDRDVRQALRERKKrELERLAKEMQEK-KL 740
Cdd:PRK00409 521 LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeAEKEAQQAIKEAKK-EADEIIKELRQLqKG 599
|
90 100 110
....*....|....*....|....*....|....*.
gi 1720427463 741 QQELERQKEEDELKRKVKrpKAGPAAKEEPPLKKAQ 776
Cdd:PRK00409 600 GYASVKAHELIEARKRLN--KANEKKEKKKKKQKEK 633
|
|
| CCDC66 |
pfam15236 |
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
668-751 |
1.29e-03 |
|
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.
Pssm-ID: 434558 [Multi-domain] Cd Length: 154 Bit Score: 42.09 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEENKRKEALAKEKERLQtlDEDEYDALTAEEKVAFDRDVRQALRERKKRElERLAKEMQEKKLQQELErQ 747
Cdd:pfam15236 72 KKLEEERRRQEEQEEEERLRREREEEQ--KQFEEERRKQKEKEEAMTRKTQALLQAMQKA-QELAQRLKQEQRIRELA-E 147
|
....
gi 1720427463 748 KEED 751
Cdd:pfam15236 148 KGHD 151
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
668-854 |
1.34e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEENKRKEALAKEKERLQTlDEDEYDalTAEEKVAFDRDVRQALRERKKRELERLAKEMQEKKLQQELERQ 747
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEELEE-RHELYE--EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 748 KEED---ELKRKVKRPKagpAAKEEppLKKAQG---ATNKQLAAVAKIELKME-SIERKVSVREHATLEETTRK-KKAMT 819
Cdd:PRK03918 409 KITArigELKKEIKELK---KAIEE--LKKAKGkcpVCGRELTEEHRKELLEEyTAELKRIEKELKEIEEKERKlRKELR 483
|
170 180 190
....*....|....*....|....*....|....*
gi 1720427463 820 EypLLIPISQEQEDSEGDFLKDSDKNLAQKFKIYD 854
Cdd:PRK03918 484 E--LEKVLKKESELIKLKELAEQLKELEEKLKKYN 516
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
670-761 |
1.41e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 41.96 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 670 QEKAKKEQ-----EENKRKEALAKEKErlqtldedeydaltAEEkvafdrdvRQALRERKKRELErlaKEMQEKKLQQEL 744
Cdd:pfam15346 75 EERKKREElerilEENNRKIEEAQRKE--------------AEE--------RLAMLEEQRRMKE---ERQRREKEEEER 129
|
90
....*....|....*..
gi 1720427463 745 ERQKEEDELKRKVKRPK 761
Cdd:pfam15346 130 EKREQQKILNKKNSRPK 146
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
668-811 |
1.58e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEE----NKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDRDVRQALRERKKRELERLAkEMQEKKlqQE 743
Cdd:PRK02224 562 EAEEEAEEAREEvaelNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLA-EKRERK--RE 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 744 LERQKEED---ELKRKVKR---------PKAGPAAKEEPPLKKAQGATNKQLAAVAKIELKMESIERKV----SVREHA- 806
Cdd:PRK02224 639 LEAEFDEArieEAREDKERaeeyleqveEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVealeALYDEAe 718
|
....*
gi 1720427463 807 TLEET 811
Cdd:PRK02224 719 ELESM 723
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
672-817 |
1.62e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 42.77 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 672 KAKKEQEEnkrKEALAKEKERLQtldedeydaltaeekvafdrdvRQALRERKKRELERLAKEMQEKKLQQELERQKEED 751
Cdd:pfam13904 62 AAKQRQRQ---KELQAQKEEREK----------------------EEQEAELRKRLAKEKYQEWLQRKARQQTKKREESH 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720427463 752 ELKRKVKRPKAGPAakeePPLKKAQGATNKQLAA--VAKIELKMESIERKVSVREHATLEETTRKKKA 817
Cdd:pfam13904 117 KQKAAESASKSLAK----PERKVSQEEAKEVLQEweRKKLEQQQRKREEEQREQLKKEEEEQERKQLA 180
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
658-820 |
2.03e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 658 INMSQdyvvMKAQEKAKKEQEEnkRKEALAKEKERLQTLDEdEYDALtaeekvafdrdvrQALRERKKRELERLakEMQE 737
Cdd:COG4717 68 LNLKE----LKELEEELKEAEE--KEEEYAELQEELEELEE-ELEEL-------------EAELEELREELEKL--EKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 738 KKLQQELERQKEEDELKRKVKRPKAGPAAKEEppLKKAQGATNKQLAAVAKIELKMESIERKVSVREHATLEETTRKKKA 817
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEE--LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
...
gi 1720427463 818 MTE 820
Cdd:COG4717 204 LQQ 206
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
665-817 |
2.14e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 665 VVMKAQEKAKKEQEENKRKEALAKEKERLQT-LDEDEYDALTAEEKVAFDRDVRQALRERKKRELERLA--KEMQEKKLQ 741
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAeaEEALLEAEA 372
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720427463 742 QELERQKEEDELKRKVKRPKAgpAAKEEppLKKAQGATNKQLAAVAKIE-LKMESIERKVSVREHATLEETTRKKKA 817
Cdd:COG1196 373 ELAEAEEELEELAEELLEALR--AAAEL--AAQLEELEEAEEALLERLErLEEELEELEEALAELEEEEEEEEEALE 445
|
|
| Utp11 |
pfam03998 |
Utp11 protein; This protein is found to be part of a large ribonucleoprotein complex ... |
668-799 |
2.15e-03 |
|
Utp11 protein; This protein is found to be part of a large ribonucleoprotein complex containing the U3 snoRNA. Depletion of the Utp proteins impedes production of the 18S rRNA, indicating that they are part of the active pre-rRNA processing complex. This large RNP complex has been termed the small subunit (SSU) processome.
Pssm-ID: 461122 [Multi-domain] Cd Length: 241 Bit Score: 42.61 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEENKRKEALAKEKERLQTldedeyDALTAEEKVAFDRDVRQALRERKKRELE-RLAKEMQEKKLQQELER 746
Cdd:pfam03998 136 EEVKNFDPAEYFDTDPELLDRRENRLKK------EQLESNSLTAATLKKLDKKKEKLYKELKaRLEREKELKKAEQKLEL 209
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1720427463 747 QKeedELKRKVKRpkagpaakeepplKKAQGATNKQlAAVAKIELkmesiERK 799
Cdd:pfam03998 210 QR---ALMKKGAK-------------KKVKGGTTKK-GPVYKWKK-----ERK 240
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
668-849 |
2.30e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDRDVRQALRERKKRELERLAKEMQEK--KLQQELE 745
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDlsSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 746 RQKEEDELKRKVKRPKAGPAAKEE------------PPLKKAQGATNKQLAAVAKIELKMESIERKVSvREHATLEETTR 813
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEealndlearlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLN-RLTLEKEYLEK 833
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720427463 814 KKKAMTEYPLLIpisQEQEDSEGDFLKDSDKNLAQK 849
Cdd:TIGR02169 834 EIQELQEQRIDL---KEQIKSIEKEIENLNGKKEEL 866
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
660-787 |
2.36e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 660 MSQDYVVMKAQEKAKKEQEeNKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDRDVRQALRERKKRELERLAKEMQEKK 739
Cdd:COG3883 128 ADADADLLEELKADKAELE-AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1720427463 740 LQQELERQKEEDELKRKVKRPKAGPAAKEEPPLKKAQGATNKQLAAVA 787
Cdd:COG3883 207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
697-815 |
2.53e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.32 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 697 DEDEY-DAL--------TAEEKVA---FDRDVR----QALRERKKRELERLAKEMQEKKLQQELERQKEEDELKRKVKRP 760
Cdd:COG2268 181 DENNYlDALgrrkiaeiIRDARIAeaeAERETEiaiaQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETA 260
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 761 KAgpAAKEEPPLKK--AQGATNKQLAAVAK---IELKMESIERKVsvrehATLEETTRKK 815
Cdd:COG2268 261 RA--EAEAAYEIAEanAEREVQRQLEIAERereIELQEKEAEREE-----AELEADVRKP 313
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
670-817 |
3.71e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.01 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 670 QEKAK-KEQEENKRKEALAKEK--ERLQTLDEDEYD-----ALTAEEKVAFDRDVRQALRERKKRELERLAKEMQEKKLQ 741
Cdd:PRK05035 433 QAKAEiRAIEQEKKKAEEAKARfeARQARLEREKAArearhKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGA 512
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720427463 742 QELERQ--KEEDELKRKVKRPKAGPAAKEEPPLKKAQGAtnkqlAAVAKIELKmesieRKVSVREHATLEETTRKKKA 817
Cdd:PRK05035 513 RPDNSAviAAREARKAQARARQAEKQAAAAADPKKAAVA-----AAIARAKAK-----KAAQQAANAEAEEEVDPKKA 580
|
|
| DDRGK |
pfam09756 |
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ... |
674-774 |
3.83e-03 |
|
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.
Pssm-ID: 370664 [Multi-domain] Cd Length: 188 Bit Score: 41.18 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 674 KKEQEENKRKEALaKEKERLQTLDEDEYdaltaEEkvafdrdvrqalrERKKRELERLAKEMQEKKLQQELERQKEEDEL 753
Cdd:pfam09756 1 KKLGAKKRAKLEL-KEAKRQQREAEEEE-----RE-------------EREKLEEKREEEYKEREEREEEAEKEKEEEER 61
|
90 100
....*....|....*....|.
gi 1720427463 754 KRKVKRpkagpAAKEEPPLKK 774
Cdd:pfam09756 62 KQEEEQ-----ERKEQEEYEK 77
|
|
| adk |
PRK00279 |
adenylate kinase; Reviewed |
604-660 |
3.85e-03 |
|
adenylate kinase; Reviewed
Pssm-ID: 234711 [Multi-domain] Cd Length: 215 Bit Score: 41.67 E-value: 3.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427463 604 PDDLLIQILAERIQLSNCFRGVVFDGldtlFARNAP--SALHCLLKAIGsREHIYVINM 660
Cdd:PRK00279 60 PDEIVIGLVKERLAQPDCKNGFLLDG----FPRTIPqaEALDEMLKELG-IKLDAVIEI 113
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
668-759 |
3.95e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDRDVRQALRERKKRELERLAKEMQEKKLQQELERQ 747
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
90 100
....*....|....*....|....*.
gi 1720427463 748 KE--------------EDELKRKVKR 759
Cdd:COG1196 746 ELleeealeelpeppdLEELERELER 771
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
662-849 |
4.02e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 662 QDYVVMKAQEKAKKEQEENKRKEAlakekerlqtldEDEYDALTAEEKVAfdRDVRQALRERK----------KRELERL 731
Cdd:TIGR00618 424 GQLAHAKKQQELQQRYAELCAAAI------------TCTAQCEKLEKIHL--QESAQSLKEREqqlqtkeqihLQETRKK 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 732 AKEMQEKKLQQELERQKEEDELKRKVKRPKAGPAAKEEPPLKKAQGATNKQLAAVAKIELKMESI-ERKVSVREHATLEE 810
Cdd:TIGR00618 490 AVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSErKQRASLKEQMQEIQ 569
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720427463 811 TTRKKKAM--TEYPLLIPISQEQEDsegDFLKDSDKNLAQK 849
Cdd:TIGR00618 570 QSFSILTQcdNRSKEDIPNLQNITV---RLQDLTEKLSEAE 607
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
659-757 |
4.21e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 41.47 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 659 NMSQDYVVMKAQEKAKKEQEEnKRKEAlakEKERLQTLDEdeydaltAEEKVafdrdvrQALRERKKRELERLAKEMQEK 738
Cdd:COG1390 1 MMSLEKIIEEILEEAEAEAEE-ILEEA---EEEAEKILEE-------AEEEA-------EEIKEEILEKAEREAEREKRR 62
|
90 100
....*....|....*....|
gi 1720427463 739 KLQQ-ELERQKEEDELKRKV 757
Cdd:COG1390 63 IISSaELEARKELLEAKEEL 82
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
667-941 |
5.25e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 667 MKAQEKAKKEQEENKRKeaLAKEKERLQTLdedeydaLTAEEKVAFDRDVRQALRERKKrELERLAKEMQEKKlQQELER 746
Cdd:PRK03918 461 LKRIEKELKEIEEKERK--LRKELRELEKV-------LKKESELIKLKELAEQLKELEE-KLKKYNLEELEKK-AEEYEK 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 747 QKEE-DELKRKVKRPKAgpAAKEEPPLKKAQGATNKQLAavaKIELKMESIERKVSVREHATLEETTRK----KKAMTEY 821
Cdd:PRK03918 530 LKEKlIKLKGEIKSLKK--ELEKLEELKKKLAELEKKLD---ELEEELAELLKELEELGFESVEELEERlkelEPFYNEY 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 822 PLLIPISQEQEDSEgDFLKDSDKNLAQKFKIYDMCLKDVQNIlmywdRKQgmmvphtgTDEMSHEADDQRQApsgggGRK 901
Cdd:PRK03918 605 LELKDAEKELEREE-KELKKLEEELDKAFEELAETEKRLEEL-----RKE--------LEELEKKYSEEEYE-----ELR 665
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1720427463 902 GRKDRERERLEKERAEKERLEREKAERER-LEKLKA-LEERS 941
Cdd:PRK03918 666 EEYLELSRELAGLRAELEELEKRREEIKKtLEKLKEeLEERE 707
|
|
| Adk |
COG0563 |
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ... |
604-660 |
5.38e-03 |
|
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440329 [Multi-domain] Cd Length: 212 Bit Score: 41.27 E-value: 5.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427463 604 PDDLLIQILAERIQLSNCFRGVVFDGldtlFARNAPSA--LHCLLKAIGSREHiYVINM 660
Cdd:COG0563 60 PDEIVIGLVKERLAQPDCANGFILDG----FPRTVAQAeaLDELLAELGIKLD-AVIEL 113
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
668-757 |
5.77e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 39.73 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEENKRKEALAKEKerlqtldedeydaltAEEKVAFDRDVRQALRERKKRELERLAKEMQEKKLQQ-ELER 746
Cdd:cd06503 44 KAKEEAEELLAEYEEKLAEARAE---------------AQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEiEQEK 108
|
90
....*....|.
gi 1720427463 747 QKEEDELKRKV 757
Cdd:cd06503 109 EKALAELRKEV 119
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
668-750 |
6.13e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 668 KAQEKAKKEQEENKRKEALAKEKERLQTLDEDEYDALTAEEKVAFDRDVRQALRERKKRELERL----------AKEMQE 737
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaieeYEELEE 795
|
90
....*....|...
gi 1720427463 738 KKlqQELERQKEE 750
Cdd:COG1196 796 RY--DFLSEQRED 806
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
669-757 |
6.48e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 669 AQEKAKKEQEE------NKRKEALAKE----KERLQTLDEDEYDALTAEEKVAFDRDVRQALRERKKRELERLAKEMQE- 737
Cdd:COG1579 71 VEARIKKYEEQlgnvrnNKEYEALQKEieslKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEe 150
|
90 100
....*....|....*....|..
gi 1720427463 738 -KKLQQELER-QKEEDELKRKV 757
Cdd:COG1579 151 lAELEAELEElEAEREELAAKI 172
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
659-892 |
7.19e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 659 NMSQDYVVMKAQEKAKKEQEENKRKEALAK-EKERlqtldeDEYDALTAEEKvafdrDVRQALRERKKRELErlakemQE 737
Cdd:pfam15709 298 SPTQTFVVTGNMESEEERSEEDPSKALLEKrEQEK------ASRDRLRAERA-----EMRRLEVERKRREQE------EQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 738 KKLQQE-LERQKE-EDELKRKVKRpkagpaAKEEPPLKKAQGATNKQlaavakielKMESIERKVSVREHATLEETTRKK 815
Cdd:pfam15709 361 RRLQQEqLERAEKmREELELEQQR------RFEEIRLRKQRLEEERQ---------RQEEEERKQRLQLQAAQERARQQQ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 816 KAMTEYPLLIPISQEQEDSEGdflKDSDKnlaQKFKIYDMCLKDVQNILM---------YWDRKQgmmvphTGTDEMSHE 886
Cdd:pfam15709 426 EEFRRKLQELQRKKQQEEAER---AEAEK---QRQKELEMQLAEEQKRLMemaeeerleYQRQKQ------EAEEKARLE 493
|
....*.
gi 1720427463 887 ADDQRQ 892
Cdd:pfam15709 494 AEERRQ 499
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
662-956 |
9.91e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 662 QDYVVMKAQEKAKKE------------QEENKRKEAL--AKEKERLQTLDEDEyDALTAEE--KVAFDRDVRQALR--ER 723
Cdd:PTZ00121 1085 EDNRADEATEEAFGKaeeakktetgkaEEARKAEEAKkkAEDARKAEEARKAE-DARKAEEarKAEDAKRVEIARKaeDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 724 KKRELERLAKEMQEKKLQQELERQKEEDELKR--KVKRPKAGPAAKEEPPLKKAQGATN-KQLAAVAKI-ELKMESIERK 799
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKaeDARKAEAARKAEEERKAEEARKAEDaKKAEAVKKAeEAKKDAEEAK 1243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427463 800 VSVREHATLEETTRKKKAMTEYPLLIPISQEQEDSEGDFLKDS-DKNLAQKFKIYDMCLKdvqnilmywdrkqgmmvpht 878
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAeEKKKADEAKKAEEKKK-------------------- 1303
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427463 879 gTDEMSHEADDQRQAPSGGGGRKGRKDRERERLEKERAEKERLEREKAERE-RLEKLKALEERSDVEGEGEEEHEGKKD 956
Cdd:PTZ00121 1304 -ADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEaAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
|
| |
