|
Name |
Accession |
Description |
Interval |
E-value |
| RUN_FYCO1 |
cd17698 |
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ... |
7-164 |
5.60e-103 |
|
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and Phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. This model represents the RUN domain of FYCO1.
Pssm-ID: 439060 Cd Length: 158 Bit Score: 324.73 E-value: 5.60e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 7 ESQLQRIIRDLQDAVTELSKEFQEAGEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGAND 86
Cdd:cd17698 1 ESQLQKIIRDLQDCVTELKKEFEETGEPITDDSTTLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFCECLAKVKGLND 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1894925332 87 GIRFVKSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLQPKLSSDIVGQLYELTEVQFDL 164
Cdd:cd17698 81 GIRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDWYYPRSVFLNHKYSSDIINSLYDLNEVQFDL 158
|
|
| RUN_RUFY4 |
cd17697 |
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ... |
15-164 |
4.38e-61 |
|
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain; this model represents the RUN domain of RUFY4.
Pssm-ID: 439059 Cd Length: 150 Bit Score: 205.80 E-value: 4.38e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 15 RDLQDAVTELSKEFQEAGEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSI 94
Cdd:cd17697 1 KDLQASIAELQKDQEEQQLPITDGSPELHRLCARLEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNST 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 95 SELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLQPKLSSDIVGQLYELTEVQFDL 164
Cdd:cd17697 81 DKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNPELTGEWYYARSPFLSPELRSDILDSLYELNGVNFDL 150
|
|
| RUN_RUFY4_like |
cd17682 |
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ... |
16-164 |
1.44e-53 |
|
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil domain-containing protein 1 (FYCO1), and similar proteins; The family includes RUFY4 and FYCO1. RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. Both RUFY4 and FYCO1 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.
Pssm-ID: 439044 Cd Length: 150 Bit Score: 183.97 E-value: 1.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 16 DLQDAVTELSKEFqeaGEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKV----KGANDGIRFV 91
Cdd:cd17682 1 DLKGCVLDLKSEF---GEITDPDNPYLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEELLKKLnkipKSLSDAVKFV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925332 92 KSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLQPKLSSDIVGQLYELTEVQFDL 164
Cdd:cd17682 78 KSCKKVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEILSEILLSLLYQLNEINFDL 150
|
|
| FYVE_FYCO1 |
cd15726 |
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ... |
1170-1227 |
9.82e-37 |
|
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also termed zinc finger FYVE domain-containing protein 7, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that is associated with the exterior of autophagosomes and mediates microtubule plus-end-directed vesicle transport. It acts as an effector of GTP-bound Rab7, a GTPase that recruits FYCO1 to autophagosomes and has been implicated in autophagosome-lysosomal fusion. FYCO1 also interacts with two microtubule motor proteins, kinesin (KIF) 5B and KIF23, and thus functions as a platform for assembly of vesicle fusion and trafficking factors. FYCO1 contains an N-terminal alpha-helical RUN domain followed by a long central coiled-coil region, a FYVE domain and a GOLD (Golgi dynamics) domain in C-terminus.
Pssm-ID: 277265 [Multi-domain] Cd Length: 58 Bit Score: 132.68 E-value: 9.82e-37
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1894925332 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1227
Cdd:cd15726 1 WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKACF 58
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
243-1050 |
6.67e-29 |
|
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: 126.32 E-value: 6.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 243 EVREKQLR---ERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCL 319
Cdd:TIGR02168 221 ELRELELAllvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 320 QGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPSDAAQE 399
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 400 MQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQ-LKEDARASLERLVK-EMAPLQEELSGKGQEADQLWRRLQELL 477
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 478 AHTSSweeeLAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLER-- 555
Cdd:TIGR02168 461 EALEE----LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGye 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 556 ----LAGPPGPELPVAGEKNEALVPVNSSLQEAWGK------PEEEQRGLQEAQLDDTKVQEGSQE--EELRQANRELEK 623
Cdd:TIGR02168 537 aaieAALGGRLQAVVVENLNAAKKAIAFLKQNELGRvtflplDSIKGTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRK 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 624 ELQNVVGRNQLLEGKLQALQadyqalQQRESAIQGSLASLEAEQASIRHL----GDQMEASLLA-------VRKAKEAMK 692
Cdd:TIGR02168 617 ALSYLLGGVLVVDDLDNALE------LAKKLRPGYRIVTLDGDLVRPGGVitggSAKTNSSILErrreieeLEEKIEELE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 693 AQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptDNEARELAAQLA 772
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL------SKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 773 LSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLkeqnealnrahvQELLQCSERE 852
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL------------RERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 853 GALQEERADEAQQREEELRALQEELSqakcsseeaqLEHAELQEQLhrantdtAELGIQVCALTVEKERVEEALAcavqE 932
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLA----------AEIEELEELI-------EELESELEALLNERASLEEALA----L 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 933 LQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIM 1012
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQ----------LELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961
|
810 820 830
....*....|....*....|....*....|....*...
gi 1894925332 1013 DYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLK 1050
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELK 999
|
|
| FYVE |
pfam01363 |
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ... |
1169-1232 |
4.19e-25 |
|
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.
Pssm-ID: 426221 [Multi-domain] Cd Length: 68 Bit Score: 99.76 E-value: 4.19e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925332 1169 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVL---SKHGGKKERCCRACFQKLSE 1232
Cdd:pfam01363 2 VWVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISllpELGSNKPVRVCDACYDTLQK 68
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
402-1144 |
7.98e-25 |
|
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: 112.84 E-value: 7.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 402 ELGEKLQALERERTKVEEVnRQQSAQLEQLVKELQLKEdarasLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTS 481
Cdd:TIGR02168 197 ELERQLKSLERQAEKAERY-KELKAELRELELALLVLR-----LEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 482 SWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPG 561
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 562 PELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQ------EAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQ-L 634
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRskvaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 635 LEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLRE 714
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 715 EVEQCQQLA----------EARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELA---------AQLALSQ 775
Cdd:TIGR02168 511 LLKNQSGLSgilgvlseliSVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTflpldsikgTEIQGND 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 776 AQLEVHQGEVQRLQAQVVDLQAKMRAALDD-------QDKVQSQLSMAEAvLREHKTLV---------------QQLKEQ 833
Cdd:TIGR02168 591 REILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKK-LRPGYRIVtldgdlvrpggvitgGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 834 NEALNRAhvQELLQCsEREGALQEERADEAQQR----EEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELG 909
Cdd:TIGR02168 670 SSILERR--REIEEL-EEKIEELEEKIAELEKAlaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 910 IQVCALTVEKERVE---EALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAE 986
Cdd:TIGR02168 747 ERIAQLSKELTELEaeiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 987 QRAQSLQEAAHQELNTLKFQ---LSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCT 1063
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQieeLSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1064 SNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVtnrERNDQKMLADLDDLNRTKKYLEERLIE 1143
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA---EALENKIEDDEEEARRRLKRLENKIKE 983
|
.
gi 1894925332 1144 L 1144
Cdd:TIGR02168 984 L 984
|
|
| FYVE |
smart00064 |
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ... |
1169-1231 |
2.29e-24 |
|
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.
Pssm-ID: 214499 [Multi-domain] Cd Length: 68 Bit Score: 97.50 E-value: 2.29e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925332 1169 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGG--KKERCCRACFQKLS 1231
Cdd:smart00064 3 HWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGieRPVRVCDDCYENLN 67
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
589-1099 |
6.08e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.48 E-value: 6.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 589 EEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQA 668
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 669 SIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEV-EQCQQLAEARHRELRALESQCQQQTQLIEVL 747
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 748 TAEKGQQgvgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAqvvdLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLV 827
Cdd:COG1196 407 EAEEALL------ERLERLEEELEELEEALAELEEEEEEEEEA----LEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 828 QQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQ-AKCSSEEAQLEHAELQEQLHRANTDTA 906
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVlIGVEAAYEAALEAALAAALQNIVVEDD 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 907 ELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAE 986
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 987 QRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEEcKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNH 1066
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL-LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
490 500 510
....*....|....*....|....*....|...
gi 1894925332 1067 LAECQAAMLRKDKEGAALREDLERTQKELEKAT 1099
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
226-963 |
5.47e-21 |
|
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: 100.52 E-value: 5.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 226 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERgrtaaedNVRLTCLVAELQKQWEVT 305
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE-------LYALANEISRLEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 306 QATQNTVKELQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDT 385
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 386 KGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLE---------QLVKELQLKEDARASLERLVKEMAPLQ 456
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkelqaELEELEEELEELQEELERLEEALEELR 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 457 EELSGKGQEADQLWRRLQEL---LAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQF-------LETQLAQVS 526
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVdegyeaaIEAALGGRL 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 527 QH--VSDLEEQKKQLIQDKDHLSQQVGML---------------ERLAGPPG------------PELPVAGEKNEALVPV 577
Cdd:TIGR02168 548 QAvvVENLNAAKKAIAFLKQNELGRVTFLpldsikgteiqgndrEILKNIEGflgvakdlvkfdPKLRKALSYLLGGVLV 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 578 NSSLQEAWGKPEEEQRGLQEAQLDDTKV-----------------QEGSQE--------EELRQANRELEKELQNVVGRN 632
Cdd:TIGR02168 628 VDDLDNALELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssiLERRREieeleekiEELEEKIAELEKALAELRKEL 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 633 QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQL 712
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 713 REEVEQCQQLAEARHRELRALESQCQQQTqlIEVLTAEKGQQGVgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAQV 792
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLN--EEAANLRERLESL----ERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 793 VDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRaHVQELlqcserEGALQEERADEAQQREEELRA 872
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES-KRSEL------RRELEELREKLAQLELRLEGL 934
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 873 LQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEaasrEREGLERQVA 952
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKE----RYDFLTAQKE 1010
|
810
....*....|.
gi 1894925332 953 GLQQEKESLQE 963
Cdd:TIGR02168 1011 DLTEAKETLEE 1021
|
|
| RUN |
cd17671 |
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ... |
14-164 |
5.06e-20 |
|
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new molecule containing SH3 at the carboxyl-terminus), is a less conserved protein motif that comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases. RUN domains are often found in proteins linked particularly to the functions of GTPases in the Rap and Rab families, suggesting the RUN domain may be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. RUN domain-containing proteins could hence play important roles in multiple Ras-like GTPase signalling pathways.
Pssm-ID: 439038 Cd Length: 154 Bit Score: 88.25 E-value: 5.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 14 IRDLQDAVTELSKEFQEAGEPITDDSTSLHKFSYKLEYLLQFDQKEKAtLLGNKKDYWDYFCACLAKVKGANDG--IRFV 91
Cdd:cd17671 3 VKELLESFADNGEADDSAALTLTDDDPVVGRLCAALEAILSHGLKPKR-FGGGKVSFWDFLEALEKLLPAPSLKqaIRDI 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925332 92 KSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLQPKLSSDIVGQLYELTEVQFDL 164
Cdd:cd17671 82 NSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRDPEEAELFLSLLVGLSSLDFNL 154
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
400-1102 |
3.05e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.62 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 400 MQELGEKLQALERERTKVEEVnRQQSAQLEQLVKELQLKEDARaslerlvkemapLQEELSGKGQEADQLWRRLQELLAH 479
Cdd:COG1196 195 LGELERQLEPLERQAEKAERY-RELKEELKELEAELLLLKLRE------------LEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 480 TSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQvgmlerlagp 559
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE---------- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 560 pgpelpvAGEKNEALVPVNSSLQEAwgkpeEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQnvvgRNQLLEGKL 639
Cdd:COG1196 332 -------LEELEEELEELEEELEEA-----EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE----ELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 640 QALQADYQALQQRESAIQGSLASLEAEQASIrhlgdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 719
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEEL-------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 720 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKM 799
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 800 RAALDDQDKVQSQlsmAEAVLREHKtlvqQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQ 879
Cdd:COG1196 549 QNIVVEDDEVAAA---AIEYLKAAK----AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 880 AkcssEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALAcAVQELQDAKEAASREREGLERQVAGLQQEKE 959
Cdd:COG1196 622 L----LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG-SRRELLAALLEAEAELEELAERLAEEELELE 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 960 SLQEKLKAAKAAagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEEckslrgqlEEQGRQL 1039
Cdd:COG1196 697 EALLAEEEEERE------LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE--------LPEPPDL 762
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1894925332 1040 QAAEEAVEKLKATQADMGeklscTSNHLAECQAAMLRKDKEG-AALREDLERTQKELEKATTKI 1102
Cdd:COG1196 763 EELERELERLEREIEALG-----PVNLLAIEEYEELEERYDFlSEQREDLEEARETLEEAIEEI 821
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
247-861 |
2.37e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.54 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 247 KQLRERMQQLDREnqELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCLQGLELGA 326
Cdd:COG1196 216 RELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 327 AEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASfpgwlamAQQKADTASDtkgrqepipsDAAQEMQELGEK 406
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE-------LEEELEELEE----------ELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 407 LQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEE 486
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 487 LAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQqvgMLERLAGPPGPELPV 566
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE---AEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 567 AGEKNEALVPVNSSLQEAWGK------PEEEQRGLQEAQLDDTKVQEGSQEEELRQ---------ANRELEKELQNVVGR 631
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAayeaalEAALAAALQNIVVEDDEVAAAAIEYLKAAkagratflpLDKIRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 632 NQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQ 711
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 712 LREEVEQCQQLAEARHRELRALESQCQQQTQLIEvltaekgqqgvgpptdnEARELAAQLALSQAQLEVHQGEVQRLQAQ 791
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEER-----------------ELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925332 792 VVDLQAKMRAALDDQDKVQSQLSMAEAVLREHktlVQQLKEQNEAL---NRAHVQELLQCSEREGALQEERAD 861
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERE---LERLEREIEALgpvNLLAIEEYEELEERYDFLSEQRED 806
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
820-1166 |
3.80e-18 |
|
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: 91.27 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 820 LREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLH 899
Cdd:TIGR02168 205 LERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 900 RANTDTAELGIQVCALTVEKERVEEALacavQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQ 979
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERL----ANLERQLEELEAQLEELESKLDELAEELAELEEKLEE----------LK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 980 AQLAQAEQRAQSLqEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEK 1059
Cdd:TIGR02168 351 EELESLEAELEEL-EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1060 LS-----CTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLcQEVTNRERNDQKMLADLDDLNRTK 1134
Cdd:TIGR02168 430 LEeaelkELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL-AQLQARLDSLERLQENLEGFSEGV 508
|
330 340 350
....*....|....*....|....*....|..
gi 1894925332 1135 KYLEERLIELLRDKDALWQKsdaLEFQQKLSA 1166
Cdd:TIGR02168 509 KALLKNQSGLSGILGVLSEL---ISVDEGYEA 537
|
|
| FYVE_like_SF |
cd00065 |
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ... |
1178-1227 |
6.95e-18 |
|
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.
Pssm-ID: 277249 [Multi-domain] Cd Length: 52 Bit Score: 78.73 E-value: 6.95e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1894925332 1178 HCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKH--GGKKERCCRACF 1227
Cdd:cd00065 1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSfgSGKPVRVCDSCY 52
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
284-961 |
2.76e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.07 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 284 AAEDN-VRLTCLVAELQKQWEV--TQATQ-NTVKELQTCLQGLELGAAEKE-EDYHTALRRLESMLQPLAQELEATRDSL 358
Cdd:COG1196 183 ATEENlERLEDILGELERQLEPleRQAEKaERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 359 DKKNQHLASfpgwLAMAQQKADTASDTKGrqepipsdaaQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQL- 437
Cdd:COG1196 263 AELEAELEE----LRLELEELELELEEAQ----------AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEl 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 438 ---KEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAelrrekkqqqeekelleqevrSLTRQ 514
Cdd:COG1196 329 eeeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE---------------------ELAEE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 515 LQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLsqqvgmlerlagppgpelpvageknealvpvnsslqeawgkpEEEQRG 594
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERL------------------------------------------EEELEE 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 595 LQEAQLddtkvQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLG 674
Cdd:COG1196 426 LEEALA-----ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 675 DQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALEsqcqqqtQLIEVLTAEKGQQ 754
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA-------AAIEYLKAAKAGR 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 755 GVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQN 834
Cdd:COG1196 574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 835 EALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKcSSEEAQLEHAELQEQLHRANTDTAELGIQVCA 914
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL-AEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1894925332 915 LTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESL 961
Cdd:COG1196 733 EREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| FYVE_PIKfyve_Fab1 |
cd15725 |
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ... |
1170-1228 |
2.93e-17 |
|
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, also termed FYVE finger-containing phosphoinositide kinase, or 1-phosphatidylinositol 3-phosphate 5-kinase, or phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase), is a phosphoinositide 5-kinase that forms a complex with its regulators, the scaffolding protein Vac14 and the lipid phosphatase Fig4. The complex is responsible for synthesizing phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2] from phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). Then phosphatidylinositol-5-phosphate (PtdIns5P) is generated directly from PtdIns(3,5)P2. PtdIns(3,5)P2 and PtdIns5P regulate endosomal trafficking and responses to extracellular stimuli. At this point, PIKfyve is vital in early embryonic development. Moreover, PIKfyve forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, which plays a role in receptor tyrosine kinase (RTK) degradation. The phosphorylation of PIKfyve by AKT can facilitate Epidermal growth factor receptor (EGFR) degradation. In addition, PIKfyve may participate in the regulation of the glutamate transporters EAAT2, EAAT3 and EAAT4, and the cystic fibrosis transmembrane conductance regulator (CFTR). It is also essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle. It can be activated by protein kinase B (PKB/Akt) and further up-regulates human ether-a-go-go (hERG) channels. This family also includes the yeast and plant orthologs of human PIKfyve, Fab1. PIKfyve and its orthologs share a similar architecture. They contain an N-terminal FYVE domain, a middle region related to the CCT/TCP-1/Cpn60 chaperonins that are involved in productive folding of actin and tubulin, a second middle domain that contains a number of conserved cysteine residues (CCR) unique to this family, and a C-terminal lipid kinase domain related to PtdInsP kinases.
Pssm-ID: 277264 [Multi-domain] Cd Length: 62 Bit Score: 76.98 E-value: 2.93e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925332 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE--RCCRACFQ 1228
Cdd:cd15725 2 WMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGdlRVCTYCCK 62
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
689-1061 |
3.62e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.68 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 689 EAMKAQMAEKEAILQSKEGECQQLREEVEQcqqlAEaRHRELRALESQCQQQTQLIEVLTAEKgqqgvgpptdnEARELA 768
Cdd:COG1196 182 EATEENLERLEDILGELERQLEPLERQAEK----AE-RYRELKEELKELEAELLLLKLRELEA-----------ELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 769 AQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlrEHKTLVQQLKEQNEALNRAHVQEllqc 848
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA---ELARLEQDIARLEERRRELEERL---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 849 sEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAelgiqvcaltvEKERVEEALAC 928
Cdd:COG1196 319 -EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA-----------EAEEELEELAE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 929 AVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKfQLS 1008
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE----------LEEALAELEEEEEEEEEALEEAAEEEA-ELE 455
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1894925332 1009 AEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLS 1061
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| FYVE_EEA1 |
cd15730 |
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ... |
1169-1227 |
4.57e-17 |
|
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed endosome-associated protein p162, or zinc finger FYVE domain-containing protein 2, is an essential component of the endosomal fusion machinery and required for the fusion and maturation of early endosomes in endocytosis. It forms a parallel coiled-coil homodimer in cells. EEA1 serves as the p97 ATPase substrate and the p97 ATPase may regulate the size of early endosomes by governing the oligomeric state of EEA1. It can interact with the GTP-bound form of Rab22a and be involved in endosomal membrane trafficking. EEA1 also functions as an obligate scaffold for angiotensin II-induced Akt activation in early endosomes. It can be phosphorylated by p38 mitogen-activated protein kinase (MAPK) and further regulate mu opioid receptor endocytosis. EEA1 consists of an N-terminal C2H2 Zn2+ finger, four long heptad repeats, and a C-terminal region containing a calmodulin binding (IQ) motif, a Rab5 interaction site, and a FYVE domain. This model corresponds to the FYVE domain that is responsible for binding phosphatidyl inositol-3-phosphate (PtdIns3P or PI3P) on the membrane.
Pssm-ID: 277269 [Multi-domain] Cd Length: 63 Bit Score: 76.67 E-value: 4.57e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1894925332 1169 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1227
Cdd:cd15730 2 KWADDEEVQNCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDACF 60
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
821-1140 |
9.95e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.14 E-value: 9.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 821 REHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELsqakcssEEAQLEHAELQEQLHR 900
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL-------EELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 901 ANTDTAELGIQVCALTVEKERVEEALacavQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSlpgLQA 980
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE---AEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 981 QLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKL 1060
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELE-ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1061 SCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLcQEVTNRERNDQKMLADLDDLNRTKKYLEER 1140
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL-AEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
402-1141 |
6.47e-16 |
|
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: 83.96 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 402 ELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQL-KEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAht 480
Cdd:TIGR02169 195 EKRQQLERLRREREKAERYQALLKEKREYEGYELLKeKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ-- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 481 ssweEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLI-------QDKDHLSQQVGML 553
Cdd:TIGR02169 273 ----LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEaeidkllAEIEELEREIEEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 554 ERLAGPPGPELPVAGEKNEALV----PVNSSLQEAWGKPEEEQRGLQEAQ------------LDDTKVQEGSQEEELRQA 617
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRaeleEVDKEFAETRDELKDYREKLEKLKreinelkreldrLQEELQRLSEELADLNAA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 618 -------NRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEA 690
Cdd:TIGR02169 429 iagieakINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 691 MKAQMAEKEAILQSKEGecqqlreeveQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGV--------GPPTDN 762
Cdd:TIGR02169 509 GRAVEEVLKASIQGVHG----------TVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIellkrrkaGRATFL 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 763 EARELAAQLALSQAqleVHQGEVQRLQAQVVDLQAKMRAA----LDDQDKVQSqLSMAEAVLREHK--TLVQQLKEQNEA 836
Cdd:TIGR02169 579 PLNKMRDERRDLSI---LSEDGVIGFAVDLVEFDPKYEPAfkyvFGDTLVVED-IEAARRLMGKYRmvTLEGELFEKSGA 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 837 LNRAHVQ-------------ELLQCSEREGALQEERADEAQQREE---ELRALQEELSQAKCSSEEAQLEHAELQEQLHR 900
Cdd:TIGR02169 655 MTGGSRAprggilfsrsepaELQRLRERLEGLKRELSSLQSELRRienRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 901 ANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEK-ESLQEKLKAAKAAAGSLPGLQ 979
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARL 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 980 AQLAQAEQRAQSLQEAAHQELNTLKfqlsAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEK 1059
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQELQ----EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1060 LSCTSNHLAECQaamlRKDKEGAALREDLERTQKELeKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEE 1139
Cdd:TIGR02169 891 RDELEAQLRELE----RKIEELEAQIEKKRKRLSEL-KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
|
..
gi 1894925332 1140 RL 1141
Cdd:TIGR02169 966 EI 967
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
596-1151 |
8.52e-16 |
|
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: 83.57 E-value: 8.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 596 QEAQLDDTKVQEGSQEEELRQANREL---EKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRH 672
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELqelEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 673 LGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHR------------------------ 728
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrleeleeqletlrskvaqlelqia 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 729 ----ELRALESQCQQQTQLIEVLTAEKGQQGvGPPTDNEARELAAQLALS-------QAQLEVHQGEVQRLQAQVVDLQA 797
Cdd:TIGR02168 397 slnnEIERLEARLERLEDRRERLQQEIEELL-KKLEEAELKELQAELEELeeeleelQEELERLEEALEELREELEEAEQ 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 798 KMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAH-----VQELLQCSER-----EGALQE---------- 857
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSgilgvLSELISVDEGyeaaiEAALGGrlqavvvenl 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 858 ERADEAQQ------------------REEELRALQEELSQAKCSSEEAQLEHAELQEQLHRA------------NTDTA- 906
Cdd:TIGR02168 556 NAAKKAIAflkqnelgrvtflpldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvdDLDNAl 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 907 ELGIQ---------------------------VCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKE 959
Cdd:TIGR02168 636 ELAKKlrpgyrivtldgdlvrpggvitggsakTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 960 SLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGE---ECKSLRGQLEEQ- 1035
Cdd:TIGR02168 716 QLRKELEELSRQ---ISALRKDLARLEAEVEQLEERIAQLSKELT-ELEAEIEELEERLEEAEEelaEAEAEIEELEAQi 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1036 ----------GRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT---KI 1102
Cdd:TIGR02168 792 eqlkeelkalREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEElieEL 871
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1894925332 1103 QEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDAL 1151
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
|
| FYVE_LST2 |
cd15731 |
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ... |
1169-1227 |
1.60e-15 |
|
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; Lst2, also termed zinc finger FYVE domain-containing protein 28, is a monoubiquitinylated phosphoprotein that functions as a negative regulator of epidermal growth factor receptor (EGFR) signaling. Unlike other FYVE domain-containing proteins, Lst2 displays primarily non-endosomal localization. Its endosomal localization is regulated by monoubiquitinylation. Lst2 physically binds Trim3, also known as BERP or RNF22, which is a coordinator of endosomal trafficking and interacts with Hrs and a complex that biases cargo recycling.
Pssm-ID: 277270 [Multi-domain] Cd Length: 65 Bit Score: 72.38 E-value: 1.60e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925332 1169 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYC-CNNYVLSKHG-GKKERCCRACF 1227
Cdd:cd15731 4 LWVPDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCsSNSVPLPRYGqMKPVRVCNHCF 64
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
393-1123 |
2.41e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 81.94 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 393 PSDAAQEMQELgEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKED--------ARASLERLVKEMAPLQEELSGKGQ 464
Cdd:TIGR00618 162 SKEKKELLMNL-FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLctpcmpdtYHERKQVLEKELKHLREALQQTQQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 465 EADQLwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLetQLAQVSQHVSDLEEQKKQLIQDkd 544
Cdd:TIGR00618 241 SHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTE-- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 545 hLSQQVGMLERLAGPPGPELpvageKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLD--DTKVQEGSQEEELRQANRELE 622
Cdd:TIGR00618 316 -LQSKMRSRAKLLMKRAAHV-----KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSirEISCQQHTLTQHIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 623 KELQNVVGRNQLLEgKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASL---LAVRKAKEAMKAQMAEKE 699
Cdd:TIGR00618 390 TLTQKLQSLCKELD-ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAItctAQCEKLEKIHLQESAQSL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 700 AILQSKEGECQQLREEVEQCQQLAEARHRELRalESQCQQQTQLIEvLTAEKGQQGVGPPTDNEARELAAQLALSQAQLE 779
Cdd:TIGR00618 469 KEREQQLQTKEQIHLQETRKKAVVLARLLELQ--EEPCPLCGSCIH-PNPARQDIDNPGPLTRRMQRGEQTYAQLETSEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 780 VHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEER 859
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 860 ADeaQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRAntdtaelgiqvcALTVEKERVEEALACAVQELQDAKEA 939
Cdd:TIGR00618 626 DL--QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL------------SIRVLPKELLASRQLALQKMQSEKEQ 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 940 ASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQ-RAQSLQEAAHQELNTLKFQLSAEIMDYQSRL 1018
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDaLNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1019 --KNAGEECKSLRGQLEEQGRQLqaaEEAVEKLKATQADMGEKLsctsnhlaecQAAMLRKDKEGAALREDLERTQKELE 1096
Cdd:TIGR00618 772 aaLQTGAELSHLAAEIQFFNRLR---EEDTHLLKTLEAEIGQEI----------PSDEDILNLQCETLVQEEEQFLSRLE 838
|
730 740
....*....|....*....|....*..
gi 1894925332 1097 KATTKIQEYYNKLCQEVTNRERNDQKM 1123
Cdd:TIGR00618 839 EKSATLGEITHQLLKYEECSKQLAQLT 865
|
|
| FYVE_endofin |
cd15729 |
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ... |
1170-1230 |
1.09e-14 |
|
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE domain-containing protein 16 (ZFY16), or endosome-associated FYVE domain protein, is a FYVE domain-containing protein that is localized to EEA1-containing endosomes. It is regulated by phosphoinositol lipid and engaged in endosome-mediated receptor modulation. Endofin is involved in Bone morphogenetic protein (BMP) signaling through interacting with Smad1 preferentially and enhancing Smad1 phosphorylation and nuclear localization upon BMP stimulation. It also functions as a scaffold protein that brings Smad4 to the proximity of the receptor complex in Transforming growth factor (TGF)-beta signaling. Moreover, endofin is a novel tyrosine phosphorylation target downstream of epidermal growth factor receptor (EGFR) in EGF-signaling. In addition, endofin plays a role in endosomal trafficking by recruiting cytosolic TOM1, an important molecule for membrane recruitment of clathrin, onto endosomal membranes.
Pssm-ID: 277268 [Multi-domain] Cd Length: 68 Bit Score: 70.07 E-value: 1.09e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925332 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCN-NYVLSKHGGKKERCCRACFQKL 1230
Cdd:cd15729 7 WVPDSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSACCSlKARLEYLDNKEARVCVPCYQTL 68
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
567-1024 |
1.46e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.19 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 567 AGEKNEALVPV---NSSLQEAWgkpeeEQRGLQEAQLDDTKVQEGSQE-EELRQANRELEKELQNVVGRNQLLEGKLQAL 642
Cdd:COG4913 247 AREQIELLEPIrelAERYAAAR-----ERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 643 QADYQALQQRESAIQGS-LASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQ 721
Cdd:COG4913 322 REELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 722 LAEARHRELRALESQCQQQ-TQLIEVLTAEKGQQGVGPPTDNEAR-ELAAQLALSQAQL-------EVHQGEV------- 785
Cdd:COG4913 402 ALEEALAEAEAALRDLRRElRELEAEIASLERRKSNIPARLLALRdALAEALGLDEAELpfvgeliEVRPEEErwrgaie 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 786 -------------QRLQAQVVDL--QAKMRAALDDQdKVQSQLSMAEAVLREHKTLVQQLK-EQNEAlnRAHVQELLQ-- 847
Cdd:COG4913 482 rvlggfaltllvpPEHYAAALRWvnRLHLRGRLVYE-RVRTGLPDPERPRLDPDSLAGKLDfKPHPF--RAWLEAELGrr 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 848 ----CSEREGALQEER----------------------------------ADEAQQREEELRALQEELSQAKCSSEEAQL 889
Cdd:COG4913 559 fdyvCVDSPEELRRHPraitragqvkgngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEA 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 890 EHAELQEQLHRANT---------DTAELGIQVCALTVEKERVE------EALACAVQELQDAKEAASREREGLERQVAGL 954
Cdd:COG4913 639 ELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDassddlAALEEQLEELEAELEELEEELDELKGEIGRL 718
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925332 955 QQEKESLQEKLKAAKAAAGSLPGLQAQLAQA---EQRAQSLQEAAHQElntLKFQLSAEIMDYQSRLKNAGEE 1024
Cdd:COG4913 719 EKELEQAEEELDELQDRLEAAEDLARLELRAlleERFAAALGDAVERE---LRENLEERIDALRARLNRAEEE 788
|
|
| FYVE_RUFY1_like |
cd15721 |
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ... |
1170-1227 |
3.59e-14 |
|
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1 and RUFY2. RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. Both RUFY1 and RUFY2 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.
Pssm-ID: 277261 [Multi-domain] Cd Length: 58 Bit Score: 68.18 E-value: 3.59e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1894925332 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1227
Cdd:cd15721 1 WADDKEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
|
|
| FYVE_MTMR3 |
cd15732 |
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ... |
1169-1227 |
4.69e-14 |
|
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also termed Myotubularin-related phosphatase 3, or FYVE domain-containing dual specificity protein phosphatase 1 (FYVE-DSP1), or zinc finger FYVE domain-containing protein 10, is a ubiquitously expressed phosphoinositide 3-phosphatase specific for phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and PIKfyve, which produces PtdIns(3,5)P2 from PtdIns3P. It regulates cell migration through modulating phosphatidylinositol 5-phosphate (PtdIns5P) levels. MTMR3 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain. Unlike conventional FYVE domains, the FYVE domain of MTMR3 neither confers endosomal localization nor binds to PtdIns3P. It is also not required for the enzyme activity of MTMR3. In contrast, the PH-G domain binds phosphoinositides.
Pssm-ID: 277271 [Multi-domain] Cd Length: 61 Bit Score: 68.00 E-value: 4.69e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925332 1169 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNN--YVLSKHGGKKERCCRACF 1227
Cdd:cd15732 1 RWVPDHLAASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQklPVPSQQLFEPSRVCKSCF 61
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
228-1145 |
6.93e-14 |
|
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: 77.03 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 228 ALEGFDEMRLELDQLEVREKQLRERMQQLdrenqelraavsqQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQA 307
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKRQQLERL-------------RREREKAERYQALLKEKREYEGYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 308 TQNTVKELQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKnqhLASFPGWLAMAQQKADtasdtkg 387
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK---IGELEAEIASLERSIA------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 388 rqepipsDAAQEMQELGEKLQALERERTKVEEvnrqqsaQLEQLVKELqlkedaraslERLVKEMAPLQEELSGKGQEAD 467
Cdd:TIGR02169 312 -------EKERELEDAEERLAKLEAEIDKLLA-------EIEELEREI----------EEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 468 QLWRRLQELLAHTSSWEeelaelrREKKQQQEEKELLEQEVRSLTRQ-------LQFLETQLAQVSQHVSDLEEQKKQLI 540
Cdd:TIGR02169 368 DLRAELEEVDKEFAETR-------DELKDYREKLEKLKREINELKREldrlqeeLQRLSEELADLNAAIAGIEAKINELE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 541 QDKDHLSQQVGMLERlagppgpELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQE--AQLDDTKVQEGSQEEELRQAN 618
Cdd:TIGR02169 441 EEKEDKALEIKKQEW-------KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRelAEAEAQARASEERVRGGRAVE 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 619 RELEKELQNVVGrnqlLEGKLQALQADYQAlqQRESAIQGSLASLEAE-----QASIRHLGDQM--EASLLAVRKakeaM 691
Cdd:TIGR02169 514 EVLKASIQGVHG----TVAQLGSVGERYAT--AIEVAAGNRLNNVVVEddavaKEAIELLKRRKagRATFLPLNK----M 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 692 KAQMAEKEAIlqSKEGECQQLREEVEQCQQLAEA------------RHRELRALESQCQQQTQLIEVL----------TA 749
Cdd:TIGR02169 584 RDERRDLSIL--SEDGVIGFAVDLVEFDPKYEPAfkyvfgdtlvveDIEAARRLMGKYRMVTLEGELFeksgamtggsRA 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 750 EKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEavlREHKTLVQQ 829
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE---QEEEKLKER 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 830 LKEQnealnRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELsqakcSSEEAQLEHAELQeqlhrantdtaELG 909
Cdd:TIGR02169 739 LEEL-----EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL-----NDLEARLSHSRIP-----------EIQ 797
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 910 IQVCALTVEKERVEEALACAVQELQD---AKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAE 986
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRltlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN----------LNGKKEELE 867
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 987 QRAQSLQeaahqelntlkfqlsAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNH 1066
Cdd:TIGR02169 868 EELEELE---------------AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1067 LAECQAAmLRKDKEGAALREDLERTQKELEKATTKIQEYynklcQEVTNRERND-QKMLADLDDLNRTKKYLEERLIELL 1145
Cdd:TIGR02169 933 LSEIEDP-KGEDEEIPEEELSLEDVQAELQRVEEEIRAL-----EPVNMLAIQEyEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
227-779 |
7.79e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.90 E-value: 7.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 227 EALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQ 306
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 307 ATQNTVKELQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFpgwLAMAQQKADTASDTK 386
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL---AAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 387 GRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEA 466
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 467 DQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTrqlqfLETQLAQVSQH-VSDLEEQKKQLIQDkdh 545
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA-----LEAALAAALQNiVVEDDEVAAAAIEY--- 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 546 lsqqvgmLERLAGPPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRElekel 625
Cdd:COG1196 566 -------LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE----- 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 626 qNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLgdQMEASLLAVRKAKEAMKAQMAEKEAILQSK 705
Cdd:COG1196 634 -AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE--LEELAERLAEEELELEEALLAEEEEERELA 710
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1894925332 706 EGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkgqqgvgPPTDNEARELAAQLALSQAQLE 779
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE-------LPEPPDLEELERELERLEREIE 777
|
|
| FYVE_MTMR4 |
cd15733 |
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ... |
1170-1227 |
1.51e-13 |
|
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also termed FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2), or zinc finger FYVE domain-containing protein 11, is an dual specificity protein phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). It is localizes to early endosomes, as well as to Rab11- and Sec15-positive recycling endosomes, and regulates sorting from early endosomes. Moreover, MTMR4 is preferentially associated with and dephosphorylated the activated regulatory Smad proteins (R-Smads) in cytoplasm to keep transforming growth factor (TGF) beta signaling in homeostasis. It also functions as an essential negative modulator for the homeostasis of bone morphogenetic protein (BMP)/decapentaplegic (Dpp) signaling. In addition, MTMR4 acts as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4) and may play a role in the biological process of muscle breakdown. MTMR4 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain.
Pssm-ID: 277272 [Multi-domain] Cd Length: 60 Bit Score: 66.69 E-value: 1.51e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925332 1170 WLGDTEANHCLDCKREFsWMV-RRHHCRICGRIFCYYCCNnyvlSKHGGKKE------RCCRACF 1227
Cdd:cd15733 1 WVPDHAASHCFGCDCEF-WLAkRKHHCRNCGNVFCADCSN----YKLPIPDEqlydpvRVCNSCY 60
|
|
| FYVE_ZF21 |
cd15727 |
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ... |
1167-1212 |
1.56e-13 |
|
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ZF21 is phosphoinositide-binding protein that functions as a regulator of focal adhesions and cell movement through interaction with focal adhesion kinase. It can also bind to the cytoplasmic tail of membrane type 1 matrix metalloproteinase, a potent invasion-promoting protease, and play a key role in regulating multiple aspects of cancer cell migration and invasion. ZF21 contains a FYVE domain, which corresponds to this model.
Pssm-ID: 277266 [Multi-domain] Cd Length: 64 Bit Score: 66.63 E-value: 1.56e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1894925332 1167 EERWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVL 1212
Cdd:cd15727 1 EPPWVPDKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVP 46
|
|
| RUN_RUFY1_like |
cd17681 |
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ... |
20-135 |
3.28e-13 |
|
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1, RUFY2, and RUFY3. RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. RUFY1, RUFY2, and RUFY3 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.
Pssm-ID: 439043 Cd Length: 155 Bit Score: 68.75 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 20 AVTELS-KEFQEA----GEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSI 94
Cdd:cd17681 7 NLAKLSiKELIESalsfGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEITASVRDL 86
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1894925332 95 SELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWY 135
Cdd:cd17681 87 PGIKTPLGRARAWLRLALMQKKLADYFRALIENKDLLSEFY 127
|
|
| FYVE_scVPS27p_like |
cd15760 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1175-1227 |
7.99e-13 |
|
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and similar proteins; scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif.
Pssm-ID: 277299 [Multi-domain] Cd Length: 59 Bit Score: 64.63 E-value: 7.99e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925332 1175 EANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYV-LSKHGGKKERC--CRACF 1227
Cdd:cd15760 4 PDSRCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIpLPHLGPLGVPQrvCDRCF 59
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
511-1167 |
8.49e-13 |
|
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: 73.56 E-value: 8.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 511 LTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLagppgpelpvagekneaLVPVNSSLQEawgKPEE 590
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL-----------------LEELNKKIKD---LGEE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 591 EQRGLQEaQLDDTKVQEGSQEEELRQANRELEKelqnvvgrnqlLEGKLQALQADYqalqqreSAIQGSLASLEAEQASI 670
Cdd:TIGR02169 288 EQLRVKE-KIGELEAEIASLERSIAEKERELED-----------AEERLAKLEAEI-------DKLLAEIEELEREIEEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 671 RHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAE 750
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 751 -KGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQ 829
Cdd:TIGR02169 429 iAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 830 LKEQNEALNR------AHVQELLQCSERE---------GALQ------EERADEAQQREEE----------LRALQEELS 878
Cdd:TIGR02169 509 GRAVEEVLKAsiqgvhGTVAQLGSVGERYataievaagNRLNnvvvedDAVAKEAIELLKRrkagratflpLNKMRDERR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 879 QAKCSSEEAQLEHA----ELQEQLHRA------------NTDTA-ELGIQVCALTVEKERVE-----------EALACAV 930
Cdd:TIGR02169 589 DLSILSEDGVIGFAvdlvEFDPKYEPAfkyvfgdtlvveDIEAArRLMGKYRMVTLEGELFEksgamtggsraPRGGILF 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 931 QELQDAKEAASRER-EGLERQVAGLQQEKESLQ----EKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHqelntlkf 1005
Cdd:TIGR02169 669 SRSEPAELQRLRERlEGLKRELSSLQSELRRIEnrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE-------- 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1006 QLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADmgEKLSCTSNHLAECQAAMLRKDKEGAALR 1085
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1086 EDLERTQKELEKATTKIQEYYNKL----------CQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDAL-WQK 1154
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRidlkeqiksiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELeAQL 898
|
730
....*....|...
gi 1894925332 1155 SDALEFQQKLSAE 1167
Cdd:TIGR02169 899 RELERKIEELEAQ 911
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
395-1019 |
1.30e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 395 DAAQEMQELgekLQALERERTKVEEVnRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQeelsgkgqeadqLWRRLQ 474
Cdd:COG4913 225 EAADALVEH---FDDLERAHEALEDA-REQIELLEPIRELAERYAAARERLAELEYLRAALR------------LWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 475 ELLAhtssWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVS-QHVSDLEEQKKQLIQDKDHLSQQVGML 553
Cdd:COG4913 289 RLEL----LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 554 ERLAGPPGPELPVAGEKNEALVPVNSSLQEAWgkpeEEQRGLQEAQLDDTKVqegsQEEELRQANRELEKELQNVVGRNQ 633
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAALLEAL----EEELEALEEALAEAEA----ALRDLRRELRELEAEIASLERRKS 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 634 LLEGKLQALQADY-QALQQRES--------------------AIQGSLASL------EAEQAS-----IRHLGDQMEASL 681
Cdd:COG4913 437 NIPARLLALRDALaEALGLDEAelpfvgelievrpeeerwrgAIERVLGGFaltllvPPEHYAaalrwVNRLHLRGRLVY 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 682 LAVRKAKEAMKAQMAEKEAI---LQSKEGECQQ-LREEVEQ-----CQQLAEARHRELRALESQCQ--QQTQLievltAE 750
Cdd:COG4913 517 ERVRTGLPDPERPRLDPDSLagkLDFKPHPFRAwLEAELGRrfdyvCVDSPEELRRHPRAITRAGQvkGNGTR-----HE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 751 KGQQGVGPPT-----DNEAR--ELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKmRAALDDQDKVQSQLSMAEAVLREh 823
Cdd:COG4913 592 KDDRRRIRSRyvlgfDNRAKlaALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVASAERE- 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 824 ktlVQQLKEQNEALNRAHvQELLQCSEREGALQEERaDEAQQREEELRALQEELSQAKcssEEAQLEHAELQEQLHRANT 903
Cdd:COG4913 670 ---IAELEAELERLDASS-DDLAALEEQLEELEAEL-EELEEELDELKGEIGRLEKEL---EQAEEELDELQDRLEAAED 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 904 DTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQE-KESLQEKLKAAKAAAGSLPGLQAQL 982
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALL 821
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1894925332 983 AQ--------AEQR-AQSLQEAAHQELNTLKFQLSAEIMDYQSRLK 1019
Cdd:COG4913 822 DRleedglpeYEERfKELLNENSIEFVADLLSKLRRAIREIKERID 867
|
|
| FYVE_Hrs |
cd15720 |
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ... |
1174-1230 |
1.37e-12 |
|
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) and similar proteins; Hrs, also termed protein pp110, is a tyrosine phosphorylated protein that plays an important role in the signaling pathway of HGF. It is localized to early endosomes and an essential component of the endosomal sorting and trafficking machinery. Hrs interacts with hypertonia-associated protein Trak1, a novel regulator of endosome-to-lysosome trafficking. It can also forms an Hrs/actinin-4/BERP/myosin V protein complex that is required for efficient transferrin receptor (TfR) recycling but not for epidermal growth factor receptor (EGFR) degradation. Moreover, Hrs, together with STAM proteins, STAM1 and STAM2, and EPs15, forms a multivalent ubiquitin-binding complex that sorts ubiquitinated proteins into the multivesicular body pathway, and plays a regulatory role in endocytosis/exocytosis. Furthermore, Hrs functions as an interactor of the neurofibromatosis 2 tumor suppressor protein schwannomin/merlin. It is also involved in the inhibition of citron kinase-mediated HIV-1 budding. Hrs contains a single ubiquitin-interacting motif (UIM) that is crucial for its function in receptor sorting, and a FYVE domain that harbors double Zn2+ binding sites.
Pssm-ID: 277260 [Multi-domain] Cd Length: 61 Bit Score: 63.94 E-value: 1.37e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1894925332 1174 TEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNY-VLSKHGGKKE-RCCRACFQKL 1230
Cdd:cd15720 3 KDGDECHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSsTIPKFGIEKEvRVCDPCYEKL 61
|
|
| FYVE_RUFY1 |
cd15758 |
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ... |
1170-1226 |
1.43e-12 |
|
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.
Pssm-ID: 277297 [Multi-domain] Cd Length: 71 Bit Score: 64.32 E-value: 1.43e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925332 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRAC 1226
Cdd:cd15758 6 WLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSC 62
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
861-1168 |
1.50e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 861 DEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEealacaVQELQDAKEAA 940
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE------LEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 941 SREREGLERQVAGLQQEKESLQEKLkaakaaagslpglqAQLAQAEQRAQSLQEAAHQELNTLKfqlsAEIMDYQSRLKN 1020
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERL--------------EELEEELAELEEELEELEEELEELE----EELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1021 AGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT 1100
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1894925332 1101 KIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEE 1168
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
619-1183 |
1.76e-12 |
|
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: 72.46 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 619 RELEKELQNVVGRNQLLEGKLQALQADYQ-----ALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKA 693
Cdd:pfam15921 227 RELDTEISYLKGRIFPVEDQLEALKSESQnkielLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 694 QMAEKEAI----LQSKEGECQQLREEVEQCQQLAEARHRELRalESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAA 769
Cdd:pfam15921 307 QARNQNSMymrqLSDLESTVSQLRSELREAKRMYEDKIEELE--KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 770 -------QLALSQAQ---------------------LEVHQGEVQRLQAQVVDLQAKMRAALDDQdkvQSQLSMAEAVLR 821
Cdd:pfam15921 385 dlhkrekELSLEKEQnkrlwdrdtgnsitidhlrreLDDRNMEVQRLEALLKAMKSECQGQMERQ---MAAIQGKNESLE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 822 EHKTLVQQLKEQNEALnRAHVQEL------LQCSERE-----GALQE-ERADEAQQRE------------EELRALQEE- 876
Cdd:pfam15921 462 KVSSLTAQLESTKEML-RKVVEELtakkmtLESSERTvsdltASLQEkERAIEATNAEitklrsrvdlklQELQHLKNEg 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 877 --LSQAKCSSEEAQLEHAE-------LQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQ------DAKEAAS 941
Cdd:pfam15921 541 dhLRNVQTECEALKLQMAEkdkvieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQefkilkDKKDAKI 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 942 REregLERQVAGLQQEKESLqeklkaakAAAGSlPGLQAQLAQAEQRAQSLQEA--AHQELNTLkfqlSAEIMDYQSRLK 1019
Cdd:pfam15921 621 RE---LEARVSDLELEKVKL--------VNAGS-ERLRAVKDIKQERDQLLNEVktSRNELNSL----SEDYEVLKRNFR 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1020 NAGEECKSLRGQLEeqgRQLQAAEEAVEKLKATQADMgeklSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKAT 1099
Cdd:pfam15921 685 NKSEEMETTTNKLK---MQLKSAQSELEQTRNTLKSM----EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1100 TK-------IQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERL--IELLRDKDALwQKSDALEFQQKLSAEERW 1170
Cdd:pfam15921 758 TNankekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVanMEVALDKASL-QFAECQDIIQRQEQESVR 836
|
650
....*....|...
gi 1894925332 1171 LgdtEANHCLDCK 1183
Cdd:pfam15921 837 L---KLQHTLDVK 846
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
611-995 |
3.20e-12 |
|
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: 71.64 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 611 EEELRQANRELEKELQNVvGRNQLLEG----KLQALQAD------YQALQQRESAIQGSLASLEaeqasirhlgdqmeas 680
Cdd:TIGR02169 169 DRKKEKALEELEEVEENI-ERLDLIIDekrqQLERLRRErekaerYQALLKEKREYEGYELLKE---------------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 681 LLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQlievltaekgqqgvgppt 760
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK------------------ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 761 dNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAkmraaldDQDKVQSQLSMAEAVLREHKTLVQQLKEqnEALNRA 840
Cdd:TIGR02169 294 -EKIGELEAEIASLERSIAEKERELEDAEERLAKLEA-------EIDKLLAEIEELEREIEEERKRRDKLTE--EYAELK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 841 HVQELLQCSeregaLQEERADEAQQREEeLRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQvcaLTVEKE 920
Cdd:TIGR02169 364 EELEDLRAE-----LEEVDKEFAETRDE-LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA---IAGIEA 434
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925332 921 RVEEaLACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQEA 995
Cdd:TIGR02169 435 KINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKE---LSKLQRELAEAEAQARASEER 505
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
219-1096 |
3.44e-12 |
|
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: 71.69 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 219 DLNSPLNNEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQT---ERERGRTAAEDNVRltclv 295
Cdd:pfam15921 60 ELDSPRKIIAYPGKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTklqEMQMERDAMADIRR----- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 296 AELQKQWEVTQATQNTVKELQT--CLQGLELGAAEKE-EDYHTALRRLESMLQPLAQELEATRDSLDKK--------NQH 364
Cdd:pfam15921 135 RESQSQEDLRNQLQNTVHELEAakCLKEDMLEDSNTQiEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmsTMH 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 365 LASFPGWLAMAQQKADTA-SDTKGRQEPIPsdaaqemqelgEKLQALERE-RTKVEEVNRQQSAQLEQLVKELQLK---- 438
Cdd:pfam15921 215 FRSLGSAISKILRELDTEiSYLKGRIFPVE-----------DQLEALKSEsQNKIELLLQQHQDRIEQLISEHEVEitgl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 439 ----EDARASLERLVKEMAPLQEElsGKGQEADQLwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSltrQ 514
Cdd:pfam15921 284 tekaSSARSQANSIQSQLEIIQEQ--ARNQNSMYM-RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANS---E 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 515 LQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQqvgmlerlagppgpELPVAGEKNEALvpvnsslqeaWgkpeeeqrg 594
Cdd:pfam15921 358 LTEARTERDQFSQESGNLDDQLQKLLADLHKREK--------------ELSLEKEQNKRL----------W--------- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 595 lqeaqldDTKVQEGSQEEELRqanRELEKELQNVvgrnQLLEGKLQALQADYQA-LQQRESAIQGSLASLEaeqaSIRHL 673
Cdd:pfam15921 405 -------DRDTGNSITIDHLR---RELDDRNMEV----QRLEALLKAMKSECQGqMERQMAAIQGKNESLE----KVSSL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 674 GDQMEASLLAVRKAKEAMKAqmaeKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkGQ 753
Cdd:pfam15921 467 TAQLESTKEMLRKVVEELTA----KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE-GD 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 754 QGVGPPTDNEARELaaQLALSQAQLEVHQGEVQRLqAQVVDLQAKMRAALD-DQDKVQSQLSMAEAVLREHKTL------ 826
Cdd:pfam15921 542 HLRNVQTECEALKL--QMAEKDKVIEILRQQIENM-TQLVGQHGRTAGAMQvEKAQLEKEINDRRLELQEFKILkdkkda 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 827 -VQQLKEQNEALNRAHVQELLQCSEREGALQeeraDEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDT 905
Cdd:pfam15921 619 kIRELEARVSDLELEKVKLVNAGSERLRAVK----DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTT 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 906 AELGIQVCALTVEKERVEEALacavQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQA 985
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTL----KSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQF----------LEEAMTNA 760
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 986 EQRAQSLQEAahqelntlKFQLSAEimdyqsrLKNAGEECKSLRGQLEeqgrQLQAAEeavEKLKATQADMGEKLSCTSN 1065
Cdd:pfam15921 761 NKEKHFLKEE--------KNKLSQE-------LSTVATEKNKMAGELE----VLRSQE---RRLKEKVANMEVALDKASL 818
|
890 900 910
....*....|....*....|....*....|.
gi 1894925332 1066 HLAECQAAMLRKDKEGAALREDLERTQKELE 1096
Cdd:pfam15921 819 QFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
331-880 |
3.63e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 331 EDYHTALRRLE---SMLQPL---AQELEATRDSLDKKNQHLASFPGWlaMAQQKADTASDTKGRQEPIPSDAAQEMQELG 404
Cdd:COG4913 238 ERAHEALEDAReqiELLEPIrelAERYAAARERLAELEYLRAALRLW--FAQRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 405 EKLQALERERTKVEEVNRQQS--------AQLEQLVKELQLKEDARASLERLVKEmapLQEELSGkgqEADQLWRRLQEL 476
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGgdrleqleREIERLERELEERERRRARLEALLAA---LGLPLPA---SAEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 477 LAHTSSWEEELAELRREkkqqqeekelleqeVRSLTRQLQFLETQLAQVSQHVSDLEEQKK----QLIQDKDHLSQQVGM 552
Cdd:COG4913 390 AALLEALEEELEALEEA--------------LAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGL 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 553 LERlagppgpELPVAGEkneaLVPVnsslqeawgKPEEEQ-RGLQEAQLddtkvqeGSQ-------EEELRQANReleke 624
Cdd:COG4913 456 DEA-------ELPFVGE----LIEV---------RPEEERwRGAIERVL-------GGFaltllvpPEHYAAALR----- 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 625 lqnVVGRNQLlEGKLQALQAD-YQALQQRESAIQGSLAS-LEAEQASIR-----HLGDQM-------EASLLAVRKA--K 688
Cdd:COG4913 504 ---WVNRLHL-RGRLVYERVRtGLPDPERPRLDPDSLAGkLDFKPHPFRawleaELGRRFdyvcvdsPEELRRHPRAitR 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 689 EAM---KAQMAEK----------------EAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTA 749
Cdd:COG4913 580 AGQvkgNGTRHEKddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWD 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 750 EKGQQGVgpptDNEARELAAQLAlsqaQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQ 829
Cdd:COG4913 660 EIDVASA----EREIAELEAELE----RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE 731
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1894925332 830 LKEQNEALNRAHVQELLQCSE--REGALQEERADEAQQR-EEELRALQEELSQA 880
Cdd:COG4913 732 LQDRLEAAEDLARLELRALLEerFAAALGDAVERELRENlEERIDALRARLNRA 785
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
584-962 |
3.72e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 71.53 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 584 AWGKPEEEQRGLQEAQLddtkvqegSQEEELRQANRELEKE---LQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSL 660
Cdd:PRK04863 273 DYMRHANERRVHLEEAL--------ELRRELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 661 ASLEAE---QASIRHLGDQMEASLLAVRKAKEamkaQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRE-------L 730
Cdd:PRK04863 345 RQQEKIeryQADLEELEERLEEQNEVVEEADE----QQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRaiqyqqaV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 731 RALESqCQQQTQL-----------IEVLTAEKGQQgvgpptDNEARELAAQLALSQAQLEVHQ----------GEVQRLQ 789
Cdd:PRK04863 421 QALER-AKQLCGLpdltadnaedwLEEFQAKEQEA------TEELLSLEQKLSVAQAAHSQFEqayqlvrkiaGEVSRSE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 790 AQVVdlqakMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAlnrahvQELLQCSEREGALQEERADEAQQREEE 869
Cdd:PRK04863 494 AWDV-----ARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRA------ERLLAEFCKRLGKNLDDEDELEQLQEE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 870 LRALQEELSQAKCSSEEAQLEHAELQEQL--------------HRANTDTAELGIQVCALTVEKERVEEALacavQELQD 935
Cdd:PRK04863 563 LEARLESLSESVSEARERRMALRQQLEQLqariqrlaarapawLAAQDALARLREQSGEEFEDSQDVTEYM----QQLLE 638
|
410 420
....*....|....*....|....*..
gi 1894925332 936 AKEAASREREGLERQVAGLQQEKESLQ 962
Cdd:PRK04863 639 RERELTVERDELAARKQALDEEIERLS 665
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
857-1169 |
5.55e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 857 EERADEAQQREEELRALQEELsqakcsseEAQLEHAELQ-EQLHRANTDTAELGI-QVCALTVEKERVEEALACAVQELQ 934
Cdd:COG1196 178 ERKLEATEENLERLEDILGEL--------ERQLEPLERQaEKAERYRELKEELKElEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 935 DAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDY 1014
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE-ELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1015 QSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKE 1094
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925332 1095 LEKATTKIQEYYnklcQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEER 1169
Cdd:COG1196 409 EEALLERLERLE----EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| FYVE_RUFY4 |
cd15745 |
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ... |
1178-1227 |
5.63e-12 |
|
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain. The FYVE domain of RUFY4 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue). The biological function of RUFY4 still remains unclear.
Pssm-ID: 277284 [Multi-domain] Cd Length: 52 Bit Score: 61.75 E-value: 5.63e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1894925332 1178 HCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKH--GGKKERCCRACF 1227
Cdd:cd15745 1 ACAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVLSVpdTCIYLRVCKTCY 52
|
|
| RUN_RUNDC3 |
cd17684 |
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ... |
33-135 |
6.22e-12 |
|
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 contains two isoforms, RUNDC3A and RUNDC3B. RUNDC3A, also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. RUNDC3B, also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. Both RUNDC3A and RUNDC3B contain a RUN domain.
Pssm-ID: 439046 Cd Length: 150 Bit Score: 64.73 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 33 EPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGN--KKDYWDYFCACLAKVkgANDGIRFVKSISELRTSLGKGRAFIRY 110
Cdd:cd17684 20 ETIDDSSEELINFAAILEQILSHRLKPVKPWYGSeePRTFWDYIRVACKKV--PQNCIASIEQMENIKSPKAKGRAWIRV 97
|
90 100
....*....|....*....|....*
gi 1894925332 111 SLVHQRLADTLQQCFMNTKVTSDWY 135
Cdd:cd17684 98 ALMEKRLSEYLSTALKQTRLTRNFY 122
|
|
| FYVE_RABE_unchar |
cd15739 |
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ... |
1167-1227 |
6.77e-12 |
|
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This family includes a group of uncharacterized rab GTPase-binding effector proteins found in bilateria. Although their biological functions remain unclear, they all contain a FYVE domain that harbors a putative phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding site.
Pssm-ID: 277278 [Multi-domain] Cd Length: 73 Bit Score: 62.36 E-value: 6.77e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925332 1167 EERWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1227
Cdd:cd15739 1 EVRWQHEDDVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCH 61
|
|
| FYVE_PKHF |
cd15717 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ... |
1170-1227 |
1.01e-11 |
|
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), and similar proteins; This family includes protein containing both PH and FYVE domains 1 (phafin-1) and 2 (phafin-2). Phafin-1 is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway. Phafin-2 is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.
Pssm-ID: 277257 [Multi-domain] Cd Length: 61 Bit Score: 61.23 E-value: 1.01e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1170 WLGDTEANHCLDCKR-EFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE-RCCRACF 1227
Cdd:cd15717 2 WVPDSEAPVCMHCKKtKFTAINRRHHCRKCGAVVCGACSSKKFLLPHQSSKPlRVCDTCY 61
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
315-1007 |
1.56e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 69.23 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 315 LQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPS 394
Cdd:TIGR00618 199 LTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 395 DA-AQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEElsgkgQEADQLWRRL 473
Cdd:TIGR00618 279 LEeTQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-----RRLLQTLHSQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 474 QELLAhtssweeelaelrrekkqqqeekelleqevRSLTRQLQFLETQLAQVS--QHVSDLEEQKKQLIQDKDHLSQQVG 551
Cdd:TIGR00618 354 EIHIR------------------------------DAHEVATSIREISCQQHTltQHIHTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 552 MLERLAGPPGPELpvageknEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKV-QEGSQEE----ELRQANRELEKELQ 626
Cdd:TIGR00618 404 ILQREQATIDTRT-------SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTaQCEKLEKihlqESAQSLKEREQQLQ 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 627 NVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGdqmeasllAVRKAKEAMKAQMAEKEAILQSKE 706
Cdd:TIGR00618 477 TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG--------PLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 707 GECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkgQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQ 786
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNI--TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 787 RLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERAD----- 861
Cdd:TIGR00618 627 LQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQcqtll 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 862 -EAQQREEELRALQEELSQAKcSSEEAQLEhAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQ---ELQDAK 937
Cdd:TIGR00618 707 rELETHIEEYDREFNEIENAS-SSLGSDLA-AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQtgaELSHLA 784
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 938 EAASREREGLERQVAGLQQEKESLQEKLkaaKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQL 1007
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTLEAEIGQEI---PSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
234-1034 |
2.12e-11 |
|
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: 69.21 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 234 EMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQgEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQA----TQ 309
Cdd:COG3096 310 EMARELEELSARESDLEQDYQAASDHLNLVQTALRQQ-EKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEArleaAE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 310 NTVKELQTCL----QGLELgAAEKEEDYHTALRRLESmlqplAQELeatrdsLDKKNQHLASFPGWLAMAQQKADTASDT 385
Cdd:COG3096 389 EEVDSLKSQLadyqQALDV-QQTRAIQYQQAVQALEK-----ARAL------CGLPDLTPENAEDYLAAFRAKEQQATEE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 386 KGRQEPIPSDAAQEMQELGEKLQALERertKVEEVNRQQSAQLEQlvkelQLKEDARaSLERLVKEMAPLQEELSgkgqE 465
Cdd:COG3096 457 VLELEQKLSVADAARRQFEKAYELVCK---IAGEVERSQAWQTAR-----ELLRRYR-SQQALAQRLQQLRAQLA----E 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 466 ADQLWRRLQELlahtssweeelaelRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDH 545
Cdd:COG3096 524 LEQRLRQQQNA--------------ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 546 LSQQVGMLERLAgppgpelPVAGEKNEALvpvnSSLQEAWGKPEEEQRGLQEA--QLDDTKVQEGSQEEELRQANRELEK 623
Cdd:COG3096 590 LRARIKELAARA-------PAWLAAQDAL----ERLREQSGEALADSQEVTAAmqQLLEREREATVERDELAARKQALES 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 624 ELQNVVGRNQLLEGKLQALQADYQALQQRE-------------SAIQGSLAS------LEAEQASIRHLGDQMEASLL-- 682
Cdd:COG3096 659 QIERLSQPGGAEDPRLLALAERLGGVLLSEiyddvtledapyfSALYGPARHaivvpdLSAVKEQLAGLEDCPEDLYLie 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 683 --------AVRKAKEAMKAQMA--EKEAILQSKEGEC------------QQLREEVEQcqqLAEaRHRELRALESQCQQQ 740
Cdd:COG3096 739 gdpdsfddSVFDAEELEDAVVVklSDRQWRYSRFPEVplfgraarekrlEELRAERDE---LAE-QYAKASFDVQKLQRL 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 741 TQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLqakmRAALDDQDKVQSQLS-MAEAV 819
Cdd:COG3096 815 HQAFSQFVGGHLAVAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQL----KEQLQLLNKLLPQANlLADET 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 820 LREhktLVQQLKEQNEALNRAhVQELLQCSEREGALqEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAEL----Q 895
Cdd:COG3096 891 LAD---RLEELREELDAAQEA-QAFIQQHGKALAQL-EPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALsevvQ 965
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 896 EQLHRANTDTAELGIQVCALTvekERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSL 975
Cdd:COG3096 966 RRPHFSYEDAVGLLGENSDLN---EKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQEL 1042
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 976 PGLQAQL-AQAEQRAQSLQEAAHQELNTLKFQLS----------AEIMDYQSRLKNAGEECKSLRGQLEE 1034
Cdd:COG3096 1043 EELGVQAdAEAEERARIRRDELHEELSQNRSRRSqlekqltrceAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| FYVE_RBNS5 |
cd15716 |
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ... |
1170-1231 |
3.54e-11 |
|
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and similar proteins; Rbsn-5, also termed zinc finger FYVE domain-containing protein 20, is a novel Rab5 effector that is complexed to the Sec1-like protein VPS45 and recruited in a phosphatidylinositol-3-kinase-dependent fashion to early endosomes. It also binds to Rab4 and EHD1/RME-1, two regulators of the recycling route, and is involved in cargo recycling to the plasma membrane. Moreover, Rbsn-5 regulates endocytosis at the apical side of the wing epithelium and plays a role of the apical endocytic trafficking of Fmi in the establishment of planar cell polarity (PCP).
Pssm-ID: 277256 [Multi-domain] Cd Length: 61 Bit Score: 59.66 E-value: 3.54e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925332 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCcnnyvlSKHGGKKERCCRACFQKLS 1231
Cdd:cd15716 4 WVNDSDVPFCPDCGKKFNLARRRHHCRLCGSIMCNKC------SQFLPLHIRCCHHCKDLLE 59
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
867-1176 |
3.89e-11 |
|
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: 68.17 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 867 EEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELgIQVCALTVEKERVEealacaVQELQDAKEAASREREG 946
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKEKREYE------GYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 947 LERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQ-----AEQRAQSLQEAAHqELNTLKFQLSAEIMDYQSRLKNA 1021
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIG-ELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1022 GEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTK 1101
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1102 IqeyyNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALE-----FQQKLSAEERWLGDTEA 1176
Cdd:TIGR02169 401 I----NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkleqLAADLSKYEQELYDLKE 476
|
|
| FYVE_ZFYV1 |
cd15734 |
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ... |
1170-1227 |
4.30e-11 |
|
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar proteins; ZFYV1, also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYV1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by wortmannin, a PI3-kinase inhibitor. In addition to C-terminal tandem FYVE domain, ZFYV1 contains an N-terminal putative C2H2 type zinc finger and a possible nucleotide binding P-loop.
Pssm-ID: 277273 [Multi-domain] Cd Length: 61 Bit Score: 59.65 E-value: 4.30e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE--RCCRACF 1227
Cdd:cd15734 2 WVPDSEIKECSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRGWDHpvRVCDPCA 61
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
238-1104 |
5.38e-11 |
|
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: 67.51 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 238 ELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTC-----------LVAELQKQWEVTQ 306
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAArkqeleeilheLESRLEEEEERSQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 307 ATQNTVKELQTCLQGLElGAAEKEEDYHTALR----RLESMLQPLAQELEATRDSLDKKN-------QHLASFPGWLAMA 375
Cdd:pfam01576 93 QLQNEKKKMQQHIQDLE-EQLDEEEAARQKLQlekvTTEAKIKKLEEDILLLEDQNSKLSkerklleERISEFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 376 QQKADTASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEevnrQQSAQLEQLVKELQLK-EDARASLERLVKEMAP 454
Cdd:pfam01576 172 EEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLE----GESTDLQEQIAELQAQiAELRAQLAKKEEELQA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 455 LQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQ-FLETQLAQV---SQHVS 530
Cdd:pfam01576 248 ALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdTLDTTAAQQelrSKREQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 531 DLEEQKKQLIQDKDHLSQQVGMLERlagppgpelpvagEKNEALVPVNSSLqeawgkpeeEQRGLQEAQLDDTKVQEGSQ 610
Cdd:pfam01576 328 EVTELKKALEEETRSHEAQLQEMRQ-------------KHTQALEELTEQL---------EQAKRNKANLEKAKQALESE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 611 EEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEA 690
Cdd:pfam01576 386 NAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 691 MKAQMAEKEAILQ-------SKEGECQQLREEVEQCQQLAEARHRELRALESQCQQ-QTQLIEVLTAEKGQQGVGPPTDN 762
Cdd:pfam01576 466 LESQLQDTQELLQeetrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTlQAQLSDMKKKLEEDAGTLEALEE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 763 EARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEavlREHKTLVQQLKEQNEALNRAhv 842
Cdd:pfam01576 546 GKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLE---KKQKKFDQMLAEEKAISARY-- 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 843 qellqCSEREGAlqeeradEAQQREEELRALQeeLSQAkcsSEEAQlehaELQEQLHRANTdtaELGIQVCALTVEKERV 922
Cdd:pfam01576 621 -----AEERDRA-------EAEAREKETRALS--LARA---LEEAL----EAKEELERTNK---QLRAEMEDLVSSKDDV 676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 923 EEalacAVQELQDAKEAasreregLERQVAGLQQEKESLQEKLKAAKAAAGSLP-GLQAQLAQAEQRAQSLQEAAHQELN 1001
Cdd:pfam01576 677 GK----NVHELERSKRA-------LEQQVEEMKTQLEELEDELQATEDAKLRLEvNMQALKAQFERDLQARDEQGEEKRR 745
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1002 TLKFQ---LSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAA----EEAVEKLKATQADMGEklsctsnHLAECQAAM 1074
Cdd:pfam01576 746 QLVKQvreLEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAAnkgrEEAVKQLKKLQAQMKD-------LQRELEEAR 818
|
890 900 910
....*....|....*....|....*....|
gi 1894925332 1075 LRKDKEGAALREDlERTQKELEKATTKIQE 1104
Cdd:pfam01576 819 ASRDEILAQSKES-EKKLKNLEAELLQLQE 847
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
226-887 |
5.38e-11 |
|
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: 67.77 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 226 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEdnvRLTCLVAELQKQWEVT 305
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA---RLERLEDRRERLQQEI 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 306 QATQNTVKELQtcLQGLELGAAEKEEDYHTALRRLESmlqpLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDT 385
Cdd:TIGR02168 424 EELLKKLEEAE--LKELQAELEELEEELEELQEELER----LEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 386 KGRQEPIPSDAAQEMQE----------------------------LGEKLQAL------------------ERERTKVEE 419
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNqsglsgilgvlselisvdegyeaaieaaLGGRLQAVvvenlnaakkaiaflkqnELGRVTFLP 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 420 VNRQQSAQLEQLVKE-LQLKEDARASLERLVKEMAPLQEELSG---------KGQEADQLWRRLQ----------ELLAH 479
Cdd:TIGR02168 578 LDSIKGTEIQGNDREiLKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvvdDLDNALELAKKLRpgyrivtldgDLVRP 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 480 TSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERlagp 559
Cdd:TIGR02168 658 GGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK---- 733
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 560 pgpELPVAGEKNEALVPVNSSLQEAWGKPEEeqrglQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKL 639
Cdd:TIGR02168 734 ---DLARLEAEVEQLEERIAQLSKELTELEA-----EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 640 QALQADYQALQQRESAIQGSLASLEAEQASIrhlgdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 719
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAAT-------ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 720 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQqgvgppTDNEARELAAQLALSQAQLEVHQGEVQRLQAQV-VDLQAK 798
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSE------LRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLT 952
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 799 MRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAlnrahvqellqcseregALQEerADEAQQREEELRALQEELS 878
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA-----------------AIEE--YEELKERYDFLTAQKEDLT 1013
|
....*....
gi 1894925332 879 QAKCSSEEA 887
Cdd:TIGR02168 1014 EAKETLEEA 1022
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
581-996 |
7.27e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 7.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 581 LQEAWGKPEEEQRGLQEAQLDDTKVQEGSQE-EELRQANRELEKELQN--VVGRNQLLEGKLQALQADYQALQQRESAIQ 657
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAElEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 658 GSLASLEAEQASIRHLGDQMEAsllAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQC 737
Cdd:COG4717 160 ELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 738 ---------QQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALS-------------QAQLEVHQGEVQRLQAQVVDL 795
Cdd:COG4717 237 eaaaleerlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgllallflllarEKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 796 QAKMRAALDDQDKVQSQLS--MAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcsEREGALQEERADEaqqrEEELRAL 873
Cdd:COG4717 317 EEEELEELLAALGLPPDLSpeELLELLDRIEELQELLREAEELEEELQLEELEQ--EIAALLAEAGVED----EEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 874 QEELSQAkcssEEAQLEHAELQEQLHRANTDTAELgiqvcALTVEKERVEEALacavQELQDAKEAASREREGLERQVAG 953
Cdd:COG4717 391 LEQAEEY----QELKEELEELEEQLEELLGELEEL-----LEALDEEELEEEL----EELEEELEELEEELEELREELAE 457
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1894925332 954 LQQEKESLQEKlkaakaaaGSLPGLQAQLAQAEQRAQSLQEAA 996
Cdd:COG4717 458 LEAELEQLEED--------GELAELLQELEELKAELRELAEEW 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
784-1046 |
9.37e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 9.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 784 EVQRLQAQVVDLQAKMRAALDDQDKVQsQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQEllqcSEREGALQEERADEA 863
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAALRLWF----AQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 864 qqrEEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDT-AELGIQVCALTVEKERVEEALACAVQELQDAKEAASR 942
Cdd:COG4913 301 ---RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 943 EREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQelntlkfqLSAEIMDYQSRLKNAG 1022
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEA----------LEEALAEAEAALRDLRRELRE--------LEAEIASLERRKSNIP 439
|
250 260
....*....|....*....|....
gi 1894925332 1023 EECKSLRGQLEEqgrQLQAAEEAV 1046
Cdd:COG4913 440 ARLLALRDALAE---ALGLDEAEL 460
|
|
| FYVE_RUFY2 |
cd15759 |
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ... |
1170-1226 |
1.39e-10 |
|
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions.
Pssm-ID: 277298 [Multi-domain] Cd Length: 71 Bit Score: 58.50 E-value: 1.39e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925332 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRAC 1226
Cdd:cd15759 4 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSC 60
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
654-1097 |
1.52e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.13 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 654 SAIQGSLAS-LEAEQASIRHLGDQMEASLLAVRKAKEAMKaqmaekeaILQSKEGECQQLREEVEQCQQLAEARHRELRA 732
Cdd:PRK04863 211 SAITRSLRDyLLPENSGVRKAFQDMEAALRENRMTLEAIR--------VTQSDRDLFKHLITESTNYVAADYMRHANERR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 733 LESQcqqqtqliEVLTAEKGQQGvgpptdneARElaaQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQ 812
Cdd:PRK04863 283 VHLE--------EALELRRELYT--------SRR---QLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 813 LSMAEAVLR---EHKTLVQQLKEQNEAlnRAHVQELLQCSEREGALQEERADEA-------QQREEEL--RALQEElsQA 880
Cdd:PRK04863 344 LRQQEKIERyqaDLEELEERLEEQNEV--VEEADEQQEENEARAEAAEEEVDELksqladyQQALDVQqtRAIQYQ--QA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 881 KCSSEEAQlehaelqEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLE--RQVAG----- 953
Cdd:PRK04863 420 VQALERAK-------QLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQlvRKIAGevsrs 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 954 -LQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEA----------------AHQELNTLKFQLSAEIMDYQS 1016
Cdd:PRK04863 493 eAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAerllaefckrlgknldDEDELEQLQEELEARLESLSE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1017 RLKNAGEECKSLRGQLEEQGRQLQ----------AAEEAVEKLkatQADMGEKLScTSNHLAECQAAMLRKDKEGAALRE 1086
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARIQrlaarapawlAAQDALARL---REQSGEEFE-DSQDVTEYMQQLLERERELTVERD 648
|
490
....*....|.
gi 1894925332 1087 DLERTQKELEK 1097
Cdd:PRK04863 649 ELAARKQALDE 659
|
|
| FYVE2_Vac1p_like |
cd15737 |
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ... |
1169-1203 |
1.79e-10 |
|
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the second FYVE domain that is responsible for the ability of Pep7p to efficiently interact with Vac1p and Vps45p.
Pssm-ID: 277276 [Multi-domain] Cd Length: 83 Bit Score: 58.67 E-value: 1.79e-10
10 20 30
....*....|....*....|....*....|....*
gi 1894925332 1169 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFC 1203
Cdd:cd15737 1 PWEDDSSVTHCPICLRSFGLLLRKHHCRLCGKVVC 35
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
509-1056 |
2.01e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 509 RSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQqvgMLERLAgppgpelpvagEKNEALVPVnsslqeawgkp 588
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADE---VLEEHE-----------ERREELETL----------- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 589 EEEQRGLQEAQLDDTKVQEGSQEE--ELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLA----- 661
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEvrDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecrva 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 662 --SLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQL----------AEARHRE 729
Cdd:PRK02224 337 aqAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdlgnAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 730 LRALESQCQQQTQLIEVlTAEKGQQGVgpptdNEARELAAQLALSQAQLEV----HQGEVQRLQAQVVDLQAKMRAALDD 805
Cdd:PRK02224 417 LREERDELREREAELEA-TLRTARERV-----EEAEALLEAGKCPECGQPVegspHVETIEEDRERVEELEAELEDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 806 QDKVQSQLSMAEAvLREHKTLVQQLKEQNEAlnrahVQELLqcseregALQEERADEAQQREEELRALQEEL-SQAKCSS 884
Cdd:PRK02224 491 VEEVEERLERAED-LVEAEDRIERLEERRED-----LEELI-------AERRETIEEKRERAEELRERAAELeAEAEEKR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 885 EEAQLEHAELQEQLHRAntdtAELGIQVCALTVEKERVEeALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEK 964
Cdd:PRK02224 558 EAAAEAEEEAEEAREEV----AELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 965 LKAAKAAAGSLPGLQAQLAQAE-QRAQSLQEAAHQELNTL---KFQLSAEIMDYQSRLKNAgEECKSLRGQLEEQGRQLQ 1040
Cdd:PRK02224 633 RERKRELEAEFDEARIEEAREDkERAEEYLEQVEEKLDELreeRDDLQAEIGAVENELEEL-EELRERREALENRVEALE 711
|
570
....*....|....*.
gi 1894925332 1041 AAEEAVEKLKATQADM 1056
Cdd:PRK02224 712 ALYDEAEELESMYGDL 727
|
|
| FYVE_ZFY26 |
cd15724 |
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ... |
1170-1228 |
3.45e-10 |
|
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed FYVE domain-containing centrosomal protein (FYVE-CENT), or spastizin, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that localizes to the centrosome and midbody. ZFY26 and its interacting partners TTC19 and KIF13A are required for cytokinesis. It also interacts with Beclin 1, a subunit of class III phosphatidylinositol 3-kinase complex, and may have potential implications for carcinogenesis. In addition, it has been considered as the causal agent of a rare form of hereditary spastic paraplegia. ZFY26 contains a FYVE domain that is important for targeting of FYVE-CENT to the midbody.
Pssm-ID: 277263 [Multi-domain] Cd Length: 61 Bit Score: 57.14 E-value: 3.45e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925332 1170 WLGDTEANHCLDCKRE-FSWMVRRHHCRICGRIFCYYCCNNYVL-SKHGGKKERCCRACFQ 1228
Cdd:cd15724 1 WVPDEAVSVCMVCQVErFSMFNRRHHCRRCGRVVCSSCSTKKMLvEGYRENPVRVCDQCYE 61
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
563-1176 |
3.48e-10 |
|
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: 65.09 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 563 ELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANrELEKELQNVVGRNQLLEGKLQAL 642
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKE-ALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 643 QADYQALQQRESAIqgsLASLEAEQASIRHLGdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQL 722
Cdd:TIGR02169 257 TEEISELEKRLEEI---EQLLEELNKKIKDLG---EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 723 AEARHRELRALESQCQQQTQLIEVLTAE-KGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRA 801
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 802 ALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALN---RAHVQELLQCSE-REGALQEERADEAQQR--EEELRALQE 875
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAleiKKQEWKLEQLAAdLSKYEQELYDLKEEYDrvEKELSKLQR 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 876 ELSQAkcsseEAQLEHAELQEQLHRANTDTAELGIQ-VCALTVEKERVEEALACAVQ-----ELQ----DAKEAASRERE 945
Cdd:TIGR02169 491 ELAEA-----EAQARASEERVRGGRAVEEVLKASIQgVHGTVAQLGSVGERYATAIEvaagnRLNnvvvEDDAVAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 946 GLERQVAGLQ--------QEKESLQEKLKAAKAAA--------------------------------------------- 972
Cdd:TIGR02169 566 LLKRRKAGRAtflplnkmRDERRDLSILSEDGVIGfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgkyrmvtle 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 973 ------------GSLPGLQAQLAQAEQRAQSLQEAAH-QELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQL 1039
Cdd:TIGR02169 646 gelfeksgamtgGSRAPRGGILFSRSEPAELQRLRERlEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1040 QAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT--------KIQEYYNKLCQ 1111
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsripEIQAELSKLEE 805
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925332 1112 EVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALwqKSDALEFQQKLSAEERWLGDTEA 1176
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL--KEQIKSIEKEIENLNGKKEELEE 868
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
403-1050 |
3.70e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 403 LGEKLQALERERTKVEEVnRQQSAQLEQLVKElqlKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELlahtss 482
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKF-IKRTENIEELIKE---KEKELEEVLREINEISSELPELREELEKLEKEVKELEEL------ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 483 weeelaelRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQliqdkdhlsqqvgmLERLAGPPGP 562
Cdd:PRK03918 237 --------KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE--------------LKELKEKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 563 ELPVAGEKNEALVPVNsSLQEAWGKPEEEQRGLQEaqlddtKVQEGSQEEELRQANRELEKELQNVVGRnqlLEGKLQAL 642
Cdd:PRK03918 295 YIKLSEFYEEYLDELR-EIEKRLSRLEEEINGIEE------RIKELEEKEERLEELKKKLKELEKRLEE---LEERHELY 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 643 QaDYQALQQRESAIQGSLASLEAEQAsirhlgdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEqcqql 722
Cdd:PRK03918 365 E-EAKAKKEELERLKKRLTGLTPEKL---------EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE----- 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 723 aearhrELRALESQCQQQTQLIevltaekgqqgvgppTDNEARELaaqlalsqaqLEVHQGEVQRLQAQVVDLQAKMRAA 802
Cdd:PRK03918 430 ------ELKKAKGKCPVCGREL---------------TEEHRKEL----------LEEYTAELKRIEKELKEIEEKERKL 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 803 LDDQDKVQSQLSMAEAVLREHKTLvQQLKEQNEALNRAHVQELlqcsEREGALQEERADEAQQREEELRALQEELSQAK- 881
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELA-EQLKELEEKLKKYNLEEL----EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEe 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 882 CSSEEAQLEHA--ELQEQLHRANTDTAELGIQvcALTVEKERVEEaLACAVQELQDAKEAASREREGLERqvagLQQEKE 959
Cdd:PRK03918 554 LKKKLAELEKKldELEEELAELLKELEELGFE--SVEELEERLKE-LEPFYNEYLELKDAEKELEREEKE----LKKLEE 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 960 SLQEKLKAAKAAAGSLPGLQAQLAQAEQRaqsLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQL 1039
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKK---YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
650
....*....|.
gi 1894925332 1040 QAAEEAVEKLK 1050
Cdd:PRK03918 704 EEREKAKKELE 714
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
762-1098 |
4.47e-10 |
|
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: 64.59 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 762 NEARELAAQLAlsqaQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRah 841
Cdd:COG3096 278 NERRELSERAL----ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIER-- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 842 vqellqcseregalqeeradeaqqREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVC----ALTV 917
Cdd:COG3096 352 ------------------------YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqALDV 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 918 EKER----------VEEALAC-------------------------------AVQELQDAKEAASREREGLE--RQVAG- 953
Cdd:COG3096 408 QQTRaiqyqqavqaLEKARALcglpdltpenaedylaafrakeqqateevleLEQKLSVADAARRQFEKAYElvCKIAGe 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 954 ------LQQEKESLqEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEA----------------AHQELNTLKFQLSAEI 1011
Cdd:COG3096 488 versqaWQTARELL-RRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAerlleefcqrigqqldAAEELEELLAELEAQL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1012 MDYQSRLKNAGE---ECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAM---LRKDKEGAALR 1085
Cdd:COG3096 567 EELEEQAAEAVEqrsELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMqqlLEREREATVER 646
|
410
....*....|...
gi 1894925332 1086 EDLERTQKELEKA 1098
Cdd:COG3096 647 DELAARKQALESQ 659
|
|
| FYVE_PKHF2 |
cd15755 |
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ... |
1170-1230 |
4.55e-10 |
|
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar proteins; Phafin-2, also termed endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains (EAPF), or pleckstrin homology domain-containing family F member 2 (PKHF2), or PH domain-containing family F member 2, or PH and FYVE domain-containing protein 2, or zinc finger FYVE domain-containing protein 18, is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.
Pssm-ID: 277294 [Multi-domain] Cd Length: 64 Bit Score: 56.97 E-value: 4.55e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925332 1170 WLGDTEANHCLDCKR-EFSWMVRRHHCRICGRIFCYYCC-NNYVLSKHGGKKERCCRACFQKL 1230
Cdd:cd15755 2 WVPDSEATVCMRCQKaKFTPVNRRHHCRKCGFVVCGPCSeKKFLLPSQSSKPVRVCDFCYDLL 64
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
611-1105 |
8.98e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 8.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 611 EEELRQANRELEKE----LQNVVGRNQLLEGKLQALQ---ADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEA--SL 681
Cdd:COG4717 48 LERLEKEADELFKPqgrkPELNLKELKELEEELKEAEekeEEYAELQEELEELEEELEELEAELEELREELEKLEKllQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 682 LAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEarhrELRALESQCQQQTQLIEVLTAEKGQQgvgppTD 761
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA----ELAELQEELEELLEQLSLATEEELQD-----LA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 762 NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAAlDDQDKVQSQLSMAEAVLRehkTLVQQLKEQNEALNRAH 841
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAAA---LLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 842 VQELLQcseregALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLhrantdtAELGIqvcALTVEKER 921
Cdd:COG4717 275 IAGVLF------LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL-------AALGL---PPDLSPEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 922 VEEALAcAVQELQDAKEAASREREglERQVAGLQQEKESLQEKLKAAKAaagslpglqAQLAQAEQRAQSLQEAAhQELN 1001
Cdd:COG4717 339 LLELLD-RIEELQELLREAEELEE--ELQLEELEQEIAALLAEAGVEDE---------EELRAALEQAEEYQELK-EELE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1002 TLKFQLSAEIMDYQSRLKNAGEEckSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSctsnhlaecqaaMLRKDKEG 1081
Cdd:COG4717 406 ELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELE------------QLEEDGEL 471
|
490 500
....*....|....*....|....
gi 1894925332 1082 AALREDLERTQKELEKATTKIQEY 1105
Cdd:COG4717 472 AELLQELEELKAELRELAEEWAAL 495
|
|
| FYVE_FGD6 |
cd15743 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ... |
1170-1227 |
9.51e-10 |
|
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar proteins; FGD6, also termed zinc finger FYVE domain-containing protein 24 is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) whose biological function remains unclear. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Moreover, the FYVE domain of FGD6 is a canonical FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site.
Pssm-ID: 277282 [Multi-domain] Cd Length: 61 Bit Score: 55.91 E-value: 9.51e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1894925332 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNN-YVLSKHGGKKERCCRACF 1227
Cdd:cd15743 3 WIPDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNkAPLEYLKNKSARVCDECF 61
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
392-1168 |
1.24e-09 |
|
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: 63.07 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 392 IPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLE--------RLVKEMAPLQEELSGKG 463
Cdd:pfam02463 157 EIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlkeklELEEEYLLYLDYLKLNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 464 QEADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDK 543
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 544 DHLSQQVGMLERLagppgpelpvagEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEK 623
Cdd:pfam02463 317 KESEKEKKKAEKE------------LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 624 ELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIR----------HLGDQMEASLLAVRKAKEAMKA 693
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILeeeeesielkQGKLTEEKEELEKQELKLLKDE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 694 QMAEKEAILQSKEGECQQLREEVEQC--QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQL 771
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLsrQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 772 ALSQAQLEVHQGEVQRLQAQVvdLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLvqqlkEQNEALNRAHVQELLQCSER 851
Cdd:pfam02463 545 ISTAVIVEVSATADEVEERQK--LVRALTELPLGARKLRLLIPKLKLPLKSIAVL-----EIDPILNLAQLDKATLEADE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 852 EGALQEERADeaqQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQ 931
Cdd:pfam02463 618 DDKRAKVVEG---ILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEI 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 932 ELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEI 1011
Cdd:pfam02463 695 LRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1012 MDYQSRLKNageECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLsctsnhLAECQAAMLRKDKEGAALREDLERT 1091
Cdd:pfam02463 775 ELAEEREKT---EKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEE------QLLIEQEEKIKEEELEELALELKEE 845
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925332 1092 QKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEE 1168
Cdd:pfam02463 846 QKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEER 922
|
|
| FYVE_FGD1_2_4 |
cd15741 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ... |
1169-1230 |
1.45e-09 |
|
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia FGD1, FGD2, FGD4; This family represents a group of Rho GTPase cell division cycle 42 (Cdc42)-specific guanine nucleotide exchange factors (GEFs), including FYVE, RhoGEF and PH domain-containing protein FGD1, FGD2 and FGD4. FGD1, also termed faciogenital dysplasia 1 protein, or Rho/Rac guanine nucleotide exchange factor FGD1 (Rho/Rac GEF), or zinc finger FYVE domain-containing protein 3, is a central regulator of extracellular matrix remodeling and belongs to the DBL family of GEFs that regulate the activation of the Rho GTPases. FGD1 is encoded by gene FGD1. Disabling mutations in the FGD1 gene cause the human X-linked developmental disorder faciogenital dysplasia (FGDY, also known as Aarskog-Scott syndrome). FGD2, also termed zinc finger FYVE domain-containing protein 4, is expressed in antigen-presenting cells, including B lymphocytes, macrophages, and dendritic cells. It localizes to early endosomes and active membrane ruffles. It plays a role in leukocyte signaling and vesicle trafficking in cells specialized to present antigen in the immune system. FGD4, also termed actin filament-binding protein frabin, or FGD1-related F-actin-binding protein, or zinc finger FYVE domain-containing protein 6, functions as an F-actin-binding (FAB) protein showing significant homology to FGD1. It induces the formation of filopodia through the activation of Cdc42 in fibroblasts. Those FGD proteins possess a similar domain organization that contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus. However, each FGD has a unique N-terminal region that may directly or indirectly interact with F-actin. FGD1 and FGD4 have an N-terminal proline-rich domain (PRD) and an N-terminal F-actin binding (FAB) domain, respectively. This model corresponds to the FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site. FGD1 possesses a FYVE-like domain that lack the N-terminal WxxD motif. Moreover, FGD2 is the only known RhoGEF family member shown to have a functional FYVE domain and endosomal binding activity.
Pssm-ID: 277280 [Multi-domain] Cd Length: 65 Bit Score: 55.57 E-value: 1.45e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1894925332 1169 RWLGDTEANHCLDCKREFSWMV-RRHHCRICGRIFCYYCCNNYV-LSKHGGKKERCCRACFQKL 1230
Cdd:cd15741 2 RWVRDNEVTMCMRCKEPFNALTrRRHHCRACGYVVCWKCSDYKAtLEYDGNKLNRVCKHCYVIL 65
|
|
| FYVE_ANFY1 |
cd15728 |
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ... |
1167-1230 |
1.63e-09 |
|
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins; ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain.
Pssm-ID: 277267 [Multi-domain] Cd Length: 63 Bit Score: 55.12 E-value: 1.63e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925332 1167 EERWlgdTEANHCLDCKREFSWMVRRHHCRICGRIFCYYC-CNNYVLSKHG-GKKERCCRACFQKL 1230
Cdd:cd15728 1 EPPW---ADGDYCYECGVKFGITTRKHHCRHCGRLLCSKCsTKEVPIIKFDlNKPVRVCDVCFDVL 63
|
|
| FYVE_WDFY3 |
cd15719 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ... |
1170-1230 |
1.97e-09 |
|
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar proteins; WDFY3, also termed autophagy-linked FYVE protein (Alfy), is a ubiquitously expressed phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein required for selective macroautophagic degradation of aggregated proteins. It regulates the protein degradation through the direct interaction with the autophagy protein Atg5. Moreover, WDFY3 acts as a scaffold that bridges its cargo to the macroautophagic machinery via the creation of a greater complex with Atg12, Atg16L, and LC3. It also functionally associates with sequestosome-1/p62 (SQSTM1) in osteoclasts. WDFY3 shuttles between the nucleus and cytoplasm. It predominantly localizes to the nucleus and nuclear membrane under basal conditions, but is recruited to cytoplasmic ubiquitin-positive protein aggregates under stress conditions. WDFY3 contains a PH-BEACH domain assemblage, five WD40 repeats and a PtdIns3P-binding FYVE domain.
Pssm-ID: 277259 [Multi-domain] Cd Length: 65 Bit Score: 55.08 E-value: 1.97e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925332 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNN--YVLSKHGGKKERCCRACFQKL 1230
Cdd:cd15719 3 WVKDEGGDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFesEIRRLRISRPVRVCQACYNIL 65
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
596-1104 |
4.15e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 596 QEAQLDDTKVQ-EGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLg 674
Cdd:PRK02224 185 QRGSLDQLKAQiEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDL- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 675 dqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVE---QCQQLAEARHRELRALESQCQQQTQLIEVLTAEK 751
Cdd:PRK02224 264 ---RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAH 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 752 GQQGVGPPTD------------NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLsmaEAV 819
Cdd:PRK02224 341 NEEAESLREDaddleeraeelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL---EEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 820 LREHKTLVQQLKE-----QNEALNRAHVQELL---QCSEREGALQE-ERADEAQQREEELRALQEELsqakcssEEAQLE 890
Cdd:PRK02224 418 REERDELREREAEleatlRTARERVEEAEALLeagKCPECGQPVEGsPHVETIEEDRERVEELEAEL-------EDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 891 HAELQEQLHRAnTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKA 970
Cdd:PRK02224 491 VEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 971 AAGSLPGLQAQLAQAEQRAQSLqeaahqelntlkfqlsAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLK 1050
Cdd:PRK02224 570 AREEVAELNSKLAELKERIESL----------------ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR 633
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1894925332 1051 ATQADMGEKLSctsnhlaecqaamlrkDKEGAALREDLERTQKELEKATTKIQE 1104
Cdd:PRK02224 634 ERKRELEAEFD----------------EARIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| FYVE_spVPS27p_like |
cd15735 |
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ... |
1174-1227 |
4.83e-09 |
|
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 (spVps27p) and similar proteins; spVps27p, also termed suppressor of ste12 deletion protein 4 (Sst4p), is a conserved homolog of budding Saccharomyces cerevisiae Vps27 and of mammalian Hrs. It functions as a downstream factor for phosphatidylinositol 3-kinase (PtdIns 3-kinase) in forespore membrane formation with normal morphology. It colocalizes and interacts with Hse1p, a homolog of Saccharomyces cerevisiae Hse1p and of mammalian STAM, to form a complex whose ubiquitin-interacting motifs (UIMs) are important for sporulation. spVps27p contains a VHS (Vps27p/Hrs/Stam) domain, a FYVE domain, and two UIMs.
Pssm-ID: 277274 [Multi-domain] Cd Length: 59 Bit Score: 53.69 E-value: 4.83e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925332 1174 TEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE--RCCRACF 1227
Cdd:cd15735 4 VDSDVCMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPHFGINQpvRVCDGCY 59
|
|
| FYVE_ZFY19 |
cd15749 |
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ... |
1179-1227 |
5.10e-09 |
|
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ZFY19, also termed mixed lineage leukemia (MLL) partner containing FYVE domain, is encoded by a novel gene, MLL partner containing FYVE domain (MPFYVE). The FYVE domain of ZFY19 resembles FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. The biological function of ZFY19 remains unclear.
Pssm-ID: 277288 [Multi-domain] Cd Length: 51 Bit Score: 53.28 E-value: 5.10e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1179 CLDCKREFSWMVRRHHCRICGRIFCYYCCN-NYVLSKHGGKKERCCRACF 1227
Cdd:cd15749 2 CFGCAAKFSLFKKECGCKNCGRSFCKGCLTfSAVVPRKGNQKQKVCKQCH 51
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
590-956 |
5.82e-09 |
|
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: 61.12 E-value: 5.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 590 EEQRGLQEAQLDDTKVQEGSQEE--ELRQANRELEKELQNVVGRNQLLEGKLQA----LQADYQALQQRESaiqgslasL 663
Cdd:COG3096 278 NERRELSERALELRRELFGARRQlaEEQYRLVEMARELEELSARESDLEQDYQAasdhLNLVQTALRQQEK--------I 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 664 EAEQASIRHLGDQMEASLLAVRKAKEamkaQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRE-------LRALEsQ 736
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAE----QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRaiqyqqaVQALE-K 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 737 CQQQTQLIEvLTAE-----------KGQQGvgpptDNEARELAAQLALSQAQLEVHQ----------GEVQRLQA----- 790
Cdd:COG3096 425 ARALCGLPD-LTPEnaedylaafraKEQQA-----TEEVLELEQKLSVADAARRQFEkayelvckiaGEVERSQAwqtar 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 791 QVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNR-------------AHVQELLQCSEREGALQE 857
Cdd:COG3096 499 ELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQqldaaeeleellaELEAQLEELEEQAAEAVE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 858 ERAdEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELgIQVCALTVEKERveealacavqELQDAK 937
Cdd:COG3096 579 QRS-ELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEV-TAAMQQLLERER----------EATVER 646
|
410
....*....|....*....
gi 1894925332 938 EAASREREGLERQVAGLQQ 956
Cdd:COG3096 647 DELAARKQALESQIERLSQ 665
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
511-1164 |
5.91e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.13 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 511 LTRQLQFLETQLAQVSQH---VSDLEEQKKQLIQDKDHLsqqvgmlerlagppgpelpvaGEKNEALVPVNSSLQEAWGK 587
Cdd:PRK04863 319 LNEAESDLEQDYQAASDHlnlVQTALRQQEKIERYQADL---------------------EELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 588 PEEEQRGLQEAQL--DDTK-----VQEGSQEEELR-----QANRELEK----------ELQNVVGRNQLLEGKLQALQAD 645
Cdd:PRK04863 378 QEENEARAEAAEEevDELKsqladYQQALDVQQTRaiqyqQAVQALERakqlcglpdlTADNAEDWLEEFQAKEQEATEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 646 YQALQQRESAIQGSLASLEAEQASIRHLGDQMEASlLAVRKAKEAmkaqmaekeailqskegeCQQLREEVEQCQQLaEA 725
Cdd:PRK04863 458 LLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRS-EAWDVAREL------------------LRRLREQRHLAEQL-QQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 726 RHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLalsQAQLEVHQGEvqrlQAQVVDLQAKMRAALDD 805
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEEL---EARLESLSES----VSEARERRMALRQQLEQ 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 806 QDKVQSQLSMAEAVLREHKTLVQQLKEQNEA--LNRAHVQELLQ-CSEREGALQEERaDEAQQREEELRALQEELSQAKC 882
Cdd:PRK04863 591 LQARIQRLAARAPAWLAAQDALARLREQSGEefEDSQDVTEYMQqLLERERELTVER-DELAARKQALDEEIERLSQPGG 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 883 SSEEAQLEHAE------LQE-----QLHRANTDTAELGIQVCALTV-EKERVEEALA----C------------------ 928
Cdd:PRK04863 670 SEDPRLNALAErfggvlLSEiyddvSLEDAPYFSALYGPARHAIVVpDLSDAAEQLAgledCpedlyliegdpdsfddsv 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 929 -AVQELQDA--KEAASRE-------------REGLERQVAGLQQEKESLQEKLkaakaaagslpglqAQLAQAEQRAQSL 992
Cdd:PRK04863 750 fSVEELEKAvvVKIADRQwrysrfpevplfgRAAREKRIEQLRAEREELAERY--------------ATLSFDVQKLQRL 815
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 993 QEAAHQELNT---LKFQL--SAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADM--------GEK 1059
Cdd:PRK04863 816 HQAFSRFIGShlaVAFEAdpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLnlladetlADR 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1060 LSCTSNHLAECQAAMLRKDKEGAALR-------------EDLERTQKELEKATTKIQEYYNK---LCQEVTNRE----RN 1119
Cdd:PRK04863 896 VEEIREQLDEAEEAKRFVQQHGNALAqlepivsvlqsdpEQFEQLKQDYQQAQQTQRDAKQQafaLTEVVQRRAhfsyED 975
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1120 DQKMLADLDDLN-RTKKYLEERLIELLRDKDALWQK----SDALEFQQKL 1164
Cdd:PRK04863 976 AAEMLAKNSDLNeKLRQRLEQAEQERTRAREQLRQAqaqlAQYNQVLASL 1025
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
767-994 |
8.46e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.03 E-value: 8.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 767 LAAQLALSQAQLEVHQGEVQRLQAQ--VVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNeALNRAHVQE 844
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL-GSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 845 LLQcSEREGALQEERADEAQQREEELRALQEELSQAKcsseeaqlehaELQEQLhrantdtaelgiqvcaltvekERVEE 924
Cdd:COG3206 259 LLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVI-----------ALRAQI---------------------AALRA 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 925 ALAcavQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKaakaaagSLPGLQAQLAQAEQRAQSLQE 994
Cdd:COG3206 306 QLQ---QEAQRILASLEAELEALQAREASLQAQLAQLEARLA-------ELPELEAELRRLEREVEVARE 365
|
|
| RUN_RUNDC3A |
cd17699 |
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ... |
33-162 |
1.06e-08 |
|
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN domain-containing protein 3A (RUNDC3A), also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. It contains a RUN domain.
Pssm-ID: 439061 Cd Length: 151 Bit Score: 55.80 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 33 EPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGN--KKDYWDYFCACLAKVkgANDGIRFVKSISELRTSLGKGRAFIRY 110
Cdd:cd17699 20 EPIDDSSEEFVNFAAILEQILSHRFKGPVSWFSSdgQRGFWDYIRLACSKV--PNNCISSIENMENISTSRAKGRAWIRV 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1894925332 111 SLVHQRLADTLQQCFMNTKVTSDWYYARSPFLQPKlSSDIVGQLYELTEVQF 162
Cdd:cd17699 98 ALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREE-STVLTGMLIGLSAIDF 148
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
720-964 |
1.27e-08 |
|
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: 58.62 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 720 QQLAEARHRELRALESQCQQQTQLIEVLTAEKgqqgvgpptdneaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKM 799
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEE-------------KALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 800 RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcSEREGALQEERADEAQQREEELRALQEELSQ 879
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 880 AKcssEEAQLEHAELQEQLHRANTDTAELGiqvcALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKE 959
Cdd:COG4942 165 LR---AELEAERAELEALLAELEEERAALE----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....*
gi 1894925332 960 SLQEK 964
Cdd:COG4942 238 AAAER 242
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
234-965 |
2.26e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 234 EMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQG--EQLQTERERGRTAAEDNVRLTCLVAELQKQWEV-TQATQN 310
Cdd:PRK04863 311 EMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEkiERYQADLEELEERLEEQNEVVEEADEQQEENEArAEAAEE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 311 TVKELQTCL----QGLELgAAEKEEDYHTALRRLESM-----LQPLAQE-LEATRDSLDKKNQHLASFpgwLAMAQQKAD 380
Cdd:PRK04863 391 EVDELKSQLadyqQALDV-QQTRAIQYQQAVQALERAkqlcgLPDLTADnAEDWLEEFQAKEQEATEE---LLSLEQKLS 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 381 TASDTKGRQE-----------PI-PSDAAQEMQEL----------GEKLQALERERTKVEEVNRQQsAQLEQLVKEL--- 435
Cdd:PRK04863 467 VAQAAHSQFEqayqlvrkiagEVsRSEAWDVARELlrrlreqrhlAEQLQQLRMRLSELEQRLRQQ-QRAERLLAEFckr 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 436 ------------QLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAelrrekkqqqeekel 503
Cdd:PRK04863 546 lgknlddedeleQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQD--------------- 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 504 leqevrSLTR-QLQFLETQL--AQVSQHVSDLEEQKKQLIQDKDHLSQQVGML----ERLAGPPGPELPVAGEKNEALVP 576
Cdd:PRK04863 611 ------ALARlREQSGEEFEdsQDVTEYMQQLLERERELTVERDELAARKQALdeeiERLSQPGGSEDPRLNALAERFGG 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 577 VnsSLQEAWgkpeeeqrglqeaqlDDTKVQEGSQEE----ELRQA--NRELEKELQNVVGRNQLLEgKLQALQADYQALQ 650
Cdd:PRK04863 685 V--LLSEIY---------------DDVSLEDAPYFSalygPARHAivVPDLSDAAEQLAGLEDCPE-DLYLIEGDPDSFD 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 651 QresaiqGSLASLEAEQASIRHLGD-QMEAS------LLAvRKAKEAmkaQMAEKEAILQSKEGECQQLREEVEQCQQLA 723
Cdd:PRK04863 747 D------SVFSVEELEKAVVVKIADrQWRYSrfpevpLFG-RAAREK---RIEQLRAEREELAERYATLSFDVQKLQRLH 816
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 724 EA------------------------------RHRELRALESQCQQQTQLIEvlTAEKGQQGVG-----------PPTDN 762
Cdd:PRK04863 817 QAfsrfigshlavafeadpeaelrqlnrrrveLERALADHESQEQQQRSQLE--QAKEGLSALNrllprlnlladETLAD 894
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 763 EARELAAQLA-LSQAQLEVHQGevQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEalNRAH 841
Cdd:PRK04863 895 RVEEIREQLDeAEEAKRFVQQH--GNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQ--RRAH 970
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 842 ------VQELLQCSEREGALQEERADEAQQRE---EELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQV 912
Cdd:PRK04863 971 fsyedaAEMLAKNSDLNEKLRQRLEQAEQERTrarEQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPA 1050
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1894925332 913 CaltvekERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKL 965
Cdd:PRK04863 1051 D------SGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL 1097
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
234-898 |
2.78e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 58.83 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 234 EMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQgEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVK 313
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQT-QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 314 ELQTCLQglELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLAsfpgwlAMAQQKADTASDTKgrqepip 393
Cdd:TIGR00618 281 ETQERIN--RARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA------AHVKQQSSIEEQRR------- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 394 sdAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEElSGKGQEADQLWRRL 473
Cdd:TIGR00618 346 --LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE-QATIDTRTSAFRDL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 474 QELLAHTSSWEEELAELRREKKQ----QQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQ 549
Cdd:TIGR00618 423 QGQLAHAKKQQELQQRYAELCAAaitcTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 550 VGMLERLAGPPGPELPVAGEKNEALVPV---------------------NSSLQEAWGKPEEEQRGLQEAQLDDTKVQEG 608
Cdd:TIGR00618 503 PCPLCGSCIHPNPARQDIDNPGPLTRRMqrgeqtyaqletseedvyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRS 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 609 SQE--------EELRQANRELEKELQNVVGRNQLLEGKLQALQADYQA---LQQRESAIQGSLASLEAEQASIrhLGDQM 677
Cdd:TIGR00618 583 KEDipnlqnitVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVrlhLQQCSQELALKLTALHALQLTL--TQERV 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 678 EASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLievltaekgqqgvg 757
Cdd:TIGR00618 661 REHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENA-------------- 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 758 pptdneareLAAQLALSQAQLEVHQGEVQRLQAQvvdlqakMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAL 837
Cdd:TIGR00618 727 ---------SSSLGSDLAAREDALNQSLKELMHQ-------ARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFF 790
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925332 838 NRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQL 898
Cdd:TIGR00618 791 NRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| FYVE_PKHF1 |
cd15754 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ... |
1170-1230 |
2.98e-08 |
|
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar proteins; Phafin-1, also termed lysosome-associated apoptosis-inducing protein containing PH (pleckstrin homology) and FYVE domains (LAPF), or pleckstrin homology domain-containing family F member 1 (PKHF1), or PH domain-containing family F member 1, or apoptosis-inducing protein, or PH and FYVE domain-containing protein 1, or zinc finger FYVE domain-containing protein 15, is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway.
Pssm-ID: 277293 [Multi-domain] Cd Length: 64 Bit Score: 51.88 E-value: 2.98e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925332 1170 WLGDTEANHCLDCKR-EFSWMVRRHHCRICGRIFCYYCCN-NYVLSKHGGKKERCCRACFQKL 1230
Cdd:cd15754 2 WIPDKATDICMRCTQtNFSLLTRRHHCRKCGFVVCHECSRqRFLIPRLSPKPVRVCSLCYRKL 64
|
|
| FYVE_FGD5 |
cd15742 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ... |
1179-1230 |
3.95e-08 |
|
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar proteins; FGD5, also termed zinc finger FYVE domain-containing protein 23, is an endothelial cell (EC)-specific guanine nucleotide exchange factor (GEF) that regulates endothelial adhesion, survival, and angiogenesis by modulating phosphatidylinositol 3-kinase signaling. It functions as a novel genetic regulator of vascular pruning by activation of endothelial cell-targeted apoptosis. FGD5 is a homologue of FGD1 and contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. The FYVE domain of FGD5 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.
Pssm-ID: 277281 [Multi-domain] Cd Length: 67 Bit Score: 51.47 E-value: 3.95e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1894925332 1179 CLDCKREFSWMVRRHHCRICGRIFCYYCC-NNYVLSKHGGKKERCCRACFQKL 1230
Cdd:cd15742 12 CMNCGSDFTLTLRRHHCHACGKIVCRNCSrNKYPLKYLKDRPAKVCDGCFAEL 64
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
219-965 |
4.57e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 219 DLNSPLNNEALEGFDEMRLELDQLEVREkqlrerMQQLDRENQ-----ELRAAVSQQGEQLQTERERGRTAAEDNVRLTC 293
Cdd:PTZ00121 1019 DFNQNFNIEKIEELTEYGNNDDVLKEKD------IIDEDIDGNhegkaEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEA 1092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 294 LVAELQKQWEVTQATQNTVKELQTCLQglelgAAEKEEDYHTA--LRRLESmlqplAQELEATRDSLDKKNQHLASfpgw 371
Cdd:PTZ00121 1093 TEEAFGKAEEAKKTETGKAEEARKAEE-----AKKKAEDARKAeeARKAED-----ARKAEEARKAEDAKRVEIAR---- 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 372 lamAQQKADTASDTKGRQEPIPSDAAQEMQELGEKlqaleRERTKVEEVNRQQSAQLEQLVKELqlkEDARASLERLVKE 451
Cdd:PTZ00121 1159 ---KAEDARKAEEARKAEDAKKAEAARKAEEVRKA-----EELRKAEDARKAEAARKAEEERKA---EEARKAEDAKKAE 1227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 452 MAPLQEELSGKGQEAdqlwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSD 531
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEA----KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 532 LEEQKKQLIQDK--DHLSQQVGMLERLAGPPGPELPVAGEKNEAlvpvnsSLQEAWGKPEEEQRGLQEAQLDDTKVQEGS 609
Cdd:PTZ00121 1304 ADEAKKKAEEAKkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEA------AKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 610 QE--------EELRQANrELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQA----SIRHLGDQM 677
Cdd:PTZ00121 1378 KKadaakkkaEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAkkadEAKKKAEEA 1456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 678 EASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEV----EQCQQLAEARHR--ELRALES--------QCQQQTQL 743
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAkkkaDEAKKAAEAKKKadEAKKAEEakkadeakKAEEAKKA 1536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 744 IEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLR-- 821
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKae 1616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 822 EHKTLVQQLKEQNEAlnRAHVQELLQCSEREGALQEE----------RADEAQQREEELRALQEELSQA---KCSSEEAQ 888
Cdd:PTZ00121 1617 EAKIKAEELKKAEEE--KKKVEQLKKKEAEEKKKAEElkkaeeenkiKAAEEAKKAEEDKKKAEEAKKAeedEKKAAEAL 1694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 889 LEHAELQ---EQLHRANTDTAELGIQV-CALTVEKERVEEALACAVQELQDAKEAasREREGLERQVAGLQQEKESLQEK 964
Cdd:PTZ00121 1695 KKEAEEAkkaEELKKKEAEEKKKAEELkKAEEENKIKAEEAKKEAEEDKKKAEEA--KKDEEEKKKIAHLKKEEEKKAEE 1772
|
.
gi 1894925332 965 L 965
Cdd:PTZ00121 1773 I 1773
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
579-1168 |
5.15e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.93 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 579 SSLQEAWGKPEEEQRGL--QEAQLDDTKVQEGSQEEELRQanrELEKELQNVVGRNQLLEGKLQALQADYQALQQ-RESA 655
Cdd:pfam12128 311 SAADAAVAKDRSELEALedQHGAFLDADIETAAADQEQLP---SWQSELENLEERLKALTGKHQDVTAKYNRRRSkIKEQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 656 IQGSLASLEAEQASIRhlgdqmeasllavrkakEAMKAQMAEKEAILQskeGECQQLREEVEQcqQLAEARhrelrales 735
Cdd:pfam12128 388 NNRDIAGIKDKLAKIR-----------------EARDRQLAVAEDDLQ---ALESELREQLEA--GKLEFN--------- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 736 qcQQQTQLIEVLTAEKGQQGVGPPTDnearELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSM 815
Cdd:pfam12128 437 --EEEYRLKSRLGELKLRLNQATATP----ELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQ 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 816 AEAVLREHKTLVQQLKEQNEAlnRAHvqELLQCSEREGALQEERADEAQQREEELRA-LQEELSQAKCSSEEA------- 887
Cdd:pfam12128 511 ASRRLEERQSALDELELQLFP--QAG--TLLHFLRKEAPDWEQSIGKVISPELLHRTdLDPEVWDGSVGGELNlygvkld 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 888 --QLEH---AELQEQLhRANTDTAELGIQvcALTVEKERVEEALACAVQELQDAKEAASREREGLE-------RQVAGLQ 955
Cdd:pfam12128 587 lkRIDVpewAASEEEL-RERLDKAEEALQ--SAREKQAAAEEQLVQANGELEKASREETFARTALKnarldlrRLFDEKQ 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 956 QEKESLQEKlkaakaaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEImdyqsrlknageeckslRGQLEEQ 1035
Cdd:pfam12128 664 SEKDKKNKA-------------LAERKDSANERLNSLEAQLKQLDKKHQ-AWLEEQ-----------------KEQKREA 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1036 GRQLQAAEEAVEKLKATQADM--GEKLSCTSNHLAECQAAMLRKDKEGAAL-------------REDLERTQKELEKATT 1100
Cdd:pfam12128 713 RTEKQAYWQVVEGALDAQLALlkAAIAARRSGAKAELKALETWYKRDLASLgvdpdviaklkreIRTLERKIERIAVRRQ 792
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925332 1101 KIQEYYNKLcQEVTNRERndQKMLADLDDLNRTKKYLEERLIELL----RDKDALWQKSDALEFQQKLSAEE 1168
Cdd:pfam12128 793 EVLRYFDWY-QETWLQRR--PRLATQLSNIERAISELQQQLARLIadtkLRRAKLEMERKASEKQQVRLSEN 861
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
767-1032 |
5.83e-08 |
|
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: 56.70 E-value: 5.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 767 LAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRahvqELL 846
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----ELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 847 QCSEREGALQEERADEAQQREEELRALQEelsqakcSSEEAQLEHAELQEQLHRANTDTAELGiqvcALTVEKERVEEAL 926
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYR-------LGRQPPLALLLSPEDFLDAVRRLQYLK----YLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 927 ACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQEAAhQELNTLKFQ 1006
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEA-EELEALIAR 231
|
250 260
....*....|....*....|....*.
gi 1894925332 1007 LSAEIMDYQSRLKNAGEecKSLRGQL 1032
Cdd:COG4942 232 LEAEAAAAAERTPAAGF--AALKGKL 255
|
|
| FYVE_scVPS27p_Vac1p_like |
cd15736 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1179-1227 |
6.42e-08 |
|
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; The family includes Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and protein VAC1 (Vac1p). scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The FYVE domain in both Vps27p and Vac1p harbors a zinc-binding site composed of seven Cysteines and one Histidine, which is different from that of other FYVE domain containing proteins.
Pssm-ID: 277275 [Multi-domain] Cd Length: 56 Bit Score: 50.64 E-value: 6.42e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1894925332 1179 CLDCKREFSWMVRRHHCRICGRIFC-YYCCNNYVLSKHG-----GKKERCCRACF 1227
Cdd:cd15736 2 CHTCSRTFNLNIRAHHCRKCGKLFCrRHLPNMIPLNLSAydprnGKWYRCCHSCF 56
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
400-924 |
6.76e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 6.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 400 MQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAH 479
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 480 TSSWEEElaelrrekkqqqeekelleqevRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLiqdkDHLSQQVGMLERlagp 559
Cdd:COG4717 128 LPLYQEL----------------------EALEAELAELPERLEELEERLEELRELEEEL----EELEAELAELQE---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 560 pgpelpvagEKNEALVPVNSSLQEAWGKPEEEQrglqeaqlddtkvqegsqeEELRQANRELEKELQNVVGRNQLLEGKL 639
Cdd:COG4717 178 ---------ELEELLEQLSLATEEELQDLAEEL-------------------EELQQRLAELEEELEEAQEELEELEEEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 640 QALQADYQALQQRES-AIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQ 718
Cdd:COG4717 230 EQLENELEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 719 CQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVgpptdnEARELAAQL--ALSQAQLEVHQGEVQRLQAQVvdlQ 796
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE------ELQELLREAeeLEEELQLEELEQEIAALLAEA---G 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 797 AKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcsEREGALQEERADEAQQRE---EELRAL 873
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEelrEELAEL 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1894925332 874 QEELSQAKCSSE--EAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEE 924
Cdd:COG4717 459 EAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
388-1090 |
8.77e-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: 57.11 E-value: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 388 RQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLK-------EDARASLERLVKEMAPLQEELS 460
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAEtelcaeaEEMRARLAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 461 GKGQEADQLWRRLQ----ELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQK 536
Cdd:pfam01576 82 SRLEEEEERSQQLQnekkKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 537 KQLIQDKDHLSQQVGMLERLAGPPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQE------AQLDDTKVQEGSQ 610
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEqiaelqAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 611 EEELRQANRELEKElqnvVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQasiRHLGDQMEasllAVRKAKEA 690
Cdd:pfam01576 242 EEELQAALARLEEE----TAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQR---RDLGEELE----ALKTELED 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 691 MKAQMAEKEAILQSKEGECQQLREEVEQ-----CQQLAEARHRELRALESQCQQQTQLIEVLTA-EKGQQGVgpptDNEA 764
Cdd:pfam01576 311 TLDTTAAQQELRSKREQEVTELKKALEEetrshEAQLQEMRQKHTQALEELTEQLEQAKRNKANlEKAKQAL----ESEN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 765 RELAAQL-ALSQAQLEVHQGEvQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQ 843
Cdd:pfam01576 387 AELQAELrTLQQAKQDSEHKR-KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 844 ELLQCSEREGALQEER------ADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTV 917
Cdd:pfam01576 466 LESQLQDTQELLQEETrqklnlSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 918 EKERVEEALACAVQELQDAKEAASReregLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQ--AEQRAQSLQ-- 993
Cdd:pfam01576 546 GKKRLQRELEALTQQLEEKAAAYDK----LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQmlAEEKAISARya 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 994 ------EAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEE-------QGRQLQAAEEAVEKLKATQADMGEKL 1060
Cdd:pfam01576 622 eerdraEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDlvsskddVGKNVHELERSKRALEQQVEEMKTQL 701
|
730 740 750
....*....|....*....|....*....|
gi 1894925332 1061 SCTSNHLAECQAAMLRKDKEGAALREDLER 1090
Cdd:pfam01576 702 EELEDELQATEDAKLRLEVNMQALKAQFER 731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
373-1108 |
1.14e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 373 AMAQQKAD-TASDTKGRQEPIPSDAAQEMQELGEKLQALER--ERTKVEEVNRQQSAQLEQLVKELQlkEDARASLERLV 449
Cdd:PTZ00121 1083 AKEDNRADeATEEAFGKAEEAKKTETGKAEEARKAEEAKKKaeDARKAEEARKAEDARKAEEARKAE--DAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 450 KEMAplQEELSGKGQEAdqlwRRLQEllAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHV 529
Cdd:PTZ00121 1161 EDAR--KAEEARKAEDA----KKAEA--ARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 530 SDL---EEQKKQLIQDKDHLSQQVGMLERLAGPPGPELPVAGE---KNEALVPVNSSLQEAWGKPEEEQRGLQEAQlddT 603
Cdd:PTZ00121 1233 EEAkkdAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEearKADELKKAEEKKKADEAKKAEEKKKADEAK---K 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 604 KVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLA 683
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 684 VRKAKEAMK--------AQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQtqliEVLTAEKGQQG 755
Cdd:PTZ00121 1390 KKKADEAKKkaeedkkkADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE----EAKKAEEAKKK 1465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 756 VGPPTDNEARELAAQLALSQAQLEvHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLK---E 832
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAK-KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaeE 1544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 833 QNEALNRAHVQELLQCSEREGALQEERADE---------------AQQREEELRALQEELSQAKCSSEEAQLEHAELQEQ 897
Cdd:PTZ00121 1545 KKKADELKKAEELKKAEEKKKAEEAKKAEEdknmalrkaeeakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 898 LHRANTDTAELGIQVCALTVEKERVEEAL----ACAVQELQDAKEAASREREGLERQVAglQQEKESLQEKLKAAKAAAG 973
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKkaeeENKIKAAEEAKKAEEDKKKAEEAKKA--EEDEKKAAEALKKEAEEAK 1702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 974 SLPGLQAQLAQAEQRAQSLQEAahQELNTLKfqlsaeimdyqsrlknaGEECKslRGQLEEQGRQLQAAEEAVEKLKATQ 1053
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKA--EEENKIK-----------------AEEAK--KEAEEDKKKAEEAKKDEEEKKKIAH 1761
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1894925332 1054 ADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNK 1108
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
606-832 |
1.53e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 606 QEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQ--ALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLA 683
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 684 VRKAKEAMKAQMAE--KEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEvltaekgqqgvgpptd 761
Cdd:COG3206 245 LRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ---------------- 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925332 762 neaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKE 832
Cdd:COG3206 309 ---QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
513-889 |
1.65e-07 |
|
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: 56.50 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 513 RQLQFLETQLAQVSQHVSDLEEQKKQLIQD----KDHLS------QQVGMLERLAGPPGPELPVAGEKNEALVPVNSSLQ 582
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDyqaaSDHLNlvqtalRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 583 EAwgkpeEEQRGLQEAQLDDTKVQEGSQEEEL----------RQANRELEKElQNVVGRNQL----LEGKLQALQADYQA 648
Cdd:COG3096 379 EA-----EARLEAAEEEVDSLKSQLADYQQALdvqqtraiqyQQAVQALEKA-RALCGLPDLtpenAEDYLAAFRAKEQQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 649 LQQRESAIQGSLASLEAEQAsirhlgdQMEASLLAVRKAKEAMKAQMAEKEAIlqskegecQQLREEVEQCQQLA----- 723
Cdd:COG3096 453 ATEEVLELEQKLSVADAARR-------QFEKAYELVCKIAGEVERSQAWQTAR--------ELLRRYRSQQALAQrlqql 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 724 EARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptdneaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAAL 803
Cdd:COG3096 518 RAQLAELEQRLRQQQNAERLLEEFCQRIGQQ----------LDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 804 DDQDKVQSQLSMAEAVLREHKTLVQQLKEQ-NEAL-NRAHVQELLQCS-EREGALQEERaDEAQQREEELRALQEELSQA 880
Cdd:COG3096 588 EQLRARIKELAARAPAWLAAQDALERLREQsGEALaDSQEVTAAMQQLlEREREATVER-DELAARKQALESQIERLSQP 666
|
....*....
gi 1894925332 881 KcSSEEAQL 889
Cdd:COG3096 667 G-GAEDPRL 674
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
860-1099 |
1.79e-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: 55.16 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 860 ADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAelgiqvcaltvekerveeALACAVQELQDAKEA 939
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA------------------ALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 940 ASREREGLERQVAGLQQEKESLQEKLKA---AKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQS 1016
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAEllrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1017 RLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELE 1096
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
...
gi 1894925332 1097 KAT 1099
Cdd:COG4942 241 ERT 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
436-690 |
2.29e-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: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 436 QLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELlahtssweeelaelrrekkqqqeekellEQEVRSLTRQL 515
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----------------------------ERRIAALARRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 516 QFLETQLAQVSQHVSDLEEQ----KKQLIQDKDHLSQQVGMLERLAGPPGPELPVAGEKNEALVPVNSSLQEAwgkpeEE 591
Cdd:COG4942 72 RALEQELAALEAELAELEKEiaelRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-----AP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 592 QRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIR 671
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*....
gi 1894925332 672 HLGDQMEASLLAVRKAKEA 690
Cdd:COG4942 227 ALIARLEAEAAAAAERTPA 245
|
|
| FYVE_MTMR_unchar |
cd15738 |
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ... |
1170-1227 |
2.44e-07 |
|
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from eumetazoa; This family includes a group of uncharacterized myotubularin-related proteins mainly found in eumetazoa. Although their biological functions remain unclear, they share similar domain architecture that consists of an N-terminal pleckstrin homology (PH) domain, a highly conserved region related to myotubularin proteins, a C-terminal FYVE domain. The model corresponds to the FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.
Pssm-ID: 277277 [Multi-domain] Cd Length: 61 Bit Score: 48.86 E-value: 2.44e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1170 WLGDTEANHClDCKREFSWMVRRHHCRICGRIFCYYCCNNYV-LSKH-GGKKERCCRACF 1227
Cdd:cd15738 3 WKSFRNVTEC-SCSTPFDHFSKKHHCWRCGNVFCTRCIDKQRaLPGHlSQRPVPVCRACY 61
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
590-802 |
3.03e-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: 54.38 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 590 EEQRGLQEAQLDDTKVQEGSQEEELRQANREL---EKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAE 666
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIaalARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 667 QASIRHLG-----------DQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALES 735
Cdd:COG4942 113 LYRLGRQPplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925332 736 QCQQQTQLIevltaekgqqgvgpptdneaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAA 802
Cdd:COG4942 193 LKAERQKLL--------------------ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
849-1167 |
3.20e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 849 SEREGALQEERADEAQQREEELRALQEELSQaKCSSEEAQLEHAELQEQLHRANTDTAELgiqvcALTVEKERVEE--AL 926
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERLNGLES-ELAELDEEIERYEEQREQARETRDEADE-----VLEEHEERREEleTL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 927 ACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAG----SLPGLQAQLAQAEQRAQSLQE------AA 996
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREELEDRDEELRDrleecrVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 997 HQELNTLKFQLSAEIMDYQSRLKNAGEECKSL-------RGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAE 1069
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELeseleeaREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1070 CQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLC-QEVTNRERNDQkmladLDDLNRTKKYLEERLIELLRDK 1148
Cdd:PRK02224 417 LREERDELREREAELEATLRTARERVEEAEALLEAGKCPECgQPVEGSPHVET-----IEEDRERVEELEAELEDLEEEV 491
|
330
....*....|....*....
gi 1894925332 1149 DALWQKSDALEFQQKLSAE 1167
Cdd:PRK02224 492 EEVEERLERAEDLVEAEDR 510
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
241-597 |
3.37e-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: 55.07 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 241 QLEVREKQLRERMQQLDRENQELRAAVSQQgEQLQTERERGRTAAEDNVRltclvaELQKQWEVTQATQNTVKELQTclq 320
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRI-ENRLDELSQELSDASRKIG------EIEKEIEQLEQEEEKLKERLE--- 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 321 glelgaaekeedyhtalrRLESMLQPLAQELEATRDSLDKKNQHLasfpgwlamAQQKADTASDTKGRQEPIPSDAAQEM 400
Cdd:TIGR02169 741 ------------------ELEEDLSSLEQEIENVKSELKELEARI---------EELEEDLHKLEEALNDLEARLSHSRI 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 401 QELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEmapLQEELSGKGQEADQLWRRLQELLAHT 480
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID---LKEQIKSIEKEIENLNGKKEELEEEL 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 481 SSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLErlagPP 560
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE----EI 946
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925332 561 GPELPVAG----------EKNEALVPVN--------------SSLQEAWGKPEEEQRGLQE 597
Cdd:TIGR02169 947 PEEELSLEdvqaelqrveEEIRALEPVNmlaiqeyeevlkrlDELKEKRAKLEEERKAILE 1007
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
316-963 |
3.66e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 316 QTCLQGLELGAAEKEE-DYHTALRRLEsmlqplaQELEATRDSLDKKNqhlasfpgwlamaqQKADTASDTKGRQEPIPS 394
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEkDLHERLNGLE-------SELAELDEEIERYE--------------EQREQARETRDEADEVLE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 395 DAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLvkelqlkEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQ 474
Cdd:PRK02224 245 EHEERREELETLEAEIEDLRETIAETEREREELAEEV-------RDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 475 EllahtssweeelaelrrekkqqqeekelleqevrsLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQvgmle 554
Cdd:PRK02224 318 E-----------------------------------LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER----- 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 555 rlagppgpelpvAGEKnealvpvnsslqeawgkpeEEQRGLQEAQLDDTKVQEGSQEEELrqanRELEKELQNVVGRNQL 634
Cdd:PRK02224 358 ------------AEEL-------------------REEAAELESELEEAREAVEDRREEI----EELEEEIEELRERFGD 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 635 LEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHlgdqmeasllAVRKAKEAMKAqmaekeailqSKEGECQQLRE 714
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARE----------RVEEAEALLEA----------GKCPECGQPVE 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 715 EVEQCQQLAEARHR------ELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRL 788
Cdd:PRK02224 463 GSPHVETIEEDRERveeleaELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 789 QAQVVDLQAKMRAALDDQDKVQSQlsmAEAVLREHKTLVQQLKEQNEALNR-AHVQELL----QCSEREGALQEERADEA 863
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEE---AEEAREEVAELNSKLAELKERIESlERIRTLLaaiaDAEDEIERLREKREALA 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 864 Q---QREEELRALQEELSQAKCSSEEAQLEhaELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAA 940
Cdd:PRK02224 620 ElndERRERLAEKRERKRELEAEFDEARIE--EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELR 697
|
650 660
....*....|....*....|....*.
gi 1894925332 941 SReREGLERQVAGLQ---QEKESLQE 963
Cdd:PRK02224 698 ER-REALENRVEALEalyDEAEELES 722
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
939-1177 |
3.80e-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: 54.00 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 939 AASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSlpgLQAQLAQAEQRAQSLQEAAhQELNTLKFQLSAEIMDYQSRL 1018
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA---LLKQLAALERRIAALARRI-RALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1019 KNAGEECKSLRGQLEEQGRQLQAAEEAVE-KLKATQAD------MGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERT 1091
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPlALLLSPEDfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1092 QKELEKATTKIQEYYNKLCQEVTNRERNdqkmladLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEERWL 1171
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKL-------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
....*.
gi 1894925332 1172 GDTEAN 1177
Cdd:COG4942 246 AGFAAL 251
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
251-1143 |
4.38e-07 |
|
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: 55.05 E-value: 4.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 251 ERMQQLdreNQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCLQGLE--LGAAE 328
Cdd:TIGR00606 189 ETLRQV---RQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEhnLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 329 KEEDYHTALRRLESMLQPLAQELEATRDSL----DKKNQHLASFPGwlAMAQQKADTASDTKGRQEPIpsdaAQEMQELG 404
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDLYHNHQ--RTVREKERELVDCQRELEKL----NKERRLLN 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 405 EKLQALERERTKVE---EVNRQQSAQLEQLVKELQLKEDAR-----ASLERLVKEMAPL-QEELSGKGQEADQLWRRLQE 475
Cdd:TIGR00606 340 QEKTELLVEQGRLQlqaDRHQEHIRARDSLIQSLATRLELDgfergPFSERQIKNFHTLvIERQEDEAKTAAQLCADLQS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 476 LLAHTsswEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSqqvgMLER 555
Cdd:TIGR00606 420 KERLK---QEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELS----KAEK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 556 LAGPPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVG---RN 632
Cdd:TIGR00606 493 NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGyfpNK 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 633 QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVR-KAKEAMKAQmaekeailqSKEGECQQ 711
Cdd:TIGR00606 573 KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEdKLFDVCGSQ---------DEESDLER 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 712 LREEVEQCQQ----LAEARH------RELRALESQC--------QQQTQLIEVLTAEKGQQGVGP----PTDNEARELAA 769
Cdd:TIGR00606 644 LKEEIEKSSKqramLAGATAvysqfiTQLTDENQSCcpvcqrvfQTEAELQEFISDLQSKLRLAPdklkSTESELKKKEK 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 770 QLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEA-------------VLREHKTLVQQLKEQNEA 836
Cdd:TIGR00606 724 RRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETllgtimpeeesakVCLTDVTIMERFQMELKD 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 837 LNRAHVQEL--LQCSEREGALQEERaDEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCA 914
Cdd:TIGR00606 804 VERKIAQQAakLQGSDLDRTVQQVN-QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 915 LTVEKERVEEaLACAVQELQDAKEAASREREGLERQVAGLQQEKESLQeklkaakaaagslpglqaqlaqaeQRAQSLQE 994
Cdd:TIGR00606 883 RQQFEEQLVE-LSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELI------------------------SSKETSNK 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 995 AAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAA-EEAVEKLKATQADMGE-KLSCTSNHLAEC-- 1070
Cdd:TIGR00606 938 KAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQlEECEKHQEKINEDMRLmRQDIDTQKIQERwl 1017
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925332 1071 --QAAMLRKDKEGAALREDLERTQKEL-EKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIE 1143
Cdd:TIGR00606 1018 qdNLTLRKRENELKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
784-1166 |
4.89e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 784 EVQRLQAQVVDLQAKM---RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAlnRAHVQELLQCsEREGALQEERA 860
Cdd:COG4717 72 ELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQL--LPLYQELEAL-EAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 861 DEAQQREEELRALQEELsqakcssEEAQLEHAELQEQLHRANTDTAELGIQvcALTVEKERVEEALAcAVQELQDAKEAA 940
Cdd:COG4717 149 EELEERLEELRELEEEL-------EELEAELAELQEELEELLEQLSLATEE--ELQDLAEELEELQQ-RLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 941 SREREGLERQVAGLQQEKESLQEK------------------LKAAKAAAGSLP-----------GLQAQLAQAEQRAQS 991
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEerlkearlllliaaallaLLGLGGSLLSLIltiagvlflvlGLLALLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 992 LQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNH--LAE 1069
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAalLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1070 CQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVtnRERNDQKMLADLDDLNRTKKYLEERLIELLRDKD 1149
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL--EALDEEELEEELEELEEELEELEEELEELREELA 456
|
410
....*....|....*..
gi 1894925332 1150 ALWQKSDALEFQQKLSA 1166
Cdd:COG4717 457 ELEAELEQLEEDGELAE 473
|
|
| RUN_RUFY1 |
cd17694 |
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ... |
32-135 |
5.72e-07 |
|
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.
Pssm-ID: 439056 Cd Length: 156 Bit Score: 50.67 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 32 GEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRTSLGKGRAFIRYS 111
Cdd:cd17694 24 GRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIATSARNLPELKTAVGRGRAWLHLA 103
|
90 100
....*....|....*....|....
gi 1894925332 112 LVHQRLADTLQQCFMNTKVTSDWY 135
Cdd:cd17694 104 LMQKKLADYLKVLIDRKDLLSEFY 127
|
|
| RUN_RUNDC3B |
cd17700 |
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ... |
33-135 |
8.08e-07 |
|
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN domain-containing protein 3B (RUNDC3B), also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. RUNDC3B contains a RUN domain.
Pssm-ID: 439062 Cd Length: 151 Bit Score: 50.35 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 33 EPITDDSTSLHKFSYKLEYLLQFDQKEKATLLG--NKKDYWDYFCACLAKVkgANDGIRFVKSISELRTSLGKGRAFIRY 110
Cdd:cd17700 20 ETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGyeSPRSFWDYIRVACSKV--PHNCICSIENMENVSSSRAKGRAWIRV 97
|
90 100
....*....|....*....|....*
gi 1894925332 111 SLVHQRLADTLQQCFMNTKVTSDWY 135
Cdd:cd17700 98 ALMEKRLSEYISTALRDFKTTRRFY 122
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
690-941 |
8.96e-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: 52.84 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 690 AMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQqgvgppTDNEARELAA 769
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA------LEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 770 QLALSQAQLEVHQGEVQRL--QAQVVDLQAKMRAALDDQDKVQSQ--LSMAEAVLREHKTLVQQLKEQNEALNRAHvqel 845
Cdd:COG4942 91 EIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVrrLQYLKYLAPARREQAEELRADLAELAALR---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 846 lqcseregALQEERADEAQQREEELRALQEELSQAKcsseeaqlehAELQEQLHRANTDTAELGIQVCALTVEKERVEEA 925
Cdd:COG4942 167 --------AELEAERAELEALLAELEEERAALEALK----------AERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250
....*....|....*.
gi 1894925332 926 LACAVQELQDAKEAAS 941
Cdd:COG4942 229 IARLEAEAAAAAERTP 244
|
|
| FYVE1_Vac1p_like |
cd15761 |
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ... |
1170-1238 |
9.88e-07 |
|
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the first FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.
Pssm-ID: 277300 Cd Length: 76 Bit Score: 47.65 E-value: 9.88e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925332 1170 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYV-LSKHG------GKKERCCRACFqklSEGPGSPD 1238
Cdd:cd15761 4 WKKPSGKSRCSECGKTLNKKNGIVNCRKCGELFCNEHCRNRIkLNNSAeydpknGKWCRCCEKCF---TSRPGYND 76
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
638-887 |
1.02e-06 |
|
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: 52.84 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 638 KLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQskegecqQLREEVE 717
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 718 QCQQLAEARHRELRALESQCQ---QQTQLIEVLTAEkgqqgvgpptdnEARELAAQLALSQAQLEVHQGEVQRLQAQVVD 794
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYrlgRQPPLALLLSPE------------DFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 795 LQAKMRAALDDQDKVQSQLSMAEAvlrEHKTLVQQLKEQNEALNRAhvqellqcsEREGALQEERADEAQQREEELRALQ 874
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEE---ERAALEALKAERQKLLARL---------EKELAELAAELAELQQEAEELEALI 229
|
250
....*....|...
gi 1894925332 875 EELSQAKCSSEEA 887
Cdd:COG4942 230 ARLEAEAAAAAER 242
|
|
| RUN_RUFY2 |
cd17695 |
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ... |
32-164 |
1.20e-06 |
|
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. This model represents the RUN domain of RUFY2.
Pssm-ID: 439057 Cd Length: 156 Bit Score: 49.98 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 32 GEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRTSLGKGRAFIRYS 111
Cdd:cd17695 24 GRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIAASVRDLPGLKTPLGRARAWLRLA 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1894925332 112 LVHQRLADTLQQCFMNTKVTSDWYYARSPFLQPKlSSDIVGQLYELTEVQFDL 164
Cdd:cd17695 104 LMQKKLADYLRCLIIRRDLLSEFYEYHALMMEEE-GAVIVGLLVGLNVIDANL 155
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
515-871 |
1.31e-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: 53.42 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 515 LQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLagppgpeLPVAGEKNEAlvpvnsSLQEAWGKPEEEQRG 594
Cdd:COG3096 838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKL-------LPQANLLADE------TLADRLEELREELDA 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 595 LQEAQLddtkvqegsqeeELRQANRELEkELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLG 674
Cdd:COG3096 905 AQEAQA------------FIQQHGKALA-QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFS 971
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 675 DQMEASLLAVRKA-KEAMKAQMAEKEAilqskegECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQ 753
Cdd:COG3096 972 YEDAVGLLGENSDlNEKLRARLEQAEE-------ARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEE 1044
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 754 QGVGPPTDNEAR------ELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlreHKTLV 827
Cdd:COG3096 1045 LGVQADAEAEERarirrdELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKA----GWCAV 1120
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1894925332 828 QQLKEQNEALNRAHVQELLQCSERE---------GALQEERADeaqqrEEELR 871
Cdd:COG3096 1121 LRLARDNDVERRLHRRELAYLSADElrsmsdkalGALRLAVAD-----NEHLR 1168
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
813-1159 |
1.35e-06 |
|
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: 53.10 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 813 LSMAEAVLREHKTLVQQ---LKEQNEALNRAhvqellqcseregalQEERADEAQQREEELRALQEELSQAKCSSEEAQL 889
Cdd:TIGR04523 203 LSNLKKKIQKNKSLESQiseLKKQNNQLKDN---------------IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 890 EHAELQEQLHRANTDTAELGIQVCALTVE-----KERVEEALACAVQELQDAKEaasrEREGLERQVAGLQQEKESLQEK 964
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEisdlnNQKEQDWNKELKSELKNQEK----KLEEIQNQISQNNKIISQLNEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 965 LKAAKAAAGSLPG----LQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQ 1040
Cdd:TIGR04523 344 ISQLKKELTNSESenseKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1041 AAEEAVEKLKATQADMGEKLSCTSNhlaecqaamlrKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRERND 1120
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTN-----------QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
330 340 350
....*....|....*....|....*....|....*....
gi 1894925332 1121 QKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALE 1159
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
514-740 |
1.45e-06 |
|
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: 52.46 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 514 QLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERlagppgpelpvagekneALVPVNSSLQEAwgkpeEEQR 593
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-----------------RIAALARRIRAL-----EQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 594 GLQEAQLDDTKVQEGSQEEELRQANRELEKELQNV--VGRNQLLEG------------KLQALQADYQALQQRESAIQGS 659
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLRALyrLGRQPPLALllspedfldavrRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 660 LASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQ 739
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
.
gi 1894925332 740 Q 740
Cdd:COG4942 239 A 239
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
648-1169 |
1.50e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 648 ALQQRESAIQGSLASLEAEQASIRH-LG-DQMEASLLAVRKAKEAMKAQMAEKEAILQSKEgECQQLREEVEQcqQLAEA 725
Cdd:PRK03918 129 AIYIRQGEIDAILESDESREKVVRQiLGlDDYENAYKNLGEVIKEIKRRIERLEKFIKRTE-NIEELIKEKEK--ELEEV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 726 RhRELRALESQCQQQTQLIEVLTAEKgqqgvgpptdNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQ---AKMRAA 802
Cdd:PRK03918 206 L-REINEISSELPELREELEKLEKEV----------KELEELKEEIEELEKELESLEGSKRKLEEKIRELEeriEELKKE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 803 LDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRahVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKC 882
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE--IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 883 SSEEAQLEHAELQE---QLHRANTDTAELGIQvcaltvEKERVEEALacavQELQDAKEAASREREGLERQVAGLQQEKE 959
Cdd:PRK03918 353 RLEELEERHELYEEakaKKEELERLKKRLTGL------TPEKLEKEL----EELEKAKEEIEEEISKITARIGELKKEIK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 960 SLQEKLKAAKAAAGSLPGLQAQLAqaEQRAQSLQEAAHQELNtlkfQLSAEIMDYQSRLKNAGEECKSLRGQLEEQgRQL 1039
Cdd:PRK03918 423 ELKKAIEELKKAKGKCPVCGRELT--EEHRKELLEEYTAELK----RIEKELKEIEEKERKLRKELRELEKVLKKE-SEL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1040 QAAEEAVEKLKATQadmgEKLSCTSnhlaecqaamlrkdkegaalREDLERTQKELEKattkIQEYYNKLCQEVTNRERN 1119
Cdd:PRK03918 496 IKLKELAEQLKELE----EKLKKYN--------------------LEELEKKAEEYEK----LKEKLIKLKGEIKSLKKE 547
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1120 dqkmLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEER 1169
Cdd:PRK03918 548 ----LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
579-1111 |
1.68e-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: 52.80 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 579 SSLQEAWGKPEEEQRGLQEAQLDDTKV----QEGSQE--------------------------EELRQANRELEKELQNV 628
Cdd:pfam05483 106 NKLQENRKIIEAQRKAIQELQFENEKVslklEEEIQEnkdlikennatrhlcnllketcarsaEKTKKYEYEREETRQVY 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 629 VGRNQLLEGKLQALQadyQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEA-------I 701
Cdd:pfam05483 186 MDLNNNIEKMILAFE---ELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENkmkdltfL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 702 LQSKEGECQQLREEV----EQCQQLAEARHRELRALES-QCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQA 776
Cdd:pfam05483 263 LEESRDKANQLEEKTklqdENLKELIEKKDHLTKELEDiKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNK 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 777 QLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKE--QNEALNRAHVQELLqcSEREGA 854
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKfkNNKEVELEELKKIL--AEDEKL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 855 LQEERADEA----------------QQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVE 918
Cdd:pfam05483 421 LDEKKQFEKiaeelkgkeqelifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLE 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 919 KERVEEALACAVQELQDAKE---AASREREGLERQVAGLQQEKESLQEKLKAAKAA-AGSLPGLQAQLAQAEQRAQSLQE 994
Cdd:pfam05483 501 NKELTQEASDMTLELKKHQEdiiNCKKQEERMLKQIENLEEKEMNLRDELESVREEfIQKGDEVKCKLDKSEENARSIEY 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 995 AAHQELNTLKF------QLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKL-SCTSNHL 1067
Cdd:pfam05483 581 EVLKKEKQMKIlenkcnNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFeEIIDNYQ 660
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1894925332 1068 AECQAAMLRKDKegaaLREDLERTQKELEKAtTKIQEYYNKLCQ 1111
Cdd:pfam05483 661 KEIEDKKISEEK----LLEEVEKAKAIADEA-VKLQKEIDKRCQ 699
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
611-965 |
1.77e-06 |
|
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: 52.20 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 611 EEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEA 690
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 691 MKAqmaEKEAILQSKEGECQQLREEVEQCQQLAEA---RHRELRALESQCQQQT-QLIEVLTAEKGQQGVGPPTDNEARE 766
Cdd:pfam07888 113 LSE---EKDALLAQRAAHEARIRELEEDIKTLTQRvleRETELERMKERAKKAGaQRKEEEAERKQLQAKLQQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 767 LAAQLALSQAQLEVHQGEVQRLQAQVVDLQ----------AKMRAALDDQDKVQSQLSM----AEAVLREHKTLVQQLKE 832
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTqklttahrkeAENEALLEELRSLQERLNAserkVEGLGEELSSMAAQRDR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 833 QNEALNRAHVQEL---LQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELG 909
Cdd:pfam07888 270 TQAELHQARLQAAqltLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELG 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925332 910 IQV-CALTVEKERVEEalacaVQELQDAKEAASREREGLERQVAGLQQEKESLQEKL 965
Cdd:pfam07888 350 REKdCNRVQLSESRRE-----LQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| FYVE_WDFY1_like |
cd15718 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ... |
1174-1227 |
1.82e-06 |
|
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and similar proteins; This family includes WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2. WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. Both WDFY1 and WDFY2 contain a FYVE domain and multiple WD-40 repeats.
Pssm-ID: 277258 [Multi-domain] Cd Length: 70 Bit Score: 46.93 E-value: 1.82e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925332 1174 TEANHCLDCKREFSW----M-------VRRHHCRICGRIFCYYCCNNY-VLSKHGGKKE-RCCRACF 1227
Cdd:cd15718 4 AESDNCQKCSRPFFWnfkqMwekktlgVRQHHCRKCGKAVCDKCSSNRsTIPVMGFEFPvRVCNECY 70
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
403-806 |
2.35e-06 |
|
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: 51.82 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 403 LGEKLQALERERTkveEVNRQQSAQLEQLVKELQLKEDARASLERLVKEM----APLQEELSGKGQEADQLWRRLQELLA 478
Cdd:pfam07888 32 LQNRLEECLQERA---ELLQAQEAANRQREKEKERYKRDREQWERQRRELesrvAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 479 HTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLErlag 558
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTE---- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 559 ppgpelpvageknEALVPVNSSLQEAwgKPEEEQRGLQEAQLDDTKVQegsqeeelrqanrelekeLQNVVGRNQLLEGK 638
Cdd:pfam07888 185 -------------EELRSLSKEFQEL--RNSLAQRDTQVLQLQDTITT------------------LTQKLTTAHRKEAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 639 LQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAekEAILQSKEGECQQLREEvEQ 718
Cdd:pfam07888 232 NEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLA--DASLALREGRARWAQER-ET 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 719 CQQLAEARH-------RELRALESQCQQQTQLIEVLTAEKGQQ-----GVGPPTDNEARELAAQLALSQAQLEVHQGEVQ 786
Cdd:pfam07888 309 LQQSAEADKdrieklsAELQRLEERLQEERMEREKLEVELGREkdcnrVQLSESRRELQELKASLRVAQKEKEQLQAEKQ 388
|
410 420
....*....|....*....|
gi 1894925332 787 RLQAQVVDLQAKMRAALDDQ 806
Cdd:pfam07888 389 ELLEYIRQLEQRLETVADAK 408
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
681-1161 |
2.99e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 681 LLAVRKAKEAMKAQMAEKEAILQSKEGecqqlREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgppt 760
Cdd:TIGR00618 148 LLPQGEFAQFLKAKSKEKKELLMNLFP-----LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDT------ 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 761 dneARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKmraaLDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRA 840
Cdd:TIGR00618 217 ---YHERKQVLEKELKHLREALQQTQQSHAYLTQKREA----QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 841 --------HVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQv 912
Cdd:TIGR00618 290 rkaaplaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 913 caltvEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLaQAEQRAQSL 992
Cdd:TIGR00618 369 -----EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ-ELQQRYAEL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 993 QEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAEC-- 1070
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdn 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1071 ----QAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNK---LCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIE 1143
Cdd:TIGR00618 523 pgplTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQmqeIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602
|
490
....*....|....*...
gi 1894925332 1144 LLRDKDALWQKSDALEFQ 1161
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRK 620
|
|
| RUN |
pfam02759 |
RUN domain; This domain is present in several proteins that are linked to the functions of ... |
49-164 |
3.64e-06 |
|
RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.
Pssm-ID: 460679 Cd Length: 134 Bit Score: 48.04 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 49 LEYLLQ------FDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRT---SLGKGRAFIRYSLVHQRLAD 119
Cdd:pfam02759 6 LEALLShglkrsSLLILRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNEKLLDQ 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1894925332 120 TLQQCFMNTKVTSDWYYARSPFLQPKLSSDIVGQLYELTEVQFDL 164
Cdd:pfam02759 86 WLKLLLSNKELLSEYYEPWALLADPEFGEILLGLLVGLSALDFNL 130
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
763-895 |
4.74e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 50.43 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 763 EARELAAQLALSQAQLEVHQGEVQRLQAQVvDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHV 842
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARLEAEL-GAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARA 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1894925332 843 QELLQCSEREGALQEERADEAQQRE-EELRALQEELSQAkcsseEAQLEHAELQ 895
Cdd:COG1566 156 ALDAAQAQLEAAQAQLAQAQAGLREeEELAAAQAQVAQA-----EAALAQAELN 204
|
|
| RUN_RUFY3 |
cd17696 |
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ... |
32-143 |
4.91e-06 |
|
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. This model represents the RUN domain of RUFY3.
Pssm-ID: 439058 Cd Length: 156 Bit Score: 48.07 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 32 GEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRTSLGKGRAFIRYS 111
Cdd:cd17696 24 GRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLA 103
|
90 100 110
....*....|....*....|....*....|..
gi 1894925332 112 LVHQRLADTLQQCFMNTKVTSDWYYARSPFLQ 143
Cdd:cd17696 104 LMQKKLSEYMKALINRKDLLSEFYEPNALMME 135
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
226-679 |
5.16e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 226 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERgRTAAEDNVRLTCLVAE--LQKQWE 303
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE-RDDLLAEAGLDDADAEavEARREE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 304 VTQATQNTVKELQTCLQGLEL------GAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQ 377
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAhneeaeSLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 378 KADTASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLE--------QLVKE---LQLKEDARASLE 446
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgQPVEGsphVETIEEDRERVE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 447 RLVKEMAPLQEELSGKGQEADQLwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQ-- 524
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEkr 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 525 ------------VSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGpPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQ 592
Cdd:PRK02224 558 eaaaeaeeeaeeAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREALAELNDERRERLAEKRERK 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 593 RGLqEAQLDDTKVqegsqeEELRQANRELEKELQNVvgrnqllEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRH 672
Cdd:PRK02224 637 REL-EAEFDEARI------EEAREDKERAEEYLEQV-------EEKLDELREERDDLQAEIGAVENELEELEELRERREA 702
|
....*..
gi 1894925332 673 LGDQMEA 679
Cdd:PRK02224 703 LENRVEA 709
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
609-1159 |
6.65e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 609 SQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQ---QRESAIQGSLASLEAEQASIRHLGDQMEASLLAVR 685
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 686 KAKEAMKAQMAEkeaiLQSKEGECQQLREEVEqcqqlaeaRHRELRALESQCQQQTQLIEVLTAEkgqqgvgppTDNEAR 765
Cdd:PRK03918 266 ERIEELKKEIEE----LEEKVKELKELKEKAE--------EYIKLSEFYEEYLDELREIEKRLSR---------LEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 766 ELAAQLAlsqaQLEVHQGEVQRLQAQVVDLQAKMrAALDDQDKVQSQLSMAEAVLREHKTlvqqlKEQNEALNRAhVQEL 845
Cdd:PRK03918 325 GIEERIK----ELEEKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKK-----RLTGLTPEKL-EKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 846 LQCSEREGALQEE------RADEAQQREEELRALQEELSQAK-----CSSEEAQLEHAELQE----QLHRANTDTAELGI 910
Cdd:PRK03918 394 EELEKAKEEIEEEiskitaRIGELKKEIKELKKAIEELKKAKgkcpvCGRELTEEHRKELLEeytaELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 911 QVCALTVEKERVEEALAcAVQELQDAKEAASREREgLERQVAGLQQEKesLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQ 990
Cdd:PRK03918 474 KERKLRKELRELEKVLK-KESELIKLKELAEQLKE-LEEKLKKYNLEE--LEKKAEEYEKLKEKLIKLKGEIKSLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 991 SLQEaahqelntlkfqLSAEIMDYQSRLKNAGEECKSLRGQLEEQGrqLQAAEEAVEKLKATQADMGEKLScTSNHLAEC 1070
Cdd:PRK03918 550 KLEE------------LKKKLAELEKKLDELEEELAELLKELEELG--FESVEELEERLKELEPFYNEYLE-LKDAEKEL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1071 QAAMLRKDKEGAAL---REDLERTQKELEKATTKI--------QEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEE 1139
Cdd:PRK03918 615 EREEKELKKLEEELdkaFEELAETEKRLEELRKELeelekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
570 580
....*....|....*....|
gi 1894925332 1140 RLIELLRDKDALWQKSDALE 1159
Cdd:PRK03918 695 TLEKLKEELEEREKAKKELE 714
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
236-733 |
7.06e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 236 RLELDQLEVREKQLRERMQQLDrENQELRAAVSQQGEQLQTERERgRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKEL 315
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAE-LEELREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 316 QTCLQGLElgaaEKEEDYHTALRRLESmlqpLAQELEATRDSLDKKNQHLaSFPGWLAMaqqkadtasdtkgrqepipSD 395
Cdd:COG4717 145 PERLEELE----ERLEELRELEEELEE----LEAELAELQEELEELLEQL-SLATEEEL-------------------QD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 396 AAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARaslerlvkemaplqeelsgKGQEADQLWRRLQE 475
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-------------------RLKEARLLLLIAAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 476 LLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLsqqvgmler 555
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL--------- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 556 lagppGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLddtkvqEGSQEEELRQANRELEKELQNVVGRNQLL 635
Cdd:COG4717 329 -----GLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL------EQEIAALLAEAGVEDEEELRAALEQAEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 636 EGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHlgDQMEASLLAVRKAKEAMKAQMAEKEAILQ--SKEGECQQLR 713
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEELEEEL--EELEEELEELEEELEELREELAELEAELEqlEEDGELAELL 475
|
490 500
....*....|....*....|
gi 1894925332 714 EEVEQCQQLAEARHRELRAL 733
Cdd:COG4717 476 QELEELKAELRELAEEWAAL 495
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
762-999 |
7.64e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 762 NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREH----------KTLVQQL- 830
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsVSYLDVLl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 831 --KEQNEALNRAHVQELLQcseregALQEERADEAQQREEELRALQEELSQAKcssEEAQLEHAELQEQLHRANTDTAEL 908
Cdd:COG3883 110 gsESFSDFLDRLSALSKIA------DADADLLEELKADKAELEAKKAELEAKL---AELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 909 GIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQR 988
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAG 260
|
250
....*....|.
gi 1894925332 989 AQSLQEAAHQE 999
Cdd:COG3883 261 SAGAAGAAAGA 271
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
226-452 |
1.14e-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: 50.06 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 226 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVT 305
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 306 QAT-----------QNTVKELQTCLQGLELGAAEKEEDYHTALRRLESM---LQPLAQELEATRDSLDKKNQHLASFPGW 371
Cdd:TIGR02168 851 SEDieslaaeieelEELIEELESELEALLNERASLEEALALLRSELEELseeLRELESKRSELRRELEELREKLAQLELR 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 372 LAMAQQKADT--------ASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVN-------RQQSAQLEQLVKELQ 436
Cdd:TIGR02168 931 LEGLEVRIDNlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNlaaieeyEELKERYDFLTAQKE 1010
|
250
....*....|....*.
gi 1894925332 437 LKEDARASLERLVKEM 452
Cdd:TIGR02168 1011 DLTEAKETLEEAIEEI 1026
|
|
| FYVE_protrudin |
cd15723 |
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ... |
1179-1230 |
1.32e-05 |
|
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc finger FYVE domain-containing protein 27 (ZFY27 or ZFYVE27), is a FYVE domain-containing protein involved in transport of neuronal cargoes and implicated in the onset of hereditary spastic paraplegia (HSP). It is involved in neurite outgrowth through binding to spastin. Moreover, it functions as a key regulator of the Rab11-dependent membrane trafficking during neurite extension. It serves as an adaptor molecule that links its associated proteins, such as Rab11-GDP, VAP-A and -B, Surf4, and RTN3, to KIF5, a motor protein that mediates anterograde vesicular transport in neurons, and thus plays a key role in the maintenance of neuronal function. The FYVE domain of protrudin resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. In addition, unlike canonical FYVE domains that is located to early endosomes and specifically binds to phosphatidylinositol 3-phosphate (PtdIns3P or PI3P), the FYVE domain of protrudin is located to plasma membrane and preferentially binds phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2), and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). In addition to FYVE-related domain, protrudin also contains a Rab11-binding domain (RBD11), two hydrophobic domains, HP-1 and HP-2, an FFAT motif, and a coiled-coil domain.
Pssm-ID: 277262 [Multi-domain] Cd Length: 62 Bit Score: 44.03 E-value: 1.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925332 1179 CLDCKREFS-WMVRRHHCRICGRIFCYYCCNNYVLSKHGG------KKE--RCCRACFQKL 1230
Cdd:cd15723 2 CTGCGASFSvLLKKRRSCNNCGNAFCSRCCSKKVPRSVMGatapaaQREtvFVCSGCNDKL 62
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
686-1167 |
1.54e-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: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 686 KAKEAMKAQMAEKEAILQSKEGECQQLREEVEQ----CQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptd 761
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIIEAqrkaIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLC------- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 762 NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQdKVQSQLSMAEA--VLREHKTLVQQLKE--QNEAL 837
Cdd:pfam05483 158 NLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL-RVQAENARLEMhfKLKEDHEKIQHLEEeyKKEIN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 838 NRAHVQELL--QCSEREGALQ------EERADEAQQREEELRALQEELSQA--KCSSEEAQLEHAELQEQLHRANTDTAE 907
Cdd:pfam05483 237 DKEKQVSLLliQITEKENKMKdltfllEESRDKANQLEEKTKLQDENLKELieKKDHLTKELEDIKMSLQRSMSTQKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 908 LGIQV-----CALTVEKErveealaCAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLP-GLQAQ 981
Cdd:pfam05483 317 EDLQIatktiCQLTEEKE-------AQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITmELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 982 LAQAEQRAQsLQEAAHQELNTLKFQLSAE--IMDYQSRLKNAGEEcksLRGQLEEQGRQLQAAEEAVEKLKATQADMGEK 1059
Cdd:pfam05483 390 SSELEEMTK-FKNNKEVELEELKKILAEDekLLDEKKQFEKIAEE---LKGKEQELIFLLQAREKEIHDLEIQLTAIKTS 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1060 LSCTSNHLAECQAAMLR---KDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKY 1136
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKeklKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN 545
|
490 500 510
....*....|....*....|....*....|.
gi 1894925332 1137 LEErliELLRDKDALWQKSDALEFQQKLSAE 1167
Cdd:pfam05483 546 LRD---ELESVREEFIQKGDEVKCKLDKSEE 573
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
610-1100 |
1.68e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.80 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 610 QEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAiQGSLASLEAEQ--ASIRHLGD---QMEASLLAV 684
Cdd:PRK10246 231 EEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKA-QPQLAALSLAQpaRQLRPHWEriqEQSAALAHT 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 685 RKAKEAMKAQMAEKEA----ILQSKEGECQQLREEVEQCQQ-LAEAR-----HREL---RALESQC----QQQTQLIEVL 747
Cdd:PRK10246 310 RQQIEEVNTRLQSTMAlrarIRHHAAKQSAELQAQQQSLNTwLAEHDrfrqwNNELagwRAQFSQQtsdrEQLRQWQQQL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 748 TAEKGQQGVGPPT--DNEARELAAQLALSQAQLEVHQgEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKt 825
Cdd:PRK10246 390 THAEQKLNALPAItlTLTADEVAAALAQHAEQRPLRQ-RLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMR- 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 826 lvQQLKEQNEALNRahVQELLQCSEREGALQEERA---------------------------DEAQQR----EEELRALQ 874
Cdd:PRK10246 468 --QRYKEKTQQLAD--VKTICEQEARIKDLEAQRAqlqagqpcplcgstshpaveayqalepGVNQSRldalEKEVKKLG 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 875 EELSQAKcsseeAQLEhaELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAK----EAASRERE----- 945
Cdd:PRK10246 544 EEGAALR-----GQLD--ALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQpwldAQEEHERQlrlls 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 946 ----------GLERQVAGLQQEKESLQEKLKAAKAAAG-SLPGLQAQ---LAQAEQRAQSLQeAAHQELNTLKFQLSA-- 1009
Cdd:PRK10246 617 qrhelqgqiaAHNQQIIQYQQQIEQRQQQLLTALAGYAlTLPQEDEEaswLATRQQEAQSWQ-QRQNELTALQNRIQQlt 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1010 ---------EIMDYQS------RLKNAGEECKSLRGQLEEQGRQlqaaeEAVEKLKATQADMGEKLSCTSNHLAECQA-- 1072
Cdd:PRK10246 696 plletlpqsDDLPHSEetvaldNWRQVHEQCLSLHSQLQTLQQQ-----DVLEAQRLQKAQAQFDTALQASVFDDQQAfl 770
|
570 580
....*....|....*....|....*...
gi 1894925332 1073 AMLRKDKEGAALREDLERTQKELEKATT 1100
Cdd:PRK10246 771 AALLDEETLTQLEQLKQNLENQRQQAQT 798
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
777-1141 |
1.97e-05 |
|
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: 49.25 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 777 QLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTL-------VQQLKEQNEALNRAHVQELLQCS 849
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKikelekqLNQLKSEISDLNNQKEQDWNKEL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 850 EREGALQEERADEAQ----QREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEA 925
Cdd:TIGR04523 313 KSELKNQEKKLEEIQnqisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 926 LACAVQELQDAKEaasrEREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQ------E 999
Cdd:TIGR04523 393 INDLESKIQNQEK----LNQQKDEQIKKLQQEKELLEKEIER----------LKETIIKNNSEIKDLTNQDSVkeliikN 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1000 LNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDK 1079
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925332 1080 EGAALREDLER-----TQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERL 1141
Cdd:TIGR04523 539 KISDLEDELNKddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
698-963 |
2.06e-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: 48.74 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 698 KEAILQSKEGECQQLREEVEQCQQLA------------------EARHRELRA----LESQCQQQTQLIEVLTAE-KGQQ 754
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAAnrqrekekerykrdreqwERQRRELESrvaeLKEELRQSREKHEELEEKyKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 755 GVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQN 834
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 835 EALNRAHVQELLQCSEREGALQE---------ERADEAQQRE-------EELRALQEELSQAKCSSEEAQLEHAEL---- 894
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQlqdtittltQKLTTAHRKEaeneallEELRSLQERLNASERKVEGLGEELSSMaaqr 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925332 895 ---QEQLHRANTDTAELGIQVCALTVEkerVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQE 963
Cdd:pfam07888 268 drtQAELHQARLQAAQLTLQLADASLA---LREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
590-900 |
3.09e-05 |
|
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: 48.58 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 590 EEQRGLQEAQlddtkvqEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGS-LASLEAEQA 668
Cdd:pfam17380 313 ERRRKLEEAE-------KARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISrMRELERLQM 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 669 SIRHLGDQMEASLLAVRKakeaMKAQMAEKEAILQSKEGECQQLREEVEqcqqlaEARHRELRALESQCQQQTQLIEVLT 748
Cdd:pfam17380 386 ERQQKNERVRQELEAARK----VKILEEERQRKIQQQKVEMEQIRAEQE------EARQREVRRLEEERAREMERVRLEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 749 AEKgQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQsqlsMAEAVLREHKTLVQ 828
Cdd:pfam17380 456 QER-QQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK----LLEKEMEERQKAIY 530
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925332 829 QLKEQNEAlnrahvqellqcseregalQEERadEAQQREEELRALQEELSQAkcSSEEAQLEHAELQEQLHR 900
Cdd:pfam17380 531 EEERRREA-------------------EEER--RKQQEMEERRRIQEQMRKA--TEERSRLEAMEREREMMR 579
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
246-1048 |
3.32e-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: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 246 EKQLRERMQQLDRENQElRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEvtQATQNTVKELQTCLQGLELG 325
Cdd:pfam01576 270 EAQISELQEDLESERAA-RNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKRE--QEVTELKKALEEETRSHEAQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 326 AAEKEEDYHTALRRLESMLQPLA---QELEATRDSLDKKNQHLasfpgwlamaQQKADTASDTKGRQEPIPSDAAQEMQE 402
Cdd:pfam01576 347 LQEMRQKHTQALEELTEQLEQAKrnkANLEKAKQALESENAEL----------QAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 403 LGEKLQALERERTKVEEVNRQQSAQLEQLVKELqlkEDARASLERLVKEMAPLQEELsgkgQEADQLwrrLQELLAHTSS 482
Cdd:pfam01576 417 LQARLSESERQRAELAEKLSKLQSELESVSSLL---NEAEGKNIKLSKDVSSLESQL----QDTQEL---LQEETRQKLN 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 483 WEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLA-------QVSQHVSDLEEQKKQLIQDKDHLSQQvgMLER 555
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSdmkkkleEDAGTLEALEEGKKRLQRELEALTQQ--LEEK 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 556 LAGPPGPELP---VAGEKNEALVPVNSSLQEAwGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELqnvvgRN 632
Cdd:pfam01576 565 AAAYDKLEKTknrLQQELDDLLVDLDHQRQLV-SNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKET-----RA 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 633 QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGecQQL 712
Cdd:pfam01576 639 LSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATED--AKL 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 713 REEVeqcqqlaearhrELRALESQCQQQTQLIEVLTAEKGQQGVgpptdNEARELAAQLALSQAQLEVHQGEVQRLQAQV 792
Cdd:pfam01576 717 RLEV------------NMQALKAQFERDLQARDEQGEEKRRQLV-----KQVRELEAELEDERKQRAQAVAAKKKLELDL 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 793 VDLQAKMRAALDDQDKVQSQLSMAEAVLREHKtlvqqlKEQNEAlnRAHVQELLQCSeregalqEERADEAQQREEELRA 872
Cdd:pfam01576 780 KELEAQIDAANKGREEAVKQLKKLQAQMKDLQ------RELEEA--RASRDEILAQS-------KESEKKLKNLEAELLQ 844
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 873 LQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAelgiqvcALTVEKERVEEALACAVQELQDAKEAAsrerEGLERQVA 952
Cdd:pfam01576 845 LQEDLAASERARRQAQQERDELADEIASGASGKS-------ALQDEKRRLEARIAQLEEELEEEQSNT----ELLNDRLR 913
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 953 GLQQEKESLQEKLKAAKAAAGSLPGLQAQLaqaEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEeckslrgQL 1032
Cdd:pfam01576 914 KSTLQVEQLTTELAAERSTSQKSESARQQL---ERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEE-------QL 983
|
810
....*....|....*.
gi 1894925332 1033 EEQGRQLQAAEEAVEK 1048
Cdd:pfam01576 984 EQESRERQAANKLVRR 999
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
613-748 |
3.33e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.88 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 613 ELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQ--------------ASIRHLGDQME 678
Cdd:pfam15905 160 ELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKieekseteklleyiTELSCVSEQVE 239
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1894925332 679 ASLLAVRKAKEAMKAQMAE----KEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLT 748
Cdd:pfam15905 240 KYKLDIAQLEELLKEKNDEieslKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELK 313
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
240-478 |
3.51e-05 |
|
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: 47.84 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 240 DQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQterergrtaaednvrltclvaELQKQWEVTQATQNTVKELQTCL 319
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK---------------------QLAALERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 320 QGLELGAAEKEEDYHTALRRLESMLQPLAQEL-EATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIpSDAAQ 398
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA-EELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 399 EMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLErlvKEMAPLQEELSGKGQEADQLWRRLQELLA 478
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEA 234
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
395-730 |
4.00e-05 |
|
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: 48.41 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 395 DAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLkedarasLERLVKEMAPLQEE-LSGKGQEADQLWRRL 473
Cdd:COG3096 833 DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQL-------LNKLLPQANLLADEtLADRLEELREELDAA 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 474 QELLAHTSSweeelaelrrekkqqqeekelLEQEVRSLTRQLQFLET---QLAQVSQHVSDLEEQKKQLIQDKDHLSQQV 550
Cdd:COG3096 906 QEAQAFIQQ---------------------HGKALAQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVV 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 551 GMLERLagppgpelpvAGEKNEALVPVNSSLQEAWgkpeeeqrglqEAQLDDTKVQEGSQEEELRQANRELEKELQnvvg 630
Cdd:COG3096 965 QRRPHF----------SYEDAVGLLGENSDLNEKL-----------RARLEQAEEARREAREQLRQAQAQYSQYNQ---- 1019
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 631 RNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHlgDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGEC- 709
Cdd:COG3096 1020 VLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRR--DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLr 1097
|
330 340 350
....*....|....*....|....*....|..
gi 1894925332 710 ------QQLREEVEQ-----CQQLAEARHREL 730
Cdd:COG3096 1098 kaerdyKQEREQVVQakagwCAVLRLARDNDV 1129
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
609-1165 |
4.06e-05 |
|
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: 48.09 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 609 SQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQ---MEASLLAVR 685
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQiseLKKQNNQLK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 686 KAKEAMKAQMAEKEAILQSKEGECQQLREE-------VEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKgQQGVGP 758
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEqnkikkqLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK-EQDWNK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 759 PTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLsmaeavlREHKTLVQQLKEQNEALN 838
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL-------EEKQNEIEKLKKENQSYK 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 839 RAHVQELLQCSEREGALQEERaDEAQQREEELRALQEELsqakcssEEAQLEHAELQEQLHRANTDTAELgiqvcaltve 918
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQE-KLNQQKDEQIKKLQQEK-------ELLEKEIERLKETIIKNNSEIKDL---------- 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 919 kERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQE---- 994
Cdd:TIGR04523 446 -TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE---LKKLNEEKKELEEKVKDLTKkiss 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 995 --AAHQELNTLKFQLSAEIMDYQSRLKNAGEECKS--LRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAEC 1070
Cdd:TIGR04523 522 lkEKIEKLESEKKEKESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1071 QAAMLRKDKEGAALREDLERTQKELEKATT---KIQEYYNKLCQEVTNRE---RNDQKMLADLDDLNRTKKYLEERLIEL 1144
Cdd:TIGR04523 602 IKEIEEKEKKISSLEKELEKAKKENEKLSSiikNIKSKKNKLKQEVKQIKetiKEIRNKWPEIIKKIKESKTKIDDIIEL 681
|
570 580
....*....|....*....|.
gi 1894925332 1145 LRDkdalWQKSDALEFQQKLS 1165
Cdd:TIGR04523 682 MKD----WLKELSLHYKKYIT 698
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
396-1042 |
4.12e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 48.26 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 396 AAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQE--------ELSGKGQEAD 467
Cdd:PRK10246 214 TPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKaqpqlaalSLAQPARQLR 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 468 QLWRRLQEllaHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEE------------- 534
Cdd:PRK10246 294 PHWERIQE---QSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRfrqwnnelagwra 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 535 QKKQLIQDKDHLSQQVGML-----ERLAGPPGPELPVAGEKNEALVPVN---------SSLQEAWGKPEEEQRGLQEA-- 598
Cdd:PRK10246 371 QFSQQTSDREQLRQWQQQLthaeqKLNALPAITLTLTADEVAAALAQHAeqrplrqrlVALHGQIVPQQKRLAQLQVAiq 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 599 QLDDTKVQEGSQEEELRQANRELEKELQNVVG------RNQLLEGKLQALQA----------------DYQALQQreSAI 656
Cdd:PRK10246 451 NVTQEQTQRNAALNEMRQRYKEKTQQLADVKTiceqeaRIKDLEAQRAQLQAgqpcplcgstshpaveAYQALEP--GVN 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 657 QGSLASLEAEQASIRHLGdqmeaslLAVRKAKEAMKAQmaekeaiLQSKEGECQQLREEVeqcQQLAEARHRELRALESQ 736
Cdd:PRK10246 529 QSRLDALEKEVKKLGEEG-------AALRGQLDALTKQ-------LQRDESEAQSLRQEE---QALTQQWQAVCASLNIT 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 737 CQQQTQLIEVLTAEKGQQgvgpptdNEARELAAQLALsQAQLEVHQGEVQRLQAQVVDLQAKMRAALD-------DQDKV 809
Cdd:PRK10246 592 LQPQDDIQPWLDAQEEHE-------RQLRLLSQRHEL-QGQIAAHNQQIIQYQQQIEQRQQQLLTALAgyaltlpQEDEE 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 810 QSQLSMAEAvlrEHKTLVQQLKEQNEALNR-AHVQELLQCSEREGALQEERADEAQqreEELRALQEElsqakCSSEEAQ 888
Cdd:PRK10246 664 ASWLATRQQ---EAQSWQQRQNELTALQNRiQQLTPLLETLPQSDDLPHSEETVAL---DNWRQVHEQ-----CLSLHSQ 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 889 LEHAELQEQLHRANTDTAElgiqvcaltvekERVEEALACAVQELQDAKEAASREREGLERqvagLQQEKESLQEKLKAA 968
Cdd:PRK10246 733 LQTLQQQDVLEAQRLQKAQ------------AQFDTALQASVFDDQQAFLAALLDEETLTQ----LEQLKQNLENQRQQA 796
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925332 969 KAaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGEECKSLRGQL--EEQGRQLQAA 1042
Cdd:PRK10246 797 QT-------LVTQTAQALAQHQQHRPDGLDLTVTVE-QIQQELAQLAQQLRENTTRQGEIRQQLkqDADNRQQQQA 864
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
611-991 |
4.49e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.13 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 611 EEELRQanrELeKELQNVVGRNQLleGKLQALQADYQALQQResaiQGSLASLEAEQASI-------RHLGDQMEASLLA 683
Cdd:PRK10929 25 EKQITQ---EL-EQAKAAKTPAQA--EIVEALQSALNWLEER----KGSLERAKQYQQVIdnfpklsAELRQQLNNERDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 684 VRKAKEAMKAQMAEKEaILQSKegecQQLREEVEQCQQLAEaRHRELRALESQC-QQQTQLIEVLT-AEKGQQGVGPPTD 761
Cdd:PRK10929 95 PRSVPPNMSTDALEQE-ILQVS----SQLLEKSRQAQQEQD-RAREISDSLSQLpQQQTEARRQLNeIERRLQTLGTPNT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 762 nearelaaqlALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEavlREHKTLVQQLKEQNEALNRAH 841
Cdd:PRK10929 169 ----------PLAQAQLTALQAESAALKALVDELELAQLSANNRQELARLRSELAK---KRSQQLDAYLQALRNQLNSQR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 842 VQELLQCSEREGALQEERADEAQQREEELRaLQEELSQAkcSSEEAQlEHAELQEQLHRANTDTaelgIQV-CALTVEKE 920
Cdd:PRK10929 236 QREAERALESTELLAEQSGDLPKSIVAQFK-INRELSQA--LNQQAQ-RMDLIASQQRQAASQT----LQVrQALNTLRE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 921 RVE---------EALACAVQELQDAKEAASREREGLERQVAGLQQEK--ESLQEKLKAAKAAAGSLPGLQAQLAQAEQRA 989
Cdd:PRK10929 308 QSQwlgvsnalgEALRAQVARLPEMPKPQQLDTEMAQLRVQRLRYEDllNKQPQLRQIRQADGQPLTAEQNRILDAQLRT 387
|
..
gi 1894925332 990 QS 991
Cdd:PRK10929 388 QR 389
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
512-846 |
4.80e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 512 TRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPGPELPVAG------EKNEALVPVNSS----- 580
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaereiaELEAELERLDASsddla 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 581 -LQEAWGKPEEEQRGLQEaQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLE-GKLQALQADYQAL--QQRESAI 656
Cdd:COG4913 689 aLEEQLEELEAELEELEE-ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERFAAAlgDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 657 QGSL-ASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEveqcqQLAEARHRELRALES 735
Cdd:COG4913 768 RENLeERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEED-----GLPEYEERFKELLNE 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 736 QCQQ-QTQLIEVLTAEKgqqgvgpptdNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAkMRAALDDQDKVQSQLS 814
Cdd:COG4913 843 NSIEfVADLLSKLRRAI----------REIKERIDPLNDSLKRIPFGPGRYLRLEARPRPDPE-VREFRQELRAVTSGAS 911
|
330 340 350
....*....|....*....|....*....|....*..
gi 1894925332 815 MAEAVLREH-----KTLVQQLKEQNEALNRAHVQELL 846
Cdd:COG4913 912 LFDEELSEArfaalKRLIERLRSEEEESDRRWRARVL 948
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
241-805 |
4.96e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 241 QLEVREKQLRERMQQLDRENQELRAAVSQQGE-QLQTERERGRTAAEDNVRL-----TCLVAELQKQWEVTQATQNTVKE 314
Cdd:TIGR00618 308 QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSiEEQRRLLQTLHSQEIHIRDahevaTSIREISCQQHTLTQHIHTLQQQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 315 LQTCLQGLELGAAEKEEdyhtaLRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPS 394
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDI-----LQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 395 DAAQEMQELGEKLQALER-----ERTKVEEVNRQQSAQLEQLVKELQLKEDARAS-----LERLVKEMAPLQEELSGKGQ 464
Cdd:TIGR00618 463 ESAQSLKEREQQLQTKEQihlqeTRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLET 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 465 EADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQH------VSDLEEQKKQ 538
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAedmlacEQHALLRKLQ 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 539 LIQDKDHLSQQVGMLER-----LAGPPGPELPVAGEKNEALVPVNSSLQEAWGkpeeEQRGLQEAQLDDTKVQEGSQEEE 613
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQelalkLTALHALQLTLTQERVREHALSIRVLPKELL----ASRQLALQKMQSEKEQLTYWKEM 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 614 LRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASirhlgdqmeasllaVRKAKEAMKA 693
Cdd:TIGR00618 699 LAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART--------------VLKARTEAHF 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 694 QMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQT---QLIEVLTAEKGQQGVgPPTDNEARELAAQ 770
Cdd:TIGR00618 765 NNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIpsdEDILNLQCETLVQEE-EQFLSRLEEKSAT 843
|
570 580 590
....*....|....*....|....*....|....*
gi 1894925332 771 LALSQAQLEvHQGEVQRLQAQVVDLQAKMRAALDD 805
Cdd:TIGR00618 844 LGEITHQLL-KYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
640-1096 |
6.70e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 47.55 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 640 QALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 719
Cdd:COG3899 770 RALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREA 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 720 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKM 799
Cdd:COG3899 850 LELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAA 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 800 RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQ 879
Cdd:COG3899 930 ALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAA 1009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 880 AkCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKE 959
Cdd:COG3899 1010 A-AAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAAL 1088
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 960 SLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQL 1039
Cdd:COG3899 1089 AAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAA 1168
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925332 1040 QAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELE 1096
Cdd:COG3899 1169 LALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLL 1225
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
819-1159 |
8.25e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 819 VLREHKTL--VQQLKEQNEALNRAHvQELLQCSEREGALQ--EERADEAQQREEELRALQEELSQAKcsSEEAQLEHAEL 894
Cdd:COG4913 217 MLEEPDTFeaADALVEHFDDLERAH-EALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALR--LWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 895 QEQLHRantdtaelgiqvcaLTVEKERVEEALAcavqELQDAKEAASREREGLERQVAGLQ-QEKESLQEKLKaakaaag 973
Cdd:COG4913 294 EAELEE--------------LRAELARLEAELE----RLEARLDALREELDELEAQIRGNGgDRLEQLEREIE------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 974 slpGLQAQLAQAEQRAQSLQEAahqeLNTLKFQLSAEImdyqsrlknagEECKSLRGQLEEQGRQLQAAEEAVEKLKAtq 1053
Cdd:COG4913 349 ---RLERELEERERRRARLEAL----LAALGLPLPASA-----------EEFAALRAEAAALLEALEEELEALEEALA-- 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1054 admgeklsctsnhlaecqaamlrkdkegaalreDLERTQKELEKATTKIQeyynklcQEVTNRERN----DQKMLADLDD 1129
Cdd:COG4913 409 ---------------------------------EAEAALRDLRRELRELE-------AEIASLERRksniPARLLALRDA 448
|
330 340 350
....*....|....*....|....*....|....*
gi 1894925332 1130 LNRTKKYLEERL---IELL--RDKDALWQksDALE 1159
Cdd:COG4913 449 LAEALGLDEAELpfvGELIevRPEEERWR--GAIE 481
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
698-965 |
8.43e-05 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 46.60 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 698 KEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVgpptdnEARELAAQLALSQAQ 777
Cdd:pfam15742 4 GEKLKYQQQEEVQQLRQNLQRLQILCTSAEKELRYERGKNLDLKQHNSLLQEENIKIKA------ELKQAQQKLLDSTKM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 778 LEVHQGEVQRLQAQVVDLQAKMraaLDDQDKVQSQLSMAEAVLREHKTLVQQLK---EQNEALNRAHVQELLQCSEREGA 854
Cdd:pfam15742 78 CSSLTAEWKHCQQKIRELELEV---LKQAQSIKSQNSLQEKLAQEKSRVADAEEkilELQQKLEHAHKVCLTDTCILEKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 855 LQEERADEAQQREEELRA-LQEELSQAKCSSEEAQlehaELQEQLhRANTDTAELGIQVCALTVEKERVEEALACAVQEL 933
Cdd:pfam15742 155 QLEERIKEASENEAKLKQqYQEEQQKRKLLDQNVN----ELQQQV-RSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENE 229
|
250 260 270
....*....|....*....|....*....|..
gi 1894925332 934 QDAKEAASREREGLERQVAGLQQEKESLQEKL 965
Cdd:pfam15742 230 KRKSDEHLKSNQELSEKLSSLQQEKEALQEEL 261
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
236-805 |
1.23e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 236 RLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERgrtaaednvrltclVAELQKQWEvtQATQNTVKEL 315
Cdd:COG4913 280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREE--------------LDELEAQIR--GNGGDRLEQL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 316 QTCLQGLELGAAEKE---EDYHTALRRLESMLQPLAQELEATRDSLDkknQHLASFPGWLAMAQQKADTASDTKgrqepi 392
Cdd:COG4913 344 EREIERLERELEERErrrARLEALLAALGLPLPASAEEFAALRAEAA---ALLEALEEELEALEEALAEAEAAL------ 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 393 pSDAAQEMQELGEKLQALERERTKVEEvnRQQSAqLEQLVKELQLKEDaraslerlvkEMAPLQEELSGKGQEADqlWRR 472
Cdd:COG4913 415 -RDLRRELRELEAEIASLERRKSNIPA--RLLAL-RDALAEALGLDEA----------ELPFVGELIEVRPEEER--WRG 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 473 LQELLAHTSSweeelaelrrekkqqqeekelleqevRSLtrqlqfL--ETQLAQVSQHVSDLeeqkkqliqdkdHLSQQV 550
Cdd:COG4913 479 AIERVLGGFA--------------------------LTL------LvpPEHYAAALRWVNRL------------HLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 551 gMLERLAGPPGPELPVAGEKNE--ALVPVNSSLQEAWGKPEEEQRGL-----QEAQLDDTK---VQEG--SQEEELRQAN 618
Cdd:COG4913 515 -VYERVRTGLPDPERPRLDPDSlaGKLDFKPHPFRAWLEAELGRRFDyvcvdSPEELRRHPraiTRAGqvKGNGTRHEKD 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 619 RELEKELQNVVGRN-----QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLgDQMEASLLAVRKAKEAMKA 693
Cdd:COG4913 594 DRRRIRSRYVLGFDnraklAALEAELAELEEELAEAEERLEALEAELDALQERREALQRL-AEYSWDEIDVASAEREIAE 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 694 QMAEKEAILQSKeGECQQLREEVEQCQQLAEARHRELRALESQC----QQQTQLIEVLTAEKGQQGVGPPTDNEARELAA 769
Cdd:COG4913 673 LEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIgrleKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
570 580 590
....*....|....*....|....*....|....*..
gi 1894925332 770 QLALSQAQLEVHQGEVQR-LQAQVVDLQAKMRAALDD 805
Cdd:COG4913 752 EERFAAALGDAVERELREnLEERIDALRARLNRAEEE 788
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
273-926 |
1.30e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.74 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 273 QLQTERERgrtAAEDNVRLTCLVAELQKQWEVTQATQNT----VKELQTCLQGLELGAAEKEED---------YHTALRR 339
Cdd:pfam10174 120 RLQSEHER---QAKELFLLRKTLEEMELRIETQKQTLGArdesIKKLLEMLQSKGLPKKSGEEDwertrriaeAEMQLGH 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 340 LESMLQPLAQELEATRDSLDKKNQhlasfpgwlamaqqkadtasdtkGRQEPIPSDAAQEMQELGE-KLQALERERTKVE 418
Cdd:pfam10174 197 LEVLLDQKEKENIHLREELHRRNQ-----------------------LQPDPAKTKALQTVIEMKDtKISSLERNIRDLE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 419 -EVNRQQSAQL---EQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRREK 494
Cdd:pfam10174 254 dEVQMLKTNGLlhtEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 495 KQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERlagppgpELPVAGEKNEAL 574
Cdd:pfam10174 334 TAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKER-------KINVLQKKIENL 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 575 VPVNSSLQEAWGKPEEEQRGLQ--------------EAQLDDTKVQEGSQEEELRQaNRELEKELQNVVGRNQLLEGKLQ 640
Cdd:pfam10174 407 QEQLRDKDKQLAGLKERVKSLQtdssntdtalttleEALSEKERIIERLKEQRERE-DRERLEELESLKKENKDLKEKVS 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 641 ALQADYQA-------LQQRESAIQGS-------LASLEAEQASIRHLGDQMEASLLAVRKAKEA--MKAQMAEKeaiLQS 704
Cdd:pfam10174 486 ALQPELTEkesslidLKEHASSLASSglkkdskLKSLEIAVEQKKEECSKLENQLKKAHNAEEAvrTNPEINDR---IRL 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 705 KEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTdnearelaaqlalSQAQLEVHQGE 784
Cdd:pfam10174 563 LEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNK-------------KVANIKHGQQE 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 785 VQRLQAQVVDLQakmRAALDDQDKVQSQLSMAEAVLREHKTLvQQLKEQNEALnrAHVQELLQcsEREGALQEERADEAQ 864
Cdd:pfam10174 630 MKKKGAQLLEEA---RRREDNLADNSQQLQLEELMGALEKTR-QELDATKARL--SSTQQSLA--EKDGHLTNLRAERRK 701
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925332 865 QREEELRALQEELsQAKCSSEEAQLEHAELQEQLHRANTDtaelgiQVCALTVEKERVEEAL 926
Cdd:pfam10174 702 QLEEILEMKQEAL-LAAISEKDANIALLELSSSKKKKTQE------EVMALKREKDRLVHQL 756
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
586-1154 |
1.59e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.35 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 586 GKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEG--KLQALQADYQALQQRESAIQGSLASL 663
Cdd:pfam10174 173 PKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDpaKTKALQTVIEMKDTKISSLERNIRDL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 664 EAEQASIRHLGD-----------QMEAsllaVRKAKEAMKAQMAEKEAILQSKEGE-----------------CQQ---- 711
Cdd:pfam10174 253 EDEVQMLKTNGLlhtedreeeikQMEV----YKSHSKFMKNKIDQLKQELSKKESEllalqtkletltnqnsdCKQhiev 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 712 LREEVEQCQQLAEARHRELRAL-------ESQCQQQTQLIEVLTAEKGQQGvgpptdNEARELAAQLALSQAQLEVHQGE 784
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEVDALrlrleekESFLNKKTKQLQDLTEEKSTLA------GEIRDLKDMLDVKERKINVLQKK 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 785 VQRLQAQVVD-------LQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELlqcseregalqE 857
Cdd:pfam10174 403 IENLQEQLRDkdkqlagLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEEL-----------E 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 858 ERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVcaltveKERVEEALACAVQeLQDAK 937
Cdd:pfam10174 472 SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAV------EQKKEECSKLENQ-LKKAH 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 938 EAASREREGLE--RQVAGLQQEKESLQEKlkaAKAAAGSLPGLQAQLAQAEQRA----------QSLQEAAHQELNTLKF 1005
Cdd:pfam10174 545 NAEEAVRTNPEinDRIRLLEQEVARYKEE---SGKAQAEVERLLGILREVENEKndkdkkiaelESLTLRQMKEQNKKVA 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1006 QLSAeiMDYQSRLKNAGEECKSLRGQLEE----QGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAEcqaamlrKDKEG 1081
Cdd:pfam10174 622 NIKH--GQQEMKKKGAQLLEEARRREDNLadnsQQLQLEELMGALEKTRQELDATKARLSSTQQSLAE-------KDGHL 692
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925332 1082 AALRedLERtQKELEKATTKIQEyynKLCQEVTNRERNdqkmLADLDDLNRTKKYLEERLIELLRDKDALWQK 1154
Cdd:pfam10174 693 TNLR--AER-RKQLEEILEMKQE---ALLAAISEKDAN----IALLELSSSKKKKTQEEVMALKREKDRLVHQ 755
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
376-822 |
1.64e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 376 QQKADTASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLV------ 449
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllply 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 450 KEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRRE----KKQQQEEKELLEQEVRSLTRQLQFLETQLAQV 525
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELqeelEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 526 SQHVSDLEEQKKQLIQDKDHLSQQ-------------------VGMLERLAGPPGPELPVAGEKNEALVPVNS--SLQEA 584
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENEleaaaleerlkearlllliAAALLALLGLGGSLLSLILTIAGVLFLVLGllALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 585 WGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQgsLASLE 664
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 665 AEQasirhlgdqmeASLLAvrkakeamKAQMAEKEailqskegecqQLREEVEQCQQLAEARhRELRALESQCQQQTQLI 744
Cdd:COG4717 370 QEI-----------AALLA--------EAGVEDEE-----------ELRAALEQAEEYQELK-EELEELEEQLEELLGEL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 745 EVLTAekgqqgvgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQ--DKVQSQLSMAEAVLRE 822
Cdd:COG4717 419 EELLE-----------ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRE 487
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
856-1056 |
1.87e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 856 QEERADEAQQReeeLRALQEELSQAKcsseeAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALAcavqELQD 935
Cdd:COG3206 166 LELRREEARKA---LEFLEEQLPELR-----KELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLA----EARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 936 AKEAASREREGLERQVAGLQQEKESLQEklkaakaaAGSLPGLQAQLAQAEQRAQSLQE----------AAHQELNTLKF 1005
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQ--------SPVIQQLRAQLAELEAELAELSArytpnhpdviALRAQIAALRA 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1894925332 1006 QLSAEIMDYQSRLKNageECKSLRGQLEEQGRQLQAAEEAVEKLKATQADM 1056
Cdd:COG3206 306 QLQQEAQRILASLEA---ELEALQAREASLQAQLAQLEARLAELPELEAEL 353
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
596-878 |
2.10e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 596 QEAQLDDTKVQEGSQEEELRQANRELE--KELQNVVGRNQL-------LEGKLQALQADYQALQQRESAIQGSLASLEAe 666
Cdd:PRK11281 78 QKEETEQLKQQLAQAPAKLRQAQAELEalKDDNDEETRETLstlslrqLESRLAQTLDQLQNAQNDLAEYNSQLVSLQT- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 667 qASIRhlgdqmeasllaVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVeqcQQLAEArhrELRALESQCQQQTQLIEV 746
Cdd:PRK11281 157 -QPER------------AQAALYANSQRLQQIRNLLKGGKVGGKALRPSQ---RVLLQA---EQALLNAQNDLQRKSLEG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 747 LTaekgqqgvgpptdnearelaaQL-ALSQAQLEVHQGEVQRLQAQVVDLQakmrAALDDQDKVQSQLSMAEAVLREHKT 825
Cdd:PRK11281 218 NT---------------------QLqDLLQKQRDYLTARIQRLEHQLQLLQ----EAINSKRLTLSEKTVQEAQSQDEAA 272
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925332 826 LVQQ--LKEQNEALNRAHVQELLQCSEREGAL--QEERA----DEAQQREeelRALQEELS 878
Cdd:PRK11281 273 RIQAnpLVAQELEINLQLSQRLLKATEKLNTLtqQNLRVknwlDRLTQSE---RNIKEQIS 330
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
432-1149 |
2.26e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 432 VKELQLKEDARASLERLVKEMApLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSL 511
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEA-LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 512 TRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPGP----ELPVAGEKNEALVPVNSSLQEAWGK 587
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKlqeeELKLLAKEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 588 PEEEQRGLQE--AQLDDTKVQEGSQEEELRQANRELEK---ELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLAS 662
Cdd:pfam02463 312 DEEKLKESEKekKKAEKELKKEKEEIEELEKELKELEIkreAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 663 LEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEarhRELRALESQCQQQTQ 742
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEEL---EKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 743 LIEVLTAEKgqQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQ----------------AKMRAALDDQ 806
Cdd:pfam02463 469 KSEDLLKET--QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggriisahgrlgdlgvAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 807 DKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEE 886
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 887 AQLEHAELQEQLHRANTDTAELGIQVcalTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLK 966
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGV---SLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 967 AAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNageecKSLRGQLEEQGRQLQAAEEAV 1046
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL-----KKEEKEEEKSELSLKEKELAE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1047 EKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLAD 1126
Cdd:pfam02463 779 EREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELER 858
|
730 740
....*....|....*....|...
gi 1894925332 1127 LDDLNRTKKYLEERLIELLRDKD 1149
Cdd:pfam02463 859 LEEEITKEELLQELLLKEEELEE 881
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
795-965 |
2.42e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.19 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 795 LQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcseregalqeeradeaqqrEEELRALQ 874
Cdd:pfam15905 168 LEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE-------------------TEKLLEYI 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 875 EELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERqvaGL 954
Cdd:pfam15905 229 TELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQ---TL 305
|
170
....*....|.
gi 1894925332 955 QQEKESLQEKL 965
Cdd:pfam15905 306 NAELEELKEKL 316
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
640-904 |
2.81e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 640 QALQADYQALQQRESaiqgslasLEAEQASIRHLGDQMEASLlavrKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 719
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 720 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptdNEARELAAQLALSQAQLEVHQGE----VQRLQ---AQV 792
Cdd:PRK11281 107 KDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQ-------NDLAEYNSQLVSLQTQPERAQAAlyanSQRLQqirNLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 793 VDLQAKMRAALDDQ-DKVQSQLSMAEAVLRehktLVQQLKEQNEALnrahvQELLQcSEREgalqeERADEAQQREEELR 871
Cdd:PRK11281 180 KGGKVGGKALRPSQrVLLQAEQALLNAQND----LQRKSLEGNTQL-----QDLLQ-KQRD-----YLTARIQRLEHQLQ 244
|
250 260 270
....*....|....*....|....*....|...
gi 1894925332 872 ALQEELSQAKCSSEEAQLEHAELQEQLHRANTD 904
Cdd:PRK11281 245 LLQEAINSKRLTLSEKTVQEAQSQDEAARIQAN 277
|
|
| FYVE_RUFY3 |
cd15744 |
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ... |
1179-1227 |
3.04e-04 |
|
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).
Pssm-ID: 277283 [Multi-domain] Cd Length: 52 Bit Score: 40.09 E-value: 3.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1894925332 1179 CLDCKREFSWMVR-RHHCRICGRIFCYYCCNNYV-LSKHGGKKERCCRACF 1227
Cdd:cd15744 2 CSLCQEDFASLALpKHNCYNCGGTFCDACSSNELpLPSSIYEPARVCDVCY 52
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
250-451 |
3.30e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 250 RERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEdnvRLTCLVAELQKQWEV--TQATQNTVKELQTCLQGLELGAA 327
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQE---RREALQRLAEYSWDEidVASAEREIAELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 328 EkeedyhtaLRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDtkgRQEPIPSDAAQEMQELGEKL 407
Cdd:COG4913 686 D--------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD---RLEAAEDLARLELRALLEER 754
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1894925332 408 QALERERTKVEEVNRQQSAQLEQLVKELqlkEDARASLERLVKE 451
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARL---NRAEEELERAMRA 795
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
867-1118 |
3.47e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 867 EEELRALQEELSQAKCSSEEAQLEHAELQEQLhrantdtaelgiqvcALTVEKERVEEALACAVQELQDAKEAASREREG 946
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTL---------------ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 947 LERQVAGLQQEKESLQEKLkaakaaagSLPGLQAQLAQAEQRAQSLQEAahqeLNTLKFQLSAeimdYQSRLKNAGEECK 1026
Cdd:PRK11281 103 LEALKDDNDEETRETLSTL--------SLRQLESRLAQTLDQLQNAQND----LAEYNSQLVS----LQTQPERAQAALY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1027 SLRGQLEEQGRQLQAAEEAVEKLKATQADMGEklscTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYY 1106
Cdd:PRK11281 167 ANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQ----AEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQ 242
|
250
....*....|..
gi 1894925332 1107 NKLCQEVTNRER 1118
Cdd:PRK11281 243 LQLLQEAINSKR 254
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
942-1125 |
4.14e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 942 REREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEA-AHQELNTLKFQLSAEIMDYQSRLKN 1020
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1021 AGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKlscTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT 1100
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180
....*....|....*....|....*
gi 1894925332 1101 KIQEYYNKLCQEVTNRERNDQKMLA 1125
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLL 252
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
249-958 |
4.35e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.74 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 249 LRERMQQLDRENQELRaavsQQGEQLQTERErgrTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCLQGLELGAAE 328
Cdd:pfam07111 61 LSQQAELISRQLQELR----RLEEEVRLLRE---TSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKN 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 329 KEEDYHTALRRLESMLQplaqeleatrdsldkknQHLASfpgwLAMAQQKA--DTASDTKGRQEPIPSdaaQEMQELGEK 406
Cdd:pfam07111 134 LEEGSQRELEEIQRLHQ-----------------EQLSS----LTQAHEEAlsSLTSKAEGLEKSLNS---LETKRAGEA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 407 LQALERERtKVEEVNRQQSAQLEQLVKELQLKEdaraSLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSweee 486
Cdd:pfam07111 190 KQLAEAQK-EAELLRKQLSKTQEELEAQVTLVE----SLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRAD---- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 487 laelrrekkqQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQ-----------------------KKQLIQDK 543
Cdd:pfam07111 261 ----------LQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEfpkkcrsllnrwrekvfalmvqlKAQDLEHR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 544 DHLSQQVGMLERLAgppgpELPVAGEKNEALvpVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANreLEK 623
Cdd:pfam07111 331 DSVKQLRGQVAELQ-----EQVTSQSQEQAI--LQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTAS--AEE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 624 ELQNVVGrnqllegklqalqadyqALQQRESAIQGSLASLEAEQASIRHLGDQMEaslLAVRKAkEAMKAQMAEKEAILQ 703
Cdd:pfam07111 402 QLKFVVN-----------------AMSSTQIWLETTMTRVEQAVARIPSLSNRLS---YAVRKV-HTIKGLMARKVALAQ 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 704 SKEGEC------QQLREEVE-QCQQLAEARHRelraLESQCQQQTQLIevltaekgQQGVGpptdnEARElaaqlalsqa 776
Cdd:pfam07111 461 LRQESCpppppaPPVDADLSlELEQLREERNR----LDAELQLSAHLI--------QQEVG-----RARE---------- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 777 qlevhQGEVQRLQAQVVDLQAkmraaldDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAhvQELLQCSEREGALQ 856
Cdd:pfam07111 514 -----QGEAERQQLSEVAQQL-------EQELQRAQESLASVGQQLEVARQGQQESTEEAASLR--QELTQQQEIYGQAL 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 857 EERADEAQQReeelraLQEELSQAKCSSEEAQLEHAE----LQEQLHRAntdtaelgiqvcalTVEKERVEEalacaVQE 932
Cdd:pfam07111 580 QEKVAEVETR------LREQLSDTKRRLNEARREQAKavvsLRQIQHRA--------------TQEKERNQE-----LRR 634
|
730 740
....*....|....*....|....*.
gi 1894925332 933 LQDakEAASREREGLERQVAGLQQEK 958
Cdd:pfam07111 635 LQD--EARKEEGQRLARRVQELERDK 658
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
593-814 |
4.36e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 593 RGLQEaQLDDTKVQEGSQEEELRQANReLEKELQNVVGRNqllegkLQALQADYQALQQRESAIQGSLASLEAEQASIRH 672
Cdd:PHA02562 177 RELNQ-QIQTLDMKIDHIQQQIKTYNK-NIEEQRKKNGEN------IARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 673 LGDQMEASLLAVRKAKEAMKAQMA--EKEAILQSKEGEC----QQLREEVEQC----QQLAEARHRELRALESQCQQQTQ 742
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEqfQKVIKMYEKGGVCptctQQISEGPDRItkikDKLKELQHSLEKLDTAIDELEEI 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925332 743 LIEVLTAEKGQQGVgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLS 814
Cdd:PHA02562 329 MDEFNEQSKKLLEL----KNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKS 396
|
|
| FYVE_FGD3 |
cd15740 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ... |
1173-1227 |
4.37e-04 |
|
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar proteins; FGD3, also termed zinc finger FYVE domain-containing protein 5, is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) that undergoes the ubiquitin ligase SCFFWD1/beta-TrCP-mediated proteasomal degradation. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Due to this difference, FGD3 may play different roles from that of FGD1 to regulate cell morphology or motility. The FYVE domain of FGD3 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.
Pssm-ID: 277279 [Multi-domain] Cd Length: 54 Bit Score: 39.60 E-value: 4.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925332 1173 DTEANHCLDCKREFSWMV-RRHHCRICGRIFCYYCCNnyvLSKHGGKKERCCRACF 1227
Cdd:cd15740 2 EKEKQTCKGCNESFNSITkRRHHCKQCGAVICGKCSE---FKDLASRHNRVCRDCF 54
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
765-1005 |
4.86e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.68 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 765 RELAAQLalsqaqLEVH-QGEVQRLqaqvvdLQAKM-RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQnealnrahv 842
Cdd:COG0497 119 RELGELL------VDIHgQHEHQSL------LDPDAqRELLDAFAGLEELLEEYREAYRAWRALKKELEEL--------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 843 qellqcseregalqEERADEAQQREEELRALQEELSQAKCSS-EEAQLE-------HAE-LQEQLHRA------NTDTAE 907
Cdd:COG0497 178 --------------RADEAERARELDLLRFQLEELEAAALQPgEEEELEeerrrlsNAEkLREALQEAlealsgGEGGAL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 908 LGIQVCALTVEK------------ERVEEALAcavqELQDAKEAASREREGLE------------------------RQV 951
Cdd:COG0497 244 DLLGQALRALERlaeydpslaelaERLESALI----ELEEAASELRRYLDSLEfdperleeveerlallrrlarkygVTV 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1894925332 952 AGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQR---------------AQSLQEAAHQELNTLKF 1005
Cdd:COG0497 320 EELLAYAEELRAELAELENSDERLEELEAELAEAEAElleaaeklsaarkkaAKKLEKAVTAELADLGM 388
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
789-951 |
5.05e-04 |
|
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: 43.37 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 789 QAQVVDLQAkmraaLDDQ-DKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERA----DEA 863
Cdd:COG1579 6 LRALLDLQE-----LDSElDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikkYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 864 QQRE----EELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEA 939
Cdd:COG1579 81 QLGNvrnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
170
....*....|..
gi 1894925332 940 ASREREGLERQV 951
Cdd:COG1579 161 LEAEREELAAKI 172
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
829-1169 |
6.88e-04 |
|
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: 44.34 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 829 QLKEQNEALNrahvqELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQlhrantdtAEL 908
Cdd:pfam17380 263 QTMTENEFLN-----QLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQ--------AEM 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 909 GIQVcALTVEKERVeealacavqelqdakeAASREREgLER-QVAGLQQEKESL-QEKLKAAKAAAGSLPGLQAQLAQAE 986
Cdd:pfam17380 330 DRQA-AIYAEQERM----------------AMERERE-LERiRQEERKRELERIrQEEIAMEISRMRELERLQMERQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 987 QRAQSLQEAAHqelntlKFQLSAEimDYQSRLKNAGEECKSLRGQLEE-QGRQLQAAEEA----VEKLKATQADMGEKLS 1061
Cdd:pfam17380 392 ERVRQELEAAR------KVKILEE--ERQRKIQQQKVEMEQIRAEQEEaRQREVRRLEEErareMERVRLEEQERQQQVE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1062 CTSNHLAECQAAMLRKDKEgaalredlERTQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEE-- 1139
Cdd:pfam17380 464 RLRQQEEERKRKKLELEKE--------KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEErr 535
|
330 340 350
....*....|....*....|....*....|
gi 1894925332 1140 RLIELLRDKDALWQKSDALEFQQKLSAEER 1169
Cdd:pfam17380 536 REAEEERRKQQEMEERRRIQEQMRKATEER 565
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
933-1131 |
7.05e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 933 LQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAG--SLPG------------------LQAQLAQAEQRAQSL 992
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEeaklllqqlselesqlaeARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 993 QEAAHQELNTLKFQL-SAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLsctsnhLAECQ 1071
Cdd:COG3206 246 RAQLGSGPDALPELLqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI------LASLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1072 AAMLRKDKEGAALREDLERTQKELEKATTKIQEyYNKLCQEVTNRERNDQKMLADLDDLN 1131
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVARELYESLLQRLEEAR 378
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
979-1112 |
8.93e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 979 QAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGE-ECKSLRGQLEEQGRQLQAAEEAVEKLKatqadmg 1057
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEkELRERRNELQKLEKRLLQKEENLDRKL------- 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1894925332 1058 EKLSctsnhlaecqaamlRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQE 1112
Cdd:PRK12704 103 ELLE--------------KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
766-936 |
9.90e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.13 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 766 ELAAQLALSQAQLEVhQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLK--------EQNEAL 837
Cdd:cd22656 98 ELIDDLADATDDEEL-EEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEkalkdlltDEGGAI 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 838 NRAHVQELLQcseregALQEERADEAQQREEELRALQEELsqakcSSEEAQLEHAE-LQEQLHRANTDTAELgiqvcalt 916
Cdd:cd22656 177 ARKEIKDLQK------ELEKLNEEYAAKLKAKIDELKALI-----ADDEAKLAAALrLIADLTAADTDLDNL-------- 237
|
170 180
....*....|....*....|
gi 1894925332 917 veKERVEEALAcAVQELQDA 936
Cdd:cd22656 238 --LALIGPAIP-ALEKLQGA 254
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
649-1176 |
1.04e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 649 LQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKE--AMKAQMAEK-------EAILQSKEGECQQLREEV--- 716
Cdd:pfam10174 139 LEEMELRIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEdwERTRRIAEAemqlghlEVLLDQKEKENIHLREELhrr 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 717 ----------EQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkgqqGVGPPTDNEARELAAQLALSQA-----QLEVH 781
Cdd:pfam10174 219 nqlqpdpaktKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTN----GLLHTEDREEEIKQMEVYKSHSkfmknKIDQL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 782 QGEVQRLQAQVVDLQAKmraaLDDQDKVQSQLSMAEAVLREHKTlvqqLKEQNEALNRAHVQELLQCSEREGALQEERAD 861
Cdd:pfam10174 295 KQELSKKESELLALQTK----LETLTNQNSDCKQHIEVLKESLT----AKEQRAAILQTEVDALRLRLEEKESFLNKKTK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 862 EAQQREEELRALQEELS----------------QAKCSSEEAQLEH-----AELQE-----QLHRANTDTAeLGIQVCAL 915
Cdd:pfam10174 367 QLQDLTEEKSTLAGEIRdlkdmldvkerkinvlQKKIENLQEQLRDkdkqlAGLKErvkslQTDSSNTDTA-LTTLEEAL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 916 TvEKERVEEALacavqelqdaKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEA 995
Cdd:pfam10174 446 S-EKERIIERL----------KEQREREDRERLEELESLKKENKDLKEKVSA----------LQPELTEKESSLIDLKEH 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 996 AhQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQL---EEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQA 1072
Cdd:pfam10174 505 A-SSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkaHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVER 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1073 AM--LR--------KDKEGAALREDLERTQKELEKATTKIqeyynKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLI 1142
Cdd:pfam10174 584 LLgiLRevenekndKDKKIAELESLTLRQMKEQNKKVANI-----KHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLE 658
|
570 580 590
....*....|....*....|....*....|....
gi 1894925332 1143 ELLRDKDALWQKSDALefQQKLSAEERWLGDTEA 1176
Cdd:pfam10174 659 ELMGALEKTRQELDAT--KARLSSTQQSLAEKDG 690
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
588-745 |
1.13e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 588 PEEEQRGLQEAQLDDTKVQEgsqeeeLRQANRELEKELQNvvgrnqlLEGKLQALQADYQALQQRESAIQGSLASLEAEQ 667
Cdd:COG1579 2 MPEDLRALLDLQELDSELDR------LEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 668 ASIRHLGDQMEASLLAVRKAKE---------AMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQ 738
Cdd:COG1579 69 EEVEARIKKYEEQLGNVRNNKEyealqkeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
....*..
gi 1894925332 739 QQTQLIE 745
Cdd:COG1579 149 EELAELE 155
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
510-670 |
1.26e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 510 SLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMlerlagppgpelpvaGEKNEALVPVNSSLQEAwgkpe 589
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS---------------GPDALPELLQSPVIQQL----- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 590 EEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVvgrNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQAS 669
Cdd:COG3206 269 RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL---QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345
|
.
gi 1894925332 670 I 670
Cdd:COG3206 346 L 346
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
770-996 |
1.36e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 770 QLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlrEHKTLVQQLKEQNEALNRAhvQELLqcs 849
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA---EIDKLQAEIAEAEAEIEER--REEL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 850 eregalqEERADEAQQREEELRALQEELSQakcSSEEAQLEHAELQEQLHRANTDTAElgiQVCALTVEKERVEEALACA 929
Cdd:COG3883 89 -------GERARALYRSGGSVSYLDVLLGS---ESFSDFLDRLSALSKIADADADLLE---ELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925332 930 VQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAA 996
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
700-1049 |
1.62e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.25 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 700 AILQSKEGECQQLREEVE------QCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQ---GVGPPTDNEARELAAQ 770
Cdd:PRK10246 160 AFLNAKPKERAELLEELTgteiygQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSltaSLQVLTDEEKQLLTAQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 771 LALSQA-QLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAE--AVLR-------EHKTLVQQLKEQNEALN-R 839
Cdd:PRK10246 240 QQQQQSlNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQpaRQLRphweriqEQSAALAHTRQQIEEVNtR 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 840 AHVQELLQCSEREGALQEERADEAQQRE--------EELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAEL-GI 910
Cdd:PRK10246 320 LQSTMALRARIRHHAAKQSAELQAQQQSlntwlaehDRFRQWNNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLnAL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 911 QVCALTVEKERVEEALAcavqelQDAKEAASRER-EGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQ----- 984
Cdd:PRK10246 400 PAITLTLTADEVAAALA------QHAEQRPLRQRlVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQrykek 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 985 ----AEQRAQSLQEAAHQELNTLKFQLSA---------------------EIMDYQSRL-------KNAGEECKSLRGQL 1032
Cdd:PRK10246 474 tqqlADVKTICEQEARIKDLEAQRAQLQAgqpcplcgstshpaveayqalEPGVNQSRLdalekevKKLGEEGAALRGQL 553
|
410
....*....|....*..
gi 1894925332 1033 EEQGRQLQAAEEAVEKL 1049
Cdd:PRK10246 554 DALTKQLQRDESEAQSL 570
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
233-467 |
1.66e-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: 42.44 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 233 DEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQAT-QNT 311
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 312 VKELQTCLQGLELGAAEKEEDYHTALRRLEsMLQPLAQELEATRDSLDKKNQHLasfpgwlamAQQKADTASDTKgrqep 391
Cdd:COG4942 110 LRALYRLGRQPPLALLLSPEDFLDAVRRLQ-YLKYLAPARREQAEELRADLAEL---------AALRAELEAERA----- 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925332 392 ipsDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEAD 467
Cdd:COG4942 175 ---ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
738-1038 |
1.74e-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: 42.80 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 738 QQQTQLIEVLTAEKGQQgvgpPTDNEARELAAQLALSQAQlEVHQGEVQRlQAQVVDLQAKM---------RAALDDQDK 808
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQ----EKEEKAREVERRRKLEEAE-KARQAEMDR-QAAIYAEQERMamerereleRIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 809 V-----QSQLSMAEAVLREHKTLVQQLKEQNE----ALNRAHVQELLQcSEREGALQEE-------RADEAQQREEELRA 872
Cdd:pfam17380 361 ElerirQEEIAMEISRMRELERLQMERQQKNErvrqELEAARKVKILE-EERQRKIQQQkvemeqiRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 873 LQEELSQakcSSEEAQLEHAELQEQLHRANTDTAELGIQvcALTVEKERVEEALACAVQELQDAKEAASREREGLErqva 952
Cdd:pfam17380 440 LEEERAR---EMERVRLEEQERQQQVERLRQQEEERKRK--KLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE---- 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 953 glQQEKESLQEKlkaakaaagSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIM---DYQSRLKNAGEECKSLR 1029
Cdd:pfam17380 511 --EERKRKLLEK---------EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRkatEERSRLEAMEREREMMR 579
|
....*....
gi 1894925332 1030 GQLEEQGRQ 1038
Cdd:pfam17380 580 QIVESEKAR 588
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
701-908 |
1.80e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.05 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 701 ILQSKEGECQQLRE---------------EVEQCQQLAEARHRELRALESQCQQ-QTQLIEVltaEKGQQgvgpptdNEA 764
Cdd:pfam09787 19 ILQSKEKLIASLKEgsgvegldsstaltlELEELRQERDLLREEIQKLRGQIQQlRTELQEL---EAQQQ-------EEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 765 RELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLsmaEAVLREHKTLVQQLKEQ--NEALNRAHV 842
Cdd:pfam09787 89 ESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQltSKSQSSSSQ 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925332 843 QELlqcseregalqeeradeaqqrEEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAEL 908
Cdd:pfam09787 166 SEL---------------------ENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKEL 210
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
588-1010 |
1.93e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 588 PEEEQRGLQEAQLDDTKVQEGSQEEELRQAN-----RELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLAS 662
Cdd:COG5278 103 PEQQARLDELEALIDQWLAELEQVIALRRAGgleaaLALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 663 LEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQ 742
Cdd:COG5278 183 AALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAAL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 743 LIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLRE 822
Cdd:COG5278 263 LAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAA 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 823 HKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRAN 902
Cdd:COG5278 343 ALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEAL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 903 TDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQL 982
Cdd:COG5278 423 ELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLA 502
|
410 420
....*....|....*....|....*...
gi 1894925332 983 AQAEQRAQSLQEAAHQELNTLKFQLSAE 1010
Cdd:COG5278 503 LALAALLLAAAEAALAAALAAALASAEL 530
|
|
| FYVE_CARP |
cd15750 |
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ... |
1178-1226 |
2.04e-03 |
|
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 are a novel group of caspase regulators by the presence of a FYVE-type zinc finger domain. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains.
Pssm-ID: 277289 [Multi-domain] Cd Length: 47 Bit Score: 37.34 E-value: 2.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1894925332 1178 HCLDCKREFSWMVRRHHCRICGRIFCYYCcnnyvLSKHGGKKeRCCRAC 1226
Cdd:cd15750 2 PCESCGAKFSVFKRKRTCADCKRYFCSNC-----LSKEERGR-RRCRRC 44
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
919-1060 |
2.13e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 919 KERVEEALACAVQELQDAKEAASREREGLERQVAGLQQE---KESLQEKLKaakaaaGSLPGLQAQLAQAEQRAQSLQea 995
Cdd:PRK09039 51 KDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASlsaAEAERSRLQ------ALLAELAGAGAAAEGRAGELA-- 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925332 996 ahQELNTLKfQLSAEIMdyqSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKL 1060
Cdd:PRK09039 123 --QELDSEK-QVSARAL---AQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
227-752 |
2.28e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 227 EALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRA-AVSQQGEQLQTERERGRTAA--EDNVRLTCLVAELQKQWE 303
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLEGSKRKleEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 304 VTQATQNTVKELQ-TCLQGLELGaaEKEEDYHTALRRLESMLQPLAQELEATRDSLDKknqhlasfpgwlamAQQKADTA 382
Cdd:PRK03918 277 ELEEKVKELKELKeKAEEYIKLS--EFYEEYLDELREIEKRLSRLEEEINGIEERIKE--------------LEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 383 SDTKGRQEPIpsdaAQEMQELGEKLQALERERTKVEEVNRQQSA----QLEQLVKELQLKEDARASLERLVKEmapLQEE 458
Cdd:PRK03918 341 EELKKKLKEL----EKRLEELEERHELYEEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEISK---ITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 459 LSGKGQEADQLWRRLQELlahtssweeELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQ 538
Cdd:PRK03918 414 IGELKKEIKELKKAIEEL---------KKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 539 ----------LIQDKDHLSQQVGMLERLAGPPGPELPVAGEKNEalvpvnsSLQEAWGKPEEEQRGLQEaqlDDTKVQE- 607
Cdd:PRK03918 485 lekvlkkeseLIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE-------KLKEKLIKLKGEIKSLKK---ELEKLEEl 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 608 GSQEEELRQANRELEKELQNVVGR--------NQLLEGKLQALQADYQ---ALQQRESAIQGSLASLEAEQASIrhlgDQ 676
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKEleelgfesVEELEERLKELEPFYNeylELKDAEKELEREEKELKKLEEEL----DK 630
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925332 677 MEASLLAVRKAKEAMKAQMAEKEAILQSKEGEcqQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKG 752
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSEEEYE--ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
799-1118 |
2.34e-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: 42.47 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 799 MRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREgALQEERADEAQQREEELRALQEELS 878
Cdd:pfam01576 7 MQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAE-EMRARLAARKQELEEILHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 879 QAKCSSEEAQLEHAELQEQL-----HRANTDTAELGIQVCALTVE---KERVEEALAcavqeLQDAKEAASREREGLERQ 950
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIqdleeQLDEEEAARQKLQLEKVTTEakiKKLEEDILL-----LEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 951 VAGLQQEKESLQEKLKAAKAAAGSLpglQAQLAQAEQRAQSlQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRG 1030
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKH---EAMISDLEERLKK-EEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1031 QLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQ-------AAMLRKDKEGAALREDLERTQKELEK---ATT 1100
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQedleserAARNKAEKQRRDLGEELEALKTELEDtldTTA 316
|
330
....*....|....*...
gi 1894925332 1101 KIQEYYNKLCQEVTNRER 1118
Cdd:pfam01576 317 AQQELRSKREQEVTELKK 334
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
959-1169 |
2.56e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 959 ESLQEKLKAAKAAAGSLPGL---QAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRgqleeq 1035
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELnlkELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE------ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1036 grQLQAAEEAVEKLKATQADMgeklsctsNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVtn 1115
Cdd:COG4717 123 --KLLQLLPLYQELEALEAEL--------AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT-- 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1894925332 1116 rERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEER 1169
Cdd:COG4717 191 -EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
930-1104 |
2.92e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 930 VQELQDAKEAASREREGLERQVAGLQQEKEslqeklkaakaaagslpGLQAQLAQAEQRAQSLqEAAHQELNTLKFQLSA 1009
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELA-----------------ALEARLEAAKTELEDL-EKEIKRLELEIEEVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1010 EIMDYQSRLKNAG--EECKSLRGQLEEQGRQLQAAE-------EAVEKLKATQADMGEKLSCTSNHLAECQAamlRKDKE 1080
Cdd:COG1579 74 RIKKYEEQLGNVRnnKEYEALQKEIESLKRRISDLEdeilelmERIEELEEELAELEAELAELEAELEEKKA---ELDEE 150
|
170 180
....*....|....*....|....
gi 1894925332 1081 GAALREDLERTQKELEKATTKIQE 1104
Cdd:COG1579 151 LAELEAELEELEAEREELAAKIPP 174
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
827-1169 |
3.00e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 827 VQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEElsqaKCSSEEAQLEHAELQEQLHRANTDTA 906
Cdd:PTZ00121 1199 ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEE----RNNEEIRKFEEARMAHFARRQAAIKA 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 907 ELGIQVCAL--TVEKERVEEAL-ACAVQELQDAKEAA--SREREGLERQVAGLQQEKESLQEKLKAAKAAAgslpglQAQ 981
Cdd:PTZ00121 1275 EEARKADELkkAEEKKKADEAKkAEEKKKADEAKKKAeeAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA------EAA 1348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 982 LAQAEQRAQSLQEAAHQ----ELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKL-----KAT 1052
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKaeaaEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdeakkKAE 1428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1053 QADMGEKLSCTSNHLAecQAAMLRKDKEGAALREDLERTQKELEKA-TTKIQEYYNKLCQEVTNRERNDQKMLADLDDLN 1131
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAK--KADEAKKKAEEAKKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506
|
330 340 350
....*....|....*....|....*....|....*....
gi 1894925332 1132 RTKKYLEE-RLIELLRDKDALWQKSDALEFQQKLSAEER 1169
Cdd:PTZ00121 1507 EAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
516-839 |
3.63e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 516 QFLET---QLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPGPELPVAGEK--------------------NE 572
Cdd:PRK11281 63 QDLEQtlaLLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTlslrqlesrlaqtldqlqnaQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 573 ALVPVNSSLQEAWGKPEEEQRGLQEAQ---------LDDTKVQEGSQEEELRQanrELEKELQNVVGRN----QLLEG-- 637
Cdd:PRK11281 143 DLAEYNSQLVSLQTQPERAQAALYANSqrlqqirnlLKGGKVGGKALRPSQRV---LLQAEQALLNAQNdlqrKSLEGnt 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 638 KLQAL---QADYQALQQresaiqgslASLEAEQASIRHLGDQ--MEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQL 712
Cdd:PRK11281 220 QLQDLlqkQRDYLTARI---------QRLEHQLQLLQEAINSkrLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 713 REE-VEQCQQLAEARHRELRA---LESQCQQQTQLIEVLTAEKG---------QQGVGPPTDNEARELAAQLA-LSQAQL 778
Cdd:PRK11281 291 SQRlLKATEKLNTLTQQNLRVknwLDRLTQSERNIKEQISVLKGslllsrilyQQQQALPSADLIEGLADRIAdLRLEQF 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925332 779 EVHQ--GEVQRLQAQVVDLQAKMRAALDDQdkvqsqlsmaeavlrEHKTLVQQLKEQNEALNR 839
Cdd:PRK11281 371 EINQqrDALFQPDAYIDKLEAGHKSEVTDE---------------VRDALLQLLDERRELLDQ 418
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
227-933 |
3.86e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 227 EALEGFDEMRLELDQLEVREKQLRE---RMQQLDRENQELRAAVSQQGEQLQTERErgrtaaednvrltclVAELQKQWE 303
Cdd:PRK04863 500 ELLRRLREQRHLAEQLQQLRMRLSEleqRLRQQQRAERLLAEFCKRLGKNLDDEDE---------------LEQLQEELE 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 304 VTqatqntvkelqtcLQGLELGAAEKEEDYhTALRRLESMLQPLAQELEATRdsldkknqhlasfPGWLAmAQQKADTAS 383
Cdd:PRK04863 565 AR-------------LESLSESVSEARERR-MALRQQLEQLQARIQRLAARA-------------PAWLA-AQDALARLR 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 384 DTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQL--------VKELQLKEDARASL-----ERLVK 450
Cdd:PRK04863 617 EQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLsqpggsedPRLNALAERFGGVLlseiyDDVSL 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 451 EMAPLQEELSGKGQEA------DQLWRRLQELlahtssweeelaelrrekkqqqeekelleqevRSLTRQLQFLETQLAQ 524
Cdd:PRK04863 697 EDAPYFSALYGPARHAivvpdlSDAAEQLAGL--------------------------------EDCPEDLYLIEGDPDS 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 525 VSQHVSDLEEQKKQLIQDkdhLSQQVGMLERLagppgPELPVAGEKN-----EALVPVNSSLQEAWGKPEEEQRGLQEAq 599
Cdd:PRK04863 745 FDDSVFSVEELEKAVVVK---IADRQWRYSRF-----PEVPLFGRAArekriEQLRAEREELAERYATLSFDVQKLQRL- 815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 600 lddtkVQEGSQ--------------EEELRQANR---ELEKELQNVVGRNQLLEGKLQALQADYQALQQRESaiQGSLAS 662
Cdd:PRK04863 816 -----HQAFSRfigshlavafeadpEAELRQLNRrrvELERALADHESQEQQQRSQLEQAKEGLSALNRLLP--RLNLLA 888
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 663 LEAEQASIRHLGDQMEASLLAVR--KAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALesqcqqq 740
Cdd:PRK04863 889 DETLADRVEEIREQLDEAEEAKRfvQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL------- 961
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 741 TQLIEVLTAEKGQQGVGPPTDNEarELAAQLalsQAQLEvhQGEVQRLQAQVVDLQAKmrAALDDQDKVQSQLSMAEAVL 820
Cdd:PRK04863 962 TEVVQRRAHFSYEDAAEMLAKNS--DLNEKL---RQRLE--QAEQERTRAREQLRQAQ--AQLAQYNQVLASLKSSYDAK 1032
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 821 REhktLVQQLKEQNEALNRAHVQELlqcseregalqEERAdeAQQREEelraLQEELS--QAKCSSEEAQL-----EHAE 893
Cdd:PRK04863 1033 RQ---MLQELKQELQDLGVPADSGA-----------EERA--RARRDE----LHARLSanRSRRNQLEKQLtfceaEMDN 1092
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1894925332 894 LQEQLHRANTDtaelgiqvcaLTVEKERVEEALA--CAVQEL 933
Cdd:PRK04863 1093 LTKKLRKLERD----------YHEMREQVVNAKAgwCAVLRL 1124
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
978-1164 |
3.89e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 978 LQAQLAQAEQRAQ--SLQEAAHQELNTLKFQLsAEIMDYQSRLKnageeckSLRGQLEEQGRQLQAAEEAVEKLKATQ-- 1053
Cdd:PRK11281 41 VQAQLDALNKQKLleAEDKLVQQDLEQTLALL-DKIDRQKEETE-------QLKQQLAQAPAKLRQAQAELEALKDDNde 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 1054 -----------ADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRE--RND 1120
Cdd:PRK11281 113 etretlstlslRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKalRPS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1894925332 1121 QKM-----LADLD---DLNRTKKYLEERLIELLRDK-DALWQKSDALEFQQKL 1164
Cdd:PRK11281 193 QRVllqaeQALLNaqnDLQRKSLEGNTQLQDLLQKQrDYLTARIQRLEHQLQL 245
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
510-745 |
4.03e-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: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 510 SLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKD--HLSQQVGMLErlagppgpelpvageknEALVPVNSSLQEAwgk 587
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLL-----------------QQLSELESQLAEA--- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 588 peEEQRGLQEAQLDDTKVQEGSQEEELRQANREleKELQNVVGRNQLLEGKLQALQADYQ----ALQQRESAIQGSLASL 663
Cdd:COG3206 232 --RAELAEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTpnhpDVIALRAQIAALRAQL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 664 EAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAE---ARHRELRALESQCQQQ 740
Cdd:COG3206 308 QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYEsllQRLEEARLAEALTVGN 387
|
....*
gi 1894925332 741 TQLIE 745
Cdd:COG3206 388 VRVID 392
|
|
| DUF745 |
pfam05335 |
Protein of unknown function (DUF745); This family consists of several uncharacterized ... |
797-934 |
4.12e-03 |
|
Protein of unknown function (DUF745); This family consists of several uncharacterized Drosophila melanogaster proteins of unknown function.
Pssm-ID: 398808 [Multi-domain] Cd Length: 180 Bit Score: 39.86 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 797 AKMRAALDDQDKVQSQLS--------MAEAVLREHKTLVQQL-KEQNEAlnRAHVQEL---LQCSEREGALQEERADEAQ 864
Cdd:pfam05335 23 AQAAAAEAAARQVKNQLAdkalqaakAAEAALAGKQQIVEQLeQELREA--EAVVQEEsasLQQSQANANAAQRAAQQAQ 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925332 865 QREEELRAL----QEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEAL---ACAVQELQ 934
Cdd:pfam05335 101 QQLEALTAAlkaaQANLENAEQVAAGAQQELAEKTQLLEAAKKRVERLQRQLAEARADLEKTKKAAykaACAAVEAK 177
|
|
| FYVE_WDFY1 |
cd15756 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ... |
1169-1232 |
4.55e-03 |
|
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar proteins; WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. In addition to FYVE domain, WDFY1 harbors multiple WD-40 repeats.
Pssm-ID: 277295 [Multi-domain] Cd Length: 76 Bit Score: 37.36 E-value: 4.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925332 1169 RWLgdtEANHCLDCKREFSWMV-----------RRHHCRICGRIFCYYCCNNYVLSKHGG--KKERCCRACFQKLSE 1232
Cdd:cd15756 2 QWL---ESDSCQKCEQPFFWNIkqmwdtktlglRQHHCRKCGQAVCGKCSSKRSSYPIMGfeFQVRVCDSCFETIKD 75
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
796-1061 |
5.18e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 796 QAKMRAALDDQDKVQSQLsmaeAVLREHKTLVQQLKEQNEALNRAhvQELLQCSERegalQEERADEAQQR----EEELR 871
Cdd:PRK11281 28 RAASNGDLPTEADVQAQL----DALNKQKLLEAEDKLVQQDLEQT--LALLDKIDR----QKEETEQLKQQlaqaPAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 872 ALQEELSQAKCSSEE-----------AQLEH--AELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDake 938
Cdd:PRK11281 98 QAQAELEALKDDNDEetretlstlslRQLESrlAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 939 aasreregLERQVAGLQQEKE----SLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDY 1014
Cdd:PRK11281 175 --------IRNLLKGGKVGGKalrpSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLL 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925332 1015 QS-----RLKnageeckslrgQLEEQGRQLQAAEEAVE----KLKATQADMGEKLS 1061
Cdd:PRK11281 247 QEainskRLT-----------LSEKTVQEAQSQDEAARiqanPLVAQELEINLQLS 291
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
590-1050 |
5.61e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 590 EEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQAS 669
Cdd:pfam05557 92 LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 670 IRHLGD--QMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEV- 746
Cdd:pfam05557 172 IKELEFeiQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLe 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 747 LTAEKGQQ------------GVGPPTDNEARELAAQLalsQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLS 814
Cdd:pfam05557 252 LEKEKLEQelqswvklaqdtGLNLRSPEDLSRRIEQL---QQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 815 MAEAVLREHKTLVQQLKEQNEALN--RAHVQELLQCSEREGALQEERADEAQQREEELRALQEelSQAKCSSEEAQLEHA 892
Cdd:pfam05557 329 DLNKKLKRHKALVRRLQRRVLLLTkeRDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQK--MQAHNEEMEAQLSVA 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 893 ELQEQLHRANTDTAELGIQVCAltvEKERVEEALACA--VQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKA 970
Cdd:pfam05557 407 EEELGGYKQQAQTLERELQALR---QQESLADPSYSKeeVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPK 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 971 AAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLK 1050
Cdd:pfam05557 484 KTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLK 563
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
729-843 |
5.84e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.80 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 729 ELRALESQCQQQTQLIEVLTAEKGQQgvgpptdNEARELAAQLALSQAQLEVHQGEVQRL----------QAQVVDLQAK 798
Cdd:COG1566 84 ALAQAEAQLAAAEAQLARLEAELGAE-------AEIAAAEAQLAAAQAQLDLAQRELERYqalykkgavsQQELDEARAA 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1894925332 799 MRAALDDQDKVQSQLSMAEAVLREHKTLVQ---QLKEQNEALNRAHVQ 843
Cdd:COG1566 157 LDAAQAQLEAAQAQLAQAQAGLREEEELAAaqaQVAQAEAALAQAELN 204
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
583-725 |
8.03e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.17 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 583 EAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGslAS 662
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEA--AA 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925332 663 LEAEQASIRHLGDQMEASLLAVRKAKEAMK---AQMAEKEAILQSKEGECQQLREEVEQCQQLAEA 725
Cdd:PRK09510 140 KAAAAAKAKAEAEAKRAAAAAKKAAAEAKKkaeAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
761-934 |
8.12e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 761 DNEARELAAQLA-LSQAqLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlrehktlvqqlkeqneALNR 839
Cdd:PRK09039 52 DSALDRLNSQIAeLADL-LSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAG-----------------AGAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 840 AhvqellqcSEREGALQEERADEAQQREEELRalQEELSQAKCSSEEAQLehAELQEQLHRANTDTAELGIQVCALtveK 919
Cdd:PRK09039 114 A--------EGRAGELAQELDSEKQVSARALA--QVELLNQQIAALRRQL--AALEAALDASEKRDRESQAKIADL---G 178
|
170
....*....|....*
gi 1894925332 920 ERVEEALACAVQELQ 934
Cdd:PRK09039 179 RRLNVALAQRVQELN 193
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
702-881 |
8.74e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 702 LQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptDNEARELAAQLALSQAQLEVH 781
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL------ELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 782 QG--EVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEER 859
Cdd:COG1579 86 RNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
170 180
....*....|....*....|..
gi 1894925332 860 ADEAQQREEELRALQEELSQAK 881
Cdd:COG1579 166 EELAAKIPPELLALYERIRKRK 187
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
777-1006 |
8.76e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 777 QLEVHQGEVQRLQAQVVD-LQAKMRAaLDDQDKVQSQLSMAEAVLREHKTLVQQLKEQ--NEALNRAHV----------Q 843
Cdd:PRK10929 31 ELEQAKAAKTPAQAEIVEaLQSALNW-LEERKGSLERAKQYQQVIDNFPKLSAELRQQlnNERDEPRSVppnmstdaleQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 844 ELLQCSERegaLQEErADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELG-IQVCALTVE---- 918
Cdd:PRK10929 110 EILQVSSQ---LLEK-SRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAqAQLTALQAEsaal 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925332 919 KERVEE-----ALACAVQELQDAK-EAASREREGLERQVAGL--------QQEKESLQEKLKAAKAAAGSLP-GLQAQLA 983
Cdd:PRK10929 186 KALVDElelaqLSANNRQELARLRsELAKKRSQQLDAYLQALrnqlnsqrQREAERALESTELLAEQSGDLPkSIVAQFK 265
|
250 260
....*....|....*....|...
gi 1894925332 984 QAEQRAQSLQEAAhQELNTLKFQ 1006
Cdd:PRK10929 266 INRELSQALNQQA-QRMDLIASQ 287
|
|
| |
