|
Name |
Accession |
Description |
Interval |
E-value |
| CortBP2 |
pfam09727 |
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ... |
36-179 |
6.60e-49 |
|
Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.
Pssm-ID: 462860 [Multi-domain] Cd Length: 187 Bit Score: 172.40 E-value: 6.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 36 LSKSELRMLLSVMEGELEARDLVIEALRARR-KEVFIQERYGRFNLNDPFLALQRDYEAGPG-----DKEKPVCTNPLSI 109
Cdd:pfam09727 2 LSKDDLLKLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDqsqdeDVYEAMYEKPLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 110 LEAVMAHCRKMQERMSAQLVAAESRQKK------------------------------------LEMEKLQLQALEQEHK 153
Cdd:pfam09727 82 LEKLVEKQRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKELK 161
|
170 180
....*....|....*....|....*.
gi 91982738 154 KLAAHLEEERGKNKHVVLMLVKECKQ 179
Cdd:pfam09727 162 KLLEKLEEELSKQKQIALLLVKERKR 187
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
688-959 |
1.15e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 167.05 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 688 LLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNG 767
Cdd:COG0666 41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 768 FTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVD 847
Cdd:COG0666 121 ETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 848 SLKLLMyhrvrAHGnslsseepksglfslnggesptgpskpvvpADlINHADKEGWTAAHIAASKGFKNCLEVLCRHGGL 927
Cdd:COG0666 201 IVKLLL-----EAG------------------------------AD-VNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
|
250 260 270
....*....|....*....|....*....|..
gi 91982738 928 EPERRDKCNRTVHDVATDDCKHLLENLNALKI 959
Cdd:COG0666 245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
666-862 |
8.90e-36 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 138.55 E-value: 8.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 666 RSPGASDSLLVAASGWSPSLTPLLMSGGP---APLAGRPTLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAA 742
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEAGAdvnARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 743 KNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEA 822
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 91982738 823 GTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHRVRAHGN 862
Cdd:COG0666 242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
702-943 |
2.14e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 137.39 E-value: 2.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 702 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFE 781
Cdd:COG0666 22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 782 CIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMyhrvrAHG 861
Cdd:COG0666 102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL-----EAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 862 nslsseepksglfslnggesptgpskpvvpADlINHADKEGWTAAHIAASKGFKNCLEVLCRHGGlEPERRDKCNRTVHD 941
Cdd:COG0666 177 ------------------------------AD-VNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALD 224
|
..
gi 91982738 942 VA 943
Cdd:COG0666 225 LA 226
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
702-837 |
1.75e-24 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 105.42 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 702 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFE 781
Cdd:COG0666 155 TPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 91982738 782 CIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPI 837
Cdd:COG0666 234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
715-953 |
4.79e-23 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 101.18 E-value: 4.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 715 LLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANIN 794
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 795 HSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMyhrvrAHGnslsseepksglf 874
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-----EAG------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 875 slnggesptgpskpvvpADlINHADKEGWTAAHIAASKGFKNCLEVLCRHGGlEPERRDKCNRTVHDVA-----TDDCKH 949
Cdd:COG0666 144 -----------------AD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAaenghLEIVKL 204
|
....
gi 91982738 950 LLEN 953
Cdd:COG0666 205 LLEA 208
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
738-825 |
1.89e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 93.26 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 738 LYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYnANINHSaAGGQTPLYLACKNGNKECIK 817
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78
|
....*...
gi 91982738 818 LLLEAGTD 825
Cdd:pfam12796 79 LLLEKGAD 86
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
704-794 |
1.92e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 87.48 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 704 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNaEARVDAADkNGFTPLCVAAAQGHFECI 783
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|.
gi 91982738 784 ELLTAYNANIN 794
Cdd:pfam12796 78 KLLLEKGADIN 88
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
771-855 |
5.04e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 83.24 E-value: 5.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 771 LCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGtDRSIKTrDGWTPIHAAVDTGNVDSLK 850
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78
|
....*
gi 91982738 851 LLMYH 855
Cdd:pfam12796 79 LLLEK 83
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
703-852 |
8.42e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 78.91 E-value: 8.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 703 LLQQAAAQGNVTLLSM-LLNEEGLDINYSCEDGHSALYSAAKNGHTDC---VRLLLNAEARVDAADKNGFTPL-CVAAAQ 777
Cdd:PHA03095 15 LYDYLLNASNVTVEEVrRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLhLYLYNA 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982738 778 GHFECIELLTAYNANINHSAAGGQTPL--YLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVD--SLKLL 852
Cdd:PHA03095 95 TTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLL 173
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
722-841 |
1.26e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.08 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 722 EEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQ 801
Cdd:PHA02874 112 DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE 191
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 91982738 802 TPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAV 841
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
804-933 |
2.77e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 69.76 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 804 LYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHrvrahgnslsseepksglfslnggespt 883
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 91982738 884 gpskpvVPADLINHadkeGWTAAHIAASKGFKNCLEVLCRHgGLEPERRD 933
Cdd:pfam12796 53 ------ADVNLKDN----GRTALHYAARSGHLEIVKLLLEK-GADINVKD 91
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
707-853 |
1.02e-13 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 76.45 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 707 AAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELL 786
Cdd:PLN03192 532 VASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982738 787 TAYnANINHSAAGGQTpLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLM 853
Cdd:PLN03192 611 YHF-ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
707-856 |
2.22e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 74.26 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 707 AAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELL 786
Cdd:PHA02875 9 AILFGELDIARRLLDI-GINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982738 787 TAYNANINHSA-AGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHR 856
Cdd:PHA02875 88 LDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
711-856 |
4.40e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 73.16 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 711 GNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLNAEARVDAADKngftplcvaaaqghfecIELLTA 788
Cdd:PHA03100 119 NSYSIVEYLLDN-GANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLS 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982738 789 YNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHR 856
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
688-853 |
6.11e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 69.63 E-value: 6.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 688 LLMSGGPAPLAGRPTL---LQQAAAQGNVTLLSMLL--NEEGLDINYscEDGHSALYSAAKNGHTDCVRLLLNAEARVDA 762
Cdd:PHA02875 53 LLMKHGAIPDVKYPDIeseLHDAVEEGDVKAVEELLdlGKFADDVFY--KDGMTPLHLATILKKLDIMKLLIARGADPDI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 763 ADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDG-WTPIHAAV 841
Cdd:PHA02875 131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAI 210
|
170
....*....|..
gi 91982738 842 DTGNVDSLKLLM 853
Cdd:PHA02875 211 ENNKIDIVRLFI 222
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
720-857 |
4.04e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 67.00 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 720 LNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGH-----FECIELLTAYNANIN 794
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVN 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982738 795 HSAAGGQTPLYLA--CKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDS--LKLLMYHRV 857
Cdd:PHA03100 101 APDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGV 167
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
734-786 |
4.07e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 59.60 E-value: 4.07e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 91982738 734 GHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELL 786
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
769-820 |
5.20e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 59.21 E-value: 5.20e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 91982738 769 TPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLL 820
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
702-909 |
8.21e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 66.14 E-value: 8.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 702 TLLQQAAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLL-----------------------LNAEA 758
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKH-GADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 759 RVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIH 838
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 839 AAVDTGNVDSLKLLMyhrvrAHGNSLSSEepksglfsLNGGESPTGPS----KPVVPAdLINHA-----DKEGWTAAHIA 909
Cdd:PHA02874 196 NAAEYGDYACIKLLI-----DHGNHIMNK--------CKNGFTPLHNAiihnRSAIEL-LINNAsindqDIDGSTPLHHA 261
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
122-249 |
1.18e-10 |
|
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: 63.41 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 122 ERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEE--ERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLE 199
Cdd:COG1579 41 AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIE 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 91982738 200 EEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKlsREEA 249
Cdd:COG1579 121 ELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE--REEL 168
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
712-863 |
2.33e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 64.90 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 712 NVTLLSMLL-----NEEGLDINYSCEDGHSALYSaaknghTDCVRLLLNAEARVDAADKN-GFTPLCVAAAQGHFECIEL 785
Cdd:PHA02878 113 NVEIFKIILtnrykNIQTIDLVYIDKKSKDDIIE------AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTEL 186
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982738 786 LTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDT-GNVDSLKLLMYHRVRAHGNS 863
Cdd:PHA02878 187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKS 265
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
276-703 |
3.16e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 65.73 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 276 PGLSLPRKTKDK-RLASISVATEGPVTRSVACQTDVVTESTDP----VKKLPLTVPIKPSTGSPLVPTNTKGNVGPSALL 350
Cdd:PHA03247 2659 GRVSRPRRARRLgRAAQASSPPQRPRRRAARPTVGSLTSLADPppppPTPEPAPHALVSATPLPPGPAAARQASPALPAA 2738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 351 IRPGIDRQSSHSDLGPSPPTALPSSAnrieenGPSTGNAPdlsnstpstpsstapaaaQTPGTAPQNHSQAPTVHSLhSP 430
Cdd:PHA03247 2739 PAPPAVPAGPATPGGPARPARPPTTA------GPPAPAPP------------------AAPAAGPPRRLTRPAVASL-SE 2793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 431 CANTHPglNPRIQAARfrfQGNANDPDQNGNNTQSPPSRDVSPTsrdnlvakqlarnTVTQALSRFTSPQAGASSRLG-- 508
Cdd:PHA03247 2794 SRESLP--SPWDPADP---PAAVLAPAAALPPAASPAGPLPPPT-------------SAQPTAPPPPPGPPPPSLPLGgs 2855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 509 VSPGGDAGTCPPVGRTGLK--TPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQlrasnagakvdnkivasPPSTLPQGTK 586
Cdd:PHA03247 2856 VAPGGDVRRRPPSRSPAAKpaAPARPPVRRLARPAVSRSTESFALPPDQPERP-----------------PQPQAPPPPQ 2918
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 587 VVNEENVPKSSSPQLPPKPSIDLTVAPagcpvsalatsQVGAWPAGTPGLNQPACSDSSLViPATVAFCSSINPVSASSR 666
Cdd:PHA03247 2919 PQPQPPPPPQPQPPPPPPPRPQPPLAP-----------TTDPAGAGEPSGAVPQPWLGALV-PGRVAVPRFRVPQPAPSR 2986
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 91982738 667 SPGAS------DSLLVAASGWSPSLTpLLMSGGPAPLAGRPTL 703
Cdd:PHA03247 2987 EAPASstppltGHSLSRVSSWASSLA-LHEETDPPPVSLKQTL 3028
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
674-764 |
3.75e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 58.20 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 674 LLVAASGWSPSLTPLLMSGGPAPLAGRP---TLLQQAAAQGNVTLLSMLLNEEGLDInysCEDGHSALYSAAKNGHTDCV 750
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKngrTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 91982738 751 RLLLNAEARVDAAD 764
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
22-258 |
5.31e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 22 ATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVfiQERYgrfnlndpFLALQRdyeagpgdkekp 101
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA--QAEE--------YELLAE------------ 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 102 vctnpLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKL----QLQALEQEHKKLAA---HLEEERGKNKHVVLMLV 174
Cdd:COG1196 297 -----LARLEQDIARLEERRRELEERLEELEEELAELEEELEeleeELEELEEELEEAEEeleEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 175 KECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQ---LEKQLSEFDTEREQLRAKLSREEAHT 251
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEleeLEEALAELEEEEEEEEEALEEAAEEE 451
|
....*..
gi 91982738 252 TDLKEEI 258
Cdd:COG1196 452 AELEEEE 458
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
771-860 |
3.09e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 61.84 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 771 LCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLK 850
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
90
....*....|
gi 91982738 851 LLMYHRVRAH 860
Cdd:PTZ00322 166 LLSRHSQCHF 175
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
21-258 |
3.35e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 21 GATAEAAKKEFDvdTLSKSELRMllsvmEGELEARDL--VIEALRARRKEVFIqerygRFNLNDPFLALQRDYEAgpgdK 98
Cdd:COG4913 224 FEAADALVEHFD--DLERAHEAL-----EDAREQIELlePIRELAERYAAARE-----RLAELEYLRAALRLWFA----Q 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 99 EKpvctnpLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEH--------KKLAAHLEEERGKNKHVV 170
Cdd:COG4913 288 RR------LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 171 LMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAH 250
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
|
....*...
gi 91982738 251 TTDLKEEI 258
Cdd:COG4913 442 LLALRDAL 449
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
711-869 |
4.12e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 60.75 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 711 GNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYN 790
Cdd:PHA02874 12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 791 AN-----------------------INHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVD 847
Cdd:PHA02874 92 VDtsilpipciekdmiktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171
|
170 180
....*....|....*....|..
gi 91982738 848 SLKLLMYHRVRAHGNSLSSEEP 869
Cdd:PHA02874 172 IIKLLLEKGAYANVKDNNGESP 193
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
802-852 |
6.53e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.43 E-value: 6.53e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 91982738 802 TPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLL 852
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
702-754 |
1.19e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 1.19e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 91982738 702 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLL 754
Cdd:pfam13637 3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
45-259 |
1.88e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 45 LSVMEGELEA---------RDLVIEALRARRKEVF-IQERYGRFNLNDpFLALQRDYEAGPGDKEKpvctnpLSILEAVM 114
Cdd:COG4717 25 LNVIYGPNEAgkstllafiRAMLLERLEKEADELFkPQGRKPELNLKE-LKELEEELKEAEEKEEE------YAELQEEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 115 AHCRKMQERMSAQLVAAESRQKKLEmEKLQLQALEQEHKKLAAHLEEERGKNKhvvlmlvkeckqlsgKVVEEAQKLEEV 194
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERLE---------------ELEERLEELREL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982738 195 MAQLEEEKKKTSELEEQLSAEKQRSSgmeAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG4717 162 EEELEELEAELAELQEELEELLEQLS---LATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-259 |
2.65e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 110 LEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnkhvVLMLVKECKQLSGKVVEEAQ 189
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE----EYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 190 KLEEVMAQLEEEKKKTSELEEQLSAEKQRssgmEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
111-253 |
2.83e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.03 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 111 EAVMAHCRKMQ---ERMSAQLVAAESRQKKLEMEKlqlQALEQEHKKLAAHLEEERG--KNKHVVLMLVKECK------- 178
Cdd:pfam01576 906 ELLNDRLRKSTlqvEQLTTELAAERSTSQKSESAR---QQLERQNKELKAKLQEMEGtvKSKFKSSIAALEAKiaqleeq 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 179 --------QLSGKVVEEAQK-LEEVMAQLEEEKKKTSELEEQlsAEKqrSSGMEAQLEKQLSEfdTEREQLRA-----KL 244
Cdd:pfam01576 983 leqesrerQAANKLVRRTEKkLKEVLLQVEDERRHADQYKDQ--AEK--GNSRMKQLKRQLEE--AEEEASRAnaarrKL 1056
|
....*....
gi 91982738 245 SREEAHTTD 253
Cdd:pfam01576 1057 QRELDDATE 1065
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
119-259 |
3.75e-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: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 119 KMQERMSAQLVAAEsRQKKLEMEK----------------LQLQALEQEHKKLAAHLEEERGK---NKHVVLMLVKECKQ 179
Cdd:pfam13868 39 KEEERRLDEMMEEE-RERALEEEEekeeerkeerkryrqeLEEQIEEREQKRQEEYEEKLQEReqmDEIVERIQEEDQAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 180 LSGKVVEEAQKLEEVMAQLEE-------EKKKTSELEEQLSA---EKQRssgMEAQLEKQLSEFDTEREQLRAKLSREEA 249
Cdd:pfam13868 118 AEEKLEKQRQLREEIDEFNEEqaewkelEKEEEREEDERILEylkEKAE---REEEREAEREEIEEEKEREIARLRAQQE 194
|
170
....*....|
gi 91982738 250 HTTDLKEEID 259
Cdd:pfam13868 195 KAQDEKAERD 204
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
118-259 |
4.33e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 58.26 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 118 RKMQERMS---AQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnkhvvlmLVKECKQL-------SGKVVEE 187
Cdd:pfam01576 99 KKMQQHIQdleEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK-------LSKERKLLeerisefTSNLAEE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 188 AQKL----------EEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEE 257
Cdd:pfam01576 172 EEKAkslsklknkhEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALAR 251
|
..
gi 91982738 258 ID 259
Cdd:pfam01576 252 LE 253
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
109-257 |
5.79e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 57.21 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 109 ILEAVMAHCRKMQ-ERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEE-----ERGKNKHVVLML-VKECKQLS 181
Cdd:pfam07888 31 LLQNRLEECLQERaELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAElkeelRQSREKHEELEEkYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 182 GKVVEEAQKLeevMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEK----------QLSEFDTEREQLRAKLSREEAHT 251
Cdd:pfam07888 111 EELSEEKDAL---LAQRAAHEARIRELEEDIKTLTQRVLERETELERmkerakkagaQRKEEEAERKQLQAKLQQTEEEL 187
|
....*.
gi 91982738 252 TDLKEE 257
Cdd:pfam07888 188 RSLSKE 193
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
719-832 |
5.98e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 57.34 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 719 LLNEEGLDINYSCEDGHSALYSAAKNGHT-DCVRLLLNAEARVDAADKNGFTPL--CVAAAQGHFECIELLTAYNANINH 795
Cdd:PHA03095 68 LLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNA 147
|
90 100 110
....*....|....*....|....*....|....*....
gi 91982738 796 SAAGGQTPL--YLACKNGNKECIKLLLEAGTDrsIKTRD 832
Cdd:PHA03095 148 LDLYGMTPLavLLKSRNANVELLRLLIDAGAD--VYAVD 184
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-259 |
6.03e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 110 LEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERgknKHVVLMLvkecKQLSGKVVEEAQ 189
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI---ARLEERR----RELEERLEELEE 323
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 190 KLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
785-840 |
7.42e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 50.42 E-value: 7.42e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 91982738 785 LLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAA 840
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
135-258 |
9.22e-08 |
|
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: 52.23 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 135 QKKLEMEKlQLQALEQEHKKLAAHLEEERGKnkhvVLMLVKECKQLSgkvvEEAQKLEEVMAQLEEEKKKtseLEEQlsA 214
Cdd:pfam20492 6 REKQELEE-RLKQYEEETKKAQEELEESEET----AEELEEERRQAE----EEAERLEQKRQEAEEEKER---LEES--A 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 91982738 215 EKQRSSgmEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:pfam20492 72 EMEAEE--KEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEL 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
114-258 |
9.45e-08 |
|
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: 57.37 E-value: 9.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 114 MAHCRKMQERMSAQLVAAEsrqKKLEMEKLQLQALEQEHKKLAAHLEEERGK---NKHVVLMLVKECKQLSGKVVEEAQK 190
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982738 191 LEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKlsREEAhtTDLKEEI 258
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL--RAEL--TLLNEEA 819
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
126-259 |
1.11e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 126 AQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERgknkhvvlmlvKECKQLSGKVVEEAQKLEEVMAQLEEEKKKT 205
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELE-----------AELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 91982738 206 SELEEQLSAEKQRssgmEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG1196 298 ARLEQDIARLEER----RRELEERLEELEEELAELEEELEELEEELEELEEELE 347
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
22-258 |
1.80e-07 |
|
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: 56.22 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 22 ATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVfiQERYGRFNLNDPFLALQRDYEAGPGDKEKP 101
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL--EERIAQLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 102 vctnPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKlqlqaleQEHKKLAAHLEEERGKNKHVVLMLVKECKQLS 181
Cdd:TIGR02168 776 ----ELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-------TLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 182 GKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRA---KLSREEAHTTDLKEEI 258
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRElesKRSELRRELEELREKL 924
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
110-249 |
2.56e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.91 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 110 LEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHvvlmLVKECKQLSgkvvEEAQ 189
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ----AQEELESLQ----EEAE 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 190 KLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEA 249
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
107-259 |
2.67e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 107 LSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQA-LEQEHKKLAAHLEE--ERGKNKHVVLML---------- 173
Cdd:COG4942 57 LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELAELLRAlyRLGRQPPLALLLspedfldavr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 174 --------VKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLS 245
Cdd:COG4942 137 rlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
170
....*....|....
gi 91982738 246 REEAHTTDLKEEID 259
Cdd:COG4942 217 ELQQEAEELEALIA 230
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
719-855 |
3.05e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 54.89 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 719 LLNEEGLDINYSCED-GHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSA 797
Cdd:PHA02878 152 LLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 798 AGGQTPLYLA---CKN------------------------------GNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDT- 843
Cdd:PHA02878 232 KCGNTPLHISvgyCKDydilklllehgvdvnaksyilgltalhssiKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQy 311
|
170
....*....|..
gi 91982738 844 GNVDSLKLLMYH 855
Cdd:PHA02878 312 LCINIGRILISN 323
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
125-258 |
3.36e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 125 SAQLVAAES---RQKKLEMEKLQ--LQALEQEHKKLAAHLEEERGKnkhvvlmLVKECKQLSgkvvEEAQKLEEVMAQLE 199
Cdd:COG4372 22 TGILIAALSeqlRKALFELDKLQeeLEQLREELEQAREELEQLEEE-------LEQARSELE----QLEEELEELNEQLQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 91982738 200 EEKKKTSELEEQLSAEKQRssgmEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:COG4372 91 AAQAELAQAQEELESLQEE----AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-253 |
3.41e-07 |
|
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: 55.45 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 25 EAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEvfiqerygrfnLNDPFLALQRDYEAGPGDKEKpvCT 104
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-----------LEEEIEELQKELYALANEISR--LE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 105 NPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQA----LEQEHKKLAAHLEEERGKnkhvvlmlvkeckql 180
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEkleeLKEELESLEAELEELEAE--------------- 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91982738 181 sgkVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLE---KQLSEFDTEREQLRAKLSREEAHTTD 253
Cdd:TIGR02168 367 ---LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLErleDRRERLQQEIEELLKKLEEAELKELQ 439
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
38-259 |
4.00e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.18 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 38 KSELRMLLSVMEGELEARDLVIEALRARRKEvfIQErygrfNLNDpfLALQRDYEAGPGDKEKpvctnplsiLEAVM--A 115
Cdd:pfam01576 70 KQELEEILHELESRLEEEEERSQQLQNEKKK--MQQ-----HIQD--LEEQLDEEEAARQKLQ---------LEKVTteA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 116 HCRKMQERMsaqLVAAE-----SRQKKL--------------EMEKLQ-LQALEQEHKKLAAHLEEERGKNKHVVLMLVK 175
Cdd:pfam01576 132 KIKKLEEDI---LLLEDqnsklSKERKLleeriseftsnlaeEEEKAKsLSKLKNKHEAMISDLEERLKKEEKGRQELEK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 176 ECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQ----------LEKQLSEFDTEREQLRAKLS 245
Cdd:pfam01576 209 AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQknnalkkireLEAQISELQEDLESERAARN 288
|
250
....*....|....
gi 91982738 246 REEAHTTDLKEEID 259
Cdd:pfam01576 289 KAEKQRRDLGEELE 302
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
20-320 |
4.98e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 20 EGATAEAAKKEFDV---DTLSKSE-LRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGP 95
Cdd:PTZ00121 1532 EAKKADEAKKAEEKkkaDELKKAEeLKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 96 GDK--EKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKL---QLQALEQEHKKLAAHL---EEERGKNK 167
Cdd:PTZ00121 1612 AKKaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaaEEAKKAEEDKKKAEEAkkaEEDEKKAA 1691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 168 HVVLMLVKECK---QLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSgmEAQLE----KQLSEFDTEREQL 240
Cdd:PTZ00121 1692 EALKKEAEEAKkaeELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE--EAKKDeeekKKIAHLKKEEEKK 1769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 241 RAKLSREEAHTtdLKEEIDKmkkmmeqmkkgSDGKPGLSLPRKTKDKR---------------LASISVATEGPVTRSVA 305
Cdd:PTZ00121 1770 AEEIRKEKEAV--IEEELDE-----------EDEKRRMEVDKKIKDIFdnfaniieggkegnlVINDSKEMEDSAIKEVA 1836
|
330
....*....|....*
gi 91982738 306 CQTDVVTESTDPVKK 320
Cdd:PTZ00121 1837 DSKNMQLEEADAFEK 1851
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
107-259 |
5.30e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 107 LSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVE 186
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91982738 187 EAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLE---KQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEelaEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
777-865 |
6.30e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 54.30 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 777 QGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHR 856
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
|
....*....
gi 91982738 857 VRAHGNSLS 865
Cdd:PHA02876 235 SNINKNDLS 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
30-259 |
6.63e-07 |
|
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: 54.30 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 30 EFDVDtlsKSELRMLLSVMEGELEARDLVIEALRAR----RKEVFIQERYgrfnlnDPFLALQRDYEAGPGDKEKPVCTN 105
Cdd:TIGR02169 167 EFDRK---KEKALEELEEVEENIERLDLIIDEKRQQlerlRREREKAERY------QALLKEKREYEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 106 PLSILEAVMAHCRKMQERMSAQLvaaesRQKKLEMEKLqLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVV 185
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEI-----SELEKRLEEI-EQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 186 E---EAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEA-------HTTDLK 255
Cdd:TIGR02169 312 EkerELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKefaetrdELKDYR 391
|
....
gi 91982738 256 EEID 259
Cdd:TIGR02169 392 EKLE 395
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
122-243 |
6.74e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 122 ERMSAQLVA--AESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKhvvlmLVKECKQLSGKVVEEAQKLEEVMAQLE 199
Cdd:PRK04863 490 SRSEAWDVAreLLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAER-----LLAEFCKRLGKNLDDEDELEQLQEELE 564
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 91982738 200 EEKKktsELEEQLSAEKQRSSGMEAQLEkqlsEFDTEREQLRAK 243
Cdd:PRK04863 565 ARLE---SLSESVSEARERRMALRQQLE----QLQARIQRLAAR 601
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-256 |
8.28e-07 |
|
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: 54.29 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 18 DTEGATAEAAKKEFDVDTLsKSELRmllsvmEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEagpgD 97
Cdd:TIGR02168 685 KIEELEEKIAELEKALAEL-RKELE------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL----S 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 98 KEkpvctnpLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEME----KLQLQALEQEHKKLAAHLEEERGKnkhvVLML 173
Cdd:TIGR02168 754 KE-------LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieqlKEELKALREALDELRAELTLLNEE----AANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 174 VKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTD 253
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
...
gi 91982738 254 LKE 256
Cdd:TIGR02168 903 LRE 905
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
121-259 |
9.35e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.87 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 121 QERMSAQLvaaESRQKKLEMEKlqlQALEQEHKKLAAHLEEERG-----KNKHVVLMLV------------KECKQLSGK 183
Cdd:TIGR04523 403 QEKLNQQK---DEQIKKLQQEK---ELLEKEIERLKETIIKNNSeikdlTNQDSVKELIiknldntresleTQLKVLSRS 476
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91982738 184 VVEEAQKLEEVMAQLeeeKKKTSELEEqLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:TIGR04523 477 INKIKQNLEQKQKEL---KSKEKELKK-LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
17-476 |
1.05e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.97 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 17 GDTEGAT-AEAAK--KEFDVDTLSKSELRMLLSVMEG---ELEAR--DLVIEAL--------RARRKEVFIQERygrfnl 80
Cdd:pfam15921 582 GRTAGAMqVEKAQleKEINDRRLELQEFKILKDKKDAkirELEARvsDLELEKVklvnagseRLRAVKDIKQER------ 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 81 nDPFLalqrdyeagpgdKEKPVCTNPLSIL----EAVMAHCRKMQERMsaqlvaaESRQKKLEMeklQLQALEQEHKKLA 156
Cdd:pfam15921 656 -DQLL------------NEVKTSRNELNSLsedyEVLKRNFRNKSEEM-------ETTTNKLKM---QLKSAQSELEQTR 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 157 AHLEEERGKNKHVVLMLVKECKQLSGK------VVEEAQKLEEVMAQ-------LEEEKKKTS---------------EL 208
Cdd:pfam15921 713 NTLKSMEGSDGHAMKVAMGMQKQITAKrgqidaLQSKIQFLEEAMTNankekhfLKEEKNKLSqelstvateknkmagEL 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 209 EEQLSAE---KQRSSGMEAQLEKQLSEF--------DTEREQLRAKLSreeaHTTDLKEeidkmkkmmeqmKKGsdgkPG 277
Cdd:pfam15921 793 EVLRSQErrlKEKVANMEVALDKASLQFaecqdiiqRQEQESVRLKLQ----HTLDVKE------------LQG----PG 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 278 LSLPRKTKDKRLASISVA---TEGPVTRSVAC-----QTDVVTESTDPVKKLP-----LTVPIKPSTGSPLVPTNTKGNV 344
Cdd:pfam15921 853 YTSNSSMKPRLLQPASFTrthSNVPSSQSTASflshhSRKTNALKEDPTRDLKqllqeLRSVINEEPTVQLSKAEDKGRA 932
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 345 GPSALL---IRPGIDRQSSHSDLGPSPPTALPSSANRIEE---NGPSTGNAPDLSNSTPSTPSSTAPAAAqTPGTAPQNH 418
Cdd:pfam15921 933 PSLGALddrVRDCIIESSLRSDICHSSSNSLQTEGSKSSEtcsREPVLLHAGELEDPSSCFTFPSTASPS-VKNSASRSF 1011
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982738 419 SQAPT---VHSLHSPCANTHPGLNPRIQAARfrfqgNANDPDqNGNNTQSPPSRDVSPTSR 476
Cdd:pfam15921 1012 HSSPKkspVHSLLTSSAEGSIGSSSQYRSAK-----TIHSPD-SVKDSQSLPIETTGKTCR 1066
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
136-258 |
1.09e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 136 KKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSae 215
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE-- 83
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 91982738 216 kqrssgmeaQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:COG4372 84 ---------ELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
736-840 |
1.23e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 52.29 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 736 SALYSAAKNGHTDCVRLLL----NAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANIN-HSAAGGQTPLYLACKN 810
Cdd:PHA02884 35 NILYSSIKFHYTDIIDAILklgaDPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLH 114
|
90 100 110
....*....|....*....|....*....|
gi 91982738 811 GNKECIKLLLEAGTDRSIKTRDGWTPIHAA 840
Cdd:PHA02884 115 GCLKCLEILLSYGADINIQTNDMVTPIELA 144
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
110-245 |
1.42e-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: 49.66 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 110 LEAVMaHCRKMQ-ERMSAQLVAAE----SRQKKLEMEKLQLQALEQEHKKLaahlEEERgknkhvvlmlvKECKQLSGKV 184
Cdd:pfam15346 24 VEEEL-EKRKDEiEAEVERRVEEArkimEKQVLEELEREREAELEEERRKE----EEER-----------KKREELERIL 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982738 185 VEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLS 245
Cdd:pfam15346 88 EENNRKIEEAQRKEAEERLAMLEEQRRMKEERQRREKEEEEREKREQQKILNKKNSRPKLS 148
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
146-259 |
1.46e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.94 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 146 QALE-QEHKKLAAHLEEERGKNKHVVLML---VKECKQLSGKV---VEEAQKLEEvmaQLEEEKKKTSELEEQLSaEKQR 218
Cdd:COG2433 380 EALEeLIEKELPEEEPEAEREKEHEERELteeEEEIRRLEEQVerlEAEVEELEA---ELEEKDERIERLERELS-EARS 455
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 91982738 219 SSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG2433 456 EERREIRKDREISRLDREIERLERELEEERERIEELKRKLE 496
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
712-853 |
1.51e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 52.72 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 712 NVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIEL--LT 787
Cdd:PHA03095 166 NVELLRLLI-DAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLL 244
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91982738 788 AYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLM 853
Cdd:PHA03095 245 IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
40-259 |
1.55e-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: 52.23 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 40 ELRMLLSVMEgELEARDLVIEALRARRKEVFIQERygrfnlnDPFLALQRDYEAGpgDKEKPVCTNplsilEAVMAHCRK 119
Cdd:pfam13868 99 EREQMDEIVE-RIQEEDQAEAEEKLEKQRQLREEI-------DEFNEEQAEWKEL--EKEEEREED-----ERILEYLKE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 120 MQERMSAQlvaaESRQKKLEMEKlqlqalEQEHKKLAAHLEEERGKnkhvvlmlvKECK-QLSGKVVEEAQKLEEVMAQL 198
Cdd:pfam13868 164 KAEREEER----EAEREEIEEEK------EREIARLRAQQEKAQDE---------KAERdELRAKLYQEEQERKERQKER 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982738 199 EEEKKK-------TSELEEQLsAEKQRSSGMEAQLEKQLSE-------FDTEREQLRAKLSRE--EAHTTDLKEEID 259
Cdd:pfam13868 225 EEAEKKarqrqelQQAREEQI-ELKERRLAEEAEREEEEFErmlrkqaEDEEIEQEEAEKRRMkrLEHRRELEKQIE 300
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-259 |
1.68e-06 |
|
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: 53.15 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 38 KSELRML---LSVMEGELEArdlVIEALRARRKEVFiQERYGRFNLNDPFLALQRDYEAGPGDKEKPVctnplSILEAVM 114
Cdd:TIGR02169 673 PAELQRLrerLEGLKRELSS---LQSELRRIENRLD-ELSQELSDASRKIGEIEKEIEQLEQEEEKLK-----ERLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 115 AHCRKMQErmsaQLVAAESRQKKLEMEK----LQLQALEQEHKKLAAHLEEERgknkhvvlmlVKECKQLSGKVVEEAQK 190
Cdd:TIGR02169 744 EDLSSLEQ----EIENVKSELKELEARIeeleEDLHKLEEALNDLEARLSHSR----------IPEIQAELSKLEEEVSR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 191 LEEVMAQLEEEKKKTSELEEQLSAEKQ-----------RSSGMEAQLE---KQLSEFDTEREQLRAKLSREEAHTTDLKE 256
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEYLEKEIQelqeqridlkeQIKSIEKEIEnlnGKKEELEEELEELEAALRDLESRLGDLKK 889
|
...
gi 91982738 257 EID 259
Cdd:TIGR02169 890 ERD 892
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
352-649 |
1.84e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.02 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 352 RPGIDRQSSHSDLGPSPPTALPSSANRIEEngPSTGNAPDLSNSTPSTPSSTAPAAAQTPGTAPQNHSQAPTVHSLHSPC 431
Cdd:PHA03247 2597 RPRAPVDDRGDPRGPAPPSPLPPDTHAPDP--PPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAA 2674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 432 ANTHPGLNPRIQAARFRFQGNAN--DPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVTQAlsrftSPQAGASSRLGV 509
Cdd:PHA03247 2675 QASSPPQRPRRRAARPTVGSLTSlaDPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPA-----APAPPAVPAGPA 2749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 510 SPGGDAGTCPPVGRTGLKTPGAARVD------RGNPPPIPPKKPGLSQTPSPPHPqlraSNAGAKVDNKIVASPPSTLPQ 583
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAPPAAPaagpprRLTRPAVASLSESRESLPSPWDP----ADPPAAVLAPAAALPPAASPA 2825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 584 GTkvvneENVPKSSSPQLPPKPSIDL--------TVAPAGcPVSALATSQVGAWPAGTPG------LNQPACSDSSLVIP 649
Cdd:PHA03247 2826 GP-----LPPPTSAQPTAPPPPPGPPppslplggSVAPGG-DVRRRPPSRSPAAKPAAPArppvrrLARPAVSRSTESFA 2899
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
702-841 |
1.92e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 52.76 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 702 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGH-TDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHF 780
Cdd:PHA02876 275 TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRN 354
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982738 781 ECIEL-LTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAV 841
Cdd:PHA02876 355 KDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
702-838 |
2.77e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 51.94 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 702 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAR-----VDAADKNGFTPLCVAAA 776
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAVV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982738 777 QGHFECIELLTAYNAN-INHSAAG-------------GQTPLYLACKNGNKECIKLLLEAGTDrsIKTRDGW--TPIH 838
Cdd:cd22192 99 NQNLNLVRELIARGADvVSPRATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGAD--IRAQDSLgnTVLH 174
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
719-771 |
2.85e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 2.85e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 91982738 719 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPL 771
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
704-803 |
2.94e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.21 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 704 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECI 783
Cdd:PTZ00322 86 LCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
|
90 100
....*....|....*....|
gi 91982738 784 ELLTAYnaNINHSAAGGQTP 803
Cdd:PTZ00322 165 QLLSRH--SQCHFELGANAK 182
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
118-290 |
3.57e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 118 RKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKhvvLMLVKECKQLSGKVVEEAQKLEEVMAQ 197
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE---AEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 198 LEEEKKKTSELEEQLSAEKQRSSGME--AQLEKQLSEFDTEREQLR----AKLSREEAHTTD-LKEEIDKMKKMMEQMKK 270
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKkadeAKKKAEEAKKADeAKKKAEEAKKAEEAKKK 1465
|
170 180
....*....|....*....|
gi 91982738 271 GSDGKPGLSLPRKTKDKRLA 290
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKA 1485
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
118-242 |
3.57e-06 |
|
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: 52.05 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 118 RKMQ-ERMSAQlvAAESRQKKLEMEKLQ--LQALEQEHKKLaahLEEERGKNKHVVL-------MLVKECKQLSGKVVEE 187
Cdd:pfam17380 458 RQQQvERLRQQ--EEERKRKKLELEKEKrdRKRAEEQRRKI---LEKELEERKQAMIeeerkrkLLEKEMEERQKAIYEE 532
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91982738 188 AQKLEEvmaqlEEEKKKTSELEEQ---------LSAEKQRSSGMEAQLE--KQLSEFDTEREQLRA 242
Cdd:pfam17380 533 ERRREA-----EEERRKQQEMEERrriqeqmrkATEERSRLEAMEREREmmRQIVESEKARAEYEA 593
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
105-249 |
4.68e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 49.44 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 105 NPLSILEAVMahcRKMQErmsaQLVAAES-------RQKKLEMeklQLQALEQEHKKLaahleEERgknkhVVLMLVKEC 177
Cdd:COG1842 23 DPEKMLDQAI---RDMEE----DLVEARQalaqviaNQKRLER---QLEELEAEAEKW-----EEK-----ARLALEKGR 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982738 178 KQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQrssgmeaQLEKQLSEFDTEREQLRAKLSREEA 249
Cdd:COG1842 83 EDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALR-------QLESKLEELKAKKDTLKARAKAAKA 147
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
122-258 |
4.73e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.65 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 122 ERMsaqLVAAESRQKKLEMEKLQLQ-ALEQEHKKLAaHLEEE-----RGKNKHVVLMLVKeckqlsgkVVEEAQKLEEVM 195
Cdd:pfam05483 193 EKM---ILAFEELRVQAENARLEMHfKLKEDHEKIQ-HLEEEykkeiNDKEKQVSLLLIQ--------ITEKENKMKDLT 260
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982738 196 AQLEEEKKKTSELEEQlsaEKQRSSGMEAQLEKQlSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:pfam05483 261 FLLEESRDKANQLEEK---TKLQDENLKELIEKK-DHLTKELEDIKMSLQRSMSTQKALEEDL 319
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
120-259 |
5.33e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 120 MQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHvvlmLVKECKQLSGKVVEEAQKLEEVMAQLE 199
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ----LEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982738 200 EEKKKTSELE---EQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG4372 105 SLQEEAEELQeelEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
135-249 |
5.48e-06 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 47.19 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 135 QKKLEMEKLQLQALEQEHKKLaahleeergKNKHVVLML----VKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEE 210
Cdd:pfam18595 1 SSTLAEEKEELAELERKAREL---------QAKIDALQVvekdLRSCIKLLEEIEAELAKLEEAKKKLKELRDALEEKEI 71
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 91982738 211 QLSAEKQRssgmEAQLEKQLS--EFDTEREQLRAKLSREEA 249
Cdd:pfam18595 72 ELRELERR----EERLQRQLEnaQEKLERLREQAEEKREAA 108
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
116-259 |
6.58e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 116 HCRKMQERMSAQLVAAESRQKKL--EMEKLQLQALEQEHK---KL------AAHLEEERGKNKHVVLMLVKECKQLSGKV 184
Cdd:pfam05483 524 NCKKQEERMLKQIENLEEKEMNLrdELESVREEFIQKGDEvkcKLdkseenARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 185 VEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLE-------------------KQLSEFDTEREQLRAKLS 245
Cdd:pfam05483 604 ENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAsakqkfeeiidnyqkeiedKKISEEKLLEEVEKAKAI 683
|
170
....*....|....
gi 91982738 246 REEAhtTDLKEEID 259
Cdd:pfam05483 684 ADEA--VKLQKEID 695
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
144-243 |
7.10e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.11 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 144 QLQALEQEHKKLaahleEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKktsELEEQLSAEKQRSSGME 223
Cdd:COG3096 513 RLQQLRAQLAEL-----EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLE---ELEEQAAEAVEQRSELR 584
|
90 100
....*....|....*....|
gi 91982738 224 AQLEkqlsEFDTEREQLRAK 243
Cdd:COG3096 585 QQLE----QLRARIKELAAR 600
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
39-259 |
7.26e-06 |
|
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: 51.21 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 39 SELRMLLSVMEGELEARDLVIEALRARRKEvfIQERYGRFN-----LNDPFLALQRDYEAgpgdkekpvctnplsiLEAV 113
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKA--LREALDELRaeltlLNEEAANLRERLES----------------LERR 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 114 MAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnKHVVLMLVKECKQlsgKVVEEAQKLEE 193
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-LEEALALLRSELE---ELSEELRELES 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 194 VMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSE---------------FDTEREQLRAKLSReeahttdLKEEI 258
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeysltleeaealenkIEDDEEEARRRLKR-------LENKI 981
|
.
gi 91982738 259 D 259
Cdd:TIGR02168 982 K 982
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
742-820 |
8.52e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 50.67 E-value: 8.52e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982738 742 AKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLL 820
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
118-256 |
9.35e-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: 46.45 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 118 RKMQE---RMSAQLVAAESRQKKLEMEklqLQALEQEhkklAAHLEEERgknkhvvlmlvkeckqlsgkvveeaQKLEEV 194
Cdd:pfam20492 16 KQYEEetkKAQEELEESEETAEELEEE---RRQAEEE----AERLEQKR-------------------------QEAEEE 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982738 195 MAQLEEEKKKTSELEEQLSAEKqrssgMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKE 256
Cdd:pfam20492 64 KERLEESAEMEAEEKEQLEAEL-----AEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
25-257 |
1.02e-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: 50.74 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 25 EAAKKEFDVDTLSKSELRMLLsvMEGELEARDLVIEALRARRKEvfiQERYGRFNLNDPFLALQRDYEAGPGDKEKpvct 104
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDL--EELKLQELKLKEQAKKALEYY---QLKEKLELEEEYLLYLDYLKLNEERIDLL---- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 105 npLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLsgkv 184
Cdd:pfam02463 243 --QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL---- 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982738 185 veeaQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQlsEFDTEREQLRAKLSREEAHTTDLKEE 257
Cdd:pfam02463 317 ----KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEE--EEELEKLQEKLEQLEEELLAKKKLES 383
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
118-258 |
1.04e-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: 49.53 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 118 RKMQERMSAQLvaAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKH-VVLMLVKECKQLsgkvVEEAQKLEEVMA 196
Cdd:pfam13868 183 EREIARLRAQQ--EKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKArQRQELQQAREEQ----IELKERRLAEEA 256
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982738 197 QLEEE-----KKKTSELE--EQLSAEKQR------SSGMEAQLEKQLSEFDTEREQLR---AKLSREEAHTTDLKEEI 258
Cdd:pfam13868 257 EREEEefermLRKQAEDEeiEQEEAEKRRmkrlehRRELEKQIEEREEQRAAEREEELeegERLREEEAERRERIEEE 334
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
703-916 |
1.05e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 50.05 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 703 LLQQAAAQGNVTLLSMLLNEEGLD-------------INYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFT 769
Cdd:PHA02946 28 MLQAIEPSGNYHILHAYCGIKGLDerfveellhrgysPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 770 PLCVAAAQGH--FECIELLTAYNANINHSA-AGGQTPLyLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHaavdtgnv 846
Cdd:PHA02946 108 PLYYLSGTDDevIERINLLVQYGAKINNSVdEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH-------- 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982738 847 dslkllmyhrvrahgNSLSSEEPKSGLFS--LNGGESPTGPskpvvpadlinhaDKEGWTAAHIAASKGFKN 916
Cdd:PHA02946 179 ---------------RHLMSDNPKASTISwmMKLGISPSKP-------------DHDGNTPLHIVCSKTVKN 222
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
121-258 |
1.05e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.56 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 121 QERMSA---QLVAAESRQKKLEMEklqLQALEQEHKKLAAH---LEEERgknkHVVLMLVKECKQLSGKVVEEAQKLEEV 194
Cdd:pfam01576 4 EEEMQAkeeELQKVKERQQKAESE---LKELEKKHQQLCEEknaLQEQL----QAETELCAEAEEMRARLAARKQELEEI 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982738 195 M----AQLEEEKKKTSeleeQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:pfam01576 77 LheleSRLEEEEERSQ----QLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDI 140
|
|
| APG6_N |
pfam17675 |
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ... |
117-244 |
1.29e-05 |
|
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.
Pssm-ID: 465452 [Multi-domain] Cd Length: 127 Bit Score: 46.05 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 117 CRKMQERMSAQLVAAES-RQ------KKLEMEKL-QLQALEQEHKKLaaHLEEERgknkhvvlmLVKECKQLSgkvvEEA 188
Cdd:pfam17675 7 TDLLLEELDKQLEDAEKeRDayisflKKLEKETPeELEELEKELEKL--EKEEEE---------LLQELEELE----KER 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 91982738 189 QKLEEVMAQLEEEKKKTSELEEQLSAEkqrssgmEAQLEKQLSEFDTEREQLRAKL 244
Cdd:pfam17675 72 EELDAELEALEEELEALDEEEEEFWRE-------YNALQLQLLEFQDERDSLEAQY 120
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
131-258 |
1.47e-05 |
|
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: 50.07 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 131 AESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKhvvlmlvKECKQLSGKVVEEAQKLEEVMAQLEEekkktseLEE 210
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIE-------NRLDELSQELSDASRKIGEIEKEIEQ-------LEQ 730
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 91982738 211 QLSAEKQRSsgmeAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:TIGR02169 731 EEEKLKERL----EELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
118-253 |
1.49e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.75 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 118 RKMQERMSAQLVAAESRQKKLEM----EKLQLQAlEQEHKKLAAHLEEergKNKHVVLM---------LVKECKQLSGKV 184
Cdd:COG1340 143 KELEKELEKAKKALEKNEKLKELraelKELRKEA-EEIHKKIKELAEE---AQELHEEMielykeadeLRKEADELHKEI 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982738 185 VEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSsgMEAQLEKQLSEFDTEREQLRAKLSREEAHTTD 253
Cdd:COG1340 219 VEAQEKADELHEEIIELQKELRELRKELKKLRKKQ--RALKREKEKEELEEKAEEIFEKLKKGEKLTTE 285
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
18-255 |
1.55e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.72 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 18 DTEGATAEAAKK-EFDvdtlsKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGPG 96
Cdd:pfam05483 162 ETCARSAEKTKKyEYE-----REETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEIN 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 97 DKEKPVCTNPLSILEAVmahcRKMQErmsAQLVAAESRQKKLEME---KLQLQALEQEHKK---LAAHLEE-----ERGK 165
Cdd:pfam05483 237 DKEKQVSLLLIQITEKE----NKMKD---LTFLLEESRDKANQLEektKLQDENLKELIEKkdhLTKELEDikmslQRSM 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 166 NKHVVLmlvKECKQLSGKVVeeAQKLEEVMAQLEEEKK--------------KTSELEEQLSAEKQRSSGMEAQLE---K 228
Cdd:pfam05483 310 STQKAL---EEDLQIATKTI--CQLTEEKEAQMEELNKakaahsfvvtefeaTTCSLEELLRTEQQRLEKNEDQLKiitM 384
|
250 260
....*....|....*....|....*..
gi 91982738 229 QLSEFDTEREQLRAKLSREEAHTTDLK 255
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELK 411
|
|
| PRK11331 |
PRK11331 |
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional |
1071-1357 |
1.87e-05 |
|
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
Pssm-ID: 183088 [Multi-domain] Cd Length: 459 Bit Score: 49.31 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 1071 EQVLALLSGPQEGCLSSVTYASMIPLQMLQNYLRLVEQYHNVIFHGPEGSLQDYIANQLAlcmkYRQMAAGFPCEIVRAE 1150
Cdd:PRK11331 156 KSVIPPMSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLA----YLLTGEKAPQRVNMVQ 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 1151 VDSGFSKEQLV-------------DVFIRNACLiPVKQFPvKKKIIVILENLEKSSLSELLGDFLAPLEN----RSTESP 1213
Cdd:PRK11331 232 FHQSYSYEDFIqgyrpngvgfrrkDGIFYNFCQ-QAKEQP-EKKYVFIIDEINRANLSKVFGEVMMLMEHdkrgENWSVP 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 1214 CTFQKGNgtSECYYFHENCFLVGTI--AKACLQGSDLLVQQHFRWVqlrwDCEPiqGLLQRFLRRKVVSKfrGQLPAPCD 1291
Cdd:PRK11331 310 LTYSEND--EERFYVPENVYIIGLMntADRSLAVVDYALRRRFSFI----DIEP--GFDTPQFRNFLLNK--KAEPSFVE 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982738 1292 PVCKIVDwalsvwrQLNSCLARLGTpeaLLGPKY-----FLSCPVVPGHAQATvKWMSKLWNAVIAPRVQE 1357
Cdd:PRK11331 380 SLCQKMN-------ELNQEISKEAT---ILGKGFrighsYFCCGLEDGTSPDT-QWLKEIVMTDIAPLLEE 439
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
800-825 |
1.87e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 42.96 E-value: 1.87e-05
10 20
....*....|....*....|....*.
gi 91982738 800 GQTPLYLACKNGNKECIKLLLEAGTD 825
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
18-260 |
2.14e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.33 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 18 DTEGATAEAAKKEFDVDTLSKSELRMLLSV---MEGELEARDlvieALRARRKEvFIQERygrfnlNDPFLALQRDYE-A 93
Cdd:pfam05483 507 EASDMTLELKKHQEDIINCKKQEERMLKQIenlEEKEMNLRD----ELESVREE-FIQKG------DEVKCKLDKSEEnA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 94 GPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLE----MEKLQLQALEQEHKKLAAHLEEERGKNKHV 169
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgsAENKQLNAYEIKVNKLELELASAKQKFEEI 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 170 VLMLVKECK-------QLSGKV------VEEAQKLE------------EVMAQLEEEKKKTSELEEQLSAE-------KQ 217
Cdd:pfam05483 656 IDNYQKEIEdkkiseeKLLEEVekakaiADEAVKLQkeidkrcqhkiaEMVALMEKHKHQYDKIIEERDSElglyknkEQ 735
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 91982738 218 RSSGMEAQLEKQLSEFDTEREQLRAKLSREeahttdlKEEIDK 260
Cdd:pfam05483 736 EQSSAKAALEIELSNIKAELLSLKKQLEIE-------KEEKEK 771
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
124-256 |
2.19e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 48.92 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 124 MSAQLVAAESRQKklemeklqLQALEQEHKKLAAHLEEErgknkhvvlmlvkeckqlsgkvveEAQKLEEVMAQLEEEKK 203
Cdd:pfam05622 271 LAAEIMPAEIREK--------LIRLQHENKMLRLGQEGS------------------------YRERLTELQQLLEDANR 318
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 91982738 204 KTSELEEQLSAEKQRSSGMEAQLE---KQLSEFDTERE---QLRAKLsreEAHTTDLKE 256
Cdd:pfam05622 319 RKNELETQNRLANQRILELQQQVEelqKALQEQGSKAEdssLLKQKL---EEHLEKLHE 374
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
22-244 |
2.25e-05 |
|
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: 49.28 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 22 ATAEAAKKEFDVDTL--SKSELRMLLSVMEGELEArdLVIEALRARRKEVFIQERygRFNLNDPFLALQRDYEAgpgDKE 99
Cdd:TIGR02168 258 LTAELQELEEKLEELrlEVSELEEEIEELQKELYA--LANEISRLEQQKQILRER--LANLERQLEELEAQLEE---LES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 100 KPVC--------TNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQA----LEQEHKKLAA---------- 157
Cdd:TIGR02168 331 KLDElaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaqLELQIASLNNeierlearle 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 158 HLEEERGKNKHVVLMLVKecKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRssgmEAQLEKQLSEFDTER 237
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQEELERLEEALEELREE----LEEAEQALDAAEREL 484
|
....*..
gi 91982738 238 EQLRAKL 244
Cdd:TIGR02168 485 AQLQARL 491
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
752-807 |
2.26e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 2.26e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 91982738 752 LLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLA 807
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
126-257 |
2.78e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 126 AQLVAAESRQKKLEmEKLQLQALEQEHKKL--AAHLEEERgknkhvvlMLVKECKQLSgKVVEEAQKLEEVMAQLEEEKK 203
Cdd:COG4717 347 EELQELLREAEELE-EELQLEELEQEIAALlaEAGVEDEE--------ELRAALEQAE-EYQELKEELEELEEQLEELLG 416
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 91982738 204 KTSELEEQLSAEKQRSsgMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEE 257
Cdd:COG4717 417 ELEELLEALDEEELEE--ELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
154-259 |
3.04e-05 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 45.08 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 154 KLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAqLEEEKKKTS----ELEEQLSAEKQRSSGMEAQLEKQ 229
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSKQYNSLEQKESQAKE-LEAEVKKLEealkKLKAELSEEKQKEKEKQSELDDL 79
|
90 100 110
....*....|....*....|....*....|...
gi 91982738 230 L---SEFDTEREQLRAKLsreEAHTTDLKEEID 259
Cdd:pfam04871 80 LlllGDLEEKVEKYKARL---KELGEEVLSDDE 109
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
414-712 |
3.06e-05 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 48.76 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 414 APQNHSQAPTVHSLHSPCANTHPGL----------------NPRIQAArfrfqgNANDPDQNGNNTQSPPSRDvSPTSRD 477
Cdd:pfam05109 424 APESTTTSPTLNTTGFAAPNTTTGLpssthvptnltapastGPTVSTA------DVTSPTPAGTTSGASPVTP-SPSPRD 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 478 NlvAKQLARNTVTQALSRFTSPQAGASSRL-GVSPGGDAGTCPPVGRTglkTPGAArvdrgnpppippkkpglSQTPSP- 555
Cdd:pfam05109 497 N--GTESKAPDMTSPTSAVTTPTPNATSPTpAVTTPTPNATSPTLGKT---SPTSA-----------------VTTPTPn 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 556 ---PHPQLRASNAGAKVDNKIVASPPSTL----PQGTKVVNEENVPKSSSPQ--LPPKPSIDLTVAPAGCPVSALATSQV 626
Cdd:pfam05109 555 atsPTPAVTTPTPNATIPTLGKTSPTSAVttptPNATSPTVGETSPQANTTNhtLGGTSSTPVVTSPPKNATSAVTTGQH 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 627 GAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVAASGWSpslTPLLMSGGPAPlagRPTLLQQ 706
Cdd:pfam05109 635 NITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTS---THHVSTSSPAP---RPGTTSQ 708
|
....*.
gi 91982738 707 AAAQGN 712
Cdd:pfam05109 709 ASGPGN 714
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
704-841 |
3.39e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 48.54 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 704 LQQAAAQGNVTLLSMLLNEEGLDInyscEDGHSALYSAAKNGHtDCVRLLLNAEARVDAADKN--------------GFT 769
Cdd:TIGR00870 56 LFVAAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYV-DAVEAILLHLLAAFRKSGPlelandqytseftpGIT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 770 PLCVAAAQGHFECIELLTAYNANINHSAAG--------------GQTPLYLACKNGNKECIKLLLEAGTDrsIKTRD--G 833
Cdd:TIGR00870 131 ALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPAD--ILTADslG 208
|
....*...
gi 91982738 834 WTPIHAAV 841
Cdd:TIGR00870 209 NTLLHLLV 216
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
48-246 |
3.53e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 48 MEGELEARDLVIEALRARRKEVFIQERYGRFNLNDpflaLQRDYEAGPGDKEKPVCTN-----PLSILEAVMAHcrkMQE 122
Cdd:pfam01576 775 LELDLKELEAQIDAANKGREEAVKQLKKLQAQMKD----LQRELEEARASRDEILAQSkesekKLKNLEAELLQ---LQE 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 123 rmsaQLVAAESRQKKLEMEKLQLQ-----------ALEQEHKKLAA---HLEEERGKNKHVVLML-------VKECKQLS 181
Cdd:pfam01576 848 ----DLAASERARRQAQQERDELAdeiasgasgksALQDEKRRLEAriaQLEEELEEEQSNTELLndrlrksTLQVEQLT 923
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982738 182 GKVVEE---AQKLEEVMAQLE----EEKKKTSELEEQLSAeKQRSS--GMEA---QLEKQLSEFDTEReQLRAKLSR 246
Cdd:pfam01576 924 TELAAErstSQKSESARQQLErqnkELKAKLQEMEGTVKS-KFKSSiaALEAkiaQLEEQLEQESRER-QAANKLVR 998
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
40-245 |
3.88e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.14 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 40 ELRMLLSVME---GELEA--------RDLVIEALRARRKE---------VFIQERYGRFNLNDPFLALQRDYEAGPGDKE 99
Cdd:pfam19220 7 LLRVRLGEMAdrlEDLRSlkadfsqlIEPIEAILRELPQAksrlleleaLLAQERAAYGKLRRELAGLTRRLSAAEGELE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 100 KPVC-----TNPLSILEAVMAHCRKMQERMSAQLVAAEsRQKKLEMEklQLQALEQEHK----------KLAAHLEEERG 164
Cdd:pfam19220 87 ELVArlaklEAALREAEAAKEELRIELRDKTAQAEALE-RQLAAETE--QNRALEEENKalreeaqaaeKALQRAEGELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 165 KNKHVVLMLVKECKQL-------SGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTER 237
Cdd:pfam19220 164 TARERLALLEQENRRLqalseeqAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAER 243
|
....*...
gi 91982738 238 EQLRAKLS 245
Cdd:pfam19220 244 ASLRMKLE 251
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
24-259 |
5.04e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 24 AEAAKKEFDVdtlsKSELRMLLSVMEGELEARDL--VIEALRArrkevfIQERYGRFNLNDpflaLQRDYEAGPGDKEKp 101
Cdd:PRK03918 469 KEIEEKERKL----RKELRELEKVLKKESELIKLkeLAEQLKE------LEEKLKKYNLEE----LEKKAEEYEKLKEK- 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 102 vctnplsileavMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEE----------------ERGK 165
Cdd:PRK03918 534 ------------LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesveeleerlkelEPFY 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 166 NKHVVLM--------LVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEK-QRSSGMEAQLEKQLSEFDTE 236
Cdd:PRK03918 602 NEYLELKdaekelerEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAE 681
|
250 260
....*....|....*....|...
gi 91982738 237 REQLRAKLSREEAHTTDLKEEID 259
Cdd:PRK03918 682 LEELEKRREEIKKTLEKLKEELE 704
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
121-244 |
5.59e-05 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 44.55 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 121 QERMSAQLVAAESRQKKLeMEKLQLQAleqehkKLAAHLEE--ERGKNKHVvlmlvkeckqlsgkvvEEAQKLEEVMAQL 198
Cdd:pfam07926 10 IKRLKEEAADAEAQLQKL-QEDLEKQA------EIAREAQQnyERELVLHA----------------EDIKALQALREEL 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 91982738 199 EEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKL 244
Cdd:pfam07926 67 NELKAEIAELKAEAESAKAELEESEESWEEQKKELEKELSELEKRI 112
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
110-259 |
6.31e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 110 LEAVMAHCRKMQERMsaqlvaaESRQKKLEMEKLQLQALEQEHKKLaahlEEERGKNKHVVlmlvkecKQLSGKVVEEAQ 189
Cdd:COG4372 89 LQAAQAELAQAQEEL-------ESLQEEAEELQEELEELQKERQDL----EQQRKQLEAQI-------AELQSEIAEREE 150
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 190 KLEEVMAQLEEEKKKTSELEEQLSAEKQRSSgmEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG4372 151 ELKELEEQLESLQEELAALEQELQALSEAEA--EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAE 218
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
105-249 |
6.36e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 45.83 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 105 NPLSILEAvmaHCRKMQERM------SAQLVAaesRQKKLEMEklqLQALEQEHKKLaahleEERGKnkhvvLMLVKECK 178
Cdd:pfam04012 22 DPEKMLEQ---AIRDMQSELvkarqaLAQTIA---RQKQLERR---LEQQTEQAKKL-----EEKAQ-----AALTKGNE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982738 179 QLSGKVVEEAQKLEEVMAQLEEEkkktseleeqlsAEKQRSsgMEAQLEKQLSEFDTEREQLRAK----LSREEA 249
Cdd:pfam04012 83 ELAREALAEKKSLEKQAEALETQ------------LAQQRS--AVEQLRKQLAALETKIQQLKAKknllKARLKA 143
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
126-259 |
7.38e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 126 AQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGknkhvvlmlvkeckqlSGKVVEEAQKLEEVMAQLEEEKKKT 205
Cdd:COG4913 624 EELAEAEERLEALEAELDALQERREALQRLAEYSWDEID----------------VASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 91982738 206 SELEEQLsaekqrssgmeAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG4913 688 AALEEQL-----------EELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
129-257 |
7.95e-05 |
|
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: 45.06 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 129 VAAESRQKKLEMEKLQLQAlEQEHKKLAAHLEEERGKNKHvvlmLVKECKQLSGKVVEEAQ-KLEEVMAQLEEEKKKTSE 207
Cdd:pfam11600 2 RSQKSVQSQEEKEKQRLEK-DKERLRRQLKLEAEKEEKER----LKEEAKAEKERAKEEARrKKEEEKELKEKERREKKE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 91982738 208 LEEQLSAEKQRSSgMEAQLEKQlsefdterEQLRAKLS--REEAHTTDLKEE 257
Cdd:pfam11600 77 KDEKEKAEKLRLK-EEKRKEKQ--------EALEAKLEekRKKEEEKRLKEE 119
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
40-246 |
8.04e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 40 ELRMLLSVMEGELEARD--LVI---EALRARRKEVfIQERYgrfnlndpflALQRDYEAGPGDKEKPVCTNPLSILEAVM 114
Cdd:pfam07888 5 ELVTLEEESHGEEGGTDmlLVVpraELLQNRLEEC-LQERA----------ELLQAQEAANRQREKEKERYKRDREQWER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 115 AHcRKMQERMS-AQLVAAESRQKKLEMEKLQ--LQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKL 191
Cdd:pfam07888 74 QR-RELESRVAeLKEELRQSREKHEELEEKYkeLSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982738 192 EEV-------MAQL--EEEKKKTSELEEQLSAEKQRSSGMEAQ-LEKQLSEFDTEREQLRAKLSR 246
Cdd:pfam07888 153 ERMkerakkaGAQRkeEEAERKQLQAKLQQTEEELRSLSKEFQeLRNSLAQRDTQVLQLQDTITT 217
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
800-831 |
1.02e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.74 E-value: 1.02e-04
10 20 30
....*....|....*....|....*....|...
gi 91982738 800 GQTPLYLAC-KNGNKECIKLLLEAGTDRSIKTR 831
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
186-249 |
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: 44.26 E-value: 1.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982738 186 EEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTERE---QLRAKLSREEA 249
Cdd:pfam05672 40 EERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREqeeQERLQKQKEEA 106
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
703-771 |
1.06e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 47.17 E-value: 1.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 703 LLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAAD-KNGFTPL 771
Cdd:PLN03192 625 LLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSPT 693
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
119-256 |
1.11e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 119 KMQ---ERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAhlEEERGKnkhvvLMLVKECKQLSgkvvEEAQKLEEvm 195
Cdd:pfam01576 437 KLQselESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ--EETRQK-----LNLSTRLRQLE----DERNSLQE-- 503
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982738 196 aQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTeREQLRAKLSRE-EAHTTDLKE 256
Cdd:pfam01576 504 -QLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-LEEGKKRLQRElEALTQQLEE 563
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
118-232 |
1.17e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 118 RKMQERMSA----QLVAAE-SRQKKLEMEKLQLQAlEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLsgKVVEEAQKLE 192
Cdd:PRK09510 81 RKKKEQQQAeelqQKQAAEqERLKQLEKERLAAQE-QKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA--KAEAEAKRAA 157
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 91982738 193 EVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSE 232
Cdd:PRK09510 158 AAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAA 197
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
719-795 |
1.42e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 46.20 E-value: 1.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982738 719 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINH 795
Cdd:PHA03100 177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
137-258 |
1.50e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 137 KLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGK--VVEEAQK---------------LEEVMAQLE 199
Cdd:TIGR04523 198 KLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKttEISNTQTqlnqlkdeqnkikkqLSEKQKELE 277
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982738 200 EEKKKTSELEEQLSA--------EKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:TIGR04523 278 QNNKKIKELEKQLNQlkseisdlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQI 344
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-259 |
1.53e-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: 46.59 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 110 LEAVMAHCRKMQERMSAQLVAAES-RQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnkhvVLMLVKECKQLSGKVVEEA 188
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEKAERyKELKAELRELELALLVLRLEELREELEELQEE----LKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982738 189 QKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEkqlsEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ----ILRERLANLERQLEELEAQLEELESKLD 333
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
129-246 |
1.58e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 129 VAAESRQKKLEMEKLqLQAlEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVveeaQKLEEVMAQLEEEKKKTSEL 208
Cdd:PRK03918 170 VIKEIKRRIERLEKF-IKR-TENIEELIKEKEKELEEVLREINEISSELPELREEL----EKLEKEVKELEELKEEIEEL 243
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 91982738 209 EEQLSAEKQRSSGMEA---QLEKQLSEFDTEREQLRAKLSR 246
Cdd:PRK03918 244 EKELESLEGSKRKLEEkirELEERIEELKKEIEELEEKVKE 284
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
833-921 |
1.69e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.72 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 833 GWTPIHAAVDTGNVDSLKLLMYHRVRahgnslsseepksglfslnggesptgpskpvvpadlINHADKEGWTAAHIAASK 912
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGAD------------------------------------INAVDGNGETALHFAASN 44
|
....*....
gi 91982738 913 GFKNCLEVL 921
Cdd:pfam13637 45 GNVEVLKLL 53
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
180-259 |
1.78e-04 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 46.29 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 180 LSGKVVEEAQ---------------KLEEVMAQLEEEKKKTSELEEQLSAEKQRssgmeaqLEKQLSEFDTEREQLRAKL 244
Cdd:COG1193 497 LPEEIIERARellgeesidveklieELERERRELEEEREEAERLREELEKLREE-------LEEKLEELEEEKEEILEKA 569
|
90
....*....|....*..
gi 91982738 245 sREEAHT--TDLKEEID 259
Cdd:COG1193 570 -REEAEEilREARKEAE 585
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
126-244 |
1.82e-04 |
|
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 42.21 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 126 AQLVAAESRQKKLEMEKLQLQALEQEHKKLaahLEEergknkhvvLMLVKE---CKQLSGKV-VEeaQKLEEVMAQLEEE 201
Cdd:pfam01920 2 NKFQQLQQQLQLLAQQIKQLETQLKELELA---LEE---------LELLDEdtkVYKLIGDVlVK--QDKEEVKEQLEER 67
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 91982738 202 KKKtseLEEQLSAekqrssgMEAQLEKQLSEFDTEREQLRAKL 244
Cdd:pfam01920 68 KET---LEKEIKT-------LEKQLEKLEKELEELKEELYKKF 100
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-259 |
1.87e-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: 46.59 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 132 ESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGK-NKHVVLMLVKEckqlsgKVVEEAQK----LEEVMAQLEEEKKKTS 206
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKlEELRLEVSELE------EEIEELQKelyaLANEISRLEQQKQILR 308
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 91982738 207 ELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
118-258 |
2.03e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 118 RKMQERMSAQLVAAE--------SRQKKLEMEKLQLQALE--QEH-----KKLAAHLEEERGKNKHVVL---MLVKECKQ 179
Cdd:pfam05483 424 KKQFEKIAEELKGKEqelifllqAREKEIHDLEIQLTAIKtsEEHylkevEDLKTELEKEKLKNIELTAhcdKLLLENKE 503
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982738 180 LSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEV 582
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
173-259 |
2.10e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 173 LVKECKQLSGkvvEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLsREEAH-- 250
Cdd:PRK00409 503 IIEEAKKLIG---EDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA-EKEAQqa 578
|
....*....
gi 91982738 251 TTDLKEEID 259
Cdd:PRK00409 579 IKEAKKEAD 587
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
121-258 |
2.33e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 121 QERMSAQLVAAESRQKKLEmEKLQLQALEQEHKKLAA---HLEEERgKNKHVVLM-------LVKECKQLSGKVVEEAQK 190
Cdd:PRK03918 134 QGEIDAILESDESREKVVR-QILGLDDYENAYKNLGEvikEIKRRI-ERLEKFIKrtenieeLIKEKEKELEEVLREINE 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982738 191 LEEVMAQLEEEKKKTSELEEQLSAEKQRSsgmeAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEELKEEI----EELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
703-938 |
2.43e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 45.82 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 703 LLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFEC 782
Cdd:PHA02876 148 LIKERIQQDELLIAEMLL-EGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 783 IELLTAYNANINHSaaggQTPLYLACKNGNKECIKLLLEAGTdrSIKTRDGW--TPIHAAVDTGNVDSLKLLMYHR-VRA 859
Cdd:PHA02876 227 IKAIIDNRSNINKN----DLSLLKAIRNEDLETSLLLYDAGF--SVNSIDDCknTPLHHASQAPSLSRLVPKLLERgADV 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982738 860 HGNSLSSEEPKSgLFSLNGGESPTGPSKPVVPADlINHADKEGWTAAHIAASKGFKNCLEVLCRHGGLEPERRDKCNRT 938
Cdd:PHA02876 301 NAKNIKGETPLY-LMAKNGYDTENIRTLIMLGAD-VNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKT 377
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
109-259 |
2.54e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 109 ILEAVMAHCRKMQERMS--AQLVAAESR------QKKLEMEKLQLQALEQEHKKLAAH---LEEERGKNKHVVLMLVKEC 177
Cdd:COG4913 253 LLEPIRELAERYAAARErlAELEYLRAAlrlwfaQRRLELLEAELEELRAELARLEAElerLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 178 KQLSGKVVEEAQK-LEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQ-------LSEFDTEREQLRAKLSREEA 249
Cdd:COG4913 333 RGNGGDRLEQLEReIERLERELEERERRRARLEALLAALGLPLPASAEEFAALraeaaalLEALEEELEALEEALAEAEA 412
|
170
....*....|
gi 91982738 250 HTTDLKEEID 259
Cdd:COG4913 413 ALRDLRRELR 422
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
766-794 |
2.67e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.49 E-value: 2.67e-04
10 20
....*....|....*....|....*....
gi 91982738 766 NGFTPLCVAAAQGHFECIELLTAYNANIN 794
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
363-714 |
2.68e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 363 DLGPSPPTALPssanrieenGPSTGNAPDlsnstpstpsstapaaaqtPGTAPQNHSQAPTVHSLHSPCANTHPGLNPRI 442
Cdd:PHA03247 2486 ARFPFAAGAAP---------DPGGGGPPD-------------------PDAPPAPSRLAPAILPDEPVGEPVHPRMLTWI 2537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 443 QAARFRFQGNANDPDQNGNNTQSPPSRDVS-PTSRdnlvakQLARNTVTQALSRFTSPQAGASSRLGVSPGGDAG----- 516
Cdd:PHA03247 2538 RGLEELASDDAGDPPPPLPPAAPPAAPDRSvPPPR------PAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGdprgp 2611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 517 ---TCPPVGRTGLKTPGAARVDRGNPPPippkkpGLSQTPSPPHPQLRASNAGAKV------DNKIVASPPSTLPQGTK- 586
Cdd:PHA03247 2612 appSPLPPDTHAPDPPPPSPSPAANEPD------PHPPPTVPPPERPRDDPAPGRVsrprraRRLGRAAQASSPPQRPRr 2685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 587 ------VVNEENVPKSSSPQLPPKPSIDLTVApaGCPVSALATSQVGAWPAgTPGLNQPACSDSSLVIPATVAfcssINP 660
Cdd:PHA03247 2686 raarptVGSLTSLADPPPPPPTPEPAPHALVS--ATPLPPGPAAARQASPA-LPAAPAPPAVPAGPATPGGPA----RPA 2758
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 91982738 661 VSASSRSPGASDSLLVAASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVT 714
Cdd:PHA03247 2759 RPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVL 2812
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
122-248 |
2.69e-04 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 43.90 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 122 ERMSAQLVAAESRQKklEMEKLQLQALEQEHKKLAAHLEE-ERGKNKhvvlmLVKECKQLSGkVVEEAQKLEEVMaqlee 200
Cdd:pfam05010 49 EKTIAQMIEEKQKQK--ELEHAEIQKVLEEKDQALADLNSvEKSFSD-----LFKRYEKQKE-VISGYKKNEESL----- 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 91982738 201 eKKKTSELEEQLSAEKQRSSGMEAQLEKQL-----------SEFDTEREQLRAKLSREE 248
Cdd:pfam05010 116 -KKCAQDYLARIKKEEQRYQALKAHAEEKLdqaneeiaqvrSKAKAETAALQASLRKEQ 173
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
132-249 |
2.80e-04 |
|
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: 45.33 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 132 ESRQKKLEMEK---LQLQAlEQEHkklaAHLEEERGKNKHVVLMLVKECKQLSgKVVEEAQKLEEVMAQLEEEKKKTSEL 208
Cdd:pfam15709 398 EERQRQEEEERkqrLQLQA-AQER----ARQQQEEFRRKLQELQRKKQQEEAE-RAEAEKQRQKELEMQLAEEQKRLMEM 471
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 91982738 209 EEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEA 249
Cdd:pfam15709 472 AEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEA 512
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
121-242 |
2.94e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 121 QERMSAQLVAAESRQKKLEMEKlQLQALEQEHKKLAAHLEEERgkNKHVVLMLVKECkqlSGKVVEEAQKLEEVMAQLEE 200
Cdd:PRK04863 565 ARLESLSESVSEARERRMALRQ-QLEQLQARIQRLAARAPAWL--AAQDALARLREQ---SGEEFEDSQDVTEYMQQLLE 638
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 91982738 201 EKKKTSELEEQLSAEKQRssgMEAQLEKqLSEFDT-EREQLRA 242
Cdd:PRK04863 639 RERELTVERDELAARKQA---LDEEIER-LSQPGGsEDPRLNA 677
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
125-258 |
3.91e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 125 SAQLVAAESRQKK-LEMEKLQLQALEQEhKKLAAHLEEERGKNKHVvlmlvKECKQLSgkvvEEAQKLEEVMAQLEEE-K 202
Cdd:PRK12704 30 EAKIKEAEEEAKRiLEEAKKEAEAIKKE-ALLEAKEEIHKLRNEFE-----KELRERR----NELQKLEKRLLQKEENlD 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982738 203 KKTSEL---EEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKL------SREEAhttdlKEEI 258
Cdd:PRK12704 100 RKLELLekrEEELEKKEKELEQKQQELEKKEEELEELIEEQLQELerisglTAEEA-----KEIL 159
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
326-702 |
3.92e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 326 PIKPSTGSP-LVPTNTKGNVGPSALL--IRpGIDRQSSHSDLGPSP---PTALPSSANRieeNGPSTGNAPDLSNSTPST 399
Cdd:PHA03247 2509 PPAPSRLAPaILPDEPVGEPVHPRMLtwIR-GLEELASDDAGDPPPplpPAAPPAAPDR---SVPPPRPAPRPSEPAVTS 2584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 400 PSSTAPAAAQ-TPGTAPQNHSQAPTVHSLHSPCA-NTH----PGLNPRIQAARFRFQGNANDPDQNGNNTQSPPSRdVSP 473
Cdd:PHA03247 2585 RARRPDAPPQsARPRAPVDDRGDPRGPAPPSPLPpDTHapdpPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGR-VSR 2663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 474 TSRdnlvAKQLARNTVTQALSRFTSPQAgasSRLGVSPGGDAGTCPPVGRT----------GLKTPGAARVDRGNPPPIP 543
Cdd:PHA03247 2664 PRR----ARRLGRAAQASSPPQRPRRRA---ARPTVGSLTSLADPPPPPPTpepaphalvsATPLPPGPAAARQASPALP 2736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 544 PK-----KPGLSQTP----SPPHPQLRASNAGAKVDNKIVASPPSTLPQGTKVVNEENVPKSSSPQLPPKPSidltvAPA 614
Cdd:PHA03247 2737 AApappaVPAGPATPggpaRPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPP-----AAV 2811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 615 GCPVSALATSQVGAWPAGTPGLNQPAC-SDSSLVIPATVAFCSSINPVSASSRSPGASDSLLVAASGWSPSLTPLlmsgg 693
Cdd:PHA03247 2812 LAPAAALPPAASPAGPLPPPTSAQPTApPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRL----- 2886
|
....*....
gi 91982738 694 PAPLAGRPT 702
Cdd:PHA03247 2887 ARPAVSRST 2895
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
733-765 |
4.06e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.19 E-value: 4.06e-04
10 20 30
....*....|....*....|....*....|....
gi 91982738 733 DGHSALYSAA-KNGHTDCVRLLLNAEARVDAADK 765
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
118-258 |
4.08e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 118 RKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnkhvvlmlVKECKQLSGKVVEEAQKLEEVMAQ 197
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEK--------IRELEERIEELKKEIEELEEKVKE 284
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982738 198 LEEEKKKT------SELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEaHTTDLKEEI 258
Cdd:PRK03918 285 LKELKEKAeeyiklSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKEL 350
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
110-244 |
4.45e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 110 LEAVMAHCRKMQERMSAQlvAAESRQKKLEMEKlQLQALEQEHKKLAA-----HLEEERgknkhvvlmLVKECKQlSGKV 184
Cdd:COG3096 555 LEELLAELEAQLEELEEQ--AAEAVEQRSELRQ-QLEQLRARIKELAArapawLAAQDA---------LERLREQ-SGEA 621
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982738 185 VEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRssgMEAQLEkQLS----EFDTEREQLRAKL 244
Cdd:COG3096 622 LADSQEVTAAMQQLLEREREATVERDELAARKQA---LESQIE-RLSqpggAEDPRLLALAERL 681
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
313-695 |
4.48e-04 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 44.91 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 313 ESTDPVKKLPLTVPIKPSTGSPL-----VPTN--TKGNVGPS---ALLIRPGIDRQSShsdlGPSPPTALPSSanriEEN 382
Cdd:pfam05109 426 ESTTTSPTLNTTGFAAPNTTTGLpssthVPTNltAPASTGPTvstADVTSPTPAGTTS----GASPVTPSPSP----RDN 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 383 GpSTGNAPDLSNSTPSTPSSTAPAAAQTPG-TAPQNHSQAPTVHSLHSPCANTHPglNPriqaarfrfqgnandpdqngn 461
Cdd:pfam05109 498 G-TESKAPDMTSPTSAVTTPTPNATSPTPAvTTPTPNATSPTLGKTSPTSAVTTP--TP--------------------- 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 462 NTQSPPSRDVSPTSrdNLVAKQLARNTVTQALsrfTSPQAGASSrlgvspggdagtcPPVGRTglkTPGAARVDRgnppp 541
Cdd:pfam05109 554 NATSPTPAVTTPTP--NATIPTLGKTSPTSAV---TTPTPNATS-------------PTVGET---SPQANTTNH----- 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 542 ippKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGTKVVNEENVPKS---SSPQLP------PKPSIDLT-V 611
Cdd:pfam05109 608 ---TLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTsdnSTSHMPlltsahPTGGENITqV 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 612 APAGCPVSALATSQVGAWPAGTPGLNQPACSDSSlVIPATVAFCSSINPVSASSRSpgasdsllvAASGWSPSLTPLLMS 691
Cdd:pfam05109 685 TPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTS-TKPGEVNVTKGTPPKNATSPQ---------APSGQKTAVPTVTST 754
|
....
gi 91982738 692 GGPA 695
Cdd:pfam05109 755 GGKA 758
|
|
| ClassIIa_HDAC5_Gln-rich-N |
cd10164 |
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ... |
134-230 |
5.09e-04 |
|
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 5 (HDAC5). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.
Pssm-ID: 197400 [Multi-domain] Cd Length: 97 Bit Score: 40.96 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 134 RQKKLEMEKLQLQALEQEHKKLAahLEEERGKNKHVV----LMLVKECKQLSGKVVEEAQklEEVMAqleeeKKKTSELE 209
Cdd:cd10164 5 REQQLQQELLLLKQQQQLQKQLL--FAEFQKQHEHLTrqheVQLQKHLKVRAELFSEQQQ--QEILA-----AKRQQELE 75
|
90 100
....*....|....*....|..
gi 91982738 210 EQLSAEKQRSSGMEAQ-LEKQL 230
Cdd:cd10164 76 QQRKREQQRQEELEKQrLEQQL 97
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
135-228 |
5.11e-04 |
|
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: 41.40 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 135 QKKLEMEKLQ--LQALEQEHKKLAAHLEEERGK--------NKHVVL--MLVKECKQLSGKVVEEAQKLEEVMAQLEEEK 202
Cdd:pfam13863 3 EKKREMFLVQlaLDAKREEIERLEELLKQREEElekkeqelKEDLIKfdKFLKENDAKRRRALKKAEEETKLKKEKEKEI 82
|
90 100
....*....|....*....|....*.
gi 91982738 203 KKtseLEEQLSAEKQRSSGMEAQLEK 228
Cdd:pfam13863 83 KK---LTAQIEELKSEISKLEEKLEE 105
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
111-259 |
5.37e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.69 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 111 EAvMAHCRKMQERMSAQLVAAESRQKKLEMEKlqlQALEQEHKKLAAhleeergknkhvvlmlvkeckqlsgkvvEEAQK 190
Cdd:COG0542 397 EA-AARVRMEIDSKPEELDELERRLEQLEIEK---EALKKEQDEASF----------------------------ERLAE 444
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982738 191 LEEVMAQLEEEKkktSELEEQLSAEKQRSSGM---EAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:COG0542 445 LRDELAELEEEL---EALKARWEAEKELIEEIqelKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
126-254 |
5.70e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 126 AQLVAAESRQKKLEMEKLQLQALEQEHKKLAA---HLEEERGKnkhvvlmLVKECKQLSGKVVEEAQKLEEVMAQLEEeK 202
Cdd:COG4913 668 REIAELEAELERLDASSDDLAALEEQLEELEAeleELEEELDE-------LKGEIGRLEKELEQAEEELDELQDRLEA-A 739
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 91982738 203 KKTSELEEQLSAEKQRSSGMEAQLEKQLSE-FDTEREQLRAKLSREEAHTTDL 254
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDAVERELREnLEERIDALRARLNRAEEELERA 792
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
120-258 |
5.88e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 120 MQERMSAQLVAAES--RQKKLEMEKLQLQaLEQEHKKLAAhLEEERGKNKHVVLMLVKECKQLSGKVVEEAqkleevmaq 197
Cdd:COG3096 985 LNEKLRARLEQAEEarREAREQLRQAQAQ-YSQYNQVLAS-LKSSRDAKQQTLQELEQELEELGVQADAEA--------- 1053
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982738 198 leEEKKKT--SELEEQLSAEKQRSSgmeaQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:COG3096 1054 --EERARIrrDELHEELSQNRSRRS----QLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
120-259 |
5.92e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 120 MQERMSAQLVAAESRQKKLEmekLQLQALEQEHKKLAAHLEEERGKNKhvVLMLVKECKQLSGKVVEEAQKLEEVMAQLE 199
Cdd:COG3206 162 LEQNLELRREEARKALEFLE---EQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982738 200 EEKKKTSELEEQLSAEKQ-----RSSGMEAQLEKQLSEFDTEREQLRAKLSreEAHTT--DLKEEID 259
Cdd:COG3206 237 EAEARLAALRAQLGSGPDalpelLQSPVIQQLRAQLAELEAELAELSARYT--PNHPDviALRAQIA 301
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
126-299 |
6.04e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 126 AQLVAAESRQKKL--EMEKLQ--LQALEQEHKKLAAHLEEERGKNKHVVLML-----------VKECKQLSGKVVEEAQK 190
Cdd:COG3883 58 AELEALQAEIDKLqaEIAEAEaeIEERREELGERARALYRSGGSVSYLDVLLgsesfsdfldrLSALSKIADADADLLEE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 191 LEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEIDKMKKMMEQMKK 270
Cdd:COG3883 138 LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
170 180
....*....|....*....|....*....
gi 91982738 271 GSDGKPGLSLPRKTKDKRLASISVATEGP 299
Cdd:COG3883 218 AAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
18-259 |
6.61e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 18 DTEGATAEAAKKEFDVDTLSKSELRMllsvmEGELEarDLVIEALRARRKEVFIQERYGRFnlnDPFLAlqrdyeagpgd 97
Cdd:pfam01576 553 ELEALTQQLEEKAAAYDKLEKTKNRL-----QQELD--DLLVDLDHQRQLVSNLEKKQKKF---DQMLA----------- 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 98 KEKpvctnplsileavMAHCRKMQERMSAQlvaAESRQKK---------LEMEKLQLQALEQEHKKLAAHLEEergknkh 168
Cdd:pfam01576 612 EEK-------------AISARYAEERDRAE---AEAREKEtralslaraLEEALEAKEELERTNKQLRAEMED------- 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 169 vvlmLVKEcKQLSGKVVEEAQKLEEVM-AQLEEEKKKTSELEEQLSAE---KQR----SSGMEAQLE------------- 227
Cdd:pfam01576 669 ----LVSS-KDDVGKNVHELERSKRALeQQVEEMKTQLEELEDELQATedaKLRlevnMQALKAQFErdlqardeqgeek 743
|
250 260 270
....*....|....*....|....*....|....*..
gi 91982738 228 -----KQLSEFDTEREQLRAKlsREEAHTTDLKEEID 259
Cdd:pfam01576 744 rrqlvKQVRELEAELEDERKQ--RAQAVAAKKKLELD 778
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
800-825 |
6.74e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 38.39 E-value: 6.74e-04
10 20
....*....|....*....|....*.
gi 91982738 800 GQTPLYLACKNGNKECIKLLLEAGTD 825
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGAD 27
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
160-257 |
6.76e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 44.67 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 160 EEERGKNKHVVLMLVKECkqLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQ----------LEKQ 229
Cdd:pfam05911 682 ENKRLKEEFEQLKSEKEN--LEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQlkcmaesyedLETR 759
|
90 100
....*....|....*....|....*...
gi 91982738 230 LSEFDTEREQLRAKLSREEAhttDLKEE 257
Cdd:pfam05911 760 LTELEAELNELRQKFEALEV---ELEEE 784
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
111-290 |
7.10e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 111 EAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQ--EHKKLAAHLEEERGKNKHVVLMLVKecKQLSGKVVEEA 188
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKK--AAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 189 QKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKlsREEAHTTD-LKEEIDKMKKMMEQ 267
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK--AEEAKKADeAKKKAEEAKKKADE 1501
|
170 180
....*....|....*....|...
gi 91982738 268 MKKGSDGKPGLSLPRKTKDKRLA 290
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKA 1524
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
59-232 |
7.11e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 59 IEALRARRKEvfIQERYGRFN-LNDPFLALQRDYEAGpgDKEKPVCTNPLSILEAVMAHCRKMQERMSA--QLVAAESRQ 135
Cdd:COG4717 73 LKELEEELKE--AEEKEEEYAeLQEELEELEEELEEL--EAELEELREELEKLEKLLQLLPLYQELEALeaELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 136 KKLEMEKL-------QLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKqlsgkvvEEAQKLEEVMAQLEEEKKKTSEL 208
Cdd:COG4717 149 EELEERLEelreleeELEELEAELAELQEELEELLEQLSLATEEELQDLA-------EELEELQQRLAELEEELEEAQEE 221
|
170 180
....*....|....*....|....*.
gi 91982738 209 EEQLSAEKQR--SSGMEAQLEKQLSE 232
Cdd:COG4717 222 LEELEEELEQleNELEAAALEERLKE 247
|
|
| LUC7 |
pfam03194 |
LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs ... |
86-230 |
7.57e-04 |
|
LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs and only contains eukaryotic proteins. LUC7 has been shown to be a U1 snRNA associated protein with a role in splice site recognition. The family also contains human and mouse LUC7 like (LUC7L) proteins and human cisplatin resistance-associated overexpressed protein (CROP).
Pssm-ID: 460842 [Multi-domain] Cd Length: 246 Bit Score: 42.97 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 86 ALQRDYEAGPGDKEKPVCTnplsilEAVMAHCRKM-----------QERMsaQLVAAESRQKKlEMEKLQLQALEQEHKK 154
Cdd:pfam03194 64 ALKADYEKASKRKKKYGYE------REFLRFLQKLiddvdrkirkgKQRL--ELTQEEIEQTD-ELKQEQISVLEEKIKK 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982738 155 LAAHLEE--ERGKnkhvvlmlvkeckqlsgkvVEEAQKLeevMAQLEEEKKKTSELEEQLsaEKQRSSGMEAQlEKQL 230
Cdd:pfam03194 135 LLEEAEElgEEGN-------------------VDEAQKL---MKKVEELKEEKEELEQQY--ESLTKESAASQ-EKKM 187
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
107-258 |
7.86e-04 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 42.47 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 107 LSILEAVMAHCRKMQERMS---AQLVAAESRQKKLEMEKLQL--QALEQEHKKL-AAHLEEERGKNKHVVLMLVKECKQL 180
Cdd:pfam14662 7 LTCVEDLQANNQKLLQENSklkATVETREETNAKLLEENLNLrkQAKSQQQAVQkEKLLEEELEDLKLIVNSLEEARRSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 181 SGK---VVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEE 257
Cdd:pfam14662 87 LAQnkqLEKENQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIEELKST 166
|
.
gi 91982738 258 I 258
Cdd:pfam14662 167 V 167
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
118-249 |
1.03e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 118 RKMQERMSAQLVAAESRQKKLEMEKLQLQALE-QEHKKLAAH---LEEERGKNkhvvlmlVKECKQLSGKVVEEAQKLEE 193
Cdd:PRK11637 119 QAAQERLLAAQLDAAFRQGEHTGLQLILSGEEsQRGERILAYfgyLNQARQET-------IAELKQTREELAAQKAELEE 191
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982738 194 VMAQ----LEEEKKKTSELEEQLSAEKQRSSGMEAQLEK---QLSEFDTEREQLRAKLSREEA 249
Cdd:PRK11637 192 KQSQqktlLYEQQAQQQKLEQARNERKKTLTGLESSLQKdqqQLSELRANESRLRDSIARAER 254
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
25-265 |
1.23e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 25 EAAKKEFDvDTLSK-SELRMLLSVMEGELEArdlvieaLRARRKEVfiQERYGRFNlndpflALQRDYEAGPGDKEKpvc 103
Cdd:PRK03918 196 KEKEKELE-EVLREiNEISSELPELREELEK-------LEKEVKEL--EELKEEIE------ELEKELESLEGSKRK--- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 104 tnplsiLEAVMAHCRKMQERMSAQLVAAESRQKKLEmeklQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGk 183
Cdd:PRK03918 257 ------LEEKIRELEERIEELKKEIEELEEKVKELK----ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 184 VVEEAQKLEEVMAQLEEEKKKTSELE--------------------EQLSAEKQRSSGMEAQ-LEKQLSEFDTEREQLRA 242
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEkrleeleerhelyeeakakkEELERLKKRLTGLTPEkLEKELEELEKAKEEIEE 405
|
250 260
....*....|....*....|...
gi 91982738 243 KLSREEAHTTDLKEEIDKMKKMM 265
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAI 428
|
|
| PHA02917 |
PHA02917 |
ankyrin-like protein; Provisional |
783-856 |
1.28e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165231 [Multi-domain] Cd Length: 661 Bit Score: 43.45 E-value: 1.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982738 783 IELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAV-DTGNVDSLKLLMYHR 856
Cdd:PHA02917 435 INICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAInESRNIELLKMLLCHK 509
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
123-244 |
1.29e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 40.75 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 123 RMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKhvvlMLVKECKQLSGKVVEEAQKLEE---VMAQLE 199
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQ----QLEEEVEKLEEQLKEAKEKAEEsekLKTNNE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 91982738 200 EEKKKTSELEEQL---------SAEKQRSSGMEA-QLEKQLSEFDTEREQLRAKL 244
Cdd:pfam12718 77 NLTRKIQLLEEELeesdkrlkeTTEKLRETDVKAeHLERKVQALEQERDEWEKKY 131
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
124-230 |
1.30e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 124 MSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnkhvvlmLVKECKQLSGKVVEEAQKLEEVMAQLEEEKK 203
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA-------LLKQLAALERRIAALARRIRALEQELAALEA 83
|
90 100
....*....|....*....|....*..
gi 91982738 204 KTSELEEQLSAEKQRSSGMEAQLEKQL 230
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELL 110
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
129-249 |
1.47e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 43.09 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 129 VAAESRQKKLEMEKLQLQALEQEHKK---LAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEE---------VMA 196
Cdd:pfam05701 321 VAAASLRSELEKEKAELASLRQREGMasiAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQaaqeaeeakSLA 400
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 91982738 197 QL-EEEKKKTSELEEQLSAEkqrSSGMEAQLEKqlsefdTEREQLRAKLSREEA 249
Cdd:pfam05701 401 QAaREELRKAKEEAEQAKAA---ASTVESRLEA------VLKEIEAAKASEKLA 445
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
707-910 |
1.52e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 43.15 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 707 AAAQGNVTLLS-MLLNEEGLDINysCED--GHSALYSAAK-NGHTDCVRLLLNAEARVDAADKngftpLCVAAAQGHFEC 782
Cdd:TIGR00870 24 AAERGDLASVYrDLEEPKKLNIN--CPDrlGRSALFVAAIeNENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 783 IELLTAYNAninhSAAGGQTPLYLAckngNKECikllleagTDRSIKtrdGWTPIHAAVDTGNVDSLKLLMYHR----VR 858
Cdd:TIGR00870 97 VEAILLHLL----AAFRKSGPLELA----NDQY--------TSEFTP---GITALHLAAHRQNYEIVKLLLERGasvpAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982738 859 AHGNSLSSeepKSGLFSLNGGESP------TGpSKPVV------PADlINHADKEGWTAAHIAA 910
Cdd:TIGR00870 158 ACGDFFVK---SQGVDSFYHGESPlnaaacLG-SPSIVallsedPAD-ILTADSLGNTLLHLLV 216
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6-259 |
1.53e-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: 43.52 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 6 ASCEPDLSRTPGDTEGATAEAAKKEfdvdtlsKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYgrfnLNDPFL 85
Cdd:TIGR02169 782 NDLEARLSHSRIPEIQAELSKLEEE-------VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIK 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 86 ALQRDYEAGPGDKEK-----PVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEmekLQLQALEQEHKKLAAHLE 160
Cdd:TIGR02169 851 SIEKEIENLNGKKEEleeelEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE---AQIEKKRKRLSELKAKLE 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 161 EERGKNKHVVLML-----VKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTseLEEQLSAEKQRSSgmeaqLEKQLSEFDT 235
Cdd:TIGR02169 928 ALEEELSEIEDPKgedeeIPEEELSLEDVQAELQRVEEEIRALEPVNMLA--IQEYEEVLKRLDE-----LKEKRAKLEE 1000
|
250 260
....*....|....*....|....
gi 91982738 236 EREQLRaklsreeahttDLKEEID 259
Cdd:TIGR02169 1001 ERKAIL-----------ERIEEYE 1013
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
119-249 |
1.56e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 119 KMQERMSAQLVAAESRQKKLEM---EKLQLQALEQEHKKlaaHLEEERGKNKHVVLMLVKECKQ--LSGKVVEEAQKLEE 193
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQqaeELQQKQAAEQERLK---QLEKERLAAQEQKKQAEEAAKQaaLKQKQAEEAAAKAA 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 91982738 194 VMAQL--EEEKKKTSELEEQLSAEKQRSSGMEAQlEKQLSEFDTEREQLRAKLSREEA 249
Cdd:PRK09510 143 AAAKAkaEAEAKRAAAAAKKAAAEAKKKAEAEAA-KKAAAEAKKKAEAEAAAKAAAEA 199
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
717-926 |
1.68e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 43.13 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 717 SMLLNEEGLDINYSCEDGHSALYSAAKNGH-TDCVRLLLNAEARVDAADKNGFTPLCVAAAQGH-FECIELLTAYNANIN 794
Cdd:PHA02876 256 SLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVN 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 795 HSAAGGQTPLYLACK-NGNKECIKLLLEAGTDrsIKTRDGW--TPIHAAVDTGNVDSLKLLMyhrvrAHGNSLSSEEPKS 871
Cdd:PHA02876 336 AADRLYITPLHQASTlDRNKDIVITLLELGAN--VNARDYCdkTPIHYAAVRNNVVIINTLL-----DYGADIEALSQKI 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 91982738 872 GL---FSLNGGESPTGPSKPVVPADLINHADKEGWTAAHIAASKGFK-NCLEVLCRHGG 926
Cdd:PHA02876 409 GTalhFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGA 467
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
130-258 |
1.72e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 130 AAESRQKKLEMEKLQ--LQALE--QEHKKLAahLEEERgknkhvvlMLVKECKQLSG------KVVEEAQKLEEVMAQLE 199
Cdd:COG1340 101 LAELNKAGGSIDKLRkeIERLEwrQQTEVLS--PEEEK--------ELVEKIKELEKelekakKALEKNEKLKELRAELK 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982738 200 EEKKKTSELEEQLSAEKQRSSgmeaQLEKQLSEFDTEREQLRAKlsREEAHTT----------------DLKEEI 258
Cdd:COG1340 171 ELRKEAEEIHKKIKELAEEAQ----ELHEEMIELYKEADELRKE--ADELHKEiveaqekadelheeiiELQKEL 239
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
131-243 |
1.74e-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: 41.61 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 131 AESRQKKLEMEKLQLQALEQEH---KKLA-----------AHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQklEEVMA 196
Cdd:pfam13904 65 QRQRQKELQAQKEEREKEEQEAelrKRLAkekyqewlqrkARQQTKKREESHKQKAAESASKSLAKPERKVSQ--EEAKE 142
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 91982738 197 QLEE-EKKKTSELEEQlsAEKQRssgmEAQLEKQLSEFdtEREQLRAK 243
Cdd:pfam13904 143 VLQEwERKKLEQQQRK--REEEQ----REQLKKEEEEQ--ERKQLAEK 182
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
733-762 |
1.82e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.18 E-value: 1.82e-03
10 20 30
....*....|....*....|....*....|
gi 91982738 733 DGHSALYSAAKNGHTDCVRLLLNAEARVDA 762
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
771-853 |
1.86e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 42.67 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 771 LCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLK 850
Cdd:PHA02875 6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
|
...
gi 91982738 851 LLM 853
Cdd:PHA02875 86 ELL 88
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
127-259 |
1.86e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 41.57 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 127 QLVAAESRQK------KLEME---KLQLQALEQ---EHKKLAAH-LEEERGKNKHVVLMLVKECKQLSGKV------VEE 187
Cdd:pfam15665 28 QQILAETREKilqyksKIGEEldlKRRIQTLEEsleQHERMKRQaLTEFEQYKRRVEERELKAEAEHRQRVvelsreVEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 188 AQK--------LEEVMAQLEEEKKKtsELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLsreEAHTTDLKEEID 259
Cdd:pfam15665 108 AKRafeeklesFEQLQAQFEQEKRK--ALEELRAKHRQEIQELLTTQRAQSASSLAEQEKLEELH---KAELESLRKEVE 182
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
766-794 |
2.02e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.27 E-value: 2.02e-03
10 20 30
....*....|....*....|....*....|
gi 91982738 766 NGFTPLCVAAAQ-GHFECIELLTAYNANIN 794
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
110-213 |
2.07e-03 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 39.69 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 110 LEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnkhvvlmlVKECKQLSGKVVEEAQ 189
Cdd:pfam04871 6 LESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELEAEVKKLEEALKKLKAE--------LSEEKQKEKEKQSELD 77
|
90 100
....*....|....*....|....
gi 91982738 190 KLEEVMAQLEEekkKTSELEEQLS 213
Cdd:pfam04871 78 DLLLLLGDLEE---KVEKYKARLK 98
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
118-251 |
2.14e-03 |
|
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: 42.33 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 118 RKMQERMSAQLVAAESR-------QKKLEMEKLQLQALEQEHKKlaaHLEEERGKNKHVVLMLVKEckqlsgKVVEEAQK 190
Cdd:pfam15558 79 RRRADRREKQVIEKESRwreqaedQENQRQEKLERARQEAEQRK---QCQEQRLKEKEEELQALRE------QNSLQLQE 149
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982738 191 LEEVMAQleeeKKKTSELEEQLSA-EKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHT 251
Cdd:pfam15558 150 RLEEACH----KRQLKEREEQKKVqENNLSELLNHQARKVLVDCQAKAEELLRRLSLEQSLQ 207
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
141-257 |
2.44e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 39.97 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 141 EKLQLQALEQ--EHKKLAAHLEEErgknkhvVLMLVKEcKQLSGK----VVEEAQK----LEEVMAQLEEEKKKTSELEE 210
Cdd:pfam10473 2 EKKQLHVLEKlkESERKADSLKDK-------VENLERE-LEMSEEnqelAILEAENskaeVETLKAEIEEMAQNLRDLEL 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 91982738 211 QLSAEKQRSSGMEAQLEK---QLSEFDTEREQLRAKLSREEAHTTDLKEE 257
Cdd:pfam10473 74 DLVTLRSEKENLTKELQKkqeRVSELESLNSSLENLLEEKEQEKVQMKEE 123
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
720-821 |
2.64e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 42.32 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 720 LNEEGLDINYSCEDGHSALYSAAKngHTDCVRL----LLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINH 795
Cdd:PHA03095 208 LIRAGCDPAATDMLGNTPLHSMAT--GSSCKRSlvlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
|
90 100
....*....|....*....|....*.
gi 91982738 796 SAAGGQTPLYLACKNGNKECIKLLLE 821
Cdd:PHA03095 286 VSSDGNTPLSLMVRNNNGRAVRAALA 311
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
118-257 |
3.11e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 118 RKMQERMSAQLVAAESR----QKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHvvlmLVKEckqlSGKVVEEAQKLEE 193
Cdd:pfam05483 91 KKWKVSIEAELKQKENKlqenRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKD----LIKE----NNATRHLCNLLKE 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982738 194 VMAQLEEekkKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQlrAKLSREEAHTTdLKEE 257
Cdd:pfam05483 163 TCARSAE---KTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQ--AENARLEMHFK-LKED 220
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
118-253 |
3.12e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 118 RKMQERMSAQLVAAESRQKKlEMEKLQLQALEQEHKKLAAHLEEERGKnkhvvlmlVKECKqlsgKVVEEAQKLEEVMAQ 197
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAK-KADEAKKKAEEAKKAEEAKKKAEEAKK--------ADEAK----KKAEEAKKADEAKKK 1491
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 91982738 198 LEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSR--EEAHTTD 253
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaEEKKKAD 1549
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
108-233 |
3.19e-03 |
|
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: 41.41 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 108 SILEAVMAhCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKklaahlEEERGKNKHVvlmlvkecKQLSGKVVEE 187
Cdd:cd16269 185 AILQADQA-LTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLE------DQERSYEEHL--------RQLKEKMEEE 249
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 91982738 188 AQKLEEvmaqlEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEF 233
Cdd:cd16269 250 RENLLK-----EQERALESKLKEQEALLEEGFKEQAELLQEEIRSL 290
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
702-862 |
3.27e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 41.92 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 702 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCE----DGHSALYSAAKNGHTDCVRLLLNAEARVDAADKNG--FT------ 769
Cdd:cd22192 53 TALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGtfFRpgpknl 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 770 ------PLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYL----ACKNGNKECIKLLLEA-GTDRS-----IKTRDG 833
Cdd:cd22192 133 iyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlvlqPNKTFACQMYDLILSYdKEDDLqpldlVPNNQG 212
|
170 180
....*....|....*....|....*....
gi 91982738 834 WTPIHAAVDTGNVDSLKLLMYHRVRAHGN 862
Cdd:cd22192 213 LTPFKLAAKEGNIVMFQHLVQKRRHIQWT 241
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
111-254 |
3.42e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 111 EAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHlEEERGKNKhvvlmlvkecKQLSGKVVEEAQK 190
Cdd:TIGR00606 230 EAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR-KKQMEKDN----------SELELKMEKVFQG 298
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 191 LEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTE------REQLRAKLSREEAHTTDL 254
Cdd:TIGR00606 299 TDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTEllveqgRLQLQADRHQEHIRARDS 368
|
|
| ATP_synt_b |
TIGR01144 |
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ... |
114-249 |
3.76e-03 |
|
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 130214 [Multi-domain] Cd Length: 147 Bit Score: 39.69 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 114 MAHCRKMqerMSAQLVAA-ESRQKKLEMEklqLQALEQEHKKLAAHLEEERGknkhvvlmLVKECKQLSGKVVEEAQKLE 192
Cdd:TIGR01144 9 VWFCMKY---VWPPLAKAiETRQKKIADG---LASAERAKKEAALAQKKAQV--------ILKEAKDEAQEIIENANKRG 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 91982738 193 EvmAQLEEEKKKTSELEEQLSAEKQrssgmeaqlekqlSEFDTEREQLRAKLSREEA 249
Cdd:TIGR01144 75 S--EILEEAKAEAREEREKIKAQAR-------------AEIEAEKEQAREELRKQVA 116
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
51-257 |
3.84e-03 |
|
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: 42.03 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 51 ELEARDLVIEALRARRKEVfiqERYGRFNLNDPFLALQRDYEAGPGDKEK-------------PVCTNPLSILEAVMAHC 117
Cdd:pfam17380 311 EVERRRKLEEAEKARQAEM---DRQAAIYAEQERMAMERERELERIRQEErkrelerirqeeiAMEISRMRELERLQMER 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 118 RKMQERMSAQLVAA-------ESRQKKL-----EMEKLQLQALEQEHKKLAaHLEEERGKNKHVVLMLVKECKQLSGKV- 184
Cdd:pfam17380 388 QQKNERVRQELEAArkvkileEERQRKIqqqkvEMEQIRAEQEEARQREVR-RLEEERAREMERVRLEEQERQQQVERLr 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 185 -VEEAQKLEEVMAQLEEEKKKTSE------LEEQLSAEKQRSSGMEAQ---LEKQLSEFDTE-REQLRAKLSREEAHTTD 253
Cdd:pfam17380 467 qQEEERKRKKLELEKEKRDRKRAEeqrrkiLEKELEERKQAMIEEERKrklLEKEMEERQKAiYEEERRREAEEERRKQQ 546
|
....
gi 91982738 254 LKEE 257
Cdd:pfam17380 547 EMEE 550
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
118-243 |
4.00e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 41.37 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 118 RKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHK-KLAAHLEEERGKNKHVVLMLVKECKQ---LSGKVVEEA----Q 189
Cdd:TIGR02794 64 KKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAaEKAAKQAEQAAKQAEEKQKQAEEAKAkqaAEAKAKAEAeaerK 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 91982738 190 KLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAK 243
Cdd:TIGR02794 144 AKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAK 197
|
|
| Rootletin |
pfam15035 |
Ciliary rootlet component, centrosome cohesion; |
118-247 |
4.02e-03 |
|
Ciliary rootlet component, centrosome cohesion;
Pssm-ID: 464459 [Multi-domain] Cd Length: 190 Bit Score: 40.41 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 118 RKMQERMSAQlvaaeSRQKKLeMEKLQLQALEQ-------EHKKLAAHLEEERGKNKHVVLMLVKECKQLSGkvvEEAQK 190
Cdd:pfam15035 2 RKLQAYQEAQ-----QRQAQL-VQKLQAKVLQYkkrcselEQQLLEKTSELEKTELLLRKLTLEPRLQRLER---EHSAD 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982738 191 LEEVMAQLEEEKKKTSEL-----------------EEQLSAEKQR----SSGMEAQLEKQLSEFDTEREQLRAKLSRE 247
Cdd:pfam15035 73 LEEALIRLEEERQRSESLsqvnsllreqleqasraNEALREDLQKltndWERAREELEQKESEWRKEEEAFNEYLSSE 150
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
666-841 |
4.19e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 41.70 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 666 RSPGASDSLLVAASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNvtlLSMLLNEEGLDINYsceDGHSALYSAAKNG 745
Cdd:cd22193 14 RRKDLTDSEFTESSTGKTCLMKALLNLNPGTNDTIRILLDIAEKTDN---LKRFINAEYTDEYY---EGQTALHIAIERR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 746 HTDCVRLLLNAEARVDAAdkngftplcvaaAQGHFecielltaYNANINHSA-AGGQTPLYLACKNGNKECIKLLLE-AG 823
Cdd:cd22193 88 QGDIVALLVENGADVHAH------------AKGRF--------FQPKYQGEGfYFGELPLSLAACTNQPDIVQYLLEnEH 147
|
170 180
....*....|....*....|
gi 91982738 824 TDRSIKTRD--GWTPIHAAV 841
Cdd:cd22193 148 QPADIEAQDsrGNTVLHALV 167
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
111-290 |
4.44e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 111 EAVMAHCRKMQERmsaqlVAAESRQKKLEMEKlqlqaleQEHKKLAAHLEEERGKNKhvvlmlVKECKqlsgKVVEEAQK 190
Cdd:PTZ00121 1259 EARMAHFARRQAA-----IKAEEARKADELKK-------AEEKKKADEAKKAEEKKK------ADEAK----KKAEEAKK 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 191 LEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRA---KLSREEAHTTDLKEEIDKMKKMMEQ 267
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaekKKEEAKKKADAAKKKAEEKKKADEA 1396
|
170 180 190
....*....|....*....|....*....|....*..
gi 91982738 268 MKKGSDGKPGL--------------SLPRKTKDKRLA 290
Cdd:PTZ00121 1397 KKKAEEDKKKAdelkkaaaakkkadEAKKKAEEKKKA 1433
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
159-258 |
4.62e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 159 LEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRssgMEAQLEKQLSEFDTERE 238
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQ---LEEELEQARSELEQLEE 80
|
90 100
....*....|....*....|...
gi 91982738 239 QLRA---KLSREEAHTTDLKEEI 258
Cdd:COG4372 81 ELEElneQLQAAQAELAQAQEEL 103
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
769-853 |
4.96e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 40.19 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 769 TPL--CVAAAQGHFECIELLTAYNANINHSAAG-GQTPL--YLAC-KNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVD 842
Cdd:PHA02859 53 TPIfsCLEKDKVNVEILKFLIENGADVNFKTRDnNLSALhhYLSFnKNVEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132
|
90
....*....|...
gi 91982738 843 TGNV--DSLKLLM 853
Cdd:PHA02859 133 NFNVriNVIKLLI 145
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
139-259 |
5.12e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 41.39 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 139 EMEKLQLQALEQEHKKLaahleeeRGKNKHVVLMLVKECKQLSgkvveEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQR 218
Cdd:PRK00106 31 EAAELTLLNAEQEAVNL-------RGKAERDAEHIKKTAKRES-----KALKKELLLEAKEEARKYREEIEQEFKSERQE 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 91982738 219 SSGMEAQLEKQLSEFDTEREQLRAK---LSREEAHTTDLKEEID 259
Cdd:PRK00106 99 LKQIESRLTERATSLDRKDENLSSKektLESKEQSLTDKSKHID 142
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
126-249 |
5.13e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.23 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 126 AQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEergknKHVVLMLVKECKQLSGKVVEEAQKLEEVMA----QLEEE 201
Cdd:PRK12705 22 VVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEA-----KELLLRERNQQRQEARREREELQREEERLVqkeeQLDAR 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 91982738 202 KKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLrAKLSREEA 249
Cdd:PRK12705 97 AEKLDNLENQLEEREKALSARELELEELEKQLDNELYRV-AGLTPEQA 143
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
126-249 |
5.15e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 41.18 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 126 AQLVAAESR-QKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSgkvVEEAQKLEEVMAQ----LEE 200
Cdd:COG3064 5 LEEKAAEAAaQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAK---AEAEQRAAELAAEaakkLAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 91982738 201 EKKKTSELEEQLSAEKQRSsgmEAQLEKQLSEfdtEREQLRAKLSR-EEA 249
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKA---AKEAEAAAAA---EKAAAAAEKEKaEEA 125
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
126-249 |
5.68e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 126 AQLVAAESRQKKLE-------------MEKLQLQALEQEHKKLAAHLEEERGK--NKH-VVLMLVKECKQLSGKVVEEAQ 189
Cdd:COG3206 233 AELAEAEARLAALRaqlgsgpdalpelLQSPVIQQLRAQLAELEAELAELSARytPNHpDVIALRAQIAALRAQLQQEAQ 312
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982738 190 K-LEEVMAQLEEEKKKTSELEEQLSAEKQRSSGM---EAQLEKQLSEFDTEREQLRAKLSR-EEA 249
Cdd:COG3206 313 RiLASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRlEEA 377
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
118-232 |
6.18e-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: 41.09 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 118 RKMQERMSAQLVAAESRQKKLEMEKLQLQalEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEaqKLEEVMAQ 197
Cdd:pfam15709 408 RKQRLQLQAAQERARQQQEEFRRKLQELQ--RKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEE--RLEYQRQK 483
|
90 100 110
....*....|....*....|....*....|....*
gi 91982738 198 LEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSE 232
Cdd:pfam15709 484 QEAEEKARLEAEERRQKEEEAARLALEEAMKQAQE 518
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
29-259 |
6.23e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 29 KEFDVDTLSK-SELRMLLSVMEGELEARDLVIEALRARRKEvfIQERYGRFNlndpflALQRDYEAGPGDKEKpvctnpL 107
Cdd:PRK03918 299 SEFYEEYLDElREIEKRLSRLEEEINGIEERIKELEEKEER--LEELKKKLK------ELEKRLEELEERHEL------Y 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 108 SILEAVMAHCRKMQ--------ERMSAQLVAAESRQKKLEMEKLQLQA----LEQEHKKLAAHLEE-ERGKNKhvvlmlv 174
Cdd:PRK03918 365 EEAKAKKEELERLKkrltgltpEKLEKELEELEKAKEEIEEEISKITArigeLKKEIKELKKAIEElKKAKGK------- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 175 keCKqLSGKVVEEAQKLE------EVMAQLEEEKKKTSELEEQLSAEKQRssgMEAQLEKQlSEFDTER---EQLRA--- 242
Cdd:PRK03918 438 --CP-VCGRELTEEHRKElleeytAELKRIEKELKEIEEKERKLRKELRE---LEKVLKKE-SELIKLKelaEQLKElee 510
|
250 260
....*....|....*....|....*
gi 91982738 243 --------KLSREEAHTTDLKEEID 259
Cdd:PRK03918 511 klkkynleELEKKAEEYEKLKEKLI 535
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
780-846 |
6.38e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 41.13 E-value: 6.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982738 780 FECIELLTAYNANINHSAAGGQTPLYLACKNGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNV 846
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSV 267
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
174-259 |
7.53e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 174 VKECKQLSGKVVEEAQKLEEVMAQL------EEEKKKTSELEEQLSAEK-------QRSSGMEAQLEKQLSEFDTEREQL 240
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEalleakEEIHKLRNEFEKELRERRnelqkleKRLLQKEENLDRKLELLEKREEEL 112
|
90 100
....*....|....*....|..
gi 91982738 241 ---RAKLSREEAHTTDLKEEID 259
Cdd:PRK12704 113 ekkEKELEQKQQELEKKEEELE 134
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
132-259 |
7.56e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 132 ESRQKKLEMEKLQ----LQALEQEHKKL-----AAHLEEE-RGKNKHVVLM------LVKECKQLSGKVVEEAQKLEEVM 195
Cdd:TIGR04523 523 KEKIEKLESEKKEkeskISDLEDELNKDdfelkKENLEKEiDEKNKEIEELkqtqksLKKKQEEKQELIDQKEKEKKDLI 602
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982738 196 AQLEEEKKKTSELEEQLS---AEKQRSSGMEAQLEKQLSEFDTEREQL-------RAKLSREEAHTTDLKEEID 259
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEkakKENEKLSSIIKNIKSKKNKLKQEVKQIketikeiRNKWPEIIKKIKESKTKID 676
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
512-709 |
7.60e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 40.99 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 512 GGDAGTCPPVGRTGLKTPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPstlpqgtkVVNEE 591
Cdd:PRK07003 366 GAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAP--------PATAD 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 592 NVPKSSSPQLPPKPSIDLTVAPAGCPVSALATSQVGAWPAGTPGLNQPACSDSSLVIPATVAFCSSINPVSASSRSPGAS 671
Cdd:PRK07003 438 RGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAAS 517
|
170 180 190
....*....|....*....|....*....|....*....
gi 91982738 672 -DSLLVAASGWSPSLTPllmsggPAPLAGRPTLLQQAAA 709
Cdd:PRK07003 518 rEDAPAAAAPPAPEARP------PTPAAAAPAARAGGAA 550
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-264 |
8.43e-03 |
|
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: 40.81 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 107 LSILEAVMAHCRKMQERMSAQLVAA----ESRQKKLEMEKLQLQALEQEHKKL---AAHLEEERGKNKHVVLMLVKECKQ 179
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELeaeiEELEERLEEAEEELAEAEAEIEELeaqIEQLKEELKALREALDELRAELTL 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 180 LSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEID 259
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
....*
gi 91982738 260 KMKKM 264
Cdd:TIGR02168 895 ELEEL 899
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
16-259 |
8.79e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 16 PGDTEGATAEAAKKEFDVDtlsksELRMLLSVMEGELEARDLVIEALRARRKEVF--IQERYGRFNLNDPFLAlqrdyEA 93
Cdd:TIGR00606 708 PDKLKSTESELKKKEKRRD-----EMLGLAPGRQSIIDLKEKEIPELRNKLQKVNrdIQRLKNDIEEQETLLG-----TI 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 94 GPGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQLVAAESRQKKLEMEKLQLQALEQEHK--------KLAAHLEEERGK 165
Cdd:TIGR00606 778 MPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHEldtvvskiELNRKLIQDQQE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 166 NKHVVLMLVKECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKqlseFDTEREQLRAKLS 245
Cdd:TIGR00606 858 QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEK----DQQEKEELISSKE 933
|
250
....*....|....*...
gi 91982738 246 RE----EAHTTDLKEEID 259
Cdd:TIGR00606 934 TSnkkaQDKVNDIKEKVK 951
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
121-240 |
8.88e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.50 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 121 QERMSAQLVAAESRQKKLEME----KLQLQALEQEHKKLAAHLEEERGKNKhvvlMLVKECKQLSGK---VVEeaQKLEE 193
Cdd:pfam13851 80 YEKDKQSLKNLKARLKVLEKElkdlKWEHEVLEQRFEKVERERDELYDKFE----AAIQDVQQKTGLknlLLE--KKLQA 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 91982738 194 VMAQLEeekKKTSELEEQLSA---EKQRSSGMEAQLEKQLSEFDTEREQL 240
Cdd:pfam13851 154 LGETLE---KKEAQLNEVLAAanlDPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
40-258 |
9.00e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 40 ELRMLLSVMEGELEARDLVIEALRARRKEVFIQERygrfNLNDPFLALQRDYEAGPGDKEKpvctnplsileaVMAHCRK 119
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLEEETAQKNNALKKIR----ELEAQISELQEDLESERAARNK------------AEKQRRD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 120 MQERMSA---------QLVAA--ESRQKKlEMEKLQLQ-ALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLS-GKVVe 186
Cdd:pfam01576 297 LGEELEAlkteledtlDTTAAqqELRSKR-EQEVTELKkALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKrNKAN- 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982738 187 eaqkLEEVMAQLEEEKKKTSELEEQLSAEKQRSSGMEAQLEKQLSEfdtereqLRAKLSREEAHTTDLKEEI 258
Cdd:pfam01576 375 ----LEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE-------LQARLSESERQRAELAEKL 435
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
124-259 |
9.05e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 124 MSAQLVAAESRQKKLEME----KLQLQALEQEHKKLAAHLEEERGKnkhvvlmlVKECKQLSGKVVEEAQKLEEVMAQLE 199
Cdd:COG1340 6 LSSSLEELEEKIEELREEieelKEKRDELNEELKELAEKRDELNAQ--------VKELREEAQELREKRDELNEKVKELK 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 200 EEK----KKTSELEEQL------SAEKQRSSGMEAQLEKQLSEFdtEREQLRAKLSREEahttdlkeEID 259
Cdd:COG1340 78 EERdelnEKLNELREELdelrkeLAELNKAGGSIDKLRKEIERL--EWRQQTEVLSPEE--------EKE 137
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
120-258 |
9.24e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 120 MQERMSAQLVAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERgknkHVVLMLVKECKQlsgkvveEAQKLEeVMAQLE 199
Cdd:PRK04863 986 LNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY----DAKRQMLQELKQ-------ELQDLG-VPADSG 1053
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982738 200 EEKK---KTSELEEQLSAEKQRSSgmeaQLEKQLSEFDTEREQLRAKLSREEAHTTDLKEEI 258
Cdd:PRK04863 1054 AEERaraRRDELHARLSANRSRRN----QLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
141-249 |
9.70e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 40.41 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982738 141 EKLQLQALEQEHKKLAAHLEEERGKNKhvvlmlvkECKQLSGKVVEEAQKLEEVMAQLEEEKKKTSELEEQlsaekQRSS 220
Cdd:COG3064 3 EALEEKAAEAAAQERLEQAEAEKRAAA--------EAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAE-----QRAA 69
|
90 100
....*....|....*....|....*....
gi 91982738 221 GMEAQLEKQLSEFDTEREQLRAKLSREEA 249
Cdd:COG3064 70 ELAAEAAKKLAEAEKAAAEAEKKAAAEKA 98
|
|
| |
